ID   Q1IJL4_KORVE            Unreviewed;       746 AA.
AC   Q1IJL4;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=Acid345_3936 {ECO:0000313|EMBL:ABF42936.1};
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Koribacter.
OX   NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF42936.1, ECO:0000313|Proteomes:UP000002432};
RN   [1] {ECO:0000313|EMBL:ABF42936.1, ECO:0000313|Proteomes:UP000002432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345 {ECO:0000313|EMBL:ABF42936.1,
RC   ECO:0000313|Proteomes:UP000002432};
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000360; ABF42936.1; -; Genomic_DNA.
DR   RefSeq; WP_011524735.1; NC_008009.1.
DR   AlphaFoldDB; Q1IJL4; -.
DR   STRING; 204669.Acid345_3936; -.
DR   EnsemblBacteria; ABF42936; ABF42936; Acid345_3936.
DR   KEGG; aba:Acid345_3936; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG5616; Bacteria.
DR   HOGENOM; CLU_013589_0_0_0; -.
DR   OrthoDB; 9797180at2; -.
DR   Proteomes; UP000002432; Chromosome.
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   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   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 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:ABF42936.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002432};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABF42936.1};
KW   Transferase {ECO:0000313|EMBL:ABF42936.1}.
FT   DOMAIN          12..288
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   746 AA;  83188 MW;  42720CE7AE690ED1 CRC64;
     MENIIGQTLS HYVVSRKLGS GGMGVVYQAE DTTLGRHVAL KFLPDSLAQD SHALERFQRE
     ARASSALNHP NICTVYAIEQ HERQHFIVME LLEGQSLAAM IGKSAFEIEQ LLALAIQIAD
     ALESAHAKGI VHRDIKPANI FVTPRGQVKI LDFGLAKMEL LKPSVGVATV SQMETVGQRD
     DLTIPGTALG TVAYMSPEQA RGQFTDSRTD LFSLGTVLYQ MGTGVLPFQG DTTAVVYEAI
     LNRDPVPVAE VNGALPQAFA RIVEKALEKD RTLRYQTAND IKTDLTRLKR DLDSRERRAS
     SQSESRTAAA KPAAKSVAVL YFENLSGSKE DEYFRDGITE DIITELSKIK GLNIFSRPTV
     LAYRDKQVTP AHIGQQLRAA YVLAGSLRRS GNRLRITTQL VDTTTDFPIW SERYDREMKD
     VFEVQDEIAG KIAQALRVTL SPQEQQEIAA KPTDNLQAYD LYLRGKSYAR RLQRQDLEFA
     LQMFENAVIL DPNFALAFAA IANVCAQNHY NYGRDPEWMQ RAMHASETAV VLRPDLPEVQ
     VGQAWILYAN NKYDEATAVI QRAIERKRDC EGAYYILFRT LFSAGRYQEV ANLAEAAVEA
     SGDDYNIYVP IMNSLGALGK TEALRNFRQR DISALERHLK QVPEDARARI LLATDYATEG
     RMEEAARETS LAMTLRPNEA TVLYNAACVF CTMNKKSEAM DALAKAWHAG FKDPAWVRRD
     PDLELLHGDP EFERLYPPNA TGAIAN
//