ID A0A1M5G1I3_9BACT Unreviewed; 353 AA.
AC A0A1M5G1I3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:SHF97573.1};
GN ORFNames=SAMN05720760_102245 {ECO:0000313|EMBL:SHF97573.1};
OS Fibrobacter sp. UWB8.
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=1896207 {ECO:0000313|EMBL:SHF97573.1, ECO:0000313|Proteomes:UP000184492};
RN [1] {ECO:0000313|Proteomes:UP000184492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWB8 {ECO:0000313|Proteomes:UP000184492};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FQVZ01000002; SHF97573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5G1I3; -.
DR Proteomes; UP000184492; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PTHR11042:SF196; AGC FAMILY PROTEIN KINASE; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 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}; Kinase {ECO:0000313|EMBL:SHF97573.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SHF97573.1};
KW Transferase {ECO:0000313|EMBL:SHF97573.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 329..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..283
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 353 AA; 39991 MW; F8D5EEBAF5D72B99 CRC64;
MASESKKPAK IGGYTPTQEL GSGAMGQLWL CHDKSLDRMV VVKQMQQDIE DSDVNIRRFM
QEGNILAHLN HPAITKPYAL WKEKDGKLSL SMEFVHGLTL RQILDKVPQP PLWVVLNILH
EILCALGEAH RKGIVHRDLK PANIMVDNDG RVHLLDFGIA HTENPLKFSK GEDAERLTQT
GAILGTVTYM SPEQTLGEEA TPASDLFAIG IIASEMLLGQ NLFRGTSFSD TLTRIQKLRV
TEKAFSKEIP RRLRKLIERM LQKDPRKRPL TAFDAAEQVS QVMRNFPRDM VPYMAMWIYA
IKDSIKQKTE SIDETLYTEP PVYPTHRKFL LFKGFCMGAL AGSLICFLIT RFI
//
