ID A0A0F5YAW8_9CYAN Unreviewed; 546 AA.
AC A0A0F5YAW8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Serine/threonine-protein kinase B {ECO:0000256|PIRNR:PIRNR000647};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000647};
GN ORFNames=WN50_23520 {ECO:0000313|EMBL:KKD35757.1};
OS Limnoraphis robusta CS-951.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Sirenicapillariaceae; Limnoraphis.
OX NCBI_TaxID=1637645 {ECO:0000313|EMBL:KKD35757.1, ECO:0000313|Proteomes:UP000033607};
RN [1] {ECO:0000313|EMBL:KKD35757.1, ECO:0000313|Proteomes:UP000033607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-951 {ECO:0000313|EMBL:KKD35757.1,
RC ECO:0000313|Proteomes:UP000033607};
RA Willis A., Parks M., Burford M.A.;
RT "Draft genome assembly of filamentous brackish cyanobacterium Limnoraphis
RT robusta strain CS-951.";
RL Submitted (JUN-2015) 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|PIRNR:PIRNR000647};
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|PIRNR:PIRNR000647};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000647}.
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:KKD35757.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LATL02000190; KKD35757.1; -; Genomic_DNA.
DR RefSeq; WP_046281033.1; NZ_LATL02000190.1.
DR AlphaFoldDB; A0A0F5YAW8; -.
DR PATRIC; fig|1637645.4.peg.3794; -.
DR OrthoDB; 428645at2; -.
DR Proteomes; UP000033607; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.160.20.80; E3 ubiquitin-protein ligase SopA; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001646; 5peptide_repeat.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016252; Ser/Thr_kinase_SpkB.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF00805; Pentapeptide; 2.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000647; Ser/Thr_PK_SpkB; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF141571; Pentapeptide repeat-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000647, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|PIRNR:PIRNR000647, ECO:0000313|EMBL:KKD35757.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000647, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000033607};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000647,
KW ECO:0000313|EMBL:KKD35757.1}; Transferase {ECO:0000256|PIRNR:PIRNR000647}.
FT DOMAIN 34..302
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 546 AA; 61201 MW; EB78F9216A284CF4 CRC64;
MSYCINPDCP HPENPEDASQ CQACRSKLLL QNRYHVMKPL GKGGFGATFL AEDLSLPGSP
KCVVKQLRPA AKSSKILEMA RQLFQREAKT LGKIGDHPQI PRLLDYFSGK QQFYLVQEYV
DGCNLKEEVQ RLGLYTEEEI KAFLREILPI LSYIHSHEVI HRDIKPANIL RRVQDRRLVL
IDFGAVKDEV KQVTEFGTGQ TAFTNFAIGT SGFAPPEQMA LRPVYASDIY AVGMTCVYLM
TGKSPSSLDH NPMTGEVLWR SLISVSDSFA YILQKMLEMS VYQRYQSAQD VLGALDHETE
FYTDFSHGLA VQPAPRAPEA PTQLEASDDQ TTVYNDDEHT ALRPFAAQAQ QIREQKARRL
KKDYTQLGEN FASVDAGLSA TQGAPTVSLF TSAAHTRARN NSNRWDETSL RNAYARGERY
FTDCDLQGLD LRNEKFSGAY FTESRLQQTN FQNADLSKVD FSRASLSDAI FKDANLTHAR
LSYANLENAD LRGANLTYAN LSYANLRGVN LCGANLTHAL VSDQQLAFAK TNWRTVLPKG
KRKFGL
//
