ID A0A1I7VP68_LOALO Unreviewed; 1620 AA.
AC A0A1I7VP68;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Loa loa (Eye worm) (Filaria loa).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_4699};
RN [1] {ECO:0000313|Proteomes:UP000095285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Loa loa.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:EN70_4699}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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 STRING; 7209.A0A1I7VP68; -.
DR WBParaSite; EN70_4699; EN70_4699; EN70_4699.
DR eggNOG; KOG1035; Eukaryota.
DR Proteomes; UP000095285; 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:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; 3.
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; 1.
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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000095285};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 29..141
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 553..962
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 812
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 559..567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1620 AA; 183718 MW; A03C8688A4E1FF04 CRC64;
MKKRQCQQRN GAVGDIGGTL DDAKKRQGDE RIVLESVYGE DFLDAAQNAW RIWQPLDVIL
RLKPVGSSSG KIYVSLDLHV KCPKTYPLSG TPLLALENVK GISLKDVDKL KQILDNKAAS
LKGNEVILEL CQVVQEFLYE RNKPPEGSFF DGMLQQHAAV EHERRRQRVK SEQRDREDVV
AFQKMHEEKL MWRKAEEGEP TTPVDDSSCE TFSCIDGVQR RLTKSTNNFR RRPDISPFCQ
EWSAVDCTTG HELFIMEWSF AAVAKTPLSS LKPFITHFKQ LERKLQEISR ISVTEPTLCN
YEMLCVRKKK LTISEIDVWQ VLFHFLTFLF PGIFGMDSIE RCLSTWCVVI GQNIDGNDRN
LSSQFDIFET DKNSASEITQ IVHFRIAGSL LNLQTLLVRL AVQLLDGLRF LHEKNLGHFD
LDTTCVWITG KRNFRLSDYY LKTPLLDLCR IIKKCVEIVG ENISFDSMNK LPNHDLVSLG
NIFDKFRMLS TVANSPDFSG NLESFVKACI NTKNLKTLME HPFLHQDDLF HSLTDDGKDG
FQRMAHSRFR NEFIFIEMLG KGGFGYVMLA KNKLDGNDYA IKRIPLDPKD ERFNRKVTRE
AKLFSKLNHP NVVRYYSAWI EQASTTTRET GSESNGNGAS IDIDQKEEIE SSLMPLQIRN
IEKMAKRLAT DTTAEWSTSF QTTSIHEPDS VSEEQRREPV QTLFSPTGLS TVESSDFEVL
FEDEGDNEDS SDENSADTPS RLISQSETTV ESSYTLPLRI LFIQMEYCEK STLRNLIDGS
KLLKNPRQIW RLFREILLGL QYIHQEGMIH RDIKPMNVLI DGSDHAKIGD FGLATRDIVS
RNLSSLNESD LSFSMTKDIG TALYIAPELL STASGSIDYT TKIDVYSLGV VLFEMFYRPL
LPGMERIAVI KNLRGSGHFP SDFGNGILEI HQKAAKKLIK WMLEIQPDDR PSVQILLDSD
RIPVAEIEEN DFQKMFCQTI RSGGRLHHWI IDTLIANPVL PAADYLYDRG ICSADWLSLP
RLRAIEYLRN KLCRICSTHA FIPFDVHSIT PFNAKNATEM INSKSHACRF IDENGITVML
SYDLRRAFAR YCVRNGVNRL KRYGCGKVFG RPDALVSMHP VERIEFAIDA IGPASSAQML
TADILCITVE AAHQLDSISS RKWEIRLGHR DLVIATALYL GFGDFNTQNK ILNILYSIAT
SNKMLSHEQK IERLRVGTEM SFNQANSLLN VLEGDGCTLE ALVARTECLV NCRDDRVRRH
AKKALDDLTD LAVLLECFID NMTEHILFDG TFCYRPHTYC SGLMFQIRVL FLHRQRIQPV
IIGAGGRYDT LLEDERHAQD LVPPSPLCAV GCSLPLDILA QFCCRNKPDF GSVSGQALVC
SVSDQLLKTT ANLVKQMWSR GIQADILHHP VAPMQIAELD MHCNETNIEL LLMVYGEDEV
LARVNGVDLG KLTFDEMLSK LEAYRSGVSF VEAFPHLPNN NSPVKHSVNT LPVSATLANL
NIRYALIEKP AAHIRKRNET QIRACLQKMV AALAPQTVVE VIVTEISVDA IRLLATLIDR
SFTVDELSSA FTTAIRQLSK FKREFKRIEE VIEPLFQPKN TSPIVLYSKQ DCNGYYKLII
//
