ID A0A1W0W1Z2_SORBI Unreviewed; 720 AA.
AC A0A1W0W1Z2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SORBI_3002G023000 {ECO:0000313|EMBL:OQU88392.1};
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:OQU88392.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:OQU88392.1, 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; CM000761; OQU88392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W0W1Z2; -.
DR EnsemblPlants; OQU88392; OQU88392; SORBI_3002G023000.
DR Gramene; OQU88392; OQU88392; SORBI_3002G023000.
DR Proteomes; UP000000768; Chromosome 2.
DR ExpressionAtlas; A0A1W0W1Z2; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00053; EGF; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
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; IPR045274; WAK-like.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27005:SF253; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..720
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013252438"
FT TRANSMEM 344..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 295..336
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 397..678
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 425
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 720 AA; 80176 MW; 10022A2B67AB8809 CRC64;
MMTKYSPARL LSIRSLLLCL PAVWVLAATA GVPPAHRPAS CQSRCGEVDI PYPFGVGDDC
AINDGFNLSC SLVNGTERPF SGPFEVTKIS MADAKAWIKM NISWWCYDSD TSQMRQGTWG
GNFTNSAFRF SHEDNKIFVI GCNTLAYITS EYYSIGCLSR CYGEPRNMSS CSPGSGCCEA
DVPDNMGYCK SYFNPDYNDT NTCGYTVVME AKAFSYSTTY RSSSSFWHAN NGTVPVVMDW
RITFETCELA QLNLSSYACV SNNSKCVNTT NGPGYRCKCL DGYQGNPHVS NGCTDIDECQ
SNMNNCKARG ATCENTQGSY KCLCPRGKTM IDDRCMANQK SSSWVIPVVG SSVGLVALVI
TITCAYLILQ RRKLHHIKQR YFQQHGEAEL QEATDKFDEK RVLGQGGHGT VYKGLLKGNV
EVAVKRCMSI DEQHKKEFGK EMLILSQINH RNIVKLLGCC LEVQVPMLVY EFIPNGTLFQ
LIHGNHGRQI SLATRVQIAH QSAEALAYLH SWASPPILHG DVKSSNILID GDYTAKVSDF
GASILAPTDE SQFVTLVQGT CGYLDPEYMQ TCHLTDKSDV YSFGVVLLEL LTRKKPFNLD
APEDEKSLAL RFIYVTKEGR LEEILDDQIK NDENMEFLEE IAELAKQCLE ISGVNRPSMR
EVSERLDRLR KVMQHPWEQQ QNPEEMELLL GESSLASSEI VNSGILSIEK KAARNLESGR
//
