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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193900645  14 YYIPHHCVLKPSSESTKLRVVFDASCRTsNQTSLNDHLLVGPTLQDDLYLLLLRFRLHRYAITADVTKMYRQVNVDLNDR 93
Cdd:cd01644    2 WYLPHHAVIKPSKTTTKLRVVFDASARY-NGVSLNDMLLKGPDLLNSLFGVLLRFRQGKIAVSADIEKMFHQVKVRPEDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193900645  94 KYQYILWRALPDEP-LRTYQLNTVTYGTASAPYLAIRSLHILAnlSRTEYSIGAAVIESSFYVDDLLSG 161
Cdd:cd01644   81 DVLRFLWRKDGDEPkPIEYRMTVVPFGAASAPFLANRALKQHA--EDHPHEAAAKIIKRNFYVDDILVS 147

Integrase zinc binding domain; This zinc binding domain is found in a wide variety of integrase proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 193900645  202 VRHLHLRNCHAGPKALVALIRLEYWIVNDRDLARRIVRTCMACVRYKPK 250
Cdd:pfam17921  10 LKEAHDSGGHLGIEKTLARLRRRYWWPGMRKDVKKYVKSCETCQRRKPS 58

RT_pepA17: Reverse transcriptase (RTs) in retrotransposons. This subfamily represents the RT domain of a multifunctional enzyme. C-terminal to the RT domain is a domain homologous to aspartic proteinases (corresponding to Merops family A17) encoded by retrotransposons and retroviruses. RT catalyzes DNA replication from an RNA template and is responsible for the replication of retroelements.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193900645  14 YYIPHHCVLKPSSESTKLRVVFDASCRTsNQTSLNDHLLVGPTLQDDLYLLLLRFRLHRYAITADVTKMYRQVNVDLNDR 93
Cdd:cd01644    2 WYLPHHAVIKPSKTTTKLRVVFDASARY-NGVSLNDMLLKGPDLLNSLFGVLLRFRQGKIAVSADIEKMFHQVKVRPEDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193900645  94 KYQYILWRALPDEP-LRTYQLNTVTYGTASAPYLAIRSLHILAnlSRTEYSIGAAVIESSFYVDDLLSG 161
Cdd:cd01644   81 DVLRFLWRKDGDEPkPIEYRMTVVPFGAASAPFLANRALKQHA--EDHPHEAAAKIIKRNFYVDDILVS 147

Integrase zinc binding domain; This zinc binding domain is found in a wide variety of integrase proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 193900645  202 VRHLHLRNCHAGPKALVALIRLEYWIVNDRDLARRIVRTCMACVRYKPK 250
Cdd:pfam17921  10 LKEAHDSGGHLGIEKTLARLRRRYWWPGMRKDVKKYVKSCETCQRRKPS 58

RT_pepA17: Reverse transcriptase (RTs) in retrotransposons. This subfamily represents the RT domain of a multifunctional enzyme. C-terminal to the RT domain is a domain homologous to aspartic proteinases (corresponding to Merops family A17) encoded by retrotransposons and retroviruses. RT catalyzes DNA replication from an RNA template and is responsible for the replication of retroelements.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193900645  14 YYIPHHCVLKPSSESTKLRVVFDASCRTsNQTSLNDHLLVGPTLQDDLYLLLLRFRLHRYAITADVTKMYRQVNVDLNDR 93
Cdd:cd01644    2 WYLPHHAVIKPSKTTTKLRVVFDASARY-NGVSLNDMLLKGPDLLNSLFGVLLRFRQGKIAVSADIEKMFHQVKVRPEDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193900645  94 KYQYILWRALPDEP-LRTYQLNTVTYGTASAPYLAIRSLHILAnlSRTEYSIGAAVIESSFYVDDLLSG 161
Cdd:cd01644   81 DVLRFLWRKDGDEPkPIEYRMTVVPFGAASAPFLANRALKQHA--EDHPHEAAAKIIKRNFYVDDILVS 147

Integrase zinc binding domain; This zinc binding domain is found in a wide variety of integrase proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 193900645  202 VRHLHLRNCHAGPKALVALIRLEYWIVNDRDLARRIVRTCMACVRYKPK 250
Cdd:pfam17921  10 LKEAHDSGGHLGIEKTLARLRRRYWWPGMRKDVKKYVKSCETCQRRKPS 58