ID A0A085NJP7_9BILA Unreviewed; 2009 AA.
AC A0A085NJP7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=M514_10635 {ECO:0000313|EMBL:KFD69693.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD69693.1};
RN [1] {ECO:0000313|EMBL:KFD69693.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD69693.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
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|ARBA:ARBA00007494,
CC 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}.
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DR EMBL; KL367493; KFD69693.1; -; Genomic_DNA.
DR Proteomes; UP000030758; 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; IPR018314; Fmu/NOL1/Nop2p_CS.
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; PS01153; NOL1_NOP2_SUN; 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:ARBA00022527};
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 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 58..422
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT DOMAIN 1361..1621
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 314
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 175..181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 206
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2009 AA; 226894 MW; A423413C52558027 CRC64;
MTKRKWKNVK DGPKKLRDGG SERIANQKPY EEVERRSEKF ESYYKAQRVV PDNEWDTFMQ
CLKSDLPVTF RFVAGRKDSS VLLQKFRERF FQTLCESGIE ATEATMKELE WYPDGLAFEL
NMDKKSFRRH PKFRQLHKFL VAETACGILS RQEAVSMIPP LFMDVKPAHY VLDTCAAPGS
KTVQILEMLH SDESVPIPSG LVVANDSNNE RCYLLVHQAL KRSGSPCCVV TNMDAMTMPN
TVILNESGDV VNMNFDRILC DVPCSGDGTL RKNINLWKEW NAVQAYGLHK LQLKIALRCA
KLLKVGGLMV YSTCSMNPIE DEAVVATLIA QSHERLELMP TRHMLPKLIR CDGLFTWKVS
DNSGTFYENH GQLPDHFKRK IPNTAFPPDL ETAREMHLER CMRILPHHQN TGGFFVAVLR
KVGEASIPPA LRTEAITTSS EWKSVVKDKE TPRKRKFAGR QEDPFVFIEK SDDTTASITD
FYGMKGGFDH LPLLVRSSDV SKKANIYLVN NAAKSFITHN EDRIKIINAG LRIFGRSSAK
AEACTFRLAQ EGVHFLFPMI TRRVVTITVP DLTKLLKTNE NCLLKELSED LQSALLPYGE
GSIVFNCLMG ELNIIVTGWR GKVSVVLYLD KETKLHYLYL LGEEGEESEP STEGDSSVVP
RGCASIDVEN SNENKGENHS SQLRTSRSFP TRCSRCGRSP ELWASVRSVM CCPLAVAALR
SKPSPTIRKA GKKLYPFRLP KGMASTKESQ SDSASCNTDD AVVVPKLGGG RLLQAVVVID
LLLKEEGLSA RQMIWDELQA LESLLDIKVQ WIPFEKLGFG ETSTLGSFYN ADVVVVDVSN
SLQQSTLCYH LGVRESMNQN YNIVLYAFDE TFRERAPLHF KIPQNNYRTL LYALVDGALV
AWSCTHVVFG VPWFGNAPTV NGGSQGKRSF RSQIKQMLNE VQIDASKHSK EKFLADLQIA
RQNYRGEKFN TVLNQLRSRL DDPDVLSVDT VVSMLLSYRD VQNYGAMVSM VEDVESLPQA
KIFHSSAVQF HYAFALNRRN IGDDRNKALQ VILSMLEKQE NQIPDFLCLA GRIYKDRLYE
SKCQDRESLD EAIKWYRKGF EIQPNEYAGI NLATLLVIAG ESFQTCNELQ QIAMILSGLL
GRKGSLFNLL DYWDVATFFE ISVLAENYIN ACQAASRMFE LKPPAWFLKS TIGNIKLIKW
YRESTRSAMD NCTQYQHFLF WMEFFVEYTR TEPVTSDIRF PVLSMEPSKV HVPSYVSVNE
ANNSISLWHV EDATVKANVN QWIFPAESIR AISASKSDER TVYLYVYLNS DDFTLILPTD
FHRQRFLELA SQVTSTTEGT KLLGDYTDLE PISYEFELDK DGNRTVLGKG TFGTVYSGRD
FDSQRMIAIK ELEVKNPEGV QPLVEEIQLH STLKHVNIVQ YLGCEVSEDQ KVFRIFMELV
PGGSLSLLLR NKWGPLIDNE NSIAYYARQI LQGLNYLHSQ KIVHRDIKGD NVLVNTYSGL
CKISDFGTCK RLAGLNPDAE GMTGTPQYMA PEVIEEGLRG YGAPADIWSF GCTMIEMATG
KPPFFEFGLP EASMFKVGMF KVHPPIPEKL SNAAKSLILK CFEPDPSQRP TAAMLIMNSF
FDKCRWRRYN EQPEVSAFSD ASRHFGRSIS YTTSSQEEKD ESMQISSSLL SLNEILDERS
PSEKGVSIPE APGPSSRASF LRKESERREI LSGIMRESEN RIIELWLSSI QTGITGPIAS
EDVLRSLLVC LRDFIYDKDV AKLRKTGERI AELLGTDATS ATQLHLAFYA FQDVMHSVLR
RHRIRPHWMF TLDNLTRSSV QSIIEAILPE PKPLSSSDDD DANSSYSTVT SVDLSKKSNY
GLHDGRVLIS LLNDLRSELA DFFASTKRST IEFRKAVQSC QALLSAIASK ISSPSNALTH
PMDRAFGKAR PGNVDEELVD WLRRIDIDEH SINILTREEY TLQNLLEMVT SREELLQLGI
RGGVSCRIWK HIVMHRKKAA HDSCTLPGT
//
