ID A0A094FFE4_9PEZI Unreviewed; 2407 AA.
AC A0A094FFE4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Protein transport protein SEC31 {ECO:0000256|ARBA:ARBA00021236};
DE AltName: Full=Protein transport protein sec31 {ECO:0000256|ARBA:ARBA00013507};
GN ORFNames=V500_05669 {ECO:0000313|EMBL:KFY89471.1};
OS Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY89471.1, ECO:0000313|Proteomes:UP000029284};
RN [1] {ECO:0000313|EMBL:KFY89471.1, ECO:0000313|Proteomes:UP000029284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules. {ECO:0000256|ARBA:ARBA00025471}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family.
CC {ECO:0000256|ARBA:ARBA00009358}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY89471.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPKC01001889; KFY89471.1; -; Genomic_DNA.
DR STRING; 1420913.A0A094FFE4; -.
DR HOGENOM; CLU_000884_0_0_1; -.
DR Proteomes; UP000029284; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR Gene3D; 1.25.40.1030; -; 1.
DR Gene3D; 1.20.940.10; Functional domain of the splicing factor Prp18; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040251; SEC31-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR13923; SEC31-RELATED PROTEIN; 1.
DR PANTHER; PTHR13923:SF11; SECRETORY 31, ISOFORM D; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Reference proteome {ECO:0000313|Proteomes:UP000029284};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022892};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 163..205
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 253..295
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 2094..2394
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 494..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1427..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1807..1830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1886..1905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..980
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1050
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1084
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2407 AA; 263021 MW; E16DEC639577DEB2 CRC64;
MVRLREIPRT AAFAWSPGTG LPILVTGTRA GAVDADFSDE TKLELWDLNL DNLEQGVELQ
PIASISTDSR FHDIAWAPPN ENHPKGIIAG ALDNGSLDLW DAEKLLEGSS DAFMSRTSTH
AAAIKSLQFN PLKPDILATA GAKGELYIYD VNDMSNASRL GNPQARSDDL ECIAWNRKVP
HILATGSVGG FVTVWDLKTK KATLTLNNSR KAVGAIAWDP NNPTKLLTAT PDDSTPVIQL
WDLRNSNAPE RTLQGHEQGV LSLSWCEQDS DILLSSGKDN KTLCWNPQTG ELLGEFPEAT
NWTFQTRFSP HNPNLSATAS FDGKISIQTL QNTNQPVGQG ATNGLTDGED FFNKAQTQPQ
GSSFTLPKAP KWMERPIGAS FGFGGKLVIF SQQPAVAGGQ RSSKIQLSKF SADSGVAAAT
EAFETSLESG DIIGICKSHI ESANTDEETA DWEVIKALVA ESPRKSVTEY LGFSEAEDAS
VGVNDATALD ADADADAAKD SETTLDPTSK AKNNRLSTFF NDSPDTDDFL SDLTPTKTAK
TNDPFHLLSD SDSQSDREIT RALMLGQFEH AMSICLKDDR MADAFVIANC GGKELLAKAQ
KAYLAGAAKG PKYLRLLAAV TDKNLWDIVY NADLANWKDS MATLCTYANP TEFPDLCEAL
GDRIIDSGGS RKNASFCYLV GSKLDKVISI WISELHEQEQ EGLQKPGHDT NFSVHAHLLQ
NFIEKVTVFR KVTNFADTEQ DSSDGWKLGP LYERYVEYAD ILASHGFLDT ADKYLNLLPV
QYLAADVARN RVKQASKKAT LQSHARQQQP TVSRTVPRPQ QTSSYPSQQR PVEPSRVANP
YAPSPSALAP NPYAPSAPAY GSQQAYAPNQ SQGNYGSSSV PPTGFSQDNA YSQFSAPPRN
TTPSQPPPSK SKDMTNWNDT PMVTKPSISR RGTPGTAPAP ITSPFPNQPN LNVPPSAPPF
GAPPRGTPTP PPPPPKGSMA PRVASPLGAG HPLPFGQASR SSPNPNAYAP PHAHGGQGYS
QTAPPPAIAR GPSPYNAPPS GPPPTNRYAP APAAQQPSQQ VPGQVPPPPQ AGFRPPPPSN
PYAPQQTPQA AYSQQQYQHT QPGPVQAEPP RGAVSTSRPG TSQGQAPKPS APSTKYPPGD
RSHIPAFAQD MVGIFSNDMQ RVASKAPPNF AAQVKDTQKR LNILFDHLNN GDLVKPDTIE
KLGELSQALQ AKNYDMASRI QVDIQREKLD ECGNWMLKVP NSASPRSTLP KYEVVTTWSL
RLVSTGSRDD DARVDMNANQ SLPTEGQEAS RLPETGLLRR AYGAPALYAP DQRPVAIHGR
NGQQLPGRGR TLSHSPSMPH GKKKGHWDHT AMEYGSGDSS NRAMFSALTP QSLLKSGASR
SAKAQQDRDL TTGKCMTCDS MVRWPKGLAV FRCSVCVTIN DLTPIGTIQD SGSDHRRHGT
RESASSQNYS QSRASPITVH KTSSLIERCI QTYLVSRLGG DEDSYLAREK QSSDALTCYE
TSEDNIYIDP GPDAISQPVC IATGIPENST KTNEASCSEF NHVGCELCLN TEDSKVHTGG
NQYGTMVKGP LHPTERMDKT HVPCPNDGAR NIFGPLEDYI VASFQSHDCI NGSFSTKLAS
FDPRVSSEKS LEFTGPALDK KQQRTPDSMP LMGSKTVLKD LTENEAWHTG GCAIPNHPNG
SVPQGGSTEI ANGAAALNEV NKNSPQIDWN ELCQWYDLII HVGDDWGPHM DEILSSVGFG
LDSPSVDEMN HIKDEVAEAQ RHTRQVLLKA TEGLLKRPGG LLNEPSNIRF LLIILANPLL
YSSSSPSFSK NKRPVRSLMT PEDTGTGPGN HSGIIKRILG LLSNLPNECH HHLVSWFSEF
SEVHFQRTTE LVGSFVTYRL TRQNDRRRDT GHDPTGGLVP NIPSSGHRTT AALHAELSGR
GQSAKFSTEK QSKVKYNDDW QIRAAARVMA LLFAANNNGS HRHNGLLPPL SLEEHRHIVT
IPHERIYHHK QILPTSHFYN TLLDYSDLIA DFEAWEAKRG KFTFCQYPFF LSIWAKIQIM
EHDARRQMEI KAREAFFDSI TTRKSVNQYL VLKIRRECLV EDSLKVVGEV VGAGGEEIKK
GLRIEFKGEE GIDAGGLRKE WFLLLVRDVL NPEHGMFVYD EESHVCYFNP SSFETSDQFF
LVGVVLGLAI YNSTILDVAL PHFAFRKLLA AGPSSLPGSP SHAKPTMVYT LDDLAEYRPS
LARGLRQLLE FDGDVEETFC RDFVADVEKY GKIHQVPLCP DGENRAVNNS NRSEFVNLYV
KYLLDTSVVR QFEPFKRGFY TVCGGNALSL FRPEEIELLV RGSDEPLDIL SLKAVSVCEN
WGVPNPAETE PVIQWFWQSF KNADPKDQRK LLCFITGSDR IPAMGAANLL EHVSTCCRCG
GTALAQN
//