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Database: UniProt
Entry: A0A2A2LD54_9BILA
LinkDB: A0A2A2LD54_9BILA
Original site: A0A2A2LD54_9BILA 
ID   A0A2A2LD54_9BILA        Unreviewed;       731 AA.
AC   A0A2A2LD54;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PAV84074.1};
GN   ORFNames=WR25_21174 {ECO:0000313|EMBL:PAV84074.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV84074.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV84074.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV84074.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL   Curr. Biol. 0:0-0(2017).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. PKD subfamily. {ECO:0000256|ARBA:ARBA00008582}.
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:PAV84074.1}.
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DR   EMBL; LIAE01006889; PAV84074.1; -; Genomic_DNA.
DR   EMBL; LIAE01006889; PAV84075.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2LD54; -.
DR   Proteomes; UP000218231; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd20797; C1_CeDKF1-like_rpt1; 1.
DR   CDD; cd20798; C1_CeDKF1-like_rpt2; 1.
DR   CDD; cd01239; PH_PKD; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR   PANTHER; PTHR22968:SF15; SERINE_THREONINE-PROTEIN KINASE DKF-1; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          93..143
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          177..227
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          278..405
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          428..687
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         467
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   731 AA;  82669 MW;  9300FF69579D24E2 CRC64;
     MTFLHAAISP DYMQRIVLLK TCVFQVFESL RQRAMSIVEK KQPPGISNYE VHLFRHDYNS
     PSVLNHVSSI AQLDNGCVIE IIVVDRNDTP TRLHVVLPES YMKPTFCDYC GELLAGLIKQ
     GVKCQACGCN FHKKCWNAPR NNCAATQTPV LAPIRKDSNG IGHGIPFPIQ TPVSGLPHTL
     AEHSYKSFTV CKVCDHLLVG LVKQGLKCRD CGVNVHRKCA IELPSNCTLA DHAISRMSIS
     EMPDKEVEMA SASHSVPMNE NIPLFRLPGQ VTTRATSQPH VEGWMIHFVL SDPERRLKHY
     WVLANNAIHM YNEYNEGLGV NPNRVYKILP LAEIIAITQH SGPPVLSRHP PHCFEIRTTN
     NTVYCVGENL NYYSGEPVRK MPRSLSFRPP SNTQLWFQAL KESLQPPPSK SDPENAELAL
     EFANLYQVLS EKTLGSGQFG TVYSAIQRHT GKEVAVKVIS KERFAKKGTA AESMRAEVLI
     LHKMSHPGIV RLEFMCETKD KIFVVMEKMN GDMLEMILSQ ASGRLDSRVT RFLLVQILSA
     LKYLHDQGIA HCDLKPENVL LSDMSTNFPQ TKICDFGYAR FIPESQFRKT IVGTPAYLPP
     EVLQRRGYNK SLDMWSCGVI IYVTLSGTFP FNEGEEIADQ IQNAAFMFPT DPWSEVEPLA
     TDLIQRLLKV NIEERLTIEQ CLAHPWLKSE QLYRDLRSLE VRLNLPRYLT TEEDDERYAQ
     LLQQQGLIPV Q
//
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