ID A0A022QJB7_ERYGU Unreviewed; 1970 AA.
AC A0A022QJB7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=MIMGU_mgv1a000061mg {ECO:0000313|EMBL:EYU26590.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU26590.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU26590.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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; KI631651; EYU26590.1; -; Genomic_DNA.
DR STRING; 4155.A0A022QJB7; -.
DR eggNOG; KOG1139; Eukaryota.
DR eggNOG; KOG1140; Eukaryota.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000030748; 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: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; 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: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 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:UP000030748};
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 22..92
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 22..92
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 509..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1970 AA; 220598 MW; 98903437CA996A30 CRC64;
MFEGDPRVAL ERLAKMSANQ RGVCGAVWGS RDIAYRCRTC EHDPTCAICV PCFENGNHKD
HDYSIIYTGG GCCDCGDITA WKRKGFCSKH KGAEQIQPLS KDVVESLGPI LDLLLGFWRD
KLLFVKNLIG ETPTVVGHAA AVLQKAADEL TSVVVEMLLE FCNQSESLLS FISQRVYSSA
GLLDILLRAE RFVDDGIIVK LHELLLKMLG EPVFKYEFAK VFVLYYPTFI NATISEGSDA
DFKKYPLMST FSVQILTVPT LTPRLVAEMN LLGVLLQCLG SMFASCSGED GKLQVNKWAN
LYETTIRVVE DLRFVISHST VSKYLCHRRR DLVRKWMKVL ASVQGMNTQK REIGIHPEDE
NENAHLPFSL CHYIHNVLSL LVAGAFSVSI HDDTREETFF SSCILDCEDQ DSQRHAKVGR
LSQESSVSSI IGKNSLDDEA KAVDSFPVPS SALWLIYECL RSIENWLGLD KTLGPLSALS
LKTSDGSGNN FLALKRTLSR FRRGKYIFKS STSSDGKPGT FGDSVNRQSS SPSQGGLKIG
VGLEYGQPIG QASTGGSDDN FLEGESSCEL EGLRVLSLSG WPDIVYEVSS QEISIHIPLH
RLLSMVLHRA LKECYGESGS SYLQRTGSAD RSSVRYNDFF GQVLDGCHPY GFSAFLMEHP
LRIRVFCAQV HAEMWRRNGD APILFSEWYR SARWSEQGQE LDLFLLQCCA TLAPPDLYVQ
RILERFGLSD YLSLDLEQSS EHEPVLVAEM LSLLIQIVKE RRFCGLTTAE CLQRELVYKL
SIGDATRSQL VKSLSRELGA VEELQEVLDR VAEYSHPSGM TQGMYKLRSS NWKELDLYHP
RWNLRDQQAA EERYLRFCNV SALTTQLPRW TKIYHPLRGI AKIATCRTLL QVIRAVLFYA
VFSDKVTSSR APDGVLLTAL HLLALAMDIC RLHKESDDLL CHEGDVIPIL AFASEEICMS
KYGDQSMLSL LVLLMKMHEK ENARNFMEAD NFNLSSLILS IVKTIVELEP ECMTKLQKLA
PQLAAQFSHS LSNDSARDTD LSSDSEKHKA KSRERQAAIL EKMRAQQSKF LESFHFDGDD
EMDEMDDTKS EQEASDSDIS DDTQESAQAV CSLCHDAKSR SPVSFLVLLQ KSRLLGFVNQ
GPPSWEQVSR SGKEHVSYVT TSSNHLSPSS NSDDSEMISS SELEDSVQSA LKDFAYTGKP
REVNALVEFI KARFPSIKNV RAPCDSKDTR EMTSSSLETL EEHMYLSIRE FQASLNGSDS
KKGDEKCTTA GNPQDNPSAS QNDSSGLVTM KSGSSKHSTG YDNFGPDGGD GIYVSSCGHA
VHQECLDRYL SSLKERFELN YYKFLILKGT TLIFYFDLLK KCSSFFFLPM CTDISEEGEF
LCPVCRGLAN SILPALPGDL RKLPQLPAGS TINVTDASSP STSSDDGGSS FRLQDALSLL
QRAANVAESS EALKTLATQN VRIKPNPNLE PIIRLLCGMY YPGQDKILET GRISHSLILW
DALKYSLMST EIAARSVKSS LSPNYSIGAV FKELNSSSCF ILTLLLDVIQ STRTTDSQTI
LLRCHGLQLF VRSLCPGAYQ DELSNRSKRQ GGTMLYILEN ADPKVRYPDV QLWRQASEPI
LARDAFSSFM WILFCLPWPI LSCKESYFSL VHVFYVVTVT QAIIICHNAR KSKETEVEFV
DNLITDIYQL LGERREAAQY FQSYFCDPAY DINDAIRSIT FPYLRRCALL WKLINCSKIM
PFGNGVRSWG GSSYESDYFE SSANTAEELT EIQKLEKMFN IPSLNLIVND VETRSTALRW
VGCFLEMFEP DTSQSLLRCT PAVPFKLMVL PHLYQELLQR YIKKCCPDCG VVKEEPALCL
LCSKICSPNW KACCSESACQ THAMSCGAGI GVFLLIRRTT ILLQRCARQA PWPSPYLDAF
GEEDVEMYRG KPLFLNEERY AALTHMVASH GLDRSSKVLR QTTITSFFTF
//
