ID M9U6C9_SULIS Unreviewed; 254 AA.
AC M9U6C9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=SiL_0164 {ECO:0000313|EMBL:AGJ61643.1};
OS Sulfolobus islandicus LAL14/1.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=1241935;
RN [1] {ECO:0000313|EMBL:AGJ61643.1, ECO:0000313|Proteomes:UP000013006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAL14/1 {ECO:0000313|EMBL:AGJ61643.1};
RX PubMed=23594878; DOI=10.1098/rsob.130010;
RA Jaubert C., Danioux C., Oberto J., Cortez D., Bize A., Krupovic M., She Q.,
RA Forterre P., Prangishvili D., Sezonov G.;
RT "Genomics and genetics of Sulfolobus islandicus LAL14/1, a model
RT hyperthermophilic archaeon.";
RL Open Biol. 3:130010-130010(2013).
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; CP003928; AGJ61643.1; -; Genomic_DNA.
DR RefSeq; WP_015580636.1; NC_021058.1.
DR AlphaFoldDB; M9U6C9; -.
DR GeneID; 15296655; -.
DR KEGG; sic:SiL_0164; -.
DR HOGENOM; CLU_018693_3_3_2; -.
DR Proteomes; UP000013006; 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:AGJ61643.1};
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:AGJ61643.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 45..254
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 254 AA; 29779 MW; BD13D4B2B81D18E3 CRC64;
MTELPKKTKD EKRRKDEDLF KVVDSTIDYR TYLNLIQIAR RLNIEEYLGA ISSGKEARIY
PAKTFDNKYY AVKIYYTSTA QSKRAIKKYT VGDIRFEDVK VTNTKQLINT WAKKEFKNLS
RLYEAGTRVP KPILVYENIL VMEFIGENGL RAPLLKELND EEITQELYDD LIQQVEIMTK
RAKLVHGDLS EYNVMVYDNK CYIIDVSQAI PIDYEDAIML LKRDLDNINR FFEDKRINIK
PTEELLIEFG VSGD
//
