# STOCKHOLM 1.0
#=GF ID Dsl1_N
#=GF AC PF11988.9
#=GF DE Retrograde transport protein Dsl1 N terminal
#=GF AU Gavin OL;
#=GF GA 25.0 25.0
#=GF NC 22.8 19.6
#=GF TC 35.6 28.9
#=GF SE pdb_3etu
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 19151722
#=GF RT Structural characterization of Tip20p and Dsl1p, subunits of the
#=GF RT Dsl1p vesicle tethering complex.
#=GF RA Tripathi A, Ren Y, Jeffrey PD, Hughson FM;
#=GF RL Nat Struct Mol Biol. 2009;16:114-123.
#=GF RN [2]
#=GF RM 11493604
#=GF RT The coatomer-interacting protein Dsl1p is required for
#=GF RT Golgi-to-endoplasmic reticulum retrieval in yeast. 
#=GF RA Andag U, Neumann T, Schmitt HD; 
#=GF RL J Biol Chem 2001;276:39150-39160.
#=GF DR INTERPRO; IPR021875;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC Dsl1 is a peripheral membrane protein required for transport
#=GF CC between the Golgi and the endoplasmic reticulum [1]. It is
#=GF CC localised to the ER membrane, and in vitro it specifically binds
#=GF CC to coatomer, the major component of the protein coat of COPI
#=GF CC vesicles [2]. It is comprised primarily of alpha helical bundles
#=GF CC [1]. It complexes with another subunit of the Dsl1p complex
#=GF CC called Tip20 which forms heterodimers by pairing the N termini
#=GF CC of each protein [1].  A central disorganised region between the
#=GF CC N and C termini of Dsl1 contains binding sites for coatomer [1].
#=GF CC The C terminus of Dsl1 contains a binding site to the Sec39
#=GF CC subunit of the Dsl1p complex [1].
#=GF SQ 2
P53847.1/6-360      PNKGEIIRELLKDPLILKNDSKRSngSELELDSSDLLQREAILANELNILDNLKTFLNLIKEVKTNLNILELENCYYSLQSLRKKMRNNAAYLKQSFNFQQSISTYVDTLHLELVSTLYKILTNGFWKITENSIQFTPTVEWGKDKVHIEYDTFMDFVAQQYFPKGSLDNQAWFILDMTSADSQEQVRAKLNTIMKEYMNLSRIVSMIKNSIFISGKEISYENEKNIlVFSKSSSHGQHCVSTVLTSFEAVCDFMLDGLAFRDRKTLSYELGPLFNTEFTKFVKNNASIILESLDSPLKNLVSVINNKLTRLVAKsEVTNWTHSGKEIQDLLMNKQLYYNLLLDKVLESHISEIR
A0A1E3P269.1/46-173 ------------------------..-----ELSKLQQRDYEITQELQQLRELWVISTLLKETEVNLELFEFENVFDSLRNFQKKIK-SDSLTSSLIIVDKLQNEH-DRCYDLAIEKIKQCWNE-LIHVDNDSIEFNAEVEINGNLVQFE--NISDVIKTNNLQ---------------------------------------------------------------.---------------------------------------------------------------------------------------.---------------------------------------
//