ID F4XSU6_9CYAN Unreviewed; 660 AA.
AC F4XSU6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:EGJ32351.1};
GN ORFNames=LYNGBM3L_24830 {ECO:0000313|EMBL:EGJ32351.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ32351.1, ECO:0000313|Proteomes:UP000003959};
RN [1] {ECO:0000313|Proteomes:UP000003959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA Gerwick W.H., Gerwick L.;
RT "Genomic insights into the physiology and ecology of the marine filamentous
RT cyanobacterium Lyngbya majuscula.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
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; GL890925; EGJ32351.1; -; Genomic_DNA.
DR AlphaFoldDB; F4XSU6; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_407636_0_0_3; -.
DR Proteomes; UP000003959; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13414; TPR_11; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13174; TPR_6; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGJ32351.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:EGJ32351.1};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..283
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 566..599
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 660 AA; 74469 MW; 6555DCAA2F35803F CRC64;
MPAGTLLRQS HYRIEKVLGE GGFGITYQGI YLPNSAKVAI KELWPEKAAR MGKTITWPPS
IAPIDRQRQL HKFQLEASYL QKCYHPNIAQ VYDWFEENNT AYLVMEFISG KSLSKILQEE
GVLSEEKLKG YFIKVAESLT VVHSNQLLHR DIKPDNILID HQDRAVLIDF GATKEFIAGQ
TREMSATLSP GYAPLEQYSY RSKRWPATDI YALCASMYEL LTGELPAQAT ERAGSETLIP
PRQLAPEITP QTEQVILTGM RMKVEERFQT AEELIDALKG KFVSPSQRKA WGLLKQGKLA
EAVQAYQKCL TNQPNHGEAA VELALVQMHL NDSQAEVAAE TAIRLQPNDG RSYGVLGLVN
CRKSNWSTAV KQLQQAAKLA PQEVWIQANL AWAWGKLGNW QQAESAVSKA LQIDSNCTFA
LGLQAWINVN QQQWKRAIRT ATQALFKSKQ AQSRESQELQ QWIYPYLIIA LEKAVVTRQS
RDVERRIIEF TTQVPDSAVA WGLKGWKQAV QGLWPEALAN FDQASQKADV PSWVSLNQGI
TQEHLQNYQG AIQTYQAYIQ KFPSDAFALF RLGTLLGKVG QWAQARSHLE KAVQLKPDYA
EAYHNLGWVL LNIRTVDGQV ENFRPLLSAY RQASEFYMQQ YQSQLAGAIR QAFQIAGVEL
//
