ID Q020I9_SOLUE Unreviewed; 885 AA.
AC Q020I9;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
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_3693 {ECO:0000313|EMBL:ABJ84664.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ84664.1};
RN [1] {ECO:0000313|EMBL:ABJ84664.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ84664.1};
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; ABJ84664.1; -; Genomic_DNA.
DR AlphaFoldDB; Q020I9; -.
DR STRING; 234267.Acid_3693; -.
DR KEGG; sus:Acid_3693; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG0823; Bacteria.
DR HOGENOM; CLU_012906_0_0_0; -.
DR InParanoid; Q020I9; -.
DR OrthoDB; 101360at2; -.
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; 2.120.10.30; TolB, C-terminal domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR Pfam; PF07676; PD40; 5.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 1.
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:ABJ84664.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABJ84664.1};
KW Transferase {ECO:0000313|EMBL:ABJ84664.1}.
FT DOMAIN 11..276
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 885 AA; 95886 MW; 81E40D8BCC09A963 CRC64;
MLSPGTAIGP YEILSLLGSG GMGEVYRARD QRLARTVALK VLPPEFAADS IRRQRFEQEA
RAASALNHPN ILSVFDMGSQ DGLVYIVSEL IEGESLRDLI RRGPLPQSRA VEIAGQVADA
LAAAHAANIV HRDLKPENIM LTRDGRAKIL DFGLAKQVQP RVPGSDETQF LTRTSPGAIL
GTAGYMSPEQ VRGEPVDPRS DIFSFGLVLY ECLSGRAPFE RQTGAEMMTA ILREDPPELP
ETVFPALRQI VHHCLEKDAV RRFHSANDLA FALRTVQTSG TASRSGISLA PAEVNAPRRR
WLWPTLAIAL ALLLAVPHFM ELDPIDLAAY RFIPFANDHE AESGPAWSPD GKSIAYLKTV
AGIPQLMVRG LESPTAIQLT RSTTRVSSAF WSPDSAVVYC IDRAGKGELW GISPSGGHAV
KILEDLHTAD ISPDGKSLAI WRATESGGAV KSSLWISSPP GAAPRPYLPA PFEVPLESNG
GSLHFSPDGK SILLVASGIA PQVWVLPFPA SSGAPRRVFS ATNFNFVPRG AWMPDSRHAV
LSFSTGGAQP ALWFADLERE KLRKLTASTA AEEFPSLAPD GRRLVFTSVT DDFDLIELPL
DGTAPRTLLA NSRNMYSPAW SPDGDQLLYA TDRSGASEIW SRNVKASIDR PMVTARDFPP
GTTTALTHPV FSPDGSRFAF VRYATDQPAT IWVEPTVGGA PIRMASEYMV SPTWSPDGNS
IAGLMHRDRP WQPAIVEVGA NMSPHVIASA PTCLMPMEWS PTGEWLACEA RTGIELFSRD
GARRRTLPRL NSSAIAFSRD GGTLYAAGRD AGRTFLKAID LATGAIRDIA QHSGTMVISG
GATYQARLSL SHDGRSLVTS AVESQSDLWI LEGYPHPRPW WQLIK
//