ID A0A1Z4H7W7_9CYAN Unreviewed; 726 AA.
AC A0A1Z4H7W7;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=NIES2100_56230 {ECO:0000313|EMBL:BAY25815.1};
OS Calothrix sp. NIES-2100.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1954172 {ECO:0000313|EMBL:BAY25815.1, ECO:0000313|Proteomes:UP000218319};
RN [1] {ECO:0000313|EMBL:BAY25815.1, ECO:0000313|Proteomes:UP000218319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2100 {ECO:0000313|EMBL:BAY25815.1,
RC ECO:0000313|Proteomes:UP000218319};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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};
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DR EMBL; AP018178; BAY25815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4H7W7; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000218319; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031634; PknG_rubred.
DR InterPro; IPR031636; PknG_TPR.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE/THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF16919; PknG_rubred; 1.
DR Pfam; PF16918; PknG_TPR; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAY25815.1};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:BAY25815.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 149..389
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 36..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 79155 MW; 013B47B5171CE620 CRC64;
MNSDRCTRNG CTGIIEDGYC NVCGLAAVKS LNVSSQKQSA TITVRSSPVT TGTGSSPLTN
RSKGSRRSSG TSARSSRRQL GAGLISVPEL PSTEPEKAII PNPMVPENKR FCSNCNNPLR
REKGFCSKCG QKYSFIPSLN PGDLVVGQYE VKGAIAYGGL GWIYLGFDKT LSRYVVLKGL
LNTEDAASAA VAVAERQFLA AVKHANIVGI YNFVNHGTEG FIVMEYVGGK TLKDIRKSRG
ALPVAEAIAY IHRILSAFAY LHSLGMVYCD FKPDNMMVEG GDVKLIDLGG VRRIDDLDGD
IYGTVGYSAP EAGEGPTVVS DLFTVGRTLA VLLTDIKGFS REHLYTLPSP EEEPLFAHQE
SLYRFLIKAT AENPDDRFQS ADEMADQLLG ILREVVAIET NVPRPSSSSL LGGDMLALTY
SGSFDPIKPE YEQLPIPILD SSDVAFNAVI NASAIADPVK RAVSLDVVVK QFPNSSEALL
RLANALIDAG DFEEVEPSLA KIEEKDPWDW RIFWYRGRAL MAQNKAIEAQ KAFDQVYFDL
PGELAPKLAL GLAAEQAQNY QLAIKMYDLV SRTDPSYVTA AFGLARCLCA TGDRKGAVAA
LERVPPASSL FTRSRVEIAR TLINRDRAVP NLQELQSAST AIETLTLEGM DRYRLTKQVL
ETALNLLTSK QLQAAGDLKI LGQPLQEKHL RKGLEKALRD MAHLSSGKEK IHLVDEANRI
RPRSLI
//