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Database: UniProt
Entry: K9X033_9NOST
LinkDB: K9X033_9NOST
Original site: K9X033_9NOST 
ID   K9X033_9NOST            Unreviewed;       725 AA.
AC   K9X033;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=Cylst_3279 {ECO:0000313|EMBL:AFZ25434.1};
OS   Cylindrospermum stagnale PCC 7417.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Cylindrospermum.
OX   NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ25434.1, ECO:0000313|Proteomes:UP000010475};
RN   [1] {ECO:0000313|EMBL:AFZ25434.1, ECO:0000313|Proteomes:UP000010475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ25434.1,
RC   ECO:0000313|Proteomes:UP000010475};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Cylindrospermum stagnale PCC 7417.";
RL   Submitted (JUN-2012) 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; CP003642; AFZ25434.1; -; Genomic_DNA.
DR   RefSeq; WP_015208683.1; NC_019757.1.
DR   AlphaFoldDB; K9X033; -.
DR   STRING; 56107.Cylst_3279; -.
DR   KEGG; csg:Cylst_3279; -.
DR   PATRIC; fig|56107.3.peg.3589; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_011707_0_0_3; -.
DR   OrthoDB; 137117at2; -.
DR   Proteomes; UP000010475; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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:AFZ25434.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010475};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          148..479
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          36..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   725 AA;  79224 MW;  3B64F00BA9A23016 CRC64;
     MEGLRCSRNG CTGTIEDDYC NVCGLAAVKT PVVSQKQSAT ITGRNSSVTT NTGSSPLTNR
     SKGSRRTSST SARSSRRQLG AGLISVPELP STEPEKAIIP NPQVPDNKRF CGNCNHPLRR
     EKGFCSKCGQ KFSFIPSLKR GDLVVGQYEV KGAIAFGGLG WIYLGFDQTL SRYVVLKGLL
     NTEDASSAAV AVAERQFLAA VKHSNIVGIY NFVNHNNEGF IVMEYVGGQT LKEIRKSRGP
     LPVAEAIAYI HRILSAFAYL HSLGLVYCDF KPDNIMVEGG DVKLIDLGGV RRLDDPDGDI
     YGTVGYSAPE AGEGPTIVSD LYTLGRTLAV LLTEIKGFSK EHLYKLPSPQ EEPLFAEQES
     LYRFLIKATA ENADDRFQSA DEMADQLLGV LREVVAIATN IPRPYASNLF GGDMLALTNS
     GDFELITADY RQLPIPLLDS SDSGFNAVLN ASAIADPVKR CVSLEVVVQQ YPTSKEAWLR
     LANSLIDAGE YNEAEQAIAK VEAKDPWDWR VFWYRGRSLM AQGKLQEAQQ TIDQAYFDLP
     GEVAPKLALG LAAEQAQNYQ LAIKMYDLVS RTDPGYVSAS FGLGRCLCAT GDRLGAVKAL
     ERVPPTSNLF TRSRVEIARS LIDSDRTMPG TQELKAASAA VETLTLEGID RYRLTKQVLE
     TALKLLTSRT LKAAADLKIL GQPFEEKPLR CGLEKTLRDM AHLASGNEKI PLVDQANRVR
     PRTLF
//
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