ID A0A1U8P472_GOSHI Unreviewed; 1095 AA.
AC A0A1U8P472;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LOC107954845 {ECO:0000313|RefSeq:XP_016746021.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016746021.1};
RN [1] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [2] {ECO:0000313|RefSeq:XP_016746021.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016746021.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR RefSeq; XP_016746021.1; XM_016890532.1.
DR AlphaFoldDB; A0A1U8P472; -.
DR PaxDb; 3635-A0A1U8P472; -.
DR GeneID; 107954845; -.
DR KEGG; ghi:107954845; -.
DR OrthoDB; 909669at2759; -.
DR Proteomes; UP000189702; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 5.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27008:SF587; LRR RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE EFR; 1.
DR PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 5.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00365; LRR_SD22; 4.
DR SMART; SM00369; LRR_TYP; 10.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_016746021.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000313|RefSeq:XP_016746021.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189702};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 750..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 807..1095
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 835
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1095 AA; 121799 MW; 829D1E3FC67A6662 CRC64;
MPTFSMKLTT ILTDQSALLA LKDHVIRDPE NVLTTNWSAS SPVCNWFGVS CGSKHRRVTA
LDLTGLGFVG TLPPHLGNLS FLSLLYVSNN SFYGGLPVQL SNLRRLKYLS FGNNSFSGEI
PLWLGSLTEL RKLFLYQNNF KGVIPFYLGY LSKLEILSLY ENQVSGSIPS SIFNISSLQK
IDLSDNMLSG SIPSVPRALL SLELIDFSSN NLSGHIPKDM FDHLPNLKEL SLSLNLLSGR
IPTSLFKCKE LQLLSLVYNQ MEGSLPIEIG NLSMLQYIYI GRNHFEGEIP KQIVNLTLLM
LFDCCQNNFT GIIPREIGNL KNLQLLNLDL NNIAGFIPPQ VFNISTLSVI SLDTNQLSGH
LPSNMGLFLP NLEELYLGDN YLVGSIPIYI SNASQLTLLD MSNNYFSGSI PDNLGNLRNL
KLLTVENNSL TSSEMSFLFS LTNCRVLENF LFGSNPFISS ELPRVVGNLS SSLELFSAYS
CNIRGSIPSE IGNLSHLINI ELGGNQLIGQ IPTTIGGLEE LQSLSLVYNK LEGSIPSELC
HLNKLAFLFL ANNKLSGPIP ACLGDLTSLR QLFLDSNMFS SSIPSTLTRL NYLLILYLSS
NSLSGPLPTD IGKWKVLTSL DLSNNQFSGD IPTGVADLKD LTHFSLTNNR IMGSIPESFD
ELLSLEFLDL SRNNLSGEIP KSLKKLRYLK YFNVSFNRLE GEIPKGGPFG NYTIESFKGN
EALCGAARLH VPNCKTRPLR NSKAKPKLKL IIYVALPIAS TILVVALIII ILHNKRKDKL
PTQEDMIPLG TWRRFSYHEL RQATDGFNDS RLLGNGSYGS VFQGTLQDGM LIAVKVFKLE
LEGAFKSFDV ECDVLRNTRH RNLVKVISSC SNDLNFKALV LEFMPNGSLD KWLYSNNQYL
DILQRLNIMI DVASALEYLH HGNATPVVHC DLKPNNVLLN EDMVAHLSDF GIAKLLCEDV
SMIQTMTMAT FGYMAPEYGI QGIVSTKGDV YSFGILLMEI ITRKKPTDEM FEGERSLKSW
VIESISSSQN QVVDPKLLST TGREHLKVKN CALSILQVGL ECSAELPNER LHMEEVVTKL
KKIKVKLLRD MRRVR
//
