ID   Q3M2R3_TRIV2            Unreviewed;       620 AA.
AC   Q3M2R3;
DT   25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=Serine/Threonine protein kinase with TPR repeats {ECO:0000313|EMBL:ABA24723.1};
GN   OrderedLocusNames=Ava_B0009 {ECO:0000313|EMBL:ABA24723.1};
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OG   Plasmid pAnaA {ECO:0000313|Proteomes:UP000002533}.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=240292 {ECO:0000313|EMBL:ABA24723.1, 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; CP000119; ABA24723.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3M2R3; -.
DR   KEGG; ava:Ava_B0009; -.
DR   HOGENOM; CLU_033884_0_0_3; -.
DR   Proteomes; UP000002533; Plasmid pAnaA.
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   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
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   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABA24723.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Plasmid {ECO:0000313|EMBL:ABA24723.1};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABA24723.1};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:ABA24723.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          40..321
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          354..387
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   620 AA;  71682 MW;  A0F92321ACFDE703 CRC64;
     MSVYCINPLC EQRKNPDNAE VCLACGTPLI INNRIRLLKP LRELSFDPQN YFEVFEVEDR
     RTQEYPVHQR RVMKVLKWNS SKYRELIEQE FLTLQLIKYP NIPKCNINDF FTFTPHNSPL
     ELRCLLMDKI EGKNLDDWIK SHDKITQNLA WEWTKQLVEI LDVIHHNEFF HRDIKPANII
     LQPNGQLALV DFGTARRITD TYLAKISASG GTDTTIGNYE VTTVISPLYS PLEQINGRAV
     PQSDFYALGR TIVRLVTGVS LLQLPTDKKT GKLIWRNKAP QIDKPFADFL DELMSPLPGK
     RPQSTKIILE RLENLPWHSQ VHRIISSHIF KISIVSIFLL VSLASYIFLQ PVIAESFLNQ
     GKKALEQNQL DEAQNKFQQA VKIKPDIAKQ VSNFYLEQGI RRDISPQRAR QYYELSIKYN
     PQNGSAYNNL ALICQQLQDI ECVNNSYKEV FKLKPNKWES HYGLGSFYDE LGKYDLAEQQ
     YNLAIKSSDL ALDAVSNLAR IKVIQGQYEA AINIANKGLQ KAEEPELKAA LYKTIGWAKY
     EEKKYAEAEK NLEKAQSLDL QRVDTYCLLA KTQEALGKFE SARVWWEPCL LISTNLPEVV
     QWRVEILQRI QLPRNYETKK
//