ID B9T256_RICCO Unreviewed; 2073 AA.
AC B9T256;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=RCOM_0915870 {ECO:0000313|EMBL:EEF30052.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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; EQ974370; EEF30052.1; -; Genomic_DNA.
DR STRING; 3988.B9T256; -.
DR eggNOG; KOG1139; Eukaryota.
DR eggNOG; KOG1140; Eukaryota.
DR InParanoid; B9T256; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IBA:GO_Central.
DR CDD; cd16482; RING-H2_UBR1-like; 1.
DR CDD; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF53; E3 UBIQUITIN-PROTEIN LIGASE PRT6; 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 SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:EEF30052.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
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 120..190
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 120..190
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1127..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2073 AA; 233937 MW; 9D7B9B81E4E527E3 CRC64;
MDIDSPPETI NPIKPRDRVM RRLVQLGIGE EYLQRRYYPG IVAFLMDNPS WIPELVSSIL
PLDEEVAEAL QQNKSESKKV QSPTMKRYFR ECMVWLQWLM FLGEPATALK SLSKMSTGRG
VCGAVWGNND IAYRCRTCEH DPTCAICVPC FQNGNHKDHD YSIIYTGGGC CDCGDVTAWK
REGFCSSHKG AEQIQPLPEE YANSVGPVLD ALFSCWKKKL VSAETICHEN PRSSDRVVLC
KKVANELTYV VVEMLLEFCK HSESLLSFVS RKVISLVGLL EILVRAERFL SEGVARKLNE
MLLKLLGEPI FKYEFGKVFV SYYPLVVHEA LKEGGDSSLK KYPLLSTFSV QILSVPTLTP
RLVKEMNLLA MLLGCLGDIF IHCAGEDDRL QVTKWGNLYE TTIRVVEDIR FVMSHAIVPK
HVTREQRDIL RTWMRLLSYL QGMSPLRREI GLHIEEENEN INLLFVLDHS VANIHSLLVD
GAFSTSEDTD DDVFSGMSKQ NMSEEDGMRY AKVGRLSQES SVCGVLGRSN QDAEVASDSI
YHPLVPSSVS LLMYECLRAI DNWLGVDHAS GALSSANTST SNSNILALKK TFLKFRKGKS
IFSGFTSSNE DQSRNFFPPA NSGLCMSMDV ENTKSVGQDC KIMGSGEPET AKSDECLMEG
NSSTESEVFR ILSSSDWPNI VYDVSSQDVS VHIPLHRLLS LLLQKALRRC YGDPEVRSTT
SAGTYTSSSS MYDDFFGRVL GGCHPRGFSA FVMEHPLRNR VFCAEVHAGM WRKNGDAAIL
SSEWYRSVRW SEQGLELDLF LLQCCAALAP ADLYVNRILE RFGLSDYPFL HLEKSSEYEP
VLVQEMLTLI IQIIQERRFS GLTPDENLKR ELIHKLSIGD ATRSQLVKSL PRDLSKYDRL
QEILDTVAVY SNPSGFNQGM YSLRWMYWKE LDLYHPRWNS RDLQVAEERY IRYCSVSALT
TQLPRWMKIH PPLKGVASIA NCKMVLKIIR AVLFYAVFSD KLTEPRAPDG ILIMALHLLS
LGLDICLQQR EPGDLSLFCG DSIPMLAFAV EEIHEGISYG AGEQSLLSLL VSLMRMHKRD
NLDNFSESDG CNISSLIESL LKKFAELDSG CRTKLQQLAP EVVIHLSQPS PHSDAHSVGS
ASDSEKRKAK ARERQAAILA KMKAEQSKFL SSINSTNEDD LRAGLEESNT DDEQHLEESA
QDVCSLCHDP NSKNPVSFLI LLQKSRLLSL TDRGPPSWNQ ARRWEKEQVS LMTIKVIEQA
GISLSSSGLE VDSSDQLSQL VQNAVNEFAE YAQPGEIINF LEFVRAQSPS LRNIQVPSPL
KDGNDRNACS LETLERDYYI SIRKEINNHT IFSSSGLKDV DISAGEGGLK SNRGVSSVLL
GKYIAAFSRE ITEHPSSSEN SLDDIAKRES TLQAYEKFGP ADCDGVYLSS CGHAVHQGCL
DRYLSSLKER FVRRLVFEGG HIVDPDQGEF LCPVCRRLSN SILPSLPGDF QRVWKEPMIS
TVSSTDAVGH LFASCEGSDS LWLPRALSLL QSAANMIQKG DIWKTFPLQR NERMKQDLDS
ISRVLFKMYF PSRQDKFSRS TRANQFMIMW DTLKYSLVSM EIAARSGRIH MTPTYSLDAL
YKELQSSSGF VLALLLKIVH SLRSKNSLHV LQRFRGIQLF AKSICSGVSA DHASRTCGRK
GDASSILKQV EKELPYPDIQ FWNQAADPIL IHDAFSSLMW VLFCLPHPFL SCEESLLSLV
HIFYLVSIAQ AILAIYGPDQ YNNRKPGFHD CLITDISHVL EESEWIQQYF VSNHIDLSSD
TMEVIRKLSF PYLRRCALLW KLLSTSASEP FCNRDDVMDR SSLAIDDSMD FMDADVIELN
EVQKLEKFFK IPQLNVVLKD QEVRSTVLKW LHHFHNEYEV FRFQHVLHST TAVPFSLMQL
PHVYQDLLER YIKQRCADCK CVFEEPALCL LCGRLCSPHW KPCCRESGCQ THAMACGAGT
GVFLLIKRTT ILLQRCARQA PWPSPYLDAF GEEDIEMHRG KPLYLNEERL LLTALIEAPK
FLDKLLLDLY SWSSLEGVLQ GCCAVNNFYS DQY
//
