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Conserved domains on  [gi|75028765|sp|Q9XVS1|]
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RecName: Full=mRNA cap guanine-N7 methyltransferase; AltName: Full=mRNA (guanine-N(7))-methyltransferase

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 3-332 2.90e-75

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.).


The actual alignment was detected with superfamily member pfam03291:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 332  Bit Score: 236.56  E-value: 2.90e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765     3 SSEVASHYNKVLQVG--IEGRKESRIFFMRNMNNWVKSQLINDAKQRVNDNGvNNPRVLDLACGKGGDLKKWDIAGAKDV 80
Cdd:pfam03291  11 TDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNS-NKRKVLDLGCGKGGDLEKWFKGGISQL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765    81 VMADVADVSIQQAEERY-KQMFGYKKN-NIFTVQFIVADCTKENLEDRIENKD-PFDLVSCQFALHYSFVDEASARIFLK 157
Cdd:pfam03291  90 IGTDIAEVSIEQCRERYnKLRSGNKSKyYKFDAEFITGDCFVSSLREVFEDPFgKFDIVSCQFAIHYSFESEEKARTMLR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765   158 NAVGMLKPGGVFIGTLPDADRIVWSMR------NGENGQFANEVCKITYENveelAEGKVPLFGAKFHFSLDEQV-NCPE 230
Cdd:pfam03291 170 NVAELLASGGVFIGTTPDSDFISALTIkrlfaiEKDLPSFGNSIYSVKFEE----EPPQVPLFGIKYDYNLEDAVdDVPE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765   231 FLAYFPLVKHLLEELDMELLFVHNFAEAINKWLEP-GRRLLESMTGLETYPNEKlsgksddeyleakakldAFPEDERIK 309
Cdd:pfam03291 246 YIVPFETLVSLAEEYGLELVDKKTFADIFEEEIKKeFKKLIKRMSAMESRPSTR-----------------NFFGLQRSA 308

                         330       340
                  ....*....|....*....|...
gi 75028765   310 TMGTLSKSEWEAICMYLVFGFRK 332
Cdd:pfam03291 309 GKGTLGGDEWEAASFYLVFVFEK 331
 
Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 3-332 2.90e-75

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


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 236.56  E-value: 2.90e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765     3 SSEVASHYNKVLQVG--IEGRKESRIFFMRNMNNWVKSQLINDAKQRVNDNGvNNPRVLDLACGKGGDLKKWDIAGAKDV 80
Cdd:pfam03291  11 TDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNS-NKRKVLDLGCGKGGDLEKWFKGGISQL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765    81 VMADVADVSIQQAEERY-KQMFGYKKN-NIFTVQFIVADCTKENLEDRIENKD-PFDLVSCQFALHYSFVDEASARIFLK 157
Cdd:pfam03291  90 IGTDIAEVSIEQCRERYnKLRSGNKSKyYKFDAEFITGDCFVSSLREVFEDPFgKFDIVSCQFAIHYSFESEEKARTMLR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765   158 NAVGMLKPGGVFIGTLPDADRIVWSMR------NGENGQFANEVCKITYENveelAEGKVPLFGAKFHFSLDEQV-NCPE 230
Cdd:pfam03291 170 NVAELLASGGVFIGTTPDSDFISALTIkrlfaiEKDLPSFGNSIYSVKFEE----EPPQVPLFGIKYDYNLEDAVdDVPE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765   231 FLAYFPLVKHLLEELDMELLFVHNFAEAINKWLEP-GRRLLESMTGLETYPNEKlsgksddeyleakakldAFPEDERIK 309
Cdd:pfam03291 246 YIVPFETLVSLAEEYGLELVDKKTFADIFEEEIKKeFKKLIKRMSAMESRPSTR-----------------NFFGLQRSA 308

                         330       340
                  ....*....|....*....|...
gi 75028765   310 TMGTLSKSEWEAICMYLVFGFRK 332
Cdd:pfam03291 309 GKGTLGGDEWEAASFYLVFVFEK 331
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 57-175 6.18e-13

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: 65.04  E-value: 6.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765  57 RVLDLACGKGGDLKKWDIAGAkDVVMADVADVSIQQAEERYKQMfgykknnifTVQFIVADCTKENLEDRienkdPFDLV 136
Cdd:COG2227  27 RVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAEL---------NVDFVQGDLEDLPLEDG-----SFDLV 91

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 75028765 137 SCQFALHYsfVDEASAriFLKNAVGMLKPGGVFIGTLPD 175
Cdd:COG2227  92 ICSEVLEH--LPDPAA--LLRELARLLKPGGLLLLSTPN 126
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 57-170 6.03e-11

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: 58.98  E-value: 6.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765  57 RVLDLACGKGGDLKKWDIAGAKDVVMADVADVSIQQAEeryKQMFGYKKNNiftVQFIVADCtkenLEDRIENKDPFDLV 136
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELAR---KAAAALLADN---VEVLKGDA----EELPPEADESFDVI 70

                        90       100       110
                ....*....|....*....|....*....|....
gi 75028765 137 SCQFALHYSFVDEASariFLKNAVGMLKPGGVFI 170
Cdd:cd02440  71 ISDPPLHHLVEDLAR---FLEEARRLLKPGGVLV 101
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 54-170 7.89e-06

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 46.51  E-value: 7.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765    54 NNPRVLDLACGKGGDLKKWDIAGAKDVVMA-DVADVSIQQAEERYKQmfgykknnifTVQFIVADCTKENLEDRIenkdp 132
Cdd:TIGR02072  34 IPASVLDIGCGTGYLTRALLKRFPQAEFIAlDISAGMLAQAKTKLSE----------NVQFICGDAEKLPLEDSS----- 98

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 75028765   133 FDLVSCQFALHYsfVDEASAriFLKNAVGMLKPGGVFI 170
Cdd:TIGR02072  99 FDLIVSNLALQW--CDDLSQ--ALSELARVLKPGGLLA 132
PRK08317 PRK08317
hypothetical protein; Provisional
 57-181 1.35e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 39.92  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765   57 RVLDLACGKGGDLKkwDIAGA----KDVVMADVADVSIQQAEERykqmfgyKKNNIFTVQFIVADCTKENLEDrienkDP 132
Cdd:PRK08317  22 RVLDVGCGPGNDAR--ELARRvgpeGRVVGIDRSEAMLALAKER-------AAGLGPNVEFVRGDADGLPFPD-----GS 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 75028765  133 FDLV-SCQFALHYSFVDEASARIflknaVGMLKPGGVFIGTLPDADRIVW 181
Cdd:PRK08317  88 FDAVrSDRVLQHLEDPARALAEI-----ARVLRPGGRVVVLDTDWDTLVW 132
 
Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 3-332 2.90e-75

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


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 236.56  E-value: 2.90e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765     3 SSEVASHYNKVLQVG--IEGRKESRIFFMRNMNNWVKSQLINDAKQRVNDNGvNNPRVLDLACGKGGDLKKWDIAGAKDV 80
Cdd:pfam03291  11 TDIVATHYNERPETGelLKPRQASPIIYLRNFNNWIKSLLISLYASKTFQNS-NKRKVLDLGCGKGGDLEKWFKGGISQL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765    81 VMADVADVSIQQAEERY-KQMFGYKKN-NIFTVQFIVADCTKENLEDRIENKD-PFDLVSCQFALHYSFVDEASARIFLK 157
Cdd:pfam03291  90 IGTDIAEVSIEQCRERYnKLRSGNKSKyYKFDAEFITGDCFVSSLREVFEDPFgKFDIVSCQFAIHYSFESEEKARTMLR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765   158 NAVGMLKPGGVFIGTLPDADRIVWSMR------NGENGQFANEVCKITYENveelAEGKVPLFGAKFHFSLDEQV-NCPE 230
Cdd:pfam03291 170 NVAELLASGGVFIGTTPDSDFISALTIkrlfaiEKDLPSFGNSIYSVKFEE----EPPQVPLFGIKYDYNLEDAVdDVPE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765   231 FLAYFPLVKHLLEELDMELLFVHNFAEAINKWLEP-GRRLLESMTGLETYPNEKlsgksddeyleakakldAFPEDERIK 309
Cdd:pfam03291 246 YIVPFETLVSLAEEYGLELVDKKTFADIFEEEIKKeFKKLIKRMSAMESRPSTR-----------------NFFGLQRSA 308

                         330       340
                  ....*....|....*....|...
gi 75028765   310 TMGTLSKSEWEAICMYLVFGFRK 332
Cdd:pfam03291 309 GKGTLGGDEWEAASFYLVFVFEK 331
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 58-167 1.19e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.13  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765    58 VLDLACGKGGDLKKWDIAGAKDVVMADVADVSIQQAEERYKQmfgykknNIFTVQFIVADCTKENLEDrienkDPFDLVS 137
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAE-------AGLNVEFVQGDAEDLPFPD-----GSFDLVV 68

                          90       100       110
                  ....*....|....*....|....*....|
gi 75028765   138 CQFALHYsfVDEASARIFLKNAVGMLKPGG 167
Cdd:pfam13649  69 SSGVLHH--LPDPDLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 57-175 6.18e-13

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: 65.04  E-value: 6.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765  57 RVLDLACGKGGDLKKWDIAGAkDVVMADVADVSIQQAEERYKQMfgykknnifTVQFIVADCTKENLEDRienkdPFDLV 136
Cdd:COG2227  27 RVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAEL---------NVDFVQGDLEDLPLEDG-----SFDLV 91

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 75028765 137 SCQFALHYsfVDEASAriFLKNAVGMLKPGGVFIGTLPD 175
Cdd:COG2227  92 ICSEVLEH--LPDPAA--LLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 57-170 6.29e-12

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: 62.70  E-value: 6.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765  57 RVLDLACGKGGDLKKWDIAGAKdVVMADVADVSIQQAEERYKQMFgykknniFTVQFIVADCTKENLEDrienkDPFDLV 136
Cdd:COG2226  25 RVLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAEAG-------LNVEFVVGDAEDLPFPD-----GSFDLV 91

                        90       100       110
                ....*....|....*....|....*....|....
gi 75028765 137 SCQFALHYsFVDEASArifLKNAVGMLKPGGVFI 170
Cdd:COG2226  92 ISSFVLHH-LPDPERA---LAEIARVLKPGGRLV 121
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 57-170 6.03e-11

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: 58.98  E-value: 6.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765  57 RVLDLACGKGGDLKKWDIAGAKDVVMADVADVSIQQAEeryKQMFGYKKNNiftVQFIVADCtkenLEDRIENKDPFDLV 136
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELAR---KAAAALLADN---VEVLKGDA----EELPPEADESFDVI 70

                        90       100       110
                ....*....|....*....|....*....|....
gi 75028765 137 SCQFALHYSFVDEASariFLKNAVGMLKPGGVFI 170
Cdd:cd02440  71 ISDPPLHHLVEDLAR---FLEEARRLLKPGGVLV 101
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 57-178 6.31e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 61.09  E-value: 6.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765  57 RVLDLACGKGGDLkkWDIAGA--KDVVMADVADVSIQQAEERYKqmfgykKNNIFTVQFIVADCTKENLEDRienkDPFD 134
Cdd:COG0500  29 RVLDLGCGTGRNL--LALAARfgGRVIGIDLSPEAIALARARAA------KAGLGNVEFLVADLAELDPLPA----ESFD 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 75028765 135 LVSCQFALHysFVDEASARIFLKNAVGMLKPGGVFIGTLPDADR 178
Cdd:COG0500  97 LVVAFGVLH--HLPPEEREALLRELARALKPGGVLLLSASDAAA 138
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 59-170 4.26e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 53.44  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765    59 LDLACGKGGDLKKWDIAGAkDVVMADVADVSIQQAEERYKQMFgykknniftVQFIVADCTKENLEDrienkDPFDLVSC 138
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISPEMLELAREKAPREG---------LTFVVGDAEDLPFPD-----NSFDLVLS 65

                          90       100       110
                  ....*....|....*....|....*....|..
gi 75028765   139 QFALHYsfVDEASAriFLKNAVGMLKPGGVFI 170
Cdd:pfam08241  66 SEVLHH--VEDPER--ALREIARVLKPGGILI 93
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
55-170 1.01e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 49.44  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765  55 NPRVLDLACGKGGD----LKKWDIAgakDVVMADVADVSIQQAEERYKQmfgykknniftVQFIVADctkenLEDrIENK 130
Cdd:COG4106   2 PRRVLDLGCGTGRLtallAERFPGA---RVTGVDLSPEMLARARARLPN-----------VRFVVAD-----LRD-LDPP 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 75028765 131 DPFDLVSCQFALHYsfVDEASAriFLKNAVGMLKPGGVFI 170
Cdd:COG4106  62 EPFDLVVSNAALHW--LPDHAA--LLARLAAALAPGGVLA 97
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 59-169 1.03e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 49.29  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765    59 LDLACGKGGDLKKW-DIAGAKDVVMADVADVSIQQAEERYKQmfgYKKNNIFTVQFIVADCTKENLEdrienkdPFDLVS 137
Cdd:pfam08242   1 LEIGCGTGTLLRALlEALPGLEYTGLDISPAALEAARERLAA---LGLLNAVRVELFQLDLGELDPG-------SFDVVV 70

                          90       100       110
                  ....*....|....*....|....*....|..
gi 75028765   138 CQFALHYSFVdeasARIFLKNAVGMLKPGGVF 169
Cdd:pfam08242  71 ASNVLHHLAD----PRAVLRNIRRLLKPGGVL 98
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 54-170 7.89e-06

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 46.51  E-value: 7.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765    54 NNPRVLDLACGKGGDLKKWDIAGAKDVVMA-DVADVSIQQAEERYKQmfgykknnifTVQFIVADCTKENLEDRIenkdp 132
Cdd:TIGR02072  34 IPASVLDIGCGTGYLTRALLKRFPQAEFIAlDISAGMLAQAKTKLSE----------NVQFICGDAEKLPLEDSS----- 98

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 75028765   133 FDLVSCQFALHYsfVDEASAriFLKNAVGMLKPGGVFI 170
Cdd:TIGR02072  99 FDLIVSNLALQW--CDDLSQ--ALSELARVLKPGGLLA 132
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
57-177 8.70e-06

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 45.76  E-value: 8.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765  57 RVLDLACGKGGDLKKWDIAGaKDVVMADVADVSIQQAEERykqmFGYkknniftVQFIVADCTKENLEDRienkdPFDLV 136
Cdd:COG4976  49 RVLDLGCGTGLLGEALRPRG-YRLTGVDLSEEMLAKAREK----GVY-------DRLLVADLADLAEPDG-----RFDLI 111

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 75028765 137 SCQFALHYsfvDEASARIFlKNAVGMLKPGGVFIGTLPDAD 177
Cdd:COG4976 112 VAADVLTY---LGDLAAVF-AGVARALKPGGLFIFSVEDAD 148
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 57-170 1.93e-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: 1.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765  57 RVLDLACGKGGDLKKWdiagAK----DVVMADVADVSIQQAEERYKQMfGYKKNniftVQFIVADctkenLEDrIENKDP 132
Cdd:COG2230  54 RVLDIGCGWGGLALYL----ARrygvRVTGVTLSPEQLEYARERAAEA-GLADR----VEVRLAD-----YRD-LPADGQ 118

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 75028765 133 FDLVSCQFALHYsfVDEASARIFLKNAVGMLKPGGVFI 170
Cdd:COG2230 119 FDAIVSIGMFEH--VGPENYPAYFAKVARLLKPGGRLL 154
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 57-178 6.01e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.79  E-value: 6.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765    57 RVLDLACGKGGDLKKW--DIAGAKDVVMADVADVSIQQAEERYKQMfGYKKnniftVQFIVADCTKenlEDRIENKDPFD 134
Cdd:pfam13847   6 RVLDLGCGTGHLSFELaeELGPNAEVVGIDISEEAIEKARENAQKL-GFDN-----VEFEQGDIEE---LPELLEDDKFD 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 75028765   135 LVSCQFALHYSFVDEASARIFLKNavgmLKPGGVFIGTLPDADR 178
Cdd:pfam13847  77 VVISNCVLNHIPDPDKVLQEILRV----LKPGGRLIISDPDSLA 116
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 43-208 9.26e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 42.42  E-value: 9.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765    43 DAKQRVNDNGVNNPRVLDLACGKGGDLKKWDIAGAkDVVMADVADVSIQqaeerykqmfGYKKNNIFTVqfivadctkEN 122
Cdd:pfam13489  11 DLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGF-SVTGVDPSPIAIE----------RALLNVRFDQ---------FD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765   123 LEDRIENKDPFDLVSCQFALHySFVDEASArifLKNAVGMLKPGGVFIGTLPDADRIVWsMRNGENGQFANEVCKITYEN 202
Cdd:pfam13489  71 EQEAAVPAGKFDVIVAREVLE-HVPDPPAL---LRQIAALLKPGGLLLLSTPLASDEAD-RLLLEWPYLRPRNGHISLFS 145


                  ....*.
gi 75028765   203 VEELAE 208
Cdd:pfam13489 146 ARSLKR 151
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 57-210 1.21e-03

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 39.40  E-value: 1.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765  57 RVLDLACGKG--GdlkkwdIAGAK-----DVVMADVADVSIQQAEErykqmfGYKKNNIFTVQFIVADCTkENLEDrien 129
Cdd:COG2813  52 RVLDLGCGYGviG------LALAKrnpeaRVTLVDVNARAVELARA------NAAANGLENVEVLWSDGL-SGVPD---- 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765 130 kDPFDLVSC------QFALHYSFvdeasARIFLKNAVGMLKPGGVFigtlpdadRIVWSmrngeNGQFANEVCKITYENV 203
Cdd:COG2813 115 -GSFDLILSnppfhaGRAVDKEV-----AHALIADAARHLRPGGEL--------WLVAN-----RHLPYERKLEELFGNV 175


                ....*..
gi 75028765 204 EELAEGK 210
Cdd:COG2813 176 EVLARNK 182
PRK08317 PRK08317
hypothetical protein; Provisional
 57-181 1.35e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 39.92  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765   57 RVLDLACGKGGDLKkwDIAGA----KDVVMADVADVSIQQAEERykqmfgyKKNNIFTVQFIVADCTKENLEDrienkDP 132
Cdd:PRK08317  22 RVLDVGCGPGNDAR--ELARRvgpeGRVVGIDRSEAMLALAKER-------AAGLGPNVEFVRGDADGLPFPD-----GS 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 75028765  133 FDLV-SCQFALHYSFVDEASARIflknaVGMLKPGGVFIGTLPDADRIVW 181
Cdd:PRK08317  88 FDAVrSDRVLQHLEDPARALAEI-----ARVLRPGGRVVVLDTDWDTLVW 132
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
38-136 3.52e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 38.35  E-value: 3.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75028765  38 SQLINDAKQRvndNGVNNPRVLDLACGKG----GDLkkwdIAGAKDVVMADVADVSIQQAEERYKQMFGykknnifTVQF 113
Cdd:COG2263  32 AELLHLAYLR---GDIEGKTVLDLGCGTGmlaiGAA----LLGAKKVVGVDIDPEALEIARENAERLGV-------RVDF 97

                        90       100
                ....*....|....*....|...
gi 75028765 114 IVADCTkenledRIENKDPFDLV 136
Cdd:COG2263  98 IRADVT------RIPLGGSVDTV 114
 
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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