ID A0A016UAD2_9BILA Unreviewed; 466 AA.
AC A0A016UAD2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN Name=Acey_s0048.g1612 {ECO:0000313|EMBL:EYC12100.1};
GN ORFNames=Y032_0048g1612 {ECO:0000313|EMBL:EYC12100.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC12100.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC12100.1}.
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DR EMBL; JARK01001384; EYC12100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016UAD2; -.
DR STRING; 53326.A0A016UAD2; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF29; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 1A; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT DOMAIN 199..457
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 466 AA; 52096 MW; 4EA9DEC2505DEE8E CRC64;
MDVPSTSKMA PTVEVSKTQN EDMQKMVQGL KDLMSSRRPP VNRNVLKIKM EYCGEKRCIE
MDRPVSMKAL QDHLQRRYGK TINMYYQQGK GEVVVSIKNQ DELDRAIKVV DRNGQRCLRL
LLSKHQPVDT EVADTRPDQS GTYTGNIVEV PYSTNCSSCG ASRVSFARST GESSCSSGVQ
WDIDDRKLSS QSPRAPTHWK EAKCIGSGAF GSVYLAYDVD TGRDLAVKKI PIIPDNRELR
REAQGLEFDV QELGRLQHPR IVQYLGVQKT SDRILIFMEY MTGGSLKDHI ALVGSLSDPV
ARNHTAQVLE GLAFLHKNHI IHRDIKSANI LRDSLGNVKI ADFGSGKKMQ SLASQQGAFH
STIHYTAPEV LLGKTAYGRK ADVWSVGVTL VEMLTGKVPW KEFEPMAAMF QIAYEEPKID
LPSTVEPVTA DLCRVLMNKN FDERPMAAEV LLNHPAFKPV AKNHIH
//
