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Database: UniProt
Entry: A0A0C2HA47_9BILA
LinkDB: A0A0C2HA47_9BILA
Original site: A0A0C2HA47_9BILA 
ID   A0A0C2HA47_9BILA        Unreviewed;       400 AA.
AC   A0A0C2HA47;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=ANCDUO_01135 {ECO:0000313|EMBL:KIH68524.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH68524.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH68524.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH68524.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) 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};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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DR   EMBL; KN726354; KIH68524.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2HA47; -.
DR   Proteomes; UP000054047; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001180; CNH_dom.
DR   PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   SMART; SM00036; CNH; 1.
DR   PROSITE; PS50219; CNH; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          1..371
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
SQ   SEQUENCE   400 AA;  43965 MW;  7CB634650539B71E CRC64;
     MNSGYVTPPL KKLIYLYSLQ LEGNVSSCTN GSKISLHQQP LSSRDREKSF VGFFGTGALL
     GAGTVNRPGR AQDASQVQVN VNPSSQNGAH MESDAPEIRK YKKKFSGEIL CAALWGVNLL
     IGTDSGLMLL DRSGQGKANH PDLIQGSASG ALAEKRNGWV NVGDLQGAIH FKIVRYERIK
     FLVVGLENSI EIYAWAPKPY HKFMSFKSFG SLSHLPLIVD LTVEDNARLK VLYGSHEGFH
     AIDLDSAAIY DIYTPPNVCS CSFSVVSITV PLQNMVPHCI VVLPNSNGMQ LLLCYDNEGV
     YVNTYGKMSK NVVLQWGEMP SSVAYISTGQ IMGWGNKAIE IRSVDTGHLD GVFMHKKAQK
     LKFLCERNDK YFQVFFSSAK GGGSCQIYFM TLNKPGLSNW
//
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