ID A0A1Z5RQK3_SORBI Unreviewed; 733 AA.
AC A0A1Z5RQK3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=SORBI_3004G289000 {ECO:0000313|EMBL:OQU85676.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:OQU85676.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:OQU85676.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; CM000763; OQU85676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5RQK3; -.
DR EnsemblPlants; OQU85676; OQU85676; SORBI_3004G289000.
DR Gramene; OQU85676; OQU85676; SORBI_3004G289000.
DR eggNOG; ENOG502QQ1P; Eukaryota.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000768; Chromosome 4.
DR ExpressionAtlas; A0A1Z5RQK3; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16655; RING-Ubox_WDSUB1-like; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45647; OS02G0152300 PROTEIN; 1.
DR PANTHER; PTHR45647:SF100; U-BOX DOMAIN-CONTAINING PROTEIN 33; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 367..641
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 660..733
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 194..337
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 80..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 733 AA; 81499 MW; 1380887C46DF4599 CRC64;
MGAAADKHHS KKMKSLKSKT ALRLTEAAAS SCKIWFTCKG HLICTREANT TVPAIPPSPA
FTVASGSSVT SVGSRLRSMA ISHSESDASS SNGSPRHDQI RSRTEVGLYP SLESISTSSG
LYESCGRPTR TSRSSIDSWD GFGRRSQNSW HDQSRNDDAV TISGSAMPHE MQEPDDENFS
SPSHELENPG LDANANIYRR LTEALSEAER YKREAHEESA KRLRAELDMA SALGNVYESY
QHEIRQRKTI EETLASKEQE IEEMKRQHDV TSNELNDVKE QKLVLEQQIT EMASAIKDYE
EKMSANEYLT QMLKTDNDKL RQERDAAVTE AEGLRQKNDN KISAPLPAET LNTEFSYFEL
EQATEGFDER LKIGEGGFGS VYKGFLRNTI VAVKLLNPQS MQGQSEFNQE VAVLGRVRHP
NLVTLIGACR EAFGLVYEFL PNGSLEDRLA CTDNTPPLTW QVRTKIICEM CSALIFLHSN
KPHPVVHGDL KPGNILLNAN FVSKLGDFGI CRLLSQSSTT ITTTRAITTK LHRTTTPKGT
FAYMDPEFLS TGELTPRSDV YSFGIIILRL LTGRPPKSIA EVVEDAVERG QLHAVLDPTA
GDWPFVQANQ LAHIGLRCAE MSRRRRPDLA GEVWKVVEPL MKAASVDAGG WPSSSLDDAH
APSYFVCPIF QEVMSDPHIA ADGFTYEAEA ITGWFDSGRD TSPMTNLKLD HCELTPNRAL
RSAILQWQQQ RRR
//
