ID A0A2Y9QWV6_TRIMA Unreviewed; 1287 AA.
AC A0A2Y9QWV6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=LOC101342328 {ECO:0000313|RefSeq:XP_023587845.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023587845.1};
RN [1] {ECO:0000313|RefSeq:XP_023587845.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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_023587845.1; XM_023732077.1.
DR Proteomes; UP000248480; 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 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:SF391; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 6; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|RefSeq:XP_023587845.1};
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:UP000248480};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|RefSeq:XP_023587845.1}.
FT DOMAIN 641..899
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 896..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1161..1188
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 924..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 670
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1287 AA; 142321 MW; 5EE78CBB176816D7 CRC64;
MAGPCSRSGA LQRAGSCWQD PLAEALCRSR PPAAPPGRGC ARSRPLSVVY VLTREPRLAA
ETGAEGEAEP LPLRCLRDAC SQLQGPRPSP QLRSLPFETL ALGDTAALDS FYNADVVVLE
VSSSLVQPSL FYHLGVRESF SMTNNVLLCS QADLPDLQAL RDCVGSYTLI PYVVTATGRV
LCGDAGVLKG LADGLVQAGV GTEALLTPLV GRLARLLEAT PTDSCGYFRE TIRQDIRQAR
ERFSGQQLRQ ELDRLQRRLD SVELLSPDIV MNLLLSYRDV QDYSAIIELV ETLQALPTCD
VAEQHNVCFH YTFALNRRNR PGDREKALAV LLPLVQSEGS VAPDLYCLCG RVYKDMFFSS
GFQNAGHREQ AYHWYRKAFD VEPSLHSGIN AAVLLIAAGQ RFEDSEELRL IGMKLGCLLA
HKGCVEKMQY YWDVGFYLGA QILANEPTQV VLAAEQLYKL NAPIWYLVSV METFLLYQHF
RPTPEPLGGP PRRAHFWLHF LLQSCKPFKP ASLQEDQCLV LVLELNKVLL PARLEVRGTD
PVSAVTLSLL ESETQDAPSS WTFPVPSICG VSTSKRDERC CFLYALPPAQ DVQLCFPSVG
HCQWFCSLIQ TSVTNPDSTA PAEEAEGVGE VLEFDYEYSE TGERLVLGKG TYGVVYAGRE
RHTKVRIAIK EIPERDSRFS QPLHKEIALH KRLRHKNIVR YLGSASQGGY LKIFMEEVPG
GSLSSLLRSV WGPLKDNEST ISFYTRQILQ GLSYLHDNRI VHRDIKGDNV LINTFSGLLK
ISDFGTSKRL AGITPCTETF TGTLQYMAPE IIDQGPRGYG KAADIWSLGC TVIEMATGRP
PFYELGSPQA AMFQVGMYKV HPPMPSSLSA EAQDFLLRTF EPDPLLRASA QALLGDPFLQ
PGKKSRSPSS PRYAPRPSDI PSACPTPSAD STTQSQTFPC PQAPSQHLPS PPKRCFSYGG
TSQLRVPEES GAEEPPSPEE SSGLSLLHQE SKRRAMLASV LEQELSVLAD SLRLEQEQGP
QLGRSQVEQL LRCLGAHIHT PNRRQLAQDL RALQRQLRAQ GLGPVLLQGP LFAFSDAVKQ
ILRRRQICPH WMFVLDSLLS RAVRAALAVL GPEMEKDVVS PLSEEPSKEK GSQTKQQETP
VHCNPLPKDP EQGPPPLMVQ LGLLRAETNR LRAVLAEKER ECQALMQRAL QQVDGEARTR
PLASERLAAF PADQGLVQWL EELSVDSGTI QTLLNHTFTL RALLTSVTRD DLIYTRIRGG
MVCRIWRAIL EQRAGAAPGT PGLRETE
//
