ID T2M5S0_HYDVU Unreviewed; 784 AA.
AC T2M5S0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, 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};
DE Flags: Fragment;
GN Name=RIOK2 {ECO:0000313|EMBL:CDG67618.1};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG67618.1};
RN [1] {ECO:0000313|EMBL:CDG67618.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole animals {ECO:0000313|EMBL:CDG67618.1};
RX PubMed=24065732; DOI=10.1093/gbe/evt142;
RA Wenger Y., Galliot B.;
RT "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT bilaterian, euteleostome, and hominidae ancestors.";
RL Genome Biol. Evol. 5:1949-1968(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 -!- 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; HAAD01001386; CDG67618.1; -; mRNA.
DR AlphaFoldDB; T2M5S0; -.
DR EnsemblMetazoa; XM_002164409.3; XP_002164445.1; LOC100210529.
DR EnsemblMetazoa; XM_002164409.4; XP_002164445.1; LOC100210529.
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; 1.20.1480.30; Designed four-helix bundle protein; 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; IPR029390; AP3B_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PF14796; AP3B1_C; 1.
DR Pfam; PF01163; RIO1; 1.
DR Pfam; PF09202; Rio2_N; 1.
DR SMART; SM01355; AP3B1_C; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDG67618.1};
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 3..132
FT /note="AP-3 complex subunit beta C-terminal"
FT /evidence="ECO:0000259|SMART:SM01355"
FT DOMAIN 296..527
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 558..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CDG67618.1"
SQ SEQUENCE 784 AA; 88006 MW; 99F734ACAA18270A CRC64;
SVSPKNDVNI NLVPSLVSDM ESLSVDPKNC NSLSLQSSQK NSKSFELLSK INGKGLIAYY
RFPRTPCIYS GTMVAVEMEF TNSSNADVKR LRIENKKLLS GALMQEFNEV ASISPKESIT
VTVGIDFKDT VQPVTFDLCT ESGKFTVQIK VPVGELMRGV SLTQHEFTTQ QKKLTGMTES
KLACHLTESL PVLVSKIIEA VSMTQSPTVN ENVLRYEISG VVLYYLLSIK MVKLDAILLK
YMSREDFRVL TAVEMGMKNH EIVPLSLVSQ IASLKHGGCH KILKELVKNK LLCYENGRQG
TGYRLSYPGY DYLALKALAT RDVVYSVGNQ IGVGKESDIY IVADEDGTQY AMKLHRLGRT
SFRKIKEKRD YHKHRNSASW LYLSRIAAAK EFAFMKALYD RGYPVPRPVD FNRHCIIMEL
MDAFPLYQVN ELANPGAIYN DCMNLIVQLA SFGLVHCDFN EFNLMLETGN KIKVIDFPQM
VSTSHVNAAM YFARDVDCIR IFFKKRYGYE TDTYPTFSEI EREDNLDITL SASGYIKNKD
CDGNDDFQAE FEQMVSNQRH QTLDDQENED EERHSSFSDN SSDDDIVDEK KEPADNNQSC
ESDANSVVEV VNSAVDDVDS AVEVINTAVE DANSSVEVVN SAVKDVGSAI EDVSSAVEDA
NSAVEDVDSA VDDVNSAGKL ISNIDDCESE SSESESDENL ENYHTDNRNH RPYRDAKKLK
EISNTTLVKL KVQTQEDIKE KVKKIVLSKT QKDNHRRKVK KGESSVSTKL KQENRFVIKD
SLGE
//
