ID A0A803N2T2_CHEQI Unreviewed; 717 AA.
AC A0A803N2T2;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC110736410 {ECO:0000313|EnsemblPlants:AUR62039488-RA:cds};
OS Chenopodium quinoa (Quinoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Atripliceae; Chenopodium.
OX NCBI_TaxID=63459 {ECO:0000313|EnsemblPlants:AUR62039488-RA:cds, ECO:0000313|Proteomes:UP000596660};
RN [1] {ECO:0000313|EnsemblPlants:AUR62039488-RA:cds}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PI 614886 {ECO:0000313|EnsemblPlants:AUR62039488-RA:cds};
RX PubMed=28178233; DOI=10.1038/nature21370;
RA Jarvis D.E., Ho Y.S., Lightfoot D.J., Schmoeckel S.M., Li B., Borm T.J.A.,
RA Ohyanagi H., Mineta K., Michell C.T., Saber N., Kharbatia N.M.,
RA Rupper R.R., Sharp A.R., Dally N., Boughton B.A., Woo Y.H., Gao G.,
RA Schijlen E.G.W.M., Guo X., Momin A.A., Negrao S., Al-Babili S., Gehring C.,
RA Roessner U., Jung C., Murphy K., Arold S.T., Gojobori T.,
RA van der Linden C.G., van Loo E.N., Jellen E.N., Maughan P.J., Tester M.;
RT "The genome of Chenopodium quinoa.";
RL Nature 542:307-312(2017).
RN [2] {ECO:0000313|EnsemblPlants:AUR62039488-RA:cds}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2021) to UniProtKB.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR RefSeq; XP_021772323.1; XM_021916631.1.
DR AlphaFoldDB; A0A803N2T2; -.
DR SMR; A0A803N2T2; -.
DR EnsemblPlants; AUR62039488-RA; AUR62039488-RA:cds; AUR62039488.
DR GeneID; 110736410; -.
DR Gramene; AUR62039488-RA; AUR62039488-RA:cds; AUR62039488.
DR KEGG; cqi:110736410; -.
DR OMA; THTDNCV; -.
DR OrthoDB; 629492at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000596660; Unplaced.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR FunFam; 1.25.10.10:FF:000423; RING-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000455; RING-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR058678; ARM_PUB.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR057623; PUB12-19-like_N.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23315; U BOX DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23315:SF266; U-BOX DOMAIN-CONTAINING PROTEIN 17; 1.
DR Pfam; PF25598; ARM_PUB; 1.
DR Pfam; PF25368; PUB10_N; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 5.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000596660};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 288..362
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 432..474
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 517..559
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
SQ SEQUENCE 717 AA; 79002 MW; 87640006A65ADACB CRC64;
MATSAAFSSL RRRRSPPLEA FLAPVDLTDG GIIRTVLSVA NELVDLHSGK KLPFQRQNFN
SLVRKLEVFV VVLDFLKDFR SFSRFSYTAI MCFKELYLLF YRCKILLDYC SQSSKLWMLL
QNQSISGHFH DLNQEMSTLL DVLPIKELSL SEDVREQVEL LQRQLRRAKC FMDKNDEMLR
HRLYSFLYEI EKGQIPDSNE LWFFFVDKLG IRDPKSCRAE IEFLEEQIVN HEGDVEPTAA
VLNGFVALTR YCRFLLFGFE EEMEVGAERH KKLRKGMMTQ EIADTFLTIP KDFCCPISLD
LMQDPVIVST GQTYDRSSIS RWLDEGHYTC PKTGQMLANK RLIPNRALRN LITQWSVAHG
IPYEQPEGAE FSSELAAASS SKAAVTANQA TAYLLIQQLA SGSEDAQTIA AREIRLLSKT
GKENRAFIAE AGAVPHLKRL LLSANAIAQE NSVTAMLNLS IHDKNKGRIM DEEGCLNSIV
DVLRFGQTTE ARENAAATLF SLSAVHNYKK RIADESGAVE ALAYLLRDGT PRGKKDAVTA
LFNLSTHTEN CVRMIEAGAV SAVVGAIGVE GVSEEAAGAL ALIVRHPAGA EAVGREEKAV
AGLLGLMRCG TPRGKENAVA ALLELCRSGG AVATEKVLKA PTLAGLLQTL LFTGTKRARR
KAASLARVFQ RRENAALHSG GVGVGYPIAG NSTTNRDTSF VGDVSVPMSI SVPVVQG
//
