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Database: UniProt
Entry: A0A0N0NQY5_9EURO
LinkDB: A0A0N0NQY5_9EURO
Original site: A0A0N0NQY5_9EURO 
ID   A0A0N0NQY5_9EURO        Unreviewed;       698 AA.
AC   A0A0N0NQY5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=AB675_8240 {ECO:0000313|EMBL:KPI44458.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI44458.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI44458.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI44458.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|RuleBase:RU365038};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365038}.
CC   -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC       ECO:0000256|RuleBase:RU365038}.
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:KPI44458.1}.
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DR   EMBL; LFJN01000003; KPI44458.1; -; Genomic_DNA.
DR   RefSeq; XP_018004421.1; XM_018148671.1.
DR   AlphaFoldDB; A0A0N0NQY5; -.
DR   STRING; 1664694.A0A0N0NQY5; -.
DR   GeneID; 28740551; -.
DR   OrthoDB; 53681at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000038010; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   CDD; cd16499; RING-HC_Bre1-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR013956; E3_ubiquit_lig_Bre1.
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; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR   PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR   Pfam; PF08647; BRE1; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|RuleBase:RU365038};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW   Transferase {ECO:0000256|RuleBase:RU365038};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          649..685
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          48..75
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          155..210
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          253..421
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          530..631
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   698 AA;  79408 MW;  C94573D617AB838F CRC64;
     MEDRKRSMPY DQGDGPATKK QALAPNGVGK PHPDTDMPWK DDLERFTKDA ILRQMNEYKR
     EKNTLKSELD EIRKKTRHHD DHIRAIDAWF KQLLDEVKTM SPGDDDEDME LSTLPTSLLF
     EDQPHLEQHI TKRTKEVRTI LGKLLSRSKN FTPDVVELQK RISELQAEEK SHLLELETLR
     AEVANIELRL ETATERYVVA EKKVERAKSV TVAKLEKQLK GGMKGSDDGV KKEELKNGVG
     ETGEDYTRLE TEHNKVLAAS EVLKEQVEKL QEETTKLQSE VTAANAKSAT LSDEDYSKTD
     LFKQFKAQHE DVIKKLNDLD ARCTQLKDEN RMLLQERTSY QNKLDDETRA TVAEKDTQLG
     QVEKDLVRIR AERDDLQAKL SMEKSKNEEK LEAVFKVREL CEAQEERIKS LESETQRLQG
     TSAMDVDDAQ LEGLGPDEIR TKYQSLNQNY KMLSSELTSM SAAYQKASKH AKQNTLKAGE
     QEDKVQRLVA EKAKADQKYF AAMRSKDARE QEIRTLKLQT SKSSDIALQL KEAETASKAL
     IANLEKQLSD MKEAHSSKTS DCRALQNEKD SNALELSRLK KQITDLTQQL TAKDAEISGK
     SAATRTAEVE VKQLQSVLDS TRKDLEKWKS RSGQSDVVDD LHSIVFCHCK KNMKDTVLKT
     CGHVMCSSCV EERVASRSRK CPLCSKSFGS NDYMRVTL
//
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