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Conserved domains on  [gi|751451392|ref|XP_011180020|]
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mRNA cap guanine-N7 methyltransferase [Zeugodacus cucurbitae]

Protein Classification

mRNA cap guanine-N7 methyltransferase( domain architecture ID 10505544)

mRNA cap guanine-N7 methyltransferase is the catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 91-423 2.17e-135

mRNA capping enzyme; This family of enzymes are related to pfam03919.


:

Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 392.18  E-value: 2.17e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392   91 TDGNMRVVASHYNELKETG--RKERLKSRIVYMRNFNNWLKSQLIAEYLARIKEQqriGDPMRVLDLCCGKGGDLLKWEK 168
Cdd:pfam03291   7 NSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQN---SNKRKVLDLGCGKGGDLEKWFK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392  169 ANITHLICTDIAEVSVDQCKKRYeeMQTRADKSKFANKFSAEFFACDATLVRLRERYKDKSLKLNLVSCQFAFHYSFESL 248
Cdd:pfam03291  84 GGISQLIGTDIAEVSIEQCRERY--NKLRSGNKSKYYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFESE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392  249 TQAECMVRNAAECLQPGGYFIATIPDANEIM----RRLRQSH-NPRSIGNDIYKIDFICDTDPPPLFGAKYQFHLEGVV- 322
Cdd:pfam03291 162 EKARTMLRNVAELLASGGVFIGTTPDSDFISaltiKRLFAIEkDLPSFGNSIYSVKFEEEPPQVPLFGIKYDYNLEDAVd 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392  323 DCPEFLVHFPTLVKLCRKYGLKLERKTTFADYYKESLDK-GRALLQRMNGLETVVPNRRgkdpefqhlqaFFKGGSSKSI 401
Cdd:pfam03291 242 DVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIKKeFKKLIKRMSAMESRPSTRN-----------FFGLQRSAGK 310

                         330       340
                  ....*....|....*....|..
gi 751451392  402 GTLSQSEWEATTLYLVCAFRKC 423
Cdd:pfam03291 311 GTLGGDEWEAASFYLVFVFEKR 332
 
Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 91-423 2.17e-135

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 392.18  E-value: 2.17e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392   91 TDGNMRVVASHYNELKETG--RKERLKSRIVYMRNFNNWLKSQLIAEYLARIKEQqriGDPMRVLDLCCGKGGDLLKWEK 168
Cdd:pfam03291   7 NSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQN---SNKRKVLDLGCGKGGDLEKWFK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392  169 ANITHLICTDIAEVSVDQCKKRYeeMQTRADKSKFANKFSAEFFACDATLVRLRERYKDKSLKLNLVSCQFAFHYSFESL 248
Cdd:pfam03291  84 GGISQLIGTDIAEVSIEQCRERY--NKLRSGNKSKYYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFESE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392  249 TQAECMVRNAAECLQPGGYFIATIPDANEIM----RRLRQSH-NPRSIGNDIYKIDFICDTDPPPLFGAKYQFHLEGVV- 322
Cdd:pfam03291 162 EKARTMLRNVAELLASGGVFIGTTPDSDFISaltiKRLFAIEkDLPSFGNSIYSVKFEEEPPQVPLFGIKYDYNLEDAVd 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392  323 DCPEFLVHFPTLVKLCRKYGLKLERKTTFADYYKESLDK-GRALLQRMNGLETVVPNRRgkdpefqhlqaFFKGGSSKSI 401
Cdd:pfam03291 242 DVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIKKeFKKLIKRMSAMESRPSTRN-----------FFGLQRSAGK 310

                         330       340
                  ....*....|....*....|..
gi 751451392  402 GTLSQSEWEATTLYLVCAFRKC 423
Cdd:pfam03291 311 GTLGGDEWEAASFYLVFVFEKR 332
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 146-285 1.87e-10

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 58.85  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392 146 IGDPMRVLDLCCGKGGDLLKWEKANiTHLICTDIAEVSVDQCKKRYEEMQTRadkskfankfsAEFFACDATLVRLRERY 225
Cdd:COG2226   20 LRPGARVLDLGCGTGRLALALAERG-ARVTGVDISPEMLELARERAAEAGLN-----------VEFVVGDAEDLPFPDGS 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 751451392 226 KDkslklnLVSCQFAFHYsFESLTQAecmVRNAAECLQPGGYFIAT---IPDANEIMRRLRQS 285
Cdd:COG2226   88 FD------LVISSFVLHH-LPDPERA---LAEIARVLKPGGRLVVVdfsPPDLAELEELLAEA 140
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 151-272 5.91e-09

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 53.59  E-value: 5.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392 151 RVLDLCCGKGGDLLKWEKANITHLICTDIAEVSVDQCKKRYEEmqtradkskfANKFSAEFFACDAtlvrlRERYKDKSL 230
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAA----------LLADNVEVLKGDA-----EELPPEADE 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 751451392 231 KLNLVSCQFAFHYSFESLtqaECMVRNAAECLQPGGYFIATI 272
Cdd:cd02440   66 SFDVIISDPPLHHLVEDL---ARFLEEARRLLKPGGVLVLTL 104
 
Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 91-423 2.17e-135

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 392.18  E-value: 2.17e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392   91 TDGNMRVVASHYNELKETG--RKERLKSRIVYMRNFNNWLKSQLIAEYLARIKEQqriGDPMRVLDLCCGKGGDLLKWEK 168
Cdd:pfam03291   7 NSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQN---SNKRKVLDLGCGKGGDLEKWFK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392  169 ANITHLICTDIAEVSVDQCKKRYeeMQTRADKSKFANKFSAEFFACDATLVRLRERYKDKSLKLNLVSCQFAFHYSFESL 248
Cdd:pfam03291  84 GGISQLIGTDIAEVSIEQCRERY--NKLRSGNKSKYYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFESE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392  249 TQAECMVRNAAECLQPGGYFIATIPDANEIM----RRLRQSH-NPRSIGNDIYKIDFICDTDPPPLFGAKYQFHLEGVV- 322
Cdd:pfam03291 162 EKARTMLRNVAELLASGGVFIGTTPDSDFISaltiKRLFAIEkDLPSFGNSIYSVKFEEEPPQVPLFGIKYDYNLEDAVd 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392  323 DCPEFLVHFPTLVKLCRKYGLKLERKTTFADYYKESLDK-GRALLQRMNGLETVVPNRRgkdpefqhlqaFFKGGSSKSI 401
Cdd:pfam03291 242 DVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIKKeFKKLIKRMSAMESRPSTRN-----------FFGLQRSAGK 310

                         330       340
                  ....*....|....*....|..
gi 751451392  402 GTLSQSEWEATTLYLVCAFRKC 423
Cdd:pfam03291 311 GTLGGDEWEAASFYLVFVFEKR 332
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 146-285 1.87e-10

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 58.85  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392 146 IGDPMRVLDLCCGKGGDLLKWEKANiTHLICTDIAEVSVDQCKKRYEEMQTRadkskfankfsAEFFACDATLVRLRERY 225
Cdd:COG2226   20 LRPGARVLDLGCGTGRLALALAERG-ARVTGVDISPEMLELARERAAEAGLN-----------VEFVVGDAEDLPFPDGS 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 751451392 226 KDkslklnLVSCQFAFHYsFESLTQAecmVRNAAECLQPGGYFIAT---IPDANEIMRRLRQS 285
Cdd:COG2226   88 FD------LVISSFVLHH-LPDPERA---LAEIARVLKPGGRLVVVdfsPPDLAELEELLAEA 140
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 133-274 1.53e-09

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 55.79  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392 133 IAEYLARikeqqRIGDPMRVLDLCCGKGGDLLKWEKANItHLICTDIAEVSVDQCKKRYEEMqtradkskfankfSAEFF 212
Cdd:COG2227   14 LAALLAR-----LLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAEL-------------NVDFV 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751451392 213 ACDATLVRLRERYKDkslklnLVSCqfafHYSFESLTQAECMVRNAAECLQPGGYFIATIPD 274
Cdd:COG2227   75 QGDLEDLPLEDGSFD------LVIC----SEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 135-290 3.18e-09

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 56.46  E-value: 3.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392 135 EYLARIKEQQRIGDPMRVLDLCCGKGGDLLKWEKANITHLICTDIAEVSVDQCKKryeemqtRADKSKFANkfsAEFFAC 214
Cdd:COG0500   13 GLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARA-------RAAKAGLGN---VEFLVA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751451392 215 DATlvrlrERYKDKSLKLNLVSCQFAFHY-SFESLTQAecmVRNAAECLQPGGYFIATIPDANEIMRRLRQSHNPRS 290
Cdd:COG0500   83 DLA-----ELDPLPAESFDLVVAFGVLHHlPPEEREAL---LRELARALKPGGVLLLSASDAAAALSLARLLLLATA 151
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 152-266 3.27e-09

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 53.72  E-value: 3.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392  152 VLDLCCGKGGDLLKWEKANITHLICTDIAEVSVDQCKKRYEEmqtradkskfaNKFSAEFFACDATLVRLRERYKDkslk 231
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAE-----------AGLNVEFVQGDAEDLPFPDGSFD---- 65

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 751451392  232 lnLVSCQFAFHYSfeSLTQAECMVRNAAECLQPGG 266
Cdd:pfam13649  66 --LVVSSGVLHHL--PDPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 151-272 5.91e-09

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 53.59  E-value: 5.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392 151 RVLDLCCGKGGDLLKWEKANITHLICTDIAEVSVDQCKKRYEEmqtradkskfANKFSAEFFACDAtlvrlRERYKDKSL 230
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAA----------LLADNVEVLKGDA-----EELPPEADE 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 751451392 231 KLNLVSCQFAFHYSFESLtqaECMVRNAAECLQPGGYFIATI 272
Cdd:cd02440   66 SFDVIISDPPLHHLVEDL---ARFLEEARRLLKPGGVLVLTL 104
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
126-291 1.17e-08

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 54.62  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392 126 NWLKSQLIAEYLARIKEQQRIGDPMRVLDLCCGKG--GDLLKwekANITHLICTDIAEVSVDQCKKRyeemqtradkskf 203
Cdd:COG4976   24 EDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGllGEALR---PRGYRLTGVDLSEEMLAKAREK------------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392 204 anKFSAEFFACDAT-LVRLRERYkdkslklNLVSCQFAFHYsFESLTQaecMVRNAAECLQPGGYFIATIPDANEimrRL 282
Cdd:COG4976   88 --GVYDRLLVADLAdLAEPDGRF-------DLIVAADVLTY-LGDLAA---VFAGVARALKPGGLFIFSVEDADG---SG 151


                 ....*....
gi 751451392 283 RQSHNPRSI 291
Cdd:COG4976  152 RYAHSLDYV 160
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 146-275 5.83e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 45.87  E-value: 5.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392  146 IGDPMRVLDLCCGKGGDLLKWekaniTHLICTDIAEVSVDQCKKRYEEMQTRADKSKFANkfsAEFFACDATLvrLRERY 225
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFEL-----AEELGPNAEVVGIDISEEAIEKARENAQKLGFDN---VEFEQGDIEE--LPELL 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 751451392  226 KDKslKLNLVSCQFAFHYSFEsltQAECMvRNAAECLQPGGYFIATIPDA 275
Cdd:pfam13847  71 EDD--KFDVVISNCVLNHIPD---PDKVL-QEILRVLKPGGRLIISDPDS 114
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 137-273 2.21e-05

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 44.54  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392 137 LARIKEQQRIGDPMRVLDLCCGKGGDLLKWEKANITHLICTDIAEVSVDQCKKRYEEMQTRAdkskfankfSAEFFACDA 216
Cdd:COG2230   40 LDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLAD---------RVEVRLADY 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 751451392 217 TLVRLRERYkDKslklnlVSCQFAFHYsFESLTQAECMvRNAAECLQPGGYFIATIP 273
Cdd:COG2230  111 RDLPADGQF-DA------IVSIGMFEH-VGPENYPAYF-AKVARLLKPGGRLLLHTP 158
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
149-271 3.61e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 42.50  E-value: 3.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392 149 PMRVLDLCCGkGGDLLKW--EKANITHLICTDIAEVSVDQCKKRYEEmqtradkskfankfsAEFFACDATLVRLRERYk 226
Cdd:COG4106    2 PRRVLDLGCG-TGRLTALlaERFPGARVTGVDLSPEMLARARARLPN---------------VRFVVADLRDLDPPEPF- 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 751451392 227 dkslklNLVSCQFAFHYsfesLTQAECMVRNAAECLQPGGYFIAT 271
Cdd:COG4106   65 ------DLVVSNAALHW----LPDHAALLARLAAALAPGGVLAVQ 99
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 153-269 1.59e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 37.64  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392  153 LDLCCGKGGDLLKWEKANItHLICTDIAEVSVDQCKKRYEEMQtradkskfankfsAEFFACDATLVRLRERYKDkslkl 232
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISPEMLELAREKAPREG-------------LTFVVGDAEDLPFPDNSFD----- 61

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 751451392  233 nLVSCQFAFHYsFESLTQAecmVRNAAECLQPGGYFI 269
Cdd:pfam08241  62 -LVLSSEVLHH-VEDPERA---LREIARVLKPGGILI 93
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 137-282 2.67e-03

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 38.39  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751451392 137 LARIKEqqriGDpmRVLDLCCGKGGDLLKWEKANItHLICTDIAEVSVDQCKKRYEemqtradkskFANKFSAEFFACDA 216
Cdd:COG1041   21 LAGAKE----GD--TVLDPFCGTGTILIEAGLLGR-RVIGSDIDPKMVEGARENLE----------HYGYEDADVIRGDA 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751451392 217 TLVRLRERYKDkslklnLVSCQF----AFHYSFESLTQA-ECMVRNAAECLQPGGYF-IATIPDANEIMRRL 282
Cdd:COG1041   84 RDLPLADESVD------AIVTDPpygrSSKISGEELLELyEKALEEAARVLKPGGRVvIVTPRDIDELLEEA 149
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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