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Database: UniProt
Entry: A0A0H1B828_9EURO
LinkDB: A0A0H1B828_9EURO
Original site: A0A0H1B828_9EURO 
ID   A0A0H1B828_9EURO        Unreviewed;       385 AA.
AC   A0A0H1B828;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN   ORFNames=EMPG_16916 {ECO:0000313|EMBL:KLJ07604.1};
OS   Blastomyces silverae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ07604.1, ECO:0000313|Proteomes:UP000053573};
RN   [1] {ECO:0000313|Proteomes:UP000053573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLJ07604.1}.
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DR   EMBL; LDEV01002794; KLJ07604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H1B828; -.
DR   STRING; 2060906.A0A0H1B828; -.
DR   OrthoDB; 2785713at2759; -.
DR   Proteomes; UP000053573; 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   SMART; SM00184; RING; 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:UP000053573};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          16..57
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          207..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          127..171
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        250..268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   385 AA;  42485 MW;  D2BED05C9CEDF4B6 CRC64;
     MAQALDFSLR CNSLKCRVTL SERAVVTTCS HIFCLQCADH LGLSRPTTSE RQCPACNDSL
     ANPDDVVSTV LTPSEDYKTS VLSGLDPHTI MECAGRALAF WTYQSAQEVF YQEYLGKSLT
     EKYGALNQQM DKVIHDSNSE ISNLQNRISE MQINQEQLQK KNHELAEIYR EKCKNHTQIT
     NLYNLLKSRS MRSQIQTAAS DSVTHVLESL GGDPKSHPST EDLFRPVTSL APSPRRSPVK
     YPTANIGIEQ LHRHQRSGNG SGSKNRVDSA MPPPSGLPPS FRTAALPPAT PQHRTRLPGP
     LPSTRRPEYQ ERQQHGYTTH NRIFPVPQRF APEGVDSRFS NNSPGNYGLS TGIKIGRPSD
     HAAPSSDLPS NLFGVGSHIG NGSAR
//
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