ID A0A158PSK7_BRUPA Unreviewed; 1210 AA.
AC A0A158PSK7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BPAG_LOCUS13354 {ECO:0000313|EMBL:VDN94539.1};
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0001342601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BPAG_0001342601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN94539.1, ECO:0000313|Proteomes:UP000278627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UZAD01013382; VDN94539.1; -; Genomic_DNA.
DR STRING; 6280.A0A158PSK7; -.
DR WBParaSite; BPAG_0001342601-mRNA-1; BPAG_0001342601-mRNA-1; BPAG_0001342601.
DR Proteomes; UP000038020; Unplaced.
DR Proteomes; UP000278627; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd06608; STKc_myosinIII_N_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000278627};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 18..285
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 893..1184
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 300..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1210 AA; 135200 MW; 79D31F0918AB866D CRC64;
MRSFVMCDQV LQDPAGIFEL IEVVGNGTYG QVYKGRHVKT SQLAAIKIMN INEDEEEEIK
MEINMLKKYS HHRNIATYYG AFIKKLPSST GKLDQLWLVM EFCGSGSVTD LVKSTKGNSL
KEDWIAYICR EILRGLYHLH QNKVIHRDIK GQNVLLTDSG EVKLVDFGVS AQLDRTVGRR
NTFIGTPYWM APEVIACDEN PDATYDSRSD LWSLGITALE MAEGHPPLVD MHPMRALFLI
PRNAPPRLKR GKKWSKKFDS FIETVLVKDY HQRPYTDQLL RHPFIREQPP ERQTRIAIKD
HQDRHRRITT KKDETEYEYS GSDDDESHGQ ASKPLDVAAG EFSLLVKHYI TFGLLFLYQL
AGVVQSTQDN TLRKGFQRLQ ENNKNMFEHS PSQPIRQRSA LAIVLPSGQH HHISQHQQKH
PSTSQALQRN PRFGADDSRE HVKLRQQQVD PRMALNGLGH QRHGDHNRRS QRPLSHHQAR
GISPHHASAV MPQPNHPAAP HLADLANYDR KRRSEKEKEA VRMAGEQRRD RSAASRDQVR
DMSRELKTPP RTARVNTSVA ATTPVRKMSE PVLNGKVENQ DLDVLANELT RMGRHQQNGS
YSPPPPAPPP RDTSIMSAVD EASGSHDSTL LVNESTLEEG TLRGPNKPLP PTPTDQSPLS
DIPGDDGTLL ASHKVNGSVD HRRSNSDSLS RNRHSQMVKA ASMPDQTPTA AEIIIGSGSS
GSDGSGSPDE SPFDARKSNN RISGATASGQ RCGVMPDLLP RTPIERSTAF LAFTKDGSSP
SIDSQSAEEI RDMVVGSSET RQWFPSGVNS LPRIQAPLAA RDREKSFVAY FGAGMSGSGT
VNRPGRAQDT NQVYLLYMIE VQVNVNPNPA AASNGLHSDG DAPEIRKYKK KFSGDILCAA
LWGVNLLIGT DSGLMLLDRS GQGKVYQLIT RRRFEQMTVL EGQNILVTIS GRKRRIRVYY
LSWLKQKILR TEGVSGVELE KRNGWVNVGD LQGAVHFKIV RYERIKFLVV GLESTVEIYA
WAPKPYHKFM AFKAFSQLTH LPLIVDLTVE KNSRLKVLYG SREGFHAIDL DSGSIDDIYT
PANTETVVTP HCIVIMPNSN GMQLLLCYNN EGVYVSTYGK ATKSVFLQWG ETPSSVAYIS
TGQIMGWGNK AIEIRSVDTG HLDGVFMHKK AQKLKFLCER NDKVFFSSAK GGGACQIYFM
TLNKPGLSNW
//
