ID   Q01QI7_SOLUE            Unreviewed;      1030 AA.
AC   Q01QI7;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=Acid_7172 {ECO:0000313|EMBL:ABJ88083.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ88083.1};
RN   [1] {ECO:0000313|EMBL:ABJ88083.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ88083.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Janssen P.H., Kuske C.R., Richardson P.;
RT   "Complete sequence of Solibacter usitatus Ellin6076.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000473; ABJ88083.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01QI7; -.
DR   STRING; 234267.Acid_7172; -.
DR   KEGG; sus:Acid_7172; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_294381_0_0_0; -.
DR   InParanoid; Q01QI7; -.
DR   OrthoDB; 5526368at2; -.
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; 1.25.40.10; Tetratricopeptide repeat domain; 3.
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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13432; TPR_16; 2.
DR   SMART; SM00028; TPR; 9.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 3.
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:ABJ88083.1};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABJ88083.1};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:ABJ88083.1}.
FT   DOMAIN          88..360
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          782..815
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   1030 AA;  112913 MW;  C997F602881403E6 CRC64;
     MTPQRWPLAR KLFDAAVKLG PAEADAYLRA ECGDDAELLS EVRAMLEEHR RTGALDRPAW
     DFTPASPPSV PSGAAPVFGP GQVVAGRYTI VRYLSRGGMG EVYEAEHPLL PDHVALKTLL
     PAIASDEAMI ARFKQEIQLA RKIAHPNVCK VFDLEWHPAE GSTILFLTME FLPGETLAAR
     IQREGRLRPA EALPLLQQMA DALDAAHRSG VIHRDFKTSN VMLVPGAAGI RAVVTDFGLA
     RGVTTAAETT ATLTNNVAGT LDYMAPELMN GSVATFRSDI YALGAVAYKT ITGSLPFAGE
     APLAAAFLRA RKPIPSPRTL VPDLDPKWEH AILRALDPEP GRRFSDVREF PRALRGEPVS
     VTVALPTLTR RKVVAAVCVV AALAAAGIGW RTWSRSRTQP GPEAARLYQQ GVDDIHAGAY
     FAATKALDQA VQLAPAFAPA RARFAESWVE LDLPEKALRE FLPIRRQDTS SLSTLDQLQI
     EAVDRTITRE FPAAVEKYEQ MRKVTPSAEL DIDLGRIYEK AGKPDNAIEA YRRGAEGPSH
     SPAAWLRLGV LYAQRKKLTE SDAAFAEAER RYQQSSNLEG ITELTLQRGV AANRASRFPE
     AAALLRKAME HAHDAGNLQQ EISAKLTLAN VSYKAGDTDL AETLAREALA TAQTNQLESL
     TIRGLINLGT SQIGKGDLKG AEQRLQDALA LALRTNSTKF VAQTQLNLAS LHDTLHRSDD
     QIREANQALA YFQPNRWVQE TFSGLTLLGR AELYRGNFAA AIPPFQRLFD EASKAGDSPN
     MARAQEALGN AFADSEMYPQ ALENYREFLR LSADDPQLNS YAALDCALTL SRLGRAQEAL
     PELARAEAAK LTRLRISIPR ARAEMALMLN NWREARDRAR STLAEGNVNP PAILDLTRIL
     GLALLRSGDR KAGLQKCEEA LALANKLNDV GSLVDTRLAL IEALLANRDS ARTLAVFHEL
     EPLLASHPET RWRAYGLMSH ADPQYAGRAK EAFTQLDSLW GHDAFLRYLS RPDFQELTRP
     FLQPIPAKHP
//