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Conserved domains on  [gi|446509197|ref|WP_000586725|]
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MULTISPECIES: tellurite resistance methyltransferase TehB [Enterobacteriaceae]

Protein Classification

SAM-dependent methyltransferase TehB( domain architecture ID 11485272)

SAM-dependent methyltransferase TehB catalyzes the methylation of tellurite and is responsible for tellurite resistance when present in high copy number; can also methylate selenite and selenium dioxide

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
1-196 2.15e-149

tellurite resistance methyltransferase TehB;


:

Pssm-ID: 183040  Cd Length: 197  Bit Score: 412.21  E-value: 2.15e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   1 MIIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLDNL 80
Cdd:PRK11207   1 MTIRDENYFTDKYGLTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLITNMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:PRK11207  81 HTAVVDLNNLTFDGEYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446509197 161 EGWERVKYNEDVGELHRTDANGNRIKLRFATMLARK 196
Cdd:PRK11207 161 EGWEMVKYNEDVGELHRTDANGNRIKLRFATMLARK 196
 
Name Accession Description Interval E-value
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
1-196 2.15e-149

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 412.21  E-value: 2.15e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   1 MIIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLDNL 80
Cdd:PRK11207   1 MTIRDENYFTDKYGLTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLITNMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:PRK11207  81 HTAVVDLNNLTFDGEYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446509197 161 EGWERVKYNEDVGELHRTDANGNRIKLRFATMLARK 196
Cdd:PRK11207 161 EGWEMVKYNEDVGELHRTDANGNRIKLRFATMLARK 196
tehB TIGR00477
tellurite resistance protein TehB; Part of a tellurite-reducing operon tehA and tehB [Cellular ...
 1-196 8.90e-130

tellurite resistance protein TehB; Part of a tellurite-reducing operon tehA and tehB [Cellular processes, Toxin production and resistance]


Pssm-ID: 188054  Cd Length: 195  Bit Score: 362.65  E-value: 8.90e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197    1 MIIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLDnL 80
Cdd:TIGR00477   1 FYCKKEDYFSKKYNTTATHSDVVEAVKIVSPCKTLDLGCGQGRNSLYLSLLGYDVTAWDHNENSIAFVNETKEKENLN-L 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLITNMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:TIGR00477  80 STALYDINAANIQENYDFIVSTVVFMFLNAERVPSIIANMQEHTNPGGYNLIVAAMDTADYPCPLPFSFTFKENELREYY 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446509197  161 EGWERVKYNEDVGELHRTDANGNRIKLRFATMLARK 196
Cdd:TIGR00477 160 KDWEFLKYNENVGELHKTDANGNRIKLKFATMLARK 195
TehB pfam03848
Tellurite resistance protein TehB;
1-193 1.42e-124

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 349.15  E-value: 1.42e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197    1 MIIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLDNL 80
Cdd:pfam03848   1 FYCKKEDYFHKKYNLTPTHSEVLEAVKIVKPGKVLDLGCGQGRNSLYLSLLGYDVTAWDKNENSIANLQRIKEKENLDNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLITNMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:pfam03848  81 HTALYDINNATIDENYDFILSTVVLMFLEPERIPGIIANMQECTNPGGYNLIVAAMSTDDVPCTVPFSFTFKEGELKRYY 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 446509197  161 EGWERVKYNEDVGELHRTDANGNRIKLRFATML 193
Cdd:pfam03848 161 QDWERVKYNEDVGELHKTDANGNRIKLRFATML 193
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 29-135 6.57e-18

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 76.51  E-value: 6.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  29 VKPGKT-LDLGCGNGRNSLYLAAN-GYDVDAWDKNAMSIANVERIKSIENL-DNLHTRVVDLNNLTFDGQYDFILSTVVL 105
Cdd:COG2230   49 LKPGMRvLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLaDRVEVRLADYRDLPADGQFDAIVSIGMF 128

                         90       100       110
                 ....*....|....*....|....*....|
gi 446509197 106 MFLEAKTIPGLITNMQRCTKPGGYNLIVAA 135
Cdd:COG2230  129 EHVGPENYPAYFAKVARLLKPGGRLLLHTP 158
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 35-129 5.28e-10

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 54.36  E-value: 5.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  35 LDLGCGNGRNSLYLA-ANGYDVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTF--DGQYDFILSTVVLMFLEAk 111
Cdd:cd02440    3 LDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE- 81

                         90
                 ....*....|....*...
gi 446509197 112 TIPGLITNMQRCTKPGGY 129
Cdd:cd02440   82 DLARFLEEARRLLKPGGV 99
 
Name Accession Description Interval E-value
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
1-196 2.15e-149

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 412.21  E-value: 2.15e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   1 MIIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLDNL 80
Cdd:PRK11207   1 MTIRDENYFTDKYGLTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLITNMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:PRK11207  81 HTAVVDLNNLTFDGEYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446509197 161 EGWERVKYNEDVGELHRTDANGNRIKLRFATMLARK 196
Cdd:PRK11207 161 EGWEMVKYNEDVGELHRTDANGNRIKLRFATMLARK 196
tehB TIGR00477
tellurite resistance protein TehB; Part of a tellurite-reducing operon tehA and tehB [Cellular ...
 1-196 8.90e-130

tellurite resistance protein TehB; Part of a tellurite-reducing operon tehA and tehB [Cellular processes, Toxin production and resistance]


Pssm-ID: 188054  Cd Length: 195  Bit Score: 362.65  E-value: 8.90e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197    1 MIIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLDnL 80
Cdd:TIGR00477   1 FYCKKEDYFSKKYNTTATHSDVVEAVKIVSPCKTLDLGCGQGRNSLYLSLLGYDVTAWDHNENSIAFVNETKEKENLN-L 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLITNMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:TIGR00477  80 STALYDINAANIQENYDFIVSTVVFMFLNAERVPSIIANMQEHTNPGGYNLIVAAMDTADYPCPLPFSFTFKENELREYY 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446509197  161 EGWERVKYNEDVGELHRTDANGNRIKLRFATMLARK 196
Cdd:TIGR00477 160 KDWEFLKYNENVGELHKTDANGNRIKLKFATMLARK 195
TehB pfam03848
Tellurite resistance protein TehB;
1-193 1.42e-124

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 349.15  E-value: 1.42e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197    1 MIIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLDNL 80
Cdd:pfam03848   1 FYCKKEDYFHKKYNLTPTHSEVLEAVKIVKPGKVLDLGCGQGRNSLYLSLLGYDVTAWDKNENSIANLQRIKEKENLDNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   81 HTRVVDLNNLTFDGQYDFILSTVVLMFLEAKTIPGLITNMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYY 160
Cdd:pfam03848  81 HTALYDINNATIDENYDFILSTVVLMFLEPERIPGIIANMQECTNPGGYNLIVAAMSTDDVPCTVPFSFTFKEGELKRYY 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 446509197  161 EGWERVKYNEDVGELHRTDANGNRIKLRFATML 193
Cdd:pfam03848 161 QDWERVKYNEDVGELHKTDANGNRIKLRFATML 193
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 6-197 1.72e-117

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 334.99  E-value: 1.72e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   6 ENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLdNLHTRVV 85
Cdd:PRK12335  96 EDYFHKKYNLTATHSEVLEAVQTVKPGKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENL-NIRTGLY 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  86 DLNNLTFDGQYDFILSTVVLMFLEAKTIPGLITNMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYYEGWER 165
Cdd:PRK12335 175 DINSASIQEEYDFILSTVVLMFLNRERIPAIIKNMQEHTNPGGYNLIVCAMDTEDYPCPMPFSFTFKEGELKDYYQDWEI 254

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446509197 166 VKYNEDVGELHRTDANGNRIKLRFATMLARKK 197
Cdd:PRK12335 255 VKYNENVGHLHKTDENGNRIKLRFATLLAKKV 286
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 29-135 6.57e-18

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 76.51  E-value: 6.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  29 VKPGKT-LDLGCGNGRNSLYLAAN-GYDVDAWDKNAMSIANVERIKSIENL-DNLHTRVVDLNNLTFDGQYDFILSTVVL 105
Cdd:COG2230   49 LKPGMRvLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLaDRVEVRLADYRDLPADGQFDAIVSIGMF 128

                         90       100       110
                 ....*....|....*....|....*....|
gi 446509197 106 MFLEAKTIPGLITNMQRCTKPGGYNLIVAA 135
Cdd:COG2230  129 EHVGPENYPAYFAKVARLLKPGGRLLLHTP 158
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
30-133 1.50e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 74.09  E-value: 1.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  30 KPGKTLDLGCGNGRNSLYLAAN--GYDVDAWDKNAMSIAnveriKSIENLDNLHTRVVDLNNLTFDGQYDFILSTVVLMF 107
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLA-----RARARLPNVRFVVADLRDLDPPEPFDLVVSNAALHW 75

                         90       100
                 ....*....|....*....|....*.
gi 446509197 108 LEAktIPGLITNMQRCTKPGGYNLIV 133
Cdd:COG4106   76 LPD--HAALLARLAAALAPGGVLAVQ 99
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 35-128 3.26e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 72.98  E-value: 3.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   35 LDLGCGNGRNSLYLAAN-GYDVDAWDKNAMSIANVERIKSIENLdNLHTRVVDLNNLTF-DGQYDFILSTVVLMFLEAKT 112
Cdd:pfam13649   2 LDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFpDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 446509197  113 IPGLITNMQRCTKPGG 128
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 28-134 4.06e-17

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: 73.90  E-value: 4.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  28 VVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDknaMSIANVERIKSIENLDNLHTRVVDLNNLTF-DGQYDFILSTVVLM 106
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALARRGADVTGVD---ISPEALEIARERAAELNVDFVQGDLEDLPLeDGSFDLVICSEVLE 98

                         90       100
                 ....*....|....*....|....*...
gi 446509197 107 FLEakTIPGLITNMQRCTKPGGYnLIVA 134
Cdd:COG2227   99 HLP--DPAALLRELARLLKPGGL-LLLS 123
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 30-140 1.48e-16

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 74.18  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  30 KPGKTLDLGCGNGRNSLYLAA-NGYDVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTF--DGQYDFILSTVVLM 106
Cdd:COG0500   26 KGGRVLDLGCGTGRNLLALAArFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDPlpAESFDLVVAFGVLH 105

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446509197 107 FLEAKTIPGLITNMQRCTKPGGYNLIVAAMDTAD 140
Cdd:COG0500  106 HLPPEEREALLRELARALKPGGVLLLSASDAAAA 139
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 18-134 1.08e-15

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: 70.41  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  18 THSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERiKSIENLDNLHTRVVDLNNLTF-DGQY 96
Cdd:COG2226   10 GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARE-RAAEAGLNVEFVVGDAEDLPFpDGSF 88

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446509197  97 DFILSTVVLMFLEAKtiPGLITNMQRCTKPGGYnLIVA 134
Cdd:COG2226   89 DLVISSFVLHHLPDP--ERALAEIARVLKPGGR-LVVV 123
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 35-129 9.30e-14

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 63.84  E-value: 9.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   35 LDLGCGNGRNSLYLAANGYDVDAWDknaMSIANVERIKSIENLDNLHTRVVDLNNLTF-DGQYDFILSTVVLMFLEAktI 113
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVD---ISPEMLELAREKAPREGLTFVVGDAEDLPFpDNSFDLVLSSEVLHHVED--P 75

                          90
                  ....*....|....*.
gi 446509197  114 PGLITNMQRCTKPGGY 129
Cdd:pfam08241  76 ERALREIARVLKPGGI 91
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
17-158 1.64e-10

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 57.32  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  17 RTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWD--KNAMSIAnveRIKSIEnlDNLHtrVVDLNNLTF-D 93
Cdd:COG4976   33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDlsEEMLAKA---REKGVY--DRLL--VADLADLAEpD 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446509197  94 GQYDFILSTVVLMFLEAktIPGLITNMQRCTKPGGynLIVAAMDTADypcTVGFpFAFKEGELRR 158
Cdd:COG4976  106 GRFDLIVAADVLTYLGD--LAAVFAGVARALKPGG--LFIFSVEDAD---GSGR-YAHSLDYVRD 162
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 35-129 5.28e-10

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 54.36  E-value: 5.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  35 LDLGCGNGRNSLYLA-ANGYDVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTF--DGQYDFILSTVVLMFLEAk 111
Cdd:cd02440    3 LDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE- 81

                         90
                 ....*....|....*...
gi 446509197 112 TIPGLITNMQRCTKPGGY 129
Cdd:cd02440   82 DLARFLEEARRLLKPGGV 99
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 30-132 1.32e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 52.05  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   30 KPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIAnveriksiENLDNLHTRVVDLNNLTF-DGQYDFILSTvvlMFL 108
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIE--------RALLNVRFDQFDEQEAAVpAGKFDVIVAR---EVL 90

                          90       100
                  ....*....|....*....|....*
gi 446509197  109 EA-KTIPGLITNMQRCTKPGGYNLI 132
Cdd:pfam13489  91 EHvPDPPALLRQIAALLKPGGLLLL 115
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 23-101 2.25e-08

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 51.44  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   23 LEAVKVVKPGKTLDLGCGNGRNSLYLAANGYD--VDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTFDGQYDFIL 100
Cdd:pfam05175  24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESPDaeLTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLII 103


                  .
gi 446509197  101 S 101
Cdd:pfam05175 104 S 104
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 23-134 5.12e-08

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: 50.57  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  23 LEAVKVVKPGKTLDLGCGNGRNSLYLAANGYD--VDAWDKNAMSIA----NVERiksiENLDNLHTRVVDLNNLTFDGQY 96
Cdd:COG2813   42 LEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEarVTLVDVNARAVElaraNAAA----NGLENVEVLWSDGLSGVPDGSF 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446509197  97 DFILS-------------TVVLMFLEAKtipglitnmqRCTKPGGYNLIVA 134
Cdd:COG2813  118 DLILSnppfhagravdkeVAHALIADAA----------RHLRPGGELWLVA 158
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 35-129 1.10e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 48.13  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   35 LDLGCGNGRNSLYLAAN-------GYDVDAwdknAMSIANVERIKSIENLDNLHTRVVDLN-NLTFDGQYDFILSTVVLM 106
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpgleytGLDISP----AALEAARERLAALGLLNAVRVELFQLDlGELDPGSFDVVVASNVLH 76

                          90       100
                  ....*....|....*....|...
gi 446509197  107 FLeaKTIPGLITNMQRCTKPGGY 129
Cdd:pfam08242  77 HL--ADPRAVLRNIRRLLKPGGV 97
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 23-180 3.29e-06

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 45.88  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   23 LEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWD--KNAMSIANVERI---KSIENLDNLHTRVVDLNNLTFD---- 93
Cdd:pfam05724  30 WDALKLPPGLRVLVPLCGKALDMVWLAEQGHFVVGVEisELAVEKFFAEAGlspPITELSGFKEYSSGNISLYCGDfftl 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   94 -----GQYDFILSTVVLMFLEAKTIPGLITNMQRCTKPGGYNLIVaamdTADYPCT--VGFPFAFKEGELRRYY-EGWEr 165
Cdd:pfam05724 110 preelGKFDLIYDRAALCALPPEMRPRYAKQMYELLPPGGRGLLI----TLDYPQTdhEGPPFSVPAAELEALFgGGWK- 184

                         170
                  ....*....|....*
gi 446509197  166 vkynedVGELHRTDA 180
Cdd:pfam05724 185 ------VAELEREDA 193
PRK08317 PRK08317
hypothetical protein; Provisional
 29-138 3.48e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 46.08  E-value: 3.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  29 VKPGKT-LDLGCGNGRNSLYLAA---NGYDVDAWDKNAMSIANV-ERIKsiENLDNLHTRVVDLNNLTF-DGQYDFILST 102
Cdd:PRK08317  17 VQPGDRvLDVGCGPGNDARELARrvgPEGRVVGIDRSEAMLALAkERAA--GLGPNVEFVRGDADGLPFpDGSFDAVRSD 94

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446509197 103 VVLMFLEAKtiPGLITNMQRCTKPGGYnliVAAMDT 138
Cdd:PRK08317  95 RVLQHLEDP--ARALAEIARVLRPGGR---VVVLDT 125
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 30-132 4.15e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.02  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   30 KPGKTLDLGCGNGRNSLYLAANGY---DVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTF---DGQYDFILSTV 103
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPElleDDKFDVVISNC 82

                          90       100
                  ....*....|....*....|....*....
gi 446509197  104 VLMFLEAKtiPGLITNMQRCTKPGGYNLI 132
Cdd:pfam13847  83 VLNHIPDP--DKVLQEILRVLKPGGRLII 109
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 35-136 1.36e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 41.36  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  35 LDLGCGNGRNSLYLAANGYDVDAWD-KNAMSIANVERIKSIENLDNLHTRVVDLNNLTfdGQYDFILSTVVLMFLEAKTI 113
Cdd:PRK07580  68 LDAGCGVGSLSIPLARRGAKVVASDiSPQMVEEARERAPEAGLAGNITFEVGDLESLL--GRFDTVVCLDVLIHYPQEDA 145

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446509197 114 PGLITNMQRCTK--------PggYNLIVAAM 136
Cdd:PRK07580 146 ARMLAHLASLTRgsliftfaP--YTPLLALL 174
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 35-128 5.19e-04

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 39.74  E-value: 5.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  35 LDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIEnldnlHTRVVDLNNLTF-DGQYDFILSTVVLMFleAKTI 113
Cdd:PRK10258  47 LDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAAD-----HYLAGDIESLPLaTATFDLAWSNLAVQW--CGNL 119

                         90
                 ....*....|....*
gi 446509197 114 PGLITNMQRCTKPGG 128
Cdd:PRK10258 120 STALRELYRVVRPGG 134
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 2-132 6.59e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 39.73  E-value: 6.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197   2 IIRDENYFTDKYELT---RTHSEVLEAVKVvKPG-KTLDLGCGNGRNSLYLAANgYDVDA----WDKNAMSIAnVERikS 73
Cdd:PLN02336 235 ILRYERVFGEGFVSTgglETTKEFVDKLDL-KPGqKVLDVGCGIGGGDFYMAEN-FDVHVvgidLSVNMISFA-LER--A 309

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  74 IENLDNLHTRVVDLNNLTF-DGQYDFILSTVVLMFLEAKtiPGLITNMQRCTKPGGYNLI 132
Cdd:PLN02336 310 IGRKCSVEFEVADCTKKTYpDNSFDVIYSRDTILHIQDK--PALFRSFFKWLKPGGKVLI 367
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 32-129 1.51e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.58  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  32 GKT-LDLGCGNGRNSLYLAANGYDVDAWDknamSIANVerIKSIENLDNLHTRV------VDLNNLTF-DGQYDFILSTV 103
Cdd:PLN02336  38 GKSvLELGAGIGRFTGELAKKAGQVIALD----FIESV--IKKNESINGHYKNVkfmcadVTSPDLNIsDGSVDLIFSNW 111

                         90       100
                 ....*....|....*....|....*.
gi 446509197 104 VLMFLEAKTIPGLITNMQRCTKPGGY 129
Cdd:PLN02336 112 LLMYLSDKEVENLAERMVKWLKVGGY 137
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
23-129 2.41e-03

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 37.85  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509197  23 LEAV-KVVKPGKT-LDLGCGngrnS-------LYLAAN---GYDVDAWdknAMSIA--NVERiksieNldNLHTRV-VDL 87
Cdd:COG2264  139 LEALeKLLKPGKTvLDVGCG----SgilaiaaAKLGAKrvlAVDIDPV---AVEAAreNAEL-----N--GVEDRIeVVL 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446509197  88 NNLTFDGQYDF----ILSTVVLMFLEAktipglitnMQRCTKPGGY 129
Cdd:COG2264  205 GDLLEDGPYDLvvanILANPLIELAPD---------LAALLKPGGY 241
 
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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