ID Q9V137_PYRAB Unreviewed; 266 AA.
AC Q9V137;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 131.
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=PAB0405 {ECO:0000313|EMBL:CAB49514.1};
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844 {ECO:0000313|EMBL:CAB49514.1, ECO:0000313|Proteomes:UP000000810};
RN [1] {ECO:0000313|EMBL:CAB49514.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Orsay {ECO:0000313|EMBL:CAB49514.1};
RA Genoscope;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAB49514.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Orsay {ECO:0000313|EMBL:CAB49514.1};
RX PubMed=10736225; DOI=10.1006/jmbi.2000.3593;
RA Gaspin C., Cavaille J., Erauso G.;
RT "Archaeal homologs of eukaryotic methylation guide small nucleolar RNAs:
RT lessons from the Pyrococcus genomes.";
RL J. Mol. Biol. 297:895-906(2000).
RN [3] {ECO:0000313|EMBL:CAB49514.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Orsay {ECO:0000313|EMBL:CAB49514.1};
RX PubMed=11381026; DOI=10.1101/gr.GR1653R;
RA Lecompte O., Ripp R., Puzos-Barbe V., Duprat S., Heilig R., Dietrich J.,
RA Thierry J.C., Poch O.;
RT "Genome evolution at the genus level: comparison of three complete genomes
RT of hyperthermophilic archaea.";
RL Genome Res. 11:981-993(2001).
RN [4] {ECO:0000313|EMBL:CAB49514.1, ECO:0000313|Proteomes:UP000000810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay {ECO:0000313|Proteomes:UP000000810}, and Orsay
RC {ECO:0000313|EMBL:CAB49514.1};
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G., Barbe V., Flament D., Galperin M., Heilig R., Ripp R.,
RA Lecompte O., Prieur D., Poch O., Quellerou J., Thierry J.C.,
RA Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [5] {ECO:0000313|EMBL:CCE69984.1, ECO:0000313|Proteomes:UP000009139}
RP GENOME REANNOTATION.
RC STRAIN=GE5 {ECO:0000313|EMBL:CCE69984.1}, and GE5 / Orsay
RC {ECO:0000313|Proteomes:UP000009139};
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(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};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
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DR EMBL; AJ248284; CAB49514.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69984.1; -; Genomic_DNA.
DR PIR; C75179; C75179.
DR RefSeq; WP_010867716.1; NC_000868.1.
DR AlphaFoldDB; Q9V137; -.
DR STRING; 272844.PAB0405; -.
DR GeneID; 1495497; -.
DR KEGG; pab:PAB0405; -.
DR PATRIC; fig|272844.11.peg.630; -.
DR eggNOG; arCOG01180; Archaea.
DR HOGENOM; CLU_018693_3_3_2; -.
DR OrthoDB; 31344at2157; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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; cd05145; RIO1_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; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF2; SERINE_THREONINE-PROTEIN KINASE RIO1; 1.
DR Pfam; PF01163; RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAB49514.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:CAB49514.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 50..266
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 266 AA; 31720 MW; D2BE928026D1473D CRC64;
MERLDREIAE VLGLTDKREK DSELFKVFSE VFDKTTVETI SYFYRRGIIE RLYGVLSTGK
EANVFAGYNS KGEKIAVKIY RTYTTEFRRI WEYLAADPRI GALPKDIRKL VFVWTRREYK
NLQRALKYAV RAPEPIAFRN NVLVMEFIGD DMPAPRLKDV EKELEKEDFE ELYDFMMGSI
EKLWKRGDMV HGDLSEYNLL LWHEPVIIDW SQATVKRNRM SLTLLYRDIR NVINYFKRKG
IDVEDPEEKF RELAGDELWM RNLRSL
//
