ID A0A0D2SD61_GOSRA Unreviewed; 751 AA.
AC A0A0D2SD61;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=B456_005G086300 {ECO:0000313|EMBL:KJB29140.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB29140.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB29140.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00000327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00000671};
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; CM001744; KJB29140.1; -; Genomic_DNA.
DR RefSeq; XP_012482518.1; XM_012627064.1.
DR AlphaFoldDB; A0A0D2SD61; -.
DR STRING; 29730.A0A0D2SD61; -.
DR EnsemblPlants; KJB29140; KJB29140; B456_005G086300.
DR GeneID; 105797131; -.
DR Gramene; KJB29140; KJB29140; B456_005G086300.
DR KEGG; gra:105797131; -.
DR eggNOG; ENOG502QQPF; Eukaryota.
DR OMA; SNHTSVH; -.
DR OrthoDB; 101939at2759; -.
DR Proteomes; UP000032304; Chromosome 5.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR013695; WAK.
DR InterPro; IPR045274; WAK-like.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27005:SF508; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 16-RELATED; 1.
DR PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08488; WAK; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..751
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002267195"
FT TRANSMEM 347..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 293..327
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 423..705
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 751 AA; 83262 MW; BE4D52C74427B3ED CRC64;
MGLIRSVVLI VQLVILLNAT SAAKATAAVA YQANSGCQSR CGEVSIPYPF GTGGDCNVSK
HFFITCNTSF TPSKAFLTTS SIEILDISLD GQLRILADGS YDCYNKSGAT RNFRYWLQLG
KFFINNTRNK FTAIGCDTYA RVEGFSGQRY ATGCLSLCNN INDVSNGSCS GIGCCQTSIP
KGVKSYKITT ESYENHTDVL PENPCSYAFV AENDNYTFST SDLRGFDFKD KLFPVTLDWT
IGQKSCKKAK MDTKSFACKK NSKCIDSEHN SGYICKCFEG YDGNPYLPNG CQDINECETM
SPCDGTATCI NLNGTYDCSC PPNYEGDGKK NGTGCSLPNK DQSKRSLLID VALGIGIGFL
GLLLGIVLLC WMLKQRQISE LKRVNFQQNG GILLREQLSK RQGYREEVKV FTVEELEKAT
NNYHESRILG QGGQGTVYKG ILADNRIVAI KKSIIGDPSQ VEQFINEIMV LYQINHRNVV
KLLGCCLETQ VPLLVYEYIT NGTLFHHLHD DDAALDLPWE TRLRIATETA EALSYLHSAV
SIPIIHRDIK LANILLDNNY NAKVSDFGAS RLIPSDEAQI TTIVQGTFGY LDPEYMHTSL
LTEKSDVYSF GVVLMELLTG QKVVCFKRSE EKRVLAMYFV SLMKEDNLLD ILDPRVLTDK
NVEQLKEVAA LASRCVRMKG EERPTMKEVA HELAGLQAMP KHPWSKSKLQ GEESEYLLGD
MCSTYTDGAT SSSMGYDSIN NKITFELEGA R
//
