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Database: UniProt
Entry: R9NWP5_PSEHS
LinkDB: R9NWP5_PSEHS
Original site: R9NWP5_PSEHS 
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
//
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