ID A0A093QCY7_9PASS Unreviewed; 554 AA.
AC A0A093QCY7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=N305_03245 {ECO:0000313|EMBL:KFW81987.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW81987.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW81987.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW81987.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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 -!- 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; KL671380; KFW81987.1; -; Genomic_DNA.
DR RefSeq; XP_008923371.1; XM_008925123.2.
DR AlphaFoldDB; A0A093QCY7; -.
DR STRING; 328815.ENSMVIP00005027062; -.
DR GeneID; 103758833; -.
DR CTD; 55781; -.
DR OrthoDB; 21899at2759; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
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; 1.10.510.10; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR030484; Rio2.
DR InterPro; IPR015285; RIO2_wHTH_N.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
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; PF01163; RIO1; 1.
DR Pfam; PF09202; Rio2_N; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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:KFW81987.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053258};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 66..289
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 359..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 63186 MW; 935766F19EC74D63 CRC64;
MGKLNVVMLR YLSREHFRVL TAVEMGMKNH EIVPASLVAS IANLKHGGCN KILRELVKHK
LLAYEQTKTV QGYRLTNAGY DYLALKTLSS RQVITSVGNQ MGVGKESDIY IVANEEGQQF
ALKLHRLGRT SFRSLKNKRD YHKHRHKMSW LYLSRIAAMK EFAYMKALHD RNFPVPRPID
YNRHAVVMEL VDGYPLCQVH HMEDPAAVYS ELMDLIVKLA NHGLIHGDFN EFNLILDNDD
HATLIDFPQM MSTSHANAEW YFDRDVNCIK EFFKKRFTYE SELFPTFKDI RRECSLDKEI
AASGYAKEMQ EDDDLLYPPG SDKDDNTTEV LELVEDAENE LNFFSKDGEN NEDMYEVGDL
SESRTSDNAV CSSEEEVDTD ESRENAQRLS MAELSSALEK AGGQAMLWKC NGDAESSAIT
SFKGKSIKKN AAEVENQRSQ RGSCKDKENE DECPELVDSS TLNEEFRHYS EECVIPVAGH
RTRTKSISSV RSVGSCSTIP PELVKQKIKR QLTKQQKAAL KQRLQKGEAN VYTKQRRENM
HNIKSSLDAA NFWG
//
