GenomeNet

Database: UniProt
Entry: A0A1U8JYJ2_GOSHI
LinkDB: A0A1U8JYJ2_GOSHI
Original site: A0A1U8JYJ2_GOSHI 
ID   A0A1U8JYJ2_GOSHI        Unreviewed;       389 AA.
AC   A0A1U8JYJ2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Serine/threonine-protein kinase STY8-like isoform X2 {ECO:0000313|RefSeq:XP_016693364.1};
GN   Name=LOC107910115 {ECO:0000313|RefSeq:XP_016693364.1};
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_016693364.1};
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_016693364.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_016693364.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
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DR   RefSeq; XP_016693364.1; XM_016837875.1.
DR   AlphaFoldDB; A0A1U8JYJ2; -.
DR   GeneID; 107910115; -.
DR   OrthoDB; 3028364at2759; -.
DR   Proteomes; UP000189702; Chromosome 20.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
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   CDD; cd13999; STKc_MAP3K-like; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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; PTHR23257:SF891; INTEGRIN-LINKED PROTEIN KINASE FAMILY; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000654; Integrin-linked_kinase; 1.
DR   SMART; SM00248; ANK; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 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   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_016693364.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000189702};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REPEAT          62..94
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          154..389
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   389 AA;  43849 MW;  D65E6620F91617A2 CRC64;
     MSSSKSGGEP SARGSTSSDR QKEKARLSRT SQILWHAHQN DASAVRKLLQ EDRSLVNARD
     YDNRTPLHVA SLHGWIDVAT CLLEFGADVN SQDRWRNTPL ADAEGAKKHE MIELLKSYGG
     LSYGQNGSHF EPKPVPPPLP NKCDWEVDPS ELDFSNSNII GKGSFGEILR ASWRGTPVAV
     KRILPSLSDD RLVIQDFRHE VNLLVKLRHP NVVQFLGAVT DKKPLMLITE YLRGGDLHQY
     LKEKNGLNSS AAINFALDIA RGMAYLHNEP NVIIHRDLKP RNVLLVNSSA DHLKVGDFGL
     SKLIKVQNSH DVYKMTGETG SYRYMAPEVF KHRKYDKKVD VFSFAMILYE MIEGEPPFSN
     HEPYEAAKLV AEGHRPNFRS KSFLPELRE
//
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