ID A0A6I9WGB4_9HYME Unreviewed; 1302 AA.
AC A0A6I9WGB4;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
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=LOC105427967 {ECO:0000313|RefSeq:XP_011638279.1};
OS Pogonomyrmex barbatus (red harvester ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Pogonomyrmex.
OX NCBI_TaxID=144034 {ECO:0000313|Proteomes:UP000504615, ECO:0000313|RefSeq:XP_011638279.1};
RN [1] {ECO:0000313|RefSeq:XP_011638279.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:ARBA00048329};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25;
CC Evidence={ECO:0000256|ARBA:ARBA00047559};
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_011638279.1; XM_011639977.2.
DR EnsemblMetazoa; XM_011639977.2; XP_011638279.1; LOC105427967.
DR GeneID; 105427967; -.
DR KEGG; pbar:105427967; -.
DR CTD; 42366; -.
DR OrthoDB; 275301at2759; -.
DR Proteomes; UP000504615; Unplaced.
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 CDD; cd06624; STKc_ASK; 1.
DR FunFam; 1.10.510.10:FF:000054; Mitogen-activated protein kinase kinase kinase 5; 1.
DR FunFam; 3.30.200.20:FF:000487; Serine/threonine protein kinase, putative; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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:SF394; 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:ARBA00022777, ECO:0000313|RefSeq:XP_011638279.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000504615};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 565..823
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 874..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1126
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1302 AA; 146921 MW; 7C55D5007BC1888B CRC64;
MSRYSLSSIL RGILEKREIL KKTAVCLTGS EVPNNMPSVC GDMVDTGAAA SQSGVMEGIP
STDSVGTHSD ISGHTTVPGR PRMDVACVLD LQQSEHLAQR KKALDEVRQA CNLVNANIHH
IQFEKLDFGE TNVLDTFYNA DVAVVDLSIQ LQQSALFYHL GVRESFGMKE NILLYNDIDT
EATIRLKLSC GSYTFVSYRV VESCGSCVAT NPATSRITGE ETIDPKQHLT LKLKKLFQDV
EIQSKAHMKE KFLADLRKAR ETYSGEELSR ALNNMRKRLD DPNVLSGEVV LNVLISFREI
QVQPNEYAGI NLATLLVIAG NEFSKSEELQ HIGMVLNNLI GKKGSLPSLK DYWDVATFFE
ISVLAEDYSK AIQAAECMFK LKPPNWYLKS TIGNISLIDR FRKKNEEAEI APEEQIFSFW
MDYFVEATKP EVGDSIRFPI LVLEPTKILM PSYVNVNLGA EEKSIQIWNL CLDNMRNNCK
QVHDWLFTAN MIRSVSLYKR DERCLFLYVH QNSDDFQMYL PSVQCRQRFY DLILEMTRDQ
EGMVTDLDAY MTDDRMKFEY ELDDQNKRII LGKGTYGVVY AARDLNTQVR IAVKEIRERN
LGDVQPLHEE IKLHSQLRHR NIVQYLGSVS EDGYFKIFME QVPGGSLSAL LRSKWGPLKE
NESTISYYTK QMLEGLKYLH DQKIVHRDIK GDNVLVNTYS GVVKISDFGM SKRLAGLCPS
TETFTGTLQY MAPEVIDKGQ RGYGAPADIW SLGCTIVEMA TGKPPFIELG SPQAAVFKVG
YYKIHPEIPS ELSERAKSFI LRCFEPNPDI RATAAELLED PFLNEKKKSS RLVAPPDFSR
SISVPADRLE RLGKCDKTNN NHIVAAIPIQ MSQSDDSGGL TKSSPLRGRS PAHLLSPISM
PTTILSFNST IGNTPSIETS ETDTAGASIT RRSSSGGLLS PEVELGGQPG QKSGEEQEGF
YLLKKDSQRR MTLTRVLNQD EAKICEVWMR GINQAEGQTV LQMSHLVLLM RGLRDYIAEQ
NQEVIVTAIR TLKEELDFDS TAINHLHLAI YLFQTAVNEV LRMHSIKPHW MFALDNLVRN
AVQAAITVLS PELGANLLGQ ERVQPGGQGP EEGSTSGVST VNSVKSQKTA DSIDNKYWKE
YRDQMGALKM ENMKLLQELI ESQKSYQTLL QQALEEQRAQ VNTLTYLCEN INRKSVRQES
GYNSCIFGNI SQQLSSSTPT DTHRSINVHQ HTDLVEWLQN LQVDETSIDR FLYEEYTLED
ILCHVTREDL RRLNLRGGIE LRIWQAILKH RESNGNEVLE RD
//
