ID R9NWP5_PSEHS Unreviewed; 816 AA.
AC R9NWP5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=PHSY_000524 {ECO:0000313|EMBL:GAC92964.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC92964.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
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}.
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DR EMBL; DF238771; GAC92964.1; -; Genomic_DNA.
DR RefSeq; XP_012186551.1; XM_012331161.1.
DR AlphaFoldDB; R9NWP5; -.
DR STRING; 1305764.R9NWP5; -.
DR GeneID; 24105830; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_019713_0_0_1; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000014071; 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-UniPathway.
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:UP000014071};
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 763..801
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 62..96
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 161..216
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 267..294
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 333..502
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 13..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 91653 MW; 22973977C7F93AE9 CRC64;
MLQSMSGADD RKRALVGAAE DGPRKRLHSD EATPRSAATP NNDDDDEEAL HPAYAGLEAF
RKEAIYRKLL EARRDMQRIE RRSATYQDDL AVSEQRAAVL QRFWNLLLTD LATRLALQDQ
DAFASSSSSD SRSDPSAMEQ QLQQQSSAVL QSLSKQGDVN VVELQQKLHD LADEASRHKQ
DLFLTQSKLQ RAQDALAQTT QKLSKVEHEY VRYQSNLLRA TEGKPTVPAG TTVTASEPPP
AAEQPAALDV KKDAAPSSAA EAGPETSEAL QKALEELESA RQDVELTRRE SDSRYAEIQT
LNEEVRTFRY KLHETQSKLT TLPEEVLLNS ALYRELQTSL RHAQQDLQNS REAMQILERE
ASAMREERGS FQQTVEAEAS SRTEDLEKLV KAKEADVTRL RSQRDELNAE LTERRSREQV
KFTQIEEMKA LLNSKEERLT LLSSQVRRLR MTVAAFHGQS TGVSASAADA EEDQFAILSR
EAQQAQARVA ELEQRLGITS ETTAPNGKDA TIKTEDGVET KIKAEADAEA LGESELHAEN
QRLRLSLQAA EASSKAVDDE LEKISAAYAD LERQASVKVT DVSRMEEKAL RWVTEKSKAD
NKYFSAMRAK DAVDADLRMA KQVHERQQKT IEAFTETERN FTAQLGVHEK QVTAFKKTTD
VHVRRIETLE RELELAQSRL AESMRTKEAA SDSAKELINT ANVEKDQRKR AEERIVRLEK
DLESSKRQLA KAAASAAKNK GRRDTDAGEG GSERDFLNAL LQCSSCKERY RNRILTKCYH
TFCSECIDSR VQTRQRKCPH CALAFAVSDV QPLYLQ
//