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Conserved domains on  [gi|1912461801|gb|QOE77944|]
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polyprotein [Sclerotinia sclerotiorum mycoalphavirus virus 1]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ps-ssRNAv_RdRp-like super family cl40470
conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense ...
1174-1352 8.23e-15

conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense single-stranded RNA [(+)ssRNA] viruses and closely related viruses; This family contains the catalytic core domain of RdRp of RNA viruses which belong to Group IV of the Baltimore classification system, and are a group of related viruses that have positive-sense (+), single-stranded (ss) genomes made of ribonucleic acid (RNA). RdRp (also known as RNA replicase) catalyzes the replication of RNA from an RNA template; specifically, it catalyzes the synthesis of the RNA strand complementary to a given RNA template. The Baltimore Classification is divided into 7 classes, 3 of which include RNA viruses: Group IV (+) RNA viruses, Group III double-stranded (ds) RNA viruses, and Group V negative-sense (-) RNA viruses. Baltimore groups of viruses differ with respect to the nature of their genome (i.e., the nucleic acid form that is packaged into virions) and correspond to distinct strategies of genome replication and expression. (+) viral RNA is similar to mRNA and thus can be immediately translated by the host cell. (+)ssRNA viruses can also produce (+) copies of the genome from (-) strands of an intermediate dsRNA genome. This acts as both a transcription and a replication process since the replicated RNA is also mRNA. RdRps belong to the expansive class of polymerases containing so-called palm catalytic domains along with the accessory fingers and thumb domains. All RdRps also have six conserved structural motifs (A-F), located in its majority in the palm subdomain (A-E motifs) and the F motif is located on the finger subdomain. All these motifs have been shown to be implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides. In addition to Group IV viruses, this model also includes Picobirnaviruses (PBVs), members of the family Picobirnaviridae of dsRNA viruses (Baltimore classification Group III), which are bi-segmented dsRNA viruses. The phylogenetic tree of the RdRps of RNA viruses (realm Riboviria) showed that picobirnaviruses are embedded in the branch of diverse (+)RNA viruses; sometimes they are collectively referred to as the picornavirus supergroup. RdRps of members of the family Permutatetraviridae, a distinct group of RNA viruses that encompass a circular permutation within the RdRp palm domain, are not included in this model.


The actual alignment was detected with superfamily member cd23209:

Pssm-ID: 477363 [Multi-domain]  Cd Length: 183  Bit Score: 74.83  E-value: 8.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1174 TYFLKAQGKPKFGITGFSIASGQGILATDKLLNACTCPFTTAAADAMQRLLKPGFIYDQHYEAKDLDDAI----YAVVGp 1249
Cdd:cd23209      4 TFFQKDCRKFTDCEPVAHGKAGQGISAWSKELCFVFGPWFRALEKILRRALKPNVLYANGHEAEPFVDKInqahSAVFI- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1250 gphrslSIDLTQQDSSHTLVHRLIIGKVMKFLGFGDDVISLYLLSREKRhVLGLKLpVSFDVIERLFSGEPGTAFFNFIM 1329
Cdd:cd23209     83 ------ENDFTEFDSTQNLFSLLVELEILEACGMPPALAELYRALRAKW-TLQARE-GSLEGTCKKTSGEPGTLLHNTIW 154
                          170       180
                   ....*....|....*....|...
gi 1912461801 1330 STSTTAMTHDLSRVKLFVGKGDD 1352
Cdd:cd23209    155 NMAVMMHMVRGGVRKAAAFKGDD 177
Vmethyltransf super family cl46422
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ...
168-455 5.24e-12

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: 69.25  E-value: 5.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  168 VASNLSNEAHEKLCDL-FDYNIFQATaPSNHPALAAFRTLCHQYVYHKVGANN-ILEVGPN-LGKMATNHKFVpaHSCSP 244
Cdd:pfam01660    1 FPYALSPEAQELLENLgIEFSPYSVT-PHSHPAAKALENLLLEVLPSYLPNPStVLDIKGSkLRHLKRGNPNV--HCCNP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  245 TLDGRDEArailmgtrinkRHTAAntkmlLDRSNGVFSSPQRMCNNKVEDCDVQAPVIYSAF---SLQDAQPSDIPAIMD 321
Cdd:pfam01660   78 ILDPRDVA-----------RYPEA-----FSLEKSLGNGEDLRPTNTFEDCRVLAPTTSYAFmhdSLHDWSPEELADLFL 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  322 RHGSR-TAYILLMLPV-PLAYADEFREDDTGCVWKRDG-----PMATCNpgyndAGYSHNMEkIQRW-----VDGFDGLP 389
Cdd:pfam01660  142 RKPKLeRLYATLVFPPeLLFGDKESLYPELYTFWYKGDrfhfyPDGHLG-----GSYTHPLN-LLSWlttskIHLPGGFT 215
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1912461801  390 LFAEVEKQFGSSYLFKITRAT-------VGSAASYPINIATLMDQ-FVLitGTTGASVNFLTSASHYEKLTSYL 455
Cdd:pfam01660  216 YTVERLESRGAHHLFKITRGDgltpkviVPDSRTFGPFEAVLLPKiFVP--RVLNYIRGKPIPLTVVNKLFSYL 287
Viral_helicase1 super family cl26263
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
715-944 3.76e-10

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: 62.40  E-value: 3.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  715 GPAGTGKST---DAFRMlpagSLVLVPTNKLANDTAAAHPDMIVRTFDTAV--AKAHEYQDVpaiFIDEVFLCPHLYVLS 789
Cdd:pfam01443    5 GVPGCGKSTlirKLLRT----SRVIRPTAELRTEGKPDLPNLNVRTVDTFLmaLLKPTGKIL---ILDEYTLLPPGYILL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  790 MATL--GKPIIAAGCPGQRRYNGNLGPAFDPHSIP-VDHVALYRTIHRFGPDVTAQVERHAGPIYramfnlgpgaVFAPG 866
Cdd:pfam01443   78 LAAIsgAKLVILFGDPLQIPYHSRAPSFLIPHFPSsLSHRVGRRTTYLLPSLRAPILSAKGFEVV----------VERSG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  867 PNNNIRnTFQGPGM--NLVCHHNNISRVSPNAITIDSSQGSQYPDVLLHV-FSTDLPFFLANPYALSLALSRTTGAVTII 943
Cdd:pfam01443  148 EYKVDY-DPNGVLVlvYLTFTQALKESLGVRVTTVHEVQGLTFDSVTLVLdTDTDLLIISDSPEHLYVALTRHRKSLHIL 226

                   .
gi 1912461801  944 N 944
Cdd:pfam01443  227 T 227
Viral_helicase1 super family cl26263
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
2103-2356 3.41e-06

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: 50.46  E-value: 3.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 2103 LLVDAVACAGKTTALRNTLPPTAAV--GVICHSREFADEWADHGYT--AYTMHQFRnsaSHHETIVVDEVFRFPTWFLAE 2178
Cdd:pfam01443    1 IVVHGVPGCGKSTLIRKLLRTSRVIrpTAELRTEGKPDLPNLNVRTvdTFLMALLK---PTGKILILDEYTLLPPGYILL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 2179 VIA-SCVKF-ICLGDSEQTPlltYPDKHYDPdafdpgrfrVRRRFTARTAHALPPQHArfvqlYLYeaqRALASPAPSKY 2256
Cdd:pfam01443   78 LAAiSGAKLvILFGDPLQIP---YHSRAPSF---------LIPHFPSSLSHRVGRRTT-----YLL---PSLRAPILSAK 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 2257 LSPMFVANGLRTGRITmyhnmPLVPRNADLYIASSEgatNNFRRLMpevaDRIYSVERAQGMRHKHVVILV-EPGYVNFP 2335
Cdd:pfam01443  138 GFEVVVERSGEYKVDY-----DPNGVLVLVYLTFTQ---ALKESLG----VRVTTVHEVQGLTFDSVTLVLdTDTDLLII 205
                          250       260
                   ....*....|....*....|.
gi 1912461801 2336 FTNPWLVVVAFTRSTELLEVF 2356
Cdd:pfam01443  206 SDSPEHLYVALTRHRKSLHIL 226
 
Name Accession Description Interval E-value
ps-ssRNAv_Hepelivirales_RdRp cd23209
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Hepelivirales of ...
1174-1352 8.23e-15

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Hepelivirales of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the order Hepelivirales, class Alsuviricetes. This Hepelivirales order consists of four families: Alphatetraviridae, Benyviridae, Hepeviridae, and Matonaviridae. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438059 [Multi-domain]  Cd Length: 183  Bit Score: 74.83  E-value: 8.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1174 TYFLKAQGKPKFGITGFSIASGQGILATDKLLNACTCPFTTAAADAMQRLLKPGFIYDQHYEAKDLDDAI----YAVVGp 1249
Cdd:cd23209      4 TFFQKDCRKFTDCEPVAHGKAGQGISAWSKELCFVFGPWFRALEKILRRALKPNVLYANGHEAEPFVDKInqahSAVFI- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1250 gphrslSIDLTQQDSSHTLVHRLIIGKVMKFLGFGDDVISLYLLSREKRhVLGLKLpVSFDVIERLFSGEPGTAFFNFIM 1329
Cdd:cd23209     83 ------ENDFTEFDSTQNLFSLLVELEILEACGMPPALAELYRALRAKW-TLQARE-GSLEGTCKKTSGEPGTLLHNTIW 154
                          170       180
                   ....*....|....*....|...
gi 1912461801 1330 STSTTAMTHDLSRVKLFVGKGDD 1352
Cdd:cd23209    155 NMAVMMHMVRGGVRKAAAFKGDD 177
RdRP_2 pfam00978
RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The ...
1091-1427 3.41e-12

RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The family also contains the following proteins: 2A protein from bromoviruses putative RNA dependent RNA polymerase from tobamoviruses Non structural polyprotein from togaviruses


Pssm-ID: 395779  Cd Length: 440  Bit Score: 71.13  E-value: 3.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1091 ALYAIadryvKHQNVNMP--------LSRAAQLADMAFEawrvSFINP---KASAAIPSASFLAQHWLSGRSLSQVAAIL 1159
Cdd:pfam00978   48 VLLAL-----KKRNFNVPelqesvdlDDTAERVAERFKK----SFLDKeklDKLDPIINTTENVSRWLDKQSGKKAAQLK 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1160 R------AEDNTGTARMMsatyfLKAQGKPKFGITG-FSIASGQGILATDKLLNACTCPFTTAAADAMQRLLKPGFIYdq 1232
Cdd:pfam00978  119 LddlvplHEVDLDRYKHM-----IKSDVKPKLDLSPqSERPALQTITYHDKGVTAYFSPIFRELFERLLYVLKPKIVF-- 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1233 hYEAKDLDDAIYAV-VGPGPHRSLSIDLTQ----QDSSHTLVHRLIigkvMKFLGFGDDVISLYLLSREKRHVLGLKLPV 1307
Cdd:pfam00978  192 -PTGMTSSLIAEHFeFLDASEDFLEIDFSKfdksQGELHLLVQLEI----LKLLGLDPELADLWFKFHRQSYIKDRKNGV 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1308 SFDVIERLFSGEPGTAFFNFIMSTSTTAMTHDLSRVKLFVGKGDDN-----STIP-PAPRKTLAFNY-CKetgvtqktdv 1380
Cdd:pfam00978  267 GFSVDYQRKSGDANTYLGNTLVTMAMLASVYDLEKIDCAAFSGDDSlifspKPIEdPASRFATLFNMeAK---------- 336
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1912461801 1381 cdYFDFANR------IWTSSGRSFS--DPIRMLSKFTCRLRGRDNT--GEEYQAFMD 1427
Cdd:pfam00978  337 --VFDPSVPyfcskfLLEVDGGAFFvpDPLKLLQKLGKKKIPDDEQhlDEIFTSLCD 391
Vmethyltransf pfam01660
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ...
168-455 5.24e-12

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: 69.25  E-value: 5.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  168 VASNLSNEAHEKLCDL-FDYNIFQATaPSNHPALAAFRTLCHQYVYHKVGANN-ILEVGPN-LGKMATNHKFVpaHSCSP 244
Cdd:pfam01660    1 FPYALSPEAQELLENLgIEFSPYSVT-PHSHPAAKALENLLLEVLPSYLPNPStVLDIKGSkLRHLKRGNPNV--HCCNP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  245 TLDGRDEArailmgtrinkRHTAAntkmlLDRSNGVFSSPQRMCNNKVEDCDVQAPVIYSAF---SLQDAQPSDIPAIMD 321
Cdd:pfam01660   78 ILDPRDVA-----------RYPEA-----FSLEKSLGNGEDLRPTNTFEDCRVLAPTTSYAFmhdSLHDWSPEELADLFL 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  322 RHGSR-TAYILLMLPV-PLAYADEFREDDTGCVWKRDG-----PMATCNpgyndAGYSHNMEkIQRW-----VDGFDGLP 389
Cdd:pfam01660  142 RKPKLeRLYATLVFPPeLLFGDKESLYPELYTFWYKGDrfhfyPDGHLG-----GSYTHPLN-LLSWlttskIHLPGGFT 215
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1912461801  390 LFAEVEKQFGSSYLFKITRAT-------VGSAASYPINIATLMDQ-FVLitGTTGASVNFLTSASHYEKLTSYL 455
Cdd:pfam01660  216 YTVERLESRGAHHLFKITRGDgltpkviVPDSRTFGPFEAVLLPKiFVP--RVLNYIRGKPIPLTVVNKLFSYL 287
Viral_helicase1 pfam01443
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
715-944 3.76e-10

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: 62.40  E-value: 3.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  715 GPAGTGKST---DAFRMlpagSLVLVPTNKLANDTAAAHPDMIVRTFDTAV--AKAHEYQDVpaiFIDEVFLCPHLYVLS 789
Cdd:pfam01443    5 GVPGCGKSTlirKLLRT----SRVIRPTAELRTEGKPDLPNLNVRTVDTFLmaLLKPTGKIL---ILDEYTLLPPGYILL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  790 MATL--GKPIIAAGCPGQRRYNGNLGPAFDPHSIP-VDHVALYRTIHRFGPDVTAQVERHAGPIYramfnlgpgaVFAPG 866
Cdd:pfam01443   78 LAAIsgAKLVILFGDPLQIPYHSRAPSFLIPHFPSsLSHRVGRRTTYLLPSLRAPILSAKGFEVV----------VERSG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  867 PNNNIRnTFQGPGM--NLVCHHNNISRVSPNAITIDSSQGSQYPDVLLHV-FSTDLPFFLANPYALSLALSRTTGAVTII 943
Cdd:pfam01443  148 EYKVDY-DPNGVLVlvYLTFTQALKESLGVRVTTVHEVQGLTFDSVTLVLdTDTDLLIISDSPEHLYVALTRHRKSLHIL 226

                   .
gi 1912461801  944 N 944
Cdd:pfam01443  227 T 227
Viral_helicase1 pfam01443
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
2103-2356 3.41e-06

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: 50.46  E-value: 3.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 2103 LLVDAVACAGKTTALRNTLPPTAAV--GVICHSREFADEWADHGYT--AYTMHQFRnsaSHHETIVVDEVFRFPTWFLAE 2178
Cdd:pfam01443    1 IVVHGVPGCGKSTLIRKLLRTSRVIrpTAELRTEGKPDLPNLNVRTvdTFLMALLK---PTGKILILDEYTLLPPGYILL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 2179 VIA-SCVKF-ICLGDSEQTPlltYPDKHYDPdafdpgrfrVRRRFTARTAHALPPQHArfvqlYLYeaqRALASPAPSKY 2256
Cdd:pfam01443   78 LAAiSGAKLvILFGDPLQIP---YHSRAPSF---------LIPHFPSSLSHRVGRRTT-----YLL---PSLRAPILSAK 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 2257 LSPMFVANGLRTGRITmyhnmPLVPRNADLYIASSEgatNNFRRLMpevaDRIYSVERAQGMRHKHVVILV-EPGYVNFP 2335
Cdd:pfam01443  138 GFEVVVERSGEYKVDY-----DPNGVLVLVYLTFTQ---ALKESLG----VRVTTVHEVQGLTFDSVTLVLdTDTDLLII 205
                          250       260
                   ....*....|....*....|.
gi 1912461801 2336 FTNPWLVVVAFTRSTELLEVF 2356
Cdd:pfam01443  206 SDSPEHLYVALTRHRKSLHIL 226
 
Name Accession Description Interval E-value
ps-ssRNAv_Hepelivirales_RdRp cd23209
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Hepelivirales of ...
1174-1352 8.23e-15

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Hepelivirales of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the order Hepelivirales, class Alsuviricetes. This Hepelivirales order consists of four families: Alphatetraviridae, Benyviridae, Hepeviridae, and Matonaviridae. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438059 [Multi-domain]  Cd Length: 183  Bit Score: 74.83  E-value: 8.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1174 TYFLKAQGKPKFGITGFSIASGQGILATDKLLNACTCPFTTAAADAMQRLLKPGFIYDQHYEAKDLDDAI----YAVVGp 1249
Cdd:cd23209      4 TFFQKDCRKFTDCEPVAHGKAGQGISAWSKELCFVFGPWFRALEKILRRALKPNVLYANGHEAEPFVDKInqahSAVFI- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1250 gphrslSIDLTQQDSSHTLVHRLIIGKVMKFLGFGDDVISLYLLSREKRhVLGLKLpVSFDVIERLFSGEPGTAFFNFIM 1329
Cdd:cd23209     83 ------ENDFTEFDSTQNLFSLLVELEILEACGMPPALAELYRALRAKW-TLQARE-GSLEGTCKKTSGEPGTLLHNTIW 154
                          170       180
                   ....*....|....*....|...
gi 1912461801 1330 STSTTAMTHDLSRVKLFVGKGDD 1352
Cdd:cd23209    155 NMAVMMHMVRGGVRKAAAFKGDD 177
RdRP_2 pfam00978
RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The ...
1091-1427 3.41e-12

RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The family also contains the following proteins: 2A protein from bromoviruses putative RNA dependent RNA polymerase from tobamoviruses Non structural polyprotein from togaviruses


Pssm-ID: 395779  Cd Length: 440  Bit Score: 71.13  E-value: 3.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1091 ALYAIadryvKHQNVNMP--------LSRAAQLADMAFEawrvSFINP---KASAAIPSASFLAQHWLSGRSLSQVAAIL 1159
Cdd:pfam00978   48 VLLAL-----KKRNFNVPelqesvdlDDTAERVAERFKK----SFLDKeklDKLDPIINTTENVSRWLDKQSGKKAAQLK 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1160 R------AEDNTGTARMMsatyfLKAQGKPKFGITG-FSIASGQGILATDKLLNACTCPFTTAAADAMQRLLKPGFIYdq 1232
Cdd:pfam00978  119 LddlvplHEVDLDRYKHM-----IKSDVKPKLDLSPqSERPALQTITYHDKGVTAYFSPIFRELFERLLYVLKPKIVF-- 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1233 hYEAKDLDDAIYAV-VGPGPHRSLSIDLTQ----QDSSHTLVHRLIigkvMKFLGFGDDVISLYLLSREKRHVLGLKLPV 1307
Cdd:pfam00978  192 -PTGMTSSLIAEHFeFLDASEDFLEIDFSKfdksQGELHLLVQLEI----LKLLGLDPELADLWFKFHRQSYIKDRKNGV 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1308 SFDVIERLFSGEPGTAFFNFIMSTSTTAMTHDLSRVKLFVGKGDDN-----STIP-PAPRKTLAFNY-CKetgvtqktdv 1380
Cdd:pfam00978  267 GFSVDYQRKSGDANTYLGNTLVTMAMLASVYDLEKIDCAAFSGDDSlifspKPIEdPASRFATLFNMeAK---------- 336
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1912461801 1381 cdYFDFANR------IWTSSGRSFS--DPIRMLSKFTCRLRGRDNT--GEEYQAFMD 1427
Cdd:pfam00978  337 --VFDPSVPyfcskfLLEVDGGAFFvpDPLKLLQKLGKKKIPDDEQhlDEIFTSLCD 391
Vmethyltransf pfam01660
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ...
168-455 5.24e-12

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: 69.25  E-value: 5.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  168 VASNLSNEAHEKLCDL-FDYNIFQATaPSNHPALAAFRTLCHQYVYHKVGANN-ILEVGPN-LGKMATNHKFVpaHSCSP 244
Cdd:pfam01660    1 FPYALSPEAQELLENLgIEFSPYSVT-PHSHPAAKALENLLLEVLPSYLPNPStVLDIKGSkLRHLKRGNPNV--HCCNP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  245 TLDGRDEArailmgtrinkRHTAAntkmlLDRSNGVFSSPQRMCNNKVEDCDVQAPVIYSAF---SLQDAQPSDIPAIMD 321
Cdd:pfam01660   78 ILDPRDVA-----------RYPEA-----FSLEKSLGNGEDLRPTNTFEDCRVLAPTTSYAFmhdSLHDWSPEELADLFL 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  322 RHGSR-TAYILLMLPV-PLAYADEFREDDTGCVWKRDG-----PMATCNpgyndAGYSHNMEkIQRW-----VDGFDGLP 389
Cdd:pfam01660  142 RKPKLeRLYATLVFPPeLLFGDKESLYPELYTFWYKGDrfhfyPDGHLG-----GSYTHPLN-LLSWlttskIHLPGGFT 215
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1912461801  390 LFAEVEKQFGSSYLFKITRAT-------VGSAASYPINIATLMDQ-FVLitGTTGASVNFLTSASHYEKLTSYL 455
Cdd:pfam01660  216 YTVERLESRGAHHLFKITRGDgltpkviVPDSRTFGPFEAVLLPKiFVP--RVLNYIRGKPIPLTVVNKLFSYL 287
Viral_helicase1 pfam01443
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
715-944 3.76e-10

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: 62.40  E-value: 3.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  715 GPAGTGKST---DAFRMlpagSLVLVPTNKLANDTAAAHPDMIVRTFDTAV--AKAHEYQDVpaiFIDEVFLCPHLYVLS 789
Cdd:pfam01443    5 GVPGCGKSTlirKLLRT----SRVIRPTAELRTEGKPDLPNLNVRTVDTFLmaLLKPTGKIL---ILDEYTLLPPGYILL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  790 MATL--GKPIIAAGCPGQRRYNGNLGPAFDPHSIP-VDHVALYRTIHRFGPDVTAQVERHAGPIYramfnlgpgaVFAPG 866
Cdd:pfam01443   78 LAAIsgAKLVILFGDPLQIPYHSRAPSFLIPHFPSsLSHRVGRRTTYLLPSLRAPILSAKGFEVV----------VERSG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801  867 PNNNIRnTFQGPGM--NLVCHHNNISRVSPNAITIDSSQGSQYPDVLLHV-FSTDLPFFLANPYALSLALSRTTGAVTII 943
Cdd:pfam01443  148 EYKVDY-DPNGVLVlvYLTFTQALKESLGVRVTTVHEVQGLTFDSVTLVLdTDTDLLIISDSPEHLYVALTRHRKSLHIL 226

                   .
gi 1912461801  944 N 944
Cdd:pfam01443  227 T 227
ps-ssRNAv_Martellivirales_RdRp cd23208
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Martellivirales of ...
1175-1353 5.64e-10

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Martellivirales of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the order Martellivirales, class Alsuviricetes. The order Martellivirales consists of seven families: Bromoviridae, Closteroviridae, Endornaviridae, Kitaviridae, Mayoviridae, Togaviridae, and Virgaviridae. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438058 [Multi-domain]  Cd Length: 190  Bit Score: 60.84  E-value: 5.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1175 YFLKAQGKPKFGITGFS-IASGQGILATDKLLNACTCPFTTAAADAMQRLLKPGF-IYDQHYEAKDLDDAIYAVVGPGPH 1252
Cdd:cd23208      5 MMIKSDVKPKLDLTAQQeYPKLQTIVYHDKNITAIFCPIFKELFERLLSCLKKKVvIYTGMMTSAELNDFISALHLESGY 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1253 RSLSIDLTQQDSSHTLVHRLIIGKVMKFLGFGDDVISLYLLSREKRHVLGLKLPVSFDVIERLFSGEPGTAFFNFIMSTS 1332
Cdd:cd23208     85 YVLEIDFSKFDKSQGALHLLTELLILRRLGVDEPLLVLWEFAHTQSTTRDINNGISFETAYQRKSGDAFTYFGNTLVTMA 164
                          170       180
                   ....*....|....*....|.
gi 1912461801 1333 TTAMTHDLSRVKLFVGKGDDN 1353
Cdd:cd23208    165 ALLDVLDLEKIVCIAFGGDDS 185
Viral_helicase1 pfam01443
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
2103-2356 3.41e-06

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: 50.46  E-value: 3.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 2103 LLVDAVACAGKTTALRNTLPPTAAV--GVICHSREFADEWADHGYT--AYTMHQFRnsaSHHETIVVDEVFRFPTWFLAE 2178
Cdd:pfam01443    1 IVVHGVPGCGKSTLIRKLLRTSRVIrpTAELRTEGKPDLPNLNVRTvdTFLMALLK---PTGKILILDEYTLLPPGYILL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 2179 VIA-SCVKF-ICLGDSEQTPlltYPDKHYDPdafdpgrfrVRRRFTARTAHALPPQHArfvqlYLYeaqRALASPAPSKY 2256
Cdd:pfam01443   78 LAAiSGAKLvILFGDPLQIP---YHSRAPSF---------LIPHFPSSLSHRVGRRTT-----YLL---PSLRAPILSAK 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 2257 LSPMFVANGLRTGRITmyhnmPLVPRNADLYIASSEgatNNFRRLMpevaDRIYSVERAQGMRHKHVVILV-EPGYVNFP 2335
Cdd:pfam01443  138 GFEVVVERSGEYKVDY-----DPNGVLVLVYLTFTQ---ALKESLG----VRVTTVHEVQGLTFDSVTLVLdTDTDLLII 205
                          250       260
                   ....*....|....*....|.
gi 1912461801 2336 FTNPWLVVVAFTRSTELLEVF 2356
Cdd:pfam01443  206 SDSPEHLYVALTRHRKSLHIL 226
Kitaviridae_RdRp cd23254
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Kitaviridae of ...
1174-1352 3.63e-06

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Kitaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Kitaviridae, order Martellivirales. The family Kitaviridae is composed of five recognized species among the three genera: Blueberry necrotic ring blotch virus and Tea plant necrotic ring blotch virus (genus Blunervirus); Citrus leprosis virus C and Citrus leprosis virus C2 (genus Cilevirus); and Hibiscus green spot virus 2 (genus Higrevirus). Although related, there are considerable physical and genetic distinctions between members of the different genera. For example, cile- and higreviruses are associated with a bacilliform virion, whereas a spherical virion has been observed for the lone blunervirus for which microscopy has been reported. Moreover, the replication-associated polyproteins are encoded by a single genomic RNA for cile- and higreviruses, but are split between two genomic RNAs for blunerviruses. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438104  Cd Length: 267  Bit Score: 51.00  E-value: 3.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1174 TYFLKAQGKPKFGITG-FSIASGQGILATDKLLNACTCPFTTAAADAMQRLLKPGF-IY----DQHYEAKDLDDAIYAVV 1247
Cdd:cd23254      4 SFMIKRNPKPNLTVDAaYKYPALQTIAYHDKDINAIFCPIFRELKKRLLAVLKPNFvIFtdmsPEDFEELLNRRFPPEVL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1248 GPGPHrSLSIDLTQQDSSHTLVHRLIIGKVMKFLGFGDDVISLYLLSrekrHVL--------GLKLPVSFdviERLfSGE 1319
Cdd:cd23254     84 SKLLH-KLEIDISKYDKSQGELALLFECKLMRRFGVPEELVELWFNA----HVLttlydrtnKLKALVEY---QRK-SGD 154
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1912461801 1320 PGTAFFN--FIMstSTTAMTHDLSRVKLFVGKGDD 1352
Cdd:cd23254    155 ASTFFGNtlFLM--AVLADLFDLSDLELALFSGDD 187
ps-ssRNAv_Alsuviricetes_RdRp cd23182
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the class Alsuviricetes of ...
1175-1356 1.02e-03

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the class Alsuviricetes of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the class Alsuviricetes, phylum: Kitrinoviricota. Alsuviricetes is a class of [(+)ssRNA] viruses which infect eukaryotes. The name of the group is a syllabic abbreviation of "alpha supergroup" with the suffix -viricetes indicating a virus class. The class Alsuviricetes includes three orders: Hepelivirales, Martellivirales, and Tymovirales. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438032 [Multi-domain]  Cd Length: 187  Bit Score: 42.59  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1175 YFLKAQGKPKFGITGFSIASGQGILATDKLLNACTCPFTTAAADAMQRLLKPGFIYDQH---YEAKDLDDAIYAVvgpgP 1251
Cdd:cd23182      5 FLIKTQQKVSPKTPFNTGKAGQTIAAHSKSINFVLGPWIRYLEERLRDGSRTHRYSNGLmdeEEAMLSQWKINHV----P 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1252 H-RSLSIDLTQQDSSHTLVHRLIIGKVMKFLGFGDDVISLYLLSREKRHVLGLKLPVSFDVIERLFSGEPGTAFFNFIMS 1330
Cdd:cd23182     81 HaTFVSNDYTAFDKSHNGESLLLEAAIMRRIGTPAAAPNLFIELHGKRTLRAKVLGGSGELDGMRDSGAAWTYCRNTDYN 160
                          170       180
                   ....*....|....*....|....*.
gi 1912461801 1331 TSttAMTHDLSRVKLFVGKGDDNSTI 1356
Cdd:cd23182    161 LA--VMLSLYRLKVKPAAFSGDDSLL 184
Benyviridae_RdRp cd23257
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Benyviridae of ...
1194-1352 1.78e-03

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Benyviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Benyviridae, order Hepelivirales. The Benyviridae is a family of plant viruses with rod-shaped virions. Their genomes are multipartite (+)ssRNAs with 5' m7G-cap and 3' poly(A) and there is post-translational cleavage of the viral replicase. Beet necrotic yellow vein virus belongs to the genus Benyvirus and is the cause of 'rhizomania' disease of sugar beet. This widespread soil-borne disease can severely reduce sugar beet growth and beet sucrose production. BNYVV RNA1 contains one open reading frame (ORF) encoding a replicase protein that harbors motifs for methyltransferase, helicase, papain-like protease, and RdRp. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438107 [Multi-domain]  Cd Length: 188  Bit Score: 41.83  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1194 SGQGILATDKLLNACTCPFTTAAADAMQRLLKPGFIYDQHYEAKDLDDAIYAVVGPGPHRSLS--IDLTQQDSSHTLVHR 1271
Cdd:cd23257     24 AGQGILAWSKEAHVKFMVAFRVLNDLLLKSLNSNVVYDNTMSETEFVGKINAAMNTVPDSAINgvIDAAACDSGQGVFTQ 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912461801 1272 LIIGKVMKFLGFGDDVISLYLLSREkRHVLGLKLpVSFDVIERLFSGEPGTAFFNFI-MSTSTTAMTHDLSRVKLFVgKG 1350
Cdd:cd23257    104 LIERYIYAALGISDFFLDWYFSFRE-KYVMQSRY-VRAHMSYVKTSGEPGTLLGNTIlMGAMLNAMLRGTGPFCMAM-KG 180

                   ..
gi 1912461801 1351 DD 1352
Cdd:cd23257    181 DD 182
 
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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