ID K9RTY5_SYNP3 Unreviewed; 404 AA.
AC K9RTY5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Protein kinase domain with FHA domain {ECO:0000313|EMBL:AFY60764.1};
GN OrderedLocusNames=Syn6312_1604 {ECO:0000313|EMBL:AFY60764.1};
OS Synechococcus sp. (strain ATCC 27167 / PCC 6312).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=195253 {ECO:0000313|EMBL:AFY60764.1, ECO:0000313|Proteomes:UP000010379};
RN [1] {ECO:0000313|Proteomes:UP000010379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27167 / PCC 6312 {ECO:0000313|Proteomes:UP000010379};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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};
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DR EMBL; CP003558; AFY60764.1; -; Genomic_DNA.
DR RefSeq; WP_015124308.1; NC_019680.1.
DR AlphaFoldDB; K9RTY5; -.
DR STRING; 195253.Syn6312_1604; -.
DR KEGG; syne:Syn6312_1604; -.
DR PATRIC; fig|195253.3.peg.1632; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG1716; Bacteria.
DR HOGENOM; CLU_637370_0_0_3; -.
DR OrthoDB; 502205at2; -.
DR Proteomes; UP000010379; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00060; FHA; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 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}; Kinase {ECO:0000313|EMBL:AFY60764.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000010379};
KW Transferase {ECO:0000313|EMBL:AFY60764.1}.
FT DOMAIN 26..79
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 144..404
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 404 AA; 45380 MW; 790FA1A1242F6703 CRC64;
MVTLSLLDPW KRTPVKRWRF PAKPTIRIGR AADNDIILND ILIARYHAEV ACYTDPENLG
RWYVKNVGPT GTFLDGKLVS DGPLGNGSLL QLGPTGPILQ FEVLSRRNAP STLATCQHIG
NMPGNLFCIH CGQPLNVQRT IRNYQVLRLL GHGGMGTTYL VCQETDYRPN QLPQVWVLKE
LRSDVEAEDK VQELFEREAR ILQGLCHAGI PKFHDYFIED GKKYLVMELI HGLDLDRWVI
RNGPVEPAQA IQWMLQTCGV LDYLHNQDPQ VIHRDLKPSN LLVRSSDNQV VLIDFGAVKE
VGHSPGTRIA VEGYSAPEQM LGHPVVQSDL YAVGATLAFL LLGDSPIRFY RHEMGVYRLN
ILDQPSVPEN LKLVIQRATE PQVSNRYQSA IELARALKGC QENA
//
