ID A0A0V1N5S0_9BILA Unreviewed; 2118 AA.
AC A0A0V1N5S0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Mitogen-activated protein kinase kinase kinase 15 {ECO:0000313|EMBL:KRZ79355.1};
GN Name=MAP3K15 {ECO:0000313|EMBL:KRZ79355.1};
GN ORFNames=T10_4780 {ECO:0000313|EMBL:KRZ79355.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ79355.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ79355.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ79355.1};
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=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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KRZ79355.1}.
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DR EMBL; JYDO01000007; KRZ79355.1; -; Genomic_DNA.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
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:SF369; 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 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:0000313|EMBL:KRZ79355.1};
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..462
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT DOMAIN 1346..1612
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1917..1960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1991..2017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2082..2118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2090..2104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 339
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
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 1375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2118 AA; 239793 MW; 5CA37016CA5E1547 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 GGLLVYSTCS MNPAEDEAVI TQILIYSQGM
YINEIEKNEN IIYFIRSFIR AVELVDVGNQ LPELVRSKGF HHWKVLDAEG NVYSSPYEVP
DHLKSKIHDG LFPPDESLAE NLRIFPHHQN TGGFFIAVLR KVCEFSWSTG KEAEVLVPSG
QDLKSSSEKK RRYGGFKEDP FIFLNGDNNN ELIQYAQEYF GMDDRFSKFS LLMRQKEVSK
KGNIYLVNEN IKHFMKNNEH RIKIINAGLR TFSRCSVSNS ARDDFRLVQD GLRYVIPLMS
KRLVNISKDE LLKLIKSKES ILLKDLSDEL HSQLEQIGEG SVALVHGAED AKCSLQVASW
LGKCSIAPHL DKENRAHFLF MLDDFQAAYD MYKGNETDEV DKKLEAVTRD DEVEYLLRKA
VEKKHKYIII DTIEEEVMSR KVTPPGSLVS ADSVTAIKPL SRALQVAVVI DLLIKDGLSI
RQLVWDELQK LDESTNMNMQ YIPFEKLDFG EISSLDMFYN ADLAIVDVSV SSQRTTLCYH
LGVRESMHQD YNIVLCSFEE KRQPMSFMFM VPFNNYKPLI CTTSENALIA VECSQFFPGM
SSSAILASHG NNSSFRTKIK KLLKDVQIDA TAHVKEKFLA DLRQARQKCE GGDLSVVLDR
LRMRLDDPDV LSVDTVVNML LSYRDIQNYN AMVSLVEDVS SLPYDKIHES PAVQFNYAFA
LNRRNKDKDR DKALSVTLDS LSSQENQVPD FLCLAGRIYK DKLAESNFAD IEARDAAIHW
QALIIDLIEY RKGFEIQPNE YAGINLATLL VIAGETFQTS SELQQIAVIL SGLLGRKGSL
QDLKDYWDVA TFFEISVLAE NYSNSCQAAY HMFLKSTIGN IKLIKRFRET LNRSMPENQF
EYQQFLFWME FFVENTKSDE LCTDTRFPVL TMEPSKIYIP SYVSVNEDSK AISLWHVEDT
NRKNLTQWIF PAESIRAVSA ARRDERAVYL YVYLNSDDFM LFFPSDNHRK RFLQLVEEIT
CFEGTKLLAS YAELQPVLYE YETDANDQRV VLGKGTFGTV YAGRDLNSQR TIAIKEVEIK
NHEEVQPLME EIQLHSTLVH PNIVQYLGCE VSDDNRIFRI FMEQVPGGSL SLLLRNKWGP
LIDNETTIAY YARQILEGLN YLHSQKIVHR DIKGDNVLVN TYSGQCKISD FGTCKRLAGL
NPIADTFTGL CSPVGTLQYM APEVIDQGMR GYGAPADIWS FGCTMIEMAS GKPPFVELGS
PQAAIFKVGM FKAHPPIPEG LSNQAKQLIE RCFEPDPNKR STAVQLLVDP FFEQVRFRRI
AKPALESGYR DSSRFYARSI SCVNSQSDQK RESSRLSASS LLALNELSDN SAIQERQPSS
AGHDSAASKF FMLRKDSERR DTLATIMTDY ENQIIELWLS SIGNGSNSDV AVSANILRTL
LACMRKYIFD KDSTKVRTVA GNGYIDTPIF TDEIRCLISS GATSNTNIRL ALYAFQDVMH
YVLRQQRIKP HWMFALDNLI RSCVQCVVEM LLPDAVSNLS VQDSDGSSSY SSVESAKSPI
VPSFGYNDFG FTNSLAKQLR KELKDYTAEN QRLLGELLKL YTCYQKLLRP LTEHVEQKLT
STTTTTTTTT KCDSSSIGIS AKKAEEQQQM SRRNSAPAAT TSLIAAETRK LSSSLGNNSD
DQQDSIGAVV DWKKKDSSSS KNDTGTDSGS GSGVDDGDDA SLIAWLKELN VDERSIAILT
NHQYTLQDLM EMVTREELLH IGLKGGVCCR LWRSIISQRR SCAGGDGGGC GDSSSTTTAT
TIATNDEAER RENDNQSN
//
