ID T0R7G0_SAPDV Unreviewed; 1623 AA.
AC T0R7G0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=SDRG_14254 {ECO:0000313|EMBL:EQC27978.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC27978.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC27978.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC27978.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC {ECO:0000256|RuleBase:RU366018}.
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|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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DR EMBL; JH767200; EQC27978.1; -; Genomic_DNA.
DR RefSeq; XP_008618591.1; XM_008620369.1.
DR STRING; 1156394.T0R7G0; -.
DR EnsemblProtists; EQC27978; EQC27978; SDRG_14254.
DR GeneID; 19954981; -.
DR VEuPathDB; FungiDB:SDRG_14254; -.
DR eggNOG; KOG1140; Eukaryota.
DR InParanoid; T0R7G0; -.
DR OMA; KYWLEKP; -.
DR OrthoDB; 53736at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000030762; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR CDD; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF24; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000030762};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 29..102
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 29..102
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
SQ SEQUENCE 1623 AA; 178558 MW; 7A7B7B45020C0ED2 CRC64;
MAATTTTYTW LGALKAAIDG NPAAVTRKRM CGYEFRPGDM AWNCRQCQKD DTCVMCHKCF
TASHAHLTHD VMFYYAQNGN GCCDCGDEEA WSPHGFCPDH NTTEIGNAPP PDILASVPSP
LLAQARADVA SDIKLFHAFA KTRRAGFRRK LPEDGPDTLY DLYVHVPDLN HQGSASLAST
LPESVTLIQR NLSASEVLLW QSKLAKKQPA NLCSIFHSHD MHANLNVVAL CNRLSKCALS
CDVGCRLVAE QMLLPESFLV DVIVADCLFP RHDNEALHSL IMALIPDPDF KQQFAIAFAT
SYPQLFQDFL LGLGLAGHGI LGFGVQFLNR ASFVHLLMHS FGFFGTLLRT LHETLASFAA
PAMDAALPSD VLPLLQPPGR LWDSIATYLS LSSAPNLPDV AVLQSLVPYH RHAPTEAFVD
WFRQAALPLP GRLGLTLDAT GFTSHRYTQV LLDLKYTLQI AHPTLLSSFP NELRLLFHTL
SLAQGLGADA RLQASEPHVA YEGRHWIVAI ELSSMLNELV SAVYANVVQH HVQPSVLEAV
PLLVSAWHDA FCLWLATTNQ YYAPTSREDG SYMLPRYGAA DVRVSAHYPL HRSLCLLYRS
LLSKKRLCHA FRDALLTTLG ANEWHVHMLV LPLLEGLVWD AQVHAGLWKR NGWSVMNHSM
NYGEPYYCMK FRNVDLLGLQ LLADVVGIEA FVPLLLDRYD TAHLDCASTS VHEAMLAECV
ALFCQLATEV PVLDSSESRH PLYAALRHLV LLRLCVKPSS HSELFKCVNE FCATYDVLCA
SHPVAIDALL KDIAADICLP DQKVYTLKPE MYEEYNATSV HLTRKQHEVA RVNRAQARAT
RFRASTPTAM AAAPAPLHVA HRSCLLTNMC FFLVLHPSLC QIITDVVQHL ETIGSSSLVL
AIVHLLTLQM YALQQSPRDV QDTYLRVIDR LGLLDTLRSL SSTNDELLRH VAWVVQALEA
FPGLRPAPTP IALETGSSRS TVPDRHARQT SAQQRALEKI QQQQAAFSKL WMDDDAMGME
DDDDEECAMC HETSTPLSSI GFVQVSGVNV VVPPRFKTPW EDMKRDVTPL TIACCGHLVH
LSCWQAYYAT QFQKVITGEA YLNAVDVKKG EFLCPVCKSI ANVLVPLQPP AASSPSVALP
PTTDWAAWLN MALPAPSVHE PESDVAQGLG LMCMSIHRVA TGSVEKSRPD RYLASACHAI
ASTLWHTRPA PAVLLQAAQS LRAVAPAAVA YDSARALLMA GSELDGVETT ETQTPTQIQK
TWKGVVGAKP LLLQDLSAVL ARGVLLAPTQ IDQVCMVQLV SVAYAVQTFL WLVDETTAVD
ADEEPATAFV SQWFRDGSHV ASVVAQLCAL PSNAPFSAAA LAWAAEDITR FHRVATDLVP
GVDAIPVLPL DALPPAVASL VPKWIAAVHA TYTTMDDPNN VLTQWQHKHA SYVADWASVW
QQDLAVAHVP LSSAYWRHTR SSFLASLPHS YSELYMHLTK QTCPSCHLFP ARPALCLMCG
LVLCAASTCR EATVASMASV SGACTLHAHK CGRGLGLFLL TVEGTVLLVS GKLAAYDSNG
LYVDEYGEGF GERTSRFQFR GRPLFLDVSM RDRLLRLWET QSIHMEIVHN QNTVERIVIN
SFY
//
