ID   Q3MGV7_TRIV2            Unreviewed;       485 AA.
AC   Q3MGV7;
DT   25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABA19779.1};
GN   OrderedLocusNames=Ava_0153 {ECO:0000313|EMBL:ABA19779.1};
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:ABA19779.1, 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).
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DR   EMBL; CP000117; ABA19779.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MGV7; -.
DR   STRING; 240292.Ava_0153; -.
DR   KEGG; ava:Ava_0153; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_135_5_3; -.
DR   Proteomes; UP000002533; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000313|EMBL:ABA19779.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABA19779.1};
KW   Transferase {ECO:0000313|EMBL:ABA19779.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        344..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        372..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        408..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        430..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        453..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..276
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          276..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   485 AA;  53172 MW;  D016F18463D671C6 CRC64;
     MLGQLLDGRY KITQVLGAGG FGKTYIAEDI KLYNNLCVVK QLQPTANDPI TLQVARRLFA
     SEAELLHKLG THDQIPQLLA HFEEHQEFFL VQQFIDGHPL SDELTPGKRL SEAYTIALLK
     NILQPLAFVH QNNVIHRDIK PPNLIRRKSD GKVVLIDFGA VKQIGTQVVN GEGVTKMTVS
     IGTAGYMPSE QSRGSPRLSS DVYAVGMIGI QALTGLMPHQ LQEDIQTAEI IWRELVQVSP
     NLADVLDRMV RYDFRQRYQS AVEALAAVQN LGNAYAPTQT SPSPGSKPTL PVKNHVNTPP
     VAEPPLYSPP PAVPAQYRQE VPKNLIAPPP PTTAKSSKVG ISFYLQWVLV NIVGLVGGGI
     VGAIAYEIFE PLGIIISSQA VAATMGLTIG FIQALVLRRQ IPVSEKQWVL GTTLGVCISV
     LVCGDYPEYS LLWIGPIVGS IQWFILKPYV KQAVWWILVN TLFGWIGGII SGAVLVFLLK
     NLKDF
//