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Entry: W2SJR3_NECAM
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Original site: W2SJR3_NECAM 
ID   W2SJR3_NECAM            Unreviewed;       467 AA.
AC   W2SJR3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Serine/threonine-protein kinase RIO3 {ECO:0000256|PIRNR:PIRNR038146};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038146};
GN   ORFNames=NECAME_15087 {ECO:0000313|EMBL:ETN69778.1};
OS   Necator americanus (Human hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC   Necator.
OX   NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN69778.1, ECO:0000313|Proteomes:UP000053676};
RN   [1] {ECO:0000313|Proteomes:UP000053676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24441737; DOI=10.1038/ng.2875;
RA   Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA   Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA   Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA   Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA   Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT   "Genome of the human hookworm Necator americanus.";
RL   Nat. Genet. 46:261-269(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         ECO:0000256|PIRNR:PIRNR038146};
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         ECO:0000256|PIRNR:PIRNR038146};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038146};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC       kinase family. {ECO:0000256|ARBA:ARBA00009196,
CC       ECO:0000256|PIRNR:PIRNR038146}.
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DR   EMBL; KI669049; ETN69778.1; -; Genomic_DNA.
DR   RefSeq; XP_013292005.1; XM_013436551.1.
DR   AlphaFoldDB; W2SJR3; -.
DR   STRING; 51031.W2SJR3; -.
DR   EnsemblMetazoa; NECAME_15087; NECAME_15087; NECAME_15087.
DR   GeneID; 25355114; -.
DR   KEGG; nai:NECAME_15087; -.
DR   CTD; 25355114; -.
DR   OMA; HDPQLCA; -.
DR   OrthoDB; 5481355at2759; -.
DR   Proteomes; UP000053676; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR017406; Ser/Thr_kinase_Rio3.
DR   PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR   PANTHER; PTHR45723:SF1; SERINE_THREONINE-PROTEIN KINASE RIO3; 1.
DR   Pfam; PF01163; RIO1; 1.
DR   PIRSF; PIRSF038146; Ser/Thr_PK_RIO3; 2.
DR   SMART; SM00090; RIO; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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:0000256|PIRNR:PIRNR038146};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR038146};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR038146};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR038146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053676};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR038146};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038146}.
FT   DOMAIN          215..412
FT                   /note="RIO kinase"
FT                   /evidence="ECO:0000259|SMART:SM00090"
SQ   SEQUENCE   467 AA;  53268 MW;  9A9FE644989038A4 CRC64;
     MSGKGECSAW GGKTAWGRRE EDCEPIVSFV EIMSEELADS LNEEERRKEQ DYLNTVALSE
     SAPVYSNDEE MAKALQREFD REYDLSVRLN QEKQKGKSTA TITVTPDRYC PKTTQDSDQS
     SDDEDVRQFA TDLLYAKLSD DVPAHSGSVY RNAGGELVTK HDANVSARRN ADKTMNDQVN
     LAFGDMRKEQ INSRVYNSLR SFSKTEAKRH HKLKDKEEKA TIETSMDAVT RLHLFKWINQ
     GVFDRVEGII ATGKESAVLN AASDETGERF AVKVYKTSLT EFKNRMAKVG LPCPVPVKLK
     RHLLVMSFIG EQGEAAPRLK NIDWDFFTTE ERKNIFLQVQ DIMCRMYKEC KLVHGDLSEF
     NLLLAAGKIS FNSRVIFYFD FSRDIENVLA FFQKLDIVDL PTPVALFNMI TDLNMGEEGS
     LLVQVEQFSE DNRANHINKS KPADFEWAAY NKERKELRGE SPARDYN
//
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