RIO1_HALVD
ID RIO1_HALVD Reviewed; 290 AA.
AC D4GYY1;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=RIO-type serine/threonine-protein kinase Rio1;
DE EC=2.7.11.1;
DE EC=3.6.3.-;
GN Name=rio1; OrderedLocusNames=HVO_0135; ORFNames=C498_18913;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND AUTOPHOSPHORYLATION.
RX PubMed=20671954; DOI=10.1155/2010/481725;
RA Humbard M.A., Reuter C.J., Zuobi-Hasona K., Zhou G., Maupin-Furlow J.A.;
RT "Phosphorylation and methylation of proteasomal proteins of the haloarcheon
RT Haloferax volcanii.";
RL Archaea 2010:481725-481725(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase that is able to
CC autophosphorylate as well as to phosphorylate proteasome subunit alpha
CC 1 (PsmA1) in vitro (PubMed:20671954). Despite the protein kinase domain
CC is proposed to act predominantly as an ATPase (By similarity).
CC {ECO:0000250|UniProtKB:G0S3J5, ECO:0000269|PubMed:20671954}.
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:0000269|PubMed:20671954};
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:0000269|PubMed:20671954};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20671954};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20671954};
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000305}.
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DR EMBL; CP001956; ADE02358.1; -; Genomic_DNA.
DR EMBL; AOHU01000105; ELY24349.1; -; Genomic_DNA.
DR RefSeq; WP_004045247.1; NZ_AOHU01000105.1.
DR AlphaFoldDB; D4GYY1; -.
DR SMR; D4GYY1; -.
DR STRING; 309800.C498_18913; -.
DR EnsemblBacteria; ADE02358; ADE02358; HVO_0135.
DR EnsemblBacteria; ELY24349; ELY24349; C498_18913.
DR GeneID; 8925605; -.
DR KEGG; hvo:HVO_0135; -.
DR PATRIC; fig|309800.29.peg.3685; -.
DR eggNOG; arCOG01180; Archaea.
DR HOGENOM; CLU_018693_3_3_2; -.
DR OMA; EIRCAKV; -.
DR OrthoDB; 44076at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 InterPro; IPR008266; Tyr_kinase_AS.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Kinase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..290
FT /note="RIO-type serine/threonine-protein kinase Rio1"
FT /id="PRO_0000428911"
FT DOMAIN 79..290
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 235
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 85..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
SQ SEQUENCE 290 AA; 33008 MW; BD7C0D447E249F3A CRC64;
MTDEFGMVEP QEGEAFGDEW EEIDVSDDEA DRIARRKDRD FDEFRMRLKD ADQFKVEQSV
FDDATFAAIY KLVQDGHIDA FGGPISTGKE ANVFEALGGD DADVAVKIYR INASDFRHMR
DYLEGDPRFE NIGHDKGQVV RAWVRKEFAN LERAQRAGVR VPKPIAVQRN VLVMELVGVV
DDRARRLSEV RVENPQTAYE VVREYMRRLH RAGLVHGDLS EYNLIIHDGE LVVIDLGQAV
TVHHPNAEEF LRRDCRNVAN FFRRQGADAD GDSLYEFVTG DEGEDGDGDE
