ID A0A0N5AXQ9_9BILA Unreviewed; 1081 AA.
AC A0A0N5AXQ9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000973901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000973901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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=2.7.11.25;
CC Evidence={ECO:0000256|ARBA:ARBA00000478};
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=2.7.11.25; Evidence={ECO:0000256|ARBA:ARBA00000106};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0N5AXQ9; -.
DR STRING; 451379.A0A0N5AXQ9; -.
DR WBParaSite; SMUV_0000973901-mRNA-1; SMUV_0000973901-mRNA-1; SMUV_0000973901.
DR Proteomes; UP000046393; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23257:SF703; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-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; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 97..161
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 172..454
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 64..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1081 AA; 119547 MW; 444EDBC432B7668F CRC64;
MMVLLSLWEK SKVERPKVKR CLRALNLGVL DAVCGTVIPK RLPDRATVAT SNVTMALTSC
ADTSFGSNIP DRPDPTPGNE QKGFNGSGSV ALRSDFNSGF VFEPSFDYIP QRSDELRLQR
GSSTIRLLNR NDLADDGWLF GIAQDGSKGY FPQEYIKLKP LKHLEISMDE LVMTEINLGS
GGFGKVMRAV YKGNDVAVKI AHEGCNREVV LPTIREEAGI LCQLSHENII KMYGVITGEL
PGLVLELCSD TLGDLCSGSR KIRLPYRIIA YFGSQITCGM SYLHKLNIIH RDLKPKNILL
KEEPCLCTNG SNEDLSFLTL GFDKLCGHCG CKALDRITLK IADLGLCKRI QCENSTSRMS
VLGTITYLSP EAISEQKCSK GMDVWSFGMT LWEMLTGRPP YQEYSRPCIT WKIGLYNKLD
IPEYCPDDLN NVITKCWNNS HEKRPSFMEL HKTFLQLYKD YRGYKSDGNE NQMKKLVLLN
NKRPFVESVE HKENEDKNLM AKLKPIYDTK QIAKPCLPKG RKKPKPSDIS KPKDFVQIMS
LTPNNAVISD MFVVFVIVVV LYDVLAGRKE PVKLSTPITT VDLEPSISSK HHVVRTNIIS
KNTNDESVFG YVTLPRTPKA TGRTHNFEFS PSALTQNSAS KSGLDGVQHL PSKSTPDLSS
FGMKSSDLTH KLHRVNARRI KKDSLRGSID SKDSADGSSP GVFTESMAGL DHGDKENLSS
AIQVPRPRNR YMQSRSPTVS SSSIPHLIER FWHKGGKSHN SGRESRKTGF LGNIVPRKSA
VESKLSKNHN RRKFKATTPE DKDIICTENS VSFVKVSSPN GNGLFSSSSR AGQGLLLDAV
EDDRSNKISF SEANVVKNTC YVSPRHIQPK PSLPSVSPST SVGQSVSSNR SVSCDSALPS
SSNLLTNIHY NRPLFRGHRT GNSSDSPVFL DTDVAGGVEF DTIVKTNGDK NGFIDSRQDG
SYGRLASEFS GFSGANQSEC SLYVSMKKIN QEVQKMSNDN KHYIPLGAYR EQTVASLPKR
CEIAASSCSN SNYKTLTANS DVCFPQKRPT KLDFLQSDDG DISINDSLPD VISLKEAVVP
P
//
