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Database: UniProt
Entry: A0A1I8Q9N1_STOCA
LinkDB: A0A1I8Q9N1_STOCA
Original site: A0A1I8Q9N1_STOCA 
ID   A0A1I8Q9N1_STOCA        Unreviewed;      1391 AA.
AC   A0A1I8Q9N1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, 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};
GN   Name=106092329 {ECO:0000313|EnsemblMetazoa:SCAU015128-PA};
OS   Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Stomoxys.
OX   NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU015128-PA, ECO:0000313|Proteomes:UP000095300};
RN   [1] {ECO:0000313|EnsemblMetazoa:SCAU015128-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU015128-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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}.
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DR   RefSeq; XP_013114614.1; XM_013259160.1.
DR   STRING; 35570.A0A1I8Q9N1; -.
DR   EnsemblMetazoa; SCAU015128-RA; SCAU015128-PA; SCAU015128.
DR   GeneID; 106092329; -.
DR   KEGG; scac:106092329; -.
DR   VEuPathDB; VectorBase:SCAU015128; -.
DR   OrthoDB; 5388799at2759; -.
DR   Proteomes; UP000095300; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06624; STKc_ASK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR046872; DRHyd-ASK.
DR   InterPro; IPR046873; HisK-N-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR043969; MAP3K_PH.
DR   InterPro; IPR025136; MAP3K_TRAF-bd.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR11584:SF369; APOPTOTIC SIGNAL-REGULATING KINASE 1, ISOFORM C; 1.
DR   PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF19039; ASK_PH; 1.
DR   Pfam; PF20309; DRHyd-ASK; 1.
DR   Pfam; PF20302; HisK-N-like; 1.
DR   Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          608..866
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1308..1391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..962
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1308..1362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         637
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1391 AA;  159276 MW;  14F68CD437C25687 CRC64;
     MANNAAASVS TKPQQQQQQQ QPGQWNTQML TVVCVIDTQL GDHLKDRECA LEEIQQAVTS
     VGANFQRVQF DKLDFGETKK LETFYNADVA VIDLSIQSHQ RSLSYHLGVR ESFNMKENIL
     IYNDVHSKQT LSLKLSFPNY TFLSYKLNTE YGVCNLTNFN KELPADTKIP TLQVRLKRLL
     QDVEIQSKAH MREKFLTDLR QAREIYATNT KKLQSILHEM RKRLDDGHVL SGEVVHSFMC
     SLRDVQDYDA MVCLVNDLKN IPNTRKYVET GNMSFLYAFA LNRRNKKGDR EKALESSLKA
     LEKKENEFPD MLCLCGRIYK DIFVESDYSD TVSLKNAIKW YRQSFEVQPN EYAGINLATL
     LVIDGKEFSN TEELQHIGMT LNNLIGKKGS LSSLTEYWDV ATFFEISVLA EDYAKAIKAA
     ECMFKLKPPG WYLKSTIGNI SLIHRFRKKG DDHQPNIEEQ IFQFWMDFFL DATDSTKISN
     IRFPILILEP QKIYMPSYVN INMDAEEKSI QIINICLAHA KQECKKVHDF VFTASQIKSV
     SLYKRDDRCA YLYVHHNSDD FQIYFPSPEC RQRFYELILE MASDQDVFVN LNEEEPQQIE
     YEYDYDDQNR KIVLGKGTYG TVYAARDKHT QVRIAIKEVP EKNSQDVQPL HEEIKLHSQL
     RHRNIVRYLG SLSEDGYFKI FMEQVPGGSL SDLLEKKWGP LKDNESTMAF YSKQILEGLK
     YLHEQKIVHR DIKGDNVLVN TYSGVVKISD FGTSKRLAGI NPMVSTFTGT LQYMAPEVID
     LGFRGYGPAA DIWSFGCTNV EMATGKRPFI ELGSAQAAMF KVGYYKKHPT IPDELSPNAK
     NFILRCFAIQ ETERPTAAQL LEDPFLTDKH RKLRLGPPSS SDFSRSISVP ADRLFSKPRA
     GNTPTTPEIE GFHSTSVDIE NLPSHQSFNM ERRNSSGTLL SPEIEVSTPS LRTGASSETS
     ETNDFYHLKK ESQRRTTLSN ILTTDESKIC DLWLEKLNAA QNNIVAISKN ELVKLIHGMR
     EYIMNEKEKH LEACINSLKE ELNYDVVALD HLHLALYSFQ DAVIPVLRSH SIKPHWMFAL
     DNLVKQAVQA CVMILYPELG ANLLGKEPSL IDDESVHNQQ QTSTDSQEKI VVYDAAQAPH
     STTPAMDEDS TSFSSSECVR LLRDIKESNR KFHYQHLEHQ KQSLKALQNI SKELAHFYMG
     RKRTRRPRST AVGNKKPNRQ YKRQFARRSV TSYNGGLQEV DEQLEEWLTR HDVDEVSKNI
     ILNEGFSYED FIYNMEKFDL MRLELRLGIE VRIWSLILQI RSQNYASNAT NSSGERTSPN
     ATSSYVNNTN AYSDSNALNS LNNNNTTASM SNLNNNPVAL NHKPIRSSLR RNSSKHCDSE
     YVSCSEDQTS T
//
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