ID A0A1I1H3E1_9FIRM Unreviewed; 349 AA.
AC A0A1I1H3E1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:SFC18444.1};
GN ORFNames=SAMN02910398_01675 {ECO:0000313|EMBL:SFC18444.1};
OS Butyrivibrio sp. YAB3001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520812 {ECO:0000313|EMBL:SFC18444.1, ECO:0000313|Proteomes:UP000198944};
RN [1] {ECO:0000313|EMBL:SFC18444.1, ECO:0000313|Proteomes:UP000198944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YAB3001 {ECO:0000313|EMBL:SFC18444.1,
RC ECO:0000313|Proteomes:UP000198944};
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOKR01000006; SFC18444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1H3E1; -.
DR STRING; 1520812.SAMN02910398_01675; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000198944; 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; 1.10.510.10; 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 PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFC18444.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000198944};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:SFC18444.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..252
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 349 AA; 38956 MW; 15FDF9D82F695A27 CRC64;
MSRYRIIKQL GQGGNSTVFM GKDLETGQKV TVKKCRAGEM GYDIHVKKSL ENEARILGKL
KHPAIPKLIE SRDDEIVLEY VPGKSLEKVM LAEGVFKEKE ALVIAKEVIA ILRYLHGLRE
PVIYRDLKPA NVVLKPNGHV SLIDFGAARI YRYSDCSDTV NLGTLGFAAP EQFGNLGQTD
PRTDIYCFGM MLLQLVSGVD TKDTEAVANY KQNGVKGISS EFMHIIDKCT RPDRDDRFKS
AREIEDALND FPKRQIKRKA AMWVKLASIS AVASLMISFG TPKVPLLFKM AENDMNLRIP
AVLGRIANAK TRIEEMIDKK GEKDGVVSLY IYDNTDSTVS YSGNGQHSY
//
