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Conserved domains on  [gi|1398589758|ref|NP_001351105|]
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tRNA (guanine(26)-N(2))-dimethyltransferase isoform 4 [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

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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 ...
40-474 1.91e-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: 515.78  E-value: 1.91e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  40 IVFPSANEVFYNPVQEFNRDLTCAVITEfarihLGAKGIQIKVPgekdsekiavdlsdqeeetagknenlapgdwprtaa 119
Cdd:pfam02005  12 KTVSSKNPVFYNPRMEFNRDLSVLVIRQ-----LNLLHKKLGRK------------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 120 vgeiceegLRVLEGLAASGLRSIRFALEVPGLQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQKape 199
Cdd:pfam02005  51 --------IKVLDALSASGIRAIRFALEVPGVEEVFANDISPKAVESIKENVKLNEVENIVVINGDDANAFMRENHR--- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 200 RFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHSLDLHANC 279
Cdd:pfam02005 120 RFDVIDLDPFGSPAPFLDSAVQSVKRGGLLCVTATDTAVLCGTYPKSCLRKYGARPLRTEFCHEVGLRILLGFVARLAAK 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 280 YQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCgafylqrlgKASGDPGGRIKFSaacgppvtPECE 359
Cdd:pfam02005 200 YEKALEPLLSYSIDHYVRVFVKVKRGAAKVDKVIEKLGYVYHCSGC---------LSREVVTGIAKFS--------AECP 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 360 HCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPGRFHTsmRIQGVLSVVTEELPDVPLYYTLDQLSSTIHCNTPRLLQL 439
Cdd:pfam02005 263 HCGGKFHLAGPLWLGPLHDKEFVEEVLEIAEKKEEEFSK--RVLGILKLIKEELLDVPGYYDLHQLASVLKLSVPPLQDV 340
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1398589758 440 RSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 474
Cdd:pfam02005 341 VSALKSAGFEVSRTHANPTGIKTNAPWEEVWEVMR 375
ZnF_C3H1 smart00356
zinc finger;
574-600 6.36e-06

zinc finger;


:

Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 43.00  E-value: 6.36e-06
                           10        20
                   ....*....|....*....|....*..
gi 1398589758  574 RLKTFPCKRFKEGTCQLGDQCCYSHSP 600
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 ...
40-474 1.91e-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: 515.78  E-value: 1.91e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  40 IVFPSANEVFYNPVQEFNRDLTCAVITEfarihLGAKGIQIKVPgekdsekiavdlsdqeeetagknenlapgdwprtaa 119
Cdd:pfam02005  12 KTVSSKNPVFYNPRMEFNRDLSVLVIRQ-----LNLLHKKLGRK------------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 120 vgeiceegLRVLEGLAASGLRSIRFALEVPGLQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQKape 199
Cdd:pfam02005  51 --------IKVLDALSASGIRAIRFALEVPGVEEVFANDISPKAVESIKENVKLNEVENIVVINGDDANAFMRENHR--- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 200 RFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHSLDLHANC 279
Cdd:pfam02005 120 RFDVIDLDPFGSPAPFLDSAVQSVKRGGLLCVTATDTAVLCGTYPKSCLRKYGARPLRTEFCHEVGLRILLGFVARLAAK 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 280 YQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCgafylqrlgKASGDPGGRIKFSaacgppvtPECE 359
Cdd:pfam02005 200 YEKALEPLLSYSIDHYVRVFVKVKRGAAKVDKVIEKLGYVYHCSGC---------LSREVVTGIAKFS--------AECP 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 360 HCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPGRFHTsmRIQGVLSVVTEELPDVPLYYTLDQLSSTIHCNTPRLLQL 439
Cdd:pfam02005 263 HCGGKFHLAGPLWLGPLHDKEFVEEVLEIAEKKEEEFSK--RVLGILKLIKEELLDVPGYYDLHQLASVLKLSVPPLQDV 340
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1398589758 440 RSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 474
Cdd:pfam02005 341 VSALKSAGFEVSRTHANPTGIKTNAPWEEVWEVMR 375
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
29-474 1.79e-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: 1.79e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  29 PVATVTEGAAKIVFPSANE----------VFYNPVQEFNRDLTCAVItefarihlgakgiqikvpgekdsekiavdlsdq 98
Cdd:COG1867     2 DLMEITEGKVKILVPDPEKysrfepawapVFYNPRMELNRDISVAAL--------------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  99 eeetagknenlapgdwprtAAVGEICEEGLRVLEGLAASGLRSIRFALEVpGLQsVVANDASARAVELMHRNVELNGVAH 178
Cdd:COG1867    49 -------------------RAYRERLKREISYLDALAASGIRGLRYALEV-GIK-VTLNDIDPEAVELIRENLELNGLED 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 179 lVQPNQADARMLMYQHqkaPERFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKS 258
Cdd:COG1867   108 -VEVYNRDANALLHEL---GRRFDVVDLDPFGSPAPFIDSALRAARKGGLLCVTATDTAPLCGAHPKSCIRRYGAVPLNT 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 259 RACHEMALRIVLHSLDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCGAFYLQRlgkasg 338
Cdd:COG1867   184 EYHHEMGLRILLGAIARTAARYDKGIEPLLSHATDHYVRVYLEVERGAKKADEALEELGYIYHCPSCLYREAEK------ 257
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 339 dpggrikfsaacGPPVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPgrFHTSMRIQGVLSVVTEELPDVPL 418
Cdd:COG1867   258 ------------GLLAHEECPLCGSELVTAGPLWLGPLHDKEFVEEMLEEADDLE--LGTAKRARKLLETLREELDIPPT 323
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398589758 419 YYTLDQLSSTIHCNTPRLLQLRSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 474
Cdd:COG1867   324 YYDQHELCKRLKISAPSMDEFIEALREAGYKASRTHFSPTGFKTDAPLDEIREAIR 379
TRM1 TIGR00308
tRNA(guanine-26,N2-N2) methyltransferase; This enzyme is responsible for two methylations of a ...
33-479 1.80e-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: 311.01  E-value: 1.80e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  33 VTEGAAKIVFPSANEVFYNPVQEFNRDLTCAVITEFARIHLGAKGIQIkvpgekdsekiavdlsdqeeetagknenlapg 112
Cdd:TIGR00308   1 VKEGKAEILVPKKETVFYNPRMQFNRDLSVTCIQAFDNLYGKECYINI-------------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 113 dwprtaavgeiceeglrvLEGLAASGLRSIRFALEVPGLQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMY 192
Cdd:TIGR00308  49 ------------------ADALSASGIRAIRYAHEIEGVREVFANDINPKAVESIKNNVEYNSVENIEVPNEDAANVLRY 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 193 QHQkapeRFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHS 272
Cdd:TIGR00308 111 RNR----KFHVIDIDPFGTPAPFVDSAIQASAERGLLLVTATDTSALCGNYPKSCLRKYGANPVKTESCHESALRLLLGF 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 273 LDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCgafylqrlgkASGDPGGRIKfsaacgp 352
Cdd:TIGR00308 187 VKRTAAKYEKALEPLLSHSIDHYVRVYVKVKRSAIRADKVMESTGYTYHCSRC----------LHNKPVNGIS------- 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 353 PVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNpgRFHTSMRIQGVLSVVTEELPDVPLYYTLDQLSSTIHCN 432
Cdd:TIGR00308 250 QRKGRCKECGGEYHLAGPLYAGPLHDKEFIEEVLRIAEEK--EYGTRKRVLKMLSLIKNELSDPPGYYSPHHIASVLKLS 327
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1398589758 433 TPRLLQLRSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMRCWEKE 479
Cdd:TIGR00308 328 VPPLKDVVAGLKSLGFEASRTHYQPSGIKTDAPWDAIWEVLQKCDDE 374
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
32-474 3.08e-92

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


Pssm-ID: 235286  Cd Length: 382  Bit Score: 289.89  E-value: 3.08e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  32 TVTEGAAKIVFPSAN-------------EVFYNPVQEFNRDLTCAVITEFarihlgakgiqikvpGEKDSEkiavdlsdq 98
Cdd:PRK04338    3 IITEGKVKIEVPDPStyskdgkfppswaPVFYNPRMELNRDISVLVLRAF---------------GPKLPR--------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  99 eeetagknenlapgdwprtaavgeiceegLRVLEGLAASGLRSIRFALEVPGLQsVVANDASARAVELMHRNVELNGVAH 178
Cdd:PRK04338   59 -----------------------------ESVLDALSASGIRGIRYALETGVEK-VTLNDINPDAVELIKKNLELNGLEN 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 179 LVQPNQaDARMLMYQHQKaperFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKS 258
Cdd:PRK04338  109 EKVFNK-DANALLHEERK----FDVVDIDPFGSPAPFLDSAIRSVKRGGLLCVTATDTAPLCGAYPKSCLRKYGAVPLKT 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 259 RACHEMALRIVLHSLDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCGafylqrlgkasg 338
Cdd:PRK04338  184 EFYHEMGLRILIGYIAREAAKYDKGLEPLFSHSTDHYYRVFLKVERGAKKADKALENLGYVYYCPKCL------------ 251
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 339 dpggriKFSAACGPPVTpECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPGrfhTSMRIQGVLSVVTEELP-DVP 417
Cdd:PRK04338  252 ------YREEVEGLPPE-ECPVCGGKFGTAGPLWLGPLHDKEFVEEMLEEAAKELG---TSKKALKLLKTIEEESKlDTP 321
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1398589758 418 LYYTLDQLSSTIHCNTPRLLQLRSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 474
Cdd:PRK04338  322 TFYDLHELAKKLKVSAPPMDEILEALREAGFEASRTHFSPTGFKTDAPYDEIKEAIK 378
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
129-233 6.80e-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: 6.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 129 RVLEGLAASGLRSIRFALEVPGlqSVVANDASARAVELMhRNVELNGVAHLVQPNQADARMLmyqHQKAPERFDVIDLDP 208
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGA--RVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEEL---PPEADESFDVIISDP 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 1398589758 209 Y-----GSPAPFLDAAVQAVSDGGLLCVTC 233
Cdd:cd02440    75 PlhhlvEDLARFLEEARRLLKPGGVLVLTL 104
ZnF_C3H1 smart00356
zinc finger;
574-600 6.36e-06

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 43.00  E-value: 6.36e-06
                           10        20
                   ....*....|....*....|....*..
gi 1398589758  574 RLKTFPCKRFKEGTCQLGDQCCYSHSP 600
Cdd:smart00356   1 KYKTELCKFFKRGYCPRGDRCKFAHPL 27
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
576-600 8.59e-05

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 39.87  E-value: 8.59e-05
                          10        20
                  ....*....|....*....|....*.
gi 1398589758 576 KTFPCKRFKE-GTCQLGDQCCYSHSP 600
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 ...
40-474 1.91e-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: 515.78  E-value: 1.91e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  40 IVFPSANEVFYNPVQEFNRDLTCAVITEfarihLGAKGIQIKVPgekdsekiavdlsdqeeetagknenlapgdwprtaa 119
Cdd:pfam02005  12 KTVSSKNPVFYNPRMEFNRDLSVLVIRQ-----LNLLHKKLGRK------------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 120 vgeiceegLRVLEGLAASGLRSIRFALEVPGLQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQKape 199
Cdd:pfam02005  51 --------IKVLDALSASGIRAIRFALEVPGVEEVFANDISPKAVESIKENVKLNEVENIVVINGDDANAFMRENHR--- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 200 RFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHSLDLHANC 279
Cdd:pfam02005 120 RFDVIDLDPFGSPAPFLDSAVQSVKRGGLLCVTATDTAVLCGTYPKSCLRKYGARPLRTEFCHEVGLRILLGFVARLAAK 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 280 YQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCgafylqrlgKASGDPGGRIKFSaacgppvtPECE 359
Cdd:pfam02005 200 YEKALEPLLSYSIDHYVRVFVKVKRGAAKVDKVIEKLGYVYHCSGC---------LSREVVTGIAKFS--------AECP 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 360 HCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPGRFHTsmRIQGVLSVVTEELPDVPLYYTLDQLSSTIHCNTPRLLQL 439
Cdd:pfam02005 263 HCGGKFHLAGPLWLGPLHDKEFVEEVLEIAEKKEEEFSK--RVLGILKLIKEELLDVPGYYDLHQLASVLKLSVPPLQDV 340
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1398589758 440 RSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 474
Cdd:pfam02005 341 VSALKSAGFEVSRTHANPTGIKTNAPWEEVWEVMR 375
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
29-474 1.79e-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: 1.79e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  29 PVATVTEGAAKIVFPSANE----------VFYNPVQEFNRDLTCAVItefarihlgakgiqikvpgekdsekiavdlsdq 98
Cdd:COG1867     2 DLMEITEGKVKILVPDPEKysrfepawapVFYNPRMELNRDISVAAL--------------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  99 eeetagknenlapgdwprtAAVGEICEEGLRVLEGLAASGLRSIRFALEVpGLQsVVANDASARAVELMHRNVELNGVAH 178
Cdd:COG1867    49 -------------------RAYRERLKREISYLDALAASGIRGLRYALEV-GIK-VTLNDIDPEAVELIRENLELNGLED 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 179 lVQPNQADARMLMYQHqkaPERFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKS 258
Cdd:COG1867   108 -VEVYNRDANALLHEL---GRRFDVVDLDPFGSPAPFIDSALRAARKGGLLCVTATDTAPLCGAHPKSCIRRYGAVPLNT 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 259 RACHEMALRIVLHSLDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCGAFYLQRlgkasg 338
Cdd:COG1867   184 EYHHEMGLRILLGAIARTAARYDKGIEPLLSHATDHYVRVYLEVERGAKKADEALEELGYIYHCPSCLYREAEK------ 257
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 339 dpggrikfsaacGPPVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPgrFHTSMRIQGVLSVVTEELPDVPL 418
Cdd:COG1867   258 ------------GLLAHEECPLCGSELVTAGPLWLGPLHDKEFVEEMLEEADDLE--LGTAKRARKLLETLREELDIPPT 323
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398589758 419 YYTLDQLSSTIHCNTPRLLQLRSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 474
Cdd:COG1867   324 YYDQHELCKRLKISAPSMDEFIEALREAGYKASRTHFSPTGFKTDAPLDEIREAIR 379
TRM1 TIGR00308
tRNA(guanine-26,N2-N2) methyltransferase; This enzyme is responsible for two methylations of a ...
33-479 1.80e-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: 311.01  E-value: 1.80e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  33 VTEGAAKIVFPSANEVFYNPVQEFNRDLTCAVITEFARIHLGAKGIQIkvpgekdsekiavdlsdqeeetagknenlapg 112
Cdd:TIGR00308   1 VKEGKAEILVPKKETVFYNPRMQFNRDLSVTCIQAFDNLYGKECYINI-------------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 113 dwprtaavgeiceeglrvLEGLAASGLRSIRFALEVPGLQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMY 192
Cdd:TIGR00308  49 ------------------ADALSASGIRAIRYAHEIEGVREVFANDINPKAVESIKNNVEYNSVENIEVPNEDAANVLRY 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 193 QHQkapeRFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIVLHS 272
Cdd:TIGR00308 111 RNR----KFHVIDIDPFGTPAPFVDSAIQASAERGLLLVTATDTSALCGNYPKSCLRKYGANPVKTESCHESALRLLLGF 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 273 LDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCgafylqrlgkASGDPGGRIKfsaacgp 352
Cdd:TIGR00308 187 VKRTAAKYEKALEPLLSHSIDHYVRVYVKVKRSAIRADKVMESTGYTYHCSRC----------LHNKPVNGIS------- 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 353 PVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNpgRFHTSMRIQGVLSVVTEELPDVPLYYTLDQLSSTIHCN 432
Cdd:TIGR00308 250 QRKGRCKECGGEYHLAGPLYAGPLHDKEFIEEVLRIAEEK--EYGTRKRVLKMLSLIKNELSDPPGYYSPHHIASVLKLS 327
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1398589758 433 TPRLLQLRSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMRCWEKE 479
Cdd:TIGR00308 328 VPPLKDVVAGLKSLGFEASRTHYQPSGIKTDAPWDAIWEVLQKCDDE 374
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
32-474 3.08e-92

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


Pssm-ID: 235286  Cd Length: 382  Bit Score: 289.89  E-value: 3.08e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  32 TVTEGAAKIVFPSAN-------------EVFYNPVQEFNRDLTCAVITEFarihlgakgiqikvpGEKDSEkiavdlsdq 98
Cdd:PRK04338    3 IITEGKVKIEVPDPStyskdgkfppswaPVFYNPRMELNRDISVLVLRAF---------------GPKLPR--------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758  99 eeetagknenlapgdwprtaavgeiceegLRVLEGLAASGLRSIRFALEVPGLQsVVANDASARAVELMHRNVELNGVAH 178
Cdd:PRK04338   59 -----------------------------ESVLDALSASGIRGIRYALETGVEK-VTLNDINPDAVELIKKNLELNGLEN 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 179 LVQPNQaDARMLMYQHQKaperFDVIDLDPYGSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKS 258
Cdd:PRK04338  109 EKVFNK-DANALLHEERK----FDVVDIDPFGSPAPFLDSAIRSVKRGGLLCVTATDTAPLCGAYPKSCLRKYGAVPLKT 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 259 RACHEMALRIVLHSLDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCGafylqrlgkasg 338
Cdd:PRK04338  184 EFYHEMGLRILIGYIAREAAKYDKGLEPLFSHSTDHYYRVFLKVERGAKKADKALENLGYVYYCPKCL------------ 251
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 339 dpggriKFSAACGPPVTpECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAVTTNPGrfhTSMRIQGVLSVVTEELP-DVP 417
Cdd:PRK04338  252 ------YREEVEGLPPE-ECPVCGGKFGTAGPLWLGPLHDKEFVEEMLEEAAKELG---TSKKALKLLKTIEEESKlDTP 321
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1398589758 418 LYYTLDQLSSTIHCNTPRLLQLRSALLHAGFRVSLSHACKNAVKTDAPPEALWDIMR 474
Cdd:PRK04338  322 TFYDLHELAKKLKVSAPPMDEILEALREAGFEASRTHFSPTGFKTDAPYDEIKEAIK 378
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
153-234 1.16e-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: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 153 SVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQKAPERFDVIDLDPygsPApF-------LDA------- 218
Cdd:COG1092   241 SVTSVDLSATALEWAKENAALNGLDDRHEFVQADAFDWLRELAREGERFDLIILDP---PA-FakskkdlFDAqrdykdl 316
                          90
                  ....*....|....*....
gi 1398589758 219 ---AVQAVSDGGLLcVTCT 234
Cdd:COG1092   317 nrlALKLLAPGGIL-VTSS 334
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
120-229 4.07e-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: 4.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 120 VGEICEEGLRVLEGLAASGLRSIRFALEVPGLqsVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQkapE 199
Cdd:COG2520   174 IAELVKPGERVLDMFAGVGPFSIPIAKRSGAK--VVAIDINPDAVEYLKENIRLNKVEDRVTPILGDAREVAPELE---G 248
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1398589758 200 RFD--VIDLdPYGSPApFLDAAVQAVSDGGLL 229
Cdd:COG2520   249 KADriIMNL-PHSADE-FLDAALRALKPGGVI 278
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
129-233 6.80e-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: 6.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 129 RVLEGLAASGLRSIRFALEVPGlqSVVANDASARAVELMhRNVELNGVAHLVQPNQADARMLmyqHQKAPERFDVIDLDP 208
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGA--RVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEEL---PPEADESFDVIISDP 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 1398589758 209 Y-----GSPAPFLDAAVQAVSDGGLLCVTC 233
Cdd:cd02440    75 PlhhlvEDLARFLEEARRLLKPGGVLVLTL 104
ZnF_C3H1 smart00356
zinc finger;
574-600 6.36e-06

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 43.00  E-value: 6.36e-06
                           10        20
                   ....*....|....*....|....*..
gi 1398589758  574 RLKTFPCKRFKEGTCQLGDQCCYSHSP 600
Cdd:smart00356   1 KYKTELCKFFKRGYCPRGDRCKFAHPL 27
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
126-229 1.06e-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: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 126 EGLRVLEGLAASGlrsirfALevpGL-------QSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMyqHQKAP 198
Cdd:COG0742    41 EGARVLDLFAGSG------AL---GLealsrgaASVVFVEKDRKAAAVIRKNLEKLGLEDRARVIRGDALRFL--KRLAG 109
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1398589758 199 ERFDVIDLD-PYGSpaPFLDAAVQAVSDGGLL 229
Cdd:COG0742   110 EPFDLVFLDpPYAK--GLLEKALELLAENGLL 139
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
576-600 8.59e-05

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 39.87  E-value: 8.59e-05
                          10        20
                  ....*....|....*....|....*.
gi 1398589758 576 KTFPCKRFKE-GTCQLGDQCCYSHSP 600
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 ...
125-230 3.16e-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: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398589758 125 EEGLRVLEGLAASGLRSIRFALEVPGlQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQkaperFDVI 204
Cdd:pfam02475  98 EPGEVVVDMFAGIGPFSIPIAKHSKA-RRVYAIELNPESYKYLKENIKLNKVEDVVKPILGDVREVILEDV-----ADRV 171
                          90       100
                  ....*....|....*....|....*.
gi 1398589758 205 DLDPYGSPAPFLDAAVQAVSDGGLLC 230
Cdd:pfam02475 172 VMNLPGSAHEFLDKAFAAVRDGGVIH 197
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
141-204 2.32e-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: 39.40  E-value: 2.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398589758 141 SIRFALEVPGLQsVVANDASARAVELMHRNVELNGV--AHLVQPNQADARmlmyqhqkAPERFDVI 204
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.
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