ID A0C774_PARTE Unreviewed; 628 AA.
AC A0C774;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=GSPATT00035771001 {ECO:0000313|EMBL:CAK66641.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK66641.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK66641.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK66641.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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; CT868046; CAK66641.1; -; Genomic_DNA.
DR RefSeq; XP_001434038.1; XM_001434001.1.
DR AlphaFoldDB; A0C774; -.
DR STRING; 5888.A0C774; -.
DR EnsemblProtists; CAK66641; CAK66641; GSPATT00035771001.
DR GeneID; 5019823; -.
DR KEGG; ptm:GSPATT00035771001; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_435798_0_0_1; -.
DR InParanoid; A0C774; -.
DR OMA; ASRQKTC; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
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; 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:UP000000600};
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 575..614
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT COILED 121..170
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 260..483
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 628 AA; 74647 MW; DBBA38121BC18905 CRC64;
MKTKKKNESQ RVTELGEHIL KTQNTMLAAK IDQLKKEIQN MKSLPEQTEI ELIQSEELLH
YKKLSNQLSR RIRIIMAYNE EAIQKKVAQE DIQDEKFECL CGANQIDSIK YFLVNGHPQI
LQQQQQEIQQ PEENNQQTQS NQKDYIKKLI QESSEEKAQL LHQIEELKLQ QKLPEEQFFQ
TQLFAELVQQ NNYLTTTLFN IEEQLIQVQL ANKDLLEKSQ QQIQQCQLEC EQKIRELFSQ
QDIIKIEVKQ NDDQTQNTLI EELKSQVEHS SKMIEDLKIE LQQCRERNKE AHNQLGEIIN
QKQTLLNQNN ELKQYISVHK ILSKDEKIEQ VTLRYEKHKQ LLYEIEQEYA NTKSNEFIQR
FREFVGYVKM RDEKVKGLEQ QLEAKINDCN NIKKQIQQLI DELDYNSNSF NSINETNKNL
SKLVNETQKN LSRAMQEKVD ERIKFETERQ QFQQKIQTAD ETIKQLQSQN DQQKKLLNLF
DNERMIYKES IRNLQKSDGE SQQKLLQKEW DVGKILEENK IIQEREKLSE SINLKFIKKA
EKSKSKLKYL KLQMKLESKD TDNELLTSLK MMVDCQQCKK RVKQVILMKC LHMFCKPCID
DNQKNRNRAC PVCRAKYGIE EVKAIILN
//
