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Database: UniProt
Entry: V2Y114_MONRO
LinkDB: V2Y114_MONRO
Original site: V2Y114_MONRO 
ID   V2Y114_MONRO            Unreviewed;       695 AA.
AC   V2Y114;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Cbs and pb1 domain-containing protein {ECO:0000313|EMBL:ESK98450.1};
GN   ORFNames=Moror_200 {ECO:0000313|EMBL:ESK98450.1};
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:ESK98450.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK98450.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK98450.1,
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:ESK98450.1}.
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DR   EMBL; AWSO01000002; ESK98450.1; -; Genomic_DNA.
DR   RefSeq; XP_007842385.1; XM_007844194.1.
DR   AlphaFoldDB; V2Y114; -.
DR   STRING; 1381753.V2Y114; -.
DR   KEGG; mrr:Moror_200; -.
DR   HOGENOM; CLU_009026_1_1_1; -.
DR   OrthoDB; 1328303at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd17781; CBS_pair_MUG70_1; 1.
DR   CDD; cd17782; CBS_pair_MUG70_2; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 2.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR000270; PB1_dom.
DR   PANTHER; PTHR48108:SF6; CBS DOMAIN-CONTAINING PROTEIN CBSX1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48108; CBS DOMAIN-CONTAINING PROTEIN CBSX2, CHLOROPLASTIC; 1.
DR   Pfam; PF00571; CBS; 4.
DR   Pfam; PF00564; PB1; 1.
DR   SMART; SM00116; CBS; 4.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 2.
DR   PROSITE; PS51371; CBS; 4.
DR   PROSITE; PS51745; PB1; 1.
PE   4: Predicted;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        668..687
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          109..167
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          176..234
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          283..347
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          356..413
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          506..607
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   695 AA;  74881 MW;  F0639ACE6ACE421E CRC64;
     MSRIPLPVSG HSPSQTRSVS SASPVPFPGE RASSPLPPSR HHSTASASMS SLSGLQSETR
     RRQLKKDEAI RRKNEMDLAR KRTISTTQNQ QRSRRGHKST AAKGTVAALR PTPALTVPEN
     ITVAEASQLC AAKRTDCVLV VDDEEGLSGI FTAKDLAYRV TAEGLDPHTT PVHQIMTRNP
     MVTQDTTSAT EALQLMVSRH FRHLPVCNEE GNVVGLLDIT KVFHEALGKV ERSSAASEQL
     FNAMAGVQSE LGNVGSNPQA TAMLAWAEKL REKTALPDLS TVMDSRTQPA TVGPKTTVRE
     VAKLMKERRT TAVCVMEGGT GGMHPRIAGI FTSKDVVLRV IAAGLDASRC SVVRVMTPHP
     DTAPPTLSIH ESLKKMHNGH YLNLPVVEAD GRLVAIVDVL KLTYATLEQM NAVTGEQGLT
     EADGGPMWGR FFESIGGDDT ESMMSGSHIP PELRTLPSNA SLSHIQQSPH SEVHPNDSAS
     VMDDDISALE GPSRHKSAPA VLPVDDGTYV FKFRTPSGRT HRFQSRHDNI EHLREIVAGK
     LATDPFFTEY KPTDEHSTPP DPIDFTLMYT DADGDTVLMT SDHDVTDAVK IARGSHTDRV
     VLFIQGGKGW DEAGAGKSEA KAAEVAAAAK QEVQEVEKTE VPVTVPPPTY APPPPTGPEE
     VMGIPKDLLL PASIGALAVV ILGIFTFSRL TASRY
//
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