NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564398741|ref|XP_006256811|]
View 

tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase isoform X1 [Rattus norvegicus]

Protein Classification

RlmE family RNA methyltransferase( domain architecture ID 10000968)

RlmE (ribosomal RNA large subunit methyltransferase E) family RNA methyltransferase such as 23S rRNA (uridine(2552)-2'-O)-methyltransferase from bacteria and archaea, and tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase/16S rRNA (uridine(1369)-2'-O)-methyltransferase from eukaryota

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 1-199 1.26e-74

23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification


:

Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 228.42  E-value: 1.26e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741   1 MGRTSKDKR-------DVYYRLAKEKGWRARSAFKLLQLDEEFQLFKGVKRAVDLCAAPGSWSQVLSQKVGGQssGQVVA 73
Cdd:COG0293    3 MKRSKSSKRwlqrhlnDPYVKRAKKEGYRSRAAYKLLEIDEKDKLIKPGMRVVDLGAAPGGWSQVAAKRVGGK--GRVIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  74 VDLQAMAPLPGVIQIQGDITQLSTAKEIIQHFEGCPADLVVCDGAPDVTGLHDVDEYMQAQLLLAALNIATHVLKPGGCF 153
Cdd:COG0293   81 LDLLPMEPIPGVEFIQGDFREDEVLDQLLEALGGRKVDLVLSDMAPNTSGHKSVDHARSMYLVELALDFARKVLKPGGAF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564398741 154 VAKIFRGRDVTLLYSQLRIFFSSVLCAKPKSSRNSSIEAFAVCQGY 199
Cdd:COG0293  161 VVKVFQGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGF 206
 
Name Accession Description Interval E-value
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 1-199 1.26e-74

23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 228.42  E-value: 1.26e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741   1 MGRTSKDKR-------DVYYRLAKEKGWRARSAFKLLQLDEEFQLFKGVKRAVDLCAAPGSWSQVLSQKVGGQssGQVVA 73
Cdd:COG0293    3 MKRSKSSKRwlqrhlnDPYVKRAKKEGYRSRAAYKLLEIDEKDKLIKPGMRVVDLGAAPGGWSQVAAKRVGGK--GRVIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  74 VDLQAMAPLPGVIQIQGDITQLSTAKEIIQHFEGCPADLVVCDGAPDVTGLHDVDEYMQAQLLLAALNIATHVLKPGGCF 153
Cdd:COG0293   81 LDLLPMEPIPGVEFIQGDFREDEVLDQLLEALGGRKVDLVLSDMAPNTSGHKSVDHARSMYLVELALDFARKVLKPGGAF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564398741 154 VAKIFRGRDVTLLYSQLRIFFSSVLCAKPKSSRNSSIEAFAVCQGY 199
Cdd:COG0293  161 VVKVFQGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGF 206
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 21-199 5.85e-69

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 212.83  E-value: 5.85e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741   21 WRARSAFKLLQLDEEFQLFKGVKRAVDLCAAPGSWSQVLSQKvggqSSGQVVAVDLQAMA-----PLPGVIQIQGDITQL 95
Cdd:pfam01728   1 YRSRAAYKLLEIDEKFGLLKPGKTVLDLGAAPGGWSQVALQR----GAGKVVGVDLGPMQlwkprNDPGVTFIQGDIRDP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741   96 STAKEIIQHFEGcPADLVVCDGAPDVTGLHDVDEYMQAQLLLAALNIATHVLKPGGCFVAKIFRGRDVTLLYSQLRIFFS 175
Cdd:pfam01728  77 ETLDLLEELLGR-KVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFVCKVFQGEDFSELLYLLKLGFE 155

                         170       180
                  ....*....|....*....|....
gi 564398741  176 SVLCAKPKSSRNSSIEAFAVCQGY 199
Cdd:pfam01728 156 KVGVFKPPASRPESSEEYLVCLGF 179
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
10-199 4.65e-40

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;


Pssm-ID: 183025  Cd Length: 209  Bit Score: 139.48  E-value: 4.65e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  10 DVYYRLAKEKGWRARSAFKLLQLDEEFQLFKGVKRAVDLCAAPGSWSQVLSQKVGGqsSGQVVAVDLQAMAPLPGVIQIQ 89
Cdd:PRK11188  20 DKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYAVTQIGD--KGRVIACDILPMDPIVGVDFLQ 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  90 GDITQLSTAKEIIQHFEGCPADLVVCDGAPDVTGLHDVDEYMQAQLLLAALNIATHVLKPGGCFVAKIFRGRDVTLLYSQ 169
Cdd:PRK11188  98 GDFRDELVLKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALDMCRDVLAPGGSFVVKVFQGEGFDEYLRE 177

                        170       180       190
                 ....*....|....*....|....*....|
gi 564398741 170 LRIFFSSVLCAKPKSSRNSSIEAFAVCQGY 199
Cdd:PRK11188 178 IRSLFTKVKVRKPDSSRARSREVYIVATGR 207
capping_2-OMTase_viral cd20754
viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-) ...
 28-160 8.57e-04

viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Some dsDNA and dsRNA viruses, like the bluetongue virus (BTV), a member of the Reoviridae family, and Vaccinia virus, a member of the Poxviridae family, as well as some ss(+)RNA viruses, like Flaviviridae and Nidovirales, cap their mRNAs and encode their own 2'OMTase. In BTV, all four reactions are catalyzed by a single protein, VP4. In Vaccinia, the activity is located in the processing factor of the poly(A) polymerase, VP39.


Pssm-ID: 467730  Cd Length: 179  Bit Score: 39.73  E-value: 8.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  28 KLLQLDEEFQLFKGVKRAVDLCAAPGSWSQVLSQKVGGqssGQVVAVDLQAMAPLPG--VIQIQGDITQLSTAKEIIQHF 105
Cdd:cd20754    3 KLLQLEEYFLYKPEKMRVIYIGCAPGGWLYYLRDWFEG---TLWVGFDPRDTDPLGYnnVITVNKFFDHEHTKLKFLPNK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564398741 106 EgcpaDLVVCDGAPDVTGLHD-VDEYMQAQLLLAALNIATHVLKPGGCFVaKIFRG 160
Cdd:cd20754   80 K----DLLICDIRSDRSSHVTkEEDTTESFLTLQEGYIATKLAKVGSICV-KVRAP 130
 
Name Accession Description Interval E-value
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 1-199 1.26e-74

23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 228.42  E-value: 1.26e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741   1 MGRTSKDKR-------DVYYRLAKEKGWRARSAFKLLQLDEEFQLFKGVKRAVDLCAAPGSWSQVLSQKVGGQssGQVVA 73
Cdd:COG0293    3 MKRSKSSKRwlqrhlnDPYVKRAKKEGYRSRAAYKLLEIDEKDKLIKPGMRVVDLGAAPGGWSQVAAKRVGGK--GRVIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  74 VDLQAMAPLPGVIQIQGDITQLSTAKEIIQHFEGCPADLVVCDGAPDVTGLHDVDEYMQAQLLLAALNIATHVLKPGGCF 153
Cdd:COG0293   81 LDLLPMEPIPGVEFIQGDFREDEVLDQLLEALGGRKVDLVLSDMAPNTSGHKSVDHARSMYLVELALDFARKVLKPGGAF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564398741 154 VAKIFRGRDVTLLYSQLRIFFSSVLCAKPKSSRNSSIEAFAVCQGY 199
Cdd:COG0293  161 VVKVFQGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGF 206
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 21-199 5.85e-69

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 212.83  E-value: 5.85e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741   21 WRARSAFKLLQLDEEFQLFKGVKRAVDLCAAPGSWSQVLSQKvggqSSGQVVAVDLQAMA-----PLPGVIQIQGDITQL 95
Cdd:pfam01728   1 YRSRAAYKLLEIDEKFGLLKPGKTVLDLGAAPGGWSQVALQR----GAGKVVGVDLGPMQlwkprNDPGVTFIQGDIRDP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741   96 STAKEIIQHFEGcPADLVVCDGAPDVTGLHDVDEYMQAQLLLAALNIATHVLKPGGCFVAKIFRGRDVTLLYSQLRIFFS 175
Cdd:pfam01728  77 ETLDLLEELLGR-KVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFVCKVFQGEDFSELLYLLKLGFE 155

                         170       180
                  ....*....|....*....|....
gi 564398741  176 SVLCAKPKSSRNSSIEAFAVCQGY 199
Cdd:pfam01728 156 KVGVFKPPASRPESSEEYLVCLGF 179
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
10-199 4.65e-40

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;


Pssm-ID: 183025  Cd Length: 209  Bit Score: 139.48  E-value: 4.65e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  10 DVYYRLAKEKGWRARSAFKLLQLDEEFQLFKGVKRAVDLCAAPGSWSQVLSQKVGGqsSGQVVAVDLQAMAPLPGVIQIQ 89
Cdd:PRK11188  20 DKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYAVTQIGD--KGRVIACDILPMDPIVGVDFLQ 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  90 GDITQLSTAKEIIQHFEGCPADLVVCDGAPDVTGLHDVDEYMQAQLLLAALNIATHVLKPGGCFVAKIFRGRDVTLLYSQ 169
Cdd:PRK11188  98 GDFRDELVLKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALDMCRDVLAPGGSFVVKVFQGEGFDEYLRE 177

                        170       180       190
                 ....*....|....*....|....*....|
gi 564398741 170 LRIFFSSVLCAKPKSSRNSSIEAFAVCQGY 199
Cdd:PRK11188 178 IRSLFTKVKVRKPDSSRARSREVYIVATGR 207
RlmM COG2933
23S rRNA C2498 (ribose-2'-O)-methylase RlmM [Translation, ribosomal structure and biogenesis]; ...
 14-116 1.11e-06

23S rRNA C2498 (ribose-2'-O)-methylase RlmM [Translation, ribosomal structure and biogenesis]; 23S rRNA C2498 (ribose-2'-O)-methylase RlmM is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 442177 [Multi-domain]  Cd Length: 356  Bit Score: 49.46  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  14 RLAKEKGWRARSAFKLlqlDEEFQLFKGVK----------RAVDLCAAPGSWSQVLSQKvggqsSGQVVAVDLQAMAP-L 82
Cdd:COG2933  177 RLRFPADAPSRSTLKL---EEAFHVFLPRDeweerlrpgmRAVDLGAAPGGWTWQLVRR-----GMFVTAVDNGPMAPsL 248

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564398741  83 ---PGVIQIQGDITQLSTAKeiiqhfegcPADLVVCD 116
Cdd:COG2933  249 mdtGQVEHLREDGFKYRPPK---------PVDWLVCD 276
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 47-151 6.06e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 44.09  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741   47 DLCAAPGSWSQVLSQKVGGQssgqVVAVDL----------QAMAPLPGVIQIQGDITQLStakeiiqhFEGCPADLVVCD 116
Cdd:pfam13649   3 DLGCGTGRLTLALARRGGAR----VTGVDLspemlerareRAAEAGLNVEFVQGDAEDLP--------FPDGSFDLVVSS 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564398741  117 GApdvtgLHdvdeYMQAQLLLAALNIATHVLKPGG 151
Cdd:pfam13649  71 GV-----LH----HLPDPDLEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 18-159 8.80e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.98  E-value: 8.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  18 EKGWRARSAFKLLQLDEEFQLFKGVKRAVDLCAAPGSWSQVLSQKVGGQssgqVVAVDL--------QAMAP---LPGVI 86
Cdd:COG0500    3 DSYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGR----VIGIDLspeaialaRARAAkagLGNVE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564398741  87 QIQGDITQLSTAKEiiQHFegcpaDLVVCDGApdvtgLHDVDEymqaQLLLAALNIATHVLKPGGCFVAKIFR 159
Cdd:COG0500   79 FLVADLAELDPLPA--ESF-----DLVVAFGV-----LHHLPP----EEREALLRELARALKPGGVLLLSASD 135
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 43-154 9.70e-05

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 41.54  E-value: 9.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  43 KRAVDLCAAPGSWSQVLSQKvggqssG-QVVAVDL--------QAMAPLPGVIQIQGDITQLStakeiiqhFEGCPADLV 113
Cdd:COG2227   26 GRVLDVGCGTGRLALALARR------GaDVTGVDIspealeiaRERAAELNVDFVQGDLEDLP--------LEDGSFDLV 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564398741 114 VCDGApdvtgLHDVDEymqaqlLLAALNIATHVLKPGGCFV 154
Cdd:COG2227   92 ICSEV-----LEHLPD------PAALLRELARLLKPGGLLL 121
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 43-171 2.03e-04

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 40.75  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  43 KRAVDLCAAPGSWSQVLSQKvggqsSGQVVAVDL-QAM---------APLPGVIQIQGDITQLStakeiiqhFEGCPADL 112
Cdd:COG2226   24 ARVLDLGCGTGRLALALAER-----GARVTGVDIsPEMlelareraaEAGLNVEFVVGDAEDLP--------FPDGSFDL 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564398741 113 VVCdgapdVTGLHDVDEymqaqlLLAALNIATHVLKPGGCFVAKIFRGRDVTLLYSQLR 171
Cdd:COG2226   91 VIS-----SFVLHHLPD------PERALAEIARVLKPGGRLVVVDFSPPDLAELEELLA 138
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 19-154 3.36e-04

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 41.29  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  19 KGWRaRSAFKLLQLdeefqlFKGvKRAVDLCAAPGSWSQVLSQKVGgqSSGQVVAVDL-QAMaplpgviqiqgditqLST 97
Cdd:PRK00216  37 RVWR-RKTIKWLGV------RPG-DKVLDLACGTGDLAIALAKAVG--KTGEVVGLDFsEGM---------------LAV 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  98 AKEIIQHFEGCP-ADLVVCDGA----PD-----VT---GLHDVDEYMQAqlllaaLNIATHVLKPGGCFV 154
Cdd:PRK00216  92 GREKLRDLGLSGnVEFVQGDAEalpfPDnsfdaVTiafGLRNVPDIDKA------LREMYRVLKPGGRLV 155
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 44-168 6.08e-04

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


Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 41.15  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  44 RAVDLCAAPGSWSQVLSQKVGGQssGQVVAVDLQAM-----------APLPGVIQIQGDitqlstAKEIIQHFEGcPADL 112
Cdd:COG0144  252 RVLDLCAAPGGKTLHLAELMGNK--GRVVAVDISEHrlkrlrenlarLGLSNVEVVVAD------ARELLEWLPG-KFDR 322

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564398741 113 VVCD------GA----PDV---TGLHDVDEY--MQAQLLLAALNIathvLKPGGcfvakifrgrdvTLLYS 168
Cdd:COG0144  323 VLLDapcsgtGTlrrhPDIkwrRTPEDIAELaaLQRELLDAAARL----LKPGG------------RLVYS 377
capping_2-OMTase_viral cd20754
viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-) ...
 28-160 8.57e-04

viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Some dsDNA and dsRNA viruses, like the bluetongue virus (BTV), a member of the Reoviridae family, and Vaccinia virus, a member of the Poxviridae family, as well as some ss(+)RNA viruses, like Flaviviridae and Nidovirales, cap their mRNAs and encode their own 2'OMTase. In BTV, all four reactions are catalyzed by a single protein, VP4. In Vaccinia, the activity is located in the processing factor of the poly(A) polymerase, VP39.


Pssm-ID: 467730  Cd Length: 179  Bit Score: 39.73  E-value: 8.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  28 KLLQLDEEFQLFKGVKRAVDLCAAPGSWSQVLSQKVGGqssGQVVAVDLQAMAPLPG--VIQIQGDITQLSTAKEIIQHF 105
Cdd:cd20754    3 KLLQLEEYFLYKPEKMRVIYIGCAPGGWLYYLRDWFEG---TLWVGFDPRDTDPLGYnnVITVNKFFDHEHTKLKFLPNK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564398741 106 EgcpaDLVVCDGAPDVTGLHD-VDEYMQAQLLLAALNIATHVLKPGGCFVaKIFRG 160
Cdd:cd20754   80 K----DLLICDIRSDRSSHVTkEEDTTESFLTLQEGYIATKLAKVGSICV-KVRAP 130
PRK11760 PRK11760
putative 23S rRNA C2498 ribose 2'-O-ribose methyltransferase; Provisional
 24-81 4.72e-03

putative 23S rRNA C2498 ribose 2'-O-ribose methyltransferase; Provisional


Pssm-ID: 236971 [Multi-domain]  Cd Length: 357  Bit Score: 38.28  E-value: 4.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564398741  24 RSAFKLlqlDEEFQLF----------KGVKRAVDLCAAPGSWSQVLSQKvggqsSGQVVAVDLQAMAP 81
Cdd:PRK11760 187 RSTLKL---EEAFHVFiprdewderlAPGMRAVDLGAAPGGWTYQLVRR-----GMFVTAVDNGPMAQ 246
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
41-154 5.97e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 37.29  E-value: 5.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  41 GVKRAVDLCAAPGSWSQVLSQKVGgqssgQVVAVDL-QAMAPL----PGVIQ-IQGDITQLSTAKEiiqhfegcPADLVV 114
Cdd:COG4976   46 PFGRVLDLGCGTGLLGEALRPRGY-----RLTGVDLsEEMLAKarekGVYDRlLVADLADLAEPDG--------RFDLIV 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564398741 115 CdgaPDV-TGLHDVDEYMQAqlllaalniATHVLKPGGCFV 154
Cdd:COG4976  113 A---ADVlTYLGDLAAVFAG---------VARALKPGGLFI 141
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 44-160 8.65e-03

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: 35.48  E-value: 8.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398741  44 RAVDLCAAPGSWSQVLSQKVGGQssgqVVAVDL-----------QAMAPLPGVIQIQGDITQLStaKEIIQHFegcpaDL 112
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGAR----VTGVDIspvalelarkaAAALLADNVEVLKGDAEELP--PEADESF-----DV 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 564398741 113 VVCDGApdvtgLHDVDEymqaqLLLAALNIATHVLKPGGCFVAKIFRG 160
Cdd:cd02440   70 IISDPP-----LHHLVE-----DLARFLEEARRLLKPGGVLVLTLVLA 107
 
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