ID   Q3MH98_TRIV2            Unreviewed;       337 AA.
AC   Q3MH98;
DT   25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABA19638.1};
GN   OrderedLocusNames=Ava_0012 {ECO:0000313|EMBL:ABA19638.1};
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:ABA19638.1, 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; ABA19638.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MH98; -.
DR   STRING; 240292.Ava_0012; -.
DR   KEGG; ava:Ava_0012; -.
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:InterPro.
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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABA19638.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABA19638.1};
KW   Transferase {ECO:0000313|EMBL:ABA19638.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        296..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..300
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   337 AA;  37684 MW;  7D10CD21FE291EA4 CRC64;
     MELDAFNKGA IPLINHPDCS ALGYQVIREL GRNQEEGRIT YLAHHHSKQQ VVIKEFSFAH
     TYADWFGVTA YESEAQILQK LNHPRIPRYL DSFATQTAFY LVQEYKHALP LSSKRSFQAE
     EIKQIAVSIL EILVYLQQRI DPIIHRDIKP ENILVDDQLN AYLVDFGLAR VQDTKIALTS
     LLTGTPGFIP PEEQSGYSLS LASDLYSVGA TLVCLLANIR SVDIDKLINS KGYFDFQKLD
     SPIDLRFRSW LMGMVEPKWQ YRYANAADAL AALQPIQVTG NATAMEILAT VIKLKYQTTV
     LCLAIIGVLA VAGATLILSQ QGGTAQQLQE ARKSEVL
//