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Conserved domains on  [gi|1069754987|gb|AOR58760|]
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23S rRNA (guanine(745)-N(1))-methyltransferase [Pectobacterium parmentieri]

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: 517.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987   1 MSYQCPLCQLPLERHPRQWTC-GKHSFDCAKEGYVNLLPVQFKRSKQPGDSAEMMQARRSFLEAGHYQPLRDAVAQHIDN 79
Cdd:PRK11088    1 MSYQCPLCHQPLTLEENSWICpQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPLRDAVANLLAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  80 IVADDATALLDIGCGEGYYTAKLAHRLTSRKAMAIYGLDVSKAAIQRAAKRYDNVEFCVASSQRLPFRDASLDAVVKIYA 159
Cdd:PRK11088   81 RLDEKATALLDIGCGEGYYTHALADALPEITTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIIRIYA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987 160 PCNDAELQRTVKVGGWVVTVSPGPRHLYQLKAEVYEEVLLHPSKDEMLAGFQLMEQQVLAYPMQLSGNEAAALLQMTPFA 239
Cdd:PRK11088  161 PCKAEELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQLEGFELQHSERLAYPMRLTGSEAVALLQMTPFA 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1069754987 240 WRATPEVSQRLQTTTQFSCETDFIIRLHQRVD 271
Cdd:PRK11088  241 WKATPEVKQQLAAKGVFSCETDFNIRVYRRSY 272
 
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: 517.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987   1 MSYQCPLCQLPLERHPRQWTC-GKHSFDCAKEGYVNLLPVQFKRSKQPGDSAEMMQARRSFLEAGHYQPLRDAVAQHIDN 79
Cdd:PRK11088    1 MSYQCPLCHQPLTLEENSWICpQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPLRDAVANLLAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  80 IVADDATALLDIGCGEGYYTAKLAHRLTSRKAMAIYGLDVSKAAIQRAAKRYDNVEFCVASSQRLPFRDASLDAVVKIYA 159
Cdd:PRK11088   81 RLDEKATALLDIGCGEGYYTHALADALPEITTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIIRIYA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987 160 PCNDAELQRTVKVGGWVVTVSPGPRHLYQLKAEVYEEVLLHPSKDEMLAGFQLMEQQVLAYPMQLSGNEAAALLQMTPFA 239
Cdd:PRK11088  161 PCKAEELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQLEGFELQHSERLAYPMRLTGSEAVALLQMTPFA 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1069754987 240 WRATPEVSQRLQTTTQFSCETDFIIRLHQRVD 271
Cdd:PRK11088  241 WKATPEVKQQLAAKGVFSCETDFNIRVYRRSY 272
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
63-191 2.75e-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: 81.96  E-value: 2.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  63 AGHYqplrDAVAQHIDNIVADDATALLDIGCGEGYYTAKLAHRLTSrkamaIYGLDVSKAAIQRAAKRYD----NVEFCV 138
Cdd:COG2226     5 AARY----DGREALLAALGLRPGARVLDLGCGTGRLALALAERGAR-----VTGVDISPEMLELARERAAeaglNVEFVV 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987 139 ASSQRLPFRDASLDAVVKIYAPCN--D-----AELQRTVKVGGWVVTVSPGPRHLYQLKA 191
Cdd:COG2226    76 GDAEDLPFPDGSFDLVISSFVLHHlpDperalAEIARVLKPGGRLVVVDFSPPDLAELEE 135
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
89-174 3.11e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 72.21  E-value: 3.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  89 LDIGCGEGYYTAKLAHRLTSRkamaIYGLDVSKAAIQRAAKRYD----NVEFCVASSQRLPFRDASLDAVVKIYA----P 160
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGAR----VTGVDLSPEMLERARERAAeaglNVEFVQGDAEDLPFPDGSFDLVVSSGVlhhlP 77
                          90
                  ....*....|....*....
gi 1069754987 161 CND-----AELQRTVKVGG 174
Cdd:pfam13649  78 DPDleaalREIARVLKPGG 96
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
75-205 4.67e-10

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: 58.45  E-value: 4.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  75 QHIDNIVADDATALLDIGCGEGYYTAKLAHRLTsrkAMAIYGLDVSKAAIQRAAKRY-DNVEFCVASSQRLPFRDASLDA 153
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRALLKRFP---QAEFIALDISAGMLAQAKTKLsENVQFICGDAEKLPLEDSSFDL 101
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1069754987 154 VVKIYAP--CND-----AELQRTVKVGGWVVTVSPGPRHLYQLKAEVYEEVLLHPSKDE 205
Cdd:TIGR02072 102 IVSNLALqwCDDlsqalSELARVLKPGGLLAFSTFGPGTLHELRQSFGQHGLRYLSLDE 160
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
88-179 1.58e-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: 48.58  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  88 LLDIGCGEGYYTAKLAHRLTSRkamaIYGLDVSKAAIQRA-----AKRYDNVEFCVASSQRLPF-RDASLDAVVKIYAPC 161
Cdd:cd02440     2 VLDLGCGTGALALALASGPGAR----VTGVDISPVALELArkaaaALLADNVEVLKGDAEELPPeADESFDVIISDPPLH 77
                          90       100
                  ....*....|....*....|....*.
gi 1069754987 162 NDAELQ--------RTVKVGGWVVTV 179
Cdd:cd02440    78 HLVEDLarfleearRLLKPGGVLVLT 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: 517.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987   1 MSYQCPLCQLPLERHPRQWTC-GKHSFDCAKEGYVNLLPVQFKRSKQPGDSAEMMQARRSFLEAGHYQPLRDAVAQHIDN 79
Cdd:PRK11088    1 MSYQCPLCHQPLTLEENSWICpQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPLRDAVANLLAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  80 IVADDATALLDIGCGEGYYTAKLAHRLTSRKAMAIYGLDVSKAAIQRAAKRYDNVEFCVASSQRLPFRDASLDAVVKIYA 159
Cdd:PRK11088   81 RLDEKATALLDIGCGEGYYTHALADALPEITTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIIRIYA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987 160 PCNDAELQRTVKVGGWVVTVSPGPRHLYQLKAEVYEEVLLHPSKDEMLAGFQLMEQQVLAYPMQLSGNEAAALLQMTPFA 239
Cdd:PRK11088  161 PCKAEELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQLEGFELQHSERLAYPMRLTGSEAVALLQMTPFA 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1069754987 240 WRATPEVSQRLQTTTQFSCETDFIIRLHQRVD 271
Cdd:PRK11088  241 WKATPEVKQQLAAKGVFSCETDFNIRVYRRSY 272
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
63-191 2.75e-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: 81.96  E-value: 2.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  63 AGHYqplrDAVAQHIDNIVADDATALLDIGCGEGYYTAKLAHRLTSrkamaIYGLDVSKAAIQRAAKRYD----NVEFCV 138
Cdd:COG2226     5 AARY----DGREALLAALGLRPGARVLDLGCGTGRLALALAERGAR-----VTGVDISPEMLELARERAAeaglNVEFVV 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987 139 ASSQRLPFRDASLDAVVKIYAPCN--D-----AELQRTVKVGGWVVTVSPGPRHLYQLKA 191
Cdd:COG2226    76 GDAEDLPFPDGSFDLVISSFVLHHlpDperalAEIARVLKPGGRLVVVDFSPPDLAELEE 135
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
89-174 3.11e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 72.21  E-value: 3.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  89 LDIGCGEGYYTAKLAHRLTSRkamaIYGLDVSKAAIQRAAKRYD----NVEFCVASSQRLPFRDASLDAVVKIYA----P 160
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGAR----VTGVDLSPEMLERARERAAeaglNVEFVQGDAEDLPFPDGSFDLVVSSGVlhhlP 77
                          90
                  ....*....|....*....
gi 1069754987 161 CND-----AELQRTVKVGG 174
Cdd:pfam13649  78 DPDleaalREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
70-181 9.65e-14

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: 66.19  E-value: 9.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  70 RDAVAQHIDNIVADDATaLLDIGCGEGYYTAKLAhrltsRKAMAIYGLDVSKAAIQRAAKRYD--NVEFCVASSQRLPFR 147
Cdd:COG2227    11 DRRLAALLARLLPAGGR-VLDVGCGTGRLALALA-----RRGADVTGVDISPEALEIARERAAelNVDFVQGDLEDLPLE 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1069754987 148 DASLDAVVkiyapCND------------AELQRTVKVGGWVVTVSP 181
Cdd:COG2227    85 DGSFDLVI-----CSEvlehlpdpaallRELARLLKPGGLLLLSTP 125
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
89-177 3.73e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 63.84  E-value: 3.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  89 LDIGCGEGYYTAKLAHRltsrkAMAIYGLDVSKAAIQRAAKRY--DNVEFCVASSQRLPFRDASLDAVVKIYAPC--ND- 163
Cdd:pfam08241   1 LDVGCGTGLLTELLARL-----GARVTGVDISPEMLELAREKAprEGLTFVVGDAEDLPFPDNSFDLVLSSEVLHhvEDp 75
                          90
                  ....*....|....*...
gi 1069754987 164 ----AELQRTVKVGGWVV 177
Cdd:pfam08241  76 eralREIARVLKPGGILI 93
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
89-177 1.28e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 62.53  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  89 LDIGCGEGYYTAKLAHRLTSRKamaIYGLDVSKAAIQRAAKRYDNVEFCVASSQRLPFrDASLDAVVkiyapCNDA---- 164
Cdd:COG4106     6 LDLGCGTGRLTALLAERFPGAR---VTGVDLSPEMLARARARLPNVRFVVADLRDLDP-PEPFDLVV-----SNAAlhwl 76
                          90       100
                  ....*....|....*....|.
gi 1069754987 165 --------ELQRTVKVGGWVV 177
Cdd:COG4106    77 pdhaallaRLAAALAPGGVLA 97
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
83-196 2.12e-12

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 63.20  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  83 DDATALLDIGCGEGYYTAKLAHRLTSRKamAIYGLDVSKAAIQRAAKR-----YDNVEFCVASSQRLP--FRDASLDAV- 154
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELGPNA--EVVGIDISEEAIEKARENaqklgFDNVEFEQGDIEELPelLEDDKFDVVi 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1069754987 155 ---VKIYAPCNDA---ELQRTVKVGGWVVTVSpgPRHLYQLKAEVYEE 196
Cdd:pfam13847  80 sncVLNHIPDPDKvlqEILRVLKPGGRLIISD--PDSLAELPAHVKED 125
PRK08317 PRK08317
hypothetical protein; Provisional
89-181 3.69e-11

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 61.49  E-value: 3.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  89 LDIGCGEGYYTAKLAHRLTSrkAMAIYGLDVS----KAAIQRAAKRYDNVEFCVASSQRLPFRDASLDAVV--KIYAPCN 162
Cdd:PRK08317   24 LDVGCGPGNDARELARRVGP--EGRVVGIDRSeamlALAKERAAGLGPNVEFVRGDADGLPFPDGSFDAVRsdRVLQHLE 101
                          90       100
                  ....*....|....*....|....
gi 1069754987 163 D-----AELQRTVKVGGWVVTVSP 181
Cdd:PRK08317  102 DparalAEIARVLRPGGRVVVLDT 125
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
75-205 4.67e-10

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: 58.45  E-value: 4.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  75 QHIDNIVADDATALLDIGCGEGYYTAKLAHRLTsrkAMAIYGLDVSKAAIQRAAKRY-DNVEFCVASSQRLPFRDASLDA 153
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRALLKRFP---QAEFIALDISAGMLAQAKTKLsENVQFICGDAEKLPLEDSSFDL 101
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1069754987 154 VVKIYAP--CND-----AELQRTVKVGGWVVTVSPGPRHLYQLKAEVYEEVLLHPSKDE 205
Cdd:TIGR02072 102 IVSNLALqwCDDlsqalSELARVLKPGGLLAFSTFGPGTLHELRQSFGQHGLRYLSLDE 160
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
89-155 9.93e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 54.15  E-value: 9.93e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1069754987  89 LDIGCGEGYYTAKLAHRLTSRkamaIYGLDVSKAAIQRAAKRY-----DNVEFCVAS-SQRLPFRDASLDAVV 155
Cdd:COG0500    31 LDLGCGTGRNLLALAARFGGR----VIGIDLSPEAIALARARAakaglGNVEFLVADlAELDPLPAESFDLVV 99
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
65-198 9.02e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 50.77  E-value: 9.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  65 HYQPLRDAVAQHIDNIVADDATALLDIGCGEGYYTAKLAHRltsrkAMAIYGLDVSKAAIQRAAKRYDNVEFCVASSQRL 144
Cdd:COG4976    27 GYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPR-----GYRLTGVDLSEEMLAKAREKGVYDRLLVADLADL 101
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1069754987 145 PFRDASLDAVVkiyapCND------------AELQRTVKVGGWVV--TVSPGPRHLYQLKAEVYEEVL 198
Cdd:COG4976   102 AEPDGRFDLIV-----AADvltylgdlaavfAGVARALKPGGLFIfsVEDADGSGRYAHSLDYVRDLL 164
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
88-179 1.58e-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: 48.58  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  88 LLDIGCGEGYYTAKLAHRLTSRkamaIYGLDVSKAAIQRA-----AKRYDNVEFCVASSQRLPF-RDASLDAVVKIYAPC 161
Cdd:cd02440     2 VLDLGCGTGALALALASGPGAR----VTGVDISPVALELArkaaaALLADNVEVLKGDAEELPPeADESFDVIISDPPLH 77
                          90       100
                  ....*....|....*....|....*.
gi 1069754987 162 NDAELQ--------RTVKVGGWVVTV 179
Cdd:cd02440    78 HLVEDLarfleearRLLKPGGVLVLT 103
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
88-189 4.27e-06

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 46.68  E-value: 4.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  88 LLDIGCGEGYYTAKLAHRltSRKAMAIYGLDVS----KAAIQRAAKRY--DNVEFCVASSQRLPFRDASLDA-------- 153
Cdd:PRK00216   55 VLDLACGTGDLAIALAKA--VGKTGEVVGLDFSegmlAVGREKLRDLGlsGNVEFVQGDAEALPFPDNSFDAvtiafglr 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1069754987 154 -VVKIyapcNDA--ELQRTVKVGGWVVT------VSPGPRHLYQL 189
Cdd:PRK00216  133 nVPDI----DKAlrEMYRVLKPGGRLVIlefskpTNPPLKKAYDF 173
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
89-155 6.52e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 43.90  E-value: 6.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1069754987  89 LDIGCGEGYYTAKLAHRLTSRKamaIYGLDVSKAAIQRAAKRYDNVEFCVASSQRLPFRDA------SLDAVV 155
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLE---YTGLDISPAALEAARERLAALGLLNAVRVELFQLDLgeldpgSFDVVV 70
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
77-162 7.09e-06

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: 45.57  E-value: 7.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  77 IDNIVADDATALLDIGCGEGYYTAKLAHRLTSRKamaIYGLDVSKAAI---QRAAKRY--DNVEFcVASSQRLPFRDASL 151
Cdd:COG2813    42 LEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEAR---VTLVDVNARAVelaRANAAANglENVEV-LWSDGLSGVPDGSF 117
                          90
                  ....*....|.
gi 1069754987 152 DAVVkiyapCN 162
Cdd:COG2813   118 DLIL-----SN 123
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
89-177 5.73e-05

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 43.20  E-value: 5.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069754987  89 LDIGCGEGYYTAKLAHrlTSRKAMAIYGLDVSKAAIQRAAKR-----YDNVEFCVASSQRLPFRDASLDAVVKIYAPCND 163
Cdd:pfam01209  47 LDVAGGTGDWTFGLSD--SAGSSGKVVGLDINENMLKEGEKKakeegKYNIEFLQGNAEELPFEDDSFDIVTISFGLRNF 124
                          90       100
                  ....*....|....*....|.
gi 1069754987 164 A-------ELQRTVKVGGWVV 177
Cdd:pfam01209 125 PdylkvlkEAFRVLKPGGRVV 145
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
88-155 2.55e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 40.68  E-value: 2.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069754987  88 LLDIGCGEGYYTAKLAHRLTSRkamaIYGLDVSKAAIQRAAKRY------DNVEFCVASSQRLPFrDASLDAVV 155
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVR----VTGVTLSPEQLEYARERAaeaglaDRVEVRLADYRDLPA-DGQFDAIV 123
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
62-136 2.61e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 38.39  E-value: 2.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069754987  62 EAGHYQPLRDAVAQhidnIVADDATALLDIGCGEGYYTAKLAHRLtsrKAMAIYGLDVSKAAIQRAAKRYDNVEF 136
Cdd:PRK01683   13 EDERTRPARDLLAR----VPLENPRYVVDLGCGPGNSTELLVERW---PAARITGIDSSPAMLAEARSRLPDCQF 80
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
89-139 3.39e-03

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 37.76  E-value: 3.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1069754987  89 LDIGCGEGYYTAKLAHRltsrkAMAIYGLDVSKAAIQRAAKR-----YDNVEFCVA 139
Cdd:COG2518    71 LEIGTGSGYQAAVLARL-----AGRVYSVERDPELAERARERlaalgYDNVTVRVG 121
 
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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