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Database: UniProt
Entry: J9ETZ2_WUCBA
LinkDB: J9ETZ2_WUCBA
Original site: J9ETZ2_WUCBA 
ID   J9ETZ2_WUCBA            Unreviewed;       656 AA.
AC   J9ETZ2;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=AGC/RSK/MSK protein kinase {ECO:0000313|EMBL:EJW80587.1};
GN   ORFNames=WUBG_08503 {ECO:0000313|EMBL:EJW80587.1};
OS   Wuchereria bancrofti.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX   NCBI_TaxID=6293 {ECO:0000313|EMBL:EJW80587.1, ECO:0000313|Proteomes:UP000004810};
RN   [1] {ECO:0000313|Proteomes:UP000004810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA {ECO:0000313|Proteomes:UP000004810};
RA   Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Hepburn T.,
RA   Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Wuchereria bancrofti.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. S6 kinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009804}.
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:EJW80587.1}.
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DR   EMBL; ADBV01004370; EJW80587.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9ETZ2; -.
DR   Proteomes; UP000004810; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR016239; Ribosomal_S6_kinase_II.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF175; CHROMOSOMAL SERINE_THREONINE-PROTEIN KINASE JIL-1; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000606-
KW   51}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EJW80587.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000606-51};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..237
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          238..306
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          335..597
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        98
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT   ACT_SITE        453
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT   BINDING         2
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT   BINDING         341..349
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT   BINDING         364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   656 AA;  74591 MW;  82F2FB19BA7CD4A3 CRC64;
     MKVLRKSRVM TKAKTLQHTL SERHVLERLK GLPFLVEMIY AFQSDSKLHI VMEFIKGGEL
     FTHLCNKGSF DMQSAKFYIA ELVVAIDSVH KQKVVYRDLK LENVLLDENG HIKLTDFGLS
     KELKDNELHR ANSYCGTIEY MAPEVVERTA EGYDETVDWW SLGVIAFELL TGCSPFTVDG
     HSNTSRDIAR RILTKPVPFP RNFNKFALDF ISRLLEKSAR YRLGRNGVDE IKNHLFLADI
     DWHQCERHEL EPPIVPKISN DIDVTNFAPE FTNQMPVYSP ADTPLDTRNL FRGYSFVSPS
     VMFANNNIIG EECLAEDFRA LVSVSPFFSK YKLDRSESGL LGKGSFSICR KCERLSDGVV
     FAVKIVSQRF QSQASREASI LNLVSGHPNI VRLIDVQSDS LHIYLVMELL EGGELLTRIK
     KMETFTEAQA GKIMKQLVSA VSYLHFRNVV HRDLKPENIL FESNEPQAKL RLVDFGFARL
     LPSATDNLLT PCFTLHYAAP EVLESDDQLP QYNEQCDLWS LGVILFTMLS GNVPFHARSK
     YESATDIMRR IRNAEFSFDA SQWRGISTEA KTLITLLLTV DPTKRLSLDE LQRHPWLLSA
     AAQNETPLQT PTTLLRSQSH TEETFNETMN AFLNANREGF HLMEVAAAPL LVKDVV
//
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