# STOCKHOLM 1.0
#=GF ID TRAF6_Z2
#=GF AC PF18048.3
#=GF DE TNF receptor-associated factor 6 zinc finger 2
#=GF AU Smart A;0000-0002-6965-5633
#=GF GA 27.4 27.4
#=GF NC 27.3 27.3
#=GF TC 27.4 27.6
#=GF SE ECOD:EUF02238
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
#=GF TP Domain
#=GF CL CL0389
#=GF RN [1]
#=GF RM 19465916
#=GF RT E2 interaction and dimerization in the crystal structure of
#=GF RT TRAF6.
#=GF RA Yin Q, Lin SC, Lamothe B, Lu M, Lo YC, Hura G, Zheng L, Rich RL,
#=GF RA Campos AD, Myszka DG, Lenardo MJ, Darnay BG, Wu H;
#=GF RL Nat Struct Mol Biol. 2009;16:658-666.
#=GF DR INTERPRO; IPR041310;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC This domain is the second of three zinc fingers of Homo sapiens
#=GF CC TNF receptor associated factor 6 (TRAF6). TRAF6 mediates Lys63
#=GF CC (K63)-linked polyubiquitination for Necrosis Factor-kappaB
#=GF CC activation. The first three residues and the last Cys of finger
#=GF CC 1 form a classical type I beta-turn [1].
#=GF SQ 40
A0A4U1FRA5.1/158-184 FALMNCPQCQRPFQKCQLNIHIVKECP
A0A6A1QIF3.1/158-184 FALMNCPQCQRPFQKCQLNIHIVKECP
P70196.2/157-183     FALVNCPQCQRPFQKCQVNTHIIEDCP
Q9Y4K3.1/157-183     FALMDCPQCQRPFQKFHINIHILKDCP
A0A212DIB6.1/140-166 FALMSCPQCQRPFQKCHLNVHILKECP
A0A3P4QC16.1/157-183 FTLMNCPQCQRPFQKCQLNIHILKECP
G3GZ05.1/135-161     FALMNCPQCQRPFQKCHFHIHIIEDCP
A0A091CRB5.1/185-211 FALVNCSQCQHPFQKCQLNVHILKDCP
A0A5N4DMY6.1/158-184 FALMNCPQCQCSFQKCQLNFHILEECP
F6S636.1/157-183     YALVECPQCHISFQKNILHDHVVSECP
A0A1A6HQX7.1/157-183 FALMTCTQCQRPFQKCQFNIHIMEDCP
B5DF45.1/157-183     FALVICPQCQRFFQKCQINKHIIEDCP
G3WLM2.1/157-183     FALVECSQCHLSFRKYLLHNHMLTECP
A0A3L8SWV3.1/157-183 FSTVECLQCQRTFPKNYLKEHMTQECP
A0A0Q3LZU9.1/155-181 FSTVECPQCQGAFQKNHLKEHITQECP
A0A3M0JGK1.1/135-161 FSTVECPQCQGTFPKNHLKEHVTQECP
A0A1V4KG42.1/135-161 FSTVECPQCQGAFQKNHLKEHMTQECP
R0KBV6.1/139-165     FSTVECPQCQGAFQKNHLKEHMTQECP
A0A091RYI3.1/155-181 FSTVECPQCQGAFQKNHLKEHMTQECP
A0A226PQ48.1/154-180 FTTVECPQCQGTFQKNHLKEHVTQECP
Q28DL4.1/159-185     FAGVECSQCQSSFPKYSLQKHKFEECP
A0A2P4T0Z5.1/157-183 FTTVECPQCQGAFQKNHLKEHMTQECP
E1C626.2/157-183     FTTVECPQCQGAFQKNHLKEHMTQECP
A0A402EZD4.1/160-186 FASEECPQCQGCFQKNQLQEHVMLECP
M7BW57.1/196-222     FCSVECPQCQGSFQKNQLQNHMTLECP
A0A091K4D9.1/157-182 FSTVECPQCQGAFQKNHLKEHMTQEC-
A0A093BHZ4.1/157-182 FSTMECPQCQGAFQKNRLKEHMTQEC-
K7FW05.1/159-185     FSCVECLQCQGSFQKNQLQNHMMLECP
A0A2I0TUL4.1/165-190 FSPVECPQCQGAFQKNHLKEHMTQEC-
G1KDM3.1/160-186     FASEKCPQCQGIFQKNRLQEHIKLECP
A0A3Q0G5A1.1/62-88   FSCVECPQCLGFFQKNQMKEHMTQECP
A0A1U7RAW4.1/157-183 FSCVECPQCLGFFQKNQMKEHMTQECP
A0A6J1TQ62.1/160-185 FASEKCSQCQGIFQKNQLQEHML-ECP
A0A6P8P3Y7.1/158-184 FANVECPQCRAPFQRRLIEDHMRLECP
A0A6P8QAA3.1/158-184 FANVECPQCRAPFQRRLIEDHMRLECP
H2L646.2/165-191     FATVPCSQCQQPVRKSYLEEHATVECP
A0A556TLF1.1/131-156 FATVPCPQCQEPVWKNSIEEHRTQDC-
A0A5J5DQT8.1/167-192 FATVPCPQCQQSVRKSHLEEHTTVEC-
H2UXL8.3/166-191     FATVPCPHCQQSVRKTILEEHMTAEC-
A0A6A5BEF9.1/255-274 --LVECPLCQRKFTKYQIKIHM-----
//