ID   Q3MA43_TRIV2            Unreviewed;       376 AA.
AC   Q3MA43;
DT   25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABA22143.1};
GN   OrderedLocusNames=Ava_2528 {ECO:0000313|EMBL:ABA22143.1};
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=240292 {ECO:0000313|EMBL:ABA22143.1, ECO:0000313|Proteomes:UP000002533};
RN   [1] {ECO:0000313|Proteomes:UP000002533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937 {ECO:0000313|Proteomes:UP000002533};
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA22143.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MA43; -.
DR   STRING; 240292.Ava_2528; -.
DR   KEGG; ava:Ava_2528; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_135_5_3; -.
DR   Proteomes; UP000002533; Chromosome.
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; 1.10.510.10; 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   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   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABA22143.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABA22143.1};
KW   Transferase {ECO:0000313|EMBL:ABA22143.1}.
FT   DOMAIN          34..295
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          293..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   376 AA;  42153 MW;  B82DAD1DD567DC37 CRC64;
     MSYCLNPRCP KPENPHDVKF CLSCGSKLHL KERYRAIKPI GQGGFGRTFL AVDEDKPSKP
     RCVIKQFYPQ AQGTNTVQKA VELFTQEAIQ LDELGKHPQI PELLAYFTQD DRQYLVQEFI
     DGLNLAQELA HKGVFSETRT IQLLNDLLPV LQFCHNRQVI HRDIKPENII LRNSDNKLVV
     VDFGASKSAT NTALNQTGTS IGSPEYVAPE QMRGRAIFAS DIYSLGVTCI NLLTGRSPFD
     SYDTNNDTWV WQQYVKPQVS NYLSQIINKM TASVPARRYQ TVEEVLKDLN QHSPVATTPA
     KPSHQVPQNP PPQPVSKTQS QIDLELEELK TQFLPGGKSK PQNIQPQPAT NNNSAKSAID
     LELEELKAKY LGNNNG
//