ID A0A0B2UW39_TOXCA Unreviewed; 965 AA.
AC A0A0B2UW39;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative serine/threonine-protein kinase zyg-1 {ECO:0000313|EMBL:KHN73297.1};
GN Name=zyg-1 {ECO:0000313|EMBL:KHN73297.1};
GN ORFNames=Tcan_15866 {ECO:0000313|EMBL:KHN73297.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN73297.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN73297.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN73297.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:KHN73297.1}.
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DR EMBL; JPKZ01003129; KHN73297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2UW39; -.
DR STRING; 6265.A0A0B2UW39; -.
DR OMA; FECAHTD; -.
DR Proteomes; UP000031036; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:UniProt.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 3.30.1120.130; -; 2.
DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR047108; Plk4-like_POLO_box_2_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR040734; Zyg-1_PB2.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF94; SERINE_THREONINE-PROTEIN KINASE PLK4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18544; Polo_box_3; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KHN73297.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 255..501
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 965 AA; 107130 MW; FF2952CD091D5104 CRC64;
MTTWKAACLA SWKLCTIFVD EAPNQKAGKK SFSSSVSVWS SVGFTSMHSM LSVTLALLAT
ISTSNAFAFD RRARVYVFRA QQNINDAYYV MGVVDFQQER FAVKINGTIS GLTPGLHGLH
IHEKGDIGDG CMAAGPHYNP LEMQHGDAGR PYYTKRHVGD LGNINASELG IAKINAYYYG
VPLSGQCSVI GRALVVHQGR DDLGRGNAPT SKTTGDSGAR VGCGVIGIID RIVDAKIEDF
KVLVSPSPDF AIGSYENLEE IGRGGFGVVY RAKCIAKNKA WYGNIVAIKK IDISKVPGFR
VGLELQALAN LHHESIVDFY EEFRENGAQY IVMEYCKHGS LRDYVKKNGK LSDQCAAFIL
RQLVNAVKHI HSNGMMHRDL SAGNVLISSM RNGKFRVKLA DFGLATLLRQ GDVTGTIVGT
PGYIAPQVYG RSYNQKADVF SLGGILYLML VGKDPPREQN ITKELDLGIL SEEGAELIRQ
MMHPDENRRI ILQDIRMSAF SRMADEFDYY QLSYAQPVRM RAHSAQPRVT SNTKPNKESG
FESGDVEFAN FFFNVNGTLV YEVAGKHRSV SRECHGVDEC IACIVVVETK AAGGQVMSIY
STAKNTPFPH ADDPPLHLDR ACYKIYRSFE ELQLNSSHMR FYRQIVEATK RLGGRIEKIV
FKPSAATTAR LMENGDFRLK FSDGLFFFNV NGTLVYEVAG KHRSVSRECH GIDECIACIV
VVETKAAGGQ VMSIYSTAKN TPFPHADDPP LHLDRACYKI YRSFEELQLN SSHMRFYRQI
VEATKRLGGR IEKIVFKPSA ATTARLMENG DFRLKFSDGR LAVQKRGTDS ISVSDDGTSK
ATLSDEEMRL FHHSRSDALE MERLLEKGAF LCVKPFPFHF SNASEAEFPP EEVSSGHNVQ
RKSNASCGVE NQQPVLETYP EVDELFFNAN VCRYHCIPIF DGIGGEGGQH CSLLRHQSFS
ILQLL
//
