ID A0A075LVN2_9EURY Unreviewed; 307 AA.
AC A0A075LVN2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=PAP_08430 {ECO:0000313|EMBL:AIF70072.1};
OS Palaeococcus pacificus DY20341.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Palaeococcus.
OX NCBI_TaxID=1343739 {ECO:0000313|EMBL:AIF70072.1, ECO:0000313|Proteomes:UP000027981};
RN [1] {ECO:0000313|Proteomes:UP000027981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY20341 {ECO:0000313|Proteomes:UP000027981};
RA Zeng X., Shao Z.;
RT "Complete Genome Sequence of Hyperthermophilic Palaeococcus pacificus
RT DY20341T, Isolated from a Deep-Sea Hydrothermal Sediments.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AIF70072.1, ECO:0000313|Proteomes:UP000027981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY20341 {ECO:0000313|EMBL:AIF70072.1,
RC ECO:0000313|Proteomes:UP000027981};
RX PubMed=26383653;
RA Zeng X., Jebbar M., Shao Z.;
RT "Complete Genome Sequence of Hyperthermophilic Piezophilic Archaeon
RT Palaeococcus pacificus DY20341T, Isolated from Deep-Sea Hydrothermal
RT Sediments.";
RL Genome Announc. 3:e01080-e01015(2015).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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; CP006019; AIF70072.1; -; Genomic_DNA.
DR RefSeq; WP_048165564.1; NZ_CP006019.1.
DR AlphaFoldDB; A0A075LVN2; -.
DR STRING; 1343739.PAP_08430; -.
DR GeneID; 24842788; -.
DR KEGG; ppac:PAP_08430; -.
DR eggNOG; arCOG01181; Archaea.
DR HOGENOM; CLU_018693_1_0_2; -.
DR OrthoDB; 50101at2157; -.
DR Proteomes; UP000027981; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd05144; RIO2_C; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR030484; Rio2.
DR InterPro; IPR015285; RIO2_wHTH_N.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45852; SER/THR-PROTEIN KINASE RIO2; 1.
DR PANTHER; PTHR45852:SF1; SERINE_THREONINE-PROTEIN KINASE RIO2; 1.
DR Pfam; PF01163; RIO1; 1.
DR Pfam; PF09202; Rio2_N; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AIF70072.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 98..307
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 307 AA; 35957 MW; 18E2173C2FB0AE8A CRC64;
MVSKMLALDV YPNLKDVDFR VLRGVELNMR YHEWVPLEVI AKFARMDVDS ASHRLGKLDN
WKLVIRRSDI GYIGYQLTIH GYDTLAIRTF ARKGVIKALS STQIGVGKEA DVYVALTPQD
DKIAVKFNRI GLRTSFTRIK LYRREFVDKR HISWLYVSRL VAEREYEALR LLSPIAKVPK
PIAWNRHAIA MEFIDGVELV ELRDTDLTKE EAGNILDAVL EEYKKIVEFG IIHSDLSLYN
IVLKDNGDIL IIDWPQYVTT TFPQAEYYLE RDLRVILNAF ERKWRVKKNW EDVWKEFKSA
FKESLKE
//
