ID A0A427YLK2_9TREE Unreviewed; 813 AA.
AC A0A427YLK2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=EHS25_009299 {ECO:0000313|EMBL:RSH91929.1};
OS Saitozyma podzolica.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Trimorphomycetaceae; Saitozyma.
OX NCBI_TaxID=1890683 {ECO:0000313|EMBL:RSH91929.1, ECO:0000313|Proteomes:UP000279259};
RN [1] {ECO:0000313|EMBL:RSH91929.1, ECO:0000313|Proteomes:UP000279259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27192 {ECO:0000313|EMBL:RSH91929.1,
RC ECO:0000313|Proteomes:UP000279259};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Saitozyma podzolica DSM 27192.";
RL Submitted (NOV-2018) 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:RSH91929.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RSCD01000007; RSH91929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427YLK2; -.
DR STRING; 1890683.A0A427YLK2; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000279259; 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:UP000279259};
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 760..798
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..87
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 527..554
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 583..652
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 702..729
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 813 AA; 91164 MW; A850D5BBC95B3E9A CRC64;
MNADLKRVRD TSLEDAPSPT AKRRALSFSS PPIDSSDDSG MEDWMKVVEV RRKEAIYRQM
LEYRRSYEEE ARRADALEAQ RRVLEASVQA VEVCWTQLVN AVRDLAGRQD NEIKDEQVLE
PVLEPRIAQP ALGEALAKRL PQTKQLIHRF VDLASRNSIQ PTGNEELQRR CQTLQAEASS
LRSNSALLQS QISTLTESRD TYHRDLQKAQ KALDRQRMEH DKAEVEWSQA RDRDNEAGTP
GPGRPNGSGH ATPNGKVEED VKPLGNGAAP ALLPDTTELE QLAQSRLQQL ETLRADHVAL
QQEHDRLKQL AHHPSEAALR ESPFFQIYLH QLSTHTDRAN YFQTSFQAAE ANLDKLRTSN
QDFRDAVNAE AKAESDALRQ QIAKQNSDLA RLRGQRDEMN AELTERRSRE TEKMRHGEQM
EALASSRQDR IGFLTSEVRR LKGRLGAEAG SKGYLEFLRE GGIDGDYVKD LEARVADAEG
RATALSQTTD TTAQAEGEAR VELEKARRAL DKYELVLGPN PDAAGDITAL AQRLEAADKD
KAALQLQLGE AEAATNALYT EVEGLSKLWE ASERTVSSKV FELKDTELKI ARLQTEKAKA
DNKYFQAMRS KDAIDAEGKL AQRTVEKQLK LLERAQEVER SLNAQISAYE KALTSVKNDA
LALQTQLAGV AAEKTQLEVR LQHSQSSLAD AQQIMHQRVA EANAEKAARD RLQEEVEAGQ
RAVKKLKERQ EIVSASGGSV SANEVQMKDE RDKLLKLLRC SCCEQNFKQQ VITKCMHTFC
KQCLDARVAS RQRKCPACGL AFAKEDIQTL YWQ
//
