ID A0A1V9ZWF7_9STRA Unreviewed; 1241 AA.
AC A0A1V9ZWF7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=THRCLA_05259 {ECO:0000313|EMBL:OQS02353.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS02353.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQS02353.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS02353.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQS02353.1}.
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; JNBS01001144; OQS02353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9ZWF7; -.
DR STRING; 74557.A0A1V9ZWF7; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000243217; 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; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
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; PF14580; LRR_9; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00364; LRR_BAC; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51450; LRR; 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:UP000243217};
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 1188..1227
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 52..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 705..739
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 778..830
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 884..1095
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 84..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1241 AA; 140267 MW; D340CD2C024338DF CRC64;
MISSTASSAL ELLLFSTVGI SLRHPKKHNV QSEDEDDFRE CQRELAAFDV RLAEATEKEQ
PPPPVVPEFV PVLLPPTEAT PAKKQRHGTA DKSKSRPGTV SRGEDATARA ITPSSSAKNL
PDKTPAKKDV ITPAAVAALA EAEAASQTAK DEDEENLGYL RCTLKDKYSD LEACSLDWCT
ELHEIVAMAG SVMDPSKLRA AFRNVRLTKL DMETIDKAFA SLYPQLERID VSDNELRVLE
HLPPSMLEVD AYKNHIAKVN ISCENLVHLG LGLNSLQKCP NVPSRLLSLD LSYNQIIDFP
ALLTALQSLS DLRHLFLIGN PITLCRGYRH ALLTKLPTLV VVDDIALRDN EREIANSTPL
VSQDNPVVDL SITITVMGLP EPSETTPQYE STLELAPAMS TILVPETSAT GNYRIFESPQ
IPLKPNVQLR DSIKFDALIV RVFEVPKPDP TAPDAITSPV LRLSMHVELA AFLKPASLEH
NFGEISTGKA MQLNVISQES NFGGDYQLHA MDQRRKRAME DEPPTAKRCK ANEDEEIKQE
DEESVPDKQL RERNKALRGA LVEKNYRLTF LEAKCHELFA HRHAFDGRFQ VILNHWSSLL
NTLHVLLPDS SRNIESELIA IADMDINVPT GIKCEIDEWF QAGTEPTLHE QAVDAVLDGK
LHEQCDYIKA FVNRLLETTT DTTKVEVNEA LARAIEEKTT ALRTLHATKD ELNTYKRQVQ
ELKRDLDRKE VERHQVCREF ERLKQGNTAA ALPTTPKADG KQPALETTPD ASTPTVDSKE
TLEKIKQLEN DLRKATAAES VIRHSMESTK ALAEEQYARL YNEHINLKEE YSRFKVKCKD
MEVHIHDKWK KKFAKYQADS HKMKSKIDEL AVKNAELRSR IVTYTSYKEQ MREYQKLMAS
YERQVASLQE QLKGTEKYRQ YVVDAKANFE SSTVNALKSQ LDALEKSHEA LQADIKSDEL
KQVAAHEKSL RVELAAVQNK LVDTETALDS MTRQLELRKD AMVNHEAELN SIVGEVDAVN
REMEALRSQM KKTLSKLNEK ENAMAKLAQT NIKLEQANAV SFDELAGVRL QVAALQGLQK
QHKALEQGFN DVMKQKENEL LSLQAYVNDV LRMKDDAEKE RIRILREFQF YQKTTTAPIK
PEKPETPPPC EKCQEREAAE QEKPKEGTKE MTELERFELN DLRKKLRCSV CQDAVKDVII
SKCSHMFCKE CMDNNLKARN RKCPTCKKMF GQDDLKSVWW T
//
