ID A0A3B3T5Q6_9TELE Unreviewed; 1284 AA.
AC A0A3B3T5Q6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Mitogen-activated protein kinase kinase kinase 15 {ECO:0000313|Ensembl:ENSPKIP00000037995.1};
GN Name=MAP3K15 {ECO:0000313|Ensembl:ENSPKIP00000037995.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000037995.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000037995.1}
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};
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DR STRING; 1676925.ENSPKIP00000037995; -.
DR Ensembl; ENSPKIT00000018985.1; ENSPKIP00000037995.1; ENSPKIG00000015874.1.
DR GeneTree; ENSGT00940000159562; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IEA:InterPro.
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; 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 PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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}.
FT DOMAIN 613..869
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 934..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 642
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1284 AA; 145192 MW; D55E90B9C589E4A0 CRC64;
MAASTERADV TSPSQLPKQR SLRAVYVLND GLKAVAANSP ESGALQCLQR ACDAESAILT
TVTFGRLDFG ETTVLDTFYD ADIAVVDMSD VFRQPSLFYH LGVRESFDMA NNVILYHDTD
PDTAQSLKDM VTQKNTASSG NYYFIPYVMT TNHEYMCCEN DAQRRASEYM QPSWDSLLGP
LCLPLVDRFT SLLKDIHVTS CASFKDTLLN DIRKARDKYQ GEELAKELAR IKLRIDNTEV
LTQDIVMNLL FSYRDIQDYD AMVKLVQTLE MLPTCDLANQ PMIQFHYAFA LNRRNSPGDR
EQALRVMLQV LQSCDHPAPD MFCLCGRIYK DIFLDSDCKD TKNRDNAIQW YRKGFELQPT
LYSGINLAVL LIVAGQQFEN SIELRKIGVR LNSLLGRKGS LEKMNNYWDV GQFFTVSMLA
NDISKAVQAA EKLFKLKPPI WYLRSVVQNL QLIQRFKKQN LEHSPQRERL NFWMDIIVEA
TQGATNGLRF PVLILEPTKV YQPSYVSINS EAEEKNVSIW HVSPAETKGI HEWNFTGTSI
KGISISKFDE RCCFLYVHDN SDDFQIYFST EDQCGRFCSM VKELISDGSG NAVELEGEGE
GDTLEYEYDY NENGDRVVLG RGTYGVVYAG RDLSNQVRIA IKEIPERDSR YSQPLHEEIA
LHKYLKHRNI VQYLGSVSED GYIKIFMEQV PGGSLSALLR SKWGPLKEAT IVFYTRQILE
GLRYLHENQI VHRDIKGDNV LVNTYSGVLK ISDFGTSKRL AGVNPCTETF TGTLQYMAPE
IIDKGPRGYG APADIWSLGC TIIEMATGKP PFHELGEPQA AMFKVGMFKI HPEIPEALSA
EAKSFILRCF EPDPNKRATA GDLLKDVFVR QNVKGKKSKI AFKPSDYLRS VSFPAQLQTE
ATGSSSSEHG SISPECDSKQ DVFFEKKKRS ASENLIKPPS SNYLSVPDEV SVTEDRSAPP
SPEDRDSGLF LLKKDSERRA ILYKVLNEDQ EKVISNLMEN HIQGSEELKL SVDHIKQIIC
ILRDFIRSPE RRVMATTISK LKLDLDFDST SINQIQLVLF GFQDSVNKVL RNHHIKPHWM
FAMDNIIRRA VQAAVTILIP ELQTHFGPAS ESEGADKDAD EVDVEEDADF GTAEPAAPED
PGLTSGVSTL SSVLSHESQR QNQQHPLGTQ LGRMKQETNR LLEDLVQKEK EYQQVLRQSL
QQRAHDLELM RVKSRPIAHE PLLPTTDIHP PSIFHIPADV EPDKELTDWL KELGVDADTV
EKASMLERPA GMRPCRRSLH VRYS
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