#=GF ID   Birna_RdRp_C
#=GF AC   PF20489.2
#=GF DE   Birnavirus RNA dependent RNA polymerase (VP1), C-terminal
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF SE   Pfam-B_2204 (release 7.3)
#=GF GA   28.00 28.00;
#=GF TC   28.90 70.80;
#=GF NC   27.90 24.50;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 75585367 -E 1000 --cpu 4 HMM pfamseq
#=GF TP   Domain
#=GF WK   Birnaviridae
#=GF RN   [1]
#=GF RM   12069523
#=GF RT   Birnavirus VP1 Proteins Form a Distinct Subgroup of
#=GF RT   RNA-Dependent RNA Polymerases Lacking a GDD Motif. 
#=GF RA   Shwed PS, Dobos P, Cameron LA, Vakharia VN, Duncan R; 
#=GF RL   Virology 2002;296:241-250.
#=GF RN   [2]
#=GF RM   17456597
#=GF RT   The structure of a birnavirus polymerase reveals a distinct
#=GF RT   active site topology.
#=GF RA   Pan J, Vakharia VN, Tao YJ;
#=GF RL   Proc Natl Acad Sci U S A. 2007;104:7385-7390.
#=GF RN   [3]
#=GF RM   12421558
#=GF RT   The palm subdomain-based active site is internally permuted in
#=GF RT   viral RNA-dependent RNA polymerases of an ancient lineage.
#=GF RA   Gorbalenya AE, Pringle FM, Zeddam JL, Luke BT, Cameron CE,
#=GF RA   Kalmakoff J, Hanzlik TN, Gordon KH, Ward VK;
#=GF RL   J Mol Biol. 2002;324:47-62.
#=GF DR   INTERPRO; IPR046750;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   Birnaviruses are dsRNA viruses. This entry corresponds to the
#=GF CC   C-terminal domain of RNA dependent RNA polymerase also known as
#=GF CC   VP1. All of the birnavirus VP1 proteins contain conserved RdRp
#=GF CC   motifs that reside in the catalytic "palm" domain of all classes
#=GF CC   of polymerases. However, the birnavirus RdRps lack the highly
#=GF CC   conserved Gly-Asp-Asp (GDD) sequence, a component of the
#=GF CC   proposed catalytic site of this enzyme family that exists in the
#=GF CC   conserved motif VI of the palm domain of other RdRps [1]. This
#=GF CC   RdRp has the five essential RNA polymerase motifs in a permuted
#=GF CC   order of C-A-B-D-E to form a conserved catalytic active site
#=GF CC   [2,3]. This domain is mostly alpha-helical that runs across the
#=GF CC   canyon in the front of the palm, and wraps around the fingers
#=GF CC   subdomain [2], which may function to prevent back-primed RNA
#=GF CC   synthesis during protein priming.
#=GF SQ   7
#=GS RDRP_IBDVU/699-805        AC Q82630.1
#=GS RDRP_IPNVS/689-793        AC P22174.1
#=GS Q703G8_IPNVS/689-793      AC Q703G8.1
#=GS RDRP_BSNV/694-797         AC Q8AZL8.1
#=GS RDRP_IBDVB/699-805        AC A7L9Z4.1
#=GS A0A4P8PJ90_9VIRU/689-793  AC A0A4P8PJ90.1
#=GS RDRP_IPNVJ/689-793        AC P22173.1
RDRP_IBDVU/699-805                   ..PKPPNVNRPVNTG..-GLKAVSNALKTGRYRNEAGLSGLVLLATARSRLQDAVKAMAEAEKLhksKPDDPDAD.WFERSETL...SDLLEKA-DIASKVAHSALVETSDALEAVQ.
RDRP_IPNVS/689-793                   ef--DVKDRPPTPRSpgKTLAEVTAAITSGTYKDPKSAVWRLLDQRTKLRVSTLR---DHAHAL...KPAASTSDfWGDATEELaeqQQLLMKANNL----LKSSLTEAREALETVQ.
Q703G8_IPNVS/689-793                 ef--DVKDRPPTPRSpgKTLAEVTAAITSGTYKDPKSAVWRLLDQRTKLRVSTLR---DQAHAL...KPAASTSDfWGDATEELaeqQQLLMKANNL----LKSSLTEAREALETVQ.
RDRP_BSNV/694-797                    ..RKQPNVNKHHLRT..KGLKKCVSALKQGACRNPTTVAGLKLTAYSKSRINKAKAVFDEINNL...-PKTESDD.WSDRMDD-...ADRLMKANNLYMREARSALEDVHNSLLALS.
RDRP_IBDVB/699-805                   ..PKPPNVNRPVNTG..-GLKAVSNALKTGRYRNEAGLSGLVLLATARSRLQDAVKAKAEAEKLhksKPDDPDAD.WFERSETL...SDLLEKA-DIASKVAHSALVETSDALEAVQ.
A0A4P8PJ90_9VIRU/689-793             ..RKQPHVNKLALDI..KNMQQASTALTSGAFRNPNKMAGLKLNAMAKSKLMTTLQAFKEAEAA...ADQSGTDD.WGEASETL...-DTMLRASRIYQAEAEASLKDVSEALDSL-s
RDRP_IPNVJ/689-793                   ..SFDPKARPQTPRSpkKTLDEVTTAITSGTYKDPKSAVWRLLDQRTKLRVSTLR---DQALAL...KPASSSVDnWAEATEELaqqQQLLMKANNL----LKSSLTETREALETIQ.
#=GC seq_cons                        ...hsPpsp..sscu..KsLppVosAlpoGsY+sPpuhshhlLstpsK.Rlpshh...ccAcsL...KPsssosD.Wu-toEpL...ppLLhKAssl....h+SuLsEsp-ALEslQ.
//