ID A0A2T9YQY3_9FUNG Unreviewed; 820 AA.
AC A0A2T9YQY3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=BB561_002295 {ECO:0000313|EMBL:PVU94739.1};
OS Smittium simulii.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133385 {ECO:0000313|EMBL:PVU94739.1, ECO:0000313|Proteomes:UP000245383};
RN [1] {ECO:0000313|EMBL:PVU94739.1, ECO:0000313|Proteomes:UP000245383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWE-8-4 {ECO:0000313|EMBL:PVU94739.1,
RC ECO:0000313|Proteomes:UP000245383};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
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:PVU94739.1}.
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DR EMBL; MBFR01000076; PVU94739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9YQY3; -.
DR STRING; 133385.A0A2T9YQY3; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000245383; 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 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 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:UP000245383};
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 768..807
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 245..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 195..229
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 591..737
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 245..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 95411 MW; A8AD2569A89FE3F3 CRC64;
MTERKRSLET DTKMQDDVAI LSKKKRNRED DKAIQVIKEF DDNLEQMIDM ENIRNFQKEA
IWRQMNEYKR ESLRDKAKVK EVEEKQRVWA ERIGRMCAIW EGTSEKLKNS LPDSVEWKKL
DSNESRWIRL IFLEKGLYDN SLQSLEEIND PINNLQTKTK DLCSLYELIV SKFSDENFDI
KADKFTLKNY DDSDYFKLQS QLDISELQLN NLKKNLDERE EELLAAQKKF DRSLCPISRA
LDSGKSIDSI EEPETPSKKI DIPQSDSQNT NQIEVASLQK IADGRLIEIK RLSEECTKLK
LEIDKINIGI NSYSKEHISN HPEYIKLESE KNHYYADTIQ QRTETKKLFA ELEELKASRR
TYQAHLQTQE IAQRQVLEQS LQKVQQDLMR VRSHRDQIQR ELEERRMHDS VEKNGHLELQ
TLSDARRQRL IALVLENRRL RAHIASSTGD EKAVDFYTNP PITEDISVTE ELRLEIDKLK
QKLIEIEPNS INYLKENINS CGIQTDNNKS ISHSDINFLN SNGINPAHTK ENSSNDSLNK
SLPDTKELLR IALLEKEELE KTSSLMEHEM QAIISGFSKL EEQVTHKVLN LSSKEQMIHK
LIAEKAKYEE KFLALNKERE ALKGTLSSLK FQNMKQLEHI KNSDERERNL NQQLALLEQH
LLGLRLDQAK CMESLQDANN SIETLKSQLN TSEKTLQSTM ELLKARTSDA EKSSYELARE
KESLIQLQHK VEALESSRIN ANDSSNFSGS NNGNLTELVD QYKALLKCST CRRNFKNYAL
TRCMHVFCKE CIDARIETRQ RKCPTCSEPF GLNDVKQIFL
//