ID H5SD04_9BACT Unreviewed; 379 AA.
AC H5SD04;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:BAL54040.1};
GN ORFNames=HGMM_F12C05C23 {ECO:0000313|EMBL:BAL54040.1};
OS uncultured Planctomycetota bacterium.
OC Bacteria; Planctomycetota; environmental samples.
OX NCBI_TaxID=120965 {ECO:0000313|EMBL:BAL54040.1};
RN [1] {ECO:0000313|EMBL:BAL54040.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAL54040.1}
RP NUCLEOTIDE SEQUENCE.
RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT Pathway Dominates a Subsurface Ecosystem.";
RL PLoS ONE 7:e30559-e30559(2012).
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; AP011676; BAL54040.1; -; Genomic_DNA.
DR AlphaFoldDB; H5SD04; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR025874; DZR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF12773; DZR; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAL54040.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:BAL54040.1};
KW Transferase {ECO:0000313|EMBL:BAL54040.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 59..319
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 379 AA; 42415 MW; 477F4ED55A46D3A0 CRC64;
MCLECGWTCE TEPVAEAGAP VVLCTNPACG AANPVGQQYC QRCQTMLPSA PGSMLEGRYR
IEKLLAMGGF GAVYRAVDTR TNLTVAIKDM ICPDAEEFKI RLSFFRREAE ILRALSKLPI
VPRVYDFIQK GQSAHLVLEF IEGTDLVKVM EANGNRPFPI DLVIEWGKQI CDVLHHMHSM
DPPVVHRDLK PDNIMLLADG KSIKLIDFGT ARDLGRTART RLQAKTRVYT EGYAPPEQII
GKPEPRSDLF ALAGTLYHLA TGRAPEGVFT GKEIAELLAM PNGTVPPQHR WFFELIRINL
SEDVNERYFT AREFKADLEA RRVTTETHCP HCQTVNKVRE PYCLKCAAPL TDLAPPCQQC
GKTNRMGSRF CIHCGNRLR
//
