ID W3XCT5_PESFW Unreviewed; 292 AA.
AC W3XCT5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 28-JUN-2023, entry version 39.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=PFICI_05695 {ECO:0000313|EMBL:ETS83819.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS83819.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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DR EMBL; KI912111; ETS83819.1; -; Genomic_DNA.
DR RefSeq; XP_007832467.1; XM_007834276.1.
DR AlphaFoldDB; W3XCT5; -.
DR STRING; 1229662.W3XCT5; -.
DR GeneID; 19270708; -.
DR KEGG; pfy:PFICI_05695; -.
DR eggNOG; ENOG502RMFV; Eukaryota.
DR HOGENOM; CLU_049340_0_1_1; -.
DR InParanoid; W3XCT5; -.
DR OMA; VHQERMY; -.
DR OrthoDB; 2785713at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0000795; C:synaptonemal complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR042448; CCNB1IP1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14305; E3 UBIQUITIN-PROTEIN LIGASE CCNB1IP1; 1.
DR PANTHER; PTHR14305:SF0; E3 UBIQUITIN-PROTEIN LIGASE CCNB1IP1; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 12..52
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 204..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 129..187
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 292 AA; 32389 MW; 30FFAF87C1B510EE CRC64;
MEHTLRCNAL KCRRELTDKA LVTTCSHIFC TECANRLGLT DSSARHSCPA CNVPLTNPDD
AVITNLKPTE DYKTSVLSGL SPNIIVECAS RALNFWAYQT IQQIIYQEHV SKALADKYTT
LTVDLDKVIS EANAQITTLN NKVSRTQDMD LDQQALRRKN EELALALKEK NKKLMQTQEL
YDKLKRRAMM GQMQHAAEDA VDSNLPSLDA RDGGGQGSTR GGDGTVLGLH EGGMGPIFPE
SRNVRIHNNT HDNMNHARSF NHRKTSLYPW GQVASGPGGK CHFLINSITC SY
//
