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Database: UniProt
Entry: A0A0D2K744_9EURO
LinkDB: A0A0D2K744_9EURO
Original site: A0A0D2K744_9EURO 
ID   A0A0D2K744_9EURO        Unreviewed;       618 AA.
AC   A0A0D2K744;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Z520_05415 {ECO:0000313|EMBL:KIX98954.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX98954.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX98954.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX98954.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; KN848070; KIX98954.1; -; Genomic_DNA.
DR   RefSeq; XP_016633077.1; XM_016775918.1.
DR   AlphaFoldDB; A0A0D2K744; -.
DR   STRING; 1442371.A0A0D2K744; -.
DR   GeneID; 27711161; -.
DR   VEuPathDB; FungiDB:Z520_05415; -.
DR   OrthoDB; 251172at2759; -.
DR   Proteomes; UP000053411; 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; cd22584; Rcat_RBR_unk; 1.
DR   CDD; cd16449; RING-HC; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR22770:SF13; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
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, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          171..373
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          175..217
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          11..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  68858 MW;  CAEB04795F43E221 CRC64;
     MRCGNALLAR RQRTERHTVQ TSRDPGTGTT LDKQVPARST VTLRRTRPAS PASERNVRLR
     EEEMNQFLSF WRGESDTLTL FDIEMAEQTA NSSPRTTSRP YLDLSPARIG APLPDTEVAV
     GDTTLAEVMP GRLPENHQEM LKQRANPSHS NRTRQRRRLM LSELCSPGDG DPVKCRACFD
     EVAAPISLDC GHSYCRSCLN QLVRAGTANK MSWPPRCCFS WPRVDIGSIQ PHLDEEVFSR
     YLNVFEEYST RDPVYCSNKF CSLWIPSSQI QDNKEKFVSC TKCRVQTCVE CKQGHDDHVG
     AEGTTCKNLE ELMDERDRKL AETKLWKQCP SCKNLVERID GCDQIQCSCG TRFCYKCGTN
     TSSVTQCRCY PPVYPFWGAR QRPRQRLGTS QRRASRKFAS GSGFSEPNAS SSSVPLSGER
     LPPAEASRPA KLPHPPRCGL RRGLHANSGV SATDPHVNTP GLQKTTQPEP TLYSSLAWAL
     PGYHEWDMRE AGNDEAAPPE STYGDSKSTF GALGTSGYVS IPSHPTNADW LAAPAMSPSF
     EQQHWQSSQS QGMLTGTPRL VSAMQPLPFT AFPGGSQTWS ASTFQHSDPS LLSGHMNQPR
     VDRYMVNHFR DANVGWLQ
//
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