ID A0A3Q4M9Q6_NEOBR Unreviewed; 1285 AA.
AC A0A3Q4M9Q6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Mitogen-activated protein kinase kinase kinase 15-like {ECO:0000313|Ensembl:ENSNBRP00000005084.1};
GN Name=MAP3K15 {ECO:0000313|Ensembl:ENSNBRP00000005084.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000005084.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000005084.1}
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 RefSeq; XP_006799329.1; XM_006799266.1.
DR STRING; 32507.ENSNBRP00000005084; -.
DR Ensembl; ENSNBRT00000005238.1; ENSNBRP00000005084.1; ENSNBRG00000003984.1.
DR GeneTree; ENSGT00940000159562; -.
DR OMA; MQPNWDS; -.
DR OrthoDB; 5388799at2759; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000003984; Expressed in muscle tissue and 3 other cell types or tissues.
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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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:UP000261580}.
FT DOMAIN 635..891
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1194..1225
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 955..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 664
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1285 AA; 145642 MW; 015171DE7DF3CD1E CRC64;
METGQSAPAS DMGGDHTAGV CVVERDRERG DVSSPSPPTK QRSLRVVYVL NDGLKSVMAS
SPESGALQCL QRACDSESAL LTTVTFGRLD FGETSVLDSF YDADIAVVDM SDVCRQPSLF
YHLGVRESFD MANNVILYHD TDPDTAQSLK DMVAQKNTAS SGNYYFIPYI VTPNHEYMCC
ESDAQRRASE YMQPNWDNLL GPLCDPLTDR FTSLLKDIHV TSCASFKDTL LNDIRKAREK
YQGEELAKEL SRIKLRIDNT EVLTQDIVMN LLFSYRDIQD YDAMVKLVQT LEMLPTCDLA
TQPMIQFHYS FALNRRNAPG DREQALRVML QVLQSCEHPA PDMFCLCGRI YKDIFLDSDC
KDTKNRDNAI QWYRKGFELQ PTLYSGINLA VLLIVAGQQF ESSMELRKIG VRLNSLLGRK
GSLEKMNNYW DVGQFFTVSM LASDIPKATQ AAEKLFKLKP PVWYLRSVVQ NLQLIQRFKK
QNLEHSPQRE KLNFWMDIIV EATQCTTNRL RFPVLILEPT KVYQPSYVSI NNEAEEKNVS
IWHVSPAETK GIHEWNFTAM SIKGISISKF DERCCFLYVH DNSDDFQIYF STEEQCGRFC
SMVKEMISDG TGNAVELEGE GDGDTLEYEY DTDETGERVV LGRGTYGVVY AGRDLSNQVR
IAIKEIPERD SRYSQPLHEE IALHKYLKHR NIVQYLGSIS ENGYIKIFME QVPGGSLSAL
LRSKWGPLKE ATIIFYTRQI LEGLRYLHEN QIVHRDIKGD NVLVNTYSGV LKISDFGTSK
RLAGVNPCTE TFTGTLQYMA PEIIDKGPRG YGAPADIWSL GCTIIEMATG KPPFHELGEP
QAAMFKVGMF KIHPEIPESL SQEAKSFILR CFEPDPHKRA IALDLLRDTF VRHNTKGKKS
KIAFKSPDYI PNISLPVQVQ GEAAGSSSSE HGSVSPDCDA KHDIFFDKRK SSGSKNLLKP
PSSTYLSVPD EGSVSEDRSV PPSPEDRDSG LFMLKKDSER RAILYKVLNE DQEKVISNLR
ENHMQGSEDL QLSIDHIKQI ICILRDFIHS PERRVMAATI SKLKLDLDFD STSINQIQLV
LFGFQDSVNK VLRNHHIKPH WMFAMDNIIR RAVQAAITIL IPELQTHFGP ASECEGAEKE
DEVDEEEAEF GPILVQQTDE TGTTSDPTHS AVSTVNSSHS HEHLRSQHHL GAQLGRLKHE
TNRLLDELLQ KEKEYQQVLK ATLQQRTHDL ELVRVRHRPP GKLNHSHISI PAKKKGGILC
RIWRAIQRHR ERDRLANDKR SENNA
//
