ID A0A137Q368_9AGAR Unreviewed; 501 AA.
AC A0A137Q368;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=E3 ubiquitin-protein ligase cblA {ECO:0000313|EMBL:KXN81692.1};
GN ORFNames=AN958_03939 {ECO:0000313|EMBL:KXN81692.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN81692.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN81692.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN81692.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ963206; KXN81692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137Q368; -.
DR STRING; 1714833.A0A137Q368; -.
DR OrthoDB; 75723at2759; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; PTHR14879; CASPASE REGULATOR, RING FINGER DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR14879:SF5; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00184; RING; 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:UP000070249};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 17..81
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 447..486
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 150..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..228
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 56345 MW; 8DA01BFC9BFE638E CRC64;
MTSLHGIPLL SGPSPTVDPS DACRKCNKEF NFLFTRSRKC NHCGYSYCHS CSDFQALMPR
PGPESGYDPV HVCGYCIEFL NMTAAGPSQL RGMSLSKLKL YADSYNIDIS RAVEKGDIVE
AIVRARLPNG CLPSVKEDYY RKHKVPNLHA GARPRSFFSR NNPADSPPPV PPRPQGQPGS
GSYRYGPTMD DIPNISPPRF PQPHPTPHNP HQSPGGPGHP PPPFFTHQTS PYPTYQFGRP
TQQAHYHQSP PYNTYQHQPP PPPPQETRPP PPPRPNTTTA HRPPPPPRPQ PTAAPQTPPR
QRTTSTPPRP ATQPQTSVLK NILFTNHVNA SMILEKSELV SKVMTLVEDE KRERERQRMA
EEAERLEMEE RRREREEAIR REQEEKRRQE EEERLRNERR RRHRTRSNEP AGGGQSEAST
SASPPKTSAT TTPQKPFTSS LDRSGLCVIC QDEEANIAIV DCGHLAMCRS CSELIMASSK
ECPLCRTRIV TEARLLRIFK S
//
