ID A0A2T7CJ49_9POAL Unreviewed; 963 AA.
AC A0A2T7CJ49;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=GQ55_8G002400 {ECO:0000313|EMBL:PUZ43356.1};
OS Panicum hallii var. hallii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC Panicum sect. Panicum.
OX NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ43356.1, ECO:0000313|Proteomes:UP000244336};
RN [1] {ECO:0000313|EMBL:PUZ43356.1, ECO:0000313|Proteomes:UP000244336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT "WGS assembly of Panicum hallii var. hallii HAL2.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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; CM009756; PUZ43356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7CJ49; -.
DR EnsemblPlants; PUZ43356; PUZ43356; GQ55_8G002400.
DR Gramene; PUZ43356; PUZ43356; GQ55_8G002400.
DR Proteomes; UP000244336; Chromosome 8.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009882; F:blue light photoreceptor activity; IEA:UniProt.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:SF20; PHOTOTROPIN-1; 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:UP000244336};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 181..230
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 255..309
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 449..522
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 523..577
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 643..931
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 142..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 672
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 963 AA; 107148 MW; 809530B6CDDC74FC CRC64;
MDGHLTTTTS RYQLVAGSAA VSRAPACIYI PVAAESKKLI KPLLAAAADR SSSWLAIFAS
SSTSISSMAF KGLPRDSRGS LEVFNPDAPT LICPPKREPI TSPFLLSFTA DDDEVQEEDK
DAVVGRAAQR AAEWGLILQT NKHTGRPQGV TARPSGSGPT SESGNSLDET TADMARVLPR
VSEELRAALS AFQQTFVVSD ATRPDHPILY ASAGFFNMTG YSSNEVVGRN CRFLQGSGTD
PAEIAKIRQA LSAGSNYCGR VLNYKKDGTP FWNLLTVAPI KDEDGRILKF IGMQVEVSKY
TEGSKDTAVR PNGLPESLIK YDARQKDQAR GSVSELLLAL KNPRSLSEAR NSTLKRKSQE
AECVFSTEVP GKRTSESGMR SSLQKISEVP EGGNKSRKSG LRSLIGFLGM GHGNVQKNML
KPREDLLIDS DDERPESFDD DFRRKEMRRG MDLATTLERI EKNFVITDPR LPDNPIIFAS
DSFLRLTEYS REEILGRNCR FLQGPETDRG TVKKIRDAID NQTEVTVQLI NYTKSGKKFW
NLFHLQPMRD QKGDVQYFIG VQLDGTERVR DAAAKDGAML VKKTADNIDE AAKELPDANL
SPEDLWANHS KPVLPKPHMK DTASWRAIQK VLENGESIDL KHFKPVKPLG SGDTGSVHLV
ELLGTGEYFA MKAMDKSVML NRNKVHRATV ERQILDMLDH PFLPTLYASF QTKTHICLIT
DYCSGGELFM LLDRQPMKVL KEDAVRFYAA EVVTALEYLH CQGIIYRDLK PENILLHRDG
HISLTDFDLS CLTSCLPQVF LPEDNDKKKG RRKSMGSPIF FAEPMRASNS FVGTEEYIAP
EIITGAGHTS AVDWWALGIL LYEMLYGYTP FRGKTRQRTF ANVLHKDIRF PMSIEVSLAA
RQLMYRLLHR DPANRLGSYE GASEIKQHAF FRGINWALVR AAAPPKLEVE EETAVTAGHT
DMF
//
