ID A0A3P6SZP4_LITSI Unreviewed; 878 AA.
AC A0A3P6SZP4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|PIRNR:PIRNR038172};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|PIRNR:PIRNR038172};
GN ORFNames=NLS_LOCUS3247 {ECO:0000313|EMBL:VDK76319.1};
OS Litomosoides sigmodontis (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK76319.1, ECO:0000313|Proteomes:UP000277928};
RN [1] {ECO:0000313|EMBL:VDK76319.1, ECO:0000313|Proteomes:UP000277928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in the response to environmental stress.
CC Appears to act upstream of the JUN N-terminal pathway.
CC {ECO:0000256|PIRNR:PIRNR038172}.
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 ECO:0000256|PIRNR:PIRNR038172};
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 ECO:0000256|PIRNR:PIRNR038172};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000256|ARBA:ARBA00008874,
CC ECO:0000256|PIRNR:PIRNR038172}.
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DR EMBL; UYRX01000171; VDK76319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P6SZP4; -.
DR STRING; 42156.A0A3P6SZP4; -.
DR Proteomes; UP000277928; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06613; STKc_MAP4K3_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; IPR021160; MAPKKKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48012:SF18; HAPPYHOUR, ISOFORM A; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038172; MAPKKKK; 2.
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|PIRNR:PIRNR038172};
KW Kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038172};
KW Reference proteome {ECO:0000313|Proteomes:UP000277928};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Transferase {ECO:0000256|PIRNR:PIRNR038172}.
FT DOMAIN 15..265
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 476..790
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-1"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 878 AA; 98370 MW; A56426CBBCACFFF3 CRC64;
MSLDVIKRAD PTDDYELLQR VGSGTYGEVY KAKHIRTGEL SAVKVVKLEA GDNFAVIQQE
ILMIRGCVHP NIIAYHGSYL RRDRLWIVME YCSGVTGPLS ELQIAFVCRE TLKGLHYLHS
KGMVHRDIKG ANILLTHSGD VKLADFGIAA QITATIGKRK SFIGTPYWMA PEVACVERRG
GYGVECDVWA VGITAIELAE LQPPLFDLHP MQVLYLMTKS SYKSPTLKDK YKWSPFFHDF
IKQCLTKNPK KRPTPEKLLA SHHFVLGALS SRMTRDLLDK VNNPGGVPST SIFAGQFSAV
CTDDDEEGDM LTVSRIKSRG RACTRATHDA IRVYDDANAL MARIWGEPST SEDRTLPAKE
HPPLPDVVQA LSLLNDNDGV IHDTDDKTFC SSEQINGSSG SDFFVPQRPP RTKHPIKRCS
SFESSHSDPY LNEQVKHRIN GCANYFLQRP QTCFGLPPTP KVAMGACFSL IFHDCPLHIN
STATWIHPNT SRQFLLIGAE EGIFTLDMDE LHEAAMILIH KRRCSWLYVQ KNILMAVQGR
TPYLYRHDLV ALSQKNLTQR ISKPMSKIPE KYLPKKLAVT TRLPETKDVI HCNVARSGVN
GNVYLCCATP SAVILFQWYE PLAKFLMLKT VEMRIPHFPL QPFQLIYSAG TDSDFPKVCL
AVYKGVGRKF HLHYVNFNDE SVRCDLNGHD QMEAVCLNVV ALKQVDRDAL LLCYDNRCVV
INQNGIIKSS RLSPAQFKFG FQIENLVSLS DSILAFHPHG VQGRAFVDGS VTQDISDPNN
VYQVVGSDKL IVLKRRETSS AGDLCDLCIL TGHESTLAVY LVVLIQSKKF EKFDWFLADF
TKAMERFRVI SEVNAVVADP LFVVNVLLLG RIVTSALS
//
