ID A0A151R110_CAJCA Unreviewed; 949 AA.
AC A0A151R110;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=KK1_042697 {ECO:0000313|EMBL:KYP36203.1};
OS Cajanus cajan (Pigeon pea) (Cajanus indicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Cajanus.
OX NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP36203.1, ECO:0000313|Proteomes:UP000075243};
RN [1] {ECO:0000313|EMBL:KYP36203.1, ECO:0000313|Proteomes:UP000075243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX PubMed=22057054; DOI=10.1038/nbt.2022;
RA Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT of resource-poor farmers.";
RL Nat. Biotechnol. 30:83-89(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; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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 EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; KQ484250; KYP36203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151R110; -.
DR STRING; 3821.A0A151R110; -.
DR OMA; SLMGFKI; -.
DR OrthoDB; 728091at2759; -.
DR Proteomes; UP000075243; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblPlants.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009882; F:blue light photoreceptor activity; IEA:EnsemblPlants.
DR GO; GO:0010181; F:FMN binding; IEA:EnsemblPlants.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblPlants.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007623; P:circadian rhythm; IEA:EnsemblPlants.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009638; P:phototropism; IEA:EnsemblPlants.
DR GO; GO:0010118; P:stomatal movement; IEA:EnsemblPlants.
DR CDD; cd00130; PAS; 2.
DR CDD; cd05574; STKc_phototropin_like; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45637; FLIPPASE KINASE 1-RELATED; 1.
DR PANTHER; PTHR45637:SF22; FLIPPASE KINASE 1-RELATED; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
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}; Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
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:UP000075243};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KYP36203.1}.
FT DOMAIN 141..214
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 215..269
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 413..486
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 487..541
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 614..900
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 108..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 643
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 949 AA; 106804 MW; 4DE70B5AD72212F5 CRC64;
MEKLNLSAKY DPDAKSDSFP IFELQDSQNV VIAPSNSASS REPVNKWMAF AKMPDGNSAT
KEKSVTQQVN DLKNQPSPDD QILTEAAIAE RTAEWGLVVN TGNFKAIGGE NNNSDRFGES
TRTSGESNYG SESSSGVFPR VSQELKEALA TLQQTFVVSD ATKPDCPIMY ASSGFFTMTG
YSSKEIIGRN CRFLQGPETD KNEVAKIRDS TANGRSYCGR LLNYKKDGTP FWNLLTITPI
KDDLGNTIKF IGMQVEVSKY TEGVNEKALR PNGLPKSLIR YDARQKEKAL GSITEVVQTV
KDPKSIIKDM NDDSSTKIEE AEKLNFEFVL PKSADVGNTS TAVRQTSPLN MQRMSSSQDK
NKSSRKSGRI SFKSFKGKDE EKPTIIEPEV LMTKEIEWAN NWELSQRERD IRQGIDLATT
LERIEKNFVI SDPRLPDNPI IFASDSFLEL TEYTREEILG RNCRFLQGPE TDQTTVARIR
DAIREQREIT VQLINYTKSG KKFWNLFHLQ PMRDQKGELQ YFIGVQLDGS DHVEPLKNRL
SETTEQQSAK LVKATAENVD EAVRELPDAN LRPEDLWAIH SQTVFPRPHK KNNTSWIAIQ
KIAARGEKIG LQHFSPIRPL GCGDTGSVHL VELKGTDELY AMKAMEKTVM LNRNKVHRSC
IEREIISLLD HPFLPTLYTS FQTSTHVCLI TDFCHGGELF ALLDKQPMKI FREESARFYA
AEVVIGLEYL HCLGIIYRDL KPENILLQKD GHVVLTDFDL SFMTNCKPQV VKQSLPGKRR
SRSQPPPTFV AEPVTQSNSF VGTEEYIAPE IITGAGHTSA IDWWTLGILL YEMLYGRTPF
RGKNRQKTFS NILHKDLTFP SSIPASLAAR QLINALLQRD PGSRLGSTTG ANEIKQHPFF
RGINWPLIRN MTPPPLDVPL RLIGKEPVAK DLKWEDDGVL VSSIDMDIF
//
