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Database: UniProt
Entry: A0A094FFE4_9PEZI
LinkDB: A0A094FFE4_9PEZI
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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}.
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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
//
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