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Conserved domains on  [gi|569004395|ref|XP_006526256|]
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mRNA cap guanine-N7 methyltransferase isoform X1 [Mus musculus]

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.
 125-464 5.32e-160

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


:

Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 455.74  E-value: 5.32e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  125 QKLQKLEEGHSSAVAAHYNELQEVG--LAKRSQSRIFYLRNFNNWIKSILIGEILEKVRQRkTRDITVLDLGCGKGGDLL 202
Cdd:pfam03291   1 EGPFETNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQN-SNKRKVLDLGCGKGGDLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  203 KWRKGRISRLVCADIADISMKQCQQRYedMRCRRDNEHI---FSAEFITADCSKELLVEKFRDPEMYFDVCSCQFACHYS 279
Cdd:pfam03291  80 KWFKGGISQLIGTDIAEVSIEQCRERY--NKLRSGNKSKyykFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  280 FESQVQADTMLRNACGRLNPGGYFIGTTPNSFEL----IRRLEASE--TESFGNEIYTVKFQ-KKGNYPLFGCKYDFNLE 352
Cdd:pfam03291 158 FESEEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEeEPPQVPLFGIKYDYNLE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  353 GVV-DVPEFLVYFPLLTEMAKKYNMKLIYKKTFLEFYEEKIKnNENKMLLKRMQALEQYPAHENSklasekvgdythaae 431
Cdd:pfam03291 238 DAVdDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIK-KEFKKLIKRMSAMESRPSTRNF--------------- 301

                         330       340       350
                  ....*....|....*....|....*....|...
gi 569004395  432 ylKKSQVRLPLGTLSKSEWEATSIYLVFAFEKQ 464
Cdd:pfam03291 302 --FGLQRSAGKGTLGGDEWEAASFYLVFVFEKR 332
 
Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 125-464 5.32e-160

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


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 455.74  E-value: 5.32e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  125 QKLQKLEEGHSSAVAAHYNELQEVG--LAKRSQSRIFYLRNFNNWIKSILIGEILEKVRQRkTRDITVLDLGCGKGGDLL 202
Cdd:pfam03291   1 EGPFETNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQN-SNKRKVLDLGCGKGGDLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  203 KWRKGRISRLVCADIADISMKQCQQRYedMRCRRDNEHI---FSAEFITADCSKELLVEKFRDPEMYFDVCSCQFACHYS 279
Cdd:pfam03291  80 KWFKGGISQLIGTDIAEVSIEQCRERY--NKLRSGNKSKyykFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  280 FESQVQADTMLRNACGRLNPGGYFIGTTPNSFEL----IRRLEASE--TESFGNEIYTVKFQ-KKGNYPLFGCKYDFNLE 352
Cdd:pfam03291 158 FESEEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEeEPPQVPLFGIKYDYNLE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  353 GVV-DVPEFLVYFPLLTEMAKKYNMKLIYKKTFLEFYEEKIKnNENKMLLKRMQALEQYPAHENSklasekvgdythaae 431
Cdd:pfam03291 238 DAVdDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIK-KEFKKLIKRMSAMESRPSTRNF--------------- 301

                         330       340       350
                  ....*....|....*....|....*....|...
gi 569004395  432 ylKKSQVRLPLGTLSKSEWEATSIYLVFAFEKQ 464
Cdd:pfam03291 302 --FGLQRSAGKGTLGGDEWEAASFYLVFVFEKR 332
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 175-309 4.30e-11

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: 60.03  E-value: 4.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395 175 EILEKVRQRKTRDITVLDLGCGkGGDLLKWRKGRISRLVCADIADISMKQCQQRYEDMRcrrdnehifsAEFITADcske 254
Cdd:COG2227   13 RLAALLARLLPAGGRVLDVGCG-TGRLALALARRGADVTGVDISPEALEIARERAAELN----------VDFVQGD---- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 569004395 255 llVEKFRDPEMYFDVcscqFACHYSFESQVQADTMLRNACGRLNPGGYFIGTTPN 309
Cdd:COG2227   78 --LEDLPLEDGSFDL----VICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 189-304 1.10e-08

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: 52.82  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395 189 TVLDLGCGKGGDLLKWRKGRISRLVCADIADISMKQCQQryedmrcRRDNEHIFSAEFITADCSKELLvekFRDPEmyFD 268
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARK-------AAAALLADNVEVLKGDAEELPP---EADES--FD 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 569004395 269 VCSCQFACHYSFESQVQadtMLRNACGRLNPGGYFI 304
Cdd:cd02440   69 VIISDPPLHHLVEDLAR---FLEEARRLLKPGGVLV 101
 
Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 125-464 5.32e-160

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


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 455.74  E-value: 5.32e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  125 QKLQKLEEGHSSAVAAHYNELQEVG--LAKRSQSRIFYLRNFNNWIKSILIGEILEKVRQRkTRDITVLDLGCGKGGDLL 202
Cdd:pfam03291   1 EGPFETNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQN-SNKRKVLDLGCGKGGDLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  203 KWRKGRISRLVCADIADISMKQCQQRYedMRCRRDNEHI---FSAEFITADCSKELLVEKFRDPEMYFDVCSCQFACHYS 279
Cdd:pfam03291  80 KWFKGGISQLIGTDIAEVSIEQCRERY--NKLRSGNKSKyykFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  280 FESQVQADTMLRNACGRLNPGGYFIGTTPNSFEL----IRRLEASE--TESFGNEIYTVKFQ-KKGNYPLFGCKYDFNLE 352
Cdd:pfam03291 158 FESEEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEeEPPQVPLFGIKYDYNLE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  353 GVV-DVPEFLVYFPLLTEMAKKYNMKLIYKKTFLEFYEEKIKnNENKMLLKRMQALEQYPAHENSklasekvgdythaae 431
Cdd:pfam03291 238 DAVdDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIK-KEFKKLIKRMSAMESRPSTRNF--------------- 301

                         330       340       350
                  ....*....|....*....|....*....|...
gi 569004395  432 ylKKSQVRLPLGTLSKSEWEATSIYLVFAFEKQ 464
Cdd:pfam03291 302 --FGLQRSAGKGTLGGDEWEAASFYLVFVFEKR 332
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 175-309 4.30e-11

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: 60.03  E-value: 4.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395 175 EILEKVRQRKTRDITVLDLGCGkGGDLLKWRKGRISRLVCADIADISMKQCQQRYEDMRcrrdnehifsAEFITADcske 254
Cdd:COG2227   13 RLAALLARLLPAGGRVLDVGCG-TGRLALALARRGADVTGVDISPEALEIARERAAELN----------VDFVQGD---- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 569004395 255 llVEKFRDPEMYFDVcscqFACHYSFESQVQADTMLRNACGRLNPGGYFIGTTPN 309
Cdd:COG2227   78 --LEDLPLEDGSFDL----VICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 190-301 4.02e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.42  E-value: 4.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  190 VLDLGCGKGGDLLKWRKGRISRLVCADIADISMKQCQQRYEDMRCRrdnehifsAEFITADcskellVEKFRDPEMYFDV 269
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN--------VEFVQGD------AEDLPFPDGSFDL 66

                          90       100       110
                  ....*....|....*....|....*....|..
gi 569004395  270 CSCQFACHYSFESQVQAdtMLRNACGRLNPGG 301
Cdd:pfam13649  67 VVSSGVLHHLPDPDLEA--ALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 175-320 1.58e-09

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: 56.16  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395 175 EILEKVRQRKTRdiTVLDLGCGKGGDLLKWRKgRISRLVCADIADISMKQCQQRYEDMRCRrdnehifsAEFITADCskE 254
Cdd:COG2226   13 ALLAALGLRPGA--RVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEAGLN--------VEFVVGDA--E 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569004395 255 LLveKFRDPemYFDVCSCQFACHYsFESQVQAdtmLRNACGRLNPGGYFI---GTTPNSFELIRRLEAS 320
Cdd:COG2226   80 DL--PFPDG--SFDLVISSFVLHH-LPDPERA---LAEIARVLKPGGRLVvvdFSPPDLAELEELLAEA 140
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 189-304 1.10e-08

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: 52.82  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395 189 TVLDLGCGKGGDLLKWRKGRISRLVCADIADISMKQCQQryedmrcRRDNEHIFSAEFITADCSKELLvekFRDPEmyFD 268
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARK-------AAAALLADNVEVLKGDAEELPP---EADES--FD 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 569004395 269 VCSCQFACHYSFESQVQadtMLRNACGRLNPGGYFI 304
Cdd:cd02440   69 VIISDPPLHHLVEDLAR---FLEEARRLLKPGGVLV 101
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 182-304 7.43e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.53  E-value: 7.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395 182 QRKTRDITVLDLGCGKGGDLLKWRKGRISRLVCADIADISMKQCQQRYEdmrcrrdNEHIFSAEFITADCSKELlvekfR 261
Cdd:COG0500   22 ERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAA-------KAGLGNVEFLVADLAELD-----P 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 569004395 262 DPEMYFD-VCSCQFACHYSFESQVQAdtmLRNACGRLNPGGYFI 304
Cdd:COG0500   90 LPAESFDlVVAFGVLHHLPPEEREAL---LRELARALKPGGVLL 130
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
172-310 4.16e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 44.22  E-value: 4.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395 172 LIGEILEKVRQRKTRdiTVLDLGCGKGGDLLKWRKgRISRLVCADIAdismkqcqqryEDM--RCRRDNEHIfsaEFITA 249
Cdd:COG4976   34 LAEELLARLPPGPFG--RVLDLGCGTGLLGEALRP-RGYRLTGVDLS-----------EEMlaKAREKGVYD---RLLVA 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569004395 250 DcskellVEKFRDPEMYFDVCSCQFACHYsFESQvqaDTMLRNACGRLNPGGYFIGTTPNS 310
Cdd:COG4976   97 D------LADLAEPDGRFDLIVAADVLTY-LGDL---AAVFAGVARALKPGGLFIFSVEDA 147
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
189-304 1.04e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 41.35  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395 189 TVLDLGCGkGGDLLKW--RKGRISRLVCADIADISMKQCQQRYEDMRcrrdnehifsaeFITADcskellVEKFrDPEMY 266
Cdd:COG4106    4 RVLDLGCG-TGRLTALlaERFPGARVTGVDLSPEMLARARARLPNVR------------FVVAD------LRDL-DPPEP 63

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 569004395 267 FDVCSCQFACHYsFESQvqaDTMLRNACGRLNPGGYFI 304
Cdd:COG4106   64 FDLVVSNAALHW-LPDH---AALLARLAAALAPGGVLA 97
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 191-304 1.16e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 41.11  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  191 LDLGCGKGGDLLKWRKgRISRLVCADIADISMKQCQQRYEDMRcrrdnehifsAEFITADcskellVEKFRDPEMYFDVC 270
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKAPREG----------LTFVVGD------AEDLPFPDNSFDLV 63

                          90       100       110
                  ....*....|....*....|....*....|....
gi 569004395  271 SCQFACHYsFESQVQAdtmLRNACGRLNPGGYFI 304
Cdd:pfam08241  64 LSSEVLHH-VEDPERA---LREIARVLKPGGILI 93
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 191-303 3.41e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 39.66  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  191 LDLGCGKGGDLLKWRK-GRISRLVCADIADISMKQCQQRYEDmRCRRDNEHIfsaEFITADCSKELLVekfrdpemYFDV 269
Cdd:pfam08242   1 LEIGCGTGTLLRALLEaLPGLEYTGLDISPAALEAARERLAA-LGLLNAVRV---ELFQLDLGELDPG--------SFDV 68

                          90       100       110
                  ....*....|....*....|....*....|....
gi 569004395  270 CSCQFACHYSFEsqvqADTMLRNACGRLNPGGYF 303
Cdd:pfam08242  69 VVASNVLHHLAD----PRAVLRNIRRLLKPGGVL 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 175-308 4.77e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 37.60  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395 175 EILEKVRQRKTRdiTVLDLGCGKGGDLLKWRKGRISRLVCADIADISMKQCQQRYEDMRCRRdnehifSAEFITADcske 254
Cdd:COG2230   42 LILRKLGLKPGM--RVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLAD------RVEVRLAD---- 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569004395 255 llvekFRD--PEMYFD-VCSCQFACHYSFEsqvQADTMLRNACGRLNPGGYFIGTTP 308
Cdd:COG2230  110 -----YRDlpADGQFDaIVSIGMFEHVGPE---NYPAYFAKVARLLKPGGRLLLHTP 158
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 175-304 5.58e-03

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 37.95  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  175 EILEKVRQRKtRDITVLDLGCGKGG--DLLKWRKGRisRLVCADIADISMKQCQQ-----------RYEDMRCRRDNEHI 241
Cdd:pfam01728  11 EIDEKFGLLK-PGKTVLDLGAAPGGwsQVALQRGAG--KVVGVDLGPMQLWKPRNdpgvtfiqgdiRDPETLDLLEELLG 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569004395  242 FSAEFITADCSKELLVEKFRDPEMYFDVCSCQFAChysfesqvqadtmlrnACGRLNPGGYFI 304
Cdd:pfam01728  88 RKVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEV----------------ALELLRKGGNFV 134
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 184-323 9.42e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 36.63  E-value: 9.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004395  184 KTRDITVLDLGCGKGGDLLKWRK--GRISRLVCADIADISMKQCQQRyedmrcRRDNEHIFsAEFITADCSKELLVEKfR 261
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEelGPNAEVVGIDISEEAIEKAREN------AQKLGFDN-VEFEQGDIEELPELLE-D 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569004395  262 DPemyFDVCSCQFACHYSFESqvqaDTMLRNACGRLNPGGYFIGTTPNSF-ELIRRLEASETE 323
Cdd:pfam13847  73 DK---FDVVISNCVLNHIPDP----DKVLQEILRVLKPGGRLIISDPDSLaELPAHVKEDSTY 128
 
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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