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Database: UniProt
Entry: M0F5T8_9EURY
LinkDB: M0F5T8_9EURY
Original site: M0F5T8_9EURY 
ID   M0F5T8_9EURY            Unreviewed;       329 AA.
AC   M0F5T8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=C467_11610 {ECO:0000313|EMBL:ELZ54597.1};
OS   Halorubrum hochstenium ATCC 700873.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1227481 {ECO:0000313|EMBL:ELZ54597.1, ECO:0000313|Proteomes:UP000011689};
RN   [1] {ECO:0000313|EMBL:ELZ54597.1, ECO:0000313|Proteomes:UP000011689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700873 {ECO:0000313|EMBL:ELZ54597.1,
RC   ECO:0000313|Proteomes:UP000011689};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELZ54597.1}.
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DR   EMBL; AOJO01000047; ELZ54597.1; -; Genomic_DNA.
DR   RefSeq; WP_008585347.1; NZ_AOJO01000047.1.
DR   AlphaFoldDB; M0F5T8; -.
DR   STRING; 1227481.C467_11610; -.
DR   GeneID; 72713219; -.
DR   PATRIC; fig|1227481.4.peg.2294; -.
DR   OrthoDB; 31344at2157; -.
DR   Proteomes; UP000011689; Unassembled WGS sequence.
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; IPR000687; RIO_kinase.
DR   InterPro; IPR018935; RIO_kinase_CS.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   NCBIfam; NF041310; Prot_Kin_Rio1_Halo; 1.
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; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS01245; RIO1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011689};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          48..299
FT                   /note="RIO kinase"
FT                   /evidence="ECO:0000259|SMART:SM00090"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..329
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   329 AA;  36656 MW;  4D4BA2D83BFA0454 CRC64;
     MSEDFGLLEP ADQPGDEWEQ LDVSDTEADR IARRQDREFD EFRKRIKDTE QFKLQESVFD
     DATLAAVYKL VQDGYVDAFG GPVSTGKEAS VFEALGGQAG ERPEPGSEAA GGGPEGVTPE
     REVAVKVYRI NSSNFRQMRE YLEGDPRFEG IASDKKAVVL AWTRKEFANL ERARKAGVRV
     PEPIAVQRNV LVMELVGHAE ERARRLSEVD VENPETAYEV VREYMRRLYG AGLIHGDLSE
     YNMIIHEGEL VIIDLGQAVT VHHPNAGEFL ARDCENVATF FTRQGIDVDP DDLRAYVTEP
     DPDPSGEPEV ESEDNPTGDP EGEPDRDDA
//
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