ID A0A2K5F5N7_AOTNA Unreviewed; 1366 AA.
AC A0A2K5F5N7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, 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=MAP3K5 {ECO:0000313|Ensembl:ENSANAP00000040782.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000040782.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000040782.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSANAT00000058894.1; ENSANAP00000040782.1; ENSANAG00000037690.1.
DR GeneTree; ENSGT00940000159155; -.
DR Proteomes; UP000233020; 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:SF332; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 5; 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: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}; Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 672..930
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1174..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1237..1271
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1366 AA; 153562 MW; A3D0C92C8E46AB1F CRC64;
MSTEAGEGIT FSVPPFAPSG FCTIPEGGIC RRGGAAAVGE GEEHQLPPPP PGSFWNVESA
AAPGIGCPAA TSASSATRCR GSSGGGGSRR TTVAYVINEA SQGQLVVAES EALQSLREAC
EAVGATLETL HFGKLDFGET TVLDRFYNAD IAVVEMSDAF RQPSLFYHLG VRESFSMANN
IILYCDTNSD SLQSLKMCTG NYTFVPYMIT PHNKVYCCDS SFMKGLTELM QPNFELLLGP
ICLPLVDRFI QLLKVAQASS SQYFRESILN DIRKARNLYT GKELAAELAR IRQRVDNIEV
LTADIVINLL LSYRDIQDYD SIVKLVETLE KLPTFDLASH HHVKFHYAFA LNRRNLPGDR
VKALDIMIPM VQSEGQVASD MYCLVGRIYK DMFLDSNFTD TESRDHGASW FKKAFESEPT
LQSGINYAVL LLAAGHQFES SFELRKVGVK LSSLLGKKGN LEKLQSYWEV GFFLGASVLA
NDHMRVIQAS EKLFKLKTPA WYLKSIVETI LIYKHFVKLT TEQPVAKQEL VDFWMDFLVE
ATKTDVTVVR FPVLILEPTK IYQPSYLSIN NEVEEKTISI WHVLPDDKKG IHEWNFSASS
VRGVSISKFE ERCCFLYVLH NSDDFQIYFC TELHCKKFFE MVNTITEEKG RSTEEGDCES
DSLEYDYEYD ENGDRVVLGK GTYGIVYAGR DLSNQVRIAI KEIPERDSRY SQPLHEEIAL
HKHLKHKNIV QYLGSFSENG FIKIFMEQVP GGSLSALLRS KWGPLKDNEQ TIGFYTKQIL
EGLKYLHDNQ IVHRDIKGDN VLINTYSGVL KISDFGTSKR LAGINPCTET FTGTLQYMAP
EIIDKGPRGY GKAADIWSLG CTIIEMATGK PPFYELGEPQ AAMFKVGMFK VHPEIPESMS
AEAKAFILKC FEPDPDRRAC ANDLLVDEFL KVSSKKKKTQ PKLSALSAGS NEYLRSISLP
VPVLVEDTSS SSEYGSVSPD TELKVDPFSF KTRAKSCGER DVKGIRTLFL GIPDENFEDH
SAPPSPEEKD SGFFMLRKDS ERRATLHRIL TEDQDKIVRN LMESLAQGAE EPKLKWEHIT
TLIASLREFV RSTDRKIIAT TLSKLKLELD FDSHGISQVQ VVLFGFQDAV NKVLRNHNIK
PHWMFALDSI IRKAVQTAIT ILVPELRPHF SLASESDTAD QEDLDVEEDH EEQPSNQSVR
RPQAVIEDAV ATSGVSTLSS TVSHDSQSAH RSLNVQLGRM KIETNRLLEE LVRKEKELQA
LLHRAIEEKD QEIKHLKLKS QPIEIPELPV FHLNSPGTNT EDSELTNWLR ENGADEDTIS
RFLAEDYTLV DVLYYVTRDD LKCLRLRGGM LCTLWKAIID FRNKQT
//
