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
//