ID A0A084WID8_ANOSI Unreviewed; 1609 AA.
AC A0A084WID8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=ZHAS_00018021 {ECO:0000313|EMBL:KFB49982.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB49982.1};
RN [1] {ECO:0000313|EMBL:KFB49982.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC018021-PA}
RP IDENTIFICATION.
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};
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DR EMBL; ATLV01023929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE525347; KFB49982.1; -; Genomic_DNA.
DR STRING; 74873.A0A084WID8; -.
DR EnsemblMetazoa; ASIC018021-RA; ASIC018021-PA; ASIC018021.
DR VEuPathDB; VectorBase:ASIC018021; -.
DR VEuPathDB; VectorBase:ASIS019167; -.
DR OMA; EFYHRSG; -.
DR Proteomes; UP000030765; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR CDD; cd14046; STKc_EIF2AK4_GCN2_rpt2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR016255; Gcn2.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR11042:SF197; EIF-2-ALPHA KINASE GCN2; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 6.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50908; RWD; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW 2}; Initiation factor {ECO:0000313|EMBL:KFB49982.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFB49982.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Protein biosynthesis {ECO:0000313|EMBL:KFB49982.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFB49982.1}.
FT DOMAIN 13..123
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 223..522
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 516..907
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 168..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 743
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 522..530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1609 AA; 179092 MW; 09B72344FA10072F CRC64;
MAQRETFRER QENELEVIKS IFHDEVEDLR PKEGKWKPLE LQLHLTPQKG SAKEAYVKAD
LHIICNPKYP KYPPKVELKN AVGLSDSLVR ELADQLQRQA DELKGEVMIY ELANTVQTFL
HQHNVPPKGS FYDEMLANQQ KQALARQNTL QAEENLKRQA IQDELQRRKK ELARTRRESR
QSLNDSSPLH RLHSSSSTEN SDGVYCLEHR RSELLYFRDG RKVLRGACLG HSQRGCITYS
GIDQQSGELI YLTEWTLHYD GESLESKLIR ARPVDTVVTD IERLVESLTP LRHKHLIAYE
GVLCRIGKEA LTVFVAQEFI LGTSLFSISG SLGWSVEGAS MVAKGALEAL IYLHNNGVSH
DNLSDSTMFM DNAGMVRVAD FRLIPYIQEL GDGQQLHQTI RSPDLPALGS LIEALLAPHS
EMKDFIEKCK SERTISATDL LDHPFLRTIL LHTEHHQGAV GQITTVGAQK THHLERSQQT
GAQQQQQQQQ PPSPYMPLIM NNSLTAAGKS RIQMEFEILS YLGKGAYGDV LKVRNMLDNR
EYAIKRIRLP ARSKQFYKKM TREVELLSRL NHENVVRYYN SWVEAISAAE MVHVDTVGGA
DVATLSSCDW SVGGGTTPIQ GKRGRRGQKP RPPARRNNAS YAEEESSGGI EFVGSNGEVA
SYSNFNDGTS VAENGGANGK PTPTSAPPEV LYMYIQMEFC EKSTLRTAID ADLYQDVDRV
WRLFREIVEG LSHIHQQGMI HRDLKPVNIF LDSRDQVKIG DFGLATTSIL ALQNQSQPNG
QLVQLAIGNQ KAAGKSSDMG CSLTGKVGTA LYVAPELTGN ASRSTYNQKV DLYSLGIILF
EMSSPPLNTG MERVKTLMDL RADPVRLPDS LLADGRYSRL VQVIRWLLNH DPHKRPTAEE
LLSSELVPRT RLEAEEIQDV VRHILSNPQS RHYKHLIARC FAQESDPICE LSYHFDMVPM
VPILPRFDYV KEKVIALFRK HGAIEVVTPL LTPYTKQHAA RSNTVKLMTH SGSVVTLPDD
LRLPFLRHVA LNGIRNIRRY SVGRVYREKK VFNFHPKQVY ECAFDIVTPS RGYLITDAEL
LAIAMDVMRE LNLLQNRNVF FRLNHIGLLR ALLIHCNVPV DKYRELFEIV AEFLDDKISK
FQLCSLINAQ LGGGGGGASN GGGGGGGSTK VNVGYLCDAV QLELASVGQL NGSILKTIIR
GKGEAASMAK VAVRELETVV TLAQNMGVQC PLNVCPGLPV NYERAKTGGI VWQLLGELKP
KRKNPLTTIA VGGRYDGKLV EFQKSGINNG LQVPKVELSG AGFSFLLDKL VNAIAPTAGY
EPVQVMICVT GSRPQLKEVA HILRPLWSNG IKTAVVETSA TAVDDLGKEA GANVVVLLGD
GGELRVRSWD NDRFQERHVT RPDLIAYVMR TFRRPDTAPN EVASQALQNV TLGSASSVSS
FSTSFTTSAS SSSVKLSSTI GGAANASQSG SGSPPIDLVF LTNEKINTNK KRRFEHQVEH
KLSPVLSKFH RKEKVTLIMV DLPSSPLRGL VGLIDPLECG FHEEDDDDST AASNNERLEL
QNLCERYPKY KRQLMEIYSE IVDLFSQDKR TTPIVGVYSV VDTFCRLIL
//
