ID A0A1G6UBG9_9GAMM Unreviewed; 930 AA.
AC A0A1G6UBG9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=SAMN04488509_102230 {ECO:0000313|EMBL:SDD37947.1};
OS Aquimonas voraii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Aquimonas.
OX NCBI_TaxID=265719 {ECO:0000313|EMBL:SDD37947.1, ECO:0000313|Proteomes:UP000199603};
RN [1] {ECO:0000313|EMBL:SDD37947.1, ECO:0000313|Proteomes:UP000199603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16957 {ECO:0000313|EMBL:SDD37947.1,
RC ECO:0000313|Proteomes:UP000199603};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNAG01000002; SDD37947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6UBG9; -.
DR STRING; 265719.SAMN04488509_102230; -.
DR OrthoDB; 9783151at2; -.
DR Proteomes; UP000199603; Unassembled WGS sequence.
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; 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; PF13374; TPR_10; 2.
DR Pfam; PF13424; TPR_12; 1.
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; 2.
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:SDD37947.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000199603};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SDD37947.1};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:SDD37947.1}.
FT DOMAIN 75..351
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 582..615
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 930 AA; 100838 MW; 7849EED429672412 CRC64;
MSARSNRELF DQALSLAPES REGWLAGAAA NPEQLRQVRA LLAASDADSA IVGRVRRAAD
ASSRELGWSD HIGPYRLLEL LGEGGMGMVW MAERDDGEFR QRVAIKTLRG RASPSAVERL
RQERQIQAGF VHPHIARLLD GGTTAAGDPY LVMDYIDGMP LRDWLLATRP GLAQRLQLFA
LLCRAVAFAH QRLVVHCDIK PGNVMVRADG SPALLDFGVA QWLGFANEDA PELSFAGTPA
YASPEQLLRQ PVTVQTDVWG LGMLMIELLS GVRPACRIVD GRVEELPLAS SLAQTLDEKT
RAERQALAPQ ALRGDLDCLL AKALRIEARQ RYSGAAELAI DLENHLAHRP VSARGGHWRY
LLGKSLRRHR AAVAAGALSL AALTALSVSL LRQYEQTRMA LAVAEQRQQE LGSTVGFLTR
LFSEFDPNVA PGRALTPKAL TDLAKARLDA LPDMPAGARI ELMHSLGSIY NNLGANEPAL
ELSLRLIDLL HRQAASNDAL ARARLLAAIS LERLGRNREG LAMAQQAERD SRASDDPLLR
GESLLALGLA WQNAADPAAA EASYAQAETW FRRSAEGQPG LAKLLHNRGH LALYQGETQR
ALEAYREAVR IKTLLADADH PTVFTSRMGE AKALSRLGAF SEALAVLTDL IPRVERTLGT
ASDRYRILQS ELGSVYQDLG ELAPSRSAYL RAVELSQRDG HEDLNYAFLL NNLASLDELR
GDTDQALAGY AQSLALRERL GADAVSLARV RMNMARTLIA AGQVDAAQTL IGDAMAARQQ
HLAADHPDQS QAPALLLLSA VARRDSQGVE SNLAVLHAAL AGSIAGMSPL QHSQVELAIA
EGERTLQRVD RASEFAARAH QRRSELFPAG HPMRAQSALV WARVRLAAGD RAQASRLIAQ
AAPIIESQMH AGAPLRGELA RLRAALLKPR
//
