ID A0A3B5AGR4_9TELE Unreviewed; 1329 AA.
AC A0A3B5AGR4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=MAP3K15 {ECO:0000313|Ensembl:ENSSPAP00000019596.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000019596.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000019596.1}
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; ENSSPAT00000019892.1; ENSSPAP00000019596.1; ENSSPAG00000014690.1.
DR GeneTree; ENSGT00940000159562; -.
DR Proteomes; UP000261400; 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:SF363; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 15; 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};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 630..886
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 946..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1192..1222
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 946..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1329 AA; 150679 MW; 334788DEC473F39E CRC64;
METGQSAQVA DMGGEHSAGV CVLERDRERA DVSSPSPPAK QRSLRVVYVL NDGLKSVMAS
SPESGALQCL QRACDSESAL LTTVTFGRLD FGETSVLDSF YDADIAVVDM SDVFRQPSLF
YHLGVRESFD MANNVILYHD TDPDTAQSLK VLLASSGNYY FIPYIVTPNH EYMCCESDAQ
RRASEYMQPS WDNLLGPLCV PLTDRFTSLL KDIHVTSCAS FKDTLLNDIR KAREKYQGEE
LAKELSRIKL RIDNTEVLTQ DIVMNLLFSY RDIQDYDAMV KLVQTLEMLP TCDLATQPMI
QFHYAFALNR RNSPGDREQA LGVMLQVLQS CEHPAPDMFC LCGRIYKDIF LDSDCKDTKN
RDNAIQWYRK GFELQPTLYS GINLAVLLIV AGQQFESSME LRKIGVRLNS LLGRKGSLEK
MNNYWDIGQF FTVSMLASDI PKATQAAEKL FKLKPPLWYL RSVVQNLQLI QRFKKQMVEH
SPQRERLDFW MDIIVEATQG TTNRLRFPVL ILEPTKIYQP SYVSINNEAE EKNVSIWHVS
PAETKGIHEW NFTAMSIKGI SISKFDERCC FLYVHDNSDD FQIYFSTEEQ CGRFCSMVKE
MISDGTGNSV ELEGEGDGDT LEYEYDTNET GDRVVLGRGT YGVVYAGRDL SNQVRIAIKE
IPERDSRYSQ PLHEEIALHK YLKHRNIVQY LGSVSENGYI KIFMEQVPGG SLSALLRSKW
GPLKEATIIF YTRQILEGLR YLHENQIVHR DIKGDNVLVN TYSGVLKISD FGTSKRLAGV
NPCTETFTGT LQYMAPEIID KGPRGYGAPA DIWSLGCTII EMATGKPPFH ELGEPQAAMF
KVGMFKIHPE IPESLSLEAK SFILRCFEPD PHKRAIASDL LRDTFVRHNT KGKKSKIAFK
PSDYIHSVSL PVQLQCEAAG SSSSEHGSVS PDCDSKHDVF FQKKKSSGSE NLLKPPNSNY
LSVPDEGSVS EDRSAPPSPE DRDSGLFLLK KDSERRAILY KVLNDDQEKV ISNLKENHIQ
GSEELQLSVD HIKQIICILR DFIHSPERRV MAATISKLKL DLDFDSTSIN QIQLVLFGFQ
DSVNKVLRNQ HIKPHWMFAM DNIIRRAVQA AITILIPELQ THFGPASECE GAEKEDEVDE
EEAEFGPVLA SHADDPGTNA DHGHPAVITL SSAHCQEHQR SHHQLGAQLG RLKQETSRYE
LLEELLQKEK EYQQVLKATL QQRTHDLELV RVRHRPPDIS PPSIFHIPAD HEPDKQLTDW
LKEQGADPDT VDKFVVEEYT LTDILNDVTK DDLRCLRLRG GVLCRIWRAI QRHRERERQT
SNKRSEDDA
//
