ID A0A1B0GIA6_LUTLO Unreviewed; 450 AA.
AC A0A1B0GIA6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Lutzomyia longipalpis (Sand fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae;
OC Lutzomyia; Lutzomyia.
OX NCBI_TaxID=7200 {ECO:0000313|EnsemblMetazoa:LLOJ004323-PA, ECO:0000313|Proteomes:UP000092461};
RN [1] {ECO:0000313|Proteomes:UP000092461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jacobina {ECO:0000313|Proteomes:UP000092461};
RA Richards S., Qu C., Dillon R., Worley K., Scherer S., Batterton M.,
RA Taylor A., Hawes A., Hernandez B., Kovar C., Mandapat C., Pham C., Qu C.,
RA Jing C., Bess C., Bandaranaike D., Ngo D., Ongeri F., Arias F., Lara F.,
RA Weissenberger G., Kamau G., Han H., Shen H., Dinh H., Khalil I., Jones J.,
RA Shafer J., Jayaseelan J., Quiroz J., Blankenburg K., Nguyen L., Jackson L.,
RA Francisco L., Tang L.-Y., Pu L.-L., Perales L., Lorensuhewa L.,
RA Munidasa M., Coyle M., Taylor M., Puazo M., Firestine M., Scheel M.,
RA Javaid M., Wang M., Li M., Tabassum N., Saada N., Osuji N., Aqrawi P.,
RA Fu Q., Thornton R., Raj R., Goodspeed R., Mata R., Najjar R., Gubbala S.,
RA Lee S., Denson S., Patil S., Macmil S., Qi S., Matskevitch T.,
RA Palculict T., Mathew T., Vee V., Velamala V., Korchina V., Cai W., Liu W.,
RA Dai W., Zou X., Zhu Y., Zhang Y., Wu Y.-Q., Xin Y., Nazarath L., Kovar C.,
RA Han Y., Muzny D., Gibbs R.;
RT "Whole Genome Assembly of Lutzomyia longipalpis.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:LLOJ004323-PA}
RP IDENTIFICATION.
RC STRAIN=Jacobina {ECO:0000313|EnsemblMetazoa:LLOJ004323-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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; AJWK01013619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1B0GIA6; -.
DR EnsemblMetazoa; LLOJ004323-RA; LLOJ004323-PA; LLOJ004323.
DR VEuPathDB; VectorBase:LLOJ004323; -.
DR OrthoDB; 21899at2759; -.
DR Proteomes; UP000092461; 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 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
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 7..231
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 339..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 271..298
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 351..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 51952 MW; 18941344AAC0B849 CRC64;
MGKLNVHKLK YMTKEDFRIL TAIEMGMKNH ELVPGPLAAS IANVKAGGES NIYTVADPEG
QPLCLKLHRL GRVCFRNVKE KRDYHGRRNK ASWLYLSRIS ATREFAYMKA LHDRGFPVPK
PIDFNRHCIV MELVNGYPMI NVREVENVEA LYDDLMELIV SLGNCGVIHG DFNEFNIMVT
DEGKPILIDF PQMVSTSHPN AKYFFERDVK GVQELFKLGM DSPSKWRRIS CKNTEWRVKR
KRKMKQDDEE ECAGVSDDDD NERSNDIKYT KEELDNLKQH LEEEVQFSEQ KVKDQSAQSH
IEKYIASVSS HLASFSLQHA SDEEDIFEDA PGEIPEIIES TSTTSELPKI PETTADKEDK
DLEGLDPNSR MYRLKMVEKL ISDRRSMRSF STTASTIAPS VITERQKREM QKHKVREERK
RCTAKGDANA VMRRRQENKF TVKQYAGWDF
//
