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Database: UniProt
Entry: A0A0N4TQM1_BRUPA
LinkDB: A0A0N4TQM1_BRUPA
Original site: A0A0N4TQM1_BRUPA 
ID   A0A0N4TQM1_BRUPA        Unreviewed;      1654 AA.
AC   A0A0N4TQM1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
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};
GN   ORFNames=BPAG_LOCUS10862 {ECO:0000313|EMBL:VDN92048.1};
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0001090001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BPAG_0001090001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN92048.1, ECO:0000313|Proteomes:UP000278627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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};
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DR   EMBL; UZAD01013202; VDN92048.1; -; Genomic_DNA.
DR   STRING; 6280.A0A0N4TQM1; -.
DR   WBParaSite; BPAG_0001090001-mRNA-1; BPAG_0001090001-mRNA-1; BPAG_0001090001.
DR   Proteomes; UP000038020; Unplaced.
DR   Proteomes; UP000278627; 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; 3.40.50.800; Anticodon-binding domain; 1.
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; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR016255; Gcn2.
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   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:UP000278627};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          32..147
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          559..967
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          730..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        817
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT   BINDING         565..573
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT   BINDING         588
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000660-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1654 AA;  187559 MW;  E4476B57F6282C73 CRC64;
     MKSMEHRQYE QRSAAVGDIG GTLDDAKRRQ RDERIVLESV YGEDFRDAAQ NAWKIWQPLD
     VILHLKPVRS VSTTSGKIYV SLDLHVKCPK TYPLYGIPLI ALENIQGISL RDIDKLKQML
     DNKAASLKGN EIVLELCQVV QEFLYERNKP PEGSFFDGML QQHAAVEHER RRQRVRSEQR
     DREDVVAFQK MHEEKLMWRK AEEGEPTTPV DDSSYETFSC IDGVQRRLTK MNDFRRRPNI
     SPFCREWSAV DYATGHELFI TEWTFAATAK TPISSLKPFI THFKQLEKKL KQISRISVTE
     PTLCSYEMLC VQKNKLTVSE INVWQALLHI TFSDSGNISC GSHRMICINT VVSFKLQVNC
     SVIIGQNIDG NDRNLSSQID IFETDKTLLV RLAVQLLDGL RFLHERNLGH FDLDLMSIWI
     TGKRNFRLSD YFLRSLILDR YRIIKECIEM VGENIASGSS IDKLPHNDLA SLGNIFSKFR
     GLPAVANDPD FSKNLESFVK ACRNTKILKI LMEHPFLHQG ICSEEEVVRL FSDDLFQSLI
     DVEKEGFQQI AHSRLRNEFI FIEMLGKGGF GDVMLAKNKL DGNDYAIKRI PLDPKDERFS
     RKVTREAKLF SKLNHPNVVR YYSAWIEQAS TVTREAGPES SSSEVNVNSG QKVGTEDSLV
     PMQIKNNEKV AKRLAVDTTA EWSTSFQVAS MYELDSVSEE QCKEPVRTLF SPTGLSTVEN
     SDFEVLFEDE GDNEDSSDEN VDTPSNRTLP SGTTARNSST LSLRILFIQM EYCEKSTLRN
     LIDSSKLLKN PRQIWRLFRE ILLGLQYIHQ EGMIHRDIKP MNVLIDGSDH AKIGDFGLAT
     RDIMSKNLSS LNESDMNFSM TKDIGTALYI APELLSTAGE SIDYTTKIDV YSLGIVLFEM
     FYRPLLPGME RIAVIKNLRG SGHFPSDFGT GMLEIHQKAA KKLIKWMLEI QPDDRPSVQI
     LLESDRIPVA EIEENDFQKM FCQAIRSRGR LHHWIIDTLI ANPVLPAADY LYDRGICSAD
     RLSLPRLRAV ESLRNRLCRI CSTHAFIPLD MHSITPFNAK NAPEMTNSKS RACRFVDENG
     ISVMLPYDLR RAFARYCVRN GVNRLKRYDC GKVFGRPDAA GKTSTFLNIM CSSVYEQIFA
     GSEMYYVSIV SMHPIERIEF AIDAVGPISS SQMLTADILC ITVETVHQLD CISSHKWEIR
     IGHRDLIIAA ILYLGFGDFS TQNKILNILY AIATSNKMLN REQKIERLRA GTEMSFSQAN
     SLLNVLEGDD CTLEALVART ECLVNCRDDR VQKHSKKALS DLTNLAILLK CFIDDMTEHI
     LFDGTLCYRP HTYCSGLMFQ LRVLVLHKQT IRPVIIGAGG RYDTLLDDER HAQDLIPPTP
     LCAVGCSLSL DILAHFCCTN KPDFGSVCGQ ALVCSVSDQF LKTTANLVKQ MWSCGIQTDV
     LHDPVAPMQI TELIEHCNET HIEMLLVVYG EDEVLTRIGG VDLGKLTFDE MLSKFEVYQN
     DVSFVEAFPH LSNITSTVRH SLNTLPVAAT PASLNVRYAL TEKPAAHVRK RNETQIRACL
     QKVVIALAPQ TVVEVVVTEI SVDAIRLLAT LIDRNFTVDE LLSAFTAAAK QLSKFKREFK
     RIEEVIEPFF QLKNTSPIVL YSKQDCNGYY KLIL
//
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