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Conserved domains on  [gi|767997909|ref|XP_011524052|]
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mRNA cap guanine-N7 methyltransferase isoform X1 [Homo sapiens]

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.
 136-468 3.81e-141

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


:

Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 409.51  E-value: 3.81e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  136 EKQKNLEEGHSSTVAAHYNELQEVG--LEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKkRDITVLDLGCGKGGDLL 213
Cdd:pfam03291   1 EGPFETNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNS-NKRKVLDLGCGKGGDLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  214 KWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDS-EYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFE 292
Cdd:pfam03291  80 KWFKGGISQLIGTDIAEVSIEQCRERYNKLRSGNKSkYYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  293 SYEQADMMLRNACERLSPGGYFIGTTPNSFEL----IRRLEASE--TESFGNEIYTVKFQ-KKGDYPLFGCKYDFNLEGV 365
Cdd:pfam03291 160 SEEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEeEPPQVPLFGIKYDYNLEDA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  366 V-DVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKnNENKMLLKRMQALEPYPanessklvsekvddyehAAKYM 444
Cdd:pfam03291 240 VdDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIK-KEFKKLIKRMSAMESRP-----------------STRNF 301

                         330       340
                  ....*....|....*....|....
gi 767997909  445 KNSQVRLPLGTLSKSEWEATRSFL 468
Cdd:pfam03291 302 FGLQRSAGKGTLGGDEWEAASFYL 325
 
Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 136-468 3.81e-141

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


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 409.51  E-value: 3.81e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  136 EKQKNLEEGHSSTVAAHYNELQEVG--LEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKkRDITVLDLGCGKGGDLL 213
Cdd:pfam03291   1 EGPFETNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNS-NKRKVLDLGCGKGGDLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  214 KWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDS-EYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFE 292
Cdd:pfam03291  80 KWFKGGISQLIGTDIAEVSIEQCRERYNKLRSGNKSkYYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  293 SYEQADMMLRNACERLSPGGYFIGTTPNSFEL----IRRLEASE--TESFGNEIYTVKFQ-KKGDYPLFGCKYDFNLEGV 365
Cdd:pfam03291 160 SEEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEeEPPQVPLFGIKYDYNLEDA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  366 V-DVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKnNENKMLLKRMQALEPYPanessklvsekvddyehAAKYM 444
Cdd:pfam03291 240 VdDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIK-KEFKKLIKRMSAMESRP-----------------STRNF 301

                         330       340
                  ....*....|....*....|....
gi 767997909  445 KNSQVRLPLGTLSKSEWEATRSFL 468
Cdd:pfam03291 302 FGLQRSAGKGTLGGDEWEAASFYL 325
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 184-320 2.37e-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: 63.88  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909 184 IGEFLEKVRQKKKRditVLDLGCGkGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKnrrdseyifsAEFITADss 263
Cdd:COG2227   14 LAALLARLLPAGGR---VLDVGCG-TGRLALALARRGADVTGVDISPEALEIARERAAELN----------VDFVQGD-- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767997909 264 kellIDKFRDPQMCFDIcscqFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPN 320
Cdd:COG2227   78 ----LEDLPLEDGSFDL----VICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 200-315 3.52e-10

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: 57.05  E-value: 3.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909 200 TVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRyedmKNRRDSEYIfsaEFITADSSKellIDKFRDPQmcFD 279
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKA----AAALLADNV---EVLKGDAEE---LPPEADES--FD 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767997909 280 ICSCQFVCHYSFESYEQadmMLRNACERLSPGGYFI 315
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.
 136-468 3.81e-141

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


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 409.51  E-value: 3.81e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  136 EKQKNLEEGHSSTVAAHYNELQEVG--LEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKkRDITVLDLGCGKGGDLL 213
Cdd:pfam03291   1 EGPFETNSNITDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNS-NKRKVLDLGCGKGGDLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  214 KWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDS-EYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFE 292
Cdd:pfam03291  80 KWFKGGISQLIGTDIAEVSIEQCRERYNKLRSGNKSkYYKFDAEFITGDCFVSSLREVFEDPFGKFDIVSCQFAIHYSFE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  293 SYEQADMMLRNACERLSPGGYFIGTTPNSFEL----IRRLEASE--TESFGNEIYTVKFQ-KKGDYPLFGCKYDFNLEGV 365
Cdd:pfam03291 160 SEEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEeEPPQVPLFGIKYDYNLEDA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  366 V-DVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKnNENKMLLKRMQALEPYPanessklvsekvddyehAAKYM 444
Cdd:pfam03291 240 VdDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIK-KEFKKLIKRMSAMESRP-----------------STRNF 301

                         330       340
                  ....*....|....*....|....
gi 767997909  445 KNSQVRLPLGTLSKSEWEATRSFL 468
Cdd:pfam03291 302 FGLQRSAGKGTLGGDEWEAASFYL 325
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 184-320 2.37e-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: 63.88  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909 184 IGEFLEKVRQKKKRditVLDLGCGkGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKnrrdseyifsAEFITADss 263
Cdd:COG2227   14 LAALLARLLPAGGR---VLDVGCG-TGRLALALARRGADVTGVDISPEALEIARERAAELN----------VDFVQGD-- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767997909 264 kellIDKFRDPQMCFDIcscqFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPN 320
Cdd:COG2227   78 ----LEDLPLEDGSFDL----VICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 200-315 3.52e-10

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: 57.05  E-value: 3.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909 200 TVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRyedmKNRRDSEYIfsaEFITADSSKellIDKFRDPQmcFD 279
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKA----AAALLADNV---EVLKGDAEE---LPPEADES--FD 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767997909 280 ICSCQFVCHYSFESYEQadmMLRNACERLSPGGYFI 315
Cdd:cd02440   69 VIISDPPLHHLVEDLAR---FLEEARRLLKPGGVLV 101
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 201-312 5.02e-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: 5.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  201 VLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRrdseyifsAEFITADsskellIDKFRDPQMCFDI 280
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN--------VEFVQGD------AEDLPFPDGSFDL 66

                          90       100       110
                  ....*....|....*....|....*....|..
gi 767997909  281 CSCQFVCHYSfeSYEQADMMLRNACERLSPGG 312
Cdd:pfam13649  67 VVSSGVLHHL--PDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 196-331 1.37e-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: 56.54  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909 196 KRDITVLDLGCGKGGDLLKWKKgRINKLVCTDIADVSVKQCQQRYEDMKNRrdseyifsAEFITADSskELLidKFRDPQ 275
Cdd:COG2226   21 RPGARVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEAGLN--------VEFVVGDA--EDL--PFPDGS 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767997909 276 mcFDICSCQFVCHYsFESYEQAdmmLRNACERLSPGGYFI---GTTPNSFELIRRLEAS 331
Cdd:COG2226   88 --FDLVISSFVLHH-LPDPERA---LAEIARVLKPGGRLVvvdFSPPDLAELEELLAEA 140
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 193-315 1.03e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 46.45  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909 193 QKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKnrrdseyIFSAEFITADSSKELLIdkfr 272
Cdd:COG0500   22 ERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAG-------LGNVEFLVADLAELDPL---- 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767997909 273 dPQMCFD-ICSCQFVCHYSFESYEQAdmmLRNACERLSPGGYFI 315
Cdd:COG0500   91 -PAESFDlVVAFGVLHHLPPEEREAL---LRELARALKPGGVLL 130
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 202-315 2.40e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 43.04  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  202 LDLGCGKGGdLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNrrdseyifsaEFITADSSKELLIDKfrdpqmCFDIC 281
Cdd:pfam08241   1 LDVGCGTGL-LTELLARLGARVTGVDISPEMLELAREKAPREGL----------TFVVGDAEDLPFPDN------SFDLV 63

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767997909  282 SCQFVCHYsFESYEQAdmmLRNACERLSPGGYFI 315
Cdd:pfam08241  64 LSSEVLHH-VEDPERA---LREIARVLKPGGILI 93
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 202-314 9.23e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 41.58  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  202 LDLGCGKGGDLLKWKKGRIN-KLVCTDIADVSVKQCQQRYEDMKNRRDSEYifsaEFITADSSKELLIDkfrdpqmcFDI 280
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGlEYTGLDISPAALEAARERLAALGLLNAVRV----ELFQLDLGELDPGS--------FDV 68

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767997909  281 CSCQFVCHYSfesyEQADMMLRNACERLSPGGYF 314
Cdd:pfam08242  69 VVASNVLHHL----ADPRAVLRNIRRLLKPGGVL 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
183-321 1.19e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 43.06  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909 183 LIGEFLEKVRQKKKRdiTVLDLGCGKG--GDLLKWKKGRInklVCTDIADVSVKQCQQRyedmknrrdSEYIfsaEFITA 260
Cdd:COG4976   34 LAEELLARLPPGPFG--RVLDLGCGTGllGEALRPRGYRL---TGVDLSEEMLAKAREK---------GVYD---RLLVA 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767997909 261 DsskellIDKFRDPQMCFDIcscqFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNS 321
Cdd:COG4976   97 D------LADLAEPDGRFDL----IVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDA 147
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 195-353 1.30e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.40  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  195 KKRDITVLDLGCGKGGDLLKW--KKGRINKLVCTDIADVSVKQCQQryedmkNRRDSEYIFsAEFITADSSKELLIDKFR 272
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELaeELGPNAEVVGIDISEEAIEKARE------NAQKLGFDN-VEFEQGDIEELPELLEDD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909  273 dpqmCFDICSCQFVCHYSFESyeqaDMMLRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYP 352
Cdd:pfam13847  74 ----KFDVVISNCVLNHIPDP----DKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAILKKKLYEL 145


                  .
gi 767997909  353 L 353
Cdd:pfam13847 146 L 146
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 200-319 4.39e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 41.07  E-value: 4.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909 200 TVLDLGCGKGGDLLKW-KKGRInKLVCTDIADVSVKQCQQRYEDMKNRRdseyifSAEFITADsskellidkFRD--PQM 276
Cdd:COG2230   54 RVLDIGCGWGGLALYLaRRYGV-RVTGVTLSPEQLEYARERAAEAGLAD------RVEVRLAD---------YRDlpADG 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767997909 277 CFD-ICSCQFVCHYSFESYEQadmMLRNACERLSPGGYFIGTTP 319
Cdd:COG2230  118 QFDaIVSIGMFEHVGPENYPA---YFAKVARLLKPGGRLLLHTP 158
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
200-315 8.54e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 38.65  E-value: 8.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767997909 200 TVLDLGCGKGGDLLK----WKKGRInklVCTDIADVSVKQCQQRYEDmknrrdseyifsAEFITADsskellidkFRD-- 273
Cdd:COG4106    4 RVLDLGCGTGRLTALlaerFPGARV---TGVDLSPEMLARARARLPN------------VRFVVAD---------LRDld 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767997909 274 PQMCFDICSCQFVCHYSfesyEQADMMLRNACERLSPGGYFI 315
Cdd:COG4106   60 PPEPFDLVVSNAALHWL----PDHAALLARLAAALAPGGVLA 97
 
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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