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Conserved domains on  [gi|1752309242|gb|QEV86990|]
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polyprotein [Feline kobuvirus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Kobuvirus_RdRp cd23214
RNA-dependent RNA polymerase (RdRp) in the Kobuvirus genus of positive-sense single-stranded ...
1979-2430 0e+00

RNA-dependent RNA polymerase (RdRp) in the Kobuvirus genus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Kobuvirus genus within the family Picornaviridae, order Picornavirales. Kobuviruses are small, icosahedral and spherical viruses, with a (+)ssRNA genome. Unlike other picornaviruses, Kobuvirus capsids show a distinctive lumpy morphology when observed by electron microscopy; "kobu" means "knob" in Japanese. There are six species (Aichivirus A-F) in this genus. Initially, the genus Kobuvirus was divided into three species: Aichivirus A (AiVA, formerly Aichi virus), Aichivirus B (AivB, formerly Bovine kobuvirus) and Aichivirus C (AiVC, formerly Porcine kobuvirus) each possessing a single serotype. Canine kobuvirus belong to species Aichivirus A. Aichi virus infects humans, while bovine kobuvirus, porcine kobuvirus and canine kobuvirus infects cattle, swine, dogs and cats, respectively. Kobuviruses have also been detected in black goats, rabbits, European roller, and bats. RdRps are multi-domain proteins that play a pivotal role in enterovirus replication. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of kobuviruses. 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: 438064  Cd Length: 459  Bit Score: 940.04  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1979 PGVNINRMSRLKP------FPIKKEPAPLKRNDRRLNDGVDLDTQLFLKHGKGDQSEPWPGLEAAADLYFSTFPSSLPVL 2052
Cdd:cd23214      1 PGVNVNRKSRLGPspaygaFPVKKQPAPLTQKDDRLEDGIRLDDQLFLKHNKGDMDEPWPGLEAAADLYFSKFPTMIRTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2053 TQEQAIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDEPEPGFYTPRPELQILIDQTLENPDYVYSTFLKDELRPTAKVQ 2132
Cdd:cd23214     81 TQEEAINGTPNLEGLDMNQAAGYPWNTMGRSRRSLFVEVQPGIYVPKPELQAEIDKTLEDPDYFYSTFLKDELRPTAKVT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2133 DGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCNPDIHWTEFFYKFADFSQVYDLDYKCFDATLPSAAFTL 2212
Cdd:cd23214    161 LGLTRVVEAAPIHAIVAGRMLLGGLIEYMQARPGKHGSAVGCNPDLHWTKFFYKFCHYPQVFDLDYKCFDATLPSCAFRI 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2213 VAERLERLTGDPRVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQHPDFSPSQFQILAYGD 2292
Cdd:cd23214    241 VEDHLERLTGDERVTRYIESIRHSHHVYGNETYEMIGGNPSGCVGTSIINTIINNICVLSALIQHPDFSPESFRILAYGD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2293 DVIYATEPPIHPSFLRDFYQKYTPLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDIRPVYIHPVMDPDTYEQSVMWLRD 2372
Cdd:cd23214    321 DVIYGCDPPIHPSFIKEFYDKHTPLVVTPANKGSDFPETSTIYDVTFLKRWFVPDDIRPFYIHPVMDPDTYEQSVMWLRD 400
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1752309242 2373 GDFQDVVTSLCHLAFHSGPKTYERWCTKVREQCLKT-GFAPTFLPYSYLQLRWLNMLAA 2430
Cdd:cd23214    401 GDFQDLVTSLCYLAFHSGPKTYDRWCTRVRDQVMKTtGFPPTFLPYSYLQTRWLNLLAA 459
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
1449-1551 1.02e-39

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


:

Pssm-ID: 459992  Cd Length: 102  Bit Score: 143.13  E-value: 1.02e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1449 VYFYGPPGTGKSLLASLLAQTLAQRLSGDPDDVYSPTAAScEYFDGYNGQSVHFIDDIGQDPEGRDWANFPNLVSSAPYI 1528
Cdd:pfam00910    1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSVYSRNPDD-DFWDGYTGQPVVIIDDFGQNPDGPDEAELIRLVSSTPYP 79
                           90       100
                   ....*....|....*....|...
gi 1752309242 1529 LPMASLEEKGIHYTSRVIVVTSN 1551
Cdd:pfam00910   80 PPMAALEEKGTPFTSKFVIVTSN 102
rhv_like cd00205
Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA ...
381-541 7.15e-33

Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids composed of 60 copies each of 4 virus encoded proteins; alignment includes picornaviridae, like poliovirus, hepatitis A virus, rhinovirus, foot-and-mouth disease virus and encephalomyocarditis virus; common structure is an 8-stranded beta sandwich


:

Pssm-ID: 119412  Cd Length: 178  Bit Score: 126.74  E-value: 7.15e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  381 FPISTATNWGVQDQQPPTAYPLPFS-FCRAYPDSPWTAMYNTHSMWNCGWRVQVTVNGSQFHAGALTLYMVPEGATESVE 459
Cdd:cd00205      9 TTVGTNNWNSSASGTQLFQWKLSPAlGFLLLQNTPLGALLSYFTYWRGDLEVTVQFNGSKFHTGRLLVAYVPPGAPAPTT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  460 AARLNAGFVFPYVILSLYESNTATLEVPFISPTPNTSSGLH------APWTFYLQVLSPLNPPTGVPTSLSCSIYVTPVD 533
Cdd:cd00205     89 GDTRWQATLNPHVIWDLGTNSSVTFVVPYVSPTPYRSTRYDgygplnSFGTLVVRVLTPLTVPSGAPTTVDITVYVRAGD 168

                   ....*...
gi 1752309242  534 STFHGLRY 541
Cdd:cd00205    169 FELYGPRP 176
rhv_like cd00205
Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA ...
591-763 3.06e-30

Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids composed of 60 copies each of 4 virus encoded proteins; alignment includes picornaviridae, like poliovirus, hepatitis A virus, rhinovirus, foot-and-mouth disease virus and encephalomyocarditis virus; common structure is an 8-stranded beta sandwich


:

Pssm-ID: 119412  Cd Length: 178  Bit Score: 119.04  E-value: 3.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  591 EFAQRPGIMAPFPWTmAEEPGERLGIFPVSPSA--IAGTGAPISYVLSLFSQWRGELAAHLLFTGSAQHYGRLVVCYTP- 667
Cdd:cd00205      3 SFADRPTTVGTNNWN-SSASGTQLFQWKLSPALgfLLLQNTPLGALLSYFTYWRGDLEVTVQFNGSKFHTGRLLVAYVPp 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  668 AAPAPPSN--MQEAMRGTYTVWDVNAASTLEFTIPFISQSYWKTVDIfNPDALLSTTGYVSVWVLNPLTGPQSAPASAIV 745
Cdd:cd00205     82 GAPAPTTGdtRWQATLNPHVIWDLGTNSSVTFVVPYVSPTPYRSTRY-DGYGPLNSFGTLVVRVLTPLTVPSGAPTTVDI 160
                          170
                   ....*....|....*...
gi 1752309242  746 QGFLSAGEsFNVRFMQNP 763
Cdd:cd00205    161 TVYVRAGD-FELYGPRPP 177
rhv_like cd00205
Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA ...
841-994 7.97e-20

Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids composed of 60 copies each of 4 virus encoded proteins; alignment includes picornaviridae, like poliovirus, hepatitis A virus, rhinovirus, foot-and-mouth disease virus and encephalomyocarditis virus; common structure is an 8-stranded beta sandwich


:

Pssm-ID: 119412  Cd Length: 178  Bit Score: 88.99  E-value: 7.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  841 SLSPLNWQTTTNYTGLAAMLSCFTYIAADLRFTLRISNPNGVPATVLIAYAPPGATLP-RNPDRQMLSNFFMSEVPLTAS 919
Cdd:cd00205     29 KLSPALGFLLLQNTPLGALLSYFTYWRGDLEVTVQFNGSKFHTGRLLVAYVPPGAPAPtTGDTRWQATLNPHVIWDLGTN 108
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752309242  920 NAtlVSFSIPYTSPLSAIPTTYYGWedWSGANFGVLQAGSWGSLLLMPTFPAEVPhadplsATMWVAFGNFKAWV 994
Cdd:cd00205    109 SS--VTFVVPYVSPTPYRSTRYDGY--GPLNSFGTLVVRVLTPLTVPSGAPTTVD------ITVYVRAGDFELYG 173
Peptidase_C3 super family cl02893
3C cysteine protease (picornain 3C); Picornaviral proteins are expressed as a single ...
1787-1942 9.43e-08

3C cysteine protease (picornain 3C); Picornaviral proteins are expressed as a single polyprotein which is cleaved by the viral 3C cysteine protease.


The actual alignment was detected with superfamily member pfam00548:

Pssm-ID: 278947  Cd Length: 174  Bit Score: 53.99  E-value: 9.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1787 ISQNVVHVESGNGneKVVMSGFYIFSRYLLVPTHLREPHHTTL--LVGTDAYDWATLPTL--TLGELTLVHTPTSRQYKD 1862
Cdd:pfam00548   11 LKQNAVPVTTSKG--VFTCCATGVYDNVILLPRHAEPGLTIVLdgKVVTISDPEVELVDQegMPLDAAIVKLKRNEKFKD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1863 MRRFIGSYPHPTG---ILVSQYKAAPLY-----VRFSDNRV-LDMD-FPGAIVckqaygYRAATFEGLCGSPLVTDDPAG 1932
Cdd:pfam00548   89 IRKHLPNRITKGNpvvLLINNNEQGRIYvpvgaVTHSGGIKtLDGTtTPRTIS------YNAPTKAGMCGGVVIAKVEGN 162
                          170
                   ....*....|
gi 1752309242 1933 IKILGLHVAG 1942
Cdd:pfam00548  163 GKILGMHIAG 172
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
1423-1470 4.02e-04

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd19481:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 158  Bit Score: 43.04  E-value: 4.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1752309242 1423 QSLKNYTLALSQHRKRQVGPRPEPVVVYFYGPPGTGKSLLASLLAQTL 1470
Cdd:cd19481      3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGEL 50
 
Name Accession Description Interval E-value
Kobuvirus_RdRp cd23214
RNA-dependent RNA polymerase (RdRp) in the Kobuvirus genus of positive-sense single-stranded ...
1979-2430 0e+00

RNA-dependent RNA polymerase (RdRp) in the Kobuvirus genus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Kobuvirus genus within the family Picornaviridae, order Picornavirales. Kobuviruses are small, icosahedral and spherical viruses, with a (+)ssRNA genome. Unlike other picornaviruses, Kobuvirus capsids show a distinctive lumpy morphology when observed by electron microscopy; "kobu" means "knob" in Japanese. There are six species (Aichivirus A-F) in this genus. Initially, the genus Kobuvirus was divided into three species: Aichivirus A (AiVA, formerly Aichi virus), Aichivirus B (AivB, formerly Bovine kobuvirus) and Aichivirus C (AiVC, formerly Porcine kobuvirus) each possessing a single serotype. Canine kobuvirus belong to species Aichivirus A. Aichi virus infects humans, while bovine kobuvirus, porcine kobuvirus and canine kobuvirus infects cattle, swine, dogs and cats, respectively. Kobuviruses have also been detected in black goats, rabbits, European roller, and bats. RdRps are multi-domain proteins that play a pivotal role in enterovirus replication. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of kobuviruses. 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: 438064  Cd Length: 459  Bit Score: 940.04  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1979 PGVNINRMSRLKP------FPIKKEPAPLKRNDRRLNDGVDLDTQLFLKHGKGDQSEPWPGLEAAADLYFSTFPSSLPVL 2052
Cdd:cd23214      1 PGVNVNRKSRLGPspaygaFPVKKQPAPLTQKDDRLEDGIRLDDQLFLKHNKGDMDEPWPGLEAAADLYFSKFPTMIRTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2053 TQEQAIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDEPEPGFYTPRPELQILIDQTLENPDYVYSTFLKDELRPTAKVQ 2132
Cdd:cd23214     81 TQEEAINGTPNLEGLDMNQAAGYPWNTMGRSRRSLFVEVQPGIYVPKPELQAEIDKTLEDPDYFYSTFLKDELRPTAKVT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2133 DGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCNPDIHWTEFFYKFADFSQVYDLDYKCFDATLPSAAFTL 2212
Cdd:cd23214    161 LGLTRVVEAAPIHAIVAGRMLLGGLIEYMQARPGKHGSAVGCNPDLHWTKFFYKFCHYPQVFDLDYKCFDATLPSCAFRI 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2213 VAERLERLTGDPRVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQHPDFSPSQFQILAYGD 2292
Cdd:cd23214    241 VEDHLERLTGDERVTRYIESIRHSHHVYGNETYEMIGGNPSGCVGTSIINTIINNICVLSALIQHPDFSPESFRILAYGD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2293 DVIYATEPPIHPSFLRDFYQKYTPLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDIRPVYIHPVMDPDTYEQSVMWLRD 2372
Cdd:cd23214    321 DVIYGCDPPIHPSFIKEFYDKHTPLVVTPANKGSDFPETSTIYDVTFLKRWFVPDDIRPFYIHPVMDPDTYEQSVMWLRD 400
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1752309242 2373 GDFQDVVTSLCHLAFHSGPKTYERWCTKVREQCLKT-GFAPTFLPYSYLQLRWLNMLAA 2430
Cdd:cd23214    401 GDFQDLVTSLCYLAFHSGPKTYDRWCTRVRDQVMKTtGFPPTFLPYSYLQTRWLNLLAA 459
RdRP_1 pfam00680
Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase ...
1991-2396 4.10e-54

Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase found in many positive strand RNA eukaryotic viruses. Structural studies indicate that these proteins form the "right hand" structure found in all oligonucleotide polymerases, containing thumb, finger and palm domains, and also the additional bridging finger and thumb domains unique to RNA-directed RNA polymerases.


Pssm-ID: 425815  Cd Length: 450  Bit Score: 197.25  E-value: 4.10e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1991 PFPIKKEPAPLKRND-----RRLNDGVDLDTQLFLKHGKGDQSEPWPG---LEAAADLYFSTF----PSSLPVLTQEQAI 2058
Cdd:pfam00680    8 VAIPAYVPASLGPEDprwarSYLNTDPYVDDIKKYSRPKLPGPADERDkllNRSAAKMVLSELrgvpKKANSTLIVYRAI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2059 HGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDE----PEPGFYTPRPELQILIDQTLENPDYVYSTFLKDELRPTAKVQDG 2134
Cdd:pfam00680   88 DGVEQIDPLNWDTSAGYPYVGLGGKKGDLIEHlkdgTEARELAERLAADWEVLQNGTPLKLVYQTCLKDELRPLEKVEKG 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2135 LTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCNPDI-HWTEFFYKFADFSQ-VYDLDYKCFDATLPSAAFTL 2212
Cdd:pfam00680  168 KTRLVWGEPVEYLLLERAFFDPFNQAFMLNNGFHPIQVGINPFDrGWPRLLRRLARFGDyVYELDYSGFDSSVPPWLIRF 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2213 VAERLERLTGDP-------RVAKYIhsIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALI-----QHPD- 2279
Cdd:pfam00680  248 AFEILRELLGFPsnvkewrAILELL--IYTPIALPNGTVFKKTGGLPSGSPFTSIINSIVNYLLILYALLkslenDGPRv 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2280 -FSPSQFQILAYGDDVIYATEPPIHPSF------LRDFYQKYtplvvTPANKgsDFPDTSTIHEVTFLKRWFVPDDIRpv 2352
Cdd:pfam00680  326 cNLDKYFDFFTYGDDSLVAVSPDFDPVLdrlsphLKELGLTI-----TPAKK--TFPVSRELEEVSFLKRTFRKTPGG-- 396
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1752309242 2353 yIHPVMDPDTYEQSVMWLRDGD-FQDVVTSLCHLAFHSGPKTYER 2396
Cdd:pfam00680  397 -YRPPLDRKRILAQLEYIRSKPvPSGQLENIRAYASHHGYEFYRD 440
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
1449-1551 1.02e-39

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 143.13  E-value: 1.02e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1449 VYFYGPPGTGKSLLASLLAQTLAQRLSGDPDDVYSPTAAScEYFDGYNGQSVHFIDDIGQDPEGRDWANFPNLVSSAPYI 1528
Cdd:pfam00910    1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSVYSRNPDD-DFWDGYTGQPVVIIDDFGQNPDGPDEAELIRLVSSTPYP 79
                           90       100
                   ....*....|....*....|...
gi 1752309242 1529 LPMASLEEKGIHYTSRVIVVTSN 1551
Cdd:pfam00910   80 PPMAALEEKGTPFTSKFVIVTSN 102
rhv_like cd00205
Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA ...
381-541 7.15e-33

Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids composed of 60 copies each of 4 virus encoded proteins; alignment includes picornaviridae, like poliovirus, hepatitis A virus, rhinovirus, foot-and-mouth disease virus and encephalomyocarditis virus; common structure is an 8-stranded beta sandwich


Pssm-ID: 119412  Cd Length: 178  Bit Score: 126.74  E-value: 7.15e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  381 FPISTATNWGVQDQQPPTAYPLPFS-FCRAYPDSPWTAMYNTHSMWNCGWRVQVTVNGSQFHAGALTLYMVPEGATESVE 459
Cdd:cd00205      9 TTVGTNNWNSSASGTQLFQWKLSPAlGFLLLQNTPLGALLSYFTYWRGDLEVTVQFNGSKFHTGRLLVAYVPPGAPAPTT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  460 AARLNAGFVFPYVILSLYESNTATLEVPFISPTPNTSSGLH------APWTFYLQVLSPLNPPTGVPTSLSCSIYVTPVD 533
Cdd:cd00205     89 GDTRWQATLNPHVIWDLGTNSSVTFVVPYVSPTPYRSTRYDgygplnSFGTLVVRVLTPLTVPSGAPTTVDITVYVRAGD 168

                   ....*...
gi 1752309242  534 STFHGLRY 541
Cdd:cd00205    169 FELYGPRP 176
rhv_like cd00205
Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA ...
591-763 3.06e-30

Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids composed of 60 copies each of 4 virus encoded proteins; alignment includes picornaviridae, like poliovirus, hepatitis A virus, rhinovirus, foot-and-mouth disease virus and encephalomyocarditis virus; common structure is an 8-stranded beta sandwich


Pssm-ID: 119412  Cd Length: 178  Bit Score: 119.04  E-value: 3.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  591 EFAQRPGIMAPFPWTmAEEPGERLGIFPVSPSA--IAGTGAPISYVLSLFSQWRGELAAHLLFTGSAQHYGRLVVCYTP- 667
Cdd:cd00205      3 SFADRPTTVGTNNWN-SSASGTQLFQWKLSPALgfLLLQNTPLGALLSYFTYWRGDLEVTVQFNGSKFHTGRLLVAYVPp 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  668 AAPAPPSN--MQEAMRGTYTVWDVNAASTLEFTIPFISQSYWKTVDIfNPDALLSTTGYVSVWVLNPLTGPQSAPASAIV 745
Cdd:cd00205     82 GAPAPTTGdtRWQATLNPHVIWDLGTNSSVTFVVPYVSPTPYRSTRY-DGYGPLNSFGTLVVRVLTPLTVPSGAPTTVDI 160
                          170
                   ....*....|....*...
gi 1752309242  746 QGFLSAGEsFNVRFMQNP 763
Cdd:cd00205    161 TVYVRAGD-FELYGPRPP 177
rhv_like cd00205
Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA ...
841-994 7.97e-20

Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids composed of 60 copies each of 4 virus encoded proteins; alignment includes picornaviridae, like poliovirus, hepatitis A virus, rhinovirus, foot-and-mouth disease virus and encephalomyocarditis virus; common structure is an 8-stranded beta sandwich


Pssm-ID: 119412  Cd Length: 178  Bit Score: 88.99  E-value: 7.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  841 SLSPLNWQTTTNYTGLAAMLSCFTYIAADLRFTLRISNPNGVPATVLIAYAPPGATLP-RNPDRQMLSNFFMSEVPLTAS 919
Cdd:cd00205     29 KLSPALGFLLLQNTPLGALLSYFTYWRGDLEVTVQFNGSKFHTGRLLVAYVPPGAPAPtTGDTRWQATLNPHVIWDLGTN 108
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752309242  920 NAtlVSFSIPYTSPLSAIPTTYYGWedWSGANFGVLQAGSWGSLLLMPTFPAEVPhadplsATMWVAFGNFKAWV 994
Cdd:cd00205    109 SS--VTFVVPYVSPTPYRSTRYDGY--GPLNSFGTLVVRVLTPLTVPSGAPTTVD------ITVYVRAGDFELYG 173
Rhv pfam00073
picornavirus capsid protein; CAUTION: This alignment is very weak. It can not be generated by ...
422-514 3.26e-14

picornavirus capsid protein; CAUTION: This alignment is very weak. It can not be generated by clustalw. If a representative set is used for a seed, many so-called members are not recognized. The family should probably be split up into sub-families. Capsid proteins of picornaviruses. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids. They include rhinovirus (common cold) and poliovirus. Common structure is an 8-stranded beta sandwich. Variations (one or two extra strands) occur.


Pssm-ID: 395026  Cd Length: 170  Bit Score: 72.73  E-value: 3.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  422 HSMWNCGWRVQVTVNGSQFHAGALTLYMVPEGATESVEAARLNAGFVFPYVILSLYESNTATLEVPFISPTPNTSSGLHA 501
Cdd:pfam00073   77 HTYYRGGLEVTVQFNGSKFHQGKLLVAYVPPGAPPPGSRDYLWQATLNPHQFWNLGLNSSARLSVPYISIAHYYSTFYDG 156
                           90
                   ....*....|...
gi 1752309242  502 PWTFYLQVLSPLN 514
Cdd:pfam00073  157 NWTLVVAGWVPLN 169
Rhv pfam00073
picornavirus capsid protein; CAUTION: This alignment is very weak. It can not be generated by ...
635-729 1.73e-09

picornavirus capsid protein; CAUTION: This alignment is very weak. It can not be generated by clustalw. If a representative set is used for a seed, many so-called members are not recognized. The family should probably be split up into sub-families. Capsid proteins of picornaviruses. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids. They include rhinovirus (common cold) and poliovirus. Common structure is an 8-stranded beta sandwich. Variations (one or two extra strands) occur.


Pssm-ID: 395026  Cd Length: 170  Bit Score: 59.25  E-value: 1.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  635 LSLFSQWRGELAAHLLFTGSAQHYGRLVVCYTPAAPAPPSNMQ---EAMRGTYTVWDVNAASTLEFTIPFISQS---YWK 708
Cdd:pfam00073   74 LRYHTYYRGGLEVTVQFNGSKFHQGKLLVAYVPPGAPPPGSRDylwQATLNPHQFWNLGLNSSARLSVPYISIAhyySTF 153
                           90       100
                   ....*....|....*....|.
gi 1752309242  709 TVDIFNpdalLSTTGYVSVWV 729
Cdd:pfam00073  154 YDGNWT----LVVAGWVPLNY 170
Peptidase_C3 pfam00548
3C cysteine protease (picornain 3C); Picornaviral proteins are expressed as a single ...
1787-1942 9.43e-08

3C cysteine protease (picornain 3C); Picornaviral proteins are expressed as a single polyprotein which is cleaved by the viral 3C cysteine protease.


Pssm-ID: 278947  Cd Length: 174  Bit Score: 53.99  E-value: 9.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1787 ISQNVVHVESGNGneKVVMSGFYIFSRYLLVPTHLREPHHTTL--LVGTDAYDWATLPTL--TLGELTLVHTPTSRQYKD 1862
Cdd:pfam00548   11 LKQNAVPVTTSKG--VFTCCATGVYDNVILLPRHAEPGLTIVLdgKVVTISDPEVELVDQegMPLDAAIVKLKRNEKFKD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1863 MRRFIGSYPHPTG---ILVSQYKAAPLY-----VRFSDNRV-LDMD-FPGAIVckqaygYRAATFEGLCGSPLVTDDPAG 1932
Cdd:pfam00548   89 IRKHLPNRITKGNpvvLLINNNEQGRIYvpvgaVTHSGGIKtLDGTtTPRTIS------YNAPTKAGMCGGVVIAKVEGN 162
                          170
                   ....*....|
gi 1752309242 1933 IKILGLHVAG 1942
Cdd:pfam00548  163 GKILGMHIAG 172
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
1435-1573 2.47e-06

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 49.45  E-value: 2.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1435 HRKRQVGPRPEPVVVYFYGPPGTGKSLLASLLAQTLAQR----LSGDPDDVYSPTAASCEYFDGYNGQ----------SV 1500
Cdd:cd00009      8 EALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgapfLYLNASDLLEGLVVAELFGHFLVRLlfelaekakpGV 87
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752309242 1501 HFIDDIGQDPEGRDWANFPNlvssapyilpMASLEEKGIHYTSRVIVVTSNFHEPNERAARSMGALRRRVHLR 1573
Cdd:cd00009     88 LFIDEIDSLSRGAQNALLRV----------LETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
1430-1470 2.76e-04

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 45.67  E-value: 2.76e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1752309242 1430 LALSQHRKRQVGPRPEPVVVYFYGPPGTGKSLLASLLAQTL 1470
Cdd:COG0464    175 LPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGEL 215
Rhv pfam00073
picornavirus capsid protein; CAUTION: This alignment is very weak. It can not be generated by ...
856-943 3.65e-04

picornavirus capsid protein; CAUTION: This alignment is very weak. It can not be generated by clustalw. If a representative set is used for a seed, many so-called members are not recognized. The family should probably be split up into sub-families. Capsid proteins of picornaviruses. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids. They include rhinovirus (common cold) and poliovirus. Common structure is an 8-stranded beta sandwich. Variations (one or two extra strands) occur.


Pssm-ID: 395026  Cd Length: 170  Bit Score: 43.45  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  856 LAAMLSCFTYIAADLRFTLRIsNPNGVPA-TVLIAYAPPGATLPRNPDRQMLSNFFMSEVPLTASNATlVSFSIPYTSPL 934
Cdd:pfam00073   70 LGRLLRYHTYYRGGLEVTVQF-NGSKFHQgKLLVAYVPPGAPPPGSRDYLWQATLNPHQFWNLGLNSS-ARLSVPYISIA 147

                   ....*....
gi 1752309242  935 SAIPTTYYG 943
Cdd:pfam00073  148 HYYSTFYDG 156
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
1423-1470 4.02e-04

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 43.04  E-value: 4.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1752309242 1423 QSLKNYTLALSQHRKRQVGPRPEPVVVYFYGPPGTGKSLLASLLAQTL 1470
Cdd:cd19481      3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGEL 50
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1448-1573 9.50e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 41.98  E-value: 9.50e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  1448 VVYFYGPPGTGKSLLASLLAQTLAQR------LSGDPDDVYSPTAASCEYFDGYNGQSVH-------------------F 1502
Cdd:smart00382    4 VILIVGPPGSGKTTLARALARELGPPgggviyIDGEDILEEVLDQLLLIIVGGKKASGSGelrlrlalalarklkpdvlI 83
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752309242  1503 IDDIG--QDPEGRDWANFpnlvssapyILPMASLEEKGIHYTSRVIVVTSNFHEPNERAARSMgaLRRRVHLR 1573
Cdd:smart00382   84 LDEITslLDAEQEALLLL---------LEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR--FDRRIVLL 145
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
1451-1470 8.83e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 41.22  E-value: 8.83e-03
                           10        20
                   ....*....|....*....|
gi 1752309242 1451 FYGPPGTGKSLLASLLAQTL 1470
Cdd:PRK13342    41 LWGPPGTGKTTLARIIAGAT 60
 
Name Accession Description Interval E-value
Kobuvirus_RdRp cd23214
RNA-dependent RNA polymerase (RdRp) in the Kobuvirus genus of positive-sense single-stranded ...
1979-2430 0e+00

RNA-dependent RNA polymerase (RdRp) in the Kobuvirus genus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Kobuvirus genus within the family Picornaviridae, order Picornavirales. Kobuviruses are small, icosahedral and spherical viruses, with a (+)ssRNA genome. Unlike other picornaviruses, Kobuvirus capsids show a distinctive lumpy morphology when observed by electron microscopy; "kobu" means "knob" in Japanese. There are six species (Aichivirus A-F) in this genus. Initially, the genus Kobuvirus was divided into three species: Aichivirus A (AiVA, formerly Aichi virus), Aichivirus B (AivB, formerly Bovine kobuvirus) and Aichivirus C (AiVC, formerly Porcine kobuvirus) each possessing a single serotype. Canine kobuvirus belong to species Aichivirus A. Aichi virus infects humans, while bovine kobuvirus, porcine kobuvirus and canine kobuvirus infects cattle, swine, dogs and cats, respectively. Kobuviruses have also been detected in black goats, rabbits, European roller, and bats. RdRps are multi-domain proteins that play a pivotal role in enterovirus replication. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of kobuviruses. 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: 438064  Cd Length: 459  Bit Score: 940.04  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1979 PGVNINRMSRLKP------FPIKKEPAPLKRNDRRLNDGVDLDTQLFLKHGKGDQSEPWPGLEAAADLYFSTFPSSLPVL 2052
Cdd:cd23214      1 PGVNVNRKSRLGPspaygaFPVKKQPAPLTQKDDRLEDGIRLDDQLFLKHNKGDMDEPWPGLEAAADLYFSKFPTMIRTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2053 TQEQAIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDEPEPGFYTPRPELQILIDQTLENPDYVYSTFLKDELRPTAKVQ 2132
Cdd:cd23214     81 TQEEAINGTPNLEGLDMNQAAGYPWNTMGRSRRSLFVEVQPGIYVPKPELQAEIDKTLEDPDYFYSTFLKDELRPTAKVT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2133 DGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCNPDIHWTEFFYKFADFSQVYDLDYKCFDATLPSAAFTL 2212
Cdd:cd23214    161 LGLTRVVEAAPIHAIVAGRMLLGGLIEYMQARPGKHGSAVGCNPDLHWTKFFYKFCHYPQVFDLDYKCFDATLPSCAFRI 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2213 VAERLERLTGDPRVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQHPDFSPSQFQILAYGD 2292
Cdd:cd23214    241 VEDHLERLTGDERVTRYIESIRHSHHVYGNETYEMIGGNPSGCVGTSIINTIINNICVLSALIQHPDFSPESFRILAYGD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2293 DVIYATEPPIHPSFLRDFYQKYTPLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDIRPVYIHPVMDPDTYEQSVMWLRD 2372
Cdd:cd23214    321 DVIYGCDPPIHPSFIKEFYDKHTPLVVTPANKGSDFPETSTIYDVTFLKRWFVPDDIRPFYIHPVMDPDTYEQSVMWLRD 400
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1752309242 2373 GDFQDVVTSLCHLAFHSGPKTYERWCTKVREQCLKT-GFAPTFLPYSYLQLRWLNMLAA 2430
Cdd:cd23214    401 GDFQDLVTSLCYLAFHSGPKTYDRWCTRVRDQVMKTtGFPPTFLPYSYLQTRWLNLLAA 459
ps-ssRNA_Picornaviridae cd23193
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Picornaviridae of ...
2057-2402 7.41e-164

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Picornaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Picornaviridae, order Picornavirales. The Picornaviridae family consists of small, icosahedral viruses with (+)ssRNA genomes. Characteristic features of all members of the family Picornaviridae are three capsid proteins with beta-barrel folding, polyprotein processing by virus-encoded cysteine proteinase(s), and replication by an RdRp with a YGDD sequence motif. The family Picornaviridae comprises 68 genera containing 158 species, but many viruses are presently awaiting classification. The established genera of the family include: Aphthovirus, Avisivirus, Crohivirus, Enterovirus, Teschovirus, Cardiovirus, Erbovirus, Kobuvirus, Hepatovirus, Parechovirus, Aquamavirus, Avihepatovirus, Avisivirus, Cosavirus, Dicipivirus, Fipivirus, Gallivirus, Hunnivirus, Kunsagivirus, Limnipivirus, Megrivirus, Mischivirus, Mosavirus, Oscivirus, Pasivirus, Passerivirus, Rabovirus, Rosavirus, Sakobuvirus, Salivirus, Sapelovirus, Senecavirus, Sicinivirus, and Tremovirus. The Picornaviridae contains many important human and animal pathogens including enteroviruses (such as poliovirus, enterovirus, coxsackievirus, and rhinovirus), cardioviruses (such as encephalomyocarditis virus and Theiler's virus), hepatitis A virus and foot-and-mouth disease virus. Infection with various picornaviruses may cause encephalitis, febrile rash illnesses (hand-foot-and-mouth disease), aseptic meningitis, hepatitis, conjunctivitis, herpangina, myositis and myocarditis, and the common cold. 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: 438043  Cd Length: 345  Bit Score: 508.63  E-value: 7.41e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2057 AIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDePEPGFYTPRPELQILIDQTLENPDYVYSTFLKDELRPTAKVQDGLT 2136
Cdd:cd23193      1 AINGIDGLDPIDLNTSPGYPYTTQGLRRRDLID-NDKGGVSPLLEEEEQVLLDLDGPDVVFTTFLKDELRPKEKVKAGKT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2137 RIVEAAPIHAIIAGRMLLGGLIDYMQGRPG-EHGCAVGCNPDIHWTEFFYKFaDFSQVYDLDYKCFDATLPSAAFTLVAE 2215
Cdd:cd23193     80 RVIEAAPLDYVIAGRMVFGRLFAQFHSNPGiLTGSAVGCNPDTDWTRLFASL-KQDNVYDLDYSGFDASLSSQLFEAAVE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2216 RLERLTGDP-RVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQHPDFSPSQFQILAYGDDV 2294
Cdd:cd23193    159 VLAECHGDPeLVLRYLEPIINSKHVVGDERYTVEGGMPSGCPCTSILNSICNNLVVRYALLETGKFDPDEYYILAYGDDV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2295 IYATEPPIHPSFLRDFYQKYTPLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDIRpvYIHPVMDPDTYEQSVMWL-RDG 2373
Cdd:cd23193    239 LVSTDEPIDPSDLAEFYKKYFGMTVTPADKSSDFPESSPIEDVFLKRRFFVPDGTF--LIHPVMDLETLEQSLMWCgRGG 316
                          330       340
                   ....*....|....*....|....*....
gi 1752309242 2374 DFQDVVTSLCHLAFHSGPKTYERWCTKVR 2402
Cdd:cd23193    317 FFQQLLSSLCELALHHGPEEYERLVSKVR 345
Passerivirus_RdRp cd23224
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Passerivirus of ...
2056-2430 9.02e-153

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Passerivirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Passerivirus genus within the family Picornaviridae, order Picornavirales. The Passerivirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. There are two species in this genus: Passerivirus A and a second, novel passerivirus (Passerivirus B) that was discovered in 2018 in a population of Hungarian home-reared finches, where it achieved an over 50 percent mortality rate. Birds serve as natural hosts. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438074  Cd Length: 380  Bit Score: 478.81  E-value: 9.02e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2056 QAIHGTPNMEGLDMGQAAGFPWNTQgRSRRSLFDEPEPGFYTPRPELQILIDQTLENPDYVYSTFLKDELRPTAKVQDGL 2135
Cdd:cd23224      1 EAINGTPLLDGLDMKQSPGYPWSLT-TNRRSLFTQDETGKYYPVPELEEAVLACLENPDYFYTTHLKDELRPVEKALAGK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2136 TRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCNPDIHWTEFFYKFADFSQVYDLDYKCFDATLPSAAFTLVAE 2215
Cdd:cd23224     80 TRLIEAAPIHAIIAGRMLLGGLFEYMHARPGEHGSAVGCDPDYHWTPFFHSFDEFSQVWALDYSCFDSTLPSCCFDLIAQ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2216 RLERLT------GDPRVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQHPDFSPSQFQILA 2289
Cdd:cd23224    160 KLAKIItpgegiAPDAIVKYIRSISISKHVFGNEAYLMVGGNPSGCVGTSILNSMINNCVLISAFLTQKDFNPNQMRILT 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2290 YGDDVIYATEPPIHPSFLRDFYQKYTPLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDIRPVYIHPVMDPDTYEQSVMW 2369
Cdd:cd23224    240 YGDDVLYATNPPIHPRVVKKFFDENTTLIVTPATKAGDFPDESTIWDVTFLKRYFVPDEIRPWYVHPVIEPATYEQSVMW 319
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752309242 2370 LRDGDFQDVVTSLCHLAFHSGPKTYERWCTKVREQCLKTGFAPTFLPYSYLQLRWLNMLAA 2430
Cdd:cd23224    320 TRGGDFQDVVTSLSFLAHHAGPTNYMIWEEKVRKAAAAKGVSLNILPYSYLQHRWMLLVTS 380
Megrivirus_RdRp cd23223
RNA-dependent RNA polymerase (RdRp) in the genus Megrivirus of positive-sense single-stranded ...
1992-2409 5.37e-137

RNA-dependent RNA polymerase (RdRp) in the genus Megrivirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Megrivirus genus within the family Picornaviridae, order Picornavirales. The Megrivirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. The genus Megrivirus contains a five species Megrivirus A, Megrivirus B, Megrivirus C, Megrivirus D and Megrivirus E. The name Megrivirus is derived from the turkey genus name Meleagris. Megrivirus A is comprised of turkey hepatitis virus 1 (THV-1), duck megrivirus and goose megrivirus 1. Megrivirus B contains the mesiviruses. Megrivirus D contains harrier picornavirus 1 (HaPV-1). Megrivirus E was found in an Adelie penguin. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438073  Cd Length: 432  Bit Score: 436.20  E-value: 5.37e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1992 FPIKKEPAPLKRNDRRLNDGVDLDTQLFLKHgKGDQsEPWPGLEAAA---------DLYFSTFpSSLPVLTQEQAIHGTP 2062
Cdd:cd23223      5 FPVTHGPAALTNKDKRLEEGVDLDDVMFSKH-VPDH-PGWPTLEPAMsyvvedlmhKLGFSKD-EPVPMWTLEQAINGEG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2063 NMEGLDMGQAAGFPWNTQGRSRRSLFdEPEPGFYTPRPELQILIDQTLENP-DYVYSTFLKDELRPTAKVQDGLTRIVEA 2141
Cdd:cd23223     82 VMDGIDMGQSPGYPYNAQGRSRRSFF-EWNGEKWQPTEELKKEVDHALKDPdDFYFSTFLKDELRPLEKVKAGKTRLVDG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2142 APIHAIIAGRMLLGGLIDYMQGRPG-EHGCAVGCNPDIHWTEFFYKF--ADFSQVYDLDYKCFDATLPSAAFTLVAERLE 2218
Cdd:cd23223    161 DSLPRILAMRMVFGPLFEAMLRKNGpEIHSAVGCNPDTDWTRYYHEMgpDSFPYCFDLDYSCFDSTEPKIAFRLMAKYLK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2219 RLTGDPrVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQHpDFSPSQFQILAYGDDVIYAT 2298
Cdd:cd23223    241 PYFSVD-VTPFFEALATSKHVYGDKAYEMEGGMPSGCVGTSMFNCINNSAFIVSALIAL-KISPEDCAWICYGDDVIIST 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2299 EPPIHPSFLRDFYQKYTPLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDIRPVYIHPVMDPDTYEQSVMWLRDGDFQDV 2378
Cdd:cd23223    319 DEKALSKRIADFYHKNTNLVVTPASKSGDFPETSTIYDVTFLKRFFQPDSHYPHLIHPYMPLEHLEQSVMWQTDGPFQQK 398
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1752309242 2379 VTSLCHLAFHSGPKTYERWCTKVREQCLKTG 2409
Cdd:cd23223    399 LDSLCLLAFHAGGPDYREFVDAIDKKCRSRG 429
Dicipivirus_RdRp cd23222
RNA-dependent RNA polymerase (RdRp) in the genus Dicipivirus of positive-sense single-stranded ...
1992-2425 9.21e-121

RNA-dependent RNA polymerase (RdRp) in the genus Dicipivirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Dicipivirus genus within the family Picornaviridae, order Picornavirales. The Dicipivirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. The genus Dicipivirus contains two species, Cadicivirus A and Cadicivirus B. A new dicipivirus has been found in hedgehogs. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438072  Cd Length: 451  Bit Score: 390.10  E-value: 9.21e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1992 FPIKKEPAPLKRNDRRLNDGVDLDTQLFLKHGkGDQSEPWPGLEAAADLYFS----TFPSSL-PVLTQEQAIHGTPNMEG 2066
Cdd:cd23222      9 YPVTKEPAPLKPTDRRIDEGVDFNEPVFGKYG-ADMKEPFRNLDVGRDVVIArlkkVLPNKKfAPCTVSEALNGKDGLPK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2067 LDMGQAAGFPWNTQGRSRRSLFDEPEPGFYTPRPELQILIDQTLENPD-YVYSTFLKDELRPTAKVQDGLTRIVEAAPIH 2145
Cdd:cd23222     88 LDLKQASGYPYNLSAIKRKHLIESDKDGFLTATPKLLADIEESKKHPEkFPYTSFLKDELRSVKKVKAGKTRVVEAGSLP 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2146 AIIAGRMLLGGLIDYMQGRPG-EHGCAVGCNPDIHWTEFFYKFADFSQVYDLDYKCFDATLPSAAFTLVAERL-ERLTGD 2223
Cdd:cd23222    168 VIVEGRMIFGNLFAYFNTHPGfETMAAVGCDPEVCWTDWYYKMREKAHTWDYDYTGFDGSIPSCSFDALADLLcEFVENE 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2224 PRVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQ-HPDFSPSQFQILAYGDDVIYATEPPI 2302
Cdd:cd23222    248 DDVRRYISNIKNSYHAYDGNLYLIEGAMPSGCAGTSVFNCLINAMLCFSCFMDlEPEMDPFEPLLIAYGDDILVSSDHDL 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2303 HPSFLRDFYQKYTPLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDIRPVyIHPVMDPDTYEQSVMWLRDGDFQDVVTSL 2382
Cdd:cd23222    328 FPSRVSEWMKANTTFKITPADKGEIFNDDSDVSDVRFLKRLFVEDPVCEL-IHPVIETETLEPSLNWCHEGEFETKVDAI 406
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1752309242 2383 CHLAFHSGPKTYERWCTKVREQCLKTGFA-PTFLPYSYLQLRWL 2425
Cdd:cd23222    407 SMLAFHHGPEYYRDWCKKLTDICEERNISpPGLKPYSVHRNRWL 450
Rosavirus_RdRp cd23221
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Rosavirus of ...
2057-2425 1.48e-110

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Rosavirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Rosavirus genus within the family Picornaviridae, order Picornavirales. The Rosavirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. This genus contains three species Rosavirus A, Rosavirus B and Rosavirus C found in rats. The name rosavirus is derived from rodent stool-associated picornavirus. Viral RNA was detected in fecal samples of humans and rodents [canyon mouse (Peromyscus crinitus), brown rat (Rattus norvegicus), black rat (R. rattus), Sikkim rat (R. andamanensis), chestnut white-bellied rat (Niviventer fulvescens)]. Eight genetic types are distinguished by means of phylogenetic analysis (Rosavirus A: 2 types; Rosavirus B: 2 types; Rosavirus C: 4 types). RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438071  Cd Length: 381  Bit Score: 358.08  E-value: 1.48e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2057 AIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDEPEpGFYTPRPELQILIDQTLENPDY-VYSTFLKDELRPTAKVQDGL 2135
Cdd:cd23221      1 AINGIDNMDGLDMNQSPGVPYVSEGVSRRSLFDCVD-GQWVPRERLASDIAQVSGDPSLgHFATFLKDELRSTEKVAAGK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2136 TRIVEAAPIHAIIAGRMLLGGLIDYMQGRPG-EHGCAVGCNPDIHWTEFFYKFADFSQVYDLDYKCFDATLPSAAFTLVA 2214
Cdd:cd23221     80 TRVVEAGSLPHIIVGRKIFGNLFALFNSNPGfQTMCAVGCDPDVTWTELYHPLSAKTYVFDYDYSGFDGSVPSCCFDALA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2215 ERL-ERLTGDPRVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQ-HPDFSPSQFQILAYGD 2292
Cdd:cd23221    160 DLLaDFVEGEEDVRKYISSLKTSFHHYKGKLWRLDGAMPSGCCGTSVFNSLINAMLLFSAFSQiCPDFRASEPLLVAYGD 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2293 DVIYATEPPIHPSFLRDFYQKYTPLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDIRPVYIHPVMDPDTYEQSVMWLRD 2372
Cdd:cd23221    240 DVLVGTDQPLFPSKVAEWVNSHTTFRITPADKGSVFNDESDIHSVQFLKRHFTPDPDFPALIHPTIDPDTYEQSVMWQRT 319
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1752309242 2373 GDFQDVVTSLCHLAFHSGPKTYERWCTKVREQCLKTGFAPTFL-PYSYLQLRWL 2425
Cdd:cd23221    320 GDFQETVNSLALLVFHRGPKSYSRWCESVTRKCVDGGYPPPFFpPFSLLRHQWL 373
Mosavirus_RdRp cd23225
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Mosavirus of ...
2056-2425 8.06e-87

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Mosavirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Mosavirus genus within the family Picornaviridae, order Picornavirales. The Mosavirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. This genus includes two species: Mosavirus A, which found in the feces of a canyon mouse (Peromyscus crinitus), and Mosavirus B, which contains marmot mosavirus. Mosavirus stands for mouse stool-associated picornavirus. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438075  Cd Length: 378  Bit Score: 289.51  E-value: 8.06e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2056 QAIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFD---EPEPGFYTPRPELQILIDQTL---ENPDYVysTFLKDELRPTA 2129
Cdd:cd23225      1 RAMNGDGISDAMDMTKAVGYPYCLDSIKRLDLVEikeTENGKVYLPTERLVEETEKFFtgeEKPKFV--TFLKDEVRSNE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2130 KVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPG-EHGCAVGCNPDIHWTEFFYKFADfSQVYDLDYKCFDATLPSA 2208
Cdd:cd23225     79 KIKQGKTRIVDASPFPYAIAGRMVMQNFMSNMMRCNGtEVGSAVGCDPDTEWTRYFFELCD-RYVFDLDYKAFDSTHPTA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2209 AFTLVAER--LERLTGDPRVAK-YIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQHPDFSPSQF 2285
Cdd:cd23225    158 MFNLLAERffTERNGFDQQAVRiFLNGLSDSDHVYEGKHFRIRGGLPSGCPCTSILNTVINNIIVRAAILGAYQIDTVDF 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2286 Q---ILAYGDDVIYATEPPIHPSFLRDFYQKYTPLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDIRPVYIHPVMDPDT 2362
Cdd:cd23225    238 QkfrMLAYGDDVVYATPQPIKPQDLADWLHANTNYKVTPASKAGTFPEESTIWDVTFLKRSFKPDEDHGHLIRPVMAVGN 317
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752309242 2363 YEQSVMWLRDGDFQDVVTSLCHLAFHSGPKTYERWCTKVReqclktGFAPTF-LP-YSYLQLRWL 2425
Cdd:cd23225    318 LKQMLSFMRPGTFPDKVRSVAGLAVHCGEEDYNQLADAVA------LYVPGVsMPaYKYMKACWY 376
Enterovirus_RdRp cd23213
RNA-dependent RNA polymerase (RdRp) in the Enterovirus genus of positive-sense single-stranded ...
1979-2426 3.24e-84

RNA-dependent RNA polymerase (RdRp) in the Enterovirus genus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Enterovirus genus within the family Picornaviridae, order Picornavirales. Enteroviruses have small, non-enveloped (+)ssRNA genomes, and replicate within the gastrointestinal tract or other mucosal surfaces. The genus Enterovirus has been divided into 15 species based on genetic divergence (EV A-L and Rhinovirus A-C), and its major members include poliovirus, coxsackievirus and rhinovirus. More than 100 enterovirus types have been associated with several human diseases, all of which are classified into four species (Enterovirus A, Enterovirus B, Enterovirus C, and Enterovirus D). RdRps are multi-domain proteins that play a pivotal role in enterovirus replication. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of enteroviruses. 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: 438063  Cd Length: 453  Bit Score: 284.80  E-value: 3.24e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1979 PGVNINRMSRLKP------FPIKKEPAPLKRNDRRLNdgVDLDTQLFLKHGKGDQSEPWPGLEAAADLYFSTFpSSLPVL 2052
Cdd:cd23213      7 PNINAPTKTKLEPsvfhdvFEGNKEPAVLTSKDPRLK--VDFEEAIFSKYVGNTITEVDEYMKEAVDHYAGQL-ATLDID 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2053 TQ----EQAIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDEpepgfyTPR--PELQILIDQTleNPDYVYSTFLKDELR 2126
Cdd:cd23213     84 TEqmslEDAMYGTDGLEALDLHTSAGYPYVALGIKKRDILNK------KTRdtSKMKKYLDKY--GLDLPMVTYVKDELR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2127 PTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGE-HGCAVGCNPDIHWTEFFYKFADfsQVYDLDYKCFDATL 2205
Cdd:cd23213    156 SKDKVEKGKSRLIEASSLNDSVAMRMTFGNLYATFHLNPGVvTGSAVGCDPDTFWSKIPILLDG--SLFAFDYTGYDASL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2206 PSAAFTLVAERLERLTGDPRVAkYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALI---QHPDFsp 2282
Cdd:cd23213    234 SPVWFRALKMVLEKGYSEEAVS-LIDYLNHSHHLYKNKTYCVLGGMPSGCSGTSIFNSMINNIIIRTLLLktyKGIDL-- 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2283 SQFQILAYGDDVIYATEPPIHPSFLRDFYQKYTpLVVTPANKGSDFPDTsTIHEVTFLKRWFVPDDIRPVYIHPVMDPDT 2362
Cdd:cd23213    311 DELKMIAYGDDVIASYPHPIDCSLLARTGKEYG-LTMTPADKSPCFNEV-NWENVTFLKRGFRADEQYPFLIHPVMPMKE 388
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752309242 2363 YEQSVMWLRDG-DFQDVVTSLCHLAFHSGPKTYERWCTKVREqcLKTGFAPTFLPYSYLQLRWLN 2426
Cdd:cd23213    389 IHESIRWTKDPrNTQDHVRSLCLLAWHNGEEEYEKFVSKIRS--VPVGRALALPNYSTLRRNWLD 451
Aphthovirus_RdRp cd23210
RNA-dependent RNA polymerase (RdRp) in the Aphthovirus genus of positive-sense single-stranded ...
1981-2426 1.41e-83

RNA-dependent RNA polymerase (RdRp) in the Aphthovirus genus of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the Aphthovirus genus within the family Picornaviridae, order Picornavirales. Member viruses have a (+)ssRNA genome. This genus includes species such as bovine rhinitis A virus, bovine rhinitis B virus, equine rhinitis A virus, and food-and-mouth disease virus (FMDV). Aphthoviruses primarily infect via the upper respiratory tract. FMDV infects mainly cloven-hoofed animals, but has been isolated from at least 70 species of mammals. Aphthoviruses are non-enveloped and have an icosahedral capsid with a diameter of around 27 to 30 nm. The assembled viral capsid contains a single copy of the RNA genome and 60 copies of the four viral capsid proteins VP1, VP2, VP3, and VP4. 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: 438060  Cd Length: 458  Bit Score: 283.38  E-value: 1.41e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1981 VNINRMSRLKP---FPIKKE---PAPLKRNDRRLNDGVDLDTQLFLKHgKGDQ---SEPWPGLEAAADLY----FSTFPS 2047
Cdd:cd23210      6 VHVMRKTKLAPtvaHGVFNPefgPAALSNKDPRLNEGVVLDEVIFSKH-KGDTkmsAEDKALFRRCAADYasrlHSVLGT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2048 SLPVLTQEQAIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDEpEPGFYTPRPELQILIDQTLENpDYVYSTFLKDELRP 2127
Cdd:cd23210     85 ANAPLSIYEAIKGVDGLDAMEPDTAPGLPWALQGKRRGALIDF-ENGTVGPEVEAALKLMEKREY-KFACQTFLKDEIRP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2128 TAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPG-EHGCAVGCNPDIHWTEFFYKFADFSQVYDLDYKCFDATLP 2206
Cdd:cd23210    163 MEKVRAGKTRIVDVLPVEHILYTRMMIGRFCAQMHSNNGpQIGSAVGCNPDVDWQRFGTHFAQYRNVWDVDYSAFDANHC 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2207 SAAFTLVAERL--ERLTGDPRVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQH-PDFSPS 2283
Cdd:cd23210    243 SDAMNIMFEEVfrTEFGFHPNAEWILKTLVNTEHAYENKRITVEGGMPSGCSATSIINTILNNIYVLYALRRHyEGVELD 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2284 QFQILAYGDDVIYATEPPIhpsflrDFyQKYTPL------VVTPANKGSDFPDTS-TIHEVTFLKRWFVPDDIRPVYiHP 2356
Cdd:cd23210    323 TYTMISYGDDIVVASDYDL------DF-EALKPHfkslgqTITPADKSDKGFVLGhSITDVTFLKRHFHMDYGTGFY-KP 394
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752309242 2357 VMDPDTYEQSVMWLRDGDFQDVVTSLCHLAFHSGPKTYERwctkvreqcLKTGFAPTFLPYSY--LQLRWLN 2426
Cdd:cd23210    395 VMASKTLEAILSFARRGTIQEKLISVAGLAVHSGPDEYRR---------LFEPFQGLFEIPSYrsLYLRWVN 457
Mischivirus_RdRp cd23227
RNA-dependent RNA polymerase (RdRp) in the genus Mischivirus of positive-sense single-stranded ...
1972-2424 1.53e-82

RNA-dependent RNA polymerase (RdRp) in the genus Mischivirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Mischivirus genus within the family Picornaviridae, order Picornavirales. The Mischivirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. Mischivirus is a picornavirus genus containing five species Mischivirus A, Mischivirus B, Mischivirus C, Mischivirus D and the proposed Mischivirus E. The name is derived from the name originally given to the virus, Miniopterus schreibersii picornavirus, which was found in the common bent-wing bat (aka Schreiber's long-fingered bat or Schreiber's bat) in China and is most closely related to the cardioviruses. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438077  Cd Length: 466  Bit Score: 280.68  E-value: 1.53e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1972 IPTGeikPGVNINRMSRLK---PFPIKKE---PAPLKRNDRRLNDGVDLDTQLFLKHgKGDQSEpWPG-----LEAAADL 2040
Cdd:cd23227      6 LPDG---PRIHVPRKTKLRkspAYPIFKPdagPAVLSKNDPRLAEGVDFDKQVFSKH-SANQKE-YPKafrrmARWYADR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2041 YFSTFPSSLPVLTQEQAIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDEPEPGFYTP--RPELQILIDQTLEnpDYVYS 2118
Cdd:cd23227     81 VFTYLGKDNGPLSVKDAIKGIDNLDAMDPTTSPGLPYSAAGIKRTDLLDFDTGEIISPalRAEYNKYVSGDYS--DHVFQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2119 TFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPG-EHGCAVGCNPDIHWTEFFYKFADFSQVYDLD 2197
Cdd:cd23227    159 TFLKDEIRSEEKIKAGKTRIVDVPSLAHVIIGRVLLGKFCSKFQASPGtELGSAIGCNPDWDWTYFAHQLMERQWCYDID 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2198 YKCFDATLPSAAFTLVAERL--ERLTGDPRVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSAL- 2274
Cdd:cd23227    239 YSNFDSTHGTGMFELLIDCFftPENGFSPAVAPYLRSLAFSKHAWMDKRYKIEGGLPSGCSATSVLNTVMNNIIIRALLs 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2275 IQHPDFSPSQFQILAYGDDVIYATEPPIHPSFLRDFYQKYTPLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDIRPVYI 2354
Cdd:cd23227    319 LTYKNFHPEDVLVLAYGDDLLVASDYQLDFNRVREKAAEHTLYKLTTANKAPDFPETSTLLDCQFLKRKFVLHSTRNFIW 398
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2355 HPVMDPDTYEQSVMWLRDGDFQDVVTSLCHLAFHSGPKTYERWCTKVREQCLKTgfaPTFLpysYLQLRW 2424
Cdd:cd23227    399 RPVMDVTNLKTMLSFYKPNTLSEKLLSVAQLAFHSGYTVYEELFAPFKELQMTV---PSWW---YLEHEW 462
Cardiovirus_RdRp cd23211
RNA-dependent RNA polymerase (RdRp) in the Cardiovirus genus of positive-sense single-stranded ...
1972-2427 1.91e-80

RNA-dependent RNA polymerase (RdRp) in the Cardiovirus genus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Cardiovirus genus within the family Picornaviridae, order Picornavirales. Member viruses have a (+)ssRNA genome. Vertebrates serve as natural hosts for the cardioviruses. There are currently six species in the genus: Cardiovirus A-F. Diseases associated with cardioviruses include: myocarditis, encephalitis, multiple sclerosis, and type 1 diabetes. Cardiovirus A is composed of only one serotype, encephalomycarditis virus (EMCV) which causes encephalomyocarditis and reproductive disease in pigs. Cardiovirus B comprises 15 genetic types, Theiler's murine encephalomyelitis virus (TMEV), Vilyuisk human encephalomyelitis virus (VHEV), thera virus (formerly named Theiler-like virus of rats), Saffold virus (SAFV) types 1 to 11, and genet fecal theilovirus (from Geneta geneta). Of these types, only VHEV and SAFV are thought to cause infection in humans. Thus far, Cardiovirus C has only been observed in the brown rat. 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: 438061  Cd Length: 460  Bit Score: 274.03  E-value: 1.91e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1972 IPTGEIkpgVNINRMSRLKP------FPIKKEPAPLKRNDRRLNDgvDLDTQLFLKHGKGDQSEPwPGLEAAADLY---- 2041
Cdd:cd23211      6 IGTGPV---VHVPRKTKLRRtvahpvFQPKFEPAVLSKYDPRTDK--DVDEVAFSKHTTNQESLP-PVFRMVAKEYanrv 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2042 FSTFPSSLPVLTQEQAIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDEPEPGFytpRPELQILIDQtLENPDY---VYS 2118
Cdd:cd23211     80 FTLLGKDNGRLTVEQAVLGLEGMDPMEKDTSPGLPYTQQGLRRTDVVDFETATM---IPFLAEAHRK-MVEGDYsdvVYQ 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2119 TFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPG-EHGCAVGCNPDIHWTEFFYKFADFSQVYDLD 2197
Cdd:cd23211    156 SFLKDEIRPIEKVQAAKTRIVDVPPFEHCILGRQLLGRFASKFQTNPGlELGSAIGCDPDVDWTAFAVALSGFKYVYDVD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2198 YKCFDATLPSAAFTLVAERL--ERLTGDPRVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSAL- 2274
Cdd:cd23211    236 YSNFDSTHSTAMFELLIENFftEENGFDPRIGEYLRSLAVSRHAYEERRVLIRGGLPSGCAATSMLNTIMNNIIIRAGLy 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2275 IQHPDFSPSQFQILAYGDDVIYATEPPIHPSFLRDFYQKyTPLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDirPVYI 2354
Cdd:cd23211    316 LTYKNFEFDDIKVLSYGDDLLVATNYQIDFNLVKARLAK-FGYKITPANKTSTFPLTSTLEDVVFLKRKFVKEN--SYLY 392
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752309242 2355 HPVMDPDTYEQSVMWLRDGDFQDVVTSLCHLAFHSGPKTYERWCTKVREQCLktgFAPTflpYSYLQLRWLNM 2427
Cdd:cd23211    393 RPVMDRENLKAMLSYYRPGTLKEKLTSIALLAVHSGKQVYDEIFAPFREVGI---VVPT---YESVLYRWLSL 459
Cosavirus_RdRp cd23226
RNA-dependent RNA polymerase (RdRp) in the genus Cosavirus of positive-sense single-stranded ...
1979-2428 3.37e-77

RNA-dependent RNA polymerase (RdRp) in the genus Cosavirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Cosavirus genus within the family Picornaviridae, order Picornavirales. The Cosavirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. This genus consists of five species Cosavirus A, Cosavirus B, Cosavirus D, Cosavirus E and Cosavirus F. The candidate species, Cosavirus C, remains unclassified due to a lack of full genome sequence data. Cosaviruses (formerly called Dekaviruses) have been identified in the stools of south Asian children. Cosaviruses are most closely related to members of the Cardiovirus and Senecavirus genera, but they lack a leader polypeptide. The name Cosavirus stands for common stool-associated picornavirus. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438076  Cd Length: 461  Bit Score: 264.96  E-value: 3.37e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1979 PGVNINRMSRLK------PFPIKKEPAPLKRNDRRLNDGVDLDTQLFLKHGKG----DQSEPWPGLEAAADLYFSTFPS- 2047
Cdd:cd23226     10 PRVHVPRQSKLKrtnatyPATGKYGPAVLSKNDPRLDPDVDFDKVIFSKHVANvvidEDTSFWNALKMSAQIYAEKFKGv 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2048 SLPVLTQEQAIHGTPNMEGLDMGQAAGFPWNtqgRSRRSLFDepepgFYTPR---PELQILIDQTLEN--PDYVYSTFLK 2122
Cdd:cd23226     90 DFSPLTVEEAILGIPGLDRMDPNTASGLPYT---KTRRQMID-----FQEGKildPELQERLDTWLSGkqPEMLYQTFLK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2123 DELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPG-EHGCAVGCNPDIHWTEFFYKFADFSQVYDLDYKCF 2201
Cdd:cd23226    162 DEIRPIEKVKAGKTRIIDVTPLDHVLAFRIVLGRFMAHFHNNYGfELGSAVGCDPDVAWANFGFALSSKKYQYDFDYSNF 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2202 DATLPSAAFTLVAERL--ERLTGDPRVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQ-HP 2278
Cdd:cd23226    242 DASHSESIFELLKQFVftKDNGFDHRCSLMIDSLVTSTHCYEDQRMTIRGGLPSGTSGTSVINTIINNIIFKAALYHtYS 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2279 DFSPSQFQILAYGDDVIYATEPPIHPSFLRDFyQKYTPLVVTPANKGSDFPdTSTIHEVTFLKRWFVpdDIRPVYIhPVM 2358
Cdd:cd23226    322 NFEWDDVQMLAYGDDIVAASDCLLDLDRVKYF-MALIGYKITPADKGEKFI-PKDMQNIQFLKRSFR--KVAGVWA-PIM 396
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2359 DPDTYEQSVMWLRDGDFQDVVTSLCHLAFHSGPKTYErwctKVREQCLKTGFapTFLPYSYLQLRWLNML 2428
Cdd:cd23226    397 DLENLQAMLSWYKPGTLQEKLDSVARLAHFCGEKVYD----HLFTTFVKDGF--QIKPWKQLHFEWLNRF 460
Sapelovirus_RdRp cd23218
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Sapelovirus of ...
2058-2428 1.59e-76

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Sapelovirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Sapelovirus genus within the family Picornaviridae, order Picornavirales. Member viruses have a (+)ssRNA genome. Viruses in Sapelovirus are non-enveloped, with icosahedral, spherical, and round geometries, and T=pseudo3 symmetry. Sapelovirus, formerly known as porcine enterovirus (PEV)-8, is known to infect pigs asymptomatically but can cause reproductive failure and severe neurologic, enteric, or respiratory signs. Sapelovirus infections have been reported worldwide in pigs. The genus Sapelovirus contains three species, with a unique genome organization: Sapelovirus A, also known as porcine sapelovirus (PSV); Sapelovirus B as simian sapelovirus; and Avian sapelovirus represented by duck picornavirus. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438068  Cd Length: 366  Bit Score: 259.45  E-value: 1.59e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2058 IHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFdePEPGfyTPRPELQILIDqtLENPDYVYSTFLKDELRPTAKVQDGLTR 2137
Cdd:cd23218      3 VYGIDNLEGLDLNTSAGYPYNTMGIRKKDLI--PPRG--EPLSPLLKALD--LHGYDLPFTTYLKDELRPKEKVKMGKTR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2138 IVEAAPIHAIIAGRMLLGGLIDYMQGRPGEH-GCAVGCNPDIHWTEFfYKFADFSQVYDLDYKCFDATLPSAAFTLVAER 2216
Cdd:cd23218     77 LIECSSLNDTIRMKRIFGRLFQTFHKNPGTYtGSAVGCNPDVHWSKF-AEEGGMDNVCAFDYTNWDASLSPFWFDALKLF 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2217 LERLTGDPRVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQ-HPDFSPSQFQILAYGDDVI 2295
Cdd:cd23218    156 LSKLGYSERDIVLIDHLCYSNHIFKNEGYKVAGGMPSGCSGTSIFNSIINNIVVRTLVLLvYKGINLDELRILCYGDDLL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2296 YATEPPIHPSFLRDFYQKYTpLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDIRPVYIHPVMDPDTYEQSVMWLRDGDF 2375
Cdd:cd23218    236 VAYPYPLDPNVLADLGKSLG-LTMTPADKSDTFQGCTKLTEVTFLKRSFVFDEEFPFLCHPVFPMEEVHESIRWTRNAST 314
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1752309242 2376 -QDVVTSLCHLAFHSGPKTYERWCTKVREqcLKTGFAPTFLPYSYLQLRWLNML 2428
Cdd:cd23218    315 tQEHVTSLCLLAWHNGEEVYEEFCEKIRS--VPVGRALILPPYSQLRRSWLDMF 366
Rabovirus_RdRp cd23230
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Rabovirus of ...
2057-2426 3.70e-71

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Rabovirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Rabovirus genus within the family Picornaviridae, order Picornavirales. The Rabovirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. The genus Rabovirus consists of four species Rabovirus A, Rabovirus B, Rabovirus C, and Rabovirus D. Viral RNA of this genus was detected in feces of Norway rats (Rattus norvegicus) and mice (Mus musculus) in USA and Germany, in intestinal contents of Himalayan marmots (Marmota himalayana), and in tissue samples of Gairdner's shrewmice (Mus pahari). RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438080  Cd Length: 361  Bit Score: 243.64  E-value: 3.70e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2057 AIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDePEPGFYTprpELQILIDQTleNPDYVYSTFLKDELRPTAKVQDGLT 2136
Cdd:cd23230      1 AAYGIENLEGLDLNTSAGYPYVLNGIKKRDILD-PETRDTT---KLQECLDKY--GVDLPFVTYLKDELRPLEKIKKGKT 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2137 RIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEH-GCAVGCNPDIHWTEFFYKFADfsQVYDLDYKCFDATLPSAAFTLVAE 2215
Cdd:cd23230     75 RLIECSSMNDTIRMKMMFGRLFATYHRNPGPItGSAVGCNPDIHWTKFRAEMHG--EIIAFDYSNYDASLNKVWFECLKM 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2216 RLERLtGDPRVAKYIHSIRhSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQ-HPDFSPSQFQILAYGDDV 2294
Cdd:cd23230    153 VLKNF-GFKDLRPIDHIIR-SRHIYKGIEYDVEGGMPSGCSGTSIFNSIINNIIIMTLVLDaYKGIDLEQLKIIAYGDDV 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2295 IYATEPPIHPSFLRDFYQKYTpLVVTPANKGSDFpDTSTIHEVTFLKRWFVPDDIRPVYIHPVMDPDTYEQSVMWLRD-G 2373
Cdd:cd23230    231 IVTYPYPLDAALLADCGKKYG-LKMTPPDKSAEF-KNVTWEDVTFLKRRFKPAKHYPFLIHPVFDQQEILESLRWTRNpA 308
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1752309242 2374 DFQDVVTSLCHLAFHSGPKTYERWCTKVREQclKTGFAPTFLPYSYLQLRWLN 2426
Cdd:cd23230    309 HTQEHVRSLAELAWHSGRKSYEEFCNLVKST--NVGKACILPPYESFKRMWLD 359
RNA_dep_RNAP cd01699
RNA_dep_RNAP: RNA-dependent RNA polymerase (RdRp) is an essential protein encoded in the ...
2099-2370 2.77e-67

RNA_dep_RNAP: RNA-dependent RNA polymerase (RdRp) is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage. RdRp catalyzes synthesis of the RNA strand complementary to a given RNA template. RdRps of many viruses are products of processing of polyproteins. Some RdRps consist of one polypeptide chain, and others are complexes of several subunits. The domain organization and the 3D structure of the catalytic center of a wide range of RdRps, including those with a low overall sequence homology, are conserved. The catalytic center is formed by several motifs containing a number of conserved amino acid residues. This subfamily represents the RNA-dependent RNA polymerases from all positive-strand RNA eukaryotic viruses with no DNA stage.


Pssm-ID: 238843 [Multi-domain]  Cd Length: 278  Bit Score: 229.48  E-value: 2.77e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2099 RPELQILIDQTLENPDYVYSTFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCNPD- 2177
Cdd:cd01699      2 EKAVESLEDLPLIRPDLVFTTFLKDELRPLEKVEAGKTRLIQPRPLDYNIALRMYLGPFEAKLMKNRGGLPIAVGINPYs 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2178 IHWTEFFYKFADFSQV-YDLDYKCFDATLPSAAFTLVAERLERLTGDPRVA---KYIHSIRHS-HHVYGNRTYDMIGGNP 2252
Cdd:cd01699     82 RDWTILANKLRSFSPVaIALDYSRFDSSLSPQLLEAEHSIYNALYDDDDELerrNLLRSLTNNsLHIGFNEVYKVRGGRP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2253 SGCVATSILNTIINNICVLSALIQH-PDFSPSQFQILAYGDDVIYATEP---PIHPSFLRDFYQKYTpLVVTPANKgsDF 2328
Cdd:cd01699    162 SGDPLTSIGNSIINCILVRYAFRKLgGKSFFKNVRLLNYGDDCLLSVEKaddKFNLETLAEWLKEYG-LTMTDEDK--VE 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1752309242 2329 PDTSTIHEVTFLKRWFVPDDIRpvYIHPVMDPDTYEQSVMWL 2370
Cdd:cd01699    239 SPFRPLEEVEFLKRRFVLDEGG--GWRAPLDPSSILSKLSWS 278
ps-ssRNAv-Picornavirales cd23169
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Picornavirales of ...
2116-2402 1.00e-62

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Picornavirales of positive-sense single-stranded RNA [(+)ssRNA] viruses; This family contains the catalytic core domain of RdRp of Picornavirales, an order of (+)ssRNA viruses. The order Picornavirales comprises viruses that historically are referred to as picorna-like viruses and which are classified into eight virus families: Caliciviridae, Dicistroviridae, Iflaviridae, Marnaviridae, Picornaviridae, Polycipiviridae, Secoviridae, and Solinviviridae. All known genomes of Picornavirales members encode proteins with helicase, 3C-like protease, and RdRp domains, as well as capsid proteins with related structures, although the genome organizations can differ among viruses. The picornavirus genome is replicated via a negative-sense (-) RNA intermediate by the viral RdRp, named 3Dpol, which uses VPg (the product of 3B) as a primer to initiate the replication process. 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: 438019  Cd Length: 309  Bit Score: 217.46  E-value: 1.00e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2116 VYSTFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCNPDIH-WTEFFYKFA-DFSQV 2193
Cdd:cd23169      2 IFVDCLKDELRPIEKVKAGKTRLFSASPLDYTIAFRKYFGDFIAAFQKNRIKLEHAVGINPDSVeWTRLYRRLLkKGPNI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2194 YDLDYKCFDATLPSAAFTLVAERLERLT------GDPRVAK-YIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIIN 2266
Cdd:cd23169     82 FAGDYSNFDGSLPPDVMEAAFDIINDWYdeyvddEDERVRKvLFEELINTIHLVGNLVYQVHGGNPSGNPLTTIINSIVN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2267 NI---CVLSALIQHPDFSP--SQFQILAYGDDVIYATEPPIHPSF----LRDFYQKYTpLVVTPANKGSDFPDTSTIHEV 2337
Cdd:cd23169    162 LLyirYAWLRITGLTSLSDfkKNVRLVTYGDDVIISVSDEVKDEFnfvtISEFLKELG-ITYTDADKSGDIVPYRPLEEV 240
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752309242 2338 TFLKRWFVPDDIrPVYIHPVMDPDTYEQSVMWLRDGdfQDVVTSLCH-------LAFHSGPKTYERWCTKVR 2402
Cdd:cd23169    241 TFLKRGFRPHPT-PGLVLAPLDLESIEEQLNWTRKE--DDLLEATIEnaraallLAFGHGPEYYNKFRQKLN 309
Teschovirus_RdRp cd23212
RNA-dependent RNA polymerase (RdRp) in the Teschovirus genus of positive-sense single-stranded ...
2046-2396 2.55e-55

RNA-dependent RNA polymerase (RdRp) in the Teschovirus genus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Teschovirus genus within the family Picornaviridae, order Picornavirales. Member viruses have a (+)ssRNA genome. Teschoviruses are emerging pathogens and infect the porcine population only. There are two species in this genus, including Teschovirus A (previously Porcine teschovirus), which is responsible for the porcine enteroviral encephalomyelitis disease caused in pigs, and Teschovirus B. Teschovirus is also known by several other names including Teschen disease, Talfan disease, poliomyelitis suum, benign enzootic paresis, Klobauk disease and contagious porcine paralysis. Teschovirus has a single-stranded, linear, non-segmented RNA genome. The RNA genome is positively sensed meaning that it has the same polarity as the mRNA and no reverse transcription is necessary. 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: 438062  Cd Length: 354  Bit Score: 197.53  E-value: 2.55e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2046 PSSLPVLTQEQAIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDePEPGfytPRPELQILIDQTLE-NPD-YVYSTFLKD 2123
Cdd:cd23212      5 PDFLEPLSVREAVEGIDGLDPMDMDKSPGLPYVKKGLRRTDLWN-PKTG---PSIELMAEINRYLDyNYDkHVFLTFLKD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2124 ELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEH-GCAVGCNPDIHWTEFFYKfADFSQVYDLDYKCFD 2202
Cdd:cd23212     81 ELRPKEKVQAGKTRVIDVAGFGHAIVGRMLFGRLFAFFHKNPGWNtGSAVGVNPDLAWTQIFYT-APSRNVLAMDYSGFD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2203 ATLPSAAFTLVAERLERLTGDPRVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQHPDfsp 2282
Cdd:cd23212    160 ASHTSGMFCILKHFLTTLGYGTLQLSYIDSLCYSKHHWDDETYRLDGGLPSGCSGTTIFNTIMNNIVARAAASYAAE--- 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2283 SQFQILAYGDDVIYATEPPIHPSFLRDFYQKyTPLVVTPANKGSDFpDTSTIHEVTFLKRWFVPDDirpVYIHPVMDPDT 2362
Cdd:cd23212    237 GPVGILCYGDDILVSSPEKFPVSDWLEFYSK-TPYKVTAADKSEQI-DWRDITQCTFLKRGFVLDG---SLVRPVMEEQH 311
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1752309242 2363 YEQSVMWLRDGDFQDVVTSLCHLAFHSGPKTYER 2396
Cdd:cd23212    312 LAELLKWARPGTLQAKLLSIAQLAFHLPRQAYDR 345
RdRP_1 pfam00680
Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase ...
1991-2396 4.10e-54

Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase found in many positive strand RNA eukaryotic viruses. Structural studies indicate that these proteins form the "right hand" structure found in all oligonucleotide polymerases, containing thumb, finger and palm domains, and also the additional bridging finger and thumb domains unique to RNA-directed RNA polymerases.


Pssm-ID: 425815  Cd Length: 450  Bit Score: 197.25  E-value: 4.10e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1991 PFPIKKEPAPLKRND-----RRLNDGVDLDTQLFLKHGKGDQSEPWPG---LEAAADLYFSTF----PSSLPVLTQEQAI 2058
Cdd:pfam00680    8 VAIPAYVPASLGPEDprwarSYLNTDPYVDDIKKYSRPKLPGPADERDkllNRSAAKMVLSELrgvpKKANSTLIVYRAI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2059 HGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDE----PEPGFYTPRPELQILIDQTLENPDYVYSTFLKDELRPTAKVQDG 2134
Cdd:pfam00680   88 DGVEQIDPLNWDTSAGYPYVGLGGKKGDLIEHlkdgTEARELAERLAADWEVLQNGTPLKLVYQTCLKDELRPLEKVEKG 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2135 LTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCNPDI-HWTEFFYKFADFSQ-VYDLDYKCFDATLPSAAFTL 2212
Cdd:pfam00680  168 KTRLVWGEPVEYLLLERAFFDPFNQAFMLNNGFHPIQVGINPFDrGWPRLLRRLARFGDyVYELDYSGFDSSVPPWLIRF 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2213 VAERLERLTGDP-------RVAKYIhsIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALI-----QHPD- 2279
Cdd:pfam00680  248 AFEILRELLGFPsnvkewrAILELL--IYTPIALPNGTVFKKTGGLPSGSPFTSIINSIVNYLLILYALLkslenDGPRv 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2280 -FSPSQFQILAYGDDVIYATEPPIHPSF------LRDFYQKYtplvvTPANKgsDFPDTSTIHEVTFLKRWFVPDDIRpv 2352
Cdd:pfam00680  326 cNLDKYFDFFTYGDDSLVAVSPDFDPVLdrlsphLKELGLTI-----TPAKK--TFPVSRELEEVSFLKRTFRKTPGG-- 396
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1752309242 2353 yIHPVMDPDTYEQSVMWLRDGD-FQDVVTSLCHLAFHSGPKTYER 2396
Cdd:pfam00680  397 -YRPPLDRKRILAQLEYIRSKPvPSGQLENIRAYASHHGYEFYRD 440
Fipivirus_RdRp cd23229
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Fipivirus of ...
2058-2403 1.94e-52

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Fipivirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Fipivirus genus within the family Picornaviridae, order Picornavirales. The Fipivirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. This genus contains five species: Fipivirus A (Wuhan sharpbelly picornavirus 2), Fipivirus B (Wuhan sharpbelly picornavirus 3), Fipivirus C (Wenling crossorhombus picornavirus), Fipivirus D (Wenling jack mackerels picornavirus) and Fipivirus E (Wenling banjofish picornavirus 1). All contain viruses from fish. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438079  Cd Length: 394  Bit Score: 190.79  E-value: 1.94e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2058 IHGTPNMEGLDMGQAAGFPWNTQGRSRR---SLFDEPEPGFYTPRPELQILIDQTLE-----NPDYVYSTFLKDELRPTA 2129
Cdd:cd23229      2 VEGIPGMEGLDMKTSAGYPWCEQNQKKKdkiKLLAGKNFLVRPLREVVHIVVDWYIMppdmpKPEIKYVVYLKDELLSSD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2130 KVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQgrpGEH-------GCAVGCNPDIHWTEfFYKFADFSQVYDLDYKCFD 2202
Cdd:cd23229     82 KVKMGRTRWICAAPVQLVCAWKKVFGRAIAAIH---LESvtdgkstGCAVGMDPETAWTD-IALARPGWPVIALDYSNFD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2203 ATLPSAAFTLVAERLERLTGDP-----RVAKYIHsirHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQH 2277
Cdd:cd23229    158 GSLQSFVITGAVRILGYIAGLPdgqsyRLAEFVY---DVKQIVGKYLYTTVGPLPSGCPSTSIIGSLCNVLMLLYTLSHA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2278 PDFSPSQFQ----ILAYGDDVIYATEPPI--HPSFLRDFYQKYTPLVVTPANKGSDFPDTSTIHEVTFLKRWFVPDDIRP 2351
Cdd:cd23229    235 TGQRYSAFRdwmhVVTYGDDVLVFVHPEVvvVLDTLAHEMYLVFGVTATDATDKRAPPQLRELSNVTFLKRGFRQCSSVP 314
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1752309242 2352 VYIHPVMDPDTYEQSVMWLRDG-DFQDVVTSLCHLAFHSGPKTYERWCTKVRE 2403
Cdd:cd23229    315 FLVHPTMDKSTIYQMLAWKRKGtTLAENVKCAAEFMMHHGEEEYEDFVGVVKE 367
Hepatovirus_RdRp cd23215
RNA-dependent RNA polymerase (RdRp) in the genus Hepatovirus of positive-sense single-stranded ...
2052-2407 1.65e-44

RNA-dependent RNA polymerase (RdRp) in the genus Hepatovirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Hepatovirus genus within the family Picornaviridae, order Picornavirales. Hepatoviruses are 27- to 32-nm, nonenveloped, icosahedral viruses with a (+)ssRNA linear genome of approximately 7.5-kb. The Hepatovirus genus has nine species, Hepatovirus A-I, of which Hepatovirus A is responsible for a self-limiting viral hepatitis in human beings and may be transmitted by the fecal-oral route during acute infection or by the ingestion of uncooked contaminated shellfish. RdRps are multi-domain proteins that play a pivotal role in enterovirus replication. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of hepatoviruses. 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: 438065  Cd Length: 464  Bit Score: 169.64  E-value: 1.65e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2052 LTQEQAIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDEPEPGFYT---PRPELQILIDQTL-ENP---DYVYSTFLKDE 2124
Cdd:cd23215     65 FDLEQAITGVPGMDAINMDSSPGYPYVQEKLTKSDLIWLDDNGELLgmhPRLAQRILFNLTMmDNGndlDVVYTTCPKDE 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2125 LRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEH-GCAVGCNPDIHWTEFFYKFADFSQV-YDLDYKCFD 2202
Cdd:cd23215    145 LRPLEKVLESKTRAIDACPLDFTIICRMFWGPAISYFQLNPGFHtGVAVGIDPDRDWDALFKTMIRFGDYgIDLDFSSFD 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2203 ATLPSAAFTLVAERLERLTGDP--RVAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNI---CVLSALI-Q 2276
Cdd:cd23215    225 ASLSPFMIREACRVLSELSGVPdhQGQALINTIIYSKHLLYNLCYHVCGSMPSGSPCTSLLNSIVNNVnlyYVFSKIFkK 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2277 HPDFSPSQFQILAYGDDVIYATEPPIHPSFLRDFYQK----YTPLVVTPANKGSDFPDTSTIHEVTFLKRWF--VPDDIR 2350
Cdd:cd23215    305 SPVFFYDAVKFLCYGDDVLIVFSRDLEIKNLDKLGQRiqdeFKLLGMTATSADKGEPQVVPVSELTFLKRSFnlIEDRFR 384
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1752309242 2351 pvyihPVMDPDTYEQSVMWLRDG-DFQDVVTSLCHLAFHSGPKTYERWCTKVrEQCLK 2407
Cdd:cd23215    385 -----PAISEKTIWSLVAWQRSNaEFEQNLDTACWFAFMHGYDFYQNFYLQL-QSCLE 436
Dicistroviridae_RdRp cd23194
RNA-dependent RNA polymerase (RdRp) in the family Dicistroviridae of positive-sense ...
2113-2402 1.65e-43

RNA-dependent RNA polymerase (RdRp) in the family Dicistroviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the RdRp of RNA viruses belonging to the family Dicistroviridae, order Picornavirales. Dicistroviridae is a family of small non-enveloped viruses with a (+)ssRNA genome of approximately 8-10 kilobases. The family contains 3 genera: Aparavirus, Cripavirus, and Triatovirus. All members infect arthropod hosts with some having devastating economic consequences, such as acute bee paralysis virus, Kashmir bee virus, and Israeli acute paralysis virus in domesticated honeybees, and taura syndrome virus and mud crab virus in the seafood industry. On the contrary, host specificity and other desirable traits make several members of this group amenable to development as biopesticides for insect control, such as Solenopsis invicta virus 1 against fire ants, and triatoma virus against triatomine bugs that vector Chagas disease. Members in the family Dicistroviridae have similarity to viruses in the Picornavirales members (Iflaviridae, Picornaviridae, Marnaviridae and Secoviridae). The genomes of viruses of these taxa encode proteins with helicase, 3C-like protease, and RdRp domains, as well as capsid proteins with related structures, although the genome organizations can differ among viruses. 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: 438044 [Multi-domain]  Cd Length: 315  Bit Score: 162.28  E-value: 1.65e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2113 PDYVYSTFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDY-MQGRPgEHGCAVGCNP---DihWTEFFYKFA 2188
Cdd:cd23194      4 LPHVFVDTLKDERRPIEKVDAGKTRVFSAGPMDYTIAFRMYFLGFVAHlMRNRI-DNEIAVGTNVyslD--WDKLARKLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2189 DFSQ-VYDLDYKCFDATLPSAAFTLVAERLERLTGDPRVAKYI-----HSIRHSHHVYGNRTYDMIGGNPSGCVATSILN 2262
Cdd:cd23194     81 SKGDkVIAGDFSNFDGSLNPQILWAILDIINEWYDDGEENALIrrvlwEDIVNSVHICGGYVYQWTHSQPSGNPLTAIIN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2263 TIINNI----CVLSALIQHPDFSPSQFQ----ILAYGDDVIYAteppIHPSFLRDFYQKYTP-------LVVTPANKGSD 2327
Cdd:cd23194    161 SIYNSIimryVYLLLTKEAGLMTMSDFNkhvsMVSYGDDNVIN----VSDEVSEWFNQLTITeamaeigMTYTDETKTGE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2328 FPDTSTIHEVTFLKRWFVPDDIRPVYIHPvMDPDTYEQSVMWLR-----DGDFQDVV-TSLCHLAFHsGPKTYERWCTKV 2401
Cdd:cd23194    237 IVPYRSLEEVSFLKRGFRYDDDLGRWVAP-LDLDTILEMPNWVRkgkdpEEITKQNVeNALRELSLH-GEEVFDKWAPKI 314

                   .
gi 1752309242 2402 R 2402
Cdd:cd23194    315 R 315
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
1449-1551 1.02e-39

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 143.13  E-value: 1.02e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1449 VYFYGPPGTGKSLLASLLAQTLAQRLSGDPDDVYSPTAAScEYFDGYNGQSVHFIDDIGQDPEGRDWANFPNLVSSAPYI 1528
Cdd:pfam00910    1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSVYSRNPDD-DFWDGYTGQPVVIIDDFGQNPDGPDEAELIRLVSSTPYP 79
                           90       100
                   ....*....|....*....|...
gi 1752309242 1529 LPMASLEEKGIHYTSRVIVVTSN 1551
Cdd:pfam00910   80 PPMAALEEKGTPFTSKFVIVTSN 102
Parechovirus_RdRp cd23217
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Parechovirus of ...
2057-2397 7.16e-36

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Parechovirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the Parechovirus genus within the family Picornaviridae, order Picornavirales. Member viruses have a (+)ssRNA genome. The Parechovirus genus is comprised of six species, Parechovirus A (formerly named Human parechovirus), Parechovirus B (formerly named Ljungan virus), Parechovirus C (Sebokele virus) and Parechovirus D (ferret parechovirus), Parechovirus E (falcon parechovirus) and Parechovirus F (gecko parechovirus). Humans, ferrets, and various rodents serve as natural hosts. Human parechoviruses may cause gastrointestinal or respiratory illness in infants, and have been implicated in cases of myocarditis and encephalitis. Human parechoviruses replicate in the respiratory and gastrointestinal tract. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438067  Cd Length: 371  Bit Score: 141.54  E-value: 7.16e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2057 AIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFdEPEPGFYTPRPEL---QILID-QTLENPDYVYSTFLKDELRPTAKVQ 2132
Cdd:cd23217      1 AVLGTSHLNSLDLSTSPGYKYVKSGYKKRDLL-SLEPFSVSPQLEKdvkDKLHAvYKGNQPTTIFNACLKDELRKLDKIA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2133 DGLTRIVEAAPIHAIIAGRMLLGGLIDYM-QGRPGEHGCAVGCNPDIHWTEFFYKFADFSqvYDLDYKCFDATLPSAAFT 2211
Cdd:cd23217     80 QGKTRCIEACSIDYVIAYRVVMSSLYEAIyQTPCQELGLAVGMNPWTDWDFMINALNPYN--YGLDYSSYDGSLSEMLMW 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2212 LVAERLERLTGDPRVAKYIHS-IRHSHHVYGNRTYDMIGGNPSGCVATSILNTIIN-NICVLSALIQHPDFspsQFQILA 2289
Cdd:cd23217    158 EAVEVLAYCHESPDLVMQLHKpVINSDHVVMDERWLVHGGMPSGSPCTTVLNSICNlLVCIYLAYLQSPGI---ECLPIV 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2290 YGDDVIYATEPPIHPSFLRDFYQKYTPLVVTPANKgSDFPDTSTIHEVTFLKRW--FVPDDirpVYIHPVMDPDTYEQSV 2367
Cdd:cd23217    235 YGDDVIFSVSSEIDPEYLVSSAADSFGMEVTGSDK-DEPPSLLPRMEVEFLKRTtgYFPGS---TYKVGALDLETMEQHI 310
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1752309242 2368 MWLRD-GDF-QDVVTSLCHLAFHsGPKTYERW 2397
Cdd:cd23217    311 MWMKNlSTFpQQLQSFENELCLH-GKDIYDDY 341
Kunsagivirus_RdRp cd23219
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Kunsagivirus of ...
2116-2396 2.45e-33

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Kunsagivirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Kunsagivirus genus within the family Picornaviridae, order Picornavirales. The Kunsagivirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. Kunsagivirus is a new picornavirus genus containing a three species. Viral RNA of kunsagivirus A1 was detected in feces of an apparently healthy European roller (Coracias garrulus), of kunsagivirus B1 (bat kunsagivirus) in feces of the fruit bat Eidolon helvum, and of kunsagivirus C1 (bakunsavirus) in wild baboons (Papio cynocephalus). RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438069  Cd Length: 346  Bit Score: 133.45  E-value: 2.45e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2116 VYSTFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGR-PGEHGCAVGCNPdihWTEFFYKFAD-FSQV 2193
Cdd:cd23219     62 KFSSFLKDELRPLSKIRSGDTRVVECSSLDYTVAFRMQFLRVLQMCYGSdPTLTGLAPGMNV---YTDMLPLCTSlYDYN 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2194 YDLDYKCFDATLPSAAFTLVAERLERLTGDPRVA-KYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNI-CVL 2271
Cdd:cd23219    139 LCLDFSKYDSRLPLQVMHRVAQLISNLTPDPQVSmRLFQPIIISTHIVGSYEVVVEGGMPSGCPITTIMNSVCNVVmTSY 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2272 SALIQHPDfspSQFQILAYGDDVIYATEPPIHPSFLRDFYQKYTPLVVTPANKGSDFPDTSTIhEVTFLKR--WFVPDDI 2349
Cdd:cd23219    219 AMLLLDPD---SDFWPVAYGDDNIVSTRKPIDTELFCSILNEEFGMILTGADKTTTVQAVPPM-SVDFLKRrlRYTPEFP 294
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1752309242 2350 RPVyihPVMDPDTYEQSVMWLR-DGDFQDVVTSLCH-LAFHsGPKTYER 2396
Cdd:cd23219    295 LPV---PVLPLDSMLSRICWCKgETEFKDQLESFSYeLALY-GQEVYER 339
rhv_like cd00205
Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA ...
381-541 7.15e-33

Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids composed of 60 copies each of 4 virus encoded proteins; alignment includes picornaviridae, like poliovirus, hepatitis A virus, rhinovirus, foot-and-mouth disease virus and encephalomyocarditis virus; common structure is an 8-stranded beta sandwich


Pssm-ID: 119412  Cd Length: 178  Bit Score: 126.74  E-value: 7.15e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  381 FPISTATNWGVQDQQPPTAYPLPFS-FCRAYPDSPWTAMYNTHSMWNCGWRVQVTVNGSQFHAGALTLYMVPEGATESVE 459
Cdd:cd00205      9 TTVGTNNWNSSASGTQLFQWKLSPAlGFLLLQNTPLGALLSYFTYWRGDLEVTVQFNGSKFHTGRLLVAYVPPGAPAPTT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  460 AARLNAGFVFPYVILSLYESNTATLEVPFISPTPNTSSGLH------APWTFYLQVLSPLNPPTGVPTSLSCSIYVTPVD 533
Cdd:cd00205     89 GDTRWQATLNPHVIWDLGTNSSVTFVVPYVSPTPYRSTRYDgygplnSFGTLVVRVLTPLTVPSGAPTTVDITVYVRAGD 168

                   ....*...
gi 1752309242  534 STFHGLRY 541
Cdd:cd00205    169 FELYGPRP 176
Crohivirus_RdRp cd23232
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Crohivirus of ...
2055-2414 8.88e-31

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Crohivirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Crohivirus genus within the family Picornaviridae, order Picornavirales. The Crohivirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. Crohivirus is a new genus containing two species, Crohivirus A and Crohivirus B. Crohivirus A (Crohivirus 1, CroV-1) is a novel picornavirus found the lesser red musk shrew (Crocidura hirta) which is found in southern Africa. The genome sequence is most closely related to the parechoviruses. Crohivirus B consists of a virus which has been found in the straw-colored fruit bat (Eidolon helvum). RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438082  Cd Length: 373  Bit Score: 126.75  E-value: 8.88e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2055 EQAIHGTPNMEGLDMGQAAGFPWNTQGRSRRSLFDEPEpGFYTP--RPELQIL--IDQTLENPDYVYSTFLKDELRPTAK 2130
Cdd:cd23232      2 EEACFEEGDEHALDLKTSPGFKYVQMGLKKTDLVNRPN-KFIHPilRNDVRLIfdEMAKGQMPVVTFTAHLKDELRKLEK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2131 VQDGLTRIVEAAPIHAIIAGRMLLGGLIDYM-QGRPGEHGCAVGCNPDIHWTEFFYKFADFSqvYDLDYKCFDATLPSAA 2209
Cdd:cd23232     81 IRSGKTRCIEACDFDYTVAHKMMFGTLYKAIyDTPGIITGLAVGMNPWKDWELIQQSLFKYN--YDFDYKTFDGSLSREL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2210 FTLVAERLERLTGDPRVAKYI-HSIRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICVLSALIQHPDfspSQFQIL 2288
Cdd:cd23232    159 MLHAVDILSACVENDEMAKLMlSVVVESVHLVLDQKWNVSGGMPSGSPCTTVLNSVCNLIVSSTIADMCTE---GDFKIL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2289 AYGDDVIYATEPPIHPSFLRDFYQKYTPLVVTPANKGSDFpDTSTIHEVTFLKRwfVPDDIRPV-YIHPVMDPDTYEQSV 2367
Cdd:cd23232    236 VYGDDLIISSTAPLDCDRFKTLVELHYGMEVTPGDKGDEF-KVKDREQVSFLKR--VTRKFPGTnYRVGALDLDTVKQHL 312
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1752309242 2368 MWLRD-GDFQDVVTSLCHLAFHSGPKTYERWCTKVreQCLKTGF---APTF 2414
Cdd:cd23232    313 MWCKSySSFKQQLDSALMEVAMHGEETYNGFLTEI--KTKLDKFkiyPPKF 361
Caliciviridae_RdRp cd23192
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Caliciviridae of ...
2116-2398 1.16e-30

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Caliciviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Caliciviridae, order Picornavirales. Member viruses have a viral (+)ssRNA genome, which is not segmented. The family Caliciviridae, includes eleven genera: seven genera of which infect mammals (Lagovirus, Norovirus, Nebovirus, Recovirus, Sapovirus, Valovirus, and Vesivirus), two genera of which infect birds (Bavovirus, Nacovirus), and two genera of which infect fish (Minovirus and Salovirus). Each genus includes 1-2 species. Human noroviruses are a leading cause of acute gastroenteritis in humans. Furthermore, unclassified caliciviruses have been detected in geese, yellowfin seabream, greater green snake, arctic lamprey, frogs and various Australian birds, highlighting the wide host range of viruses in the family Caliciviridae. 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: 438042  Cd Length: 310  Bit Score: 124.68  E-value: 1.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2116 VYSTFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCNPDI-HWTEFFYKFADFSQVY 2194
Cdd:cd23192      2 AYALALKDELRPVEKIAEGKRRLLWGCDVGVTLVAAAAFGPVADALKAVCPTGPIAVGINMDSeDVEVIFERLSGFRYHY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2195 DLDYKCFDATLPSAAFTLVAERLERLTGDPRVAKYIHSIRHSHHV--YGNRTYDMIGGNPSGCVATSILNTIINNICVLS 2272
Cdd:cd23192     82 CLDYSKWDSTQSPAVTAAAIDILADLSEETPLRDSVVETLSSPPMgiFDDVIFVTKRGLPSGMPFTSVINSLNHWLLFSA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2273 ALIQHPD----FSPSQFQ---ILAYGDDVIYATEPPIHPSF------LRDFyqkytPLVVTPANKgSDFPDTSTIHEVTF 2339
Cdd:cd23192    162 AVLKAYElvgiYTGNVFDeadFFTYGDDGVYAMPPATASVMdeiienLKSY-----GLKPTAADK-TENPDIPPLQGPVF 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752309242 2340 LKRWFVPDDIRpvyIHPVMDPDTYEQSVMWLRDGDFQDVVTS---------------LCHLAFHSGPKTYERWC 2398
Cdd:cd23192    236 LKRTFVRTPGG---WRALLDRSSILRQLYWVKGPNTHDWTEPpteidheartvqlenVLLEAAQHGPEFYEKVL 306
rhv_like cd00205
Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA ...
591-763 3.06e-30

Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids composed of 60 copies each of 4 virus encoded proteins; alignment includes picornaviridae, like poliovirus, hepatitis A virus, rhinovirus, foot-and-mouth disease virus and encephalomyocarditis virus; common structure is an 8-stranded beta sandwich


Pssm-ID: 119412  Cd Length: 178  Bit Score: 119.04  E-value: 3.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  591 EFAQRPGIMAPFPWTmAEEPGERLGIFPVSPSA--IAGTGAPISYVLSLFSQWRGELAAHLLFTGSAQHYGRLVVCYTP- 667
Cdd:cd00205      3 SFADRPTTVGTNNWN-SSASGTQLFQWKLSPALgfLLLQNTPLGALLSYFTYWRGDLEVTVQFNGSKFHTGRLLVAYVPp 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  668 AAPAPPSN--MQEAMRGTYTVWDVNAASTLEFTIPFISQSYWKTVDIfNPDALLSTTGYVSVWVLNPLTGPQSAPASAIV 745
Cdd:cd00205     82 GAPAPTTGdtRWQATLNPHVIWDLGTNSSVTFVVPYVSPTPYRSTRY-DGYGPLNSFGTLVVRVLTPLTVPSGAPTTVDI 160
                          170
                   ....*....|....*...
gi 1752309242  746 QGFLSAGEsFNVRFMQNP 763
Cdd:cd00205    161 TVYVRAGD-FELYGPRPP 177
Limnipivirus_RdRp cd23228
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Limnipivirus of ...
2101-2404 3.66e-29

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Limnipivirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Limnipivirus genus within the family Picornaviridae, order Picornavirales. The Limnipivirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. This genus contains three species, Limnipivirus A (bluegill picornavirus 1), Limnipivirus B (carp picornavirus 1) and Limnipivirus C (fathead minnow picornavirus 1). Limnipiviruses infect freshwater fishes. The virus can be grown in various fish cell lines. Experimental infection of bluegills with bluegill picornavirus induces morbidity (inflammation and redness at the base of fins, exophthalmia, abdomen distension, internal hemorrhaging and ascites) and mortality. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438078  Cd Length: 390  Bit Score: 122.29  E-value: 3.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2101 ELQILIDQTLENPDYVYSTFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLI-DYMQGRPGEHGCAVGCNPDIH 2179
Cdd:cd23228     50 EAWEELIQSGGYPTTLFTACLKDELRSDEKVALGKTRVIEAAELDYVVAYRMYMSSIYsDLYNAYAGDTGIAAGINPPAD 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2180 WTEFFYKFADFSQVYDLDYKCFDATLPSAAFTLVAERLERLTGDPRVAKYIH-SIRHSHHVYGNRTYDMIGGNPSGCVAT 2258
Cdd:cd23228    130 GHRLREELSQYDSFLALDYSRFDGSLPEMLMRAAVEILADLHEDPDLVRRLHeTVIISKHLVVDEDWTVKGGMPSGSPCT 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2259 SILNTIINNICVLSALIQHPDFSPSQFQ---------ILAYGDDVIYA-TEPPIHPSFLRDFYQKYTpLVVTPANKGSDF 2328
Cdd:cd23228    210 TVLNCICNLLVLEYAFLVHFGVYEDDDGvglpqcdylSVVYGDDCIVAyNGMEMGLAFAETIEDTFG-MEVTPASKVGDH 288
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752309242 2329 PDTStIHEVTFLKRWFVP-DDIRPVYIHPVMDPDTYEQSVMWLRD-GDFQDVVTSLCHLAFHSGPKTYERWCTKVREQ 2404
Cdd:cd23228    289 FNVE-LHEVEFLKRKFFAfETEEYDRIALRLSENTIVQSLMWMRNlKTFPDQVQSLMMELSAWGKEKYDKLRDTCKRR 365
Avisivirus_RdRp cd23231
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Avisivirus of ...
2111-2395 1.69e-26

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Avisivirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Avisivirus genus within the family Picornaviridae, order Picornavirales. The Avisivirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. Avisivirus is a picornavirus genus containing three species Avisivirus A, Avisivirus B and Avisivirus C. The name Avisivirus is derived from Avihepato sister-clade. Turkeys serve as natural hosts. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438081  Cd Length: 362  Bit Score: 113.83  E-value: 1.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2111 ENPDYVYSTFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCNPDIHWTEFFYKFADF 2190
Cdd:cd23231     52 EPPDVYFTTYLKDELRPKEKAKAGKTRVISAASFDYTIACRMVFGPILRQLFAWGREFGFGPGLNPYTHFDELYDKILPF 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2191 sqVYDLDYKCFDATLPSAAFTLVAERLERLTGDPRVAK------YIHSIRHSHHVYGNRtydmiGGNPSGCVATSILNTI 2264
Cdd:cd23231    132 --VICLDYSGFDGSLSSELMFHAAQVIACFSEKPEAIMasaeltIGSTERVSDEVWYVY-----GGMPSGSPWTTTLNTI 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2265 INNI-CVLSALIQhpDFSPSQFQILAYGDDVIYATEPPIHPSFLRDFYQKYTPLVVTPANKGSDFPDTsTIHEVTFLKRW 2343
Cdd:cd23231    205 CNLLmCYTYLLDM--GHCWSETFVVAYGDDVVISANIKHNLEGIEQWFKTKFGATVTPSDKQGKITWT-TKNNMEFLKRR 281
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1752309242 2344 FVPDDIRPvYIHPVMDPDTYEQSVMWLRdGDFQDVVTSL-CHLAFHsGPKTYE 2395
Cdd:cd23231    282 PKQLDFLP-KIVGALDLDNMLDRIQWTK-GHFQDQLNSFyLELALH-GRETYN 331
Aalivirus_RdRp cd23216
RNA-dependent RNA polymerase (RdRp) in the genus Aalivirus of positive-sense single-stranded ...
2100-2394 4.09e-26

RNA-dependent RNA polymerase (RdRp) in the genus Aalivirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Aalivirus genus within the family Picornaviridae, order Picornavirales. Member viruses have a (+)ssRNA genome. Aalivirus is a new picornavirus found in ducks in China. It is most closely related to duck hepatitis A virus (genus Avihepatovirus) and to avisivirus A1 (genus Avisivirus). The name "aalivirus" is derived from Avihepatovirus/Avisivirus-like virus. RdRps are multi-domain proteins that play a pivotal role in enterovirus replication. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438066  Cd Length: 337  Bit Score: 112.07  E-value: 4.09e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2100 PELQILIDQTLENPDYVYSTFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLIDYM-QGRPGEHGCAVGCNPDI 2178
Cdd:cd23216     34 PKFKEDVKEILAGKPTFFTTYLKDELRSIEKIANGNTRAIEAANFDHVVAWRQVMGNIVKQLfSDHDRVTGFAPGMNPYT 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2179 HWTEFFYKFAdfSQVYDLDYKCFDATLPSAAFTLVAERLERLTGDPRVAKYIHS-IRHSHHVYGNRTYDMIGGNPSGCVA 2257
Cdd:cd23216    114 HFDSLMDQVK--WNVLALDFKKFDGSLSPQVMEEAVDILASFHDMPQMVVDIHKhTIYSTNVVSDETWFVEGGMCSGSPC 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2258 TSILNTIInNICVLSALIQHPDFSPSQFQILAYGDDVI-----YATEPPiHPSFLRDFYQKYTPLVVTPANKGSDFpDTS 2332
Cdd:cd23216    192 TTVLNTIC-NLLVNTTILLSEGIQPDNFYIAAYGDDTIisvdgLSSSLP-DPKIMQQKYKEWFGMTVTSADKGSEI-TWD 268
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752309242 2333 TIHEVTFLKR--WFVPDDIRPVyihPVMDPDTYEQSVMWLRdGDFQDVVTSLCHLAFHSGPKTY 2394
Cdd:cd23216    269 TRNHVQFLKRrpGFFPGTQKVV---GVLDLESMMEHIAWTK-GSFQDQLNSFYQELVLHGEQVY 328
Marnaviridae_RdRp cd23195
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Marnaviridae of ...
2116-2402 9.40e-25

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Marnaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Marnaviridae, order Picornavirales. Member viruses have a (+)ssRNA genome. They are mono- or dicistronic, have a polyadenylate tail and have conserved motifs for RNA helicase, RdRp, and structural protein domains. The first RNA virus isolated and characterized that infects a marine protist was Heterosigma akashiwo RNA virus (HaRNAV) in the genus Marnavirus, that infects the toxic bloom-forming Raphidophyte alga, Heterosigma akashiwo. Recently, it has undergone a major taxonomic revision and now includes 20 species within 7 genera, which include Bacillarnavirus, Kusarnavirus, Labyrnavirus, Locarnavirus, Marnavirus, Salisharnavirus, and Sogarnavirus. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438045  Cd Length: 310  Bit Score: 107.15  E-value: 9.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2116 VYSTFLKDELRPTAKvqdGLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCN---PDihWTEFF---YKFAD 2189
Cdd:cd23195      2 IFKACLKDEPTKLTK---DKVRVFQAAPVALQLLVRKYFLPIARFLQMNPLLSECAVGINaqsPE--WEELYehlTKFGE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2190 fSQVYDLDYKCFDATLPS----AAFTLVAERLERLTG-DPRVAKYIHSIRH--SHHVY---GnrtyDMI---GGNPSGCV 2256
Cdd:cd23195     77 -DRIIAGDYSKYDKRMSAqlilAAFKILIDIAAKSGGySEEDLKIMRGIATdiAYPLVdfnG----DLIqffGSNPSGHP 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2257 ATSILNTIINNICVLSA-LIQHPDFSPSQFQ----ILAYGDDVIYATEPPI----HPS---FLRDFYQKYtplvvTPANK 2324
Cdd:cd23195    152 LTVIINSIVNSLYMRYAyYSLYPEKEVPPFRdvvaLMTYGDDNIMSVSPGYpwfnHTSiaeFLAKIGIKY-----TMADK 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2325 GSDFPDTSTIHEVTFLKRWFVPDDIRPVYIHPVmDPDTYEQSV-MWLRDGD------FQDVVTSLCHLAFHSGPKTYERW 2397
Cdd:cd23195    227 EAESVPFIHISEADFLKRKFVFDPELGVYVGPL-DEDSIFKSLhCYLKSKVltpeeqAAQNIDGALREWFFHGREVYEKR 305

                   ....*
gi 1752309242 2398 CTKVR 2402
Cdd:cd23195    306 REQLK 310
rhv_like cd00205
Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA ...
841-994 7.97e-20

Picornavirus capsid protein domain_like. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids composed of 60 copies each of 4 virus encoded proteins; alignment includes picornaviridae, like poliovirus, hepatitis A virus, rhinovirus, foot-and-mouth disease virus and encephalomyocarditis virus; common structure is an 8-stranded beta sandwich


Pssm-ID: 119412  Cd Length: 178  Bit Score: 88.99  E-value: 7.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  841 SLSPLNWQTTTNYTGLAAMLSCFTYIAADLRFTLRISNPNGVPATVLIAYAPPGATLP-RNPDRQMLSNFFMSEVPLTAS 919
Cdd:cd00205     29 KLSPALGFLLLQNTPLGALLSYFTYWRGDLEVTVQFNGSKFHTGRLLVAYVPPGAPAPtTGDTRWQATLNPHVIWDLGTN 108
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752309242  920 NAtlVSFSIPYTSPLSAIPTTYYGWedWSGANFGVLQAGSWGSLLLMPTFPAEVPhadplsATMWVAFGNFKAWV 994
Cdd:cd00205    109 SS--VTFVVPYVSPTPYRSTRYDGY--GPLNSFGTLVVRVLTPLTVPSGAPTTVD------ITVYVRAGDFELYG 173
Aquamavirus_RdRp cd23220
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Aquamavirus of ...
2116-2347 5.99e-19

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Aquamavirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Aquamavirus genus within the family Picornaviridae, order Picornavirales. The Aquamavirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. Aquamavirus is a genus containing a single species, Aquamavirus A. This species consists of the previously named seal picornavirus 1, now to be called seal aquamavirus A1. Recently other aquamaviruses have been discovered in bears and seals (unassigned aquamaviruses). RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438070  Cd Length: 338  Bit Score: 90.92  E-value: 5.99e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2116 VYSTFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRM-LLGGLIDYMQGRPGEHGCAVGCNPDIHWTEFFYKFADFSqvY 2194
Cdd:cd23220     57 VFETFMKDELRPKEKIESGKTRIVESCPLDYLLLYRMvMLKSMIWWYNSDCIKTGVAPGMNVYTDFVPMVKQFKKIK--Y 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2195 DLDYKCFDATLPSAAFTLVAERLERLTGDPRVAKYIHS-IRHSHHVYGNRTYDMIGGNPSGCVATSILNTIINNICV--L 2271
Cdd:cd23220    135 CLDFSAYDSTLSDEILAAGVEVLACTSAVPSYVRKLHApIICSHHWHNNVVDLVLGGMPSGAPCTSVLNSIVNVLMAryI 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2272 SAL--IQHPdfspsqfQILAYGDDVIYATEPPIHPSFLRDFYQKYTPLVVTPANKGsdfPDTSTIHEVTFLKRW--FVPD 2347
Cdd:cd23220    215 CALmdIDYP-------VMVAYGDDNVVSFDEEIDIERMVSLYKTEFGVTATNHDKT---PVPRPMANPVFLKRRlrFNPD 284
Rhv pfam00073
picornavirus capsid protein; CAUTION: This alignment is very weak. It can not be generated by ...
422-514 3.26e-14

picornavirus capsid protein; CAUTION: This alignment is very weak. It can not be generated by clustalw. If a representative set is used for a seed, many so-called members are not recognized. The family should probably be split up into sub-families. Capsid proteins of picornaviruses. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids. They include rhinovirus (common cold) and poliovirus. Common structure is an 8-stranded beta sandwich. Variations (one or two extra strands) occur.


Pssm-ID: 395026  Cd Length: 170  Bit Score: 72.73  E-value: 3.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  422 HSMWNCGWRVQVTVNGSQFHAGALTLYMVPEGATESVEAARLNAGFVFPYVILSLYESNTATLEVPFISPTPNTSSGLHA 501
Cdd:pfam00073   77 HTYYRGGLEVTVQFNGSKFHQGKLLVAYVPPGAPPPGSRDYLWQATLNPHQFWNLGLNSSARLSVPYISIAHYYSTFYDG 156
                           90
                   ....*....|...
gi 1752309242  502 PWTFYLQVLSPLN 514
Cdd:pfam00073  157 NWTLVVAGWVPLN 169
Iflaviridae_RdRp cd23197
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Iflaviridae of ...
2113-2397 6.47e-14

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Iflaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Iflaviridae, order Picornavirales. Iflaviridae is a family of small non-enveloped viruses with (+)ssRNA genomes of approximately 9-11 kilobases in length encoding a single polyprotein. All members infect arthropod hosts with the majority infecting insects. Beneficial and pest insects serve as hosts and infections can be symptomless (Nilaparvata lugens honeydew virus 1), cause developmental abnormalities (deformed wing virus, Varroa destructor virus 1, sacbrood virus), behavioral changes (deformed wing virus, Varroa destructor virus 1, slow bee paralysis virus, sacbrood virus) and premature mortality (deformed wing virus, Varroa destructor virus 1, slow bee paralysis virus, infectious flacherie virus, sacbrood virus). RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438047  Cd Length: 319  Bit Score: 75.29  E-value: 6.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2113 PDYVYSTFLKDELRPTAKVQD-GLTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCNPD-IHWTEFFYKFADF 2190
Cdd:cd23197      4 PPCVYWAHLKDELRPSEKLRRfGGTRVFSVPPLELVLNSRRFLLPFMDAFQSFPIEAHHAIGLNPNsGDWRRLRDTLLEK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2191 SQ-VYDLDYKCFDATLP----SAAFTLVAERLER---LTgdPRVAKYIHSIRH-----SHHVYGNrTYDMIGGNPSGCVA 2257
Cdd:cd23197     84 GPcLLQMDYKNYSDAIPkecvAKAFHIIVDYYRKwhcLT--VEIENALKTLFLdtadaELLVYGD-VFKVNNGVLAGHPM 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2258 TSILNTIINNICVLSALIQHPDFSPSQF----QILAYGDDVIYATEPPIHPSF----LRDFYQKYTpLVVTPANK---GS 2326
Cdd:cd23197    161 TSVVNSVVNLILMNYMWIKITRRRASEFfkltYIIVMGDDVVISLPKQLTEEFdcrkICAEFAKYD-IKVTDSEKnltGE 239
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752309242 2327 DFPDTStIHEVTFLKRWFVPDDIRP-VYIHPVmDPDTYEQSVMWL-RDGDF-----QDVVTSLcHLAFHSGPKTYERW 2397
Cdd:cd23197    240 PKPYDS-FDKFEFLSRGFSDCDAYPdITFAPV-KTIALFDCPLWIsKGQDEeeqtiQAIQAGL-LLAFDHGPEFFGKY 314
Secoviridae_RdRp cd23196
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Secoviridae of ...
2121-2345 3.37e-13

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Secoviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Secoviridae, order Picornavirales. Members of the family Secoviridae are non-enveloped viruses with mono- or bipartite (RNA-1 and RNA-2) linear (+)ssRNA genomes of 9 to 13.7 kilobases in total. Secoviruses are related to picornaviruses and are classified in the order Picornavirales. The majority of known members infect dicotyledonous plants and many are important plant pathogens (e.g., grapevine fanleaf virus and rice tungro spherical virus). The Secoviridae includes 8 genera (Comovirus, Fabavirus, Nepovirus, Cheravirus, Sadwavirus, Torradovirus, Sequivirus, and Waikavirus) as well as unassigned species (strawberry latent ringspot virus-MEN 454, strawberry mottle virus-Thompson, black raspberry necrosis virus- 1, chocolate lily virus A-KP2, and Dioscorea mosaic associated virus-goiana). RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438046  Cd Length: 309  Bit Score: 72.80  E-value: 3.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2121 LKDELRPTAKVQDG-LTRIVEAAPIHAIIAGRMLLGGLIDYMQGRPGEHGCAVGCNP-DIHWTEFFYKFADFSQV-YDLD 2197
Cdd:cd23196      7 PKDERLKKRKVLEKpKTRLFDVLPMEYNLLLRKYFLNFVRFIQANRHRLPCQVGINPySREWTTLYDRLAEKSDTaLNCD 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2198 YKCFDATLPSAAFTLVAERLERLTGDPRVAKYIHSI------RHShhVYGNRTYDMIGGNPSGCVATSILNTIINNI--- 2268
Cdd:cd23196     87 YSRFDGLLSHQVYVWIADMINRLYGDGDEAKARRNLlmmfcgRRS--ICGRQVYMVRGGMPSGCALTVIINSIFNEIlir 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2269 -----CVLSALIQHPDfspSQFQILAYGDDVIYATEPPIHPSF----LRDFYQKYTPLVVTPANKGSDFPDTSTIHEVTF 2339
Cdd:cd23196    165 yvyrkVVPRPARNNFN---KYVRLVVYGDDNLISVKEEIIPYFdgpvIKKEMAKVGVTITDGTDKTSPTLERKPLESLDF 241

                   ....*.
gi 1752309242 2340 LKRWFV 2345
Cdd:cd23196    242 LKRGFR 247
Solinviviridae_RdRp cd23199
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Solinviviridae of ...
2170-2344 1.96e-12

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Solinviviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Solinviviridae, order Picornavirales. Solinviviridae is a family of picorna/calici-like viruses with non-segmented, linear, (+)ssRNA genomes of approximately 10-11 kb. Members of two species within the family infect ants but related unclassified virus sequences derive from a large variety of insects and other arthropods. Phylogenetic analysis of RdRp amino acid sequences shows that members of the two classified solinvivirus species form part of a large and very diverse group of arthropod-infecting viruses within the picorna/calici-like group of viruses. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg (viral protein genome-linked)-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438049  Cd Length: 323  Bit Score: 70.85  E-value: 1.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2170 CAVGCNPDIHWTEFFYKFADFSQVYDLDYKCFDATLPSAAFTLVAERLerLTGDPRVAKYIHSI----RHSHHVYGNRTY 2245
Cdd:cd23199     71 CAVGCNPYATFHKFATKFFKFKNFFSCDYKNFDRTIPKCVFEDFRDML--IQANPHMKNEIYACfqtiIDRIQVSGNSIL 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2246 DMIGGNPSGCVATSILNTIINNICVLSALI-----------QHPDFSPSQFQILAYGDDVIYATEPPIHPSFLRDFYQKY 2314
Cdd:cd23199    149 LVHGGMPSGCVPTAPLNSKVNDIMIYTAYVnilrradrgdiTSYRYYRDLVCRLFYGDDVIIAVDDSIADIFNCQTLSEE 228
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1752309242 2315 TP----LVVTPANKGSDFPDTSTIHEVTFLKRWF 2344
Cdd:cd23199    229 MKilfgMNMTDGSKSDIIPKFETIETLSFISRFF 262
Nora-virus_RdRp cd23200
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in a novel picorna-like ...
2118-2348 4.26e-12

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in a novel picorna-like Drosophila virus, Nora virus; This group contains the catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the unclassified Nora virus, a new picorna-like virus family. Nora virus has a (+)ssRNA genome followed by a poly(A) tail. Unlike other picorna-like viruses, the genome has four open reading frames (ORFs). One ORF encodes a picornavirus-like cassette of proteins for virus replication, including an iflavirus-like RdRp and a helicase that is related to those of mammalian picornaviruses. The three other ORFs are not closely related to any previously described viruses. Nora virus is present as a persistent infection in several tested laboratory stocks and wild-caught flies. 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: 438050  Cd Length: 306  Bit Score: 69.56  E-value: 4.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2118 STFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRMLLGGLID--YMQGRPGEHgcAVGCNP-DIHWTEFFYKFADFSQVY 2194
Cdd:cd23200      4 SSKLKDQPIKIAQAKSGRTRVFHCIPVDLILFSGALYGPYKEayTKAGLKCYH--AVGIDPkSVGWQQLATYMTKHPNYF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2195 DLDYKCFDATLPSAAFTLVAERLERLTGDPR-----VAKYIHSIRH-SHHVYGNRT-YDMIGGNPSGCVATSILNTIINN 2267
Cdd:cd23200     82 DADYKNYDKYLHRQVFKAVRKIQRSVIQQVCpdkwdKARAVEELDAiDTYVVDYQTvYKTNRGNKSGSYTTTIDNCLAND 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2268 ICVLSA------LIQHPDFSpSQFQILAYGDDVIYateppihpSFLRDFYQKY-----------TPLVVTPANKGSDFPD 2330
Cdd:cd23200    162 IYGLYAwvkttgLRSLWDYR-QNVSSVAFGDDIIK--------SVSDEYKDKYnyctyrdvlnaTGHIMTPGSKDGEEKP 232
                          250
                   ....*....|....*...
gi 1752309242 2331 TSTIHEVTFLKRWFVPDD 2348
Cdd:cd23200    233 FTSFENLQFLKRGFKLEN 250
Polycipiviridae_RdRp cd23198
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Polycipiviridae of ...
2120-2404 4.68e-12

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Polycipiviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Polycipiviridae (polycistronic picorna-like viruses), order Picornavirales. Polycipiviridae is a family of picorna-like viruses with non-segmented, linear, (+)ssRNA genomes of approximately 10-12 kb. Their genomes are polycistronic, with four (or more) consecutive 5'-proximal open reading frames (ORFs) encoding structural (and possibly other) proteins and a long 3' ORF encoding the replication polyprotein. Members of species within the family are typically found in ants, with Apple picorna-like virus 1 and the unnamed Polycipiviridae virus in fruit bat stool as exceptions. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438048  Cd Length: 317  Bit Score: 69.75  E-value: 4.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2120 FLKDELRPTAKV-----QDGLTRIVEAAPIHAIIAGRMLLGGLIDYM-QGRPGEHGCAVGCNPD-IHWTEFFYKFADFSQ 2192
Cdd:cd23198      6 FPKDELRPIYKAlgdpqTPPKTRSVTCMNVYYILAWRRVTLDFWASMhRAADGNFPFCPGINPEgPDWNRLYHYLNRHPN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2193 VYDLDYKCFDATLPSAAFTLVAERLERLTG-DP--RVAKYIHSIR----HSHHVYGNRTYDMIGGNPSGCVATSILNTI- 2264
Cdd:cd23198     86 AVDFDVSNWDGHLPAELFYAVLDIIKTVLGlKPnsPNAKVIYSILtevmNCHIQFEDIIYQKLRGLISGFPGTAEVNTLa 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2265 ----INNICVLSALIQHPDFSPSQF----QILAYGDDVIYATEPPIHPSF----LRDFYQK--YTplvVTPANKGSDFPD 2330
Cdd:cd23198    166 hwllIYYIYLYLAQNTIYDMTITAFlrnvSAIFYGDDIIITISDEILHWFngktIQRMYEEhgYP---VTSAAKDTEIPE 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2331 TSTIHEVTFLKRWFVPddIRPVYIHPVMDPDTYEQSVMWLRDGD------FQDVVTSLcHLAFHSGPKTYErwctKVREQ 2404
Cdd:cd23198    243 SKPLSDCQFLKSSWNP--ILPGYYIRKMDIEVVYDLVYWVRAKEhprdqfYSNYHDAL-RILFGHGEQVFE----AFREQ 315
ps-ssRNAv_Astroviridae_RdRp cd23172
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Astroviridae of ...
2114-2314 2.66e-10

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Astroviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Astroviridae, order, Stellavirales. Astrovirus has a non-segmented, (+)ssRNA genome within a non-enveloped icosahedral capsid. The family Astroviridae comprises two genera, Mamastrovirus, which infect mammals, and Avastrovirus, which infect birds. Astroviruses have been isolated from stools from a wide variety of mammals and birds. Human astroviruses have been shown to be an important cause of gastroenteritis in young children. Duck astrovirus causes an often-fatal hepatitis in ducklings. Astroviruses infecting turkeys, guinea fowl and chickens affect multiple organs, including the kidney and thymus. 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: 438022  Cd Length: 243  Bit Score: 63.26  E-value: 2.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2114 DYVYSTFLKDELRPTAKVQDGLTR-IVEAAPIHAIIAGRmllgglIDY-----MQGRPGEHGCAVGcnpdihWTEFFYKF 2187
Cdd:cd23172      1 RPLWYLFLKKEILKKEKIEDGDIRqILCPDPIFARIGAR------FEQdqnnlMKERTLTNEGQVG------WSPFYGGF 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2188 AD--------FSQVYDLDYKCFDATLPSAAFTLVAE-RLERLTGDPRVA------KYIHSI--RHSHHVYGNRTYdMIGG 2250
Cdd:cd23172     69 DArvrrlgskGNYFVEFDWTRFDGTIPAELFRHIRKlRWSFLDPEKTEEnrkvydWYVHNLlnRYVLLPTGEVTR-VTKG 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752309242 2251 NPSGCVATSILNTIINNI---CVLSALIQHPDFSPSQ----FQILAYGDDVI--YATEPPIHPSFLRDFYQKY 2314
Cdd:cd23172    148 NPSGQISTTMDNCMVNTFltaFEFAYVYGPKTGTLKElwdnYDTIVYGDDRLsgYPSLPDPYVERVVDMYKDV 220
Rhv pfam00073
picornavirus capsid protein; CAUTION: This alignment is very weak. It can not be generated by ...
635-729 1.73e-09

picornavirus capsid protein; CAUTION: This alignment is very weak. It can not be generated by clustalw. If a representative set is used for a seed, many so-called members are not recognized. The family should probably be split up into sub-families. Capsid proteins of picornaviruses. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids. They include rhinovirus (common cold) and poliovirus. Common structure is an 8-stranded beta sandwich. Variations (one or two extra strands) occur.


Pssm-ID: 395026  Cd Length: 170  Bit Score: 59.25  E-value: 1.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  635 LSLFSQWRGELAAHLLFTGSAQHYGRLVVCYTPAAPAPPSNMQ---EAMRGTYTVWDVNAASTLEFTIPFISQS---YWK 708
Cdd:pfam00073   74 LRYHTYYRGGLEVTVQFNGSKFHQGKLLVAYVPPGAPPPGSRDylwQATLNPHQFWNLGLNSSARLSVPYISIAhyySTF 153
                           90       100
                   ....*....|....*....|.
gi 1752309242  709 TVDIFNpdalLSTTGYVSVWV 729
Cdd:pfam00073  154 YDGNWT----LVVAGWVPLNY 170
Peptidase_C3 pfam00548
3C cysteine protease (picornain 3C); Picornaviral proteins are expressed as a single ...
1787-1942 9.43e-08

3C cysteine protease (picornain 3C); Picornaviral proteins are expressed as a single polyprotein which is cleaved by the viral 3C cysteine protease.


Pssm-ID: 278947  Cd Length: 174  Bit Score: 53.99  E-value: 9.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1787 ISQNVVHVESGNGneKVVMSGFYIFSRYLLVPTHLREPHHTTL--LVGTDAYDWATLPTL--TLGELTLVHTPTSRQYKD 1862
Cdd:pfam00548   11 LKQNAVPVTTSKG--VFTCCATGVYDNVILLPRHAEPGLTIVLdgKVVTISDPEVELVDQegMPLDAAIVKLKRNEKFKD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1863 MRRFIGSYPHPTG---ILVSQYKAAPLY-----VRFSDNRV-LDMD-FPGAIVckqaygYRAATFEGLCGSPLVTDDPAG 1932
Cdd:pfam00548   89 IRKHLPNRITKGNpvvLLINNNEQGRIYvpvgaVTHSGGIKtLDGTtTPRTIS------YNAPTKAGMCGGVVIAKVEGN 162
                          170
                   ....*....|
gi 1752309242 1933 IKILGLHVAG 1942
Cdd:pfam00548  163 GKILGMHIAG 172
ps-ssRNAv_EoPV-like_RdRp cd23171
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the positive-sense ...
2113-2348 9.26e-07

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the positive-sense single-stranded RNA [(+)ssRNA] picorna-like virus Ectropis obliqua, and related viruses; This group contains the catalytic core domain of RdRp of Ectropis obliqua picorna-like virus (EoPV), and related viruses. EoPV is an insect (+)ssRNA virus that causes a lethal granulosis infection of larvae of the tea looper (Ectropis obliqua), and related insect-infecting iflaviruses. Ectropis obliqua, a species of moth, is one of the most destructive pest insects on tea plants throughout growing areas of this crop in southern China. The EoPV genome contains a single large ORF encoding the capsid proteins at the 5' terminus of the genome with the non-structural proteins at the 3' end of the genome. This organization is similar to typical mammalian picornaviruses. 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: 438021  Cd Length: 239  Bit Score: 52.60  E-value: 9.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2113 PDYVYSTFLKDELRPTAKVqdglTRIVEAAPIHAIIAGRMLLGGLIDYMQGRpgEHGCAVGCnpDIHWTEFFYKFADFSQ 2192
Cdd:cd23171     12 PPTTFMDFPKDELLKPGKD----TRLINGAPLHHTLDMRRYLMEFFAAITTI--NNKIAVGI--DVHSGDWALIHGGADD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2193 VYDLDYKCFDATLPSAAFTLVAERL-----ERLTGDPR----VAKYIHSIRHSHHVYGNRTYDMIGGNPSGCVATSILNT 2263
Cdd:cd23171     84 VVDEDYSGFGPGFHSQWLDVIRRIAvawckHHKTVDPEyenvVRCLIRELQNAYHVAGDLVYQVLCGSPSGAFATDRINS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2264 IIN----NICVLSALIQHPDFspSQFQILAYGDDVIYAteppiHPSFLRDFYQKYTP---LVVTPANKGSDfpdtstihe 2336
Cdd:cd23171    164 LANlcyhCLCYLRKYGTLTGF--WSHYLLVYGDDTRRR-----ETAYTGDEFQDCMAsigITVNRDKSGVT--------- 227
                          250
                   ....*....|..
gi 1752309242 2337 vTFLKRWFVPDD 2348
Cdd:cd23171    228 -SFLKRQFIPYD 238
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
1435-1573 2.47e-06

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 49.45  E-value: 2.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 1435 HRKRQVGPRPEPVVVYFYGPPGTGKSLLASLLAQTLAQR----LSGDPDDVYSPTAASCEYFDGYNGQ----------SV 1500
Cdd:cd00009      8 EALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgapfLYLNASDLLEGLVVAELFGHFLVRLlfelaekakpGV 87
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752309242 1501 HFIDDIGQDPEGRDWANFPNlvssapyilpMASLEEKGIHYTSRVIVVTSNFHEPNERAARSMGALRRRVHLR 1573
Cdd:cd00009     88 LFIDEIDSLSRGAQNALLRV----------LETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
ps-ssRNAv_RdRp-like cd23167
conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense ...
2193-2299 5.35e-06

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.


Pssm-ID: 438017 [Multi-domain]  Cd Length: 73  Bit Score: 46.18  E-value: 5.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2193 VYDLDYKCFDATLPSAAFTLvaerlerltgdprvakyihsirhshhvygnrtydmigGNPSGCVATSILNTIINNICVLS 2272
Cdd:cd23167      2 VVESDYSGFDSSISPDLLKA-------------------------------------GQPSGSPNTSADNSLINLLLARL 44
                           90       100
                   ....*....|....*....|....*....
gi 1752309242 2273 ALIQHPDFSP--SQFQILAYGDDVIYATE 2299
Cdd:cd23167     45 ALRKACGRAEflNSVGILVYGDDSLVSVP 73
ps-ssRNAv_Potyviridae_RdRp cd23175
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Potyviridae of ...
2116-2314 2.60e-04

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Potyviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Potyviridae, order: Patatavirales. Potyviridae, is the largest family of RNA plant viruses, members of which have (+)ssRNA genomes and flexuous filamentous particles. The family is divided into eight genera: Brambyvirus, Bymovirus, Ipomovirus, Macluravirus, Poacevirus, Potyvirus, Rymovirus, and Tritimovirus. Most genomes are monopartite but those of members of the genus Bymovirus are bipartite. Some members cause serious disease epidemics in cultivated plants. 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: 438025  Cd Length: 236  Bit Score: 45.13  E-value: 2.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2116 VYSTFLKDELRPTAKVQDGLTRIVEAAPIHAIIAGRMllggLID------YMQGRPGEHgcAVGcnpdIH-----WTEFF 2184
Cdd:cd23175      5 VWNGSLKAELRPIEKVEANKTRTFTAAPIDTLLGGKV----CVDdfnnqfYSLHLKAPW--TVG----ITkfyggWDKLL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242 2185 YKF--------ADFSQvydldykcFDATLPSAAFTLVAE-RLERLTGDPrvakyIHSIRHShHVYGNRTYDMI------- 2248
Cdd:cd23175     75 RKLpdgwvycdADGSQ--------FDSSLTPYLINAVLRiRLHFMEDWD-----IGEQMLR-NLYTEIVYTPIltpdgti 140
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752309242 2249 ----GGNPSGCVATSILNTIINNICVLSALIQH---PDFSPSQFQILAYGDDVIYATePPIHPSFLrDFYQKY 2314
Cdd:cd23175    141 vkkfKGNNSGQPSTVVDNTLMVMIAMYYALLKLgidFEEIDERCVFFCNGDDLLIAV-SPEHEHIL-DTFSSS 211
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
1449-1470 2.74e-04

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 42.97  E-value: 2.74e-04
                           10        20
                   ....*....|....*....|..
gi 1752309242 1449 VYFYGPPGTGKSLLASLLAQTL 1470
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKEL 22
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
1430-1470 2.76e-04

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 45.67  E-value: 2.76e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1752309242 1430 LALSQHRKRQVGPRPEPVVVYFYGPPGTGKSLLASLLAQTL 1470
Cdd:COG0464    175 LPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGEL 215
Rhv pfam00073
picornavirus capsid protein; CAUTION: This alignment is very weak. It can not be generated by ...
856-943 3.65e-04

picornavirus capsid protein; CAUTION: This alignment is very weak. It can not be generated by clustalw. If a representative set is used for a seed, many so-called members are not recognized. The family should probably be split up into sub-families. Capsid proteins of picornaviruses. Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids. They include rhinovirus (common cold) and poliovirus. Common structure is an 8-stranded beta sandwich. Variations (one or two extra strands) occur.


Pssm-ID: 395026  Cd Length: 170  Bit Score: 43.45  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  856 LAAMLSCFTYIAADLRFTLRIsNPNGVPA-TVLIAYAPPGATLPRNPDRQMLSNFFMSEVPLTASNATlVSFSIPYTSPL 934
Cdd:pfam00073   70 LGRLLRYHTYYRGGLEVTVQF-NGSKFHQgKLLVAYVPPGAPPPGSRDYLWQATLNPHQFWNLGLNSS-ARLSVPYISIA 147

                   ....*....
gi 1752309242  935 SAIPTTYYG 943
Cdd:pfam00073  148 HYYSTFYDG 156
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
1423-1470 4.02e-04

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 43.04  E-value: 4.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1752309242 1423 QSLKNYTLALSQHRKRQVGPRPEPVVVYFYGPPGTGKSLLASLLAQTL 1470
Cdd:cd19481      3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGEL 50
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1448-1573 9.50e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 41.98  E-value: 9.50e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752309242  1448 VVYFYGPPGTGKSLLASLLAQTLAQR------LSGDPDDVYSPTAASCEYFDGYNGQSVH-------------------F 1502
Cdd:smart00382    4 VILIVGPPGSGKTTLARALARELGPPgggviyIDGEDILEEVLDQLLLIIVGGKKASGSGelrlrlalalarklkpdvlI 83
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752309242  1503 IDDIG--QDPEGRDWANFpnlvssapyILPMASLEEKGIHYTSRVIVVTSNFHEPNERAARSMgaLRRRVHLR 1573
Cdd:smart00382   84 LDEITslLDAEQEALLLL---------LEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR--FDRRIVLL 145
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
1451-1470 8.83e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 41.22  E-value: 8.83e-03
                           10        20
                   ....*....|....*....|
gi 1752309242 1451 FYGPPGTGKSLLASLLAQTL 1470
Cdd:PRK13342    41 LWGPPGTGKTTLARIIAGAT 60
 
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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