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Conserved domains on  [gi|2468519473|ref|WP_276814980|]
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class I SAM-dependent methyltransferase family protein [Desulfurococcus amylolyticus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11457541)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Bos taurus tRNA (guanine(37)-N1)-methyltransferase

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 3-285 5.50e-111

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: 323.74  E-value: 5.50e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473   3 RGSLLKELAREILGEGVAEKVWRRVEFIGDLALIRTPlDMSPEELKPLALEILKRFNFVKSVWAAIPGVEGPYRLRKHVL 82
Cdd:COG2520    58 EPPSLKELLEGGLPEELLELLPSSYDIIGDIAIIKIP-DELEEYKEEIAEAILESHPNVKTVLAKASGVEGEFRVPELEL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473  83 LAGEDRSETLYREHGCVFKVDINKVYISPSLNYEHYRIAKLVAPGETVLNMFAGAGLFSIIIARYaKPRKVYSIDINPYA 162
Cdd:COG2520   137 LAGEGRTETIHRENGCRFKLDVAKVYFSPRLATERLRIAELVKPGERVLDMFAGVGPFSIPIAKR-SGAKVVAIDINPDA 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 163 YHYMVENVRLNHVEDVVEPILGDAGEVVnSRLTNTSDRVLMPYPELALDYLDKALMALRDGrGWIHVYLHVKTakgEHYL 242
Cdd:COG2520   216 VEYLKENIRLNKVEDRVTPILGDAREVA-PELEGKADRIIMNLPHSADEFLDAALRALKPG-GVIHYYEIVPE---EDPF 290

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2468519473 243 TKAEQLVAEKLASLGvRNYDISSKRKIRNVGPRTHQVVVDIKI 285
Cdd:COG2520   291 ERAEERIEEAAEEAG-YEVEILEKRRVKSYSPGVYHVVVDVRV 332
 
Name Accession Description Interval E-value
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 3-285 5.50e-111

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: 323.74  E-value: 5.50e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473   3 RGSLLKELAREILGEGVAEKVWRRVEFIGDLALIRTPlDMSPEELKPLALEILKRFNFVKSVWAAIPGVEGPYRLRKHVL 82
Cdd:COG2520    58 EPPSLKELLEGGLPEELLELLPSSYDIIGDIAIIKIP-DELEEYKEEIAEAILESHPNVKTVLAKASGVEGEFRVPELEL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473  83 LAGEDRSETLYREHGCVFKVDINKVYISPSLNYEHYRIAKLVAPGETVLNMFAGAGLFSIIIARYaKPRKVYSIDINPYA 162
Cdd:COG2520   137 LAGEGRTETIHRENGCRFKLDVAKVYFSPRLATERLRIAELVKPGERVLDMFAGVGPFSIPIAKR-SGAKVVAIDINPDA 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 163 YHYMVENVRLNHVEDVVEPILGDAGEVVnSRLTNTSDRVLMPYPELALDYLDKALMALRDGrGWIHVYLHVKTakgEHYL 242
Cdd:COG2520   216 VEYLKENIRLNKVEDRVTPILGDAREVA-PELEGKADRIIMNLPHSADEFLDAALRALKPG-GVIHYYEIVPE---EDPF 290

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2468519473 243 TKAEQLVAEKLASLGvRNYDISSKRKIRNVGPRTHQVVVDIKI 285
Cdd:COG2520   291 ERAEERIEEAAEEAG-YEVEILEKRRVKSYSPGVYHVVVDVRV 332
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
 25-228 7.01e-63

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: 196.80  E-value: 7.01e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473  25 RRVEFIGDLALIrtPLDMSPEELKPLALEILKRFNFVKSVWAAIPGVEGPYRLRKHVLLAGEDrSETLYREHGCVFKVDI 104
Cdd:pfam02475   1 TSFDIIGDVVIL--NLREELDEYRKVIGEAILEKTKVKTVLRKVSEVYGEFRTPRYEVLAGSD-TETIHKENGCRFKVDV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 105 NKVYISPSLNYEHYRIAKLVAPGETVLNMFAGAGLFSIIIARYAKPRKVYSIDINPYAYHYMVENVRLNHVEDVVEPILG 184
Cdd:pfam02475  78 AKVYWSPRLIAERERIAKLVEPGEVVVDMFAGIGPFSIPIAKHSKARRVYAIELNPESYKYLKENIKLNKVEDVVKPILG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2468519473 185 DAGEVVNSRLtntSDRVLMPYPELALDYLDKALMALRDGrGWIH 228
Cdd:pfam02475 158 DVREVILEDV---ADRVVMNLPGSAHEFLDKAFAAVRDG-GVIH 197
PRK14968 PRK14968
putative methyltransferase; Provisional
 123-224 2.31e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 49.90  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 123 LVAPGETVLNMFAGAGLFSIIIARYAKprKVYSIDINPYAYHYMVENVRLNHVE---------DVVEPILGDAGEVVnsr 193
Cdd:PRK14968   20 VDKKGDRVLEVGTGSGIVAIVAAKNGK--KVVGVDINPYAVECAKCNAKLNNIRnngvevirsDLFEPFRGDKFDVI--- 94

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2468519473 194 LTNTsdrvlmPY----PELAL-DYLDKALMALRDGR 224
Cdd:PRK14968   95 LFNP------PYlpteEEEEWdDWLNYALSGGKDGR 124
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 127-269 1.05e-05

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 44.85  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 127 GETVLNMFAGAGLFSIIIARyaKPRKVYSIDINPYAYHYMVENVRLNHVE-DVVEpilGDAGEVVNSRLtntsDRVLMPY 205
Cdd:TIGR00537  20 PDDVLEIGAGTGLVAIRLKG--KGKCILTTDINPFAVKELRENAKLNNVGlDVVM---TDLFKGVRGKF----DVILFNP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 206 PELAL-------DYLDKALMALRDGRGWIHVYL-----HVKtAKGEHYLTKA----EQLVAEKLASLGVRnYDISSKRKI 269
Cdd:TIGR00537  91 PYLPLeddlrrgDWLDVAIDGGKDGRKVIDRFLdelpeILK-EGGRVQLIQSslngEPDTFDKLDERGFR-YEIVAERGL 168
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 129-229 5.15e-05

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: 41.65  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 129 TVLNMFAGAGLFSIIIARYaKPRKVYSIDINPYAYHYMVENvRLNHVEDVVEPILGDAGEVVNSRLTN----TSDRVLMP 204
Cdd:cd02440     1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELPPEADESfdviISDPPLHH 78

                          90       100
                  ....*....|....*....|....*
gi 2468519473 205 YPELALDYLDKALMALRDGrGWIHV 229
Cdd:cd02440    79 LVEDLARFLEEARRLLKPG-GVLVL 102
 
Name Accession Description Interval E-value
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 3-285 5.50e-111

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: 323.74  E-value: 5.50e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473   3 RGSLLKELAREILGEGVAEKVWRRVEFIGDLALIRTPlDMSPEELKPLALEILKRFNFVKSVWAAIPGVEGPYRLRKHVL 82
Cdd:COG2520    58 EPPSLKELLEGGLPEELLELLPSSYDIIGDIAIIKIP-DELEEYKEEIAEAILESHPNVKTVLAKASGVEGEFRVPELEL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473  83 LAGEDRSETLYREHGCVFKVDINKVYISPSLNYEHYRIAKLVAPGETVLNMFAGAGLFSIIIARYaKPRKVYSIDINPYA 162
Cdd:COG2520   137 LAGEGRTETIHRENGCRFKLDVAKVYFSPRLATERLRIAELVKPGERVLDMFAGVGPFSIPIAKR-SGAKVVAIDINPDA 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 163 YHYMVENVRLNHVEDVVEPILGDAGEVVnSRLTNTSDRVLMPYPELALDYLDKALMALRDGrGWIHVYLHVKTakgEHYL 242
Cdd:COG2520   216 VEYLKENIRLNKVEDRVTPILGDAREVA-PELEGKADRIIMNLPHSADEFLDAALRALKPG-GVIHYYEIVPE---EDPF 290

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2468519473 243 TKAEQLVAEKLASLGvRNYDISSKRKIRNVGPRTHQVVVDIKI 285
Cdd:COG2520   291 ERAEERIEEAAEEAG-YEVEILEKRRVKSYSPGVYHVVVDVRV 332
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
 25-228 7.01e-63

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: 196.80  E-value: 7.01e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473  25 RRVEFIGDLALIrtPLDMSPEELKPLALEILKRFNFVKSVWAAIPGVEGPYRLRKHVLLAGEDrSETLYREHGCVFKVDI 104
Cdd:pfam02475   1 TSFDIIGDVVIL--NLREELDEYRKVIGEAILEKTKVKTVLRKVSEVYGEFRTPRYEVLAGSD-TETIHKENGCRFKVDV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 105 NKVYISPSLNYEHYRIAKLVAPGETVLNMFAGAGLFSIIIARYAKPRKVYSIDINPYAYHYMVENVRLNHVEDVVEPILG 184
Cdd:pfam02475  78 AKVYWSPRLIAERERIAKLVEPGEVVVDMFAGIGPFSIPIAKHSKARRVYAIELNPESYKYLKENIKLNKVEDVVKPILG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2468519473 185 DAGEVVNSRLtntSDRVLMPYPELALDYLDKALMALRDGrGWIH 228
Cdd:pfam02475 158 DVREVILEDV---ADRVVMNLPGSAHEFLDKAFAAVRDG-GVIH 197
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
120-189 2.04e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 53.50  E-value: 2.04e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 120 IAKLVAPGETVLNMFAGAGLFSIIIARYAkPRKVYSIDINPYAYHYMVENVRLNHVEDVVEPILGDAGEV 189
Cdd:COG4076    29 IERVVKPGDVVLDIGTGSGLLSMLAARAG-AKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDL 97
PRK14968 PRK14968
putative methyltransferase; Provisional
 123-224 2.31e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 49.90  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 123 LVAPGETVLNMFAGAGLFSIIIARYAKprKVYSIDINPYAYHYMVENVRLNHVE---------DVVEPILGDAGEVVnsr 193
Cdd:PRK14968   20 VDKKGDRVLEVGTGSGIVAIVAAKNGK--KVVGVDINPYAVECAKCNAKLNNIRnngvevirsDLFEPFRGDKFDVI--- 94

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2468519473 194 LTNTsdrvlmPY----PELAL-DYLDKALMALRDGR 224
Cdd:PRK14968   95 LFNP------PYlpteEEEEWdDWLNYALSGGKDGR 124
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 125-194 6.17e-07

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 50.17  E-value: 6.17e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 125 APGETVLNMFAGAGLFSIIIARYAKprKVYSIDINPYAYHYMVENVRLNHVEDvVEPILGDAGEVVNSRL 194
Cdd:COG2265   232 TGGERVLDLYCGVGTFALPLARRAK--KVIGVEIVPEAVEDARENARLNGLKN-VEFVAGDLEEVLPELL 298
TRM pfam02005
N2,N2-dimethylguanosine tRNA methyltransferase; This enzyme EC:2.1.1.32 used S-AdoMet to ...
 113-223 1.09e-06

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: 49.30  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 113 LNYEHYRIAKLVapgeTVLNMFAGAGLFSIiiaRYAKP----RKVYSIDINPYAYHYMVENVRLNHVEDVVEPILGDAGE 188
Cdd:pfam02005  40 LNLLHKKLGRKI----KVLDALSASGIRAI---RFALEvpgvEEVFANDISPKAVESIKENVKLNEVENIVVINGDDANA 112

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2468519473 189 VV--NSRLTNTSDrvLMPYPELAlDYLDKALMALRDG 223
Cdd:pfam02005 113 FMreNHRRFDVID--LDPFGSPA-PFLDSAVQSVKRG 146
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
120-186 3.37e-06

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 47.48  E-value: 3.37e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468519473 120 IAKLVAPGETVLNMFAGAGLFSIIIARYAkPRKVYSIDINPYAYHYMVENVRLNHVEDVVEPILGDA 186
Cdd:COG2264   142 LEKLLKPGKTVLDVGCGSGILAIAAAKLG-AKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDL 207
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 124-205 7.77e-06

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 45.91  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 124 VAPGETVLNMFAGAGLFSIIIARYAKPRKVYSIDINPYAYHYMVENVRLNHVEDVVEPILGDAGEVVNSRLTNTSDRVLM 203
Cdd:COG4123    35 VKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPGSFDLVVS 114


                  ....
gi 2468519473 204 --PY 205
Cdd:COG4123   115 npPY 118
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 127-269 1.05e-05

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 44.85  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 127 GETVLNMFAGAGLFSIIIARyaKPRKVYSIDINPYAYHYMVENVRLNHVE-DVVEpilGDAGEVVNSRLtntsDRVLMPY 205
Cdd:TIGR00537  20 PDDVLEIGAGTGLVAIRLKG--KGKCILTTDINPFAVKELRENAKLNNVGlDVVM---TDLFKGVRGKF----DVILFNP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 206 PELAL-------DYLDKALMALRDGRGWIHVYL-----HVKtAKGEHYLTKA----EQLVAEKLASLGVRnYDISSKRKI 269
Cdd:TIGR00537  91 PYLPLeddlrrgDWLDVAIDGGKDGRKVIDRFLdelpeILK-EGGRVQLIQSslngEPDTFDKLDERGFR-YEIVAERGL 168
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 82-186 1.60e-05

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: 45.56  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473  82 LLAGEDRSETLYREHGCVFKVDINKvYISPSLNYEH----YRIAKLVApGETVLNMFAGAGLFSIIIARyAKPRKVYSID 157
Cdd:COG1092   170 VLYGEAPEEVEVEENGLKFLVDLTD-GQKTGLFLDQrenrARVAELAK-GKRVLNLFSYTGGFSVHAAA-GGAKSVTSVD 246

                          90       100
                  ....*....|....*....|....*....
gi 2468519473 158 INPYAYHYMVENVRLNHVEDVVEPILGDA 186
Cdd:COG1092   247 LSATALEWAKENAALNGLDDRHEFVQADA 275
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 120-231 2.22e-05

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: 44.77  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 120 IAKL-VAPGETVLNMFAGAGLFSIIIARYAKPR-KVYSIDINPYAYHYMVENVRLNHVEDVVEPILGDAGEVVNSRltnT 197
Cdd:COG2519    84 IARLdIFPGARVLEAGTGSGALTLALARAVGPEgKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIREGIDEG---D 160

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2468519473 198 SDRVL--MPYPElalDYLDKALMALRDGrGWIHVYL 231
Cdd:COG2519   161 VDAVFldMPDPW---EALEAVAKALKPG-GVLVAYV 192
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 129-229 5.15e-05

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: 41.65  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 129 TVLNMFAGAGLFSIIIARYaKPRKVYSIDINPYAYHYMVENvRLNHVEDVVEPILGDAGEVVNSRLTN----TSDRVLMP 204
Cdd:cd02440     1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELPPEADESfdviISDPPLHH 78

                          90       100
                  ....*....|....*....|....*
gi 2468519473 205 YPELALDYLDKALMALRDGrGWIHV 229
Cdd:cd02440    79 LVEDLARFLEEARRLLKPG-GVLVL 102
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 136-223 3.85e-04

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: 40.17  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 136 GAGLFSIIIARYAKPR-KVYSIDINPYAYHYMVENVRLNHVEDVVEPILGDAGEVVNSRLTNTSDRVLM-----PYPela 209
Cdd:COG4122    26 GTGYSTLWLARALPDDgRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEVLPRLADGPFDLVFIdadksNYP--- 102

                          90
                  ....*....|....
gi 2468519473 210 lDYLDKALMALRDG 223
Cdd:COG4122   103 -DYLELALPLLRPG 115
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
 127-215 5.06e-04

RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.


Pssm-ID: 370496  Cd Length: 165  Bit Score: 40.01  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468519473 127 GETVLNMFAGAGLFSIIIARYAKPrkVYSIDINP----YAYHymveNVRLNHVEDVVEPILGDAGEVVNSRLTN--TSDR 200
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDS--VISIDINLehlaCAQH----NAEVYGVSDRIWLIHGDWFELLAKLKFEkiKYDC 74

                          90
                  ....*....|....*
gi 2468519473 201 VLMPYPELALDYLDK 215
Cdd:pfam09445  75 VFASPPWGGPSYKKQ 89
PLN02672 PLN02672
methionine S-methyltransferase
 129-194 5.25e-04

methionine S-methyltransferase


Pssm-ID: 215360 [Multi-domain]  Cd Length: 1082  Bit Score: 41.30  E-value: 5.25e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468519473  129 TVLNMFAGAGLFSIIIARYAKPRKVYSIDINPYAYHYMVENVRLNHVEDVVEPILGDAGEVVNSRL 194
Cdd:PLN02672   121 TVAELGCGNGWISIAIAEKWLPSKVYGLDINPRAVKVAWINLYLNALDDDGLPVYDGEGKTLLDRV 186
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
120-180 6.19e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 40.52  E-value: 6.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468519473 120 IAKLVAPGETVLNMFAGAGLFSIIiARYAKPRKVYSIDINPYAYHYMVENVRLNHVEDVVE 180
Cdd:PRK00517  113 LEKLVLPGKTVLDVGCGSGILAIA-AAKLGAKKVLAVDIDPQAVEAARENAELNGVELNVY 172
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 123-183 1.41e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 39.56  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468519473 123 LVAPGETVLNMFAGAGLFSIIIARYAkPRKVYSIDINPYAYHYMVENVRLNHVEDVVEPIL 183
Cdd:pfam06325 158 LVKPGESVLDVGCGSGILAIAALKLG-AKKVVGVDIDPVAVRAAKENAELNGVEARLEVYL 217
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 129-179 6.36e-03

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 36.13  E-value: 6.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2468519473 129 TVLNMFAGAGLFSIIIARYAKPRKVYSIDINPYAYHYMVENVRLNHVEDVV 179
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEGRVIAFEPLPDAYEILEENVKLNNLPNVV 51
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 126-178 8.88e-03

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


Pssm-ID: 235286  Cd Length: 382  Bit Score: 37.20  E-value: 8.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2468519473 126 PGETVLNMFAGAGLFSIiiaRYAK---PRKVYSIDINPYAYHYMVENVRLNHVEDV 178
Cdd:PRK04338   57 PRESVLDALSASGIRGI---RYALetgVEKVTLNDINPDAVELIKKNLELNGLENE 109
 
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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