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Conserved domains on  [gi|553017249|gb|AGY50226|]
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tRNA(1-methyladenosine) methyltransferase-related methyltransferase [Candidatus Methanomassiliicoccus intestinalis Issoire-Mx1]

Protein Classification

tRNA (adenine-N1)-methyltransferase( domain architecture ID 11457537)

tRNA (adenine-N1)-methyltransferase, such as tRNA (adenine(58)-N(1))-methyltransferase, which is a class I SAM-dependent methyltransferase that catalyzes the methylation of N(1)-adenine at position 58 (m1A58) in tRNA using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 4-250 1.12e-107

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 310.94  E-value: 1.12e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249   4 EGDLIYLLDSKGYRHWLTLGNGMVRVQGLGVVDSSKIIGQEDGYAL-SIAGKTFTALKPMIGDLMQSLERGPQIITPKDA 82
Cdd:COG2519    1 EGDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVtTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  83 ATIAFRLGLRAGETVVEAGVGSGALTMALINSVMPTGRVISMEFREEFARGAEKNIKRAGLHEFWEVKIGDIRKDNPGVM 162
Cdd:COG2519   81 GYIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIREGIDEGD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249 163 ADAVSLDMPDPQLALDNIEAFLRPGGRISAYVPNTNQLADVVHGLEDRNYIEIDALENIQRRMEVHPGGVRPSFENLGHT 242
Cdd:COG2519  161 VDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALRESGFTDIEAVETLLREWKVEGLAVRPEHRMVGHT 240


                 ....*...
gi 553017249 243 GYLIFARK 250
Cdd:COG2519  241 GFLVFARK 248
 
Name Accession Description Interval E-value
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 4-250 1.12e-107

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 310.94  E-value: 1.12e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249   4 EGDLIYLLDSKGYRHWLTLGNGMVRVQGLGVVDSSKIIGQEDGYAL-SIAGKTFTALKPMIGDLMQSLERGPQIITPKDA 82
Cdd:COG2519    1 EGDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVtTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  83 ATIAFRLGLRAGETVVEAGVGSGALTMALINSVMPTGRVISMEFREEFARGAEKNIKRAGLHEFWEVKIGDIRKDNPGVM 162
Cdd:COG2519   81 GYIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIREGIDEGD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249 163 ADAVSLDMPDPQLALDNIEAFLRPGGRISAYVPNTNQLADVVHGLEDRNYIEIDALENIQRRMEVHPGGVRPSFENLGHT 242
Cdd:COG2519  161 VDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALRESGFTDIEAVETLLREWKVEGLAVRPEHRMVGHT 240


                 ....*...
gi 553017249 243 GYLIFARK 250
Cdd:COG2519  241 GFLVFARK 248
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 75-250 2.43e-27

tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase complex and is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.


Pssm-ID: 312288  Cd Length: 242  Bit Score: 105.27  E-value: 2.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249   75 QIITPKDAATIAFRLGLRAGETVVEAGVGSGALTMALINSVMPTGRVISMEFREEFARGAEKNIKRAGLHEFWEVKIGDI 154
Cdd:pfam08704  22 QILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADKAREEFREHGIDQLVTVTHRDV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  155 RKDN--PGV--MADAVSLDMPDPQLALDN-IEAFLRPGGRISAYVPNTNQLADVVHGLEDRNYIEIDALENIQRRMEV-- 227
Cdd:pfam08704 102 CKEGflTEVsgKADAVFLDLPSPWEAVPHaWKALKVEGGRFCSFSPCIEQVQRTCQALAELGFTEISTLEVLLRVYDVrt 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553017249  228 -----------HPGGV---------------------------RPSFENLGHTGYLIFARK 250
Cdd:pfam08704 182 vslpvidlgidREKENertrteglsnddksednsgnsmlgtalKPMSEAVGHTGYLTFATK 242
PRK08317 PRK08317
hypothetical protein; Provisional
 88-190 3.36e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.94  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  88 RLGLRAGETVVEAGVGSGALTMALINSVMPTGRVISMEFREEFARGAEKniKRAGLHEFWEVKIGDI-RKDNPGVMADAV 166
Cdd:PRK08317  14 LLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKE--RAAGLGPNVEFVRGDAdGLPFPDGSFDAV 91

                         90       100
                 ....*....|....*....|....*....
gi 553017249 167 SLD-----MPDPQLALDNIEAFLRPGGRI 190
Cdd:PRK08317  92 RSDrvlqhLEDPARALAEIARVLRPGGRV 120
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 96-190 1.31e-06

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: 45.88  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  96 TVVEAGVGSGALTMALINSvmPTGRVISMEFREEFARGAEKNiKRAGLHEFWEVKIGDIRKDNP-------GVMADAV-S 167
Cdd:cd02440    1 RVLDLGCGTGALALALASG--PGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELPPeadesfdVIISDPPlH 77

                         90       100
                 ....*....|....*....|...
gi 553017249 168 LDMPDPQLALDNIEAFLRPGGRI 190
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGGVL 100
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 89-190 2.97e-05

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 42.32  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249   89 LGLRAGETVVEAGVGSGALTMALINSVmPTGRVISMEFREEFARGAEKNIKRAGLHEFwEVKIGDIRKDNPGVM--ADAV 166
Cdd:TIGR02469  15 LRLRPGDVLWDIGAGTGSVTIEAARLV-PNGRVYAIERNPEALDLIERNLRRFGVSNI-VIVEGDAPEAPEALLpdPDAV 92

                          90       100
                  ....*....|....*....|....*.
gi 553017249  167 SLDMPDPQLA--LDNIEAFLRPGGRI 190
Cdd:TIGR02469  93 FVGGSGGLLQeiLEAVERRLRPGGRI 118
 
Name Accession Description Interval E-value
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 4-250 1.12e-107

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 310.94  E-value: 1.12e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249   4 EGDLIYLLDSKGYRHWLTLGNGMVRVQGLGVVDSSKIIGQEDGYAL-SIAGKTFTALKPMIGDLMQSLERGPQIITPKDA 82
Cdd:COG2519    1 EGDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVtTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  83 ATIAFRLGLRAGETVVEAGVGSGALTMALINSVMPTGRVISMEFREEFARGAEKNIKRAGLHEFWEVKIGDIRKDNPGVM 162
Cdd:COG2519   81 GYIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIREGIDEGD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249 163 ADAVSLDMPDPQLALDNIEAFLRPGGRISAYVPNTNQLADVVHGLEDRNYIEIDALENIQRRMEVHPGGVRPSFENLGHT 242
Cdd:COG2519  161 VDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALRESGFTDIEAVETLLREWKVEGLAVRPEHRMVGHT 240


                 ....*...
gi 553017249 243 GYLIFARK 250
Cdd:COG2519  241 GFLVFARK 248
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 75-250 2.43e-27

tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase complex and is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.


Pssm-ID: 312288  Cd Length: 242  Bit Score: 105.27  E-value: 2.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249   75 QIITPKDAATIAFRLGLRAGETVVEAGVGSGALTMALINSVMPTGRVISMEFREEFARGAEKNIKRAGLHEFWEVKIGDI 154
Cdd:pfam08704  22 QILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADKAREEFREHGIDQLVTVTHRDV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  155 RKDN--PGV--MADAVSLDMPDPQLALDN-IEAFLRPGGRISAYVPNTNQLADVVHGLEDRNYIEIDALENIQRRMEV-- 227
Cdd:pfam08704 102 CKEGflTEVsgKADAVFLDLPSPWEAVPHaWKALKVEGGRFCSFSPCIEQVQRTCQALAELGFTEISTLEVLLRVYDVrt 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553017249  228 -----------HPGGV---------------------------RPSFENLGHTGYLIFARK 250
Cdd:pfam08704 182 vslpvidlgidREKENertrteglsnddksednsgnsmlgtalKPMSEAVGHTGYLTFATK 242
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 88-190 2.13e-08

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: 51.92  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  88 RLGLRAGETVVEAGVGSGALTMALINSvmpTGRVISMEFREEFARGAEKNIKRAGLHefWEVKIGDIRK----DNP--GV 161
Cdd:COG2226   17 ALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDlpfpDGSfdLV 91

                         90       100
                 ....*....|....*....|....*....
gi 553017249 162 MADAVSLDMPDPQLALDNIEAFLRPGGRI 190
Cdd:COG2226   92 ISSFVLHHLPDPERALAEIARVLKPGGRL 120
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 85-195 6.08e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 50.70  E-value: 6.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  85 IAFRLGLRAGETVVEAGVGSG--ALTMALINSVmptgRVISMEFREEFARGAEKNIKRAGLHEFWEVKIGDIRKDNPGVM 162
Cdd:COG2230   43 ILRKLGLKPGMRVLDIGCGWGglALYLARRYGV----RVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQ 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 553017249 163 ADA-VSLDM----PDPQLA--LDNIEAFLRPGGRISAYVP 195
Cdd:COG2230  119 FDAiVSIGMfehvGPENYPayFAKVARLLKPGGRLLLHTP 158
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
89-219 1.39e-07

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 50.44  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249   89 LGLRAGETVVEAGVGSGALTMALINSVMPTGRVISMEFREEFARGAEKNIKRAGLHEFwEVKIGDIRKdnpGVMADA--- 165
Cdd:pfam01135  69 LELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLENV-IVVVGDGRQ---GWPEFApyd 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 553017249  166 ---VSLDMPD-PQLALDNieafLRPGGRISAYV-PNTNQLADVVHGLEDrNYIEIDALE 219
Cdd:pfam01135 145 aihVGAAAPEiPEALIDQ----LKEGGRLVIPVgPNGNQVLQQFDKRND-GSVVIKDLE 198
PRK08317 PRK08317
hypothetical protein; Provisional
 88-190 3.36e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.94  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  88 RLGLRAGETVVEAGVGSGALTMALINSVMPTGRVISMEFREEFARGAEKniKRAGLHEFWEVKIGDI-RKDNPGVMADAV 166
Cdd:PRK08317  14 LLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKE--RAAGLGPNVEFVRGDAdGLPFPDGSFDAV 91

                         90       100
                 ....*....|....*....|....*....
gi 553017249 167 SLD-----MPDPQLALDNIEAFLRPGGRI 190
Cdd:PRK08317  92 RSDrvlqhLEDPARALAEIARVLRPGGRV 120
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 96-190 1.31e-06

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: 45.88  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  96 TVVEAGVGSGALTMALINSvmPTGRVISMEFREEFARGAEKNiKRAGLHEFWEVKIGDIRKDNP-------GVMADAV-S 167
Cdd:cd02440    1 RVLDLGCGTGALALALASG--PGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELPPeadesfdVIISDPPlH 77

                         90       100
                 ....*....|....*....|...
gi 553017249 168 LDMPDPQLALDNIEAFLRPGGRI 190
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGGVL 100
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 91-190 1.75e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 46.64  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249   91 LRAGETVVEAGVGSGALTMALINSVMPTGRVISMEFREEFARGAEKNIKRAGLhEFWEVKIGDIRK------DNPG--VM 162
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEElpelleDDKFdvVI 79

                          90       100
                  ....*....|....*....|....*...
gi 553017249  163 ADAVSLDMPDPQLALDNIEAFLRPGGRI 190
Cdd:pfam13847  80 SNCVLNHIPDPDKVLQEILRVLKPGGRL 107
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 96-188 1.81e-06

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 46.72  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  96 TVVEAGVGSG--ALTMAlinSVMPT-GRVISMEFREEFARGAEKNIKRAGLHEFWEVKIGD----IRKDNPG----VMAD 164
Cdd:COG4122   19 RILEIGTGTGysTLWLA---RALPDdGRLTTIEIDPERAAIARENFARAGLADRIRLILGDalevLPRLADGpfdlVFID 95

                         90       100
                 ....*....|....*....|....
gi 553017249 165 AVSLDMPDpqlALDNIEAFLRPGG 188
Cdd:COG4122   96 ADKSNYPD---YLELALPLLRPGG 116
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 82-212 3.40e-06

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 47.47  E-value: 3.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  82 AATIAfRLGLRAGETVVEAGVGSGALT--MALInsvMPTGRVISMEFREEFARGAEKNIKRAGLhefWEVKIgdIRKDNP 159
Cdd:COG2242  237 ALTLA-KLALRPGDVLWDIGAGSGSVSieAARL---APGGRVYAIERDPERAALIRANARRFGV---PNVEV--VEGEAP 307

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553017249 160 GVMADavsLDMPD--------PQLA--LDNIEAFLRPGGRISAYVPNTNQLADVVHGLEDRNY 212
Cdd:COG2242  308 EALAD---LPDPDavfiggsgGNLPeiLEACWARLRPGGRLVANAVTLETLALALEALAELGY 367
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 91-196 9.20e-06

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: 43.85  E-value: 9.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  91 LRAGETVVEAGVGSGALTMALINSVMptgRVISMEFREEFARGAEKNIKRAGLHefweVKIGDIRK-DNPGVMADAV-SL 168
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALARRGA---DVTGVDISPEALEIARERAAELNVD----FVQGDLEDlPLEDGSFDLViCS 94

                         90       100       110
                 ....*....|....*....|....*....|..
gi 553017249 169 D----MPDPQLALDNIEAFLRPGGRISAYVPN 196
Cdd:COG2227   95 EvlehLPDPAALLRELARLLKPGGLLLLSTPN 126
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 71-190 2.38e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 44.14  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  71 ERGPQIITPKDAATIAFRLGLRAGETVVEAGVGSGALTMALINsvMPTGRVISMEFREEFARGAEKNIKRAGLHEFwEVK 150
Cdd:COG0500    4 SYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAA--RFGGRVIGIDLSPEAIALARARAAKAGLGNV-EFL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 553017249 151 IGDI--RKDNPGVMADAVSLDM------PDPQLA-LDNIEAFLRPGGRI 190
Cdd:COG0500   81 VADLaeLDPLPAESFDLVVAFGvlhhlpPEEREAlLRELARALKPGGVL 129
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 89-190 2.97e-05

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 42.32  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249   89 LGLRAGETVVEAGVGSGALTMALINSVmPTGRVISMEFREEFARGAEKNIKRAGLHEFwEVKIGDIRKDNPGVM--ADAV 166
Cdd:TIGR02469  15 LRLRPGDVLWDIGAGTGSVTIEAARLV-PNGRVYAIERNPEALDLIERNLRRFGVSNI-VIVEGDAPEAPEALLpdPDAV 92

                          90       100
                  ....*....|....*....|....*.
gi 553017249  167 SLDMPDPQLA--LDNIEAFLRPGGRI 190
Cdd:TIGR02469  93 FVGGSGGLLQeiLEAVERRLRPGGRI 118
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
93-190 3.19e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 41.73  E-value: 3.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  93 AGETVVEAGVGSGALTMALINSVmPTGRVISMEFREEFARGAEKNIKRAglhEFWEvkiGDIRKDNPGVMADAV----SL 168
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERF-PGARVTGVDLSPEMLARARARLPNV---RFVV---ADLRDLDPPEPFDLVvsnaAL 73

                         90       100
                 ....*....|....*....|...
gi 553017249 169 D-MPDPQLALDNIEAFLRPGGRI 190
Cdd:COG4106   74 HwLPDHAALLARLAAALAPGGVL 96
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 97-188 5.03e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 41.01  E-value: 5.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249   97 VVEAGVGSGALTMALINSVmpTGRVISMEFREEFARGAEKNIKRAGLHefWEVKIGDIRK-DNPGVMADAVS-------L 168
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG--GARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDlPFPDGSFDLVVssgvlhhL 76

                          90       100
                  ....*....|....*....|
gi 553017249  169 DMPDPQLALDNIEAFLRPGG 188
Cdd:pfam13649  77 PDPDLEAALREIARVLKPGG 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 98-190 2.96e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.89  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249   98 VEAGVGSGALTMALINSVmPTGRVISMEFREEFARGAEKNIKRAGLHEFWEVKIGDIRKDN-PGVMADAVSL-----DMP 171
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAL-PGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGElDPGSFDVVVAsnvlhHLA 79

                          90
                  ....*....|....*....
gi 553017249  172 DPQLALDNIEAFLRPGGRI 190
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 88-191 4.03e-04

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 41.04  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  88 RLGLRAGETVVEAGVG-SGALTMALiNSVMPTGRVISME---FREEFArgaekniKRAGLHEFWEVKIGD----IRKDNP 159
Cdd:cd08235  160 KAGIKPGDTVLVIGAGpIGLLHAML-AKASGARKVIVSDlneFRLEFA-------KKLGADYTIDAAEEDlvekVRELTD 231

                         90       100       110
                 ....*....|....*....|....*....|..
gi 553017249 160 GVMADAVSLDMPDPQLALDNIEAfLRPGGRIS 191
Cdd:cd08235  232 GRGADVVIVATGSPEAQAQALEL-VRKGGRIL 262
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
86-190 7.86e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 39.63  E-value: 7.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  86 AFRLGLRAGETVVEAGVGSGALTMalINSVMPTGRVISMEFREEFARGAEKNIKRAGLHEFWEVkigdirkdnpgVMADA 165
Cdd:COG4076   28 AIERVVKPGDVVLDIGTGSGLLSM--LAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITV-----------INADA 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 553017249 166 VSLDMPDP-----------------QLA--LDNIEAFLRPGGRI 190
Cdd:COG4076   95 TDLDLPEKadviisemldtalldegQVPilNHARKRLLKPGGRI 138
Methyltransf_3 pfam01596
O-methyltransferase; Members of this family are O-methyltransferases. The family includes ...
 73-156 2.41e-03

O-methyltransferase; Members of this family are O-methyltransferases. The family includes catechol o-methyltransferase, caffeoyl-CoA O-methyltransferase and a family of bacterial O-methyltransferases that may be involved in antibiotic production.


Pssm-ID: 396257 [Multi-domain]  Cd Length: 203  Bit Score: 37.86  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249   73 GPQIITPKDAAT-IAFRLGLRAGETVVEAGVGSG--ALTMALinSVMPTGRVISMEFREEFARGAEKNIKRAGLHEFWEV 149
Cdd:pfam01596  22 LAPMQVSPDEGQfLGMLVKLTGAKNVLEIGVFTGysALAMAL--ALPEDGKITAIDIDPEAYEIAKKFIQKAGVAHKISF 99


                  ....*..
gi 553017249  150 KIGDIRK 156
Cdd:pfam01596 100 ILGPALK 106
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 89-194 7.23e-03

16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 37.29  E-value: 7.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553017249  89 LGLRAGETVVEAGVGSGALTMALINSVMPTGRVISMEFREEFARGAEKNIKRAGLHEfWEVKIGDIRK--DNPGVMADAV 166
Cdd:COG0144  245 LDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRLKRLRENLARLGLSN-VEVVVADAREllEWLPGKFDRV 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 553017249 167 SLDMP---------DP-----------------QLA-LDNIEAFLRPGGRIsAYV 194
Cdd:COG0144  324 LLDAPcsgtgtlrrHPdikwrrtpediaelaalQRElLDAAARLLKPGGRL-VYS 377
 
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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