ID   Q01NG0_SOLUE            Unreviewed;       885 AA.
AC   Q01NG0;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
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_7916 {ECO:0000313|EMBL:ABJ88810.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ88810.1};
RN   [1] {ECO:0000313|EMBL:ABJ88810.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ88810.1};
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; ABJ88810.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01NG0; -.
DR   STRING; 234267.Acid_7916; -.
DR   KEGG; sus:Acid_7916; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG5616; Bacteria.
DR   HOGENOM; CLU_013589_0_1_0; -.
DR   InParanoid; Q01NG0; -.
DR   OrthoDB; 9797180at2; -.
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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 3.40.50.10070; TolB, N-terminal domain; 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   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
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; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
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:ABJ88810.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABJ88810.1};
KW   Transferase {ECO:0000313|EMBL:ABJ88810.1}.
FT   DOMAIN          107..371
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          260..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   885 AA;  97317 MW;  3CD618816596F8C9 CRC64;
     MTQGRWRQIT EILRAAWELE GRERAAYLDR ALTDDGELRA QVEALLASDG SASDFLAVPA
     VAMAGEVWVP AADAEEEQRV QAAIVRAVGQ LADEEGCELI GTRIGRYSIA GLIGRGGMGT
     VYRAEREDDF HTQVALKVLK RGTDTEKALS RFRSERQILA GLQHPNIARL LDGGATGAGL
     PYFVMEYVEG APLLEYAAPL PVRERVKLFR SLCAAVQYAH EKRIVHRDIK PSNILVNRDG
     VPKLLDFGIA KLLDAEAEDG TASTATGARP MTPDYASPEQ LRGEQVTTAS DIYSLGAVLY
     ELVTGRRARL AAKYTAAEIE AICKSDPKRP GAVCAEVGPD LDNIILMALR NEPERRYASV
     EQFAGDIDRF LQRLRVHART DKLYGIRRLV RRNRTWLGAI LVSAALVAAL AASLDKARRA
     REPAAGGVRS IAVLPLENLS GGREQDYFAD GITDALISDL AQIHGLRVIS RTSVMSYKGV
     SRRLPAIART LGVQTIAEGS VLRAGNHVRI AVRLVEASKD SPVWSGSYEG ELRDVLTVQN
     QVAAAIAGEI RVALAAPDRA RLSRHQRVDL VAYDEFLKGR HDYLAEFTRE SADRAIAHFH
     QALKLDPSYA PAYAGLADCY YMVSSMYYAP AEVMPKAKTA ALKALQLDDT LGEAHATLAL
     VQSLFEFNRA AAERGFRRAI ELKPGDAQVH LWYSLHLAGL GRFDEAAAEV EEAQKLDPVS
     PAINAYAGPP LYLAHRYDQA IQRMQPVAET FPDYVHPHAW LALSYEQKGE WDKAIAEMEK
     AYALDQEPQS LAQLGHIYAG AGRTKAARKV LRQLRGLAGQ RYVSAYDIAL LYAGLGDKEE
     AFRWLLKVEQ DRSEWFAVVN VDPRLEGFHS DPRFASVLRS VGLAR
//