NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|501854215|ref|WP_012657725|]
View 

putative RNA methyltransferase [Streptococcus uberis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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; ...
 11-243 7.88e-46

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 PRK11088:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 272  Bit Score: 154.68  E-value: 7.88e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  11 FQCPICHMSLHLSGTSLLCPQRHTFDMAKQGYVNLLLNAKK---DPHYDKNSFIQRSRILEAGFYS----HILEALKEEL 83
Cdd:PRK11088   3 YQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKrskDPGDNKEMMQARRAFLDAGHYQplrdAVANLLAERL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  84 KSNQRlTILDVACGEGYY----ARALSENPSYQLLAFDLSKDSVLLAAKKDPQkrVSWFVGDLAKLPLADDSVDVILDIF 159
Cdd:PRK11088  83 DEKAT-ALLDIGCGEGYYthalADALPEITTMQLFGLDISKVAIKYAAKRYPQ--VTFCVASSHRLPFADQSLDAIIRIY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215 160 SPANYQEFLRVLKPGGKLIKMVTASDHLQELREAAAAQLQSKTYSNQAIvdhfaEAFPDFNMTHLSQTYPIEDKALAHFV 239
Cdd:PRK11088 160 APCKAEELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQL-----EGFELQHSERLAYPMRLTGSEAVALL 234


                 ....
gi 501854215 240 QMTP 243
Cdd:PRK11088 235 QMTP 238
 
Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 11-243 7.88e-46

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 154.68  E-value: 7.88e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  11 FQCPICHMSLHLSGTSLLCPQRHTFDMAKQGYVNLLLNAKK---DPHYDKNSFIQRSRILEAGFYS----HILEALKEEL 83
Cdd:PRK11088   3 YQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKrskDPGDNKEMMQARRAFLDAGHYQplrdAVANLLAERL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  84 KSNQRlTILDVACGEGYY----ARALSENPSYQLLAFDLSKDSVLLAAKKDPQkrVSWFVGDLAKLPLADDSVDVILDIF 159
Cdd:PRK11088  83 DEKAT-ALLDIGCGEGYYthalADALPEITTMQLFGLDISKVAIKYAAKRYPQ--VTFCVASSHRLPFADQSLDAIIRIY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215 160 SPANYQEFLRVLKPGGKLIKMVTASDHLQELREAAAAQLQSKTYSNQAIvdhfaEAFPDFNMTHLSQTYPIEDKALAHFV 239
Cdd:PRK11088 160 APCKAEELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQL-----EGFELQHSERLAYPMRLTGSEAVALL 234


                 ....
gi 501854215 240 QMTP 243
Cdd:PRK11088 235 QMTP 238
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 69-196 2.35e-23

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: 92.36  E-value: 2.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  69 AGFYSHiLEALKEELKSNQRLTILDVACGEGYYARALSENpSYQLLAFDLSKDSVLLAAKKDPQK--RVSWFVGDLAKLP 146
Cdd:COG2226    5 AARYDG-REALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAglNVEFVVGDAEDLP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501854215 147 LADDSVDVILDIFS-------PANYQEFLRVLKPGGKLIKMVTASDHLQELREAAAA 196
Cdd:COG2226   83 FPDGSFDLVISSFVlhhlpdpERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 91-175 5.70e-21

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 84.92  E-value: 5.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215   91 ILDVACGEGYYARALSENPSYQLLAFDLSKDSVLLAAKK--DPQKRVSWFVGDLAKLPLADDSVDVILDIFS-------- 160
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERaaEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVlhhlpdpd 80

                          90
                  ....*....|....*.
gi 501854215  161 -PANYQEFLRVLKPGG 175
Cdd:pfam13649  81 lEAALREIARVLKPGG 96
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 53-193 8.53e-14

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: 68.85  E-value: 8.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215   53 PHYDKNSFIQRsrilEAGFysHILEALKEELKSNQRlTILDVACGEGYYARALSE-NPSYQLLAFDLSkDSVLLAAKKDP 131
Cdd:TIGR02072   7 KTYDRHAKIQR----EMAK--RLLALLKEKGIFIPA-SVLDIGCGTGYLTRALLKrFPQAEFIALDIS-AGMLAQAKTKL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501854215  132 QKRVSWFVGDLAKLPLADDSVDVIldiFSPANYQ----------EFLRVLKPGGKLIKMVTASDHLQELREA 193
Cdd:TIGR02072  79 SENVQFICGDAEKLPLEDSSFDLI---VSNLALQwcddlsqalsELARVLKPGGLLAFSTFGPGTLHELRQS 147
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 90-178 2.16e-13

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: 64.76  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  90 TILDVACGEGYYARALSENPSYQLLAFDLSKDSVLLAAKKD---PQKRVSWFVGDLAKLPL-ADDSVDVIL----DIFSP 161
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAaalLADNVEVLKGDAEELPPeADESFDVIIsdppLHHLV 80

                         90       100
                 ....*....|....*....|.
gi 501854215 162 ANYQEFL----RVLKPGGKLI 178
Cdd:cd02440   81 EDLARFLeearRLLKPGGVLV 101
 
Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 11-243 7.88e-46

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 154.68  E-value: 7.88e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  11 FQCPICHMSLHLSGTSLLCPQRHTFDMAKQGYVNLLLNAKK---DPHYDKNSFIQRSRILEAGFYS----HILEALKEEL 83
Cdd:PRK11088   3 YQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKrskDPGDNKEMMQARRAFLDAGHYQplrdAVANLLAERL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  84 KSNQRlTILDVACGEGYY----ARALSENPSYQLLAFDLSKDSVLLAAKKDPQkrVSWFVGDLAKLPLADDSVDVILDIF 159
Cdd:PRK11088  83 DEKAT-ALLDIGCGEGYYthalADALPEITTMQLFGLDISKVAIKYAAKRYPQ--VTFCVASSHRLPFADQSLDAIIRIY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215 160 SPANYQEFLRVLKPGGKLIKMVTASDHLQELREAAAAQLQSKTYSNQAIvdhfaEAFPDFNMTHLSQTYPIEDKALAHFV 239
Cdd:PRK11088 160 APCKAEELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQL-----EGFELQHSERLAYPMRLTGSEAVALL 234


                 ....
gi 501854215 240 QMTP 243
Cdd:PRK11088 235 QMTP 238
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 69-196 2.35e-23

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: 92.36  E-value: 2.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  69 AGFYSHiLEALKEELKSNQRLTILDVACGEGYYARALSENpSYQLLAFDLSKDSVLLAAKKDPQK--RVSWFVGDLAKLP 146
Cdd:COG2226    5 AARYDG-REALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAglNVEFVVGDAEDLP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501854215 147 LADDSVDVILDIFS-------PANYQEFLRVLKPGGKLIKMVTASDHLQELREAAAA 196
Cdd:COG2226   83 FPDGSFDLVISSFVlhhlpdpERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 91-175 5.70e-21

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 84.92  E-value: 5.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215   91 ILDVACGEGYYARALSENPSYQLLAFDLSKDSVLLAAKK--DPQKRVSWFVGDLAKLPLADDSVDVILDIFS-------- 160
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERaaEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVlhhlpdpd 80

                          90
                  ....*....|....*.
gi 501854215  161 -PANYQEFLRVLKPGG 175
Cdd:pfam13649  81 lEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 74-178 9.02e-18

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: 77.37  E-value: 9.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  74 HILEALKEELKSNQRltILDVACGEGYYARALSENpSYQLLAFDLSKDSVLLAAKKDPQKRVSWFVGDLAKLPLADDSVD 153
Cdd:COG2227   13 RLAALLARLLPAGGR--VLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLEDGSFD 89

                         90       100       110
                 ....*....|....*....|....*....|..
gi 501854215 154 VILD------IFSPANY-QEFLRVLKPGGKLI 178
Cdd:COG2227   90 LVICsevlehLPDPAALlRELARLLKPGGLLL 121
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 92-178 9.55e-18

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 76.16  E-value: 9.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215   92 LDVACGEGYYARALSENpSYQLLAFDLSKDSVLLAAKKDPQKRVSWFVGDLAKLPLADDSVDVILDIFS-------PANY 164
Cdd:pfam08241   1 LDVGCGTGLLTELLARL-GARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVlhhvedpERAL 79

                          90
                  ....*....|....
gi 501854215  165 QEFLRVLKPGGKLI 178
Cdd:pfam08241  80 REIARVLKPGGILI 93
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 76-199 1.47e-14

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 70.33  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  76 LEALKEELKSNqrLTILDVACGEGYYARALSENPSYQLLAFDLSKDSVLLA---AKKDPQKRVSWFVGDLAKL-PLADDS 151
Cdd:COG0500   17 LLALLERLPKG--GRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALArarAAKAGLGNVEFLVADLAELdPLPAES 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501854215 152 VDVILDI-----FSPANYQEFL----RVLKPGGKLIkmVTASDHLQELREAAAAQLQ 199
Cdd:COG0500   95 FDLVVAFgvlhhLPPEEREALLrelaRALKPGGVLL--LSASDAAAALSLARLLLLA 149
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 53-193 8.53e-14

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: 68.85  E-value: 8.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215   53 PHYDKNSFIQRsrilEAGFysHILEALKEELKSNQRlTILDVACGEGYYARALSE-NPSYQLLAFDLSkDSVLLAAKKDP 131
Cdd:TIGR02072   7 KTYDRHAKIQR----EMAK--RLLALLKEKGIFIPA-SVLDIGCGTGYLTRALLKrFPQAEFIALDIS-AGMLAQAKTKL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501854215  132 QKRVSWFVGDLAKLPLADDSVDVIldiFSPANYQ----------EFLRVLKPGGKLIKMVTASDHLQELREA 193
Cdd:TIGR02072  79 SENVQFICGDAEKLPLEDSSFDLI---VSNLALQwcddlsqalsELARVLKPGGLLAFSTFGPGTLHELRQS 147
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 90-178 2.16e-13

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: 64.76  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  90 TILDVACGEGYYARALSENPSYQLLAFDLSKDSVLLAAKKD---PQKRVSWFVGDLAKLPL-ADDSVDVIL----DIFSP 161
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAaalLADNVEVLKGDAEELPPeADESFDVIIsdppLHHLV 80

                         90       100
                 ....*....|....*....|.
gi 501854215 162 ANYQEFL----RVLKPGGKLI 178
Cdd:cd02440   81 EDLARFLeearRLLKPGGVLV 101
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 71-178 5.00e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 65.34  E-value: 5.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  71 FYSHILEALkeELKSNQRltILDVACGEGYYARALSENPSYQLLAFDLSKDSVLLA----AKKDPQKRVSWFVGDLAKLP 146
Cdd:COG2230   39 KLDLILRKL--GLKPGMR--VLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYAreraAEAGLADRVEVRLADYRDLP 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 501854215 147 lADDSVDVILDI-----FSPANYQEFL----RVLKPGGKLI 178
Cdd:COG2230  115 -ADGQFDAIVSIgmfehVGPENYPAYFakvaRLLKPGGRLL 154
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
90-178 8.57e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 62.92  E-value: 8.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  90 TILDVACGEGYYARALSEN-PSYQLLAFDLSKDSVLLAAKKDPqkRVSWFVGDLAKLPLaDDSVDVILDIFS-------P 161
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERfPGARVTGVDLSPEMLARARARLP--NVRFVVADLRDLDP-PEPFDLVVSNAAlhwlpdhA 80

                         90
                 ....*....|....*..
gi 501854215 162 ANYQEFLRVLKPGGKLI 178
Cdd:COG4106   81 ALLARLAAALAPGGVLA 97
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
74-178 1.06e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 61.94  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  74 HILEALKEELKSNQRLTILDVACGEGYYARALSENpSYQLLAFDLSKDSVLLAAKKDPQkrVSWFVGDLAKLPLADDSVD 153
Cdd:COG4976   33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPR-GYRLTGVDLSEEMLAKAREKGVY--DRLLVADLADLAEPDGRFD 109

                         90       100       110
                 ....*....|....*....|....*....|..
gi 501854215 154 VIL--DIFS-PANYQEFL----RVLKPGGKLI 178
Cdd:COG4976  110 LIVaaDVLTyLGDLAAVFagvaRALKPGGLFI 141
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 89-192 1.46e-11

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 60.89  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215   89 LTILDVACGEGYYARALSE--NPSYQLLAFDLSKDSVLLA---AKKDPQKRVSWFVGDLAKLP--LADDSVDVILDI--- 158
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAEelGPNAEVVGIDISEEAIEKArenAQKLGFDNVEFEQGDIEELPelLEDDKFDVVISNcvl 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 501854215  159 ----FSPANYQEFLRVLKPGGKLIkmVTASDHLQELRE 192
Cdd:pfam13847  85 nhipDPDKVLQEILRVLKPGGRLI--ISDPDSLAELPA 120
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 90-177 7.42e-11

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 60.55  E-value: 7.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  90 TILDVACGEGYYARALSE--NPSYQLLAFDLSKdSVLLAAKK-----DPQKRVSWFVGDLAKLPLADDSVDVI------- 155
Cdd:PRK00216  54 KVLDLACGTGDLAIALAKavGKTGEVVGLDFSE-GMLAVGREklrdlGLSGNVEFVQGDAEALPFPDNSFDAVtiafglr 132

                         90       100
                 ....*....|....*....|....
gi 501854215 156 --LDIfsPANYQEFLRVLKPGGKL 177
Cdd:PRK00216 133 nvPDI--DKALREMYRVLKPGGRL 154
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 89-177 9.12e-10

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 57.27  E-value: 9.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215   89 LTILDVACGEGYYARALSEN--PSYQLLAFDLSKDSVLLAAKKDPQK-RVSWFVGDLAKLPLADDSVDVILDIF---SPA 162
Cdd:TIGR01934  41 QKVLDVACGTGDLAIELAKSapDRGKVTGVDFSSEMLEVAKKKSELPlNIEFIQADAEALPFEDNSFDAVTIAFglrNVT 120

                          90
                  ....*....|....*....
gi 501854215  163 NYQ----EFLRVLKPGGKL 177
Cdd:TIGR01934 121 DIQkalrEMYRVLKPGGRL 139
PRK08317 PRK08317
hypothetical protein; Provisional
 90-180 4.83e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 55.33  E-value: 4.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  90 TILDVACGEGYYARALSE--NPSYQLLAFDLSKDSVLLAAKKDPQK--RVSWFVGDLAKLPLADDSVDV---------IL 156
Cdd:PRK08317  22 RVLDVGCGPGNDARELARrvGPEGRVVGIDRSEAMLALAKERAAGLgpNVEFVRGDADGLPFPDGSFDAvrsdrvlqhLE 101

                         90       100
                 ....*....|....*....|....
gi 501854215 157 DIfsPANYQEFLRVLKPGGKLIKM 180
Cdd:PRK08317 102 DP--ARALAEIARVLRPGGRVVVL 123
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 54-196 1.34e-08

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 54.38  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  54 HYDKNSFIQRsrileagfysHILEALKEELKSNQRLTILDVACGEGYYARALSENPSyQLLAFDLSkdSVLLAAKKDPQK 133
Cdd:PRK10258  19 HYEQHAELQR----------QSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGS-QVTALDLS--PPMLAQARQKDA 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501854215 134 RVSWFVGDLAKLPLADDSVDVI--------LDIFSPAnYQEFLRVLKPGGKLIKMVTASDHLQELREAAAA 196
Cdd:PRK10258  86 ADHYLAGDIESLPLATATFDLAwsnlavqwCGNLSTA-LRELYRVVRPGGVVAFTTLVQGSLPELHQAWQA 155
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
89-218 5.65e-08

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 52.06  E-value: 5.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215   89 LTILDVACGEGYYARALSEN--PSYQLLAFDLSKDSVLLAAKK---DPQKRVSWFVGDLAKLPLADDSVDVILDIFSPAN 163
Cdd:pfam01209  44 NKFLDVAGGTGDWTFGLSDSagSSGKVVGLDINENMLKEGEKKakeEGKYNIEFLQGNAEELPFEDDSFDIVTISFGLRN 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501854215  164 Y-------QEFLRVLKPGGKLIKMVTASDHLQELREA----------AAAQLQSKTYSNQAIVDHFAEAFPD 218
Cdd:pfam01209 124 FpdylkvlKEAFRVLKPGGRVVCLEFSKPENPLLSQAyelyfkyvmpFMGKMFAKSYKSYQYLQESIRDFPD 195
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 92-177 3.93e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 47.36  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215   92 LDVACGEGYYARALSE-NPSYQLLAFDLSKDSVLLAAKK------DPQKRVSWFVGDLAKLPLAddSVDVILDIFS---- 160
Cdd:pfam08242   1 LEIGCGTGTLLRALLEaLPGLEYTGLDISPAALEAARERlaalglLNAVRVELFQLDLGELDPG--SFDVVVASNVlhhl 78

                          90       100
                  ....*....|....*....|
gi 501854215  161 ---PANYQEFLRVLKPGGKL 177
Cdd:pfam08242  79 adpRAVLRNIRRLLKPGGVL 98
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 55-178 4.83e-07

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 50.52  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  55 YDKNSFIQRSRILEAGFYSHI-LEALKE-----ELKSNQRltILDVACGEGYYARALSENPSYQLLAFDLSKDSVLLAAK 128
Cdd:PLN02336 230 YKSSGILRYERVFGEGFVSTGgLETTKEfvdklDLKPGQK--VLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALE 307

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 501854215 129 KDPQKR--VSWFVGDLAKLPLADDSVDVI------LDIF-SPANYQEFLRVLKPGGKLI 178
Cdd:PLN02336 308 RAIGRKcsVEFEVADCTKKTYPDNSFDVIysrdtiLHIQdKPALFRSFFKWLKPGGKVL 366
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 91-176 1.22e-06

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 48.73  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  91 ILDVACGEGYYARALSEN--PSYQLLAFDLSKDSVLLAAKKDPQ------KRVSWFVGDLAKLPLADDSVDVILDIFSPA 162
Cdd:PLN02233  77 VLDLCCGSGDLAFLLSEKvgSDGKVMGLDFSSEQLAVAASRQELkakscyKNIEWIEGDATDLPFDDCYFDAITMGYGLR 156

                         90       100
                 ....*....|....*....|.
gi 501854215 163 N-------YQEFLRVLKPGGK 176
Cdd:PLN02233 157 NvvdrlkaMQEMYRVLKPGSR 177
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
90-177 1.35e-06

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 48.37  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  90 TILDVACGEGYYARALSENPSYQLLAFDLSKDsVLLAAKKDP------QKRVSWFVGDLAKL--PLADDSVDVIL----- 156
Cdd:COG2521  135 RVLDTCTGLGYTAIEALKRGAREVITVEKDPN-VLELAELNPwsrelaNERIKIILGDASEVikTFPDESFDAIIhdppr 213

                         90       100
                 ....*....|....*....|....*.
gi 501854215 157 -----DIFSPANYQEFLRVLKPGGKL 177
Cdd:COG2521  214 fslagELYSLEFYRELYRVLKPGGRL 239
arsM PRK11873
arsenite methyltransferase;
140-196 8.15e-06

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 46.09  E-value: 8.15e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501854215 140 GDLAKLPLADDSVDVILD---I-FSP---ANYQEFLRVLKPGGKLI--KMVTASDHLQELREAAAA 196
Cdd:PRK11873 135 GEIEALPVADNSVDVIISncvInLSPdkeRVFKEAFRVLKPGGRFAisDVVLRGELPEEIRNDAEL 200
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 76-187 8.98e-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: 45.18  E-value: 8.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  76 LEALKEELKSnqrlTILDVACGEGYYARAL-SENPSYQLLAFDLSKDSVLLAAK--KDPQ-KRVSWFVGDLAKlPLADDS 151
Cdd:COG2813   42 LEHLPEPLGG----RVLDLGCGYGVIGLALaKRNPEARVTLVDVNARAVELARAnaAANGlENVEVLWSDGLS-GVPDGS 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 501854215 152 VDVIL----------DIFSPAnyQEFL----RVLKPGGKLIkMVTASdHL 187
Cdd:COG2813  117 FDLILsnppfhagraVDKEVA--HALIadaaRHLRPGGELW-LVANR-HL 162
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
139-178 2.16e-05

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 43.70  E-value: 2.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 501854215 139 VGDLAK-LPLADDSVDVI--------LDIFSPAN-YQEFLRVLKPGGKLI 178
Cdd:COG4627   33 VGDLTDpLPFPDNSVDAIysshvlehLDYEEAPLaLKECYRVLKPGGILR 82
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 71-192 2.84e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 40.49  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215   71 FYSHILEALKEELKSNQRltILDVACGEGYYARALSENPsYQLLAFDLSKDSVLLAAKKDPQKrvsWFVGDLAKLPlaDD 150
Cdd:pfam13489   8 LLADLLLRLLPKLPSPGR--VLDFGCGTGIFLRLLRAQG-FSVTGVDPSPIAIERALLNVRFD---QFDEQEAAVP--AG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 501854215  151 SVDVILDIFS-------PANYQEFLRVLKPGGKL-IKMVTASDHLQELRE 192
Cdd:pfam13489  80 KFDVIVAREVlehvpdpPALLRQIAALLKPGGLLlLSTPLASDEADRLLL 129
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
146-237 7.14e-04

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 38.85  E-value: 7.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  146 PLADDSVDVILDIFSPANYQEFLRVLKPGGKLIKMVTASDHLQELREAAAAQLQSKTYS-----NQAIVDHFAEAFPDFN 220
Cdd:pfam13602  17 ATGGEGVDVVLDTVGGEAFEASLRVLPGGGRLVTIGGPPLSAGLLLPARKRGGRGVKYLflfvrPNLGADILQELADLIE 96

                          90       100
                  ....*....|....*....|.
gi 501854215  221 ----MTHLSQTYPIEDKALAH 237
Cdd:pfam13602  97 egklRPVIDRVFPLEEAAEAH 117
PRK05785 PRK05785
hypothetical protein; Provisional
 77-160 7.18e-04

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 40.06  E-value: 7.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  77 EALKEELKSNQR-LTILDVACGEGYYARALSENPSYQLLAFDLSKDSVLLAAKKDpqKRVswfVGDLAKLPLADDSVDVI 155
Cdd:PRK05785  40 ELVKTILKYCGRpKKVLDVAAGKGELSYHFKKVFKYYVVALDYAENMLKMNLVAD--DKV---VGSFEALPFRDKSFDVV 114


                 ....*
gi 501854215 156 LDIFS 160
Cdd:PRK05785 115 MSSFA 119
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
82-215 9.92e-04

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 39.90  E-value: 9.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  82 ELKSNQrlTILDVACGEGYY----ARALSEN------------PSYQLLAFDLSKDSVLLAAKKDPQKRVSWFVGDLAKL 145
Cdd:COG4798   63 GVKPGM--TVVEIWPGGGWYteilAPYLGPKgkvyaanfdpdsEPPEYAKRSREAFSAKLAADPALYGNVRVTAFAPPDD 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215 146 PLADD-SVDVIL----------DIFSPANYQEFLRVLKPGGKLIkmVTasDHlqELREAAAAQLQSKT-YSNQAIVDHFA 213
Cdd:COG4798  141 PIAPPgSADLVLtfrnyhnwyrAGDAAAMFAAFFKALKPGGVLG--VV--DH--RAPPGTGLEAVATLgYIDEAYVIALA 214


                 ..
gi 501854215 214 EA 215
Cdd:COG4798  215 EA 216
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 86-236 1.42e-03

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 38.97  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  86 NQRLTILDVACGEGYYARALSE-NPSYQLLAFDLSKDSVLLAAKK---DPQKRVSWFVGDLAKLP--LADDSVDVIlDIF 159
Cdd:COG0220   31 NDAPLVLEIGFGKGEFLVELAAaNPDINFIGIEVHEPGVAKALKKaeeEGLTNVRLLRGDAVELLelFPDGSLDRI-YLN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215 160 ----------------SPANYQEFLRVLKPGGKLIkmvTASDHlQELREAAAAQL-QSKTYSNQAIVDHFAEAFPDFNMT 222
Cdd:COG0220  110 fpdpwpkkrhhkrrlvQPEFLALLARVLKPGGELH---LATDW-EDYAEEMLEVLsAHPGFENLAETGDYAPRPEDRPLT 185

                        170
                 ....*....|....
gi 501854215 223 HlsqtYpiEDKALA 236
Cdd:COG0220  186 K----Y--ERKGLR 193
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 138-193 1.43e-03

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 38.39  E-value: 1.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501854215 138 FVGDLAKLPLADDSVDVI-----------------LDIFSPAnYQEFLRVLKPGGKLIkMVTASDHLQELREA 193
Cdd:COG1041   79 IRGDARDLPLADESVDAIvtdppygrsskisgeelLELYEKA-LEEAARVLKPGGRVV-IVTPRDIDELLEEA 149
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 77-156 1.47e-03

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 39.36  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501854215  77 EALkEELKSNQRLTILDVACGEGYYARAL-SENPSYQLLAFDLSKDSVLLA---AKK-DPQKRVSWFVGDLAKlPLADD- 150
Cdd:COG2890  103 LAL-ALLPAGAPPRVLDLGTGSGAIALALaKERPDARVTAVDISPDALAVArrnAERlGLEDRVRFLQGDLFE-PLPGDg 180


                 ....*.
gi 501854215 151 SVDVIL 156
Cdd:COG2890  181 RFDLIV 186
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH