ID A0A3P9NYL0_POERE Unreviewed; 982 AA.
AC A0A3P9NYL0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406, ECO:0000256|PIRNR:PIRNR038165};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406, ECO:0000256|PIRNR:PIRNR038165};
GN Name=MAP3K13 {ECO:0000313|Ensembl:ENSPREP00000014666.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000014666.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000014666.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000014666.1};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|PIRNR:PIRNR038165}.
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DR AlphaFoldDB; A0A3P9NYL0; -.
DR Ensembl; ENSPRET00000014817.1; ENSPREP00000014666.1; ENSPREG00000009876.1.
DR GeneTree; ENSGT00940000158216; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000009876; Expressed in head.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14059; STKc_MAP3K12_13; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017419; MAP3K12_MAP3K13.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257:SF945; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 13; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF038165; MAPKKK12_MAPKKK13; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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|PIRNR:PIRNR038165, ECO:0000256|PIRSR:PIRSR038165-
KW 51}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|PIRNR:PIRNR038165};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR038165,
KW ECO:0000256|PIRSR:PIRSR038165-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038165};
KW Transferase {ECO:0000256|PIRNR:PIRNR038165}.
FT DOMAIN 193..434
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 32..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 487..521
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 44..58
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 304
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038165-50"
FT BINDING 199..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038165-51"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038165-51"
SQ SEQUENCE 982 AA; 108719 MW; 61E4E8EBCE9FFC72 CRC64;
MGSSPEVLSW TSCPSLLVGK LKEELKLSVV GDAMKKSNSP NAQSQPPQAP PAALPPQIIT
DLAPPTNLPV PLHAPSQDED SMLGGISPGN TALSVDSTRS EGGHFDNSVL QLQEQDQEEA
VSPASCDGEG RPSHPRHPDD IKLHFQRAGP GSGGFLEGLF GCLRPVWNII GKTYSTEYKL
QQQDMWEVPF EEISELQWLG SGAQGAVFLG KFRSEEVAIK KVREQKETDI KHLRKLKHPN
IISFKGVCTQ APCYCIIMEY CAQGQLYEVL RAGRKVTPRL LVDWATGIAG GMNYLHLHKI
IHRDLKSPNV LVTHNDTVKI SDFGTSKELS DKSTKMSFAG TVAWMAPEVI RNEPVSEKVD
IWSFGVVLWE LLTGEIPYKD VDSSAIIWGV GSNSLHLPVP STCPDGFKIL MKQTWQGKPR
NRPSFRQILL HLDIASSDVL GTPQETYFKS QAEWREEVKK HFEKIKSEGT CIHRLDEELI
RRRRDELRHA LDIREHYERK LERANNLYME LSAIMLQLEV REKELMKREQ AVEKKYPGSY
KRHLVRPIVR SNAVEKLIKK KGSISHKPGM PPTKRPDLLR SDGIPSVDPF PSPSPLSASP
KVSTPPGKTR YRSKPRHRRA NSKGSHSEFP GALKPVAGAA EDTQSLQEQP FHHHHLHHHH
HHHPPAEGQF LPLKGREEAV VNCANNLRYF GPAAALRSPQ TDHLQRRVSD SSPDLISTAM
DADTRQQTSS ASSNLVPGAG AVLLCPCCQA HPLPGCLHCQ ETPPTLSQPE LPHYSLLSTQ
ESNQSSLAPP NKESALNGED GSLAAPQAQD PSQSKHPLPS ALPRILRPLR KGGDESSEEE
EGEVDSEVEF PRRQRPHRCM SSFQSYSTFS SENLSVSDGE EGNTSDHSHS GPLSASQEEH
LDELLSHTPD IPIDISTQSD GLSDKECAVR RVKTQISLGK LCSDEHSYEN PLQFGDSDCD
SSEAECSDTT IRNNKVGAPS SW
//
