ID   C5KKG8_PERM5            Unreviewed;       510 AA.
AC   C5KKG8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=Pmar_PMAR023405 {ECO:0000313|EMBL:EER15080.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EER15080.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) 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}.
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DR   EMBL; GG673688; EER15080.1; -; Genomic_DNA.
DR   RefSeq; XP_002783284.1; XM_002783238.1.
DR   AlphaFoldDB; C5KKG8; -.
DR   EnsemblProtists; EER15080; EER15080; Pmar_PMAR023405.
DR   GeneID; 9061963; -.
DR   InParanoid; C5KKG8; -.
DR   OMA; ASRQKTC; -.
DR   OrthoDB; 53681at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000007800; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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; PF13920; zf-C3HC4_3; 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   Ligase {ECO:0000313|EMBL:EER15080.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800};
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          435..474
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   COILED          123..164
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          201..228
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   510 AA;  58123 MW;  01360B25FC0C412E CRC64;
     MLSARESTSC TALQESLSAM KRDRDVWRDR AAKLETDHNS KIELLQQKLN ESQRIGNSCS
     ETMRERLMRS ASEVGSLRAE VTKLKADCDA SVAVNKAREE RYKVMEEFFS TYQTDLDARQ
     EECRNLHDAE KEATAKMLKM EEERREDVRK AERLEEERAV LKEQKQCRCL ASNESLKSVC
     HKMASSLVKT QVDLEYKSAE LARIQQLLDA EQRHSTKLKE RMASLRKQVD TVVSGVDDHK
     SEFSRLSQAA KVQELQNARV VDNYWDALRQ KNESLGIIQR LTEERDALQK HVQALESAHR
     QANGASMQEN QLAQQSNNNS LAAMGQCRMQ LETIVAEQKE KMESFKSTIT MLKGVADKCQ
     ADCREKNKRI LEVEKTNIRL TRQLEKARSL GSGHVVGVEG SGQSPSPGAV VDDKAQAMSI
     IEQEEVRAYR LKVKCSICQQ NDKQVALQKC MHCFCRTCVN ETMIQARNRK CPLCGQRFSE
     SDVRTSLCIT SKDDDSSLGE EDEHRRFLND
//