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Database: UniProt
Entry: V2XD25_MONRO
LinkDB: V2XD25_MONRO
Original site: V2XD25_MONRO 
ID   V2XD25_MONRO            Unreviewed;       599 AA.
AC   V2XD25;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Signal sequence binding protein {ECO:0000313|EMBL:ESK90405.1};
GN   ORFNames=Moror_13684 {ECO:0000313|EMBL:ESK90405.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK90405.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK90405.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK90405.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
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:ESK90405.1}.
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DR   EMBL; AWSO01000444; ESK90405.1; -; Genomic_DNA.
DR   RefSeq; XP_007850289.1; XM_007852098.1.
DR   AlphaFoldDB; V2XD25; -.
DR   STRING; 1381753.V2XD25; -.
DR   KEGG; mrr:Moror_13684; -.
DR   HOGENOM; CLU_455665_0_0_1; -.
DR   OrthoDB; 1602788at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR   Gene3D; 2.10.70.80; -; 1.
DR   Gene3D; 3.30.60.270; -; 1.
DR   InterPro; IPR031777; Sortilin_C.
DR   InterPro; IPR031778; Sortilin_N.
DR   InterPro; IPR006581; VPS10.
DR   PANTHER; PTHR12106; SORTILIN RELATED; 1.
DR   PANTHER; PTHR12106:SF27; VPS10 HOMOLOG 1-RELATED; 1.
DR   Pfam; PF15902; Sortilin-Vps10; 1.
DR   Pfam; PF15901; Sortilin_C; 1.
DR   SMART; SM00602; VPS10; 1.
DR   SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        494..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..490
FT                   /note="VPS10"
FT                   /evidence="ECO:0000259|SMART:SM00602"
SQ   SEQUENCE   599 AA;  66968 MW;  10F042AF615B4E95 CRC64;
     MDPHRQQKEG NQPSQPGLGL ELVEGKKYYA QGERKKLFDS VVGFAKFSEY LVVAELKPSG
     TSLELQVSLD GINFAPGVFP KGMMLDTHAY TVLESSTQSL FLFMTMSDLP PFGSILKSNS
     NGTYFIDSLD NVNRNGEGYV DFEKMIGLDG IALVNVVKDP IEAAITGRKH LVSRITHNDG
     GTWKPLRPPS TDSLGNEYDC KDTSCALHVH GYTERLDPRA TFSSPSIVGL IMAVGNVGSS
     LAPYKDSDTF LSRDGGFTWR EVHKDAHLWE FGDSGSILIM ANDEEPVDHI LFSIDEGESW
     REYRFMADGA GKMRVRFIVT VPSDTSRRFV LLGEYPGGRG SVAVQVDFSA LTNRKCVLNT
     DDPNHDDFEL WSPSEERNEV CLFGRQTLYH RRTPKANCYV GDQAKAKVKI EKNCACTESD
     FECEFNHVRD LETNKCVLVA GASPLPSDQQ CQDDGMWYER TAYRKIPHSS CEGGSRLDRG
     EGHYCPGNLA GHGFFFWFMV LAVPFGLTAM IGMWWWRKSG LARGMIRLPG DSRGLGQSGS
     GVLDTLASVP WFLIGLAGIA YEWITEKIDR VGWRYKHRRG YRNLPVDEDA QILRFEDEE
//
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