ID   SEC31_NEOFI             Reviewed;        1263 AA.
AC   A1DHK2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Protein transport protein sec31;
GN   Name=sec31; ORFNames=NFIA_088150;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The COPII coat is composed of at least 5 proteins: the
CC       sec23/24 complex, the sec13/31 complex, and the protein sar1. sec13 and
CC       sec31 make a 2:2 tetramer that forms the edge element of the COPII
CC       outer coat. The tetramer self-assembles in multiple copies to form the
CC       complete polyhedral cage. Interacts (via WD 8) with sec13 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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DR   EMBL; DS027696; EAW18859.1; -; Genomic_DNA.
DR   RefSeq; XP_001260756.1; XM_001260755.1.
DR   AlphaFoldDB; A1DHK2; -.
DR   SMR; A1DHK2; -.
DR   STRING; 36630.CADNFIAP00008199; -.
DR   EnsemblFungi; EAW18859; EAW18859; NFIA_088150.
DR   GeneID; 4587314; -.
DR   KEGG; nfi:NFIA_088150; -.
DR   VEuPathDB; FungiDB:NFIA_088150; -.
DR   eggNOG; KOG0307; Eukaryota.
DR   HOGENOM; CLU_003033_2_0_1; -.
DR   OMA; NRYAPAP; -.
DR   OrthoDB; 100998at2759; -.
DR   Proteomes; UP000006702; 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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR040251; SEC31-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR13923; PTHR13923; 2.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW   Protein transport; Reference proteome; Repeat; Transport; WD repeat.
FT   CHAIN           1..1263
FT                   /note="Protein transport protein sec31"
FT                   /id="PRO_0000295441"
FT   REPEAT          5..47
FT                   /note="WD 1"
FT   REPEAT          66..109
FT                   /note="WD 2"
FT   REPEAT          118..158
FT                   /note="WD 3"
FT   REPEAT          164..204
FT                   /note="WD 4"
FT   REPEAT          208..251
FT                   /note="WD 5"
FT   REPEAT          255..295
FT                   /note="WD 6"
FT   REPEAT          298..338
FT                   /note="WD 7"
FT   REPEAT          382..407
FT                   /note="WD 8; interaction with sec13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT   REGION          488..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..1159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..505
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..822
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        869..886
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        922..938
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        973..1025
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1033..1065
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1132
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1263 AA;  136326 MW;  5D1515D8ABD2EE2A CRC64;
     MVRLREIPRT ATFAWSPGAA SPLIATGTRA GAVDVDFSNE TCLELWDLGL SSQDASQELQ
     PIAKIGTDSG FNDLAWTDSE DNSRGVIAGA LENGSLDLWD ADKLINGSSD AVISRMTKHS
     GAIKALQFNP KHSNLLATGG AKGELYISDL NNIANPYRLG SAAARADDIE CLDWNKKVAH
     ILVTGSSAGF VTVWDVKTKK ESLTLNNMGR KAVSAVAWDP EKPTKLITST PLESDPLIYV
     WDLRNSHAPE RTLKGHESGV LSLSWCPQDP DLLLSSGKDN RTLCWNPQTG QAYGEFPVVT
     NWTFQTRWNP HNPNFFATAS FDGRISIQTV QNTRTDTARA IADQNQALDG ADFFAKAQTQ
     PQVSNFSLPK APKWLERPCG ASFGFGGRVI SVGLIEKGKR ASKIKITPFE VDEAVAKSTE
     TFENALKEGD LRSICENRAS QAASDEEKAD WKVIEALISE NPRKGLIEYL GFQDQADETA
     DKLAQLGLDK EDDEVNGESA KESRGSGAKK HKRLQSMFDA NPEADNFLSD LAASKGAKTN
     NPFQIFNGSE TEADKGITRA LLLGNFEKAL DVALKEDRMS DAFMIAICGG QKCIEKAQEH
     YFSKQTDGPN YIRLLASIVG KNLWDVVHNA DLSNWKEVMA ALCTFADDNE FADLCEALGD
     RLEEQIRSTE DKSLRKDASF CFLAGSKLEK VIAIWIEELR EYEQKSIETA ADDTSFSIHV
     RALQSLIEKV TIFRQVTKFQ DTERTKDADW KLSMLYDKYI EYADVVATHG RLQVAQKYLD
     LVPEKHPEAE IARNRIKLAM RHATPQRSQQ TVPTTRTPVN KPLPQASMYP AQPAFSATAA
     APAAATTAPR NPYAPPTAAT AQPVNPYAPP SAAATQPQTS NSYAPIGGGG YTPAGYQPLQ
     PPTYGAQPLG GSVPPPPRAS NQSPATVTTY TTATNLPAWN DLPEGFTKPP TSRRGTPAAA
     AATISSPFPN QSPTLSQGPP PPGAPPTQRA PSVPPPPKGT APPPRVTSPP TNLPGPSPAA
     NPYASLPQSP PMGSAMGVPP PASIPRGPSP YNAPPSMPPP SNRYAPSPAA QAASPQLSTR
     APVPPPPHAA ASPYASQPAS HPPPANPYAP STPPPSQLPM QQAPPPQAPP SRPSTASSQR
     KAAPAPPKYP PGDRSHIPSD AMPIYEILSA DMQRVKSRAP SSFKAQVEDA ERRLNILFDH
     LNNEDLLKPN TVADMAELAR AIQARDYETA KTIHIDIMTN RTEECGNWMV GVKRLISMSR
     ATP