ID A0A2H9ZTD1_9ASPA Unreviewed; 567 AA.
AC A0A2H9ZTD1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Serine/threonine-protein kinase CTR1 {ECO:0000313|EMBL:PKA46543.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:PKA46543.1};
GN Name=CTR1 {ECO:0000313|EMBL:PKA46543.1};
GN ORFNames=AXF42_Ash012676 {ECO:0000313|EMBL:PKA46543.1};
OS Apostasia shenzhenica.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Apostasioideae; Apostasia.
OX NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA46543.1, ECO:0000313|Proteomes:UP000236161};
RN [1] {ECO:0000313|EMBL:PKA46543.1, ECO:0000313|Proteomes:UP000236161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC TISSUE=Stem {ECO:0000313|EMBL:PKA46543.1};
RX PubMed=28902843; DOI=10.1038/nature23897;
RA Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA Van de Peer Y., Liu Z.J.;
RT "The Apostasia genome and the evolution of orchids.";
RL Nature 549:379-383(2017).
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DR EMBL; KZ454132; PKA46543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9ZTD1; -.
DR STRING; 1088818.A0A2H9ZTD1; -.
DR OrthoDB; 722200at2759; -.
DR Proteomes; UP000236161; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR23257:SF878; PAS DOMAIN-CONTAINING PROTEIN TYROSINE KINASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50112; PAS; 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}; Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PKA46543.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000236161};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PKA46543.1}.
FT DOMAIN 82..112
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 357..567
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 313..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 567 AA; 64031 MW; 9351CEC576E50461 CRC64;
MREVDEDLMK RFRDLEASQE KLREQLDLLI CGGGDKKAER GWRTRGKRNG DMMLMAGNFV
RNPYQAVLHQ LGHALHICRP VSGEIIYWNR SAENLFGWKS YEALGQKITD LLIDINRYPC
WESTLERVYY GQTWSGQFPF KKRSGELFMA MLTMSPLNES GICIGVITVS SDASMLNNGS
SEGTWTHSDE AVGEFGEPKS NFKKVHRSPQ LQIASSVSNL VQGPDNARES VKDNAYCASC
YRNVVVQKQS SSVSDINSTE EMRNLVSQLN RSTSFAHFRN AIMHNTALHR NGEHLPDDAT
DKATVLKKNA STKMEDFQPA KSQNSMETSC SSQTGSSTVC EMESYLVADS EINWEDLLLG
EKVGEGSYAV VYRGIWNGSD VAVKVYTGMD YQECVLLDYK KEIAIMKRLR HPNVLLFMGA
VYSPEHLAIV TEYLPRGSLF RALHKNNQSL VLRRRVQMAL DVARGMNYLH RRNPPIIHRD
LKSSNLLVDK NWTVKVLIDQ NAPPPRLFSF LFLSSSYSHP SFLSLSLSLS LFLSCEGGGG
GGESRRGQHK YNWGKRGREC KDEERQS
//
