#=GF ID Peptidase_A3B
#=GF AC PF21024.1
#=GF DE Peptidase A3B
#=GF AU Chuguransky S;0000-0002-0520-0736
#=GF SE Prosite (PS51817)
#=GF GA 28.20 28.20;
#=GF TC 28.20 139.60;
#=GF NC 27.80 26.30;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -E 1000 --cpu 4 -Z 75585367 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 15831103
#=GF RT Characterization of the protease domain of Rice tungro
#=GF RT bacilliform virus responsible for the processing of the capsid
#=GF RT protein from the polyprotein.
#=GF RA Marmey P, Rojas-Mendoza A, de Kochko A, Beachy RN, Fauquet CM;
#=GF RL Virol J. 2005;2:33.
#=GF RN [2]
#=GF RM 7674916
#=GF RT Families of aspartic peptidases, and those of unknown catalytic
#=GF RT mechanism.
#=GF RA Rawlings ND, Barrett AJ;
#=GF RL Methods Enzymol. 1995;248:105-120.
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC This entry includes the aspartic peptidase domain from the P3
#=GF CC polyprotein of Pararetroviruses (such as rice tungro bacilliform
#=GF CC virus), a member of the family Caulimoviridae. P3 contains a
#=GF CC putative movement protein (MP), the capsid protein (CP), the
#=GF CC aspartate protease (PR) and the reverse transcriptase (RT) with
#=GF CC a ribonuclease H activity. PR proteolytically processes P3. The
#=GF CC sequence DSGS is believed to be the RTBV protease active site
#=GF CC [1]. The RTBV PR domain forms peptidase family A3 subfamily B
#=GF CC [2].
#=GF SQ 3
#=GS A0A2R6R8L0_ACTCC/478-573 AC A0A2R6R8L0.1
#=GS POL_RTBVP/983-1077 AC P27502.1
#=GS A0A251RXY7_HELAN/19-114 AC A0A251RXY7.1
A0A2R6R8L0_ACTCC/478-573 LGLVDTGCTSCIINKKLIPDYLCKKSDRIIQGQQMDGKLHSYDTELVPGAMISFKTNRDQFSTEYTLPQTWVRNlN..VSSDFIIGLTFLLNQNGGI-f
POL_RTBVP/983-1077 TALIDSGSTHNIICPTLIPASWINNTHREIIMFAVDNSKYNLNQELIDDIKLQFQEVDETFGIKYKLGQTYVAP.K..PTKTFIIGHRFLTNENGSVT.
A0A251RXY7_HELAN/19-114 TALVDTRATKSLISHSLVPEQYHKELKYKVVSRTIENRLVGITH-YLEPTGIQFLDFTNNYSIKYDIPQVNINP.AyiQSKDFVLGLNFLFALNGSVT.
#=GC seq_cons TALVDTGuT+sIIs+oLIP-papKco+RcIlupslDN+LaulspELl-sstIQFp-sc-sFSIKYcLPQTaVsP.s..sSKDFIIGLsFLhNpNGSVT.
//