NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|257096002|ref|NP_001158032|]
View 

tRNA (guanine(26)-N(2))-dimethyltransferase isoform 2 [Mus musculus]

Protein Classification

tRNA (guanine(26)-N(2))-dimethyltransferase( domain architecture ID 10488069)

tRNA (guanine(26)-N(2))-dimethyltransferase dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine (SAM) as the methyl donor

EC:  2.1.1.216
Gene Symbol:  TRMT1
Gene Ontology:  GO:0008168|GO:1904047
SCOP:  4002351|3000118

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
TRM pfam02005
N2,N2-dimethylguanosine tRNA methyltransferase; This enzyme EC:2.1.1.32 used S-AdoMet to ...
58-492 2.94e-180

N2,N2-dimethylguanosine tRNA methyltransferase; This enzyme EC:2.1.1.32 used S-AdoMet to methylate tRNA. The TRM1 gene of Saccharomyces cerevisiae is necessary for the N2,N2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNAs. The enzyme is found in both eukaryotes and archaebacteria


:

Pssm-ID: 396545  Cd Length: 375  Bit Score: 516.16  E-value: 2.94e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002   58 IVFPSANEVFYNPVQEFNRDLTCAVITEFarihlGAKGIQIKVPgekdsekiavdlsdqeeetagknenlapgdwprtaa 137
Cdd:pfam02005  12 KTVSSKNPVFYNPRMEFNRDLSVLVIRQL-----NLLHKKLGRK------------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  138 vgeiceegLRVLEGLAASGLRSIRFALEVPGLQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQKape 217
Cdd:pfam02005  51 --------IKVLDALSASGIRAIRFALEVPGVEEVFANDISPKAVESIKENVKLNEVENIVVINGDDANAFMRENHR--- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  218 RFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHSLDLHANC 297
Cdd:pfam02005 120 RFDVIDLDPFGSPAPFLDSAVQSVKRGGLLCVTATDTAVLCGTYPKSCLRKYGARPLRTEFCHEVGLRILLGFVARLAAK 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  298 YQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCgafylqrlgKASGDPGGRIKFSaacgppvtPECE 377
Cdd:pfam02005 200 YEKALEPLLSYSIDHYVRVFVKVKRGAAKVDKVIEKLGYVYHCSGC---------LSREVVTGIAKFS--------AECP 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  378 HCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPGRFHTsmRIQGVLSVVTEELPDVPLYYTLDQLSSTIHCNTPRLLQL 457
Cdd:pfam02005 263 HCGGKFHLAGPLWLGPLHDKEFVEEVLEIAEKKEEEFSK--RVLGILKLIKEELLDVPGYYDLHQLASVLKLSVPPLQDV 340
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 257096002  458 RSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 492
Cdd:pfam02005 341 VSALKSAGFEVSRTHANPTGIKTNAPWEEVWEVMR 375
ZnF_C3H1 smart00356
zinc finger;
592-618 8.11e-06

zinc finger;


:

Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 42.62  E-value: 8.11e-06
                           10        20
                   ....*....|....*....|....*..
gi 257096002   592 RLKTFPCKRFKEGTCQLGDQCCYSHSP 618
Cdd:smart00356   1 KYKTELCKFFKRGYCPRGDRCKFAHPL 27
 
Name Accession Description Interval E-value
TRM pfam02005
N2,N2-dimethylguanosine tRNA methyltransferase; This enzyme EC:2.1.1.32 used S-AdoMet to ...
58-492 2.94e-180

N2,N2-dimethylguanosine tRNA methyltransferase; This enzyme EC:2.1.1.32 used S-AdoMet to methylate tRNA. The TRM1 gene of Saccharomyces cerevisiae is necessary for the N2,N2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNAs. The enzyme is found in both eukaryotes and archaebacteria


Pssm-ID: 396545  Cd Length: 375  Bit Score: 516.16  E-value: 2.94e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002   58 IVFPSANEVFYNPVQEFNRDLTCAVITEFarihlGAKGIQIKVPgekdsekiavdlsdqeeetagknenlapgdwprtaa 137
Cdd:pfam02005  12 KTVSSKNPVFYNPRMEFNRDLSVLVIRQL-----NLLHKKLGRK------------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  138 vgeiceegLRVLEGLAASGLRSIRFALEVPGLQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQKape 217
Cdd:pfam02005  51 --------IKVLDALSASGIRAIRFALEVPGVEEVFANDISPKAVESIKENVKLNEVENIVVINGDDANAFMRENHR--- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  218 RFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHSLDLHANC 297
Cdd:pfam02005 120 RFDVIDLDPFGSPAPFLDSAVQSVKRGGLLCVTATDTAVLCGTYPKSCLRKYGARPLRTEFCHEVGLRILLGFVARLAAK 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  298 YQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCgafylqrlgKASGDPGGRIKFSaacgppvtPECE 377
Cdd:pfam02005 200 YEKALEPLLSYSIDHYVRVFVKVKRGAAKVDKVIEKLGYVYHCSGC---------LSREVVTGIAKFS--------AECP 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  378 HCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPGRFHTsmRIQGVLSVVTEELPDVPLYYTLDQLSSTIHCNTPRLLQL 457
Cdd:pfam02005 263 HCGGKFHLAGPLWLGPLHDKEFVEEVLEIAEKKEEEFSK--RVLGILKLIKEELLDVPGYYDLHQLASVLKLSVPPLQDV 340
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 257096002  458 RSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 492
Cdd:pfam02005 341 VSALKSAGFEVSRTHANPTGIKTNAPWEEVWEVMR 375
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
47-492 3.34e-102

tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N,N-dimethylase Trm1 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441472  Cd Length: 383  Bit Score: 316.43  E-value: 3.34e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  47 PVATVTEGAAKIVFPSANE----------VFYNPVQEFNRDLTCAVItefarihlgakgiqikvpgekdsekiavdlsdq 116
Cdd:COG1867    2 DLMEITEGKVKILVPDPEKysrfepawapVFYNPRMELNRDISVAAL--------------------------------- 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 117 eeetagknenlapgdwprtAAVGEICEEGLRVLEGLAASGLRSIRFALEVpGLQsVVANDASARAVELMHRNVELNGVAH 196
Cdd:COG1867   49 -------------------RAYRERLKREISYLDALAASGIRGLRYALEV-GIK-VTLNDIDPEAVELIRENLELNGLED 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 197 lVQPNQADARMLMYQHqkaPERFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKS 276
Cdd:COG1867  108 -VEVYNRDANALLHEL---GRRFDVVDLDPFGSPAPFIDSALRAARKGGLLCVTATDTAPLCGAHPKSCIRRYGAVPLNT 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 277 RACHEMALRIVLHSLDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCGAFYLQRlgkasg 356
Cdd:COG1867  184 EYHHEMGLRILLGAIARTAARYDKGIEPLLSHATDHYVRVYLEVERGAKKADEALEELGYIYHCPSCLYREAEK------ 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 357 dpggrikfsaacGPPVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPgrFHTSMRIQGVLSVVTEELPDVPL 436
Cdd:COG1867  258 ------------GLLAHEECPLCGSELVTAGPLWLGPLHDKEFVEEMLEEADDLE--LGTAKRARKLLETLREELDIPPT 323
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 257096002 437 YYTLDQLSSTIHCNTPRLLQLRSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 492
Cdd:COG1867  324 YYDQHELCKRLKISAPSMDEFIEALREAGYKASRTHFSPTGFKTDAPLDEIREAIR 379
TRM1 TIGR00308
tRNA(guanine-26,N2-N2) methyltransferase; This enzyme is responsible for two methylations of a ...
51-497 2.20e-100

tRNA(guanine-26,N2-N2) methyltransferase; This enzyme is responsible for two methylations of a characteristic guanine of most tRNA molecules. The activity has been demonstrated for eukaryotic and archaeal proteins, which are active when expressed in E. coli, a species that lacks this enzyme. At least one Eubacterium, Aquifex aeolicus, has an ortholog, as do all completed archaeal genomes. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273006  Cd Length: 374  Bit Score: 311.39  E-value: 2.20e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002   51 VTEGAAKIVFPSANEVFYNPVQEFNRDLTCAVITEFARIHLGAKGIQIkvpgekdsekiavdlsdqeeetagknenlapg 130
Cdd:TIGR00308   1 VKEGKAEILVPKKETVFYNPRMQFNRDLSVTCIQAFDNLYGKECYINI-------------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  131 dwprtaavgeiceeglrvLEGLAASGLRSIRFALEVPGLQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMY 210
Cdd:TIGR00308  49 ------------------ADALSASGIRAIRYAHEIEGVREVFANDINPKAVESIKNNVEYNSVENIEVPNEDAANVLRY 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  211 QHQkapeRFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHS 290
Cdd:TIGR00308 111 RNR----KFHVIDIDPFGTPAPFVDSAIQASAERGLLLVTATDTSALCGNYPKSCLRKYGANPVKTESCHESALRLLLGF 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  291 LDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCgafylqrlgkASGDPGGRIKfsaacgp 370
Cdd:TIGR00308 187 VKRTAAKYEKALEPLLSHSIDHYVRVYVKVKRSAIRADKVMESTGYTYHCSRC----------LHNKPVNGIS------- 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  371 PVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNpgRFHTSMRIQGVLSVVTEELPDVPLYYTLDQLSSTIHCN 450
Cdd:TIGR00308 250 QRKGRCKECGGEYHLAGPLYAGPLHDKEFIEEVLRIAEEK--EYGTRKRVLKMLSLIKNELSDPPGYYSPHHIASVLKLS 327
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 257096002  451 TPRLLQLRSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMRCWEKE 497
Cdd:TIGR00308 328 VPPLKDVVAGLKSLGFEASRTHYQPSGIKTDAPWDAIWEVLQKCDDE 374
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
50-492 3.52e-92

N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional


Pssm-ID: 235286  Cd Length: 382  Bit Score: 290.28  E-value: 3.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  50 TVTEGAAKIVFPSAN-------------EVFYNPVQEFNRDLTCAVITEFarihlgakgiqikvpGEKDSEkiavdlsdq 116
Cdd:PRK04338   3 IITEGKVKIEVPDPStyskdgkfppswaPVFYNPRMELNRDISVLVLRAF---------------GPKLPR--------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 117 eeetagknenlapgdwprtaavgeiceegLRVLEGLAASGLRSIRFALEVPGLQsVVANDASARAVELMHRNVELNGVAH 196
Cdd:PRK04338  59 -----------------------------ESVLDALSASGIRGIRYALETGVEK-VTLNDINPDAVELIKKNLELNGLEN 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 197 LVQPNQaDARMLMYQHQKaperFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKS 276
Cdd:PRK04338 109 EKVFNK-DANALLHEERK----FDVVDIDPFGSPAPFLDSAIRSVKRGGLLCVTATDTAPLCGAYPKSCLRKYGAVPLKT 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 277 RACHEMALRIVLHSLDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCGafylqrlgkasg 356
Cdd:PRK04338 184 EFYHEMGLRILIGYIAREAAKYDKGLEPLFSHSTDHYYRVFLKVERGAKKADKALENLGYVYYCPKCL------------ 251
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 357 dpggriKFSAACGPPVTpECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPGrfhTSMRIQGVLSVVTEELP-DVP 435
Cdd:PRK04338 252 ------YREEVEGLPPE-ECPVCGGKFGTAGPLWLGPLHDKEFVEEMLEEAAKELG---TSKKALKLLKTIEEESKlDTP 321
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 257096002 436 LYYTLDQLSSTIHCNTPRLLQLRSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 492
Cdd:PRK04338 322 TFYDLHELAKKLKVSAPPMDEILEALREAGFEASRTHFSPTGFKTDAPYDEIKEAIK 378
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
147-251 7.01e-07

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 48.20  E-value: 7.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 147 RVLEGLAASGLRSIRFALEVPGlqSVVANDASARAVELMhRNVELNGVAHLVQPNQADARMLmyqHQKAPERFDVIDLDP 226
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGA--RVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEEL---PPEADESFDVIISDP 74
                         90       100       110
                 ....*....|....*....|....*....|
gi 257096002 227 Y-----GSPAPFLDAAVQAVSDGGLLCVTC 251
Cdd:cd02440   75 PlhhlvEDLARFLEEARRLLKPGGVLVLTL 104
ZnF_C3H1 smart00356
zinc finger;
592-618 8.11e-06

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 42.62  E-value: 8.11e-06
                           10        20
                   ....*....|....*....|....*..
gi 257096002   592 RLKTFPCKRFKEGTCQLGDQCCYSHSP 618
Cdd:smart00356   1 KYKTELCKFFKRGYCPRGDRCKFAHPL 27
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
594-618 1.12e-04

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 39.48  E-value: 1.12e-04
                          10        20
                  ....*....|....*....|....*.
gi 257096002  594 KTFPCKRFKE-GTCQLGDQCCYSHSP 618
Cdd:pfam00642   2 KTELCRFFLRtGYCKYGDRCKFAHGQ 27
 
Name Accession Description Interval E-value
TRM pfam02005
N2,N2-dimethylguanosine tRNA methyltransferase; This enzyme EC:2.1.1.32 used S-AdoMet to ...
58-492 2.94e-180

N2,N2-dimethylguanosine tRNA methyltransferase; This enzyme EC:2.1.1.32 used S-AdoMet to methylate tRNA. The TRM1 gene of Saccharomyces cerevisiae is necessary for the N2,N2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNAs. The enzyme is found in both eukaryotes and archaebacteria


Pssm-ID: 396545  Cd Length: 375  Bit Score: 516.16  E-value: 2.94e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002   58 IVFPSANEVFYNPVQEFNRDLTCAVITEFarihlGAKGIQIKVPgekdsekiavdlsdqeeetagknenlapgdwprtaa 137
Cdd:pfam02005  12 KTVSSKNPVFYNPRMEFNRDLSVLVIRQL-----NLLHKKLGRK------------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  138 vgeiceegLRVLEGLAASGLRSIRFALEVPGLQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQKape 217
Cdd:pfam02005  51 --------IKVLDALSASGIRAIRFALEVPGVEEVFANDISPKAVESIKENVKLNEVENIVVINGDDANAFMRENHR--- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  218 RFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHSLDLHANC 297
Cdd:pfam02005 120 RFDVIDLDPFGSPAPFLDSAVQSVKRGGLLCVTATDTAVLCGTYPKSCLRKYGARPLRTEFCHEVGLRILLGFVARLAAK 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  298 YQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCgafylqrlgKASGDPGGRIKFSaacgppvtPECE 377
Cdd:pfam02005 200 YEKALEPLLSYSIDHYVRVFVKVKRGAAKVDKVIEKLGYVYHCSGC---------LSREVVTGIAKFS--------AECP 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  378 HCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPGRFHTsmRIQGVLSVVTEELPDVPLYYTLDQLSSTIHCNTPRLLQL 457
Cdd:pfam02005 263 HCGGKFHLAGPLWLGPLHDKEFVEEVLEIAEKKEEEFSK--RVLGILKLIKEELLDVPGYYDLHQLASVLKLSVPPLQDV 340
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 257096002  458 RSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 492
Cdd:pfam02005 341 VSALKSAGFEVSRTHANPTGIKTNAPWEEVWEVMR 375
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
47-492 3.34e-102

tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N,N-dimethylase Trm1 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441472  Cd Length: 383  Bit Score: 316.43  E-value: 3.34e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  47 PVATVTEGAAKIVFPSANE----------VFYNPVQEFNRDLTCAVItefarihlgakgiqikvpgekdsekiavdlsdq 116
Cdd:COG1867    2 DLMEITEGKVKILVPDPEKysrfepawapVFYNPRMELNRDISVAAL--------------------------------- 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 117 eeetagknenlapgdwprtAAVGEICEEGLRVLEGLAASGLRSIRFALEVpGLQsVVANDASARAVELMHRNVELNGVAH 196
Cdd:COG1867   49 -------------------RAYRERLKREISYLDALAASGIRGLRYALEV-GIK-VTLNDIDPEAVELIRENLELNGLED 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 197 lVQPNQADARMLMYQHqkaPERFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKS 276
Cdd:COG1867  108 -VEVYNRDANALLHEL---GRRFDVVDLDPFGSPAPFIDSALRAARKGGLLCVTATDTAPLCGAHPKSCIRRYGAVPLNT 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 277 RACHEMALRIVLHSLDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCGAFYLQRlgkasg 356
Cdd:COG1867  184 EYHHEMGLRILLGAIARTAARYDKGIEPLLSHATDHYVRVYLEVERGAKKADEALEELGYIYHCPSCLYREAEK------ 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 357 dpggrikfsaacGPPVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPgrFHTSMRIQGVLSVVTEELPDVPL 436
Cdd:COG1867  258 ------------GLLAHEECPLCGSELVTAGPLWLGPLHDKEFVEEMLEEADDLE--LGTAKRARKLLETLREELDIPPT 323
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 257096002 437 YYTLDQLSSTIHCNTPRLLQLRSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 492
Cdd:COG1867  324 YYDQHELCKRLKISAPSMDEFIEALREAGYKASRTHFSPTGFKTDAPLDEIREAIR 379
TRM1 TIGR00308
tRNA(guanine-26,N2-N2) methyltransferase; This enzyme is responsible for two methylations of a ...
51-497 2.20e-100

tRNA(guanine-26,N2-N2) methyltransferase; This enzyme is responsible for two methylations of a characteristic guanine of most tRNA molecules. The activity has been demonstrated for eukaryotic and archaeal proteins, which are active when expressed in E. coli, a species that lacks this enzyme. At least one Eubacterium, Aquifex aeolicus, has an ortholog, as do all completed archaeal genomes. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273006  Cd Length: 374  Bit Score: 311.39  E-value: 2.20e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002   51 VTEGAAKIVFPSANEVFYNPVQEFNRDLTCAVITEFARIHLGAKGIQIkvpgekdsekiavdlsdqeeetagknenlapg 130
Cdd:TIGR00308   1 VKEGKAEILVPKKETVFYNPRMQFNRDLSVTCIQAFDNLYGKECYINI-------------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  131 dwprtaavgeiceeglrvLEGLAASGLRSIRFALEVPGLQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMY 210
Cdd:TIGR00308  49 ------------------ADALSASGIRAIRYAHEIEGVREVFANDINPKAVESIKNNVEYNSVENIEVPNEDAANVLRY 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  211 QHQkapeRFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHS 290
Cdd:TIGR00308 111 RNR----KFHVIDIDPFGTPAPFVDSAIQASAERGLLLVTATDTSALCGNYPKSCLRKYGANPVKTESCHESALRLLLGF 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  291 LDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCgafylqrlgkASGDPGGRIKfsaacgp 370
Cdd:TIGR00308 187 VKRTAAKYEKALEPLLSHSIDHYVRVYVKVKRSAIRADKVMESTGYTYHCSRC----------LHNKPVNGIS------- 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  371 PVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNpgRFHTSMRIQGVLSVVTEELPDVPLYYTLDQLSSTIHCN 450
Cdd:TIGR00308 250 QRKGRCKECGGEYHLAGPLYAGPLHDKEFIEEVLRIAEEK--EYGTRKRVLKMLSLIKNELSDPPGYYSPHHIASVLKLS 327
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 257096002  451 TPRLLQLRSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMRCWEKE 497
Cdd:TIGR00308 328 VPPLKDVVAGLKSLGFEASRTHYQPSGIKTDAPWDAIWEVLQKCDDE 374
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
50-492 3.52e-92

N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional


Pssm-ID: 235286  Cd Length: 382  Bit Score: 290.28  E-value: 3.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  50 TVTEGAAKIVFPSAN-------------EVFYNPVQEFNRDLTCAVITEFarihlgakgiqikvpGEKDSEkiavdlsdq 116
Cdd:PRK04338   3 IITEGKVKIEVPDPStyskdgkfppswaPVFYNPRMELNRDISVLVLRAF---------------GPKLPR--------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 117 eeetagknenlapgdwprtaavgeiceegLRVLEGLAASGLRSIRFALEVPGLQsVVANDASARAVELMHRNVELNGVAH 196
Cdd:PRK04338  59 -----------------------------ESVLDALSASGIRGIRYALETGVEK-VTLNDINPDAVELIKKNLELNGLEN 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 197 LVQPNQaDARMLMYQHQKaperFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKS 276
Cdd:PRK04338 109 EKVFNK-DANALLHEERK----FDVVDIDPFGSPAPFLDSAIRSVKRGGLLCVTATDTAPLCGAYPKSCLRKYGAVPLKT 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 277 RACHEMALRIVLHSLDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCGafylqrlgkasg 356
Cdd:PRK04338 184 EFYHEMGLRILIGYIAREAAKYDKGLEPLFSHSTDHYYRVFLKVERGAKKADKALENLGYVYYCPKCL------------ 251
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 357 dpggriKFSAACGPPVTpECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPGrfhTSMRIQGVLSVVTEELP-DVP 435
Cdd:PRK04338 252 ------YREEVEGLPPE-ECPVCGGKFGTAGPLWLGPLHDKEFVEEMLEEAAKELG---TSKKALKLLKTIEEESKlDTP 321
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 257096002 436 LYYTLDQLSSTIHCNTPRLLQLRSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 492
Cdd:PRK04338 322 TFYDLHELAKKLKVSAPPMDEILEALREAGFEASRTHFSPTGFKTDAPYDEIKEAIK 378
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
171-252 1.26e-09

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 60.58  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 171 SVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQKAPERFDVIDLDPygsPApF-------LDA------- 236
Cdd:COG1092  241 SVTSVDLSATALEWAKENAALNGLDDRHEFVQADAFDWLRELAREGERFDLIILDP---PA-FakskkdlFDAqrdykdl 316
                         90
                 ....*....|....*....
gi 257096002 237 ---AVQAVSDGGLLcVTCT 252
Cdd:COG1092  317 nrlALKLLAPGGIL-VTSS 334
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
138-247 4.05e-08

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 55.64  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 138 VGEICEEGLRVLEGLAASGLRSIRFALEVPGLqsVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQkapE 217
Cdd:COG2520  174 IAELVKPGERVLDMFAGVGPFSIPIAKRSGAK--VVAIDINPDAVEYLKENIRLNKVEDRVTPILGDAREVAPELE---G 248
                         90       100       110
                 ....*....|....*....|....*....|..
gi 257096002 218 RFD--VIDLdPYGSPApFLDAAVQAVSDGGLL 247
Cdd:COG2520  249 KADriIMNL-PHSADE-FLDAALRALKPGGVI 278
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
147-251 7.01e-07

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 48.20  E-value: 7.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 147 RVLEGLAASGLRSIRFALEVPGlqSVVANDASARAVELMhRNVELNGVAHLVQPNQADARMLmyqHQKAPERFDVIDLDP 226
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGA--RVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEEL---PPEADESFDVIISDP 74
                         90       100       110
                 ....*....|....*....|....*....|
gi 257096002 227 Y-----GSPAPFLDAAVQAVSDGGLLCVTC 251
Cdd:cd02440   75 PlhhlvEDLARFLEEARRLLKPGGVLVLTL 104
ZnF_C3H1 smart00356
zinc finger;
592-618 8.11e-06

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 42.62  E-value: 8.11e-06
                           10        20
                   ....*....|....*....|....*..
gi 257096002   592 RLKTFPCKRFKEGTCQLGDQCCYSHSP 618
Cdd:smart00356   1 KYKTELCKFFKRGYCPRGDRCKFAHPL 27
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
144-247 1.12e-05

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 46.23  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002 144 EGLRVLEGLAASGlrsirfALevpGL-------QSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMyqHQKAP 216
Cdd:COG0742   41 EGARVLDLFAGSG------AL---GLealsrgaASVVFVEKDRKAAAVIRKNLEKLGLEDRARVIRGDALRFL--KRLAG 109
                         90       100       110
                 ....*....|....*....|....*....|..
gi 257096002 217 ERFDVIDLD-PYGSpaPFLDAAVQAVSDGGLL 247
Cdd:COG0742  110 EPFDLVFLDpPYAK--GLLEKALELLAENGLL 139
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
594-618 1.12e-04

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 39.48  E-value: 1.12e-04
                          10        20
                  ....*....|....*....|....*.
gi 257096002  594 KTFPCKRFKE-GTCQLGDQCCYSHSP 618
Cdd:pfam00642   2 KTELCRFFLRtGYCKYGDRCKFAHGQ 27
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
143-248 3.27e-04

Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of unknown function, Swiss:O27901. However, homologous proteins have been found in yeast suggesting this protein may be involved in methionine biosynthesis, transport and/or utilization.


Pssm-ID: 396850 [Multi-domain]  Cd Length: 198  Bit Score: 42.34  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096002  143 EEGLRVLEGLAASGLRSIRFALEVPGlQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQkaperFDVI 222
Cdd:pfam02475  98 EPGEVVVDMFAGIGPFSIPIAKHSKA-RRVYAIELNPESYKYLKENIKLNKVEDVVKPILGDVREVILEDV-----ADRV 171
                          90       100
                  ....*....|....*....|....*.
gi 257096002  223 DLDPYGSPAPFLDAAVQAVSDGGLLC 248
Cdd:pfam02475 172 VMNLPGSAHEFLDKAFAAVRDGGVIH 197
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
159-222 2.35e-03

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: 39.79  E-value: 2.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257096002 159 SIRFALEVPGLQsVVANDASARAVELMHRNVELNGV--AHLVQPNQADARmlmyqhqkAPERFDVI 222
Cdd:COG2813   64 GLALAKRNPEAR-VTLVDVNARAVELARANAAANGLenVEVLWSDGLSGV--------PDGSFDLI 120
 
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