NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564393917|ref|XP_006254956|]
View 

mRNA cap guanine-N7 methyltransferase isoform X1 [Rattus norvegicus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 124-460 1.57e-156

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


:

Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 446.49  E-value: 1.57e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  124 QKLEEGHSSAVAAHYNELQEVG--LVKRSQSRIFYLRNFNNWIKSILIGEILEKVRQRKNrDITVLDLGCGKGGDLLKWR 201
Cdd:pfam03291   4 FETNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNSN-KRKVLDLGCGKGGDLEKWF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  202 KGRISRLVCADIADISMKQCQQRYedMKCRRDNE---YIFSAEFITADCSKELLVEKFHDPEMYFDICSCQFACHYSFES 278
Cdd:pfam03291  83 KGGISQLIGTDIAEVSIEQCRERY--NKLRSGNKskyYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFES 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  279 LEQADMMLRNACGRLNPGGYFIGTTPNSFEL----IRRLEASE--TESFGNEIYTVKFQ-KKGNYPLFGCKYDFNLEGVV 351
Cdd:pfam03291 161 EEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEeEPPQVPLFGIKYDYNLEDAV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  352 -DVPEFLVYFPLLTEMAKKYNMKLIYKKTFLEFYEEKIKnNENKMLLKRMQALESYPANENSklasekagdyahaaeymK 430
Cdd:pfam03291 241 dDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIK-KEFKKLIKRMSAMESRPSTRNF-----------------F 302

                         330       340       350
                  ....*....|....*....|....*....|
gi 564393917  431 NSQVRLPLGTLSKSEWEATSIYLVFAFEKQ 460
Cdd:pfam03291 303 GLQRSAGKGTLGGDEWEAASFYLVFVFEKR 332
 
Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 124-460 1.57e-156

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


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 446.49  E-value: 1.57e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  124 QKLEEGHSSAVAAHYNELQEVG--LVKRSQSRIFYLRNFNNWIKSILIGEILEKVRQRKNrDITVLDLGCGKGGDLLKWR 201
Cdd:pfam03291   4 FETNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNSN-KRKVLDLGCGKGGDLEKWF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  202 KGRISRLVCADIADISMKQCQQRYedMKCRRDNE---YIFSAEFITADCSKELLVEKFHDPEMYFDICSCQFACHYSFES 278
Cdd:pfam03291  83 KGGISQLIGTDIAEVSIEQCRERY--NKLRSGNKskyYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFES 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  279 LEQADMMLRNACGRLNPGGYFIGTTPNSFEL----IRRLEASE--TESFGNEIYTVKFQ-KKGNYPLFGCKYDFNLEGVV 351
Cdd:pfam03291 161 EEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEeEPPQVPLFGIKYDYNLEDAV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  352 -DVPEFLVYFPLLTEMAKKYNMKLIYKKTFLEFYEEKIKnNENKMLLKRMQALESYPANENSklasekagdyahaaeymK 430
Cdd:pfam03291 241 dDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIK-KEFKKLIKRMSAMESRPSTRNF-----------------F 302

                         330       340       350
                  ....*....|....*....|....*....|
gi 564393917  431 NSQVRLPLGTLSKSEWEATSIYLVFAFEKQ 460
Cdd:pfam03291 303 GLQRSAGKGTLGGDEWEAASFYLVFVFEKR 332
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 171-305 6.01e-12

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: 62.73  E-value: 6.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917 171 EILEKVRQRKNRDITVLDLGCGkGGDLLKWRKGRISRLVCADIADISMKQCQQRYEDMKcrrdneyifsAEFITADcske 250
Cdd:COG2227   13 RLAALLARLLPAGGRVLDVGCG-TGRLALALARRGADVTGVDISPEALEIARERAAELN----------VDFVQGD---- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564393917 251 llVEKFHDPEMYFDIcscqFACHYSFESLEQADMMLRNACGRLNPGGYFIGTTPN 305
Cdd:COG2227   78 --LEDLPLEDGSFDL----VICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 185-300 7.33e-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: 50.51  E-value: 7.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917 185 TVLDLGCGKGGDLLKWRKGRISRLVCADIADISMKQCQQryedmkcRRDNEYIFSAEFITADCSKELLvekFHDPEmyFD 264
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARK-------AAAALLADNVEVLKGDAEELPP---EADES--FD 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 564393917 265 ICSCQFACHYSFESLEQadmMLRNACGRLNPGGYFI 300
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.
 124-460 1.57e-156

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


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 446.49  E-value: 1.57e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  124 QKLEEGHSSAVAAHYNELQEVG--LVKRSQSRIFYLRNFNNWIKSILIGEILEKVRQRKNrDITVLDLGCGKGGDLLKWR 201
Cdd:pfam03291   4 FETNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNSN-KRKVLDLGCGKGGDLEKWF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  202 KGRISRLVCADIADISMKQCQQRYedMKCRRDNE---YIFSAEFITADCSKELLVEKFHDPEMYFDICSCQFACHYSFES 278
Cdd:pfam03291  83 KGGISQLIGTDIAEVSIEQCRERY--NKLRSGNKskyYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFES 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  279 LEQADMMLRNACGRLNPGGYFIGTTPNSFEL----IRRLEASE--TESFGNEIYTVKFQ-KKGNYPLFGCKYDFNLEGVV 351
Cdd:pfam03291 161 EEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEeEPPQVPLFGIKYDYNLEDAV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  352 -DVPEFLVYFPLLTEMAKKYNMKLIYKKTFLEFYEEKIKnNENKMLLKRMQALESYPANENSklasekagdyahaaeymK 430
Cdd:pfam03291 241 dDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIK-KEFKKLIKRMSAMESRPSTRNF-----------------F 302

                         330       340       350
                  ....*....|....*....|....*....|
gi 564393917  431 NSQVRLPLGTLSKSEWEATSIYLVFAFEKQ 460
Cdd:pfam03291 303 GLQRSAGKGTLGGDEWEAASFYLVFVFEKR 332
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 171-305 6.01e-12

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: 62.73  E-value: 6.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917 171 EILEKVRQRKNRDITVLDLGCGkGGDLLKWRKGRISRLVCADIADISMKQCQQRYEDMKcrrdneyifsAEFITADcske 250
Cdd:COG2227   13 RLAALLARLLPAGGRVLDVGCG-TGRLALALARRGADVTGVDISPEALEIARERAAELN----------VDFVQGD---- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564393917 251 llVEKFHDPEMYFDIcscqFACHYSFESLEQADMMLRNACGRLNPGGYFIGTTPN 305
Cdd:COG2227   78 --LEDLPLEDGSFDL----VICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 186-297 2.05e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.19  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  186 VLDLGCGKGGDLLKWRKGRISRLVCADIADISMKQCQQRYEDMKCRrdneyifsAEFITADcskellVEKFHDPEMYFDI 265
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN--------VEFVQGD------AEDLPFPDGSFDL 66

                          90       100       110
                  ....*....|....*....|....*....|..
gi 564393917  266 CSCQFACHYSfeSLEQADMMLRNACGRLNPGG 297
Cdd:pfam13649  67 VVSSGVLHHL--PDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 171-316 4.03e-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: 57.70  E-value: 4.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917 171 EILEKVRQRKNRdiTVLDLGCGKGGDLLKWRKgRISRLVCADIADISMKQCQQRYEDMKCRrdneyifsAEFITADcske 250
Cdd:COG2226   13 ALLAALGLRPGA--RVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEAGLN--------VEFVVGD---- 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564393917 251 llVEKFHDPEMYFDICSCQFACHYsFESLEQAdmmLRNACGRLNPGGYFI---GTTPNSFELIRRLEAS 316
Cdd:COG2226   78 --AEDLPFPDGSFDLVISSFVLHH-LPDPERA---LAEIARVLKPGGRLVvvdFSPPDLAELEELLAEA 140
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 185-300 7.33e-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: 50.51  E-value: 7.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917 185 TVLDLGCGKGGDLLKWRKGRISRLVCADIADISMKQCQQryedmkcRRDNEYIFSAEFITADCSKELLvekFHDPEmyFD 264
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARK-------AAAALLADNVEVLKGDAEELPP---EADES--FD 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 564393917 265 ICSCQFACHYSFESLEQadmMLRNACGRLNPGGYFI 300
Cdd:cd02440   69 VIISDPPLHHLVEDLAR---FLEEARRLLKPGGVLV 101
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 178-300 2.80e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 50.69  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917 178 QRKNRDITVLDLGCGKGGDLLKWRKGRISRLVCADIADISMKQCQQRYEDMKCRRdneyifsAEFITADCSKELlvekfH 257
Cdd:COG0500   22 ERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGN-------VEFLVADLAELD-----P 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 564393917 258 DPEMYFD-ICSCQFACHYSFESLEQAdmmLRNACGRLNPGGYFI 300
Cdd:COG0500   90 LPAESFDlVVAFGVLHHLPPEEREAL---LRELARALKPGGVLL 130
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
168-306 1.57e-06

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 48.46  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917 168 LIGEILEKVRQRKNRdiTVLDLGCGKGGDLLKWRKgRISRLVCADIAdismkqcqqryEDM--KCRRDNEYIfsaEFITA 245
Cdd:COG4976   34 LAEELLARLPPGPFG--RVLDLGCGTGLLGEALRP-RGYRLTGVDLS-----------EEMlaKAREKGVYD---RLLVA 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564393917 246 DcskellVEKFHDPEMYFDICSCQFACHYsFESLEQadmMLRNACGRLNPGGYFIGTTPNS 306
Cdd:COG4976   97 D------LADLAEPDGRFDLIVAADVLTY-LGDLAA---VFAGVARALKPGGLFIFSVEDA 147
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 187-300 1.30e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 43.81  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  187 LDLGCGKGGDLLKWRKgRISRLVCADIADISMKQCQQRYEDMKcrrdneyifsAEFITADcskellVEKFHDPEMYFDIC 266
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKAPREG----------LTFVVGD------AEDLPFPDNSFDLV 63

                          90       100       110
                  ....*....|....*....|....*....|....
gi 564393917  267 SCQFACHYsFESLEQAdmmLRNACGRLNPGGYFI 300
Cdd:pfam08241  64 LSSEVLHH-VEDPERA---LREIARVLKPGGILI 93
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
185-300 7.06e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 41.73  E-value: 7.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917 185 TVLDLGCGkGGDLLKW--RKGRISRLVCADIADISMKQCQQRYEDmkcrrdneyifsAEFITADcskellVEKFhDPEMY 262
Cdd:COG4106    4 RVLDLGCG-TGRLTALlaERFPGARVTGVDLSPEMLARARARLPN------------VRFVVAD------LRDL-DPPEP 63

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 564393917 263 FDICSCQFACHYsfesLEQADMMLRNACGRLNPGGYFI 300
Cdd:COG4106   64 FDLVVSNAALHW----LPDHAALLARLAAALAPGGVLA 97
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 180-319 6.02e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.09  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  180 KNRDITVLDLGCGKGGDLLKWRK--GRISRLVCADIADISMKQCQQRyedmkcRRDNEYIFsAEFITADCskELLVEKFH 257
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEelGPNAEVVGIDISEEAIEKAREN------AQKLGFDN-VEFEQGDI--EELPELLE 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564393917  258 DPEmyFDICSCQFACHYSFESleqaDMMLRNACGRLNPGGYFIGTTPNSF-ELIRRLEASETE 319
Cdd:pfam13847  72 DDK--FDVVISNCVLNHIPDP----DKVLQEILRVLKPGGRLIISDPDSLaELPAHVKEDSTY 128
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 187-299 2.20e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 37.35  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  187 LDLGCGKGGDLLKWRK-GRISRLVCADIADISMKQCQQRYEDmKCRRDNEYIfsaEFITADCSKELLVekfhdpemYFDI 265
Cdd:pfam08242   1 LEIGCGTGTLLRALLEaLPGLEYTGLDISPAALEAARERLAA-LGLLNAVRV---ELFQLDLGELDPG--------SFDV 68

                          90       100       110
                  ....*....|....*....|....*....|....
gi 564393917  266 CSCQFACHYsfesLEQADMMLRNACGRLNPGGYF 299
Cdd:pfam08242  69 VVASNVLHH----LADPRAVLRNIRRLLKPGGVL 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 171-304 6.04e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 37.22  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917 171 EILEKVRQRKNRdiTVLDLGCGKGGDLLKWRKGRISRLVCADIADISMKQCQQRYEDMKCRRdneyifSAEFITADCSKe 250
Cdd:COG2230   42 LILRKLGLKPGM--RVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLAD------RVEVRLADYRD- 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564393917 251 llvekfHDPEMYFD-ICSCQFACHYSFESLEQadmMLRNACGRLNPGGYFIGTTP 304
Cdd:COG2230  113 ------LPADGQFDaIVSIGMFEHVGPENYPA---YFAKVARLLKPGGRLLLHTP 158
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 171-300 8.96e-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: 37.18  E-value: 8.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393917  171 EILEKVRQRKnRDITVLDLGCGKGG--DLLKWRKGRisRLVCADIADISMKQCQQ-----------RYEDMKCRRDNEYI 237
Cdd:pfam01728  11 EIDEKFGLLK-PGKTVLDLGAAPGGwsQVALQRGAG--KVVGVDLGPMQLWKPRNdpgvtfiqgdiRDPETLDLLEELLG 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564393917  238 FSAEFITADCSKELLVEKFHDPEMYFDICSCQFAChysfesleqadmmlrnACGRLNPGGYFI 300
Cdd:pfam01728  88 RKVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEV----------------ALELLRKGGNFV 134
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH