NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1110865247|gb|APG77560|]
View 

RdRp [Beihai barnacle virus 2]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Kitaviridae_RdRp cd23254
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Kitaviridae of ...
1907-2173 5.36e-145

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


:

Pssm-ID: 438104  Cd Length: 267  Bit Score: 451.22  E-value: 5.36e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1907 TSYEFMIKRDVKPDLTNNAAYTYSALQTVLSHPKTINAITCPMIRRLKERILGALPSNILFFTEVTPDEFCEKISRVIPP 1986
Cdd:cd23254      1 NVYSFMIKRNPKPNLTVDAAYKYPALQTIAYHDKDINAIFCPIFRELKKRLLAVLKPNFVIFTDMSPEDFEELLNRRFPP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1987 ALSATIRQSLEVDISKYDKSQGIVALVYECRMMKFFGVPDWFVSMWFRGHIATTFSDPTTGIRGRIAFQRKSGDASTYLG 2066
Cdd:cd23254     81 EVLSKLLHKLEIDISKYDKSQGELALLFECKLMRRFGVPEELVELWFNAHVLTTLYDRTNKLKALVEYQRKSGDASTFFG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2067 NTMFLLGVLLATFKYSEMDLLLCSGDDSLILGRDFDAGVDVQDFNLIFNLETKFLRYQHYYFCSKYLFSDGQRWWLVPDP 2146
Cdd:cd23254    161 NTLFLMAVLADLFDLSDLELALFSGDDSLLFGRNLLDYDDSQHFALKFNLESKFLNYKYPYFCSKFLLPVGGRWYFVPDP 240
                          250       260
                   ....*....|....*....|....*..
gi 1110865247 2147 VKVMVKLGRHDLVNWEHCEEYRVSYSD 2173
Cdd:cd23254    241 VKLLTKLGRHDLVNWEHVEEYRISLKD 267
Viral_helicase1 pfam01443
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
1353-1599 8.99e-37

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


:

Pssm-ID: 366646 [Multi-domain]  Cd Length: 227  Bit Score: 139.44  E-value: 8.99e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1353 KLVQAAAGCGKTTDIVRKARvtrDAVILAGTVEgreDIERRLGDS-NVRVRTIQSFLLS--PFVCRVLFIDEAMMQHPGM 1429
Cdd:pfam01443    1 IVVHGVPGCGKSTLIRKLLR---TSRVIRPTAE---LRTEGKPDLpNLNVRTVDTFLMAllKPTGKILILDEYTLLPPGY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1430 VVLAAHLSGAAEVYAYGDRCQIPFVNRARQFYvkytnLADSFPTVAHLM---RSYRCPVSVAARLHDRYLSatGVGMTSV 1506
Cdd:pfam01443   75 ILLLAAISGAKLVILFGDPLQIPYHSRAPSFL-----IPHFPSSLSHRVgrrTTYLLPSLRAPILSAKGFE--VVVERSG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1507 RDQRDGEELKVITGldavpragfdVYLTFKQSEKQTllvHGYNATTVHSFQGKEAKHVAVVRLSSNAQDEIYLREEYALV 1586
Cdd:pfam01443  148 EYKVDYDPNGVLVL----------VYLTFTQALKES---LGVRVTTVHEVQGLTFDSVTLVLDTDTDLLIISDSPEHLYV 214
                          250
                   ....*....|...
gi 1110865247 1587 ALTRHTTRLVYFT 1599
Cdd:pfam01443  215 ALTRHRKSLHILT 227
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
763-942 1.19e-21

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


:

Pssm-ID: 426399  Cd Length: 179  Bit Score: 94.19  E-value: 1.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  763 YVCRSGVKLAEICYRFPaLLKNVTAALDLCAGPGGFTQFLVSRGlvvsyvnceryVPMIYrstaAVDVSEG--------- 833
Cdd:pfam01728    1 YRSRAAYKLLEIDEKFG-LLKPGKTVLDLGAAPGGWSQVALQRG-----------AGKVV----GVDLGPMqlwkprndp 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  834 -----GGDLLDDVVFQRLTETEDMYP-LVVGDGCPPGDARGVVHADDFFPLLERQVDLALTVVTIGGSYVQK-FMFPQDP 906
Cdd:pfam01728   65 gvtfiQGDIRDPETLDLLEELLGRKVdLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFVCKvFQGEDFS 144
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1110865247  907 RsavLLRRVARVFETVKLVRPCSTRPASDEFYVVAL 942
Cdd:pfam01728  145 E---LLYLLKLGFEKVGVFKPPASRPESSEEYLVCL 177
Vmethyltransf super family cl46422
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ...
85-413 6.06e-21

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


The actual alignment was detected with superfamily member pfam01660:

Pssm-ID: 480762  Cd Length: 308  Bit Score: 95.83  E-value: 6.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247   85 VDYVLTDSEKsvmkKMYPQYLLEFTGK--IRHEHAFSAAtrdadERMFLDEFRGMRQSqhYDVMVKDIGGNPGRHLTRGR 162
Cdd:pfam01660    1 FPYALSPEAQ----ELLENLGIEFSPYsvTPHSHPAAKA-----LENLLLEVLPSYLP--NPSTVLDIKGSKLRHLKRGN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  163 LNVHSCFPRLRPADQVRHTRFMadmarfrpdlrgrdsrcVYNNYLRGINLCSR--VAEECRVTAP---YLISVHSAYDMG 237
Cdd:pfam01660   70 PNVHCCNPILDPRDVARYPEAF-----------------SLEKSLGNGEDLRPtnTFEDCRVLAPttsYAFMHDSLHDWS 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  238 REKLASAMISADA-NILRGSMIFHPDVLVFDK-GLIPD---QEMHFQRFerngvpyirFFHP---MGGStdYTHDYrKYI 309
Cdd:pfam01660  133 PEELADLFLRKPKlERLYATLVFPPELLFGDKeSLYPElytFWYKGDRF---------HFYPdghLGGS--YTHPL-NLL 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  310 ELIETIGFTHRGFD-FSVEIDQMCGGRIIFTMFRhyASGVPRGVESRTIQLGHDDKLVV----YYWRARDPGVGIWsflp 384
Cdd:pfam01660  201 SWLTTSKIHLPGGFtYTVERLESRGAHHLFKITR--GDGLTPKVIVPDSRTFGPFEAVLlpkiFVPRVLNYIRGKP---- 274
                          330       340
                   ....*....|....*....|....*....
gi 1110865247  385 fvnqtrlsrvrmvVPKKLFEKMYTYATTL 413
Cdd:pfam01660  275 -------------IPLTVVNKLFSYLRSL 290
OTU super family cl45892
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
593-700 4.67e-10

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


The actual alignment was detected with superfamily member cd22792:

Pssm-ID: 459237 [Multi-domain]  Cd Length: 108  Bit Score: 58.77  E-value: 4.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  593 VEIPVAADGNCFFHALR-AVGASALDpvsLRQKLlaaRDSwglePYLASEQVSRLtDFSEKPLVphWADETTFLVAARVL 671
Cdd:cd22792      1 KVVPVPGDGNCFWHSLGhFLGLSALE---LKKLL---RDS----LFDDPELDEEL-DEQLEPGV--YAEDEAIAAAAKLF 67
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1110865247  672 GVTICLH--MRGTVRRY---GKGPVFHLQLTSEH 700
Cdd:cd22792     68 GVNICVHdpDEGVLYTFtpnESSKSIHLLLENEH 101
 
Name Accession Description Interval E-value
Kitaviridae_RdRp cd23254
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Kitaviridae of ...
1907-2173 5.36e-145

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


Pssm-ID: 438104  Cd Length: 267  Bit Score: 451.22  E-value: 5.36e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1907 TSYEFMIKRDVKPDLTNNAAYTYSALQTVLSHPKTINAITCPMIRRLKERILGALPSNILFFTEVTPDEFCEKISRVIPP 1986
Cdd:cd23254      1 NVYSFMIKRNPKPNLTVDAAYKYPALQTIAYHDKDINAIFCPIFRELKKRLLAVLKPNFVIFTDMSPEDFEELLNRRFPP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1987 ALSATIRQSLEVDISKYDKSQGIVALVYECRMMKFFGVPDWFVSMWFRGHIATTFSDPTTGIRGRIAFQRKSGDASTYLG 2066
Cdd:cd23254     81 EVLSKLLHKLEIDISKYDKSQGELALLFECKLMRRFGVPEELVELWFNAHVLTTLYDRTNKLKALVEYQRKSGDASTFFG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2067 NTMFLLGVLLATFKYSEMDLLLCSGDDSLILGRDFDAGVDVQDFNLIFNLETKFLRYQHYYFCSKYLFSDGQRWWLVPDP 2146
Cdd:cd23254    161 NTLFLMAVLADLFDLSDLELALFSGDDSLLFGRNLLDYDDSQHFALKFNLESKFLNYKYPYFCSKFLLPVGGRWYFVPDP 240
                          250       260
                   ....*....|....*....|....*..
gi 1110865247 2147 VKVMVKLGRHDLVNWEHCEEYRVSYSD 2173
Cdd:cd23254    241 VKLLTKLGRHDLVNWEHVEEYRISLKD 267
RdRP_2 pfam00978
RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The ...
1784-2221 3.33e-97

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


Pssm-ID: 395779  Cd Length: 440  Bit Score: 321.90  E-value: 3.33e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1784 SEDLNVPISNVSVLPYRDVYVPPRYDS-LRPRLITSMPRRRPTTMRESLVALLKRNANVPDMAGVVDIPALVSRMFESVV 1862
Cdd:pfam00978    1 TSDISLDLDDCRLDPSKSKPKPKDKEPyLVPVLRTAAPSPRQNTLKEVLLALKKRNFNVPELQESVDLDDTAERVAERFK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1863 AVLMKTD----FDEIQLSAGDIADWLHDQ-PPAVAEKLLEPLG-THEMEMTSYEFMIKRDVKPDLTNNAAYTYSALQTVL 1936
Cdd:pfam00978   81 KSFLDKEkldkLDPIINTTENVSRWLDKQsGKKAAQLKLDDLVpLHEVDLDRYKHMIKSDVKPKLDLSPQSERPALQTIT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1937 SHPKTINAITCPMIRRLKERILGALPSNILFFTEVTPDEFCEKisrvipPALSATIRQSLEVDISKYDKSQGIVALVYEC 2016
Cdd:pfam00978  161 YHDKGVTAYFSPIFRELFERLLYVLKPKIVFPTGMTSSLIAEH------FEFLDASEDFLEIDFSKFDKSQGELHLLVQL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2017 RMMKFFGVPDWFVSMWFRGHIATTFSDPTTGIRGRIAFQRKSGDASTYLGNTMFLLGVLLATFKYSEMDLLLCSGDDSLI 2096
Cdd:pfam00978  235 EILKLLGLDPELADLWFKFHRQSYIKDRKNGVGFSVDYQRKSGDANTYLGNTLVTMAMLASVYDLEKIDCAAFSGDDSLI 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2097 LGRDFDAGvDVQDFNLIFNLETKFLRYQHYYFCSKYLFSDGQRWWLVPDPVKVMVKLGR-HDLVNWEHCEEYRVSYSDNV 2175
Cdd:pfam00978  315 FSPKPIED-PASRFATLFNMEAKVFDPSVPYFCSKFLLEVDGGAFFVPDPLKLLQKLGKkKIPDDEQHLDEIFTSLCDLT 393
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1110865247 2176 VAYADARVATVLAR-AVRERYAYADVNIETLISALHVIASPDYFSSL 2221
Cdd:pfam00978  394 KSFNDDCVVLELLDlAVARYYKYAPEGYAALCALHKALSSFTLFFSL 440
Viral_helicase1 pfam01443
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
1353-1599 8.99e-37

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


Pssm-ID: 366646 [Multi-domain]  Cd Length: 227  Bit Score: 139.44  E-value: 8.99e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1353 KLVQAAAGCGKTTDIVRKARvtrDAVILAGTVEgreDIERRLGDS-NVRVRTIQSFLLS--PFVCRVLFIDEAMMQHPGM 1429
Cdd:pfam01443    1 IVVHGVPGCGKSTLIRKLLR---TSRVIRPTAE---LRTEGKPDLpNLNVRTVDTFLMAllKPTGKILILDEYTLLPPGY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1430 VVLAAHLSGAAEVYAYGDRCQIPFVNRARQFYvkytnLADSFPTVAHLM---RSYRCPVSVAARLHDRYLSatGVGMTSV 1506
Cdd:pfam01443   75 ILLLAAISGAKLVILFGDPLQIPYHSRAPSFL-----IPHFPSSLSHRVgrrTTYLLPSLRAPILSAKGFE--VVVERSG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1507 RDQRDGEELKVITGldavpragfdVYLTFKQSEKQTllvHGYNATTVHSFQGKEAKHVAVVRLSSNAQDEIYLREEYALV 1586
Cdd:pfam01443  148 EYKVDYDPNGVLVL----------VYLTFTQALKES---LGVRVTTVHEVQGLTFDSVTLVLDTDTDLLIISDSPEHLYV 214
                          250
                   ....*....|...
gi 1110865247 1587 ALTRHTTRLVYFT 1599
Cdd:pfam01443  215 ALTRHRKSLHILT 227
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
763-942 1.19e-21

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 94.19  E-value: 1.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  763 YVCRSGVKLAEICYRFPaLLKNVTAALDLCAGPGGFTQFLVSRGlvvsyvnceryVPMIYrstaAVDVSEG--------- 833
Cdd:pfam01728    1 YRSRAAYKLLEIDEKFG-LLKPGKTVLDLGAAPGGWSQVALQRG-----------AGKVV----GVDLGPMqlwkprndp 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  834 -----GGDLLDDVVFQRLTETEDMYP-LVVGDGCPPGDARGVVHADDFFPLLERQVDLALTVVTIGGSYVQK-FMFPQDP 906
Cdd:pfam01728   65 gvtfiQGDIRDPETLDLLEELLGRKVdLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFVCKvFQGEDFS 144
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1110865247  907 RsavLLRRVARVFETVKLVRPCSTRPASDEFYVVAL 942
Cdd:pfam01728  145 E---LLYLLKLGFEKVGVFKPPASRPESSEEYLVCL 177
Vmethyltransf pfam01660
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ...
85-413 6.06e-21

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


Pssm-ID: 396298  Cd Length: 308  Bit Score: 95.83  E-value: 6.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247   85 VDYVLTDSEKsvmkKMYPQYLLEFTGK--IRHEHAFSAAtrdadERMFLDEFRGMRQSqhYDVMVKDIGGNPGRHLTRGR 162
Cdd:pfam01660    1 FPYALSPEAQ----ELLENLGIEFSPYsvTPHSHPAAKA-----LENLLLEVLPSYLP--NPSTVLDIKGSKLRHLKRGN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  163 LNVHSCFPRLRPADQVRHTRFMadmarfrpdlrgrdsrcVYNNYLRGINLCSR--VAEECRVTAP---YLISVHSAYDMG 237
Cdd:pfam01660   70 PNVHCCNPILDPRDVARYPEAF-----------------SLEKSLGNGEDLRPtnTFEDCRVLAPttsYAFMHDSLHDWS 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  238 REKLASAMISADA-NILRGSMIFHPDVLVFDK-GLIPD---QEMHFQRFerngvpyirFFHP---MGGStdYTHDYrKYI 309
Cdd:pfam01660  133 PEELADLFLRKPKlERLYATLVFPPELLFGDKeSLYPElytFWYKGDRF---------HFYPdghLGGS--YTHPL-NLL 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  310 ELIETIGFTHRGFD-FSVEIDQMCGGRIIFTMFRhyASGVPRGVESRTIQLGHDDKLVV----YYWRARDPGVGIWsflp 384
Cdd:pfam01660  201 SWLTTSKIHLPGGFtYTVERLESRGAHHLFKITR--GDGLTPKVIVPDSRTFGPFEAVLlpkiFVPRVLNYIRGKP---- 274
                          330       340
                   ....*....|....*....|....*....
gi 1110865247  385 fvnqtrlsrvrmvVPKKLFEKMYTYATTL 413
Cdd:pfam01660  275 -------------IPLTVVNKLFSYLRSL 290
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
593-700 4.67e-10

OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438613 [Multi-domain]  Cd Length: 108  Bit Score: 58.77  E-value: 4.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  593 VEIPVAADGNCFFHALR-AVGASALDpvsLRQKLlaaRDSwglePYLASEQVSRLtDFSEKPLVphWADETTFLVAARVL 671
Cdd:cd22792      1 KVVPVPGDGNCFWHSLGhFLGLSALE---LKKLL---RDS----LFDDPELDEEL-DEQLEPGV--YAEDEAIAAAAKLF 67
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1110865247  672 GVTICLH--MRGTVRRY---GKGPVFHLQLTSEH 700
Cdd:cd22792     68 GVNICVHdpDEGVLYTFtpnESSKSIHLLLENEH 101
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
762-942 7.99e-10

23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 60.85  E-value: 7.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  762 GYVCRSGVKLAEICYRFpALLKNVTAALDLCAGPGGFTQFLVSR----GLVVsyvnceryvpmiyrstaAVDVSE----G 833
Cdd:COG0293     29 GYRSRAAYKLLEIDEKD-KLIKPGMRVVDLGAAPGGWSQVAAKRvggkGRVI-----------------ALDLLPmepiP 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  834 G-----GDLLDDVVFQRLTETEDMYP--LVVGDGCPP--G----DARGVVHaddffpLLERQVDLALTVVTIGGSYVQKf 900
Cdd:COG0293     91 GvefiqGDFREDEVLDQLLEALGGRKvdLVLSDMAPNtsGhksvDHARSMY------LVELALDFARKVLKPGGAFVVK- 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1110865247  901 MFpQDPRSAVLLRRVARVFETVKLVRPCSTRPASDEFYVVAL 942
Cdd:COG0293    164 VF-QGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAK 204
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
762-941 1.19e-08

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;


Pssm-ID: 183025  Cd Length: 209  Bit Score: 57.44  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  762 GYVCRSGVKLAEICYRfPALLKNVTAALDLCAGPGGFTQFLVS----RGLVVSyvnCErYVPMiyRSTAAVDVSEGggDL 837
Cdd:PRK11188    30 GLRSRAWFKLDEIQQS-DKLFKPGMTVVDLGAAPGGWSQYAVTqigdKGRVIA---CD-ILPM--DPIVGVDFLQG--DF 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  838 LDDVVFQRLTET--EDMYPLVVGDGCPPGDARGVVHADDFFPLLERQVDLALTVVTIGGSYVQKFMfpQDPRSAVLLRRV 915
Cdd:PRK11188   101 RDELVLKALLERvgDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALDMCRDVLAPGGSFVVKVF--QGEGFDEYLREI 178
                          170       180
                   ....*....|....*....|....*.
gi 1110865247  916 ARVFETVKLVRPCSTRPASDEFYVVA 941
Cdd:PRK11188   179 RSLFTKVKVRKPDSSRARSREVYIVA 204
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
1544-1615 2.93e-03

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 42.66  E-value: 2.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1110865247 1544 LVHGYnATTVHSFQGKEAKHVAVVrLSSnaQDEIYLREEYALVALTRHTTRLVYFTmcTTDALARLIASVPS 1615
Cdd:COG0507    439 LELAY-AITVHKSQGSTFDRVILV-LPS--EHSPLLSRELLYTALTRARELLTLVG--DRDALARAVRRDTA 504
 
Name Accession Description Interval E-value
Kitaviridae_RdRp cd23254
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Kitaviridae of ...
1907-2173 5.36e-145

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


Pssm-ID: 438104  Cd Length: 267  Bit Score: 451.22  E-value: 5.36e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1907 TSYEFMIKRDVKPDLTNNAAYTYSALQTVLSHPKTINAITCPMIRRLKERILGALPSNILFFTEVTPDEFCEKISRVIPP 1986
Cdd:cd23254      1 NVYSFMIKRNPKPNLTVDAAYKYPALQTIAYHDKDINAIFCPIFRELKKRLLAVLKPNFVIFTDMSPEDFEELLNRRFPP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1987 ALSATIRQSLEVDISKYDKSQGIVALVYECRMMKFFGVPDWFVSMWFRGHIATTFSDPTTGIRGRIAFQRKSGDASTYLG 2066
Cdd:cd23254     81 EVLSKLLHKLEIDISKYDKSQGELALLFECKLMRRFGVPEELVELWFNAHVLTTLYDRTNKLKALVEYQRKSGDASTFFG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2067 NTMFLLGVLLATFKYSEMDLLLCSGDDSLILGRDFDAGVDVQDFNLIFNLETKFLRYQHYYFCSKYLFSDGQRWWLVPDP 2146
Cdd:cd23254    161 NTLFLMAVLADLFDLSDLELALFSGDDSLLFGRNLLDYDDSQHFALKFNLESKFLNYKYPYFCSKFLLPVGGRWYFVPDP 240
                          250       260
                   ....*....|....*....|....*..
gi 1110865247 2147 VKVMVKLGRHDLVNWEHCEEYRVSYSD 2173
Cdd:cd23254    241 VKLLTKLGRHDLVNWEHVEEYRISLKD 267
RdRP_2 pfam00978
RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The ...
1784-2221 3.33e-97

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


Pssm-ID: 395779  Cd Length: 440  Bit Score: 321.90  E-value: 3.33e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1784 SEDLNVPISNVSVLPYRDVYVPPRYDS-LRPRLITSMPRRRPTTMRESLVALLKRNANVPDMAGVVDIPALVSRMFESVV 1862
Cdd:pfam00978    1 TSDISLDLDDCRLDPSKSKPKPKDKEPyLVPVLRTAAPSPRQNTLKEVLLALKKRNFNVPELQESVDLDDTAERVAERFK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1863 AVLMKTD----FDEIQLSAGDIADWLHDQ-PPAVAEKLLEPLG-THEMEMTSYEFMIKRDVKPDLTNNAAYTYSALQTVL 1936
Cdd:pfam00978   81 KSFLDKEkldkLDPIINTTENVSRWLDKQsGKKAAQLKLDDLVpLHEVDLDRYKHMIKSDVKPKLDLSPQSERPALQTIT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1937 SHPKTINAITCPMIRRLKERILGALPSNILFFTEVTPDEFCEKisrvipPALSATIRQSLEVDISKYDKSQGIVALVYEC 2016
Cdd:pfam00978  161 YHDKGVTAYFSPIFRELFERLLYVLKPKIVFPTGMTSSLIAEH------FEFLDASEDFLEIDFSKFDKSQGELHLLVQL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2017 RMMKFFGVPDWFVSMWFRGHIATTFSDPTTGIRGRIAFQRKSGDASTYLGNTMFLLGVLLATFKYSEMDLLLCSGDDSLI 2096
Cdd:pfam00978  235 EILKLLGLDPELADLWFKFHRQSYIKDRKNGVGFSVDYQRKSGDANTYLGNTLVTMAMLASVYDLEKIDCAAFSGDDSLI 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2097 LGRDFDAGvDVQDFNLIFNLETKFLRYQHYYFCSKYLFSDGQRWWLVPDPVKVMVKLGR-HDLVNWEHCEEYRVSYSDNV 2175
Cdd:pfam00978  315 FSPKPIED-PASRFATLFNMEAKVFDPSVPYFCSKFLLEVDGGAFFVPDPLKLLQKLGKkKIPDDEQHLDEIFTSLCDLT 393
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1110865247 2176 VAYADARVATVLAR-AVRERYAYADVNIETLISALHVIASPDYFSSL 2221
Cdd:pfam00978  394 KSFNDDCVVLELLDlAVARYYKYAPEGYAALCALHKALSSFTLFFSL 440
Virgaviridae_RdRp cd23251
RNA-dependent RNA polymerase (RdRp) in the family Virgaviridae of positive-sense ...
1767-2193 8.22e-95

RNA-dependent RNA polymerase (RdRp) in the family Virgaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Virgaviridae, order Martellivirales. The Virgaviridae is a family of plant viruses with rod-shaped virions, a (+)ssRNA genome with a 3'-terminal tRNA-like structure and a replication protein similar to those of the alpha-like supergroup. Plants serve as natural hosts. The name of the family is derived from the Latin word virga (rod), as all viruses in this family are rod-shaped. There are currently 59 species in this family, divided among seven genera: Goravirus, Furovirus, Hordeivirus, Pecluvirus, Pomovirus, Tobamovirus, and Tobravirus. 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: 438101  Cd Length: 427  Bit Score: 314.17  E-value: 8.22e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1767 FPGCVYVNQDFDTLQFHSEDLNVPISNVSVLPYRDVYVPPRYDSLRPRLITSMPRRRPTTMRESLVALLKRNANVPDMAG 1846
Cdd:cd23251      1 FPGNSTRDSDFDGYTVATSDINLNVEDCTLDPSKSVKVWQEKEGLKPVLRTAMPEKRQNGLLESLLALIKRNMAAPKLQG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1847 VVDIpalvSRMFESVVAVLMKTDFDEIQLSAGDIAD------WLHDQPPAVAEKLL-EPLGTHEMEMTSYEFMIKRDVKP 1919
Cdd:cd23251     81 AVNE----FETIERVIKKAKDVFFDEDLIDRSPLSTresflrWWDKQSTTARAQLLaDDRVLDEIDVCTYNFMIKNDVKP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1920 DLTNNAAYTYSALQTVLSHPKTINAITCPMIRRLKERILGALPSNILFFTEVTPDEFCEKISrVIPPALSAtirQSLEVD 1999
Cdd:cd23251    157 KLDLSPQSEYAALQTVVYPDKIVNALFGPIFKEINERILSALDPHVVFNTRMTAEELNETVE-FLDPDEEY---DALEID 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2000 ISKYDKSQGI--VALVYEcrMMKFFGVPDWFVSMWFRGHIATTFSDPTTGIRGRIAFQRKSGDASTYLGNTMFLLGVLLA 2077
Cdd:cd23251    233 FSKFDKSKTSlhIRAVIE--LYKLFGLDGMLAFLWEKSQCQTTVKDRQNGIKAYLLYQQKSGNCDTYGSNTWSAALALLS 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2078 TFKYSEMDLLLCSGDDSLILgrdFDAGVDVQD----FNLIFNLETKFLRYQHYYFCSKYLFSDGQRWWLVPDPVKVMVKL 2153
Cdd:cd23251    311 MLPLEKAIFMIFGGDDSLIL---FPKGLVIPDpcrrLASLWNFECKLFKFKYGYFCGKFLLKHGDGYIFYPDPLKLITKL 387
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1110865247 2154 GRHDLVNWEHCEEYRVSYSDNVVAYADARVATVLARAVRE 2193
Cdd:cd23251    388 GRKDIKDGEHLSEIFVSICDNYKSYRDYRVLEALDVAVVE 427
Closteroviridae_RdRp cd23253
RNA-dependent RNA polymerase (RdRp) in the family Closteroviridae of positive-sense ...
1907-2155 1.36e-58

RNA-dependent RNA polymerase (RdRp) in the family Closteroviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Closteroviridae, order Martellivirales. Viruses in the family Closteroviridae have a mono-, bi- or tripartite (+)ssRNA genome of 13-19 kb, and non-enveloped, filamentous particles 650-2200 nm long and 12 nm in diameter. They infect plants, mainly dicots, many of which are fruit crops. Members of the family are classified into four genera: Ampelovirus, Closterovirus, Crinivirus and Velarivirus. Their genetic diversity is primarily influenced by strong negative selection and recombination. Closteroviridae viruses are mostly phloem-restricted and induce specific cytoplasmic aggregates of virus particles intermingled with membranous vesicles derived from the endoplasmic reticulum and possibly mitochondria. Their transmission is by aphids, whiteflies, pseudococcid mealybugs or soft scale insects in a semi-persistent manner. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438103  Cd Length: 266  Bit Score: 203.56  E-value: 1.36e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1907 TSYEFMIKRDVKPDLTNNAAYTYSALQTVLSHPKTINAITCPMIRRLKERILGALPSNILFFTEVTPDEFCEKISRVIPP 1986
Cdd:cd23253      1 TSFKLMVKGDMKPKLDSSSLSKYPPGQNIVYHERAINAFFSPIFLEVFDRIKYCLSDKIILYSGMNLEELASLIRSKLGD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1987 ALSATIrqSLEVDISKYDKSQGIVALVYECRMMKFFGVPDWFVSMWFRG---HIATTFsdpTTGIRGRIAFQRKSGDAST 2063
Cdd:cd23253     81 PLDEYK--TVEIDFSKFDKSQGVLFKVYEELVYKFFGFSEELYDNWKCSeyfSCRATS---DSGVSLELGAQRRTGSPNT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2064 YLGNTMFLLGVLLATFKYSEMDLLLCSGDDSLILGRDfDAGVDVQDFNLIFNLETKFLRYQHYYFCSKYLFSDGQRWWLV 2143
Cdd:cd23253    156 WLGNTLVTLGILSSSYDLDDIDLLLVSGDDSLIFSKK-PLPNKANEINLDFGFEAKFIENSVPYFCSKFIIEDRGKIKVV 234
                          250
                   ....*....|..
gi 1110865247 2144 PDPVKVMVKLGR 2155
Cdd:cd23253    235 PDPVKLFEKLSV 246
ps-ssRNAv_Martellivirales_RdRp cd23208
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Martellivirales of ...
1907-2098 6.55e-52

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


Pssm-ID: 438058 [Multi-domain]  Cd Length: 190  Bit Score: 181.41  E-value: 6.55e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1907 TSYEFMIKRDVKPDLTNNAAYTYSALQTVLSHPKTINAITCPMIRRLKERILGALPSNILFFTEVtpdEFCEKISRVIPP 1986
Cdd:cd23208      1 DKYEMMIKSDVKPKLDLTAQQEYPKLQTIVYHDKNITAIFCPIFKELFERLLSCLKKKVVIYTGM---MTSAELNDFISA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1987 ALSATIRQSLEVDISKYDKSQGIVALVYECRMMKFFGVPDWFVSMWFRGHIATTFSDPTTGIRGRIAFQRKSGDASTYLG 2066
Cdd:cd23208     78 LHLESGYYVLEIDFSKFDKSQGALHLLTELLILRRLGVDEPLLVLWEFAHTQSTTRDINNGISFETAYQRKSGDAFTYFG 157
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1110865247 2067 NTMFLLGVLLATFKYSEMDLLLCSGDDSLILG 2098
Cdd:cd23208    158 NTLVTMAALLDVLDLEKIVCIAFGGDDSLIFS 189
Bromoviridae_RdRp cd23252
RNA-dependent RNA polymerase (RdRp) in the family Bromoviridae of positive-sense ...
1811-2154 8.37e-44

RNA-dependent RNA polymerase (RdRp) in the family Bromoviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Bromoviridae, order Martellivirales. The Bromoviridae family of plant viruses contains tri-segmented, (+)ssRNA viruses with a total genome size of about 8 kb. There are six genera in this family: Alfamovirus, Anulavirus, Bromovirus, Cucumovirus, Ilarvirus, and Oleavirus. Bromoviridae virions are variable in morphology (spherical or bacilliform) and are transmitted mechanically, in/on the pollen and non-persistently by insect vectors. Members of the family cause major disease epidemics in fruit, vegetable and fodder crops such as tomato, cucurbits, bananas, and alfalfa. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438102  Cd Length: 332  Bit Score: 163.55  E-value: 8.37e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1811 LRPRLITSMPRRRPTTMRESLVALLKRNANVPDMAGVVDIPAL----VSRMFESVVavlmktDFDEIQlsagdiadwlhd 1886
Cdd:cd23252     26 LEPVLNTGSGSKRVGTQREALLAIKKRNANVPELGDSVDLDRVsnavANRFLTTVI------DVDRLD------------ 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1887 qppavaeklleplgthememtSYEFMIKRDVKPDLTNN--------AAYTYsalqtvlsHPKTINAITCPMIRRLKERIL 1958
Cdd:cd23252     88 ---------------------KYMHMIKSDLKPVEDDSlhverpvpATITY--------HKKGIVMQFSPLFLAAFERLL 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1959 GALPSNIlffteVTPdefCEKISRV--IPPALSATIRQSLEVDISKYDKSQGIVALVYECRMMKFFGVPDWFVSMWFRGH 2036
Cdd:cd23252    139 RCLRSKI-----VIP---SGKIHQLfmIDPSVLNASKHFKEIDFSKFDKSQGELHHEIQEHILNALGCPAPFTKWWFDFH 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2037 IATTFSDPTTGIRGRIAFQRKSGDASTYLGNTMfllgVLLATFKY------SEMDLLLCSGDDSLILGRDFDAGVDVQDF 2110
Cdd:cd23252    211 RRSYISDRRAGVGFSVDFQRRTGDAFTYLGNTL----VTLAELAYvydlddPNFDFVVASGDDSLIGSVEPLPRDDEDLF 286
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1110865247 2111 NLIFNLETKFLRYQHyYFCSKYLFSD---GQRWWLVPDPVKVMVKLG 2154
Cdd:cd23252    287 TTLFNFEAKFPHNQP-FICSKFLLSDefgDENVFSVPDPLKLLQRLG 332
Mayoviridae_RdRp cd23256
RNA-dependent RNA polymerase (RdRp) in the family Mayoviridae of positive-sense ...
1891-2195 8.27e-40

RNA-dependent RNA polymerase (RdRp) in the family Mayoviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Mayoviridae, order Martellivirales. The Mayoviridae family consists of two genera, Idaeovirus and Pteridovirus. The genus Idaeovirus contains Raspberry bushy dwarf virus (RBDV), named after the host with which it was first associated (red raspberry, Rubus idaeu) and the disease which is characterized by bushiness (stunting and proliferation of canes); RBDV has recently been found causing an infection in grapevines. RBDV occurs in all tissues of the plant, including seed and pollen, and is transmitted in association with pollen, both vertically to the seed and horizontally to the pollinated plant; this is the only known method of natural spread of RBDV. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438106  Cd Length: 329  Bit Score: 151.82  E-value: 8.27e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1891 VAEKLLEPLGTHEMEMTSYEFMIKRDVKPDLTNNAAYTYSALQTVLSHPKTINAITCPMIRRLKERILGALPSNIlffte 1970
Cdd:cd23256     17 VGNKVNDPVVLALTSLNKYSHMIKRDRKPVLTTAVQSEYTKAATITYHDKDITQVATPIFRQFKTRLLACKKSNL----- 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1971 VTPDEFCEKISR-VIPPALSATIRQSLEVDISKYDKSQGIVALVYECRMMKFFGVPDWFVSMWFRGHIATTFSDPTTGIR 2049
Cdd:cd23256     92 CIPLDHDHDISGwLTNRHLGSENGTFTEIDFSKFDKSQGELHQLIQDLILLRFGCDPEFVSLWSTAHRSSSIKDQNVGIS 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2050 GRIAFQRKSGDASTYLGNTMFLLGVL---LATFKYSEMDLLLCSGDDSLILGRDfDAGVDVQDFNLIFNLETKFLRYQHY 2126
Cdd:cd23256    172 FKTDFQRRTGDAFTFLGNSLVTAVMLayvLSFEDEKKIRYMLVGGDDSLICSYG-PISVPLEPLSTIFNMSCKLIQPSCP 250
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2127 YFCSKYLFSDGQRWWLVPDPVKVMVKLGRHDLV-NWEHCEEYRVSYSDNVVAYADARVATVLARAVRERY 2195
Cdd:cd23256    251 YFASRYIIRVGDEILCVPDPYKLLVKMGRKDIPdNEASLEEVRTGLADSAKPLFDDEVKQKLSILVQIRY 320
Viral_helicase1 pfam01443
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ...
1353-1599 8.99e-37

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


Pssm-ID: 366646 [Multi-domain]  Cd Length: 227  Bit Score: 139.44  E-value: 8.99e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1353 KLVQAAAGCGKTTDIVRKARvtrDAVILAGTVEgreDIERRLGDS-NVRVRTIQSFLLS--PFVCRVLFIDEAMMQHPGM 1429
Cdd:pfam01443    1 IVVHGVPGCGKSTLIRKLLR---TSRVIRPTAE---LRTEGKPDLpNLNVRTVDTFLMAllKPTGKILILDEYTLLPPGY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1430 VVLAAHLSGAAEVYAYGDRCQIPFVNRARQFYvkytnLADSFPTVAHLM---RSYRCPVSVAARLHDRYLSatGVGMTSV 1506
Cdd:pfam01443   75 ILLLAAISGAKLVILFGDPLQIPYHSRAPSFL-----IPHFPSSLSHRVgrrTTYLLPSLRAPILSAKGFE--VVVERSG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1507 RDQRDGEELKVITGldavpragfdVYLTFKQSEKQTllvHGYNATTVHSFQGKEAKHVAVVRLSSNAQDEIYLREEYALV 1586
Cdd:pfam01443  148 EYKVDYDPNGVLVL----------VYLTFTQALKES---LGVRVTTVHEVQGLTFDSVTLVLDTDTDLLIISDSPEHLYV 214
                          250
                   ....*....|...
gi 1110865247 1587 ALTRHTTRLVYFT 1599
Cdd:pfam01443  215 ALTRHRKSLHILT 227
ps-ssRNAv_Alsuviricetes_RdRp cd23182
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the class Alsuviricetes of ...
1907-2098 1.01e-29

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


Pssm-ID: 438032 [Multi-domain]  Cd Length: 187  Bit Score: 117.70  E-value: 1.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1907 TSYEFMIKRDVKPDlTNNAAYTYSALQTVLSHPKTINAITCPMIRRLKERILGALPSNILFFTEvtPDEFCEKISRVIPP 1986
Cdd:cd23182      1 TDIDFLIKTQQKVS-PKTPFNTGKAGQTIAAHSKSINFVLGPWIRYLEERLRDGSRTHRYSNGL--MDEEEAMLSQWKIN 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1987 ALSATirQSLEVDISKYDKSQGIVALVYECRMMKFFGVPDWFVSMWFRGHIATTFSDPTTGIRGRIAFQRKSGDASTYLG 2066
Cdd:cd23182     78 HVPHA--TFVSNDYTAFDKSHNGESLLLEAAIMRRIGTPAAAPNLFIELHGKRTLRAKVLGGSGELDGMRDSGAAWTYCR 155
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1110865247 2067 NTMFLLGVLLATFKYSEMDLLLcSGDDSLILG 2098
Cdd:cd23182    156 NTDYNLAVMLSLYRLKVKPAAF-SGDDSLLCG 186
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
763-942 1.19e-21

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 94.19  E-value: 1.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  763 YVCRSGVKLAEICYRFPaLLKNVTAALDLCAGPGGFTQFLVSRGlvvsyvnceryVPMIYrstaAVDVSEG--------- 833
Cdd:pfam01728    1 YRSRAAYKLLEIDEKFG-LLKPGKTVLDLGAAPGGWSQVALQRG-----------AGKVV----GVDLGPMqlwkprndp 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  834 -----GGDLLDDVVFQRLTETEDMYP-LVVGDGCPPGDARGVVHADDFFPLLERQVDLALTVVTIGGSYVQK-FMFPQDP 906
Cdd:pfam01728   65 gvtfiQGDIRDPETLDLLEELLGRKVdLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFVCKvFQGEDFS 144
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1110865247  907 RsavLLRRVARVFETVKLVRPCSTRPASDEFYVVAL 942
Cdd:pfam01728  145 E---LLYLLKLGFEKVGVFKPPASRPESSEEYLVCL 177
Vmethyltransf pfam01660
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ...
85-413 6.06e-21

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


Pssm-ID: 396298  Cd Length: 308  Bit Score: 95.83  E-value: 6.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247   85 VDYVLTDSEKsvmkKMYPQYLLEFTGK--IRHEHAFSAAtrdadERMFLDEFRGMRQSqhYDVMVKDIGGNPGRHLTRGR 162
Cdd:pfam01660    1 FPYALSPEAQ----ELLENLGIEFSPYsvTPHSHPAAKA-----LENLLLEVLPSYLP--NPSTVLDIKGSKLRHLKRGN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  163 LNVHSCFPRLRPADQVRHTRFMadmarfrpdlrgrdsrcVYNNYLRGINLCSR--VAEECRVTAP---YLISVHSAYDMG 237
Cdd:pfam01660   70 PNVHCCNPILDPRDVARYPEAF-----------------SLEKSLGNGEDLRPtnTFEDCRVLAPttsYAFMHDSLHDWS 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  238 REKLASAMISADA-NILRGSMIFHPDVLVFDK-GLIPD---QEMHFQRFerngvpyirFFHP---MGGStdYTHDYrKYI 309
Cdd:pfam01660  133 PEELADLFLRKPKlERLYATLVFPPELLFGDKeSLYPElytFWYKGDRF---------HFYPdghLGGS--YTHPL-NLL 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  310 ELIETIGFTHRGFD-FSVEIDQMCGGRIIFTMFRhyASGVPRGVESRTIQLGHDDKLVV----YYWRARDPGVGIWsflp 384
Cdd:pfam01660  201 SWLTTSKIHLPGGFtYTVERLESRGAHHLFKITR--GDGLTPKVIVPDSRTFGPFEAVLlpkiFVPRVLNYIRGKP---- 274
                          330       340
                   ....*....|....*....|....*....
gi 1110865247  385 fvnqtrlsrvrmvVPKKLFEKMYTYATTL 413
Cdd:pfam01660  275 -------------IPLTVVNKLFSYLRSL 290
ps-ssRNAv_Hepelivirales_RdRp cd23209
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Hepelivirales of ...
1907-2098 7.40e-16

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


Pssm-ID: 438059 [Multi-domain]  Cd Length: 183  Bit Score: 77.91  E-value: 7.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1907 TSYEFMIK--RDVKPDLTNNAAytySALQTVLSHPKTINAITCPMIRRLKERILGALPSNILFFTEVTPDEFCEKISrvi 1984
Cdd:cd23209      1 RKITFFQKdcRKFTDCEPVAHG---KAGQGISAWSKELCFVFGPWFRALEKILRRALKPNVLYANGHEAEPFVDKIN--- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1985 ppalSATIRQSLEVDISKYDKSQGIVALVYECRMMKFFGVPDWFVSMWFRGHIATTFSDPttGIRGRIAFQRKSGDASTY 2064
Cdd:cd23209     75 ----QAHSAVFIENDFTEFDSTQNLFSLLVELEILEACGMPPALAELYRALRAKWTLQAR--EGSLEGTCKKTSGEPGTL 148
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1110865247 2065 LGNTMFLLGVLLATFKYSEMDLLLCSGDDSLILG 2098
Cdd:cd23209    149 LHNTIWNMAVMMHMVRGGVRKAAAFKGDDSVVCC 182
Hepeviridae_RdRp cd23259
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Hepeviridae of ...
1939-2102 5.11e-15

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Hepeviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Hepeviridae, order Hepelivirales. The family Hepeviridae includes enterically transmitted small non-enveloped [(+)ssRNA viruses. It includes the genera Piscihepevirus, whose members infect fish, and Orthohepevirus, whose members infect mammals and birds. Members of the genus Orthohepevirus include hepatitis E virus, which is responsible for self-limiting acute hepatitis in humans and several mammalian species; the infection may become chronic in immunocompromised individuals. Avian hepatitis E virus causes hepatitis-splenomegaly syndrome in chickens. Hepeviridae genomes (approximately 7.2 kb) have 5' methyl G caps and 3' poly (A) tails, and contain three ORFS. They have two mRNAs, a genome length and a subgenomic mRNA: the genome-length mRNA is translated to produce proteins required for RNA replication while the subgenomic mRNA is used to produce the capsid protein. Some of the capsid protein is glycosylated, which is an unusual finding for an unenveloped virus. 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: 438109  Cd Length: 274  Bit Score: 77.48  E-value: 5.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1939 PKTINAITCPMIRRLKERILGALPSNILFFTEVTPDEFCEKISrvippalSATIRQSLEVDISKYDKSQGIVALVYECRM 2018
Cdd:cd23259     96 SKTFCALFGPWFRAIEKAIVALLPPNIFYGDAYEESVFSAAVA-------GAGSCRVFENDFSEFDSTQNNFSLGLECEI 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2019 MKFFGVPDWFVSMWFRGHIATTFSDPTTGIRGRiaFQRKSGDASTYLGNTMFLLGVLLATFKYSEMDLLLCSGDDSLILG 2098
Cdd:cd23259    169 MEECGMPQWLVRLYHLVRSAWVLQAPKESLRGF--WKKHSGEPGTLLWNTVWNMAVIAHCYEFRDLAVAAFKGDDSVVLC 246

                   ....
gi 1110865247 2099 RDFD 2102
Cdd:cd23259    247 SDYR 250
Endornaviridae_RdRp cd23255
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Endornaviridae of ...
1938-2113 1.12e-13

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Endornaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Endornaviridae, order Martellivirales. The family Endornaviridae includes viruses with linear (+)ssRNA genomes that range from 9.7 to 17.6 kb. The family consists of two genera, Alphaendornavirus and Betaendornavirus. Alphaendornavirus includes species whose members infect plants, fungi and oomycetes, while the genus Betaendornavirus includes species whose members infect ascomycete fungi. Plant endornaviruses are transmitted only through the gametes. A conserved RNA-dependent RNA polymerase domain located in the C-terminal region of the polyprotein is a feature common to all endornaviruses. 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: 438105  Cd Length: 237  Bit Score: 72.95  E-value: 1.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1938 HPKTINAITCPMIRRLKERILGALPSNILFFTEVTPDEfcekisrvippaLSATIRQS------LEVDISKYDK--SQGI 2009
Cdd:cd23255     64 QRKGICAIFSPIFNEAKKRLKSLLKPKVVYADGLTPDE------------LSARLRLVknvkyfFEDDLSKQDRqtDKPI 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2010 VAlvYECRMMKFFGVPDWFVSMWFRGHIATTFSdpTTGIRGRIAFQRKSGDASTYLGNTMFLLGVLLATFKY--SEMDLL 2087
Cdd:cd23255    132 ID--VEMELYKLLGVDPNVIELWREVHENWRFK--GKGVRGVGDAMRLTGQATTALGNVITNLLVHSRLVKRngSNLKLM 207
                          170       180
                   ....*....|....*....|....*.
gi 1110865247 2088 LCSGDDSLILgrdFDAGVDVQDFNLI 2113
Cdd:cd23255    208 LVLGDDNLIL---TDTKIDLENLRKE 230
ps-ssRNA_RdRp_Tymovirales cd23207
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Tymovirales of ...
1948-2099 6.03e-11

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Tymovirales of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the order Tymovirales. The Tymovirales order contains viruses that mostly infect plants, have a single molecule of (+)ssRNA, and which are united by the similarities in their replication-associated polyproteins. Tymovirales contains five families (Alpha-, Beta-, Delta- and Gammaflexiviridae and Tymoviridae) and groups mostly plant-infecting agents, although a few Tymovirales members have either fungal or insect hosts. Botrytis virus F (BVF), isolated from the fungus Botrytis cinerea, is a flexuous mycovirus that is typical of members of the genus Mycoflexivirus (family Gammaflexiviridae). The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438057 [Multi-domain]  Cd Length: 188  Bit Score: 63.58  E-value: 6.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1948 PMIRRLKERILGALPSNILFFTEVTPDEFCEKISRVIPPalsatiRQSLEVDISKYDKSQGIVALVYECRMMKFFGVPDW 2027
Cdd:cd23207     49 PYARYMRRFINADLPPNIYIHCGKTPEDLSKWCKEHWQH------GPSTANDYTAFDQSQDGEFVVFEVLLMRHLHIPDD 122
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1110865247 2028 FVSMW--FRGHIATTFsdpttgirGRIAFQRKSGDASTYLGNTMFLLGVLLATFKYSEMDLLLCSGDDSLILGR 2099
Cdd:cd23207    123 LIELYvdIKTNAYSHL--------GPLSIMRLTGEPGTFDFNTDYNLALTYAKYDLPPGTPICFSGDDSVANGT 188
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
593-700 4.67e-10

OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438613 [Multi-domain]  Cd Length: 108  Bit Score: 58.77  E-value: 4.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  593 VEIPVAADGNCFFHALR-AVGASALDpvsLRQKLlaaRDSwglePYLASEQVSRLtDFSEKPLVphWADETTFLVAARVL 671
Cdd:cd22792      1 KVVPVPGDGNCFWHSLGhFLGLSALE---LKKLL---RDS----LFDDPELDEEL-DEQLEPGV--YAEDEAIAAAAKLF 67
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1110865247  672 GVTICLH--MRGTVRRY---GKGPVFHLQLTSEH 700
Cdd:cd22792     68 GVNICVHdpDEGVLYTFtpnESSKSIHLLLENEH 101
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
762-942 7.99e-10

23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 60.85  E-value: 7.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  762 GYVCRSGVKLAEICYRFpALLKNVTAALDLCAGPGGFTQFLVSR----GLVVsyvnceryvpmiyrstaAVDVSE----G 833
Cdd:COG0293     29 GYRSRAAYKLLEIDEKD-KLIKPGMRVVDLGAAPGGWSQVAAKRvggkGRVI-----------------ALDLLPmepiP 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  834 G-----GDLLDDVVFQRLTETEDMYP--LVVGDGCPP--G----DARGVVHaddffpLLERQVDLALTVVTIGGSYVQKf 900
Cdd:COG0293     91 GvefiqGDFREDEVLDQLLEALGGRKvdLVLSDMAPNtsGhksvDHARSMY------LVELALDFARKVLKPGGAFVVK- 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1110865247  901 MFpQDPRSAVLLRRVARVFETVKLVRPCSTRPASDEFYVVAL 942
Cdd:COG0293    164 VF-QGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAK 204
Togaviridae_RdRp cd23250
RNA-dependent RNA polymerase (RdRp) in the family Togaviridae of positive-sense ...
1805-2214 6.96e-09

RNA-dependent RNA polymerase (RdRp) in the family Togaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Togaviridae, order Martellivirales. Togaviridae is a family of small, enveloped viruses with [(+)ssRNA] genomes of 10-12 kb, and contains a single genus, Alphavirus. Alphavirus includes a large number of species that are mostly mosquito-borne and pathogenic in their vertebrate hosts. Many are important human and veterinary pathogens (e.g., chikungunya virus, eastern equine encephalitis virus). The genus Alphavirus mainly consists of mosquito-borne viruses although other hematophagous insects, including ticks, lice, and cliff swallow bugs, have been implicated in transmission. Vertebrate hosts include humans, non-human primates, equids, birds, amphibians, reptiles, rodents, and pigs. There are two aquatic alphaviruses, southern elephant seal virus and salmon pancreas disease virus, infecting sea mammals and fish respectively. Interestingly, Eilat virus (EILV) has been shown to only infect insect cells and is incapable of replicating in vertebrate cells. 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: 438100  Cd Length: 458  Bit Score: 60.55  E-value: 6.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1805 PPRYDSLRPRLITSMPRRRPTTMRESLVALLKRNANVPDMAgvvDIPALVSRMFEsvVAVLMK-----TDFDE-----IQ 1874
Cdd:cd23250     23 PKKHAYHQPQIRSAVPSPFQNTLQNVLAAATKRNCNVTQMR---ELPTLDSAAFN--VECFKKfacnnEYWEEfkekpIR 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1875 LSAGDIADWL-HDQPPAVAEKL-----LEPLgtHEMEMTSYEFMIKRDVKpdLTNNAAYTYS--ALQTVLSHPKTINAIT 1946
Cdd:cd23250     98 LTTENVTTYVtKLKGPKAAALFakthnLVPL--QEVPMDRFVMDMKRDVK--VTPGTKHTEErpKVQVIQAADPLATAYL 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1947 CPMIRRLKERILGALPSNILFFTEVTPDEFCEKISRVIPPALSAtirqsLEVDISKYDKSQGIVALVYECRMMKFFGVPD 2026
Cdd:cd23250    174 CGIHRELVRRLNAVLLPNIHTLFDMSAEDFDAIIAEHFQPGDKV-----LETDIASFDKSQDDAMALTALMILEDLGVDQ 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2027 WFVSMwfrghIATTFSDPT-----TGIRGRIAFQRKSGDASTYLGNTmfLLGVLLATFKYSEMdlLLCS------GDDSL 2095
Cdd:cd23250    249 ELLDL-----IEAAFGEITsvhlpTGTRFKFGAMMKSGMFLTLFVNT--VLNIVIASRVLRER--LTNSrcaafiGDDNI 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2096 ILGRDFDAgVDVQDFNLIFNLETKFLRY----QHYYFCSKYLFSDG--QRWWLVPDPVKVMVKLGRHDLVNWEHCEEYRV 2169
Cdd:cd23250    320 VHGVVSDK-LMADRCATWLNMEVKIIDAvigeKPPYFCGGFILYDSvtGTACRVADPLKRLFKLGKPLPADDEQDEDRRR 398
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1110865247 2170 SYSDNVVAYADARVATVLARAVRERYAYadVNIETLISALHVIAS 2214
Cdd:cd23250    399 ALHDEVKRWFRVGITSELEVAVESRYEV--NGLSNILLAMATLAQ 441
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
762-941 1.19e-08

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;


Pssm-ID: 183025  Cd Length: 209  Bit Score: 57.44  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  762 GYVCRSGVKLAEICYRfPALLKNVTAALDLCAGPGGFTQFLVS----RGLVVSyvnCErYVPMiyRSTAAVDVSEGggDL 837
Cdd:PRK11188    30 GLRSRAWFKLDEIQQS-DKLFKPGMTVVDLGAAPGGWSQYAVTqigdKGRVIA---CD-ILPM--DPIVGVDFLQG--DF 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  838 LDDVVFQRLTET--EDMYPLVVGDGCPPGDARGVVHADDFFPLLERQVDLALTVVTIGGSYVQKFMfpQDPRSAVLLRRV 915
Cdd:PRK11188   101 RDELVLKALLERvgDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALDMCRDVLAPGGSFVVKVF--QGEGFDEYLREI 178
                          170       180
                   ....*....|....*....|....*.
gi 1110865247  916 ARVFETVKLVRPCSTRPASDEFYVVA 941
Cdd:PRK11188   179 RSLFTKVKVRKPDSSRARSREVYIVA 204
Gammaflexiviridae_RdRp cd23249
RNA-dependent RNA polymerase (RdRp) in the family Gammaflexiviridae of positive-sense ...
1911-2099 2.45e-07

RNA-dependent RNA polymerase (RdRp) in the family Gammaflexiviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Tymovirales; This group contains the RdRp of RNA viruses belonging to the family Gammaflexiviridae, order Tymovirales. Virions within the Gammaflexiviridae family are flexuous filaments of 720 nm modal length and about 13 nm in diameter. Members of the Tymovirales order are mainly plant pathogens that are characterized by similarities in their replication-associated polyproteins, which account for the majority of their genomic coding capacity. They are considered to form a group, phylogenetically, referred to as flexiviruses, with filamentous virions. 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: 438099  Cd Length: 354  Bit Score: 55.29  E-value: 2.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1911 FMIKRDVKPDLTNNAAYTysALQTVLSHPKTINAITCPMIRRLKERILGALPSNILFFTEVTPDEFCEKISRVIPPALsa 1990
Cdd:cd23249     76 FIKGQTVTKLGKMGSDAT--AGQSIASFRAQVLLAWGPLARYLDRRIRALLPPHIYIHSGRTNEDFERFVAAHWDFTR-- 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1991 tirQSLEVDISKYDKSQGIVALVYECRMMKFFGVP----DWFVSMwfRGHIATTFsdpttgirGRIAFQRKSGDASTYLG 2066
Cdd:cd23249    152 ---ESTEGDYTAFDASQDADFLNFETLLMRALGVPldliEAYLEM--KASITSHL--------GPLAIMRFSGEVWTYLF 218
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1110865247 2067 NTMFLLGVLLATFKYSEMDLLLCSGDDSLILGR 2099
Cdd:cd23249    219 NTLGNMAYTAAKYEVPPPVPRVYGGDDKSINSR 251
Tymoviridae_RdRp cd23247
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Tymoviridae of ...
1962-2098 9.76e-07

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Tymoviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Tymovirales; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Tymoviridae, order Tymovirales. Virions of the family Tymoviridae are isometric, non-enveloped, about 30 nm in diameter, and contain a single molecule of (+)ssRNA constituting 25#35% of the particle weight. There are 42 species in this family, assigned to three genera (Maculavirus, Marafivirus, and Tymovirus), with two species unassigned to a genus. Members of the Tymovirales order are mainly plant pathogens that are characterized by similarities in their replication-associated polyproteins, which account for the majority of their genomic coding capacity. They are considered to form a group, phylogenetically, referred to as flexiviruses, with filamentous virions. 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: 438097  Cd Length: 373  Bit Score: 53.35  E-value: 9.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1962 PSNILFFTEVTPDEFCEKISRVIPPALSATirqsleVDISKYDKSQGIVALVYECRMMKFFGVPDWFVSM--WFRGHIAT 2039
Cdd:cd23247    142 PPNIYIHAGHTPSQLSSWCQSHLKSSVSLA------NDYTAFDQSQHGEAVVFERLKMERLSIPQHLIDLhvHLKTNVST 215
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1110865247 2040 TFsdpttgirGRIAFQRKSGDASTYLGNTMFLLGVLlatfkYSEMDL----LLCSGDDSLILG 2098
Cdd:cd23247    216 QF--------GPLTCMRLTGEPGTYDDNTDYNLAVI-----YSQYDIsstpIMVSGDDSVIDG 265
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
595-678 4.86e-06

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 47.82  E-value: 4.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  595 IPVAADGNCFFHAL-RAVGASALDPVSLRQK----LLAARDSWGLEPYLASEQVSRLTDFSEKPLVP-HWADETTFLVAA 668
Cdd:cd22744      3 VDVPGDGNCLFRALaHALYGDQESHRELRQEvvdyLRENPDLYEPAELADEDDGEDFDEYLQRMRKPgTWGGELELQALA 82
                           90
                   ....*....|
gi 1110865247  669 RVLGVTICLH 678
Cdd:cd22744     83 NALNVPIVVY 92
Benyviridae_RdRp cd23257
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Benyviridae of ...
1909-2079 1.13e-05

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


Pssm-ID: 438107 [Multi-domain]  Cd Length: 188  Bit Score: 48.38  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1909 YEFMIKrDVKPDLTNNAAYTYSALQTVLSHPKTINAITCPMIRRLKERILGALPSNILFFTEVTPDEFCEKISRVIPPAL 1988
Cdd:cd23257      3 YRFQLK-DIEKPLKDPETDLAKAGQGILAWSKEAHVKFMVAFRVLNDLLLKSLNSNVVYDNTMSETEFVGKINAAMNTVP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1989 SATIRQSleVDISKYDKSQGIVALVYECRMMKFFGVPDWFVSMWF--RGHiattFSDPTTGIRGRIAFQRKSGDASTYLG 2066
Cdd:cd23257     82 DSAINGV--IDAAACDSGQGVFTQLIERYIYAALGISDFFLDWYFsfREK----YVMQSRYVRAHMSYVKTSGEPGTLLG 155
                          170
                   ....*....|...
gi 1110865247 2067 NTMfLLGVLLATF 2079
Cdd:cd23257    156 NTI-LMGAMLNAM 167
Carmotetraviridae_RdRp cd23205
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Carmotetraviridae ...
2046-2152 8.21e-04

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Carmotetraviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, and related Erinaceus virus H14; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Carmotetraviridae, and related Erinaceus virus H14, order Tolivirales. Carmotetraviridae includes only one genus, Alphacarmotetravirus, which has one species: Providence virus. Lepidopteran insects serve as the natural host. Recent studies indicated that Providence virus, a non-enveloped insect RNA virus, isolated from a lepidopteran midgut cell line can establish a productive infection in plants as well as in animal cells. 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: 438055  Cd Length: 268  Bit Score: 43.46  E-value: 8.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2046 TGIRGRIAFQRKSGDASTYLGNTmfllgVLLATFKYSEMDLLLCSGDDSLILGRDFDAGVDVQDFNLIFNLETKFLR--- 2122
Cdd:cd23205    133 KGIRYHVDGGIMSGDMTTGLGNC-----IAVLVIVMSFRLSILDDGDDHVIICEKSHTWICERVLPLWWTAMGHSLRvdg 207
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1110865247 2123 ----YQHYYFCSKYLFSDGQRWWLVPDPVKVMVK 2152
Cdd:cd23205    208 taedFEQIEFCQHKPWNGATRLTMVPNPAKVLPK 241
Alphacarmovirus_RdRp cd23239
RNA-dependent RNA polymerase (RdRp) in the genus Alphacarmovirus of positive-sense ...
1999-2162 1.77e-03

RNA-dependent RNA polymerase (RdRp) in the genus Alphacarmovirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the Procedovirinae subfamily; This group contains the RdRp of RNA viruses belonging to the Alphacarmovirus genus within the subfamily Procedovirinae, family Tombusviridae, order Tolivirales. The Alphacarmovirus genus was split in 2015 into three genera, each retaining -carmovirus as part of their name: Alphacarmovirus, Betacarmovirus, and Gammacarmovirus. Different carmoviruses infect a wide range of both monocotyledonous and dicotyledonous plants. Viruses tend to remain localized, forming necrosis in artificially infected hosts. There are 8 species in the genus Alphacarmovirus: Adonis mosaic virus, Angelonia flower break virus, Calibrachoa mottle virus, Carnation mottle virus, Honeysuckle ringspot virus, Nootka lupine vein clearing virus, Pelargonium flower break virus, and Saguaro cactus virus. 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: 438089 [Multi-domain]  Cd Length: 470  Bit Score: 43.20  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 1999 DISKYDKSQGIVALVYE--CRMMKFFGVPDW--FVSMWFRGHiATTFSDptTG-IRGRIAFQRKSGDASTYLGNTmfLLG 2073
Cdd:cd23239    209 DMSRFDQHVSVPALQFEhsCYLACFPGDRHLaqLLSWQLKNF-GVGFAS--NGmIRYKKEGCRMSGDMNTALGNC--LLA 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247 2074 VLLAtfKYSEMDL---LLCSGDDSLILGRDFDAGVDVQdfnlifNLETKFLRY-------------QHYYFCSKYLFSDG 2137
Cdd:cd23239    284 CLIT--KHLMKGVncrLINNGDDCVLICERKDLGFVVS------NLTTGWRRFgftciaeepvyelEKIRFCQMAPVYDG 355
                          170       180
                   ....*....|....*....|....*
gi 1110865247 2138 QRWWLVPDPVKVMVKlGRHDLVNWE 2162
Cdd:cd23239    356 ETWVMVRDPKVSMSK-DAFSLVHWN 379
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
592-705 2.91e-03

OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase L is also called protein L, large structural protein, replicase, transcriptase, or ubiquitin thioesterase. It displays RNA-directed RNA polymerase (EC 2.7.7.48), deubiquitinase (DUB)/ubiquitin thiolesterase (EC 3.4.19.12), and deISGylating activities. It is a viral homolog of ovarian tumor protease (vOTU) that has been implicated in the downregulation of type I interferon immune response by removing post-translational modifying proteins ubiquitin (Ub) and the Ub-like interferon-simulated gene 15 (ISG15) from host cellular proteins. The attachment of Ub and ISG15 to cellular proteins mediates important innate antiviral responses, and their removal inhibits these antiviral pathways. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438580  Cd Length: 148  Bit Score: 40.28  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110865247  592 FVEIPVAADGNCFFHALravgASALDPVSLRQKLL------AARDSWGLEP-----YLASEQ-VSRLTDFSEkplvphWA 659
Cdd:cd21880     22 FEIERVPGDGNCFFRSI----AELLFDTEDEWRLVkntiesYARANWDECPearlyYLSLEEyLRDAMKDGY------WG 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1110865247  660 --DETTFLvaARVLGVTICL-----HMRGT-VRRYGKGPV---FHLQLTSEHVTGLK 705
Cdd:cd21880     92 gsLEAEIL--SKALGITIIIwvvddSDWVTaAVRFGDGDVstsLNLLHSGGHFDALR 146
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
1544-1615 2.93e-03

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 42.66  E-value: 2.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1110865247 1544 LVHGYnATTVHSFQGKEAKHVAVVrLSSnaQDEIYLREEYALVALTRHTTRLVYFTmcTTDALARLIASVPS 1615
Cdd:COG0507    439 LELAY-AITVHKSQGSTFDRVILV-LPS--EHSPLLSRELLYTALTRARELLTLVG--DRDALARAVRRDTA 504
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH