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Conserved domains on  [gi|149292712|gb|EDM42786|]
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rRNA (guanine-N1-)-methyltransferase [Yersinia pestis CA88-4125]

Protein Classification

23S rRNA (guanine(745)-N(1))-methyltransferase( domain architecture ID 10793530)

23S rRNA (guanine(745)-N(1))-methyltransferase specifically methylates the guanosine in position 745 of 23S rRNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 1-271 0e+00

23S rRNA methyltransferase A; Provisional


:

Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 529.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712   1 MSYQCPLCHQALQLSQQQWCCSNNHQFDCAKEGYVNLMPVQHKGSKQPGDSPEMMQARRAFLDAGYYQPLQQRVSEILDE 80
Cdd:PRK11088   1 MSYQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPLRDAVANLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  81 ALPLDATRLLDIGCGEGYYTAAVADRLNKLRQMAIFGLDVAKVAVRYGAKRYHQVNFCVASSHRLPFANGALDAVLRIYA 160
Cdd:PRK11088  81 RLDEKATALLDIGCGEGYYTHALADALPEITTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIIRIYA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712 161 PCKAVELARTVKPGGIVVTVAPGPRHLYQLKALIYAQVQLHDDTEEHLDGFELIRRETLAYDMKLTGEQGFNLLQMTPFA 240
Cdd:PRK11088 161 PCKAEELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQLEGFELQHSERLAYPMRLTGSEAVALLQMTPFA 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 149292712 241 WRASVDTGQKLAAQPSFSCETDFVISLHRRK 271
Cdd:PRK11088 241 WKATPEVKQQLAAKGVFSCETDFNIRVYRRS 271
 
Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 1-271 0e+00

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 529.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712   1 MSYQCPLCHQALQLSQQQWCCSNNHQFDCAKEGYVNLMPVQHKGSKQPGDSPEMMQARRAFLDAGYYQPLQQRVSEILDE 80
Cdd:PRK11088   1 MSYQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPLRDAVANLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  81 ALPLDATRLLDIGCGEGYYTAAVADRLNKLRQMAIFGLDVAKVAVRYGAKRYHQVNFCVASSHRLPFANGALDAVLRIYA 160
Cdd:PRK11088  81 RLDEKATALLDIGCGEGYYTHALADALPEITTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIIRIYA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712 161 PCKAVELARTVKPGGIVVTVAPGPRHLYQLKALIYAQVQLHDDTEEHLDGFELIRRETLAYDMKLTGEQGFNLLQMTPFA 240
Cdd:PRK11088 161 PCKAEELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQLEGFELQHSERLAYPMRLTGSEAVALLQMTPFA 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 149292712 241 WRASVDTGQKLAAQPSFSCETDFVISLHRRK 271
Cdd:PRK11088 241 WKATPEVKQQLAAKGVFSCETDFNIRVYRRS 271
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 64-194 8.53e-19

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: 80.42  E-value: 8.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  64 AGYYQPLQqrvsEILDEALPLDATRLLDIGCGEGYYTAAVADRLNKlrqmaIFGLDVAKVAVRYGAKRYH----QVNFCV 139
Cdd:COG2226    5 AARYDGRE----ALLAALGLRPGARVLDLGCGTGRLALALAERGAR-----VTGVDISPEMLELARERAAeaglNVEFVV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149292712 140 ASSHRLPFANGALDAVLRIYA------PCKAV-ELARTVKPGGIVVTVAPGPRHLYQLKALI 194
Cdd:COG2226   76 GDAEDLPFPDGSFDLVISSFVlhhlpdPERALaEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 90-175 1.99e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.81  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712   90 LDIGCGEGYYTAAVADRLNKlrqmAIFGLDVAKVAVRYGAKRY----HQVNFCVASSHRLPFANGALDAV--------LR 157
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGA----RVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFPDGSFDLVvssgvlhhLP 77

                          90
                  ....*....|....*....
gi 149292712  158 IYAPCKAV-ELARTVKPGG 175
Cdd:pfam13649  78 DPDLEAALrEIARVLKPGG 96
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 67-193 3.46e-09

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: 55.76  E-value: 3.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712   67 YQPLQQRVS----EILDEALPLDATRLLDIGCGEGYYTAAVADRLNklrQMAIFGLDVAKVAVRYGAKRY-HQVNFCVAS 141
Cdd:TIGR02072  12 HAKIQREMAkrllALLKEKGIFIPASVLDIGCGTGYLTRALLKRFP---QAEFIALDISAGMLAQAKTKLsENVQFICGD 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 149292712  142 SHRLPFANGALD-----AVLRIYAPCKAV--ELARTVKPGGIVVTVAPGPRHLYQLKAL 193
Cdd:TIGR02072  89 AEKLPLEDSSFDlivsnLALQWCDDLSQAlsELARVLKPGGLLAFSTFGPGTLHELRQS 147
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 88-180 2.29e-07

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: 48.20  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  88 RLLDIGCGEGYYTAAVADRLNKLrqmaIFGLDVAKVAVRYG-----AKRYHQVNFCVASSHRLPF-ANGALDAVLRIYAP 161
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGAR----VTGVDISPVALELArkaaaALLADNVEVLKGDAEELPPeADESFDVIISDPPL 76

                         90       100
                 ....*....|....*....|....*..
gi 149292712 162 CKAV--------ELARTVKPGGIVVTV 180
Cdd:cd02440   77 HHLVedlarfleEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 1-271 0e+00

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 529.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712   1 MSYQCPLCHQALQLSQQQWCCSNNHQFDCAKEGYVNLMPVQHKGSKQPGDSPEMMQARRAFLDAGYYQPLQQRVSEILDE 80
Cdd:PRK11088   1 MSYQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPLRDAVANLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  81 ALPLDATRLLDIGCGEGYYTAAVADRLNKLRQMAIFGLDVAKVAVRYGAKRYHQVNFCVASSHRLPFANGALDAVLRIYA 160
Cdd:PRK11088  81 RLDEKATALLDIGCGEGYYTHALADALPEITTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIIRIYA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712 161 PCKAVELARTVKPGGIVVTVAPGPRHLYQLKALIYAQVQLHDDTEEHLDGFELIRRETLAYDMKLTGEQGFNLLQMTPFA 240
Cdd:PRK11088 161 PCKAEELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQLEGFELQHSERLAYPMRLTGSEAVALLQMTPFA 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 149292712 241 WRASVDTGQKLAAQPSFSCETDFVISLHRRK 271
Cdd:PRK11088 241 WKATPEVKQQLAAKGVFSCETDFNIRVYRRS 271
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 64-194 8.53e-19

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: 80.42  E-value: 8.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  64 AGYYQPLQqrvsEILDEALPLDATRLLDIGCGEGYYTAAVADRLNKlrqmaIFGLDVAKVAVRYGAKRYH----QVNFCV 139
Cdd:COG2226    5 AARYDGRE----ALLAALGLRPGARVLDLGCGTGRLALALAERGAR-----VTGVDISPEMLELARERAAeaglNVEFVV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149292712 140 ASSHRLPFANGALDAVLRIYA------PCKAV-ELARTVKPGGIVVTVAPGPRHLYQLKALI 194
Cdd:COG2226   76 GDAEDLPFPDGSFDLVISSFVlhhlpdPERALaEIARVLKPGGRLVVVDFSPPDLAELEELL 137
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 63-178 1.88e-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: 1.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  63 DAGYYQPLQQRVSEILDEALPLDAtRLLDIGCGEGYYTAAVADrlnklRQMAIFGLDVAKVAVRYGAKRYHQVN--FCVA 140
Cdd:COG2227    3 DPDARDFWDRRLAALLARLLPAGG-RVLDVGCGTGRLALALAR-----RGADVTGVDISPEALEIARERAAELNvdFVQG 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 149292712 141 SSHRLPFANGALDAVL------RIYAPCKAV-ELARTVKPGGIVV 178
Cdd:COG2227   77 DLEDLPLEDGSFDLVIcsevleHLPDPAALLrELARLLKPGGLLL 121
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 90-175 1.99e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.81  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712   90 LDIGCGEGYYTAAVADRLNKlrqmAIFGLDVAKVAVRYGAKRY----HQVNFCVASSHRLPFANGALDAV--------LR 157
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGA----RVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFPDGSFDLVvssgvlhhLP 77

                          90
                  ....*....|....*....
gi 149292712  158 IYAPCKAV-ELARTVKPGG 175
Cdd:pfam13649  78 DPDLEAALrEIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 90-178 9.29e-12

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.99  E-value: 9.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712   90 LDIGCGEGYYTAAVADRLNKlrqmaIFGLDVAKVAVRYGAKRYH--QVNFCVASSHRLPFANGALDAVLRIYA------P 161
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-----VTGVDISPEMLELAREKAPreGLTFVVGDAEDLPFPDNSFDLVLSSEVlhhvedP 75

                          90
                  ....*....|....*...
gi 149292712  162 CKAV-ELARTVKPGGIVV 178
Cdd:pfam08241  76 ERALrEIARVLKPGGILI 93
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
88-178 2.21e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 53.67  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  88 RLLDIGCGEGYYTAAVADRLNKLRqmaIFGLDVAKVAVRYGAKRYHQVNFCVASSHRLP--------FANGAL------D 153
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGAR---VTGVDLSPEMLARARARLPNVRFVVADLRDLDppepfdlvVSNAALhwlpdhA 80

                         90       100
                 ....*....|....*....|....*
gi 149292712 154 AVLRiyapckavELARTVKPGGIVV 178
Cdd:COG4106   81 ALLA--------RLAAALAPGGVLA 97
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 67-193 3.46e-09

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: 55.76  E-value: 3.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712   67 YQPLQQRVS----EILDEALPLDATRLLDIGCGEGYYTAAVADRLNklrQMAIFGLDVAKVAVRYGAKRY-HQVNFCVAS 141
Cdd:TIGR02072  12 HAKIQREMAkrllALLKEKGIFIPASVLDIGCGTGYLTRALLKRFP---QAEFIALDISAGMLAQAKTKLsENVQFICGD 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 149292712  142 SHRLPFANGALD-----AVLRIYAPCKAV--ELARTVKPGGIVVTVAPGPRHLYQLKAL 193
Cdd:TIGR02072  89 AEKLPLEDSSFDlivsnLALQWCDDLSQAlsELARVLKPGGLLAFSTFGPGTLHELRQS 147
PRK08317 PRK08317
hypothetical protein; Provisional
 66-182 3.20e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 53.02  E-value: 3.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  66 YYQPLQQRVSEILDealPLDATRLLDIGCGEGYYTAAVADRLNKlrQMAIFGLDVAKVAVRYGAKRYHQ----VNFCVAS 141
Cdd:PRK08317   3 DFRRYRARTFELLA---VQPGDRVLDVGCGPGNDARELARRVGP--EGRVVGIDRSEAMLALAKERAAGlgpnVEFVRGD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 149292712 142 SHRLPFANGALDAVL--RIYA----PCKAV-ELARTVKPGGIVVTVAP 182
Cdd:PRK08317  78 ADGLPFPDGSFDAVRsdRVLQhledPARALaEIARVLRPGGRVVVLDT 125
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 85-208 1.44e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 49.72  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712   85 DATRLLDIGCGEGYYTAAVADRLNklrQMA-IFGLDVAKVAVRYGAKR-----YHQVNFCVASSHRLP-----------F 147
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELG---PNAeVVGIDISEEAIEKARENaqklgFDNVEFEQGDIEELPelleddkfdvvI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149292712  148 ANGALDAvlrIYAPCKAVELARTV-KPGGIVVT-----VAPGPRHLYQlKALIYAQVQLHDDTEEHL 208
Cdd:pfam13847  80 SNCVLNH---IPDPDKVLQEILRVlKPGGRLIIsdpdsLAELPAHVKE-DSTYYAGCVGGAILKKKL 142
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 88-180 2.29e-07

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: 48.20  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  88 RLLDIGCGEGYYTAAVADRLNKLrqmaIFGLDVAKVAVRYG-----AKRYHQVNFCVASSHRLPF-ANGALDAVLRIYAP 161
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGAR----VTGVDISPVALELArkaaaALLADNVEVLKGDAEELPPeADESFDVIISDPPL 76

                         90       100
                 ....*....|....*....|....*..
gi 149292712 162 CKAV--------ELARTVKPGGIVVTV 180
Cdd:cd02440   77 HHLVedlarfleEARRLLKPGGVLVLT 103
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 63-217 1.85e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 47.60  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  63 DAGYYQPLQQRVSEILDEALPLDA-TRLLDIGCGEGYYTAAVADRLNKlrqmAIFGLDVAKVAVRYGAKRY-----HQVN 136
Cdd:COG0500    3 DSYYSDELLPGLAALLALLERLPKgGRVLDLGCGTGRNLLALAARFGG----RVIGIDLSPEAIALARARAakaglGNVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712 137 FCVASSHRL-PFANGALDAVLRIY-------APCKAV--ELARTVKPGGIVVTVAPGPRHLYQLKALIYAQVQLHDDTEE 206
Cdd:COG0500   79 FLVADLAELdPLPAESFDLVVAFGvlhhlppEEREALlrELARALKPGGVLLLSASDAAAALSLARLLLLATASLLELLL 158

                        170
                 ....*....|.
gi 149292712 207 HLDGFELIRRE 217
Cdd:COG0500  159 LLRLLALELYL 169
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
63-178 6.78e-06

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 45.37  E-value: 6.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  63 DAGYYQPlQQRVSEILDEALPLDATRLLDIGCGEGYYTAAVADRLNKlrqmaIFGLDVAKVAVRYGAKRYHQVNFCVASS 142
Cdd:COG4976   25 DLGYEAP-ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR-----LTGVDLSEEMLAKAREKGVYDRLLVADL 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 149292712 143 HRLPFANGALDAVLriyapCKAV------------ELARTVKPGGIVV 178
Cdd:COG4976   99 ADLAEPDGRFDLIV-----AADVltylgdlaavfaGVARALKPGGLFI 141
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
83-178 6.84e-05

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 43.20  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712   83 PLDATRLLDIGCGEGYYTAAVADRLNKLRQMAifGLDVAKVAVRYGAKR-----YHQVNFCVASSHRLPFANGALDAV-- 155
Cdd:pfam01209  40 VKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVV--GLDINENMLKEGEKKakeegKYNIEFLQGNAEELPFEDDSFDIVti 117

                          90       100
                  ....*....|....*....|....*...
gi 149292712  156 ---LRIYAPCKAV--ELARTVKPGGIVV 178
Cdd:pfam01209 118 sfgLRNFPDYLKVlkEAFRVLKPGGRVV 145
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 71-182 2.72e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 40.30  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712  71 QQRVSEILDEALPLDATRLLDIGCGEGYYTAAVADRLNklrqMAIFGLDVAKVAVRYGAKRY------HQVNFCVASSHR 144
Cdd:COG2230   37 EAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYG----VRVTGVTLSPEQLEYARERAaeaglaDRVEVRLADYRD 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 149292712 145 LPfANGALDAVLRI----YAPCKAV-----ELARTVKPGGIVVTVAP 182
Cdd:COG2230  113 LP-ADGQFDAIVSIgmfeHVGPENYpayfaKVARLLKPGGRLLLHTP 158
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 90-177 3.00e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 36.19  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149292712   90 LDIGCGEGYYTAAVADrlnKLRQMAIFGLDVAKVAVRYGAKRYHQVNFCVASSHRLP---------------FANGAL-- 152
Cdd:pfam08242   1 LEIGCGTGTLLRALLE---ALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFqldlgeldpgsfdvvVASNVLhh 77

                          90       100
                  ....*....|....*....|....*....
gi 149292712  153 ----DAVLRiyapckavELARTVKPGGIV 177
Cdd:pfam08242  78 ladpRAVLR--------NIRRLLKPGGVL 98
 
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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