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Conserved domains on  [gi|1090717115|emb|SEG37936|]
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23S rRNA Um-2552 2'-O-methyltransferase [Oleiphilus messinensis]

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

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:0001510|GO:1904047
PubMed:  31586407|10748051
SCOP:  4000658

Graphical summary

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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 ...
 1-206 2.54e-141

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: 392.51  E-value: 2.54e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115   1 MARSKTSAGWLKEHFDDRYVQKSRDDGYRSRASYKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAIEKVGESGVVIASD 80
Cdd:COG0293     3 MKRSKSSKRWLQRHLNDPYVKRAKKEGYRSRAAYKLLEIDEKDKLIKPGMRVVDLGAAPGGWSQVAAKRVGGKGRVIALD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  81 ILEMEPIADVTFIQGDFTEDKVYDEIMAAIGNRPVDMVISDMAPNMSGMSAMDQPRAMYLVELALDLASRTLKKEGTFLA 160
Cdd:COG0293    83 LLPMEPIPGVEFIQGDFREDEVLDQLLEALGGRKVDLVLSDMAPNTSGHKSVDHARSMYLVELALDFARKVLKPGGAFVV 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1090717115 161 KVFQGEGFDAYLKDLKSQFKTVITRKPDASRARSREVYLLAKGFKG 206
Cdd:COG0293   163 KVFQGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGFKG 208
 
Name Accession Description Interval E-value
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 1-206 2.54e-141

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: 392.51  E-value: 2.54e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115   1 MARSKTSAGWLKEHFDDRYVQKSRDDGYRSRASYKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAIEKVGESGVVIASD 80
Cdd:COG0293     3 MKRSKSSKRWLQRHLNDPYVKRAKKEGYRSRAAYKLLEIDEKDKLIKPGMRVVDLGAAPGGWSQVAAKRVGGKGRVIALD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  81 ILEMEPIADVTFIQGDFTEDKVYDEIMAAIGNRPVDMVISDMAPNMSGMSAMDQPRAMYLVELALDLASRTLKKEGTFLA 160
Cdd:COG0293    83 LLPMEPIPGVEFIQGDFREDEVLDQLLEALGGRKVDLVLSDMAPNTSGHKSVDHARSMYLVELALDFARKVLKPGGAFVV 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1090717115 161 KVFQGEGFDAYLKDLKSQFKTVITRKPDASRARSREVYLLAKGFKG 206
Cdd:COG0293   163 KVFQGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGFKG 208
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
3-206 4.02e-111

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


Pssm-ID: 183025  Cd Length: 209  Bit Score: 316.29  E-value: 4.02e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115   3 RSKTSAGWLKEHFDDRYVQKSRDDGYRSRASYKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAIEKVGESGVVIASDIL 82
Cdd:PRK11188    6 RSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYAVTQIGDKGRVIACDIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  83 EMEPIADVTFIQGDFTEDKVYDEIMAAIGNRPVDMVISDMAPNMSGMSAMDQPRAMYLVELALDLASRTLKKEGTFLAKV 162
Cdd:PRK11188   86 PMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALDMCRDVLAPGGSFVVKV 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1090717115 163 FQGEGFDAYLKDLKSQFKTVITRKPDASRARSREVYLLAKGFKG 206
Cdd:PRK11188  166 FQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRKL 209
rrmJ TIGR00438
cell division protein FtsJ; Methylates the 23S rRNA. Previously known as cell division protein ...
 17-204 1.00e-89

cell division protein FtsJ; Methylates the 23S rRNA. Previously known as cell division protein ftsJ.// Trusted cutoff too high? [SS 10/1/04] [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273078  Cd Length: 188  Bit Score: 261.29  E-value: 1.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  17 DRYVQKSRDDGYRSRASYKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAIEKVGESGVVIASDILEMEPIADVTFIQGD 96
Cdd:TIGR00438   1 DFYYQKAKKEKYRSRASFKLLQLNQKFKLIKPGDTVLDLGAAPGGWSQVAVEQVGGKGRVIAVDLQPMKPIENVDFIRGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  97 FTEDKVYDEIMAAIGNRPVDMVISDMAPNMSGMSAMDQPRAMYLVELALDLASRTLKKEGTFLAKVFQGEGFDAYLKDLK 176
Cdd:TIGR00438  81 FTDEEVLNKIRERVGDDKVDVVMSDAAPNISGYWDIDHLRSIDLVELALDIAKEVLKPKGNFVVKVFQGEEIDEYLNELR 160

                         170       180
                  ....*....|....*....|....*...
gi 1090717115 177 SQFKTVITRKPDASRARSREVYLLAKGF 204
Cdd:TIGR00438 161 KLFEKVKVTKPQASRKRSAEVYIVAKRF 188
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 28-204 8.93e-72

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: 215.53  E-value: 8.93e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  28 YRSRASYKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAIEKVGesGVVIASDILEM---EPIAD--VTFIQGDFTEDKV 102
Cdd:pfam01728   1 YRSRAAYKLLEIDEKFGLLKPGKTVLDLGAAPGGWSQVALQRGA--GKVVGVDLGPMqlwKPRNDpgVTFIQGDIRDPET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115 103 YDEIMAAIGnRPVDMVISDMAPNMSGMSAMDQPRAMYLVELALDLASRTLKKEGTFLAKVFQGEGFDAYLKDLKSQFKTV 182
Cdd:pfam01728  79 LDLLEELLG-RKVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFVCKVFQGEDFSELLYLLKLGFEKV 157

                         170       180
                  ....*....|....*....|..
gi 1090717115 183 ITRKPDASRARSREVYLLAKGF 204
Cdd:pfam01728 158 GVFKPPASRPESSEEYLVCLGF 179
capping_2-OMTase_viral cd20754
viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-) ...
 34-202 1.17e-08

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: 52.44  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  34 YKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAiEKVGESGVVIASDILEMEPI--ADVTFIQGDFTEDKVYDEIMAaig 111
Cdd:cd20754     2 AKLLQLEEYFLYKPEKMRVIYIGCAPGGWLYYL-RDWFEGTLWVGFDPRDTDPLgyNNVITVNKFFDHEHTKLKFLP--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115 112 nRPVDMVISDMAPNMSGM-SAMDQPRAMYLVELAlDLASRTLKKEGTFLAKVFQGEGFDAYlkdlKSQFKTVITRKPDAS 190
Cdd:cd20754    78 -NKKDLLICDIRSDRSSHvTKEEDTTESFLTLQE-GYIATKLAKVGSICVKVRAPDLKDDG----HFSSGTLFPQPYAAS 151

                         170
                  ....*....|..
gi 1090717115 191 rarSREVYLLAK 202
Cdd:cd20754   152 ---SSEMRLFSA 160
 
Name Accession Description Interval E-value
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 1-206 2.54e-141

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: 392.51  E-value: 2.54e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115   1 MARSKTSAGWLKEHFDDRYVQKSRDDGYRSRASYKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAIEKVGESGVVIASD 80
Cdd:COG0293     3 MKRSKSSKRWLQRHLNDPYVKRAKKEGYRSRAAYKLLEIDEKDKLIKPGMRVVDLGAAPGGWSQVAAKRVGGKGRVIALD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  81 ILEMEPIADVTFIQGDFTEDKVYDEIMAAIGNRPVDMVISDMAPNMSGMSAMDQPRAMYLVELALDLASRTLKKEGTFLA 160
Cdd:COG0293    83 LLPMEPIPGVEFIQGDFREDEVLDQLLEALGGRKVDLVLSDMAPNTSGHKSVDHARSMYLVELALDFARKVLKPGGAFVV 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1090717115 161 KVFQGEGFDAYLKDLKSQFKTVITRKPDASRARSREVYLLAKGFKG 206
Cdd:COG0293   163 KVFQGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGFKG 208
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
3-206 4.02e-111

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


Pssm-ID: 183025  Cd Length: 209  Bit Score: 316.29  E-value: 4.02e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115   3 RSKTSAGWLKEHFDDRYVQKSRDDGYRSRASYKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAIEKVGESGVVIASDIL 82
Cdd:PRK11188    6 RSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYAVTQIGDKGRVIACDIL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  83 EMEPIADVTFIQGDFTEDKVYDEIMAAIGNRPVDMVISDMAPNMSGMSAMDQPRAMYLVELALDLASRTLKKEGTFLAKV 162
Cdd:PRK11188   86 PMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALDMCRDVLAPGGSFVVKV 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1090717115 163 FQGEGFDAYLKDLKSQFKTVITRKPDASRARSREVYLLAKGFKG 206
Cdd:PRK11188  166 FQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRKL 209
rrmJ TIGR00438
cell division protein FtsJ; Methylates the 23S rRNA. Previously known as cell division protein ...
 17-204 1.00e-89

cell division protein FtsJ; Methylates the 23S rRNA. Previously known as cell division protein ftsJ.// Trusted cutoff too high? [SS 10/1/04] [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273078  Cd Length: 188  Bit Score: 261.29  E-value: 1.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  17 DRYVQKSRDDGYRSRASYKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAIEKVGESGVVIASDILEMEPIADVTFIQGD 96
Cdd:TIGR00438   1 DFYYQKAKKEKYRSRASFKLLQLNQKFKLIKPGDTVLDLGAAPGGWSQVAVEQVGGKGRVIAVDLQPMKPIENVDFIRGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  97 FTEDKVYDEIMAAIGNRPVDMVISDMAPNMSGMSAMDQPRAMYLVELALDLASRTLKKEGTFLAKVFQGEGFDAYLKDLK 176
Cdd:TIGR00438  81 FTDEEVLNKIRERVGDDKVDVVMSDAAPNISGYWDIDHLRSIDLVELALDIAKEVLKPKGNFVVKVFQGEEIDEYLNELR 160

                         170       180
                  ....*....|....*....|....*...
gi 1090717115 177 SQFKTVITRKPDASRARSREVYLLAKGF 204
Cdd:TIGR00438 161 KLFEKVKVTKPQASRKRSAEVYIVAKRF 188
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 28-204 8.93e-72

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: 215.53  E-value: 8.93e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  28 YRSRASYKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAIEKVGesGVVIASDILEM---EPIAD--VTFIQGDFTEDKV 102
Cdd:pfam01728   1 YRSRAAYKLLEIDEKFGLLKPGKTVLDLGAAPGGWSQVALQRGA--GKVVGVDLGPMqlwKPRNDpgVTFIQGDIRDPET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115 103 YDEIMAAIGnRPVDMVISDMAPNMSGMSAMDQPRAMYLVELALDLASRTLKKEGTFLAKVFQGEGFDAYLKDLKSQFKTV 182
Cdd:pfam01728  79 LDLLEELLG-RKVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFVCKVFQGEDFSELLYLLKLGFEKV 157

                         170       180
                  ....*....|....*....|..
gi 1090717115 183 ITRKPDASRARSREVYLLAKGF 204
Cdd:pfam01728 158 GVFKPPASRPESSEEYLVCLGF 179
RlmM COG2933
23S rRNA C2498 (ribose-2'-O)-methylase RlmM [Translation, ribosomal structure and biogenesis]; ...
 30-64 3.89e-09

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: 55.24  E-value: 3.89e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1090717115  30 SRASYKLLE-------LDEKDRLFRSGMTVVDLGAAPGGWSQ 64
Cdd:COG2933   186 SRSTLKLEEafhvflpRDEWEERLRPGMRAVDLGAAPGGWTW 227
capping_2-OMTase_viral cd20754
viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-) ...
 34-202 1.17e-08

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: 52.44  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  34 YKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAiEKVGESGVVIASDILEMEPI--ADVTFIQGDFTEDKVYDEIMAaig 111
Cdd:cd20754     2 AKLLQLEEYFLYKPEKMRVIYIGCAPGGWLYYL-RDWFEGTLWVGFDPRDTDPLgyNNVITVNKFFDHEHTKLKFLP--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115 112 nRPVDMVISDMAPNMSGM-SAMDQPRAMYLVELAlDLASRTLKKEGTFLAKVFQGEGFDAYlkdlKSQFKTVITRKPDAS 190
Cdd:cd20754    78 -NKKDLLICDIRSDRSSHvTKEEDTTESFLTLQE-GYIATKLAKVGSICVKVRAPDLKDDG----HFSSGTLFPQPYAAS 151

                         170
                  ....*....|..
gi 1090717115 191 rarSREVYLLAK 202
Cdd:cd20754   152 ---SSEMRLFSA 160
PRK11760 PRK11760
putative 23S rRNA C2498 ribose 2'-O-ribose methyltransferase; Provisional
 30-63 4.19e-07

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


Pssm-ID: 236971 [Multi-domain]  Cd Length: 357  Bit Score: 49.06  E-value: 4.19e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1090717115  30 SRASYKLLEL-------DEKDRLFRSGMTVVDLGAAPGGWS 63
Cdd:PRK11760  186 SRSTLKLEEAfhvfiprDEWDERLAPGMRAVDLGAAPGGWT 226
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 47-160 3.73e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.02  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  47 RSGMTVVDLGAAPGGWSQIAIEKVGESGVVIASDI-----------LEMEPIADVTFIQGDFTedkvydEIMAAIGNRPV 115
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDIseeaiekarenAQKLGFDNVEFEQGDIE------ELPELLEDDKF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1090717115 116 DMVISDMAPNmsgmsamdqprAMYLVELALDLASRTLKKEGTFLA 160
Cdd:pfam13847  76 DVVISNCVLN-----------HIPDPDKVLQEILRVLKPGGRLII 109
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 51-163 2.19e-04

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: 39.34  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  51 TVVDLGAAPGGWSQIAIEKVGESgvVIASDILEM-----------EPIADVTFIQGDFTEDKVYdeimaaiGNRPVDMVI 119
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGAR--VTGVDISPValelarkaaaaLLADNVEVLKGDAEELPPE-------ADESFDVII 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1090717115 120 SDMAPNMSgmsamdqpraMYLVELALDLASRTLKKEGTFLAKVF 163
Cdd:cd02440    72 SDPPLHHL----------VEDLARFLEEARRLLKPGGVLVLTLV 105
capping_2-OMTase_Flaviviridae cd20761
Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; Cap-0 specific ...
 30-64 3.40e-04

Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; 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. Flaviviridae viruses, comprise a family of ss(+)RNA viruses, cap their mRNAs. The 2'OMTase activity is located in the non-structural protein 5 (NS5).


Pssm-ID: 467736  Cd Length: 225  Bit Score: 40.28  E-value: 3.40e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1090717115  30 SRASYKLLELDEKDRLFRSGmTVVDLGAAPGGWSQ 64
Cdd:cd20761    37 SRGYAKLRWLVERGYVKPSG-KVVDLGCGRGGWSQ 70
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 46-119 6.47e-04

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176226 [Multi-domain]  Cd Length: 384  Bit Score: 39.81  E-value: 6.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  46 FRSGMTVVDLGAAPGGWSQIAIEKVGESGVVIASDILE------MEPIADVTFIQGDFTEDKVYDEIMAAIGNRPVDMVI 119
Cdd:cd08265   201 FRPGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEISEerrnlaKEMGADYVFNPTKMRDCLSGEKVMEVTKGWGADIQV 280
SH3_Lasp1_C cd11934
C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic ...
 27-79 2.59e-03

C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic protein that binds focal adhesion proteins and is involved in cell signaling, migration, and proliferation. It is overexpressed in several cancer cells including breast, ovarian, bladder, and liver. In cancer cells, it can be found in the nucleus; its degree of nuclear localization correlates with tumor size and poor prognosis. Lasp1 is a 36kD protein containing an N-terminal LIM domain, two nebulin repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212867 [Multi-domain]  Cd Length: 59  Bit Score: 34.97  E-value: 2.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1090717115  27 GYRSRASYKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAIEKVGESGVVIAS 79
Cdd:cd11934     2 GKRYRAVYDYNAADEDEVSFQDGDTIVNVQQIDDGWMYGTVERTGDTGMLPAN 54
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 25-159 5.92e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 36.43  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717115  25 DDGYRSRASYKLLELDEKDRLFRSGMTVVDLGAAPGGWSQIAIEKVG---------ESGVVIASDILEMEPIADVTFIQG 95
Cdd:COG0500     3 DSYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGgrvigidlsPEAIALARARAAKAGLGNVEFLVA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1090717115  96 DFTEDKvydeimaAIGNRPVDMVISDMApnmsgMSAMDQPRAmylvELALDLASRTLKKEGTFL 159
Cdd:COG0500    83 DLAELD-------PLPAESFDLVVAFGV-----LHHLPPEER----EALLRELARALKPGGVLL 130
 
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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