ID A0A195CV26_9HYME Unreviewed; 899 AA.
AC A0A195CV26;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN ORFNames=ALC62_04529 {ECO:0000313|EMBL:KYN04538.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN04538.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYN04538.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYN04538.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN04538.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) 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=2.7.11.25;
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 -!- 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 EMBL; KQ977259; KYN04538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195CV26; -.
DR STRING; 456900.A0A195CV26; -.
DR Proteomes; UP000078542; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14058; STKc_TAK1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013057; AA_transpt_TM.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017421; MAP3K7-like.
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 PANTHER; PTHR46716; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7; 1.
DR PANTHER; PTHR46716:SF1; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7; 1.
DR Pfam; PF01490; Aa_trans; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KYN04538.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000078542};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 415..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 458..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 488..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 515..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 550..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 659..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 775..799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 805..823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 899 AA; 100604 MW; E96E77896C65029A CRC64;
MASRVMIGHQ QQFVEEIDYN EIETEQVVGK GSFGVVWKGK WRGQDVAVKH INSEGERKAF
TVEVRQLSRV AHPNIVKLYG ACTKNPVCLV MEYAEGGSLY NVLHCNPQPH YTIGHAMSWT
LQCAQGVAYL HNMKPKPLIH RDLKPPNLLL VMGGQRLKIC DFGTACDLNT YMTNNKGSAA
WMAPEVFEGS RYTEKCDVFS WGIILWEVLT RKKPFDDLGA SAYRLMWAVH VGRRPPLIEG
CPKPIEDLMT RCWQKAPEER PSMDEVVRIM AELSEFFSRH LEPVEYTLSS EDDIDGNETS
KEDTLDIIST LDFRMNGSVE NGTIRTIPKP VGKTNECSNE ENSLPFTLPQ TVPISDRSTK
FSPQQNNLGL QRNAWDLPSS SDTSWEIPNN MAGLDKVVHK TKKNNQRIPY ALHQAGFGLG
IALLILVASL TDYSLILMVR SGRICGEMSY QGLMRASFGR VGFYILTILQ LLYPFIGMYS
TEHKLTVTLH QCYYSLFNNV IVLSVVNQHA IMKRLYINVT AMVSYNVVVG DTVTKVLIRV
TGMNETNILA HRQVVILLAT LCITVPLCLY RNVARLAKIS FLSLVCVGFI LLAIFIRMDT
MSALVTIDYS PSQKDSWRFA NFPGIVPSIG IMAFAFMCHH NTFLIYSSIE RATQEKWDIV
THWSLFTSFL IAAAFGIAGY ATFTSYVQGD LMENYCWDDD LMNFARVMFS GTILLTFPIE
CFVTREVMPL MLFLLVCKNY YDRDLLSIQV LMTAIKGTDE LEGHEAYVPN SDREYLIITL
TIICMAYLIS MLTDCLGIVL ELNGILAAVP LAYILPGLCY LKLEEGSVFS SKKLPALGLM
TAGILAALSG LLLIITNTCS GTCFHGKVMP YCVDNSTTTL HLGATTMPTD NSVLSECGI
//
