ID   Q029D0_SOLUE            Unreviewed;       877 AA.
AC   Q029D0;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 99.
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_1368 {ECO:0000313|EMBL:ABJ82361.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ82361.1};
RN   [1] {ECO:0000313|EMBL:ABJ82361.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ82361.1};
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; ABJ82361.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q029D0; -.
DR   STRING; 234267.Acid_1368; -.
DR   KEGG; sus:Acid_1368; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG5616; Bacteria.
DR   HOGENOM; CLU_013589_0_1_0; -.
DR   InParanoid; Q029D0; -.
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; 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   Pfam; PF13432; TPR_16; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 4.
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.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABJ82361.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABJ82361.1};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:ABJ82361.1}.
FT   DOMAIN          81..376
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          718..751
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   BINDING         112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   877 AA;  96617 MW;  9670222D099246F9 CRC64;
     MTPERWERAK EVVQGAWEHD VAERGVYLDE ACAGDQEMRA EVESLLASDQ NASGFLATPV
     RELIQQATLP EYWAGRRLGA YQMVREIGHG GMGTVYLAER ADGEYRMQVA IKLVSPHLCT
     EAVLRRFRTE RQVEASLDHP NITRLLDGGT TDDGLPYLVM EYVDGVRIDA WCDSRKLSVR
     DRLKLFRQVC AAVQSAHEKE IVHRDIKPGN ILVTADGTIK LLDFGISKVL NRELFDTPET
     TLGETPMTPE YASPEQIRGL RVGPATDIYS LGVVLYQLLT GSLPFASQRE QRQVMRAICE
     EEPLKPSAAI HQETVLAGQQ GMVAETTSQA RGESPTGLRR LLSGDLDNIV LKALRKEPER
     RYPTVRALSE DLDRFLQDLP VEARKDSLPY RSLKFLKRNR ALITVGMISA VLVLAVDLGS
     RKSSRYNLAP DNASIAVLPF ADISPGKDQK YFAEDLTDGL LGMLASIPGL RLSGRESSSK
     FQGSTQNVAA ICKALNVSAV LDASIGNEGG HAKINAHLRA ADGRQLWAGT YNREANEIFA
     VQEEMTQAIA VALNLKPPKR TASPSMTTTP AAYRLFLQGE YFRDQGNVPQ AISYFEQTLG
     KDRGYAPAWV ALADAHAQMA GGGTIPAAEG YGKAREELES ALALNPHLAE AHALKGYIKM
     LHERDWPGAD ASVQRALALA PGSDGAIRIA AFLARILGRL DEAIVLCRRA VELNPIYYNS
     YKNLGITLYY AGRPTEATGT LQKALELNPK TRYAHAYLCL ANLAESRPQE GLTEAEKELN
     PGYRLSALAM AYQALGERAK SDASLRELIA EQGADLSYQV AEVYAFRGEK ELAFQWLDRA
     YAQNSDSLPE MKADPLFADI RSDARYSALL QKLRLPQ
//