ID   A0A0G2IYD1_9EURO        Unreviewed;       843 AA.
AC   A0A0G2IYD1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS51873};
GN   ORFNames=EMCG_00761 {ECO:0000313|EMBL:KKZ60474.1};
OS   Emmonsia crescens UAMH 3008.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX   NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ60474.1, ECO:0000313|Proteomes:UP000034164};
RN   [1] {ECO:0000313|Proteomes:UP000034164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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:KKZ60474.1}.
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DR   EMBL; LCZI01001536; KKZ60474.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2IYD1; -.
DR   VEuPathDB; FungiDB:EMCG_00761; -.
DR   Proteomes; UP000034164; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd20339; BRcat_RBR_RNF216; 1.
DR   CDD; cd20353; Rcat_RBR_RNF216; 1.
DR   CDD; cd16630; RING-HC_RBR_RNF216; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   InterPro; IPR047545; BRcat_RBR_RNF216.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR047546; Rcat_RBR_RNF216.
DR   InterPro; IPR047544; RING-HC_RBR_RNF216.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   PANTHER; PTHR22770:SF47; E3 UBIQUITIN-PROTEIN LIGASE RNF216; 1.
DR   PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR   Pfam; PF01485; IBR; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51873; TRIAD; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          248..467
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   843 AA;  96213 MW;  EC74A1BAFCC2943F CRC64;
     MKRKLPDIID LTSDDEEDAI KASRPSGCIS HPSQPSSKPI SEQNKYDHVY ARVTTIFPGI
     SFEYVRQLHK RHAEANPDID AEEALVNQIM DSGPYPQEEE LVKVEKPPQK PLQPASSKTV
     WSRDDGVVRS DSYYRDAQYL LQLDFPKIPP EYIRSVLQSR KSLFAAYVSL DQAESTYDTT
     NPPLYKRLRS RISNTREIPP NVPMNSDRLR ELQDAREERQ KREESRRREK ELAKLEAQNE
     ATCIAQGNVM ECQCCYADIP INRMIPCTGE SIHFFCKECV KSTAKTQIGV LKYEVKCMDM
     SGCSASFDKQ ILAKVLGESL MGKLEQLQQR DEIAKAELEG LHDCPFCDFK AICPPVEVDR
     EFRCQYPGCR KVSCRLCGLE SHIPKTCEQA NDKKTPARQK IEEAMSEALI RTCPNPKCKV
     KIVKEDGCNK MMCVKCRSVM CYVCKKDITA EGYKHFGKPP KRCPVHDPKS NARHFEEVSS
     AHKKAIEEVM KVNPQLNLEE LAVEAPKKEH HTPSTLADHH MYLQHLQNQQ QHYNALLRRG
     RIPGAPLYPV QPGAGDPGDG AQVPIHAPVD RNHPQPVAYP QPFPIRNGAN QPDPFGRVLE
     WMNVVEQPPR QPIVQYGFQQ AGLRNQGADF QIIPPPVMQP VPYYQPFQHE PNVQALHHNN
     HHHHHHDGHL PQGGHVEQAA PIPRHQPLEA LNQNLNQHLN QGQRTHQVPQ HLQAQHLPQK
     PERRPQFQTH QHTRHPQQAP LAPIYPTIQI GPNLVPTPPQ RWDQWPNEPL VMGGAPERNH
     TYKQTEFMRP SPQPTQPAHM HARPAISGRH VVSNHNNTHN NNRPTFRYPI DIPDIVPQQF
     PRN
//