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Database: UniProt
Entry: K1WN55_MARBU
LinkDB: K1WN55_MARBU
Original site: K1WN55_MARBU 
ID   K1WN55_MARBU            Unreviewed;       307 AA.
AC   K1WN55;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=FYVE-type domain-containing protein {ECO:0000259|PROSITE:PS50178};
GN   ORFNames=MBM_02347 {ECO:0000313|EMBL:EKD19110.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD19110.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD19110.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD19110.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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DR   EMBL; JH921431; EKD19110.1; -; Genomic_DNA.
DR   RefSeq; XP_007290236.1; XM_007290174.1.
DR   AlphaFoldDB; K1WN55; -.
DR   STRING; 1072389.K1WN55; -.
DR   GeneID; 18758282; -.
DR   KEGG; mbe:MBM_02347; -.
DR   eggNOG; KOG1729; Eukaryota.
DR   HOGENOM; CLU_082207_0_0_1; -.
DR   InParanoid; K1WN55; -.
DR   OMA; LDQDANY; -.
DR   OrthoDB; 38671at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15760; FYVE_scVPS27p_like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR47794; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR   PANTHER; PTHR47794:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          190..245
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          15..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   307 AA;  33786 MW;  CF399022AA2DAF1E CRC64;
     MFLEKSDQQI SILSFMSDNN PQRSQRPTTA PMANGFAMPV QPFTASPTQY TLFNSQQTPP
     INPETATPSN TSPTSPRSGV PAHVQQQSSH LRPRKSPMYV PAVLRATEPP RRTARQSPLT
     PPLSKDNNLD EWETARTLSR KQSGDSGKSG LGEIVEAEWS SLGLGEVTAL PTRKHWKPDA
     ESAICDDTTC HAYFGLLSRK HHCRRCGNIF CGRHSSHAVP LDQDANYHPE GAKVRACEYC
     YGDYLRWKIA LSSRSNSESS DPNEPPTPTV SCPASRVARL GSVFGMGPGE PQSLAASVPR
     DWHWSTF
//
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