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Conserved domains on  [gi|1126394319|ref|YP_009333224|]
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replicase [Beihai barnacle virus 3]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Viral_helicase1 super family cl26263
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
666-910 3.13e-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: 91.67  E-value: 3.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  666 VQGGPGCAKSTYIREQVKDGdTIIVATAAAKVEmmSKLQRHRRDVRVavntpHSSVVLADKATPGGTVYIDEYTLQPMGL 745
Cdd:pfam01443    3 VHGVPGCGKSTLIRKLLRTS-RVIRPTAELRTE--GKPDLPNLNVRT-----VDTFLMALLKPTGKILILDEYTLLPPGY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  746 NIAACQLRGATKIVLVGDYMQIGYVDRELDDQ--QIEtrwrwKELVGRVPEHTlreNYRLPHDHVLALNKRYGYNMVpks 823
Cdd:pfam01443   75 ILLLAAISGAKLVILFGDPLQIPYHSRAPSFLipHFP-----SSLSHRVGRRT---TYLLPSLRAPILSAKGFEVVV--- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  824 mkqgESSVAYVRDISevppSPGYKTVTFRQRDKNSLQHMRHDVNTCHEFQGSTAAFVHLVLRS-SDCNRLIEDSGYVVVG 902
Cdd:pfam01443  144 ----ERSGEYKVDYD----PNGVLVLVYLTFTQALKESLGVRVTTVHEVQGLTFDSVTLVLDTdTDLLIISDSPEHLYVA 215

                   ....*...
gi 1126394319  903 TSRHTDAL 910
Cdd:pfam01443  216 LTRHRKSL 223
ps-ssRNAv_RdRp-like super family cl40470
conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense ...
1187-1359 1.22e-12

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: 68.67  E-value: 1.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1187 KAGQGVVAWSKIWNIVSAPYAKVMQKRLCDDTHPWFMVASGYSEEDMARKMSQSVSnhgcffgtkgddAVMIllkdgeyh 1266
Cdd:cd23209     23 KAGQGISAWSKELCFVFGPWFRALEKILRRALKPNVLYANGHEAEPFVDKINQAHS------------AVFI-------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1267 vhSCDQTQFDSRQSTLHFSLQDEFLRRLGMPAFIIDSIWKMRERHSVRATDGTILMKNLqfgRDSGEPFTLDGNSLVTIA 1346
Cdd:cd23209     83 --ENDFTEFDSTQNLFSLLVELEILEACGMPPALAELYRALRAKWTLQAREGSLEGTCK---KTSGEPGTLLHNTIWNMA 157
                          170
                   ....*....|...
gi 1126394319 1347 INIRALQPTVQEC 1359
Cdd:cd23209    158 VMMHMVRGGVRKA 170
RdRP_2 super family cl03049
RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The ...
1105-1506 1.36e-11

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


The actual alignment was detected with superfamily member pfam00978:

Pssm-ID: 395779  Cd Length: 440  Bit Score: 69.21  E-value: 1.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1105 ELQQAF--WDTVRNIQKRGKvKAYADGPYLY------PTIAEMSCFVKEQTKCKISQwrPDASDSFEVLQNAALTY---- 1172
Cdd:pfam00978   61 ELQESVdlDDTAERVAERFK-KSFLDKEKLDkldpiiNTTENVSRWLDKQSGKKAAQ--LKLDDLVPLHEVDLDRYkhmi 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1173 ---LKEKPDGSAgLTKEKAGQGVVAWSKIWNIVSAPYAKVMQKRLCDDTHPWFMVASGyseedmarKMSQSVSNHGCFFg 1249
Cdd:pfam00978  138 ksdVKPKLDLSP-QSERPALQTITYHDKGVTAYFSPIFRELFERLLYVLKPKIVFPTG--------MTSSLIAEHFEFL- 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1250 tkgddavmillkDGEYHVHSCDQTQFDSRQSTLHFSLQDEFLRRLGMPAFIIDsIWKMRERHSVRaTDGTI-LMKNLQFG 1328
Cdd:pfam00978  208 ------------DASEDFLEIDFSKFDKSQGELHLLVQLEILKLLGLDPELAD-LWFKFHRQSYI-KDRKNgVGFSVDYQ 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1329 RDSGEPFTLDGNSLVTIAINIRALQPTVQECELV--D------INPTSESFEAAQDLFDMVIKHeFTHNIGEFIG-YIFV 1399
Cdd:pfam00978  274 RKSGDANTYLGNTLVTMAMLASVYDLEKIDCAAFsgDdslifsPKPIEDPASRFATLFNMEAKV-FDPSVPYFCSkFLLE 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1400 AEANIpKFVPNIVKRVTKeLGRAyKPQDvksqNKLVLQELRemgvhgheeyfgrlaevaTATEDFLALLADesDVAITIE 1479
Cdd:pfam00978  353 VDGGA-FFVPDPLKLLQK-LGKK-KIPD----DEQHLDEIF------------------TSLCDLTKSFND--DCVVLEL 405
                          410       420
                   ....*....|....*....|....*..
gi 1126394319 1480 ANLRYHKEYLSTSRHAAATACLRDMIS 1506
Cdd:pfam00978  406 LDLAVARYYKYAPEGYAALCALHKALS 432
Vmethyltransf super family cl46422
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ...
139-345 1.38e-05

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: 49.60  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  139 RHLKE--VSRYMSKLPNDDICTVGGHnCKVKA---SALFLNHSIYDITPDELASAFENSG------ASIAFAtftcPELL 207
Cdd:pfam01660   86 RYPEAfsLEKSLGNGEDLRPTNTFED-CRVLApttSYAFMHDSLHDWSPEELADLFLRKPklerlyATLVFP----PELL 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  208 esgslngrqgevvwsckfqrrtrmqiewakmkavltteekFSDNVSHEEWVTMTEPIKDpkaRIYFGMPGVLG--YGHSW 285
Cdd:pfam01660  161 ----------------------------------------FGDKESLYPELYTFWYKGD---RFHFYPDGHLGgsYTHPL 197
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126394319  286 nNYATWMHAPGVTCSNGITLLIER-QRFGAVVLMRIDRTSRGGILVGMPT----TTKEMVMIPDL 345
Cdd:pfam01660  198 -NLLSWLTTSKIHLPGGFTYTVERlESRGAHHLFKITRGDGLTPKVIVPDsrtfGPFEAVLLPKI 261
 
Name Accession Description Interval E-value
Viral_helicase1 pfam01443
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
666-910 3.13e-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: 91.67  E-value: 3.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  666 VQGGPGCAKSTYIREQVKDGdTIIVATAAAKVEmmSKLQRHRRDVRVavntpHSSVVLADKATPGGTVYIDEYTLQPMGL 745
Cdd:pfam01443    3 VHGVPGCGKSTLIRKLLRTS-RVIRPTAELRTE--GKPDLPNLNVRT-----VDTFLMALLKPTGKILILDEYTLLPPGY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  746 NIAACQLRGATKIVLVGDYMQIGYVDRELDDQ--QIEtrwrwKELVGRVPEHTlreNYRLPHDHVLALNKRYGYNMVpks 823
Cdd:pfam01443   75 ILLLAAISGAKLVILFGDPLQIPYHSRAPSFLipHFP-----SSLSHRVGRRT---TYLLPSLRAPILSAKGFEVVV--- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  824 mkqgESSVAYVRDISevppSPGYKTVTFRQRDKNSLQHMRHDVNTCHEFQGSTAAFVHLVLRS-SDCNRLIEDSGYVVVG 902
Cdd:pfam01443  144 ----ERSGEYKVDYD----PNGVLVLVYLTFTQALKESLGVRVTTVHEVQGLTFDSVTLVLDTdTDLLIISDSPEHLYVA 215

                   ....*...
gi 1126394319  903 TSRHTDAL 910
Cdd:pfam01443  216 LTRHRKSL 223
ps-ssRNAv_Hepelivirales_RdRp cd23209
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Hepelivirales of ...
1187-1359 1.22e-12

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: 68.67  E-value: 1.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1187 KAGQGVVAWSKIWNIVSAPYAKVMQKRLCDDTHPWFMVASGYSEEDMARKMSQSVSnhgcffgtkgddAVMIllkdgeyh 1266
Cdd:cd23209     23 KAGQGISAWSKELCFVFGPWFRALEKILRRALKPNVLYANGHEAEPFVDKINQAHS------------AVFI-------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1267 vhSCDQTQFDSRQSTLHFSLQDEFLRRLGMPAFIIDSIWKMRERHSVRATDGTILMKNLqfgRDSGEPFTLDGNSLVTIA 1346
Cdd:cd23209     83 --ENDFTEFDSTQNLFSLLVELEILEACGMPPALAELYRALRAKWTLQAREGSLEGTCK---KTSGEPGTLLHNTIWNMA 157
                          170
                   ....*....|...
gi 1126394319 1347 INIRALQPTVQEC 1359
Cdd:cd23209    158 VMMHMVRGGVRKA 170
RdRP_2 pfam00978
RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The ...
1105-1506 1.36e-11

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: 69.21  E-value: 1.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1105 ELQQAF--WDTVRNIQKRGKvKAYADGPYLY------PTIAEMSCFVKEQTKCKISQwrPDASDSFEVLQNAALTY---- 1172
Cdd:pfam00978   61 ELQESVdlDDTAERVAERFK-KSFLDKEKLDkldpiiNTTENVSRWLDKQSGKKAAQ--LKLDDLVPLHEVDLDRYkhmi 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1173 ---LKEKPDGSAgLTKEKAGQGVVAWSKIWNIVSAPYAKVMQKRLCDDTHPWFMVASGyseedmarKMSQSVSNHGCFFg 1249
Cdd:pfam00978  138 ksdVKPKLDLSP-QSERPALQTITYHDKGVTAYFSPIFRELFERLLYVLKPKIVFPTG--------MTSSLIAEHFEFL- 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1250 tkgddavmillkDGEYHVHSCDQTQFDSRQSTLHFSLQDEFLRRLGMPAFIIDsIWKMRERHSVRaTDGTI-LMKNLQFG 1328
Cdd:pfam00978  208 ------------DASEDFLEIDFSKFDKSQGELHLLVQLEILKLLGLDPELAD-LWFKFHRQSYI-KDRKNgVGFSVDYQ 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1329 RDSGEPFTLDGNSLVTIAINIRALQPTVQECELV--D------INPTSESFEAAQDLFDMVIKHeFTHNIGEFIG-YIFV 1399
Cdd:pfam00978  274 RKSGDANTYLGNTLVTMAMLASVYDLEKIDCAAFsgDdslifsPKPIEDPASRFATLFNMEAKV-FDPSVPYFCSkFLLE 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1400 AEANIpKFVPNIVKRVTKeLGRAyKPQDvksqNKLVLQELRemgvhgheeyfgrlaevaTATEDFLALLADesDVAITIE 1479
Cdd:pfam00978  353 VDGGA-FFVPDPLKLLQK-LGKK-KIPD----DEQHLDEIF------------------TSLCDLTKSFND--DCVVLEL 405
                          410       420
                   ....*....|....*....|....*..
gi 1126394319 1480 ANLRYHKEYLSTSRHAAATACLRDMIS 1506
Cdd:pfam00978  406 LDLAVARYYKYAPEGYAALCALHKALS 432
DEXXYc_viral_SF1-N cd17937
DEXXY-box helicase domain of viral superfamily 1 helicase; Superfamily 1 (SF1) helicases are ...
664-770 1.24e-07

DEXXY-box helicase domain of viral superfamily 1 helicase; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. The members here contain arterivirus equine arteritis virus (EAV) non-structural protein (nsp)10. Nsp10 is composed of two domains, ZBD (ATPase) and HEL1 (helicase) along with 2 additional non-enzymatic domains that are thought to regulate HEL1 function. The helicase activity depends on the extensive relay of interactions between the ZBD and HEL1 domains. The arterivirus helicase structurally resembles the cellular Upf1 helicase, suggesting that nidoviruses may also use their helicases for post-transcriptional quality control of their large RNA genomes. The proteins here are members 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: 350695 [Multi-domain]  Cd Length: 137  Bit Score: 52.82  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  664 EMVQGGPGCAKSTYIREQVKDGDTIIVATAAAKVEMMSKLQRHRRDVRVAVN-----TPHSS----VVLADKATPGGTVY 734
Cdd:cd17937      4 TYIEGPPGCGKTFWLKKLVQPNDVLYVPTHATMLDMIKSLGPCRFVVPFGAPdldfpTPSSSgptvRLLAVGYTPGGKAF 83
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1126394319  735 IDE-YTLQPMGLniaaCQLRGATKIVLVGDYMQIGYV 770
Cdd:cd17937     84 VDEaCYCNPVDL----ARLLTQTPVTAFGDPNQLGPV 116
Vmethyltransf pfam01660
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ...
139-345 1.38e-05

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: 49.60  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  139 RHLKE--VSRYMSKLPNDDICTVGGHnCKVKA---SALFLNHSIYDITPDELASAFENSG------ASIAFAtftcPELL 207
Cdd:pfam01660   86 RYPEAfsLEKSLGNGEDLRPTNTFED-CRVLApttSYAFMHDSLHDWSPEELADLFLRKPklerlyATLVFP----PELL 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  208 esgslngrqgevvwsckfqrrtrmqiewakmkavltteekFSDNVSHEEWVTMTEPIKDpkaRIYFGMPGVLG--YGHSW 285
Cdd:pfam01660  161 ----------------------------------------FGDKESLYPELYTFWYKGD---RFHFYPDGHLGgsYTHPL 197
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126394319  286 nNYATWMHAPGVTCSNGITLLIER-QRFGAVVLMRIDRTSRGGILVGMPT----TTKEMVMIPDL 345
Cdd:pfam01660  198 -NLLSWLTTSKIHLPGGFTYTVERlESRGAHHLFKITRGDGLTPKVIVPDsrtfGPFEAVLLPKI 261
 
Name Accession Description Interval E-value
Viral_helicase1 pfam01443
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
666-910 3.13e-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: 91.67  E-value: 3.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  666 VQGGPGCAKSTYIREQVKDGdTIIVATAAAKVEmmSKLQRHRRDVRVavntpHSSVVLADKATPGGTVYIDEYTLQPMGL 745
Cdd:pfam01443    3 VHGVPGCGKSTLIRKLLRTS-RVIRPTAELRTE--GKPDLPNLNVRT-----VDTFLMALLKPTGKILILDEYTLLPPGY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  746 NIAACQLRGATKIVLVGDYMQIGYVDRELDDQ--QIEtrwrwKELVGRVPEHTlreNYRLPHDHVLALNKRYGYNMVpks 823
Cdd:pfam01443   75 ILLLAAISGAKLVILFGDPLQIPYHSRAPSFLipHFP-----SSLSHRVGRRT---TYLLPSLRAPILSAKGFEVVV--- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  824 mkqgESSVAYVRDISevppSPGYKTVTFRQRDKNSLQHMRHDVNTCHEFQGSTAAFVHLVLRS-SDCNRLIEDSGYVVVG 902
Cdd:pfam01443  144 ----ERSGEYKVDYD----PNGVLVLVYLTFTQALKESLGVRVTTVHEVQGLTFDSVTLVLDTdTDLLIISDSPEHLYVA 215

                   ....*...
gi 1126394319  903 TSRHTDAL 910
Cdd:pfam01443  216 LTRHRKSL 223
ps-ssRNAv_Hepelivirales_RdRp cd23209
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Hepelivirales of ...
1187-1359 1.22e-12

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: 68.67  E-value: 1.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1187 KAGQGVVAWSKIWNIVSAPYAKVMQKRLCDDTHPWFMVASGYSEEDMARKMSQSVSnhgcffgtkgddAVMIllkdgeyh 1266
Cdd:cd23209     23 KAGQGISAWSKELCFVFGPWFRALEKILRRALKPNVLYANGHEAEPFVDKINQAHS------------AVFI-------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1267 vhSCDQTQFDSRQSTLHFSLQDEFLRRLGMPAFIIDSIWKMRERHSVRATDGTILMKNLqfgRDSGEPFTLDGNSLVTIA 1346
Cdd:cd23209     83 --ENDFTEFDSTQNLFSLLVELEILEACGMPPALAELYRALRAKWTLQAREGSLEGTCK---KTSGEPGTLLHNTIWNMA 157
                          170
                   ....*....|...
gi 1126394319 1347 INIRALQPTVQEC 1359
Cdd:cd23209    158 VMMHMVRGGVRKA 170
RdRP_2 pfam00978
RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The ...
1105-1506 1.36e-11

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: 69.21  E-value: 1.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1105 ELQQAF--WDTVRNIQKRGKvKAYADGPYLY------PTIAEMSCFVKEQTKCKISQwrPDASDSFEVLQNAALTY---- 1172
Cdd:pfam00978   61 ELQESVdlDDTAERVAERFK-KSFLDKEKLDkldpiiNTTENVSRWLDKQSGKKAAQ--LKLDDLVPLHEVDLDRYkhmi 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1173 ---LKEKPDGSAgLTKEKAGQGVVAWSKIWNIVSAPYAKVMQKRLCDDTHPWFMVASGyseedmarKMSQSVSNHGCFFg 1249
Cdd:pfam00978  138 ksdVKPKLDLSP-QSERPALQTITYHDKGVTAYFSPIFRELFERLLYVLKPKIVFPTG--------MTSSLIAEHFEFL- 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1250 tkgddavmillkDGEYHVHSCDQTQFDSRQSTLHFSLQDEFLRRLGMPAFIIDsIWKMRERHSVRaTDGTI-LMKNLQFG 1328
Cdd:pfam00978  208 ------------DASEDFLEIDFSKFDKSQGELHLLVQLEILKLLGLDPELAD-LWFKFHRQSYI-KDRKNgVGFSVDYQ 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1329 RDSGEPFTLDGNSLVTIAINIRALQPTVQECELV--D------INPTSESFEAAQDLFDMVIKHeFTHNIGEFIG-YIFV 1399
Cdd:pfam00978  274 RKSGDANTYLGNTLVTMAMLASVYDLEKIDCAAFsgDdslifsPKPIEDPASRFATLFNMEAKV-FDPSVPYFCSkFLLE 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1400 AEANIpKFVPNIVKRVTKeLGRAyKPQDvksqNKLVLQELRemgvhgheeyfgrlaevaTATEDFLALLADesDVAITIE 1479
Cdd:pfam00978  353 VDGGA-FFVPDPLKLLQK-LGKK-KIPD----DEQHLDEIF------------------TSLCDLTKSFND--DCVVLEL 405
                          410       420
                   ....*....|....*....|....*..
gi 1126394319 1480 ANLRYHKEYLSTSRHAAATACLRDMIS 1506
Cdd:pfam00978  406 LDLAVARYYKYAPEGYAALCALHKALS 432
ps-ssRNAv_Alsuviricetes_RdRp cd23182
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the class Alsuviricetes of ...
1187-1347 2.03e-10

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: 62.23  E-value: 2.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1187 KAGQGVVAWSKIWNIVSAPYAKVMQKRLCDDTHPWFMVASGYSEEDmaRKMSQSVSNHgcffgTKGDDAVMIllkdgeyh 1266
Cdd:cd23182     23 KAGQTIAAHSKSINFVLGPWIRYLEERLRDGSRTHRYSNGLMDEEE--AMLSQWKINH-----VPHATFVSN-------- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1267 vhscDQTQFDSRQSTLHFSLQDEFLRRLGMPAFIIDSIwkmRERHSVRATD--GTILMKNLQFGRDSGEPFTLDGNSLVT 1344
Cdd:cd23182     88 ----DYTAFDKSHNGESLLLEAAIMRRIGTPAAAPNLF---IELHGKRTLRakVLGGSGELDGMRDSGAAWTYCRNTDYN 160

                   ...
gi 1126394319 1345 IAI 1347
Cdd:cd23182    161 LAV 163
ps-ssRNAv_Martellivirales_RdRp cd23208
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Martellivirales of ...
1174-1347 6.52e-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: 6.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1174 KEKPDGSAgLTKEKAGQGVVAWSKIWNIVSAPYAKVMQKRL--CDDTHPWFmvasgYSEEDMARKMSQSVSnhgcffgtk 1251
Cdd:cd23208     12 KPKLDLTA-QQEYPKLQTIVYHDKNITAIFCPIFKELFERLlsCLKKKVVI-----YTGMMTSAELNDFIS--------- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1252 gddavmILLKDGEYHVHSCDQTQFDSRQSTLHFSLQDEFLRRLGMPAFIIDSIWKMRERHSVRATDGTILMKnLQFGRDS 1331
Cdd:cd23208     77 ------ALHLESGYYVLEIDFSKFDKSQGALHLLTELLILRRLGVDEPLLVLWEFAHTQSTTRDINNGISFE-TAYQRKS 149
                          170
                   ....*....|....*.
gi 1126394319 1332 GEPFTLDGNSLVTIAI 1347
Cdd:cd23208    150 GDAFTYFGNTLVTMAA 165
DEXXYc_viral_SF1-N cd17937
DEXXY-box helicase domain of viral superfamily 1 helicase; Superfamily 1 (SF1) helicases are ...
664-770 1.24e-07

DEXXY-box helicase domain of viral superfamily 1 helicase; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. The members here contain arterivirus equine arteritis virus (EAV) non-structural protein (nsp)10. Nsp10 is composed of two domains, ZBD (ATPase) and HEL1 (helicase) along with 2 additional non-enzymatic domains that are thought to regulate HEL1 function. The helicase activity depends on the extensive relay of interactions between the ZBD and HEL1 domains. The arterivirus helicase structurally resembles the cellular Upf1 helicase, suggesting that nidoviruses may also use their helicases for post-transcriptional quality control of their large RNA genomes. The proteins here are members 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: 350695 [Multi-domain]  Cd Length: 137  Bit Score: 52.82  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  664 EMVQGGPGCAKSTYIREQVKDGDTIIVATAAAKVEMMSKLQRHRRDVRVAVN-----TPHSS----VVLADKATPGGTVY 734
Cdd:cd17937      4 TYIEGPPGCGKTFWLKKLVQPNDVLYVPTHATMLDMIKSLGPCRFVVPFGAPdldfpTPSSSgptvRLLAVGYTPGGKAF 83
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1126394319  735 IDE-YTLQPMGLniaaCQLRGATKIVLVGDYMQIGYV 770
Cdd:cd17937     84 VDEaCYCNPVDL----ARLLTQTPVTAFGDPNQLGPV 116
Mayoviridae_RdRp cd23256
RNA-dependent RNA polymerase (RdRp) in the family Mayoviridae of positive-sense ...
1271-1348 1.56e-06

RNA-dependent RNA polymerase (RdRp) in the family Mayoviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Mayoviridae, order Martellivirales. The Mayoviridae family consists of two genera, Idaeovirus and Pteridovirus. The genus Idaeovirus contains Raspberry bushy dwarf virus (RBDV), named after the host with which it was first associated (red raspberry, Rubus idaeu) and the disease which is characterized by bushiness (stunting and proliferation of canes); RBDV has recently been found causing an infection in grapevines. RBDV occurs in all tissues of the plant, including seed and pollen, and is transmitted in association with pollen, both vertically to the seed and horizontally to the pollinated plant; this is the only known method of natural spread of RBDV. 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: 438106  Cd Length: 329  Bit Score: 52.44  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1271 DQTQFDSRQSTLHFSLQDEFLRRLGM-PAFIidSIWKMRERHS-VRATDGTILMKNLqFGRDSGEPFTLDGNSLVTIAIN 1348
Cdd:cd23256    121 DFSKFDKSQGELHQLIQDLILLRFGCdPEFV--SLWSTAHRSSsIKDQNVGISFKTD-FQRRTGDAFTFLGNSLVTAVML 197
Benyviridae_RdRp cd23257
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Benyviridae of ...
1175-1347 5.41e-06

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: 49.15  E-value: 5.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1175 EKPDGSAGLTKEKAGQGVVAWSKIWNIVSAPYAKVMQKRLCDDTHPWFMVASGYSEEDMARKMSQSVSnhgcffgtkgdd 1254
Cdd:cd23257     11 EKPLKDPETDLAKAGQGILAWSKEAHVKFMVAFRVLNDLLLKSLNSNVVYDNTMSETEFVGKINAAMN------------ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1255 AVMILLKDGEYHVHSCdqtqfDSRQSTLHFSLQDEFLRRLGMPAFIIDSIWKMRERHSVRAtdgTILMKNLQFGRDSGEP 1334
Cdd:cd23257     79 TVPDSAINGVIDAAAC-----DSGQGVFTQLIERYIYAALGISDFFLDWYFSFREKYVMQS---RYVRAHMSYVKTSGEP 150
                          170
                   ....*....|...
gi 1126394319 1335 FTLDGNSLVTIAI 1347
Cdd:cd23257    151 GTLLGNTILMGAM 163
Vmethyltransf pfam01660
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ...
139-345 1.38e-05

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: 49.60  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  139 RHLKE--VSRYMSKLPNDDICTVGGHnCKVKA---SALFLNHSIYDITPDELASAFENSG------ASIAFAtftcPELL 207
Cdd:pfam01660   86 RYPEAfsLEKSLGNGEDLRPTNTFED-CRVLApttSYAFMHDSLHDWSPEELADLFLRKPklerlyATLVFP----PELL 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319  208 esgslngrqgevvwsckfqrrtrmqiewakmkavltteekFSDNVSHEEWVTMTEPIKDpkaRIYFGMPGVLG--YGHSW 285
Cdd:pfam01660  161 ----------------------------------------FGDKESLYPELYTFWYKGD---RFHFYPDGHLGgsYTHPL 197
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126394319  286 nNYATWMHAPGVTCSNGITLLIER-QRFGAVVLMRIDRTSRGGILVGMPT----TTKEMVMIPDL 345
Cdd:pfam01660  198 -NLLSWLTTSKIHLPGGFTYTVERlESRGAHHLFKITRGDGLTPKVIVPDsrtfGPFEAVLLPKI 261
ps-ssRNA_RdRp_Tymovirales cd23207
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Tymovirales of ...
1142-1347 1.01e-04

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Tymovirales of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the order Tymovirales. The Tymovirales order contains viruses that mostly infect plants, have a single molecule of (+)ssRNA, and which are united by the similarities in their replication-associated polyproteins. Tymovirales contains five families (Alpha-, Beta-, Delta- and Gammaflexiviridae and Tymoviridae) and groups mostly plant-infecting agents, although a few Tymovirales members have either fungal or insect hosts. Botrytis virus F (BVF), isolated from the fungus Botrytis cinerea, is a flexuous mycovirus that is typical of members of the genus Mycoflexivirus (family Gammaflexiviridae). 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: 438057 [Multi-domain]  Cd Length: 188  Bit Score: 45.47  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1142 FVKEQTKCKISQWRPDAsdsfevlqnaaltylkekpdgsagltkeKAGQGVVAWSKIWNIVSAPYAKVMQKRLCDDTHPW 1221
Cdd:cd23207     14 FIKGQHKKKDEKIFSDA----------------------------KAGQTLALFHDQIILRFGPYARYMRRFINADLPPN 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1222 FMVASGYSEEDMarkmSQSVSNHgcffgtkgddavmilLKDGEYHVHscDQTQFDSRQSTLHFSLQDEFLRRLGMPAFII 1301
Cdd:cd23207     66 IYIHCGKTPEDL----SKWCKEH---------------WQHGPSTAN--DYTAFDQSQDGEFVVFEVLLMRHLHIPDDLI 124
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1126394319 1302 dsiwkmrERHSVRATDGTILMKNLQFGRDSGEPFTLDGNSLVTIAI 1347
Cdd:cd23207    125 -------ELYVDIKTNAYSHLGPLSIMRLTGEPGTFDFNTDYNLAL 163
Bromoviridae_RdRp cd23252
RNA-dependent RNA polymerase (RdRp) in the family Bromoviridae of positive-sense ...
1271-1346 2.89e-04

RNA-dependent RNA polymerase (RdRp) in the family Bromoviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Bromoviridae, order Martellivirales. The Bromoviridae family of plant viruses contains tri-segmented, (+)ssRNA viruses with a total genome size of about 8 kb. There are six genera in this family: Alfamovirus, Anulavirus, Bromovirus, Cucumovirus, Ilarvirus, and Oleavirus. Bromoviridae virions are variable in morphology (spherical or bacilliform) and are transmitted mechanically, in/on the pollen and non-persistently by insect vectors. Members of the family cause major disease epidemics in fruit, vegetable and fodder crops such as tomato, cucurbits, bananas, and alfalfa. 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: 438102  Cd Length: 332  Bit Score: 45.30  E-value: 2.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126394319 1271 DQTQFDSRQSTLHFSLQDEFLRRLGMPAFIIDSIWKMRERHSVRATDGTILMkNLQFGRDSGEPFTLDGNSLVTIA 1346
Cdd:cd23252    173 DFSKFDKSQGELHHEIQEHILNALGCPAPFTKWWFDFHRRSYISDRRAGVGF-SVDFQRRTGDAFTYLGNTLVTLA 247
Closteroviridae_RdRp cd23253
RNA-dependent RNA polymerase (RdRp) in the family Closteroviridae of positive-sense ...
1264-1427 8.36e-04

RNA-dependent RNA polymerase (RdRp) in the family Closteroviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Closteroviridae, order Martellivirales. Viruses in the family Closteroviridae have a mono-, bi- or tripartite (+)ssRNA genome of 13-19 kb, and non-enveloped, filamentous particles 650-2200 nm long and 12 nm in diameter. They infect plants, mainly dicots, many of which are fruit crops. Members of the family are classified into four genera: Ampelovirus, Closterovirus, Crinivirus and Velarivirus. Their genetic diversity is primarily influenced by strong negative selection and recombination. Closteroviridae viruses are mostly phloem-restricted and induce specific cytoplasmic aggregates of virus particles intermingled with membranous vesicles derived from the endoplasmic reticulum and possibly mitochondria. Their transmission is by aphids, whiteflies, pseudococcid mealybugs or soft scale insects in a semi-persistent manner. 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: 438103  Cd Length: 266  Bit Score: 43.70  E-value: 8.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1264 EYHVHSCDQTQFDSRQSTLHFSLQDEFLRRLGMPAFIIDSiWKMRERHSVRAT-DGTIlmkNLQFG--RDSGEPFTLDGN 1340
Cdd:cd23253     84 EYKTVEIDFSKFDKSQGVLFKVYEELVYKFFGFSEELYDN-WKCSEYFSCRATsDSGV---SLELGaqRRTGSPNTWLGN 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126394319 1341 SLVTIAinIRALQPTVQECELVDI----------NPTSESFEAAQDLFDMVIKheFTHN-----IGEFIgyIFVaEANIp 1405
Cdd:cd23253    160 TLVTLG--ILSSSYDLDDIDLLLVsgddslifskKPLPNKANEINLDFGFEAK--FIENsvpyfCSKFI--IED-RGKI- 231
                          170       180
                   ....*....|....*....|..
gi 1126394319 1406 KFVPNIVKRVTKeLGRAYKPQD 1427
Cdd:cd23253    232 KVVPDPVKLFEK-LSVPIRLED 252
 
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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