ID A0A0V1N683_9BILA Unreviewed; 2081 AA.
AC A0A0V1N683;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 18-JUN-2025, entry version 38.
DE SubName: Full=Mitogen-activated protein kinase kinase kinase 15 {ECO:0000313|EMBL:KRZ79356.1};
GN Name=MAP3K15 {ECO:0000313|EMBL:KRZ79356.1};
GN ORFNames=T10_4780 {ECO:0000313|EMBL:KRZ79356.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ79356.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ79356.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ79356.1};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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:KRZ79356.1}.
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DR EMBL; JYDO01000007; KRZ79356.1; -; Genomic_DNA.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-ARBA.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF25376; Pre-PUA_NSUN2; 1.
DR Pfam; PF25378; PUA_NSUN2; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 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:KRZ79356.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 82..414
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT DOMAIN 1295..1561
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1871..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1954..1980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2045..2081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1896..1910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2055..2064
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2070..2081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 259
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 286
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2081 AA; 235263 MW; DFE1F1694EAAD209 CRC64;
MICRKQNAAV KLNRFKISEM GKSKRHRKVK FRKRRNDLDA FGKSGMKALP KNDRFITDRH
SSRFEIFYRT QGFIPEEEWE LFLKHLASDL PQSFRFVGNS KEGTMALQIF KEKFLSEVTR
CTVENEDVIV NIREMNWYPN GLAFEINLPK KTLRRQTELQ SLHNFLVVET ACGILSRQEA
VSMIPPLFMD IKSHHSILDM CASPGSKTVQ LIEMLHADGE TLPTGFIIAN DLNNERCYLL
VHQSLRRSGS PCCVITNCDA SQFPDVFMPD KFGKLTKLKF DRILCDVPCS SDGTMRKNLN
LWKEWHVNHA YALHRLQRKI VERGLHLLAT GGAVELVDVG NQLPELVRSK GFHHWKVLDA
EGNVYSSPYE VPDHLKSKIH DGLFPPDESL AENLRIFPHH QNTGGFFIAV LRKVCEFSWS
TGKEAEVLVP SGQDLKSSSE KKRRYGGFKE DPFIFLNGDN NNELIQEYFG MDDRFSKFSL
LMRQKEVSKK GNIYLVNENI KHFMKNNEHR IKIINAGLRT FSRCSVSNSA RDDFRLVQDG
LRYVIPLMSK RLVNISKDEL LKLIKSKESI LLKDLSDELH SQLEQIGEGS VALVHGAEDA
KCSLQVASWL GKCSIAPHLD KENRAHFLFM LDDFQAAYDM YKGNETDEVD KKLEAVTRDD
EVEYLLRKAV EKKHKYIIID TIEEEVMSRK VTPPGSLVSA DSVTAIKPLS RALQVAVVID
LLIKDGLSIR QLVWDELQKL DESTNMNMQY IPFEKLDFGE ISSLDMFYNA DLAIVDVSVS
SQRTTLCYHL GVRESMHQDY NIVLCSFEEK RQPMSFMFMV PFNNYKPLIC TTSENALIAV
ECSQFFPGMS SSAILASHGN NSSFRTKIKK LLKDVQIDAT AHVKEKFLAD LRQARQKCEG
GDLSVVLDRL RMRLDDPDVL SVDTVVNMLL SYRDIQNYNA MVSLVEDVSS LPYDKIHESP
AVQFNYAFAL NRRNKDKDRD KALSVTLDSL SSQENQVPDF LCLAGRIYKD KLAESNFADI
EARDAAIHWQ ALIIDLIEYR KGFEIQPNEY AGINLATLLV IAGETFQTSS ELQQIAVILS
GLLGRKGSLQ DLKDYWDVAT FFEISVLAEN YSNSCQAAYH MFLKSTIGNI KLIKRFRETL
NRSMPENQFE YQQFLFWMEF FVENTKSDEL CTDTRFPVLT MEPSKIYIPS YVSVNEDSKA
ISLWHVEDTN RKNLTQWIFP AESIRAVSAA RRDERAVYLY VYLNSDDFML FFPSDNHRKR
FLQLVEEITC FEGTKLLASY AELQPVLYEY ETDANDQRVV LGKGTFGTVY AGRDLNSQRT
IAIKEVEIKN HEEVQPLMEE IQLHSTLVHP NIVQYLGCEV SDDNRIFRIF MEQVPGGSLS
LLLRNKWGPL IDNETTIAYY ARQILEGLNY LHSQKIVHRD IKGDNVLVNT YSGQCKISDF
GTCKRLAGLN PIADTFTGLC SPVGTLQYMA PEVIDQGMRG YGAPADIWSF GCTMIEMASG
KPPFVELGSP QAAIFKVGMF KAHPPIPEGL SNQAKQLIER CFEPDPNKRS TAVQLLVDPF
FEQVRFRRIA KPALESGYRD SSRFYARSIS CVNSQSDQKR ESSRLSASSL LALNELSDNS
AIQERQPSSA GHDSAASKFF MLRKDSERRD TLATIMTDYE NQIIELWLSS IGNGSNSDVA
VSANILRTLL ACMRKYIFDK DSTKVRTVAG NGYIDTPIFT DEIRCLISSG ATSNTNIRLA
LYAFQDVMHY VLRQQRIKPH WMFALDNLIR SCVQCVVEML LPDAVSNLSV QDSDGSSSYS
SVESAKSPIV PSFGYNDFGF TNSLAKQLRK ELKDYTAENQ RLLGELLKLY TCYQKLLRPL
TEHVEQKLTS TTTTTTTTTK CDSSSIGISA KKAEEQQQMS RRNSAPAATT SLIAAETRKC
SLIVEEESVP CGVESSSLGN NSDDQQDSIG AVVDWKKKDS SSSKNDTGTD SGSGSGVDDG
DDASLIAWLK ELNVDERSIA ILTNHQYTLQ DLMEMVTREE LLHIGLKGGV CCRLWRSIIS
QRRSCAGGDG GGCGDSSSTT TATTIATNDE AERRENDNQS N
//
