ID   Q3MGA7_TRIV2            Unreviewed;       427 AA.
AC   Q3MGA7;
DT   25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   SubName: Full=Serine/Threonine protein kinase with FHA domain modulation {ECO:0000313|EMBL:ABA19979.1};
DE            EC=2.7.11.17 {ECO:0000313|EMBL:ABA19979.1};
GN   OrderedLocusNames=Ava_0353 {ECO:0000313|EMBL:ABA19979.1};
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:ABA19979.1, 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};
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; CP000117; ABA19979.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MGA7; -.
DR   STRING; 240292.Ava_0353; -.
DR   KEGG; ava:Ava_0353; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG1716; Bacteria.
DR   HOGENOM; CLU_637370_0_0_3; -.
DR   Proteomes; UP000002533; Chromosome.
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-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00060; FHA; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000253; FHA_dom.
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; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 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:ABA19979.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABA19979.1};
KW   Transferase {ECO:0000313|EMBL:ABA19979.1}.
FT   DOMAIN          26..78
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          171..424
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   427 AA;  46833 MW;  7BC6755308E1CC9C CRC64;
     MVTLTLLEPQ QKTPLKQWCF ENSSVIRIGR AADNHVILSD NLVSRHHLEI RQVSSGGGGS
     WQVLSKGTNG TFLNGVLVIQ DALPNNALLQ LAQGGPILQF QVQGIIPPEW QSISGSDSPL
     SGVGSSAEKI SPELSNNPGS LTCTHEGNSP QNLFCIHCGQ PLSVIQTIRH YQVLRTLGQG
     GMGTTYLAWD AAGVIVGHPK LLVLKQMNAD MARIAKAQEL FEREAYTLKS LNHSGIPKYY
     DFFVEGGKKY LAMELVHGQD LEKRIYATGP VIPSQAIAWM IQTCDILDYL HSQEQPLIHR
     DIKPANLMVK TANNQIAVLD FGAVKEIGTT PGTRIGAEGY CAPEQERGQP LTQSDLYAIG
     PTIIFLLTGE NPFKFYRQKG RGFRFDVSKI PTVTPKLRDV IERTTEPLPR DRFQSAKELA
     AALAACK
//