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Database: UniProt
Entry: K1W4K3_MARBU
LinkDB: K1W4K3_MARBU
Original site: K1W4K3_MARBU 
ID   K1W4K3_MARBU            Unreviewed;       538 AA.
AC   K1W4K3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Fyve domain containing protein {ECO:0000313|EMBL:EKD11885.1};
GN   ORFNames=MBM_09964 {ECO:0000313|EMBL:EKD11885.1};
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:EKD11885.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD11885.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD11885.1,
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; JH921479; EKD11885.1; -; Genomic_DNA.
DR   RefSeq; XP_007297853.1; XM_007297791.1.
DR   AlphaFoldDB; K1W4K3; -.
DR   STRING; 1072389.K1W4K3; -.
DR   GeneID; 18765899; -.
DR   KEGG; mbe:MBM_09964; -.
DR   eggNOG; KOG1729; Eukaryota.
DR   HOGENOM; CLU_022550_3_0_1; -.
DR   InParanoid; K1W4K3; -.
DR   OrthoDB; 38671at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd16489; mRING-CH-C4HC2H_ZNRF; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23164; EARLY ENDOSOME ANTIGEN 1; 1.
DR   PANTHER; PTHR23164:SF30; LD23155P; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
DR   PROSITE; PS50089; ZF_RING_2; 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:PRU00175}.
FT   DOMAIN          198..292
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          491..533
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   538 AA;  58065 MW;  710B6F0694E55071 CRC64;
     MNSARVSATV ASTRERPLPP LPIEELEVSA AVDIPDNTAR SLSNREDREH GGSKEEISSH
     AAGNSIVKSR ANSASAAGSG TSTAAAASLD EGSFQPASSQ NQRSSGGNSV TESNVPIGAA
     SNPPAYQAQE DSHSQATTPI RDVDIETRPH GGSSGSDSPG DTPLLSRTSI RYRRRPRLAG
     RANSTEQSQV LVPRWQPDAE VTLCPICRTQ FSFFVRKHHC RKCGRVVCGS CSPHRITIPH
     QFIVQPPSEA TSPTKYPRPA LDAGRVGSFT AVENLGGGER VRLCNPCVPD PNVAPPQVAD
     NRRRPSHQGH SHSEGNTATS TNSPSIQSTQ IPTLPSTFPR RPRQPSNSSL FDQSHSGTGG
     GSRQPRAPLP RPTPEARPPL NEEDECWVCH KELPSKSLPN WETARQNHVM NCVLEASTNT
     STQPYPAASS SRTPPVQIPT ANTPEGRMVA RESAHAAVIQ AAQSSHTPPM RRSGCFPYVA
     SEKDCVDDAE CTICMEEYQV GDKMGRLECF CRFHLHCIRD WFVHHPGQCP VHQHGAGY
//
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