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Conserved domains on  [gi|2073491212|gb|QYA73756|]
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polyprotein [Sweet potato chlorotic stunt virus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Vmethyltransf super family cl46422
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ...
561-813 3.32e-23

Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA viruses, including Hordei-, Tobra-, Tobamo-, Bromo-, Clostero- and Caliciviruses. This methyltransferase is involved in mRNA capping. Capping of mRNA enhances its stability. This usually occurs in the nucleus. Therefore, many viruses that replicate in the cytoplasm encode their own. This is a specific guanine-7-methyltransferase domain involved in viral mRNA cap0 synthesis. Specificity for guanine 7 position is shown by NMR in and in vivo role in cap synthesis. Based on secondary structure prediction, the basic fold is believed to be similar to the common AdoMet-dependent methyltransferase fold. A curious feature of this methyltransferase domain is that it together with flanking sequences seems to have guanylyltransferase activity coupled to the methyltransferase activity. The domain is found throughout the so-called Alphavirus superfamily, (including alphaviruses and several other groups). It forms the defining, unique feature of this superfamily.


The actual alignment was detected with superfamily member pfam01660:

Pssm-ID: 480762  Cd Length: 308  Bit Score: 102.38  E-value: 3.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212  561 LDSNQKRKLTKLfpevTMNFEDSTY--SSHPLQTAMRTCENF-VMDKKCGGREYIDVGGDVVSLLCKESKDVHLCCPVVD 637
Cdd:pfam01660    5 LSPEAQELLENL----GIEFSPYSVtpHSHPAAKALENLLLEvLPSYLPNPSTVLDIKGSKLRHLKRGNPNVHCCNPILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212  638 VKDAHRHITRSNIIDRMKGFDESITicDKLTQDCDVSYP---NIVAV-EVYDMSLEDMARSILSH-KAKRFDLSLIIPPE 712
Cdd:pfam01660   81 PRDVARYPEAFSLEKSLGNGEDLRP--TNTFEDCRVLAPttsYAFMHdSLHDWSPEELADLFLRKpKLERLYATLVFPPE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212  713 ICDsYCDVLLFDDSMRVFVREGVVNYEYGSS-GECYRHDLKTLQdILRVQLFVV-DGVVFKKTLECSREQLHFYSIVPCv 790
Cdd:pfam01660  159 LLF-GDKESLYPELYTFWYKGDRFHFYPDGHlGGSYTHPLNLLS-WLTTSKIHLpGGFTYTVERLESRGAHHLFKITRG- 235
                          250       260
                   ....*....|....*....|...
gi 2073491212  791 NMKPGVYNLTSHYSKSRNDKVEM 813
Cdd:pfam01660  236 DGLTPKVIVPDSRTFGPFEAVLL 258
Viral_helicase1 super family cl26263
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
1690-1953 2.09e-20

Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated and NTPase activity. This helicase has multiple roles at different stages of viral RNA replication, as dissected by mutational analysis.


The actual alignment was detected with superfamily member pfam01443:

Pssm-ID: 366646 [Multi-domain]  Cd Length: 227  Bit Score: 92.06  E-value: 2.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212 1690 PGAGKTTTIVNefsrLHNEGKRCLaltctkagkiEIAEKLKARGIKSVFSNCLTYDAFLMKNTYRDVDYVFCDEIFMIHA 1769
Cdd:pfam01443    7 PGCGKSTLIRK----LLRTSRVIR----------PTAELRTEGKPDLPNLNVRTVDTFLMALLKPTGKILILDEYTLLPP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212 1770 GLWLAITCNLEFSSMSCYGDVNQIPYINRVPNTictkSMNHFYAyemfhdNISYRCPVDVCKLLSTLtdntgkliypkgV 1849
Cdd:pfam01443   73 GYILLLAAISGAKLVILFGDPLQIPYHSRAPSF----LIPHFPS------SLSHRVGRRTTYLLPSL------------R 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212 1850 YPV----GDNANVLRSLQIVPIYSPEDAMddqNVKIVTFTQPEKEEMikatrmrngvSSSVNTVNEVQGGTFSKVDVYRL 1925
Cdd:pfam01443  131 APIlsakGFEVVVERSGEYKVDYDPNGVL---VLVYLTFTQALKESL----------GVRVTTVHEVQGLTFDSVTLVLD 197
                          250       260
                   ....*....|....*....|....*....
gi 2073491212 1926 KPYDNPIYS-DLNQFVVSISRHTQLMRYR 1953
Cdd:pfam01443  198 TDTDLLIISdSPEHLYVALTRHRKSLHIL 226
 
Name Accession Description Interval E-value
Vmethyltransf pfam01660
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ...
561-813 3.32e-23

Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA viruses, including Hordei-, Tobra-, Tobamo-, Bromo-, Clostero- and Caliciviruses. This methyltransferase is involved in mRNA capping. Capping of mRNA enhances its stability. This usually occurs in the nucleus. Therefore, many viruses that replicate in the cytoplasm encode their own. This is a specific guanine-7-methyltransferase domain involved in viral mRNA cap0 synthesis. Specificity for guanine 7 position is shown by NMR in and in vivo role in cap synthesis. Based on secondary structure prediction, the basic fold is believed to be similar to the common AdoMet-dependent methyltransferase fold. A curious feature of this methyltransferase domain is that it together with flanking sequences seems to have guanylyltransferase activity coupled to the methyltransferase activity. The domain is found throughout the so-called Alphavirus superfamily, (including alphaviruses and several other groups). It forms the defining, unique feature of this superfamily.


Pssm-ID: 396298  Cd Length: 308  Bit Score: 102.38  E-value: 3.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212  561 LDSNQKRKLTKLfpevTMNFEDSTY--SSHPLQTAMRTCENF-VMDKKCGGREYIDVGGDVVSLLCKESKDVHLCCPVVD 637
Cdd:pfam01660    5 LSPEAQELLENL----GIEFSPYSVtpHSHPAAKALENLLLEvLPSYLPNPSTVLDIKGSKLRHLKRGNPNVHCCNPILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212  638 VKDAHRHITRSNIIDRMKGFDESITicDKLTQDCDVSYP---NIVAV-EVYDMSLEDMARSILSH-KAKRFDLSLIIPPE 712
Cdd:pfam01660   81 PRDVARYPEAFSLEKSLGNGEDLRP--TNTFEDCRVLAPttsYAFMHdSLHDWSPEELADLFLRKpKLERLYATLVFPPE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212  713 ICDsYCDVLLFDDSMRVFVREGVVNYEYGSS-GECYRHDLKTLQdILRVQLFVV-DGVVFKKTLECSREQLHFYSIVPCv 790
Cdd:pfam01660  159 LLF-GDKESLYPELYTFWYKGDRFHFYPDGHlGGSYTHPLNLLS-WLTTSKIHLpGGFTYTVERLESRGAHHLFKITRG- 235
                          250       260
                   ....*....|....*....|...
gi 2073491212  791 NMKPGVYNLTSHYSKSRNDKVEM 813
Cdd:pfam01660  236 DGLTPKVIVPDSRTFGPFEAVLL 258
Viral_helicase1 pfam01443
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
1690-1953 2.09e-20

Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated and NTPase activity. This helicase has multiple roles at different stages of viral RNA replication, as dissected by mutational analysis.


Pssm-ID: 366646 [Multi-domain]  Cd Length: 227  Bit Score: 92.06  E-value: 2.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212 1690 PGAGKTTTIVNefsrLHNEGKRCLaltctkagkiEIAEKLKARGIKSVFSNCLTYDAFLMKNTYRDVDYVFCDEIFMIHA 1769
Cdd:pfam01443    7 PGCGKSTLIRK----LLRTSRVIR----------PTAELRTEGKPDLPNLNVRTVDTFLMALLKPTGKILILDEYTLLPP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212 1770 GLWLAITCNLEFSSMSCYGDVNQIPYINRVPNTictkSMNHFYAyemfhdNISYRCPVDVCKLLSTLtdntgkliypkgV 1849
Cdd:pfam01443   73 GYILLLAAISGAKLVILFGDPLQIPYHSRAPSF----LIPHFPS------SLSHRVGRRTTYLLPSL------------R 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212 1850 YPV----GDNANVLRSLQIVPIYSPEDAMddqNVKIVTFTQPEKEEMikatrmrngvSSSVNTVNEVQGGTFSKVDVYRL 1925
Cdd:pfam01443  131 APIlsakGFEVVVERSGEYKVDYDPNGVL---VLVYLTFTQALKESL----------GVRVTTVHEVQGLTFDSVTLVLD 197
                          250       260
                   ....*....|....*....|....*....
gi 2073491212 1926 KPYDNPIYS-DLNQFVVSISRHTQLMRYR 1953
Cdd:pfam01443  198 TDTDLLIISdSPEHLYVALTRHRKSLHIL 226
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
1690-1758 4.68e-03

DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350690 [Multi-domain]  Cd Length: 189  Bit Score: 40.19  E-value: 4.68e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2073491212 1690 PGAGKTTTIVNEFSRLHNEGK----RCLALTCTKAGKIEIAEKLKARGIKSVFS--NCLTYDAFLMKNTYRDVDY 1758
Cdd:cd17932     21 AGSGKTRVLTHRIAYLILEGGvppeRILAVTFTNKAAKEMRERLRKLLGEQLASgvWIGTFHSFALRILRRYGDF 95
 
Name Accession Description Interval E-value
Vmethyltransf pfam01660
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ...
561-813 3.32e-23

Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA viruses, including Hordei-, Tobra-, Tobamo-, Bromo-, Clostero- and Caliciviruses. This methyltransferase is involved in mRNA capping. Capping of mRNA enhances its stability. This usually occurs in the nucleus. Therefore, many viruses that replicate in the cytoplasm encode their own. This is a specific guanine-7-methyltransferase domain involved in viral mRNA cap0 synthesis. Specificity for guanine 7 position is shown by NMR in and in vivo role in cap synthesis. Based on secondary structure prediction, the basic fold is believed to be similar to the common AdoMet-dependent methyltransferase fold. A curious feature of this methyltransferase domain is that it together with flanking sequences seems to have guanylyltransferase activity coupled to the methyltransferase activity. The domain is found throughout the so-called Alphavirus superfamily, (including alphaviruses and several other groups). It forms the defining, unique feature of this superfamily.


Pssm-ID: 396298  Cd Length: 308  Bit Score: 102.38  E-value: 3.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212  561 LDSNQKRKLTKLfpevTMNFEDSTY--SSHPLQTAMRTCENF-VMDKKCGGREYIDVGGDVVSLLCKESKDVHLCCPVVD 637
Cdd:pfam01660    5 LSPEAQELLENL----GIEFSPYSVtpHSHPAAKALENLLLEvLPSYLPNPSTVLDIKGSKLRHLKRGNPNVHCCNPILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212  638 VKDAHRHITRSNIIDRMKGFDESITicDKLTQDCDVSYP---NIVAV-EVYDMSLEDMARSILSH-KAKRFDLSLIIPPE 712
Cdd:pfam01660   81 PRDVARYPEAFSLEKSLGNGEDLRP--TNTFEDCRVLAPttsYAFMHdSLHDWSPEELADLFLRKpKLERLYATLVFPPE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212  713 ICDsYCDVLLFDDSMRVFVREGVVNYEYGSS-GECYRHDLKTLQdILRVQLFVV-DGVVFKKTLECSREQLHFYSIVPCv 790
Cdd:pfam01660  159 LLF-GDKESLYPELYTFWYKGDRFHFYPDGHlGGSYTHPLNLLS-WLTTSKIHLpGGFTYTVERLESRGAHHLFKITRG- 235
                          250       260
                   ....*....|....*....|...
gi 2073491212  791 NMKPGVYNLTSHYSKSRNDKVEM 813
Cdd:pfam01660  236 DGLTPKVIVPDSRTFGPFEAVLL 258
Viral_helicase1 pfam01443
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
1690-1953 2.09e-20

Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated and NTPase activity. This helicase has multiple roles at different stages of viral RNA replication, as dissected by mutational analysis.


Pssm-ID: 366646 [Multi-domain]  Cd Length: 227  Bit Score: 92.06  E-value: 2.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212 1690 PGAGKTTTIVNefsrLHNEGKRCLaltctkagkiEIAEKLKARGIKSVFSNCLTYDAFLMKNTYRDVDYVFCDEIFMIHA 1769
Cdd:pfam01443    7 PGCGKSTLIRK----LLRTSRVIR----------PTAELRTEGKPDLPNLNVRTVDTFLMALLKPTGKILILDEYTLLPP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212 1770 GLWLAITCNLEFSSMSCYGDVNQIPYINRVPNTictkSMNHFYAyemfhdNISYRCPVDVCKLLSTLtdntgkliypkgV 1849
Cdd:pfam01443   73 GYILLLAAISGAKLVILFGDPLQIPYHSRAPSF----LIPHFPS------SLSHRVGRRTTYLLPSL------------R 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212 1850 YPV----GDNANVLRSLQIVPIYSPEDAMddqNVKIVTFTQPEKEEMikatrmrngvSSSVNTVNEVQGGTFSKVDVYRL 1925
Cdd:pfam01443  131 APIlsakGFEVVVERSGEYKVDYDPNGVL---VLVYLTFTQALKESL----------GVRVTTVHEVQGLTFDSVTLVLD 197
                          250       260
                   ....*....|....*....|....*....
gi 2073491212 1926 KPYDNPIYS-DLNQFVVSISRHTQLMRYR 1953
Cdd:pfam01443  198 TDTDLLIISdSPEHLYVALTRHRKSLHIL 226
AAA_19 pfam13245
AAA domain;
1679-1796 9.51e-04

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 41.43  E-value: 9.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073491212 1679 LTHKVKFFNKPPGAGKTTT---IVNEFSRLHNEGKRCLALTCTKAGKIEIAEKLKARGikSVFSNCLTYD---AFLMKN- 1751
Cdd:pfam13245    9 LPSKVVLLTGGPGTGKTTTirhIVALLVALGGVSFPILLAAPTGRAAKRLSERTGLPA--STIHRLLGFDdleAGGFLRd 86
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2073491212 1752 --TYRDVDYVFCDEIFMIhaGLWLAIT--------CNLEFssmscYGDVNQIPYI 1796
Cdd:pfam13245   87 eeEPLDGDLLIVDEFSMV--DLPLAYRllkalpdgAQLLL-----VGDPDQLPSV 134
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
1690-1758 4.68e-03

DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350690 [Multi-domain]  Cd Length: 189  Bit Score: 40.19  E-value: 4.68e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2073491212 1690 PGAGKTTTIVNEFSRLHNEGK----RCLALTCTKAGKIEIAEKLKARGIKSVFS--NCLTYDAFLMKNTYRDVDY 1758
Cdd:cd17932     21 AGSGKTRVLTHRIAYLILEGGvppeRILAVTFTNKAAKEMRERLRKLLGEQLASgvWIGTFHSFALRILRRYGDF 95
 
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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