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251  structures 1683  species 0  interactions 25345  sequences 429  architectures

Family: Arf (PF00025)

Summary: ADP-ribosylation factor family

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "ADP ribosylation factor". More...

ADP ribosylation factor Edit Wikipedia article

1ksg opm.png
Membrane-bound ADP ribosylation factor-like protein 2 (ARL2 mouse, red), complex with phosphodiesterase delta (yellow) (1ksg) Blue dots show hydrocarbon boundary of the lipid bilayer
Identifiers
SymbolArf
PfamPF00025
InterProIPR006689
SMARTARF
PROSITEPDOC01020
SCOPe1hur / SUPFAM
OPM superfamily124
OPM protein1ksg
CDDcd00878
Membranome1103
Distribution of ARF in a living macrophage, highlighting the Golgi apparatus.

ADP ribosylation factors (ARFs) are members of the ARF family of GTP-binding proteins of the Ras superfamily. ARF family proteins are ubiquitous in eukaryotic cells, and six highly conserved members of the family have been identified in mammalian cells. Although ARFs are soluble, they generally associate with membranes because of N-terminus myristoylation. They function as regulators of vesicular traffic and actin remodelling.

The small ADP ribosylation factor (Arf) GTP-binding proteins are major regulators of vesicle biogenesis in intracellular traffic.[1] They are the founding members of a growing family that includes Arl (Arf-like), Arp (Arf-related proteins) and the remotely related Sar (Secretion-associated and Ras-related) proteins. Arf proteins cycle between inactive GDP-bound and active GTP-bound forms that bind selectively to effectors. The classical structural GDP/GTP switch is characterised by conformational changes at the so-called switch 1 and switch 2 regions, which bind tightly to the gamma-phosphate of GTP but poorly or not at all to the GDP nucleotide. Structural studies of Arf1 and Arf6 have revealed that although these proteins feature the switch 1 and 2 conformational changes, they depart from other small GTP-binding proteins in that they use an additional, unique switch to propagate structural information from one side of the protein to the other.

The GDP/GTP structural cycles of human Arf1 and Arf6 feature a unique conformational change that affects the beta2beta3 strands connecting switch 1 and switch 2 (interswitch) and also the amphipathic helical N-terminus. In GDP-bound Arf1 and Arf6, the interswitch is retracted and forms a pocket to which the N-terminal helix binds, the latter serving as a molecular hasp to maintain the inactive conformation. In the GTP-bound form of these proteins, the interswitch undergoes a two-residue register shift that pulls switch 1 and switch 2 up, restoring an active conformation that can bind GTP. In this conformation, the interswitch projects out of the protein and extrudes the N-terminal hasp by occluding its binding pocket.

Regulatory proteins

ARFs regularly associate with two types of protein, those involved in catalyzing GTP/GDP exchange, and those that serve other functions.

GTP/GDP exchange proteins

ARF binds to two forms of the guanosine nucleotide, guanosine triphosphate (GTP) and guanosine diphosphate (GDP). The shape of the ARF molecule is dependent upon the form to which it is bound, allowing it to serve in a regulatory capacity. ARF requires assistance from other proteins in order to switch between binding to GTP and GDP. GTPase activating proteins (GAPs) force ARF to hydrolyze bound GTP to GDP, and Guanine nucleotide exchange factors force ARF to adopt a new GTP molecule in place of a bound GDP.

Other proteins

Other proteins interact with ARF, depending upon whether or not it is bound to GTP or GDP. The active form, ARF*GTP, binds to vesicle coat proteins and adaptors, including coat protein I (COPI) and various phospholipids. The inactive form is only known to bind to a class of transmembrane proteins. Different types of ARF bind specifically different kinds of effector proteins.

Phylogeny

There are currently 6 known mammalian ARF proteins, which are divided into three classes of ARFs:

Structure

ARFs are small proteins of approximately 20 kD in size. They contain two switch regions, which change relative positions between cycles of GDP/GTP-binding. ARFs are frequently myristoylated in their N-terminal region, which contributes to their membrane association.

Examples

Human genes encoding proteins containing this domain include:

See also

References

Further reading

  • Donaldson JG, Honda A (2005). "Localization and function of Arf family GTPases". Biochemical Society Transactions. 33 (4): 639–642. doi:10.1042/BST0330639. PMID 16042562.
  • Nie Z, Hirsch DS, Randazzo PA (2003). "Arf and its many interactors". Current Opinion in Cell Biology. 15 (4): 396–404. doi:10.1016/S0955-0674(03)00071-1. PMID 12892779.
  • Amor JC, Harrison DH, Kahn RA, Ringe D (1994). "Structure of the human ADP-ribosylation factor 1 complexed with GDP". Nature. 372 (6507): 704–708. doi:10.1038/372704a0. PMID 7990966.
  • Moss J, Vaughan M; Vaughan (1995). "Structure and function of ARF proteins: Activators of cholera toxin and critical components of intracellular vesicular transport processes". The Journal of Biological Chemistry. 270 (21): 12327–12330. doi:10.1074/jbc.270.21.12327. PMID 7759471.
  • Boman AL, Kahn RA; Kahn (1995). "Arf proteins: The membrane traffic police?". Trends in Biochemical Sciences. 20 (4): 147–150. doi:10.1016/s0968-0004(00)88991-4. PMID 7770914.
  • Kahn RA, Kern FG, Clark J, Gelmann EP, Rulka C (1991). "Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins". The Journal of Biological Chemistry. 266 (4): 2606–2614. PMID 1899243.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR006689

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

ADP-ribosylation factor family Provide feedback

Pfam combines a number of different Prosite families together

Literature references

  1. Amor JC, Harrison DH, Kahn RA, Ringe D; , Nature 1994;372:704-708.: Structure of the human ADP-ribosylation factor 1 complexed with GDP. PUBMED:7990966 EPMC:7990966

  2. Moss J, Vaughan M; , J. Biol. Chem. 1995;270:12327-12330.: Structure and function of ARF proteins: Activators of cholera toxin and critical components of intracellular vesicular transport processes. PUBMED:7759471 EPMC:7759471

  3. Boman AL, Kahn RA; , Trends Biochem Sci 1995;20:147-150.: Arf proteins: the membrane traffic police? PUBMED:7770914 EPMC:7770914

  4. Kahn RA, Kern FG, Clark J, Gelmann EP, Rulka C; , J Biol Chem 1991;266:2606-2614.: Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins. PUBMED:1899243 EPMC:1899243


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006689

This entry represents a branch of the small GTPase superfamily that includes the ADP ribosylation factor Arf, Arl (Arf-like), Arp (Arf-related proteins) and the remotely related Sar (Secretion-associated and Ras-related) proteins. Arf proteins are major regulators of vesicle biogenesis in intracellular traffic [ PUBMED:12429613 ]. They cycle between inactive GDP-bound and active GTP-bound forms that bind selectively to effectors. The classical structural GDP/GTP switch is characterised by conformational changes at the so-called switch 1 and switch 2 regions, which bind tightly to the gamma-phosphate of GTP but poorly or not at all to the GDP nucleotide. Structural studies of Arf1 and Arf6 have revealed that although these proteins feature the switch 1 and 2 conformational changes, they depart from other small GTP-binding proteins in that they use an additional, unique switch to propagate structural information from one side of the protein to the other.

The GDP/GTP structural cycles of human Arf1 and Arf6 feature a unique conformational change that affects the beta2-beta3 strands connecting switch 1 and switch 2 (interswitch) and also the amphipathic helical N terminus. In GDP-bound Arf1 and Arf6, the interswitch is retracted and forms a pocket to which the N-terminal helix binds, the latter serving as a molecular hasp to maintain the inactive conformation. In the GTP-bound form of these proteins, the interswitch undergoes a two-residue register shift that pulls switch 1 and switch 2 up, restoring an active conformation that can bind GTP. In this conformation, the interswitch projects out of the protein and extrudes the N-terminal hasp by occluding its binding pocket.

Small GTPases form an independent superfamily within the larger class of regulatory GTP hydrolases. This superfamily contains proteins that control a vast number of important processes and possess a common, structurally preserved GTP-binding domain [ PUBMED:2122258 , PUBMED:1898771 ]. Sequence comparisons of small G proteins from various species have revealed that they are conserved in primary structures at the level of 30-55% similarity [ PUBMED:2029511 ].

Crystallographic analysis of various small G proteins revealed the presence of a 20kDa catalytic domain that is unique for the whole superfamily [ PUBMED:1898771 , PUBMED:2196171 ]. The domain is built of five alpha helices (A1-A5), six beta-strands (B1-B6) and five polypeptide loops (G1-G5). A structural comparison of the GTP- and GDP-bound form, allows one to distinguish two functional loop regions: switch I and switch II that surround the gamma-phosphate group of the nucleotide. The G1 loop (also called the P-loop) that connects the B1 strand and the A1 helix is responsible for the binding of the phosphate groups. The G3 loop provides residues for Mg2 and phosphate binding and is located at the N terminus of the A2 helix. The G1 and G3 loops are sequentially similar to Walker A and Walker B boxes that are found in other nucleotide binding motifs. The G2 loop connects the A1 helix and the B2 strand and contains a conserved Thr residue responsible for Mg2 binding. The guanine base is recognised by the G4 and G5 loops. The consensus sequence NKXD of the G4 loop contains Lys and Asp residues directly interacting with the nucleotide. Part of the G5 loop located between B6 and A5 acts as a recognition site for the guanine base [ PUBMED:11995995 ].

The small GTPase superfamily can be divided into at least 8 different families, including:

  • Arf small GTPases. GTP-binding proteins involved in protein trafficking by modulating vesicle budding and uncoating within the Golgi apparatus.
  • Ran small GTPases. GTP-binding proteins involved in nucleocytoplasmic transport. Required for the import of proteins into the nucleus and also for RNA export.
  • Rab small GTPases. GTP-binding proteins involved in vesicular traffic.
  • Rho small GTPases. GTP-binding proteins that control cytoskeleton reorganisation.
  • Ras small GTPases. GTP-binding proteins involved in signalling pathways.
  • Sar1 small GTPases. Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER).
  • Mitochondrial Rho (Miro). Small GTPase domain found in mitochondrial proteins involved in mitochondrial trafficking.
  • Roc small GTPases domain. Small GTPase domain always found associated with the COR domain.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan P-loop_NTPase (CL0023), which has the following description:

AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].

The clan contains the following 243 members:

6PF2K AAA AAA-ATPase_like AAA_10 AAA_11 AAA_12 AAA_13 AAA_14 AAA_15 AAA_16 AAA_17 AAA_18 AAA_19 AAA_2 AAA_21 AAA_22 AAA_23 AAA_24 AAA_25 AAA_26 AAA_27 AAA_28 AAA_29 AAA_3 AAA_30 AAA_31 AAA_32 AAA_33 AAA_34 AAA_35 AAA_5 AAA_6 AAA_7 AAA_8 AAA_9 AAA_PrkA ABC_ATPase ABC_tran ABC_tran_Xtn Adeno_IVa2 Adenylsucc_synt ADK AFG1_ATPase AIG1 APS_kinase Arf ArsA_ATPase ATP-synt_ab ATP_bind_1 ATP_bind_2 ATPase ATPase_2 Bac_DnaA BCA_ABC_TP_C Beta-Casp bpMoxR Cas_Csn2 Cas_St_Csn2 CbiA CBP_BcsQ CDC73_C CENP-M CFTR_R CLP1_P CMS1 CoaE CobA_CobO_BtuR CobU cobW CPT CSM2 CTP_synth_N Cytidylate_kin Cytidylate_kin2 DAP3 DBINO DEAD DEAD_2 DLIC DNA_pack_C DNA_pack_N DNA_pol3_delta DNA_pol3_delta2 DnaB_C dNK DO-GTPase1 DO-GTPase2 DUF1611 DUF1726 DUF2075 DUF2326 DUF2478 DUF257 DUF2791 DUF2813 DUF3584 DUF463 DUF5906 DUF6079 DUF815 DUF853 DUF87 DUF927 Dynamin_N Dynein_heavy Elong_Iki1 ELP6 ERCC3_RAD25_C Exonuc_V_gamma FeoB_N Fer4_NifH Flavi_DEAD FTHFS FtsK_SpoIIIE G-alpha Gal-3-0_sulfotr GBP GBP_C GTP_EFTU Gtr1_RagA Guanylate_kin GvpD HDA2-3 Helicase_C Helicase_C_2 Helicase_C_4 Helicase_RecD Herpes_Helicase Herpes_ori_bp Herpes_TK HSA HydF_dimer HydF_tetramer Hydin_ADK IIGP IPPT IPT iSTAND IstB_IS21 KAP_NTPase KdpD Kinase-PPPase Kinesin KTI12 LAP1C Lon_2 LpxK MCM MeaB MEDS Mg_chelatase Microtub_bd MipZ MMR_HSR1 MMR_HSR1_C MobB MukB Mur_ligase_M MutS_V Myosin_head NACHT NAT_N NB-ARC NOG1 NTPase_1 NTPase_P4 OPA1_C ORC3_N P-loop_TraG ParA Parvo_NS1 PAXNEB PduV-EutP PhoH PIF1 Ploopntkinase1 Ploopntkinase2 Ploopntkinase3 Podovirus_Gp16 Polyoma_lg_T_C Pox_A32 PPK2 PPV_E1_C PRK PSY3 Rad17 Rad51 Ras RecA ResIII RHD3 RhoGAP_pG1_pG2 RHSP RNA12 RNA_helicase Roc RsgA_GTPase RuvB_N SbcCD_C SecA_DEAD Septin Sigma54_activ_2 Sigma54_activat SKI SMC_N SNF2-rel_dom Spore_III_AA Spore_IV_A SRP54 SRPRB SulA Sulfotransfer_1 Sulfotransfer_2 Sulfotransfer_3 Sulfotransfer_4 Sulfotransfer_5 Sulphotransf SWI2_SNF2 T2SSE T4SS-DNA_transf Terminase_1 Terminase_3 Terminase_6N Terminase_GpA Thymidylate_kin TIP49 TK TniB Torsin TraG-D_C tRNA_lig_kinase TrwB_AAD_bind TsaE UvrB UvrD-helicase UvrD_C UvrD_C_2 Viral_helicase1 VirC1 VirE YqeC Zeta_toxin Zot

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(20)
Full
(25345)
Representative proteomes UniProt
(47206)
RP15
(4893)
RP35
(11719)
RP55
(20803)
RP75
(27336)
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  Seed
(20)
Full
(25345)
Representative proteomes UniProt
(47206)
RP15
(4893)
RP35
(11719)
RP55
(20803)
RP75
(27336)
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  Seed
(20)
Full
(25345)
Representative proteomes UniProt
(47206)
RP15
(4893)
RP35
(11719)
RP55
(20803)
RP75
(27336)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Swissprot
Previous IDs: arf;
Type: Domain
Sequence Ontology: SO:0000417
Author: Sonnhammer ELL
Number in seed: 20
Number in full: 25345
Average length of the domain: 156.60 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 73.82 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.3 22.3
Trusted cut-off 22.3 22.3
Noise cut-off 22.2 22.2
Model length: 175
Family (HMM) version: 23
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Arf domain has been found. There are 251 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0G2JMH3 View 3D Structure Click here
A0A0G2K4Q4 View 3D Structure Click here
A0A0G2KEX1 View 3D Structure Click here
A0A0R0EN78 View 3D Structure Click here
A0A0R0F2E8 View 3D Structure Click here
A0A0R0FW01 View 3D Structure Click here
A0A0R0HC62 View 3D Structure Click here
A0A0R0HCK0 View 3D Structure Click here
A0A0R0HCK0 View 3D Structure Click here
A0A0R0HMR0 View 3D Structure Click here
A0A0R0I1I9 View 3D Structure Click here
A0A0R0KXC5 View 3D Structure Click here
A0A143ZY58 View 3D Structure Click here
A0A1D6FI64 View 3D Structure Click here
A0A1D6FI64 View 3D Structure Click here
A0A1D6FR30 View 3D Structure Click here
A0A1D6G9N5 View 3D Structure Click here
A0A1D6G9N5 View 3D Structure Click here
A0A1D6GEU6 View 3D Structure Click here
A0A1D6HG78 View 3D Structure Click here
A0A1D6HGS7 View 3D Structure Click here
A0A1D6HGS7 View 3D Structure Click here
A0A1D6HJC2 View 3D Structure Click here
A0A1D6IJX3 View 3D Structure Click here
A0A1D6IJX3 View 3D Structure Click here
A0A1D6IUP5 View 3D Structure Click here
A0A1D6KYW2 View 3D Structure Click here
A0A1D6LL71 View 3D Structure Click here
A0A1D6LP25 View 3D Structure Click here
A0A1D6M714 View 3D Structure Click here
A0A1D6N919 View 3D Structure Click here
A0A1D6PDD6 View 3D Structure Click here
A0A1D6QH64 View 3D Structure Click here
A0A1D6QM41 View 3D Structure Click here
A0A1D8PCQ6 View 3D Structure Click here
A0A1D8PF23 View 3D Structure Click here
A0A1D8PF23 View 3D Structure Click here
A0A1D8PJ64 View 3D Structure Click here
A0A1X7YII1 View 3D Structure Click here
A0A2R8Q9C6 View 3D Structure Click here
A0A2R8QDL0 View 3D Structure Click here
A0A2R8QEE6 View 3D Structure Click here
A0A2R8QI61 View 3D Structure Click here
A0A2R8RSE9 View 3D Structure Click here
A1ZBK9 View 3D Structure Click here
A4HS29 View 3D Structure Click here
A4HS43 View 3D Structure Click here
A4HSC6 View 3D Structure Click here
A4HX34 View 3D Structure Click here
A4HX72 View 3D Structure Click here
A4I2E6 View 3D Structure Click here
A4I4E4 View 3D Structure Click here
A4I5R5 View 3D Structure Click here
A4I784 View 3D Structure Click here
A4IAR4 View 3D Structure Click here
A4ICQ2 View 3D Structure Click here
A4IE34 View 3D Structure Click here
A4IE45 View 3D Structure Click here
A5PMK4 View 3D Structure Click here
A6NH57 View 3D Structure Click here
B1ATY8 View 3D Structure Click here
B1WC73 View 3D Structure Click here
B2RZ70 View 3D Structure Click here
B4F9H8 View 3D Structure Click here
B4FA33 View 3D Structure Click here
B4FBG7 View 3D Structure Click here
B4FF78 View 3D Structure Click here
B4FIX8 View 3D Structure Click here
B4FPT6 View 3D Structure Click here
B6TA16 View 3D Structure Click here
B6TGE5 View 3D Structure Click here
B6TS42 View 3D Structure Click here
B7ZD40 View 3D Structure Click here
B8JLB2 View 3D Structure Click here
C6SVM0 View 3D Structure Click here
C6SVP4 View 3D Structure Click here
C6SW20 View 3D Structure Click here
C6SX15 View 3D Structure Click here
C6SXY9 View 3D Structure Click here
C6SZI8 View 3D Structure Click here
C6T2I8 View 3D Structure Click here
C6T7H0 View 3D Structure Click here
C6TG08 View 3D Structure Click here
C6TKB5 View 3D Structure Click here
C6TKK5 View 3D Structure Click here
D3ZES1 View 3D Structure Click here
D3ZPP2 View 3D Structure Click here
E7FAS3 View 3D Structure Click here
E9AHL7 View 3D Structure Click here
F1M6C4 View 3D Structure Click here
F1Q4Q5 View 3D Structure Click here
F1Q9Z2 View 3D Structure Click here
F1QKW5 View 3D Structure Click here
F1QXC3 View 3D Structure Click here
F1R8Q1 View 3D Structure Click here
F1RBH2 View 3D Structure Click here
F1RDR4 View 3D Structure Click here
F4HXI4 View 3D Structure Click here
F4HXI5 View 3D Structure Click here
F4IZ82 View 3D Structure Click here
F8W2P1 View 3D Structure Click here
G3V9B1 View 3D Structure Click here
G5EDC6 View 3D Structure Click here
G5EFK4 View 3D Structure Click here
H2L0N8 View 3D Structure Click here
H9XVM3 View 3D Structure Click here
I1J584 View 3D Structure Click here
I1K2E4 View 3D Structure Click here
I1KMT1 View 3D Structure Click here
I1L0L6 View 3D Structure Click here
I1L0T1 View 3D Structure Click here
I1LB56 View 3D Structure Click here
I1LG16 View 3D Structure Click here
I1LHS7 View 3D Structure Click here
I1LVU0 View 3D Structure Click here
I1M146 View 3D Structure Click here
I1MBV8 View 3D Structure Click here
I1MFE4 View 3D Structure Click here
I1MGG9 View 3D Structure Click here
I1MSU2 View 3D Structure Click here
I1N5H2 View 3D Structure Click here
I1NIB4 View 3D Structure Click here
I1NIB7 View 3D Structure Click here
I1NJ52 View 3D Structure Click here
K7LK36 View 3D Structure Click here
K7LK36 View 3D Structure Click here
K7TVI2 View 3D Structure Click here
K7V5E7 View 3D Structure Click here
M0R4K4 View 3D Structure Click here
M0R6N0 View 3D Structure Click here
M0RDU9 View 3D Structure Click here
O00909 View 3D Structure Click here
O04834 View 3D Structure Click here
O08697 View 3D Structure Click here
O45379 View 3D Structure Click here
O80489 View 3D Structure Click here
O88848 View 3D Structure Click here
P0DH91 View 3D Structure Click here
P11076 View 3D Structure Click here
P18085 View 3D Structure Click here
P19146 View 3D Structure Click here
P20606 View 3D Structure Click here
P22274 View 3D Structure Click here
P25160 View 3D Structure Click here
P34212 View 3D Structure Click here
P36397 View 3D Structure Click here
P36404 View 3D Structure Click here
P36405 View 3D Structure Click here
P36406 View 3D Structure Click here
P36407 View 3D Structure Click here
P36536 View 3D Structure Click here
P36579 View 3D Structure Click here
P37996 View 3D Structure Click here
P38116 View 3D Structure Click here
P39110 View 3D Structure Click here
P40616 View 3D Structure Click here
P40617 View 3D Structure Click here
P40940 View 3D Structure Click here
P40945 View 3D Structure Click here
P40946 View 3D Structure Click here
P40994 View 3D Structure Click here
P49076 View 3D Structure Click here
P49703 View 3D Structure Click here
P51646 View 3D Structure Click here
P51823 View 3D Structure Click here
P56559 View 3D Structure Click here
P61204 View 3D Structure Click here
P61205 View 3D Structure Click here
P61206 View 3D Structure Click here
P61208 View 3D Structure Click here
P61209 View 3D Structure Click here
P61211 View 3D Structure Click here
P61212 View 3D Structure Click here
P61213 View 3D Structure Click here
P61214 View 3D Structure Click here
P61750 View 3D Structure Click here
P61751 View 3D Structure Click here
P62330 View 3D Structure Click here
P62331 View 3D Structure Click here
P62332 View 3D Structure Click here
P84077 View 3D Structure Click here
P84078 View 3D Structure Click here
P84079 View 3D Structure Click here
P84082 View 3D Structure Click here
P84083 View 3D Structure Click here
P84084 View 3D Structure Click here
P84085 View 3D Structure Click here
Q01474 View 3D Structure Click here
Q01475 View 3D Structure Click here
Q02804 View 3D Structure Click here
Q06396 View 3D Structure Click here
Q06849 View 3D Structure Click here
Q09654 View 3D Structure Click here
Q09767 View 3D Structure Click here
Q0DYE5 View 3D Structure Click here
Q0E1L4 View 3D Structure Click here
Q0P5N6 View 3D Structure Click here
Q10943 View 3D Structure Click here
Q10QD5 View 3D Structure Click here
Q13795 View 3D Structure Click here
Q18510 View 3D Structure Click here
Q19705 View 3D Structure Click here
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