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Database: UniProt
Entry: A0A139GYR8_9PEZI
LinkDB: A0A139GYR8_9PEZI
Original site: A0A139GYR8_9PEZI 
ID   A0A139GYR8_9PEZI        Unreviewed;       855 AA.
AC   A0A139GYR8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN   ORFNames=AC578_10471 {ECO:0000313|EMBL:KXS95311.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS95311.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXS95311.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS95311.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXS95311.1}.
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DR   EMBL; LFZN01000222; KXS95311.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139GYR8; -.
DR   STRING; 321146.A0A139GYR8; -.
DR   OrthoDB; 1462937at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR036028; SH3-like_dom_sf.
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   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR   PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   SUPFAM; SSF50044; SH3-domain; 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:UP000070133};
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          25..79
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          100..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   855 AA;  95231 MW;  5C6D61033ED3C415 CRC64;
     MADNDGGGSS GGGGGLLDLE KELQCSICTD VLYQPLTLLD CLHTFCGACL KEWFTWQATA
     ATTSRNRHNP SPYTCPQCRE HVRGTKADWR TTTLLEGFLK ANPGKAKSDE EKEESRQQYT
     PGENVLLAVQ QRVEDTDSED ERLLAEVREL SMAHVDPETA RRRAERVARR RQERSQRHPR
     PEELGSQQQS SRWVAHQAAR QREEDERQVE HQPSLRSLLS DSEISSADVQ EEILQSISSE
     GLLDGIDIDH LTPAQEEELT ERIAEAYRRR QRNRDRSRNR DRGENQHETP QPEPRRTVES
     SGRRAPSPPQ QTQTQTQTRS RPPISRPHLF EQSSAGAERG QRRSASSTSQ RTRQSEVRET
     TSSQPPSAAR STTDIAVPSQ TNGRSTSQSR PRALSGNSRS STDPAGVRDN VQRVRAASNS
     LRPDSHSSTA ASRPRSRDSQ SSQPGRRRPG PATSDSVASR PEPPPSTTFV ARPQTSPTTN
     QQSVRPAASA SAFAPESAST LSAFPTIACS CCQRPDLAQS LHYNCSKCDS GNFNLCLSCY
     RDGRGCRHWF GFGLMAMYRY RRAQEEGSGQ YLSGYEYPHL LTPRKYMQAS QPDSSPELQE
     GAFCEHCLKY TNDCYWYCEI CLEGAWGYCN TCVLRGNHCT HPLLPLAHIS TLRNASHDPS
     KLAFLPVPHL KQHSYVLLPV LTDCDICRLP IPPRATRFHC YTCSDGDYDI CNDCYNSLVA
     MGKISSKDGP DGWRRCLNGH RMSVIGYQDT PYGGGQRRLT LREMVGGWRL KEEGTPSGGD
     AVLVAGRTAV VPPDGGVGYK CLAQWSRWPK EGDVDELAVP KNAEIRECED RNSDWAVGVY
     DGTVGLFPVN HTRKI
//
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