ID A0A0V1A5G9_9BILA Unreviewed; 1369 AA.
AC A0A0V1A5G9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 18-JUN-2025, entry version 34.
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|EMBL:KRY20070.1};
GN ORFNames=T12_4911 {ECO:0000313|EMBL:KRY20070.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY20070.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY20070.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY20070.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:ARBA00048329};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25;
CC Evidence={ECO:0000256|ARBA:ARBA00047559};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY20070.1}.
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DR EMBL; JYDQ01000028; KRY20070.1; -; Genomic_DNA.
DR STRING; 990121.A0A0V1A5G9; -.
DR OrthoDB; 146388at6231; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
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 Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 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:SF394; APOPTOTIC SIGNAL-REGULATING KINASE 1, ISOFORM C; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRY20070.1};
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:UP000054783};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 586..846
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1195..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1264
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 615
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1369 AA; 154416 MW; 91C714F054439DB7 CRC64;
MSRKVTPPGS LVSADSVTGI KPLSRALQVA VVIDLLIKDG LPIRQLVWDE LQKLDESTNM
NMQYIPFEKL DFGEISSLDM FYNADLAIVD VSVSSQRTTL CYHLGVRESM HQDYNIVLCS
FEEKRQPMSF MFMVPFNNYK PLICTTSDNA LIAVECSQFF PGMSSNAILA SGNNSSFRTK
IKKLLKDVQI DATAHVKEKF LADLRQARQK CEGGELSVVL DRLRMRLDDP DVLSVDTVVN
MLLSYRDIQN YNAMVSLVED VSSLPYDKIH ESPAVQFNYA FALNRRNKDK DRDKALSVTL
DSLSSQENQV PDFLCLAGRI YKDKLAEYRK GFEIQPNEYA GINLATLLVI AGETFQTSSE
LQQIGYTVIL SGLLGRKGSL QDLKDYWDVA TFFEISVLAE NYANSCQAAY HMFLKSTIGN
IKLIKRFRET LNRSMPENQF DYRQFLFWME FFVENTKSDE ICTDTRFPVL TMEPSKIYIP
SYVSVNEESK AISLWHVEDT NRKNLTQWIF PAESIRAVSA ARRDERAVYL YVYLNSDDFM
LFFPSDNHRK RFLQLVEEIT CFEGTKLLAS YTELQPVLYE YETDANDQRV VLGKGTFGTV
YAGRDLNSQR TIAIKEVEIK NHEEVQPLME EIQLHSTLVH PNIVQYLGCE VSDDNRIFRI
FMEQVPGGSL SLLLRNKWGP LIDNETTIAY YARQILEGLN YLHSQKIVHR DIKGDNVLVN
TYSGQCKISD FGTCKRLAGL NPIADTFTGT LQYMAPEVID QGMRGYGAPA DIWSFGCTMI
EMASGKPPFV ELGSPQAAIF KVGMFKAHPP IPEGLSNQAK QLIERCFEPD PNKRPTAVQL
LVDPFFEQIR FRRIAKPALE SGYRDSSRFY ARSISCVNSQ SDQKRDSFII SLFYLTKSSR
LSSSSLLALN ELSDSSGIQE RHPSSAGHDS AASKFFMLRK DSERRDTLAT IMTEYENQII
DLWLSSIGSG PNSDVAVSAN ILRTLLTCMR NYIFDKDSTK VRTVAVYFFQ SLQQTILRGK
MYRNGHIDPP IFTDEIRCLI SSGATSNTNI RLALYAFQDV MHYVLRQQRI KPHWMFALDN
LIRSCVQCVV EMLLPDAISN LSVQDSDGSS SYSSVVSAKS PIVPSFGYND FGFTNSLTKQ
LRKELKDYTA ENQRLLGELL KLYTCYQKLL KPLTEHVEQK LTATTTTTTA IKCAGSSSSN
SSGICAAGRG RKAEEQQQMS RRNSAPATTG SMAAETRKCS LIVEEEGVGG VESSASVSSS
LLDNSSDDYQ EGKSWTKDSS LPKNDDDDAL VSWLKELNVD ERSIAILTDH QYTLQDLMEM
VTREELLHIG LKGGVCCRLW RSIVSQRNST AATTVPATDE ADRRENNND
//
