ID A0A252CY39_9NOSO Unreviewed; 726 AA.
AC A0A252CY39;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=BV372_32790 {ECO:0000313|EMBL:OUL20274.1};
OS Nostoc sp. T09.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=1932621 {ECO:0000313|EMBL:OUL20274.1, ECO:0000313|Proteomes:UP000195076};
RN [1] {ECO:0000313|EMBL:OUL20274.1, ECO:0000313|Proteomes:UP000195076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T09 {ECO:0000313|EMBL:OUL20274.1};
RA Cruz-Morales P., Corona-Gomez J.A., Gutierrez-Garcia K.G., Barona-Gomez F.,
RA Cibrian-Jaramillo A.;
RT "Metagenomics of subcommunity co-cultures reveals the complexity of the
RT cycad coralloid root endophytic microbiome.";
RL Submitted (JAN-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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUL20274.1}.
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DR EMBL; MTAV01000221; OUL20274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A252CY39; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000195076; Unassembled WGS sequence.
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:OUL20274.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195076};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:OUL20274.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 149..389
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 34..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 79018 MW; D7573065B034B6FA CRC64;
MNSDRCTRNG CTGTIEDGYC NVCGLAAVKS QNVSSQKQSA TITARSSPVT TGTGSSPLTN
RSKGSRRSSS TSARSSRRQL GAGLISVPEL PSTEPEKAII PNPMVPENKR FCSNCNHPLR
REKGFCSKCG QKYSFIPSLN PGDLVVGQYE VKGAIAYGGL GWIYLGFDKT LSRYVVLKGL
LNTEDAASAA VAVAERQFLA AVKHGNIVGI YNFVNHGTEG FIVMEYVGGK TLKEIRKSRG
PLPVAEAIAY IHRILSAFAY LHSLGMVYCD FKPDNIMVEG GDVKLIDLGG VRRIDDLDGD
IYGTVGYSAP EAGEGPTVVS DLFTVGRTLA VLLTDIKGFS KEHLYTLPSP QKEPLFVQQE
SLYRFLIKAT AENPDDRFQS ADEMADQLLG VLREVVAIAT NLPRPSTSNL LSGDMLALAH
SGSLEPIQPE YQQLPIPILD ASDSGFNAVL NASAIADPIK RAVSLDVVVK QFPTSSEAWL
RLANTLIDTG DFEEVEQSLA KVEAKDPWDW RIFWYRGRAL MAQGRVIEAQ KAFDQVYFDL
PGELAPKLAL GLAAEQAQNY QLAIKMYDLV SRTDPGYVTA AFGLARCLCA TGDRKGAVAA
LERVPPASSL FTRSRVEIAR TLINRDRSAP GSQELQAAST AIETLTLEGM DRHRLTKQVL
ETALNLLTSK QLQAAADLKI LGQPFQEIHL RKGLEKALRD MAHLSSGKEK IHLVDEANKI
RPRTLI
//