ID A0A1Q9D627_SYMMI Unreviewed; 903 AA.
AC A0A1Q9D627;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=RIOK1 {ECO:0000313|EMBL:OLP90612.1};
GN ORFNames=AK812_SmicGene27797 {ECO:0000313|EMBL:OLP90612.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP90612.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP90612.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP90612.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OLP90612.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSRX01000702; OLP90612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9D627; -.
DR OrthoDB; 5481355at2759; -.
DR Proteomes; UP000186817; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05147; RIO1_euk; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
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 SUPFAM; SSF53098; Ribonuclease H-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:0000313|EMBL:OLP90612.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 325..563
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
SQ SEQUENCE 903 AA; 101252 MW; 88667AF11A8F3C80 CRC64;
MEMHTCTPEC DEVLDADLLT LSRQRSPKPA VRQRSLKGDA PERRVSFDHE RLCEVIQFVP
SSPMRRGWNS EDEYDGDTDK SALTQGRIWE TISASVAKVL GLESHEEIPP CFTQALDVPT
LVIEHDSGNC GGHKANHRCS GSTSEKEALA HLHLARLAEN HEKVMTSLKH CLSASRNGLV
VNCKALNTFF CFILKSVSNL HPQLRHGTVE RVRCRVKHSL EVCFFMAGSR EAPCEDVADA
SDAETEGSDF DEEVWDDYWS KPAGPARTDR NIAGTSTAAK QAVQRLQARV NFDPLPRAGS
MSHAAQNSAV QSERKAAAFR NLGLTQDSRA TVEQVLDSRT MHVLSKFLKR GLFDEIHGCI
STGKEANVYY ATSGDGIERA VKVYKTSILV FKDRARYVEG EFRFRQGYCK GNPRKMVAQW
AEKEMRNLRR LAAVGIPCPE VVDVRQNVLV MEFLGHDGNA APRLKDAEGL DASAWDQLYI
DCAVLMRGMM QRCKLVHGDL SEYNMLHSDG KLYIIDVSQS VESDHPQALD FLKRDCVNVN
NFFAKRTSTG AVPVKRLFDF VVTRELPRLG SAGSSDDAEA FKDCDCALSG MCDWPRDAFA
VIPSLLILLN SVAVLLRKKQ RPFLNVDGRE LRARLCRDKV DKWSNCPTGK TPEAATFVVV
RTFDWQQVIG CMPGVTMTSE TPRLECTLLP WRVVCTAVSA SDQLAAFFYR TATQSRWYAR
DHLLDFPEIS ETFSVDEPAF LDGFAFHEKD LTSQRAELYA DVLALKLAHG SVALASDCAS
VVDRAMSLKP REYRYKDIVK FDNRDLWTAF LEDVHKRPNC NITFVNVGVH VQLFHEATQD
SLNGPEYLMR ANELAGRCAK RKAREAFVMN LQELKPWLKP FIQRAVDIQT HAVSMLLCLL
GIP
//
