NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|126815|sp|P25950|]
View 

RecName: Full=mRNA-capping enzyme catalytic subunit; AltName: Full=Virus termination factor large subunit; Short=VTF large subunit; AltName: Full=mRNA-capping enzyme 97 kDa subunit; AltName: Full=mRNA-capping enzyme large subunit; Includes: RecName: Full=Polynucleotide 5'-triphosphatase; AltName: Full=mRNA 5'-triphosphatase; Short=TPase; Includes: RecName: Full=mRNA guanylyltransferase; AltName: Full=GTP--RNA guanylyltransferase; Short=GTase; Includes: RecName: Full=mRNA (guanine-N(7))-methyltransferase; AltName: Full=mRNA cap methyltransferase

Protein Classification

Pox_ATPase-GT and AdoMet_MTases domain-containing protein( domain architecture ID 10566318)

Pox_ATPase-GT and AdoMet_MTases domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Pox_ATPase-GT pfam10640
mRNA capping enzyme N-terminal, ATPase and guanylyltransferase; This domain is the N-terminus ...
26-333 8.18e-163

mRNA capping enzyme N-terminal, ATPase and guanylyltransferase; This domain is the N-terminus of the large subunit viral mRNA capping enzyme, and carries both the ATPase and the guanylyltransferase activities of the enzyme. The guanylyltransferase enzymatic region runs from residues 242 (leucine)-273(arginine), the core of the acitve site being the lysine residue at 260. The ATPase activity is at the very N-terminal part of the domain.


:

Pssm-ID: 287595  Cd Length: 311  Bit Score: 475.32  E-value: 8.18e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815      26 PVQTDDMNHEVELTFIQPPVITLSTLLPFATSQESYILFTVTN--KGVKIRNRINLSKIHGLDLKNIQLVDSIDNIIWEK 103
Cdd:pfam10640   1 PDSTDDVNHEVELIFINPPLITLSNLLNIASKQESYILFTLTNkkKKVKIRTRIPLSKVHGLDVKNVQLVDSIDNIIWEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     104 KTLVKEHKIDSVALVKYSTEEKYIFLDYKKYLSAIKLELVNVVQVKVKHVTVDFKFKYFLGSGAQAKSSLLHVLNHPKSK 183
Cdd:pfam10640  81 KTLVSEKKIDEGCLLRHSTEEKHIFLDYKKYNSSIKLELVNLIQAKIKNIVVDFKIKYFLGSGAQAKSSLLHVLNHPKSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     184 PNPSLEFEIIT-TDEKIDSASLRKELIALFKLVFMASPSNIILDVVFKNPVQTILLKKNELPGIDLTNLYVTTKTDGVGV 262
Cdd:pfam10640 161 PNVTLEFEIVVlRDEKIDKNELLNELVTLFKALFMAPPDNIFLVPPPKPPIKTHMLKKQDLNTIDLDNLYVTTKTDGVGT 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126815     263 LITVTNKGIYCFFTHLQYTIRYDTTFESNESVTLYGEAVKQNNVWQIYLIKLITPKVSDRFKEKEYVEERL 333
Cdd:pfam10640 241 YVKVDKKGIYCYFSHLGYTIRYPARREIDNPVVLYGEAVKQNKVWNVYLIKLIEPALEDRLKERAFVEERL 311
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
560-836 5.14e-129

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.).


The actual alignment was detected with superfamily member pfam03291:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 332  Bit Score: 389.10  E-value: 5.14e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     560 LSNYVKTLLISLYCSKTFLdNSNKRKVLAIDFGNGADLEKYFYGEISSLVATDPDKEAIGRCIERYNSLNSGIKSKYYKF 639
Cdd:pfam03291  42 FNNWIKSLLISLYASKTFQ-NSNKRKVLDLGCGKGGDLEKWFKGGISQLIGTDIAEVSIEQCRERYNKLRSGNKSKYYKF 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     640 DYiqETIRSVTYVSSVREVF--FFGKFDLVDWQFAIHYSFHPKHYA-TVMNNLTELTASGGKVLITTMDGDLLSQLTDKK 716
Cdd:pfam03291 121 DA--EFITGDCFVSSLREVFedPFGKFDIVSCQFAIHYSFESEEKArTMLRNVAELLASGGVFIGTTPDSDFISALTIKR 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     717 TFVIHKNLPSSENYMSVEKIHEDQILV--------YNPSSMSRPMQEYIVKRVNLTKIFSEYGFELIDCVHFDTIIERS- 787
Cdd:pfam03291 199 LFAIEKDLPSFGNSIYSVKFEEEPPQVplfgikydYNLEDAVDDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEi 278
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 126815     788 ----KRFINSVSKMEERKSTKNFFELNREALK-HEGTDIDDLLRYYIVYVFSKR 836
Cdd:pfam03291 279 kkefKKLIKRMSAMESRPSTRNFFGLQRSAGKgTLGGDEWEAASFYLVFVFEKR 332
 
Name Accession Description Interval E-value
Pox_ATPase-GT pfam10640
mRNA capping enzyme N-terminal, ATPase and guanylyltransferase; This domain is the N-terminus ...
26-333 8.18e-163

mRNA capping enzyme N-terminal, ATPase and guanylyltransferase; This domain is the N-terminus of the large subunit viral mRNA capping enzyme, and carries both the ATPase and the guanylyltransferase activities of the enzyme. The guanylyltransferase enzymatic region runs from residues 242 (leucine)-273(arginine), the core of the acitve site being the lysine residue at 260. The ATPase activity is at the very N-terminal part of the domain.


Pssm-ID: 287595  Cd Length: 311  Bit Score: 475.32  E-value: 8.18e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815      26 PVQTDDMNHEVELTFIQPPVITLSTLLPFATSQESYILFTVTN--KGVKIRNRINLSKIHGLDLKNIQLVDSIDNIIWEK 103
Cdd:pfam10640   1 PDSTDDVNHEVELIFINPPLITLSNLLNIASKQESYILFTLTNkkKKVKIRTRIPLSKVHGLDVKNVQLVDSIDNIIWEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     104 KTLVKEHKIDSVALVKYSTEEKYIFLDYKKYLSAIKLELVNVVQVKVKHVTVDFKFKYFLGSGAQAKSSLLHVLNHPKSK 183
Cdd:pfam10640  81 KTLVSEKKIDEGCLLRHSTEEKHIFLDYKKYNSSIKLELVNLIQAKIKNIVVDFKIKYFLGSGAQAKSSLLHVLNHPKSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     184 PNPSLEFEIIT-TDEKIDSASLRKELIALFKLVFMASPSNIILDVVFKNPVQTILLKKNELPGIDLTNLYVTTKTDGVGV 262
Cdd:pfam10640 161 PNVTLEFEIVVlRDEKIDKNELLNELVTLFKALFMAPPDNIFLVPPPKPPIKTHMLKKQDLNTIDLDNLYVTTKTDGVGT 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126815     263 LITVTNKGIYCFFTHLQYTIRYDTTFESNESVTLYGEAVKQNNVWQIYLIKLITPKVSDRFKEKEYVEERL 333
Cdd:pfam10640 241 YVKVDKKGIYCYFSHLGYTIRYPARREIDNPVVLYGEAVKQNKVWNVYLIKLIEPALEDRLKERAFVEERL 311
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
560-836 5.14e-129

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 389.10  E-value: 5.14e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     560 LSNYVKTLLISLYCSKTFLdNSNKRKVLAIDFGNGADLEKYFYGEISSLVATDPDKEAIGRCIERYNSLNSGIKSKYYKF 639
Cdd:pfam03291  42 FNNWIKSLLISLYASKTFQ-NSNKRKVLDLGCGKGGDLEKWFKGGISQLIGTDIAEVSIEQCRERYNKLRSGNKSKYYKF 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     640 DYiqETIRSVTYVSSVREVF--FFGKFDLVDWQFAIHYSFHPKHYA-TVMNNLTELTASGGKVLITTMDGDLLSQLTDKK 716
Cdd:pfam03291 121 DA--EFITGDCFVSSLREVFedPFGKFDIVSCQFAIHYSFESEEKArTMLRNVAELLASGGVFIGTTPDSDFISALTIKR 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     717 TFVIHKNLPSSENYMSVEKIHEDQILV--------YNPSSMSRPMQEYIVKRVNLTKIFSEYGFELIDCVHFDTIIERS- 787
Cdd:pfam03291 199 LFAIEKDLPSFGNSIYSVKFEEEPPQVplfgikydYNLEDAVDDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEi 278
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 126815     788 ----KRFINSVSKMEERKSTKNFFELNREALK-HEGTDIDDLLRYYIVYVFSKR 836
Cdd:pfam03291 279 kkefKKLIKRMSAMESRPSTRNFFGLQRSAGKgTLGGDEWEAASFYLVFVFEKR 332
 
Name Accession Description Interval E-value
Pox_ATPase-GT pfam10640
mRNA capping enzyme N-terminal, ATPase and guanylyltransferase; This domain is the N-terminus ...
26-333 8.18e-163

mRNA capping enzyme N-terminal, ATPase and guanylyltransferase; This domain is the N-terminus of the large subunit viral mRNA capping enzyme, and carries both the ATPase and the guanylyltransferase activities of the enzyme. The guanylyltransferase enzymatic region runs from residues 242 (leucine)-273(arginine), the core of the acitve site being the lysine residue at 260. The ATPase activity is at the very N-terminal part of the domain.


Pssm-ID: 287595  Cd Length: 311  Bit Score: 475.32  E-value: 8.18e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815      26 PVQTDDMNHEVELTFIQPPVITLSTLLPFATSQESYILFTVTN--KGVKIRNRINLSKIHGLDLKNIQLVDSIDNIIWEK 103
Cdd:pfam10640   1 PDSTDDVNHEVELIFINPPLITLSNLLNIASKQESYILFTLTNkkKKVKIRTRIPLSKVHGLDVKNVQLVDSIDNIIWEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     104 KTLVKEHKIDSVALVKYSTEEKYIFLDYKKYLSAIKLELVNVVQVKVKHVTVDFKFKYFLGSGAQAKSSLLHVLNHPKSK 183
Cdd:pfam10640  81 KTLVSEKKIDEGCLLRHSTEEKHIFLDYKKYNSSIKLELVNLIQAKIKNIVVDFKIKYFLGSGAQAKSSLLHVLNHPKSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     184 PNPSLEFEIIT-TDEKIDSASLRKELIALFKLVFMASPSNIILDVVFKNPVQTILLKKNELPGIDLTNLYVTTKTDGVGV 262
Cdd:pfam10640 161 PNVTLEFEIVVlRDEKIDKNELLNELVTLFKALFMAPPDNIFLVPPPKPPIKTHMLKKQDLNTIDLDNLYVTTKTDGVGT 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126815     263 LITVTNKGIYCFFTHLQYTIRYDTTFESNESVTLYGEAVKQNNVWQIYLIKLITPKVSDRFKEKEYVEERL 333
Cdd:pfam10640 241 YVKVDKKGIYCYFSHLGYTIRYPARREIDNPVVLYGEAVKQNKVWNVYLIKLIEPALEDRLKERAFVEERL 311
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
560-836 5.14e-129

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 389.10  E-value: 5.14e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     560 LSNYVKTLLISLYCSKTFLdNSNKRKVLAIDFGNGADLEKYFYGEISSLVATDPDKEAIGRCIERYNSLNSGIKSKYYKF 639
Cdd:pfam03291  42 FNNWIKSLLISLYASKTFQ-NSNKRKVLDLGCGKGGDLEKWFKGGISQLIGTDIAEVSIEQCRERYNKLRSGNKSKYYKF 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     640 DYiqETIRSVTYVSSVREVF--FFGKFDLVDWQFAIHYSFHPKHYA-TVMNNLTELTASGGKVLITTMDGDLLSQLTDKK 716
Cdd:pfam03291 121 DA--EFITGDCFVSSLREVFedPFGKFDIVSCQFAIHYSFESEEKArTMLRNVAELLASGGVFIGTTPDSDFISALTIKR 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126815     717 TFVIHKNLPSSENYMSVEKIHEDQILV--------YNPSSMSRPMQEYIVKRVNLTKIFSEYGFELIDCVHFDTIIERS- 787
Cdd:pfam03291 199 LFAIEKDLPSFGNSIYSVKFEEEPPQVplfgikydYNLEDAVDDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEi 278
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 126815     788 ----KRFINSVSKMEERKSTKNFFELNREALK-HEGTDIDDLLRYYIVYVFSKR 836
Cdd:pfam03291 279 kkefKKLIKRMSAMESRPSTRNFFGLQRSAGKgTLGGDEWEAASFYLVFVFEKR 332
 
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