ID A0A1L6Z3P9_9NIDO Unreviewed; 3925 AA.
AC A0A1L6Z3P9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Replicase polyprotein 1ab {ECO:0000256|ARBA:ARBA00022087};
DE AltName: Full=ORF1ab polyprotein {ECO:0000256|ARBA:ARBA00029611};
OS Rat arterivirus 1.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; Variarterivirinae;
OC Betaarterivirus; Chibartevirus; Betaarterivirus chinrav 1.
OX NCBI_TaxID=1734441 {ECO:0000313|EMBL:APT40619.1, ECO:0000313|Proteomes:UP000201837};
RN [1] {ECO:0000313|Proteomes:UP000201837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wu Z., Jin Q.;
RT "Detection and complete genome analysis of novel rat arteriviruses closely
RT related to porcine reproductive and respiratory syndrome virus in China,
RT 2014-2015.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Contains the activities necessary for the transcription of
CC negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion
CC RNA as well as proteinases responsible for the cleavage of the
CC polyprotein into functional products. {ECO:0000256|ARBA:ARBA00043841}.
CC -!- FUNCTION: Displays RNA and DNA duplex-unwinding activities with 5' to
CC 3' polarity. {ECO:0000256|ARBA:ARBA00043920}.
CC -!- FUNCTION: Plays a role in the inhibition of host STAT3 signaling
CC pathway by inducing the degradation of STAT3.
CC {ECO:0000256|ARBA:ARBA00043872}.
CC -!- FUNCTION: Plays a role in the initial induction of autophagosomes from
CC host reticulum endoplasmic. {ECO:0000256|ARBA:ARBA00043859}.
CC -!- FUNCTION: Responsible for replication and transcription of the viral
CC RNA genome. {ECO:0000256|ARBA:ARBA00003927}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-
CC 2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-
CC COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173079, ChEBI:CHEBI:173080;
CC Evidence={ECO:0000256|ARBA:ARBA00024600};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Host cytoplasm,
CC host perinuclear region {ECO:0000256|ARBA:ARBA00004407}. Host
CC endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004354}. Host membrane
CC {ECO:0000256|ARBA:ARBA00004301}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004301}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the arteriviridae polyprotein family.
CC {ECO:0000256|ARBA:ARBA00010965}.
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DR EMBL; KU302440; APT40619.1; -; Genomic_RNA.
DR RefSeq; YP_009337022.1; NC_032987.1.
DR GeneID; 30854465; -.
DR KEGG; vg:30854465; -.
DR Proteomes; UP000201837; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004540; F:RNA nuclease activity; IEA:UniProt.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039563; P:disruption by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd21410; 1B_av_Nsp10-like; 1.
DR CDD; cd23189; Arteriviridae_RdRp; 1.
DR CDD; cd17937; DEXXYc_viral_SF1-N; 1.
DR CDD; cd21160; NendoU_av_Nsp11-like; 1.
DR CDD; cd21166; NTD_av_Nsp11-like; 1.
DR CDD; cd18786; SF1_C; 1.
DR CDD; cd21405; ZBD_av_Nsp10-like; 1.
DR Gene3D; 3.90.70.160; -; 1.
DR Gene3D; 4.10.80.390; -; 1.
DR Gene3D; 3.30.1330.220; Arterivirus nonstructural protein 7 alpha; 1.
DR Gene3D; 2.30.31.30; Arterivirus nps1beta, nuclease domain; 1.
DR Gene3D; 3.90.70.70; Arterivirus papain-like cysteine protease beta domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.90.70.60; Porcine arterivirus-type cysteine proteinase alpha domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR031932; Arteri_nsp7a.
DR InterPro; IPR038451; Arteri_nsp7a_sf.
DR InterPro; IPR008743; Arterivirus_Nsp2_C33.
DR InterPro; IPR023338; Arterivirus_NSP4_peptidase.
DR InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR InterPro; IPR008741; AV_PCPalpha.
DR InterPro; IPR038155; AV_PCPalpha_sf.
DR InterPro; IPR025773; AV_PCPbeta.
DR InterPro; IPR038154; AV_PCPbeta_sf.
DR InterPro; IPR023183; Chymotrypsin-like_C.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR008760; EAV_peptidase_S32.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR044348; NSP10_1B_Av.
DR InterPro; IPR027355; NSP10_Av_ZBD.
DR InterPro; IPR044320; NSP11_Av_N.
DR InterPro; IPR044314; NSP11_NendoU_Av.
DR InterPro; IPR032855; NSP2-B_epitope.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF16749; Arteri_nsp7a; 1.
DR Pfam; PF14757; NSP2-B_epitope; 1.
DR Pfam; PF05410; Peptidase_C31; 1.
DR Pfam; PF05411; Peptidase_C32; 1.
DR Pfam; PF05412; Peptidase_C33; 1.
DR Pfam; PF05579; Peptidase_S32; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF142877; EndoU-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51538; AV_CP; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51493; AV_NSP4_PRO; 1.
DR PROSITE; PS51539; AV_PCP_ALPHA; 1.
DR PROSITE; PS51540; AV_PCP_BETA; 1.
DR PROSITE; PS51652; AV_ZBD; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Endonuclease {ECO:0000256|PROSITE-ProRule:PRU01303};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00023208};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01303};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00023208};
KW Inhibition of host interferon signaling pathway by virus
KW {ECO:0000256|ARBA:ARBA00022830};
KW Inhibition of host ISG15 by virus {ECO:0000256|ARBA:ARBA00023208};
KW Inhibition of host NF-kappa-B by virus {ECO:0000256|ARBA:ARBA00022863};
KW Inhibition of host PKR by virus {ECO:0000256|ARBA:ARBA00023041};
KW Inhibition of host STAT1 by virus {ECO:0000256|ARBA:ARBA00022961};
KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023208};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nuclease {ECO:0000256|PROSITE-ProRule:PRU01303};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000201837};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023208};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00985}.
FT TRANSMEM 1215..1241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1248..1264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1322..1345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1533..1556
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1614..1632
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1638..1662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1674..1702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1990..2010
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2016..2036
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2048..2066
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2086..2111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2118..2136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..180
FT /note="Peptidase C31"
FT /evidence="ECO:0000259|PROSITE:PS51539"
FT DOMAIN 260..379
FT /note="Peptidase C32"
FT /evidence="ECO:0000259|PROSITE:PS51540"
FT DOMAIN 425..532
FT /note="Peptidase C33"
FT /evidence="ECO:0000259|PROSITE:PS51538"
FT DOMAIN 1340..1371
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 1764..1967
FT /note="Peptidase S32"
FT /evidence="ECO:0000259|PROSITE:PS51493"
FT DOMAIN 2457..2619
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 2858..2992
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT DOMAIN 3113..3176
FT /note="AV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51652"
FT DOMAIN 3229..3514
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 3553..3649
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 3651..3773
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT REGION 972..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3682
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3697
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3726
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
SQ SEQUENCE 3925 AA; 428106 MW; 2764D04A8CF6C001 CRC64;
MSGMFDRCVC TPNARVFMAE GQVYCTRCLA ARPLLSLQKQ DKNLGVLGLF YAPKEPLSWT
CPQGYPTPEC SPAGCCWLSA IFPIARMTSG NGNFFQRLER VAQVIYAEGA LTPRALDHLY
VYDRGCKWYP ITGPVPGVAV FANSMHVSDR PFPGATHVLT NLPLPQRPKA QPFCPFERAN
ANVWAWGDYV VYETEGKWSW ARRGDCSVQF DPVPKEHRLA VYHLIENFPE HHIVTLANYT
FDHSGVSYRP DRHEGHLRPG SVPDGLCWRH VFGSLDAKKQ AAEIRTAVQF GYQTKHGVPG
KYIQRRLQVN GLRAVIDRDG PIAVEAFSTA TSWIRHLNVS SPTTPDFVEI CRIRVEPNTA
PLESSDEKIF RFGQHKWYGA GKKQRAKRAA KEEKEMSPPP LTARQLADAK KTEIIGQRLH
ARLNAYSPPG DGNCGWHCLS AVANRMISNV FESSLPTRFR DSHDWASDDD LVSVISAAGL
PVGLNRCGYC CDAKYVLHLT DDHWTVTCNP GVAPKQLPLA CIHGVCQHVG RQVGGSPPPV
DKIHPGFNSM LESLMSLPSS AIALGMQELL AVPADTESAR SVRRSDVSMM LPNNIDLQLP
AVPGEQVSAL DLSRSDVGTP TDSVRETWTV SQALARLDTN DAKKFCDIRD LLVGLFAASG
VTQQEVDDAI NASIASCSNL SECCAVLEKS LCRTAVTKSK CDLTAYFPEY RPANPCRAVV
PVKPVKTVTK ETGWTPHGLD VRPQQVSVPL SAETVMNFTY PGCADAHYAI TGVCRRISLG
IREKYGFGKR HPTDPWYPDT PQDLTDLIDK AEEDFTQMAG AQLSLENMIW FCQEFDVERH
VASYTWTPCD APPEVPPDSQ VQRRRHTVDA PTGSVAVVAA PAVEVPDSWE DLCDGGASQP
LPLDFTLGTL SSVSAEPVQC EPLDLSTSGS VKFGPPASQC AGITSADLGP LAPPECGSVL
DLSGSSTTVF DLTQRNESPT PSSPASSASS AVLPVERPPK SAQALIDAQG DMCRTLTEIK
FRARNMCLAA CDPTRLTDPA TEAWVNCMWD RLDLLTWKNK SKYQAAFQLG DLSMLPGMIL
ETPPPYPCPV MLPLGSPPRS ATPESDVTLR TLSEHPPCPP GACTEKDASA PALADSEDSP
PPAPAGSDPV PPPGDSQAPS RSTFCGGIFA SAASTAAGLC DGFSRQVFAV ASHLPAFFAR
AFHSGGGYTS GDWCFAAFVL CCLLLCYSYP PVGCAPLLGV FSGSGRRVRI GVFGVWLAFA
IILFRPTPDP IAAACDSDSP DCRRVLLDFE RQQPWDPVRS LVVGPLGLGT AILGRLLGGA
RYFWFVLLRL CFLGDLLLAG AYIVSQGRCK RCWGRCVRMA PSEIPLNVFP FTRATRTSLV
DLCNRYCAPK GIDPIFVASG WRGCYSGDSP IEQPSSTPIS YVNLDEKKIS SRTVVSPPYD
PSQAIKCLKV LQAGGAMAAC RVPAVVKLTQ VPFLAPFLPK LPVNPDARIV VDSETFTCAL
RSGYDTSNFI LGEGNFAELN GLKIQQLQRP KGGFTYGMAS LHAVVWVVAH MILGIYVTRP
SQCGTGTSDP WCSDPFSVPV FGSGTLCTSN LCISPSGLTL PLATALRDFG AREASIVGLV
LLAVACVAHR LAVKADALAV LFSLVAYVYP LASWALACFP VLMRWLPLHP FTALWVHFFL
VACNPPAGGL ALAFSFTCWI LGRYTQVAGL VTPYDIHSHT SGPRGAAAIL TAPEGTYLAA
VRRAALTGKT IMFCPSGVGS LLEGAFRTSK PCLNTVNVVG SSMGSGGVFT YQGKKVCVTA
THVLSGNTAR VTGPGYNRLL EFTTNGDFAY ADVPDWVGPA PEAKAAPPTW CGRAFWLTAS
GVEPGVIGDG YAFCFTACGD SGSPVLTEGG DLVGIHTGSN KQGGGLVTRP DGQTCSIRGV
KLSELSKHFA GPHVPLGDLK LGPHIETDVS TLPADLCALL SAKPTLEGGL STVQLLCVFF
LLWRMMGYAY TPFIAVGFFC LNEVLPAVLV RSCFSFGMFV LAWLTPWSAQ VLMIRLLTAA
LNRNRWSLLF YSTGAIVGFV SDFATTKGYF LGQVLSFSTY CFAPRALVMT SVSPVVIVGL
AHFMAVVLWL FKYRTLHNLL VGDGVFSAAF FLRYFAEGKL RDGVSASCGF NCESLTGALA
CKLSDDDLSF LTRLTDFKCF VSASNMRNAA NQYIEAAYAK ALRLELSQLV QVEKMKGVLA
RLDAFASTTV PSVTVGDVVV VLGSTPVGQV FELMVGSTKH AIQSIETRVL AGTKFTVGRV
VDPKPAPALR SVPVPVPTSH LEWGPASDDR VLKGKKSRKY EKISDHVIDG RKYEKWWDKA
SGDVFYRSSH DDDCHQTIIG GNGMVTRVGY EGCAPMDAPD LSKCKLIKIK DIDGRRYQHW
YDPQTKVTWL IECEGRPAVT DYSTALEAAR LNVDQALTSM GAGQELTAAE VEKLKRIIDQ
LQSLTKEQCL NLLTASGLSR CGRGGLVVSP TAVKIVRYHS RTFSLGDVNL KVTTEAEASE
SERHGHVVVA RPSDGGAVLL RPSPPTLIDV LIQHADTVPG IQPDHGPGNT GVDGSVWDFE
TNPTKEELEL SRQIIAACDL RRGDAPALGL PYLLHPVRGD PYRAFGVLKN TRFGDINYLT
PADTNNPVHV AACYTTGTTP VTDGKSVVAT TLPAGFELYV PTIPASVLEY LDSRHDCPIM
YTEHGSAQAA AKDLSKYDLS TQGFVLPGVL RLVRRYLHSH IGRCPPIHRP SNYPAKNSQA
GVNGARFPTR DIQGIPDIDL LCAQAVREHW QTVTPCTLKK QYCSKKKTRT ILGTNNFIAL
AHRAALSGVT QGFMKKGLNS PIALGKNKFK ELTQDVCGRC LEADLASCDR STPAVIRWFT
AHVLYELACS EEALLSYVLN CCHDVVSTQT GTITKRGGLS SGDPITSVSN TVYSLVIYAQ
HMVLSFLKSG HHYGLLYLQD QLKFEDMLQV QPLLVYSDDL VLHSESSLVP NYHWWVEHLD
LMLGFKTDPA KTCITDSPSF LGCRILNKRQ LVPNRDRVLA ALAYHMKATN VSEYYASAAA
ILMDSCACVE YDPDWFEDLV VGMAQCAKKD GYSFPGPPFF MSMWEKLRTC YEGKKHRLCG
ICGAVAPYAS ACGLDLCSYH THFHQHCPVI IWCGHAAGSR TCEQCSNPTA SGKSELDQVL
KQVPYKPPRT VVMRVESGLT VLDPGRYQTR RGLIAVRRGI RGNEVDLPDG DHQCTPLLPT
CKDINMVAVA RNVLLSKFVI GPPGSGKTSW LLRQVQEGDV VYTPTHQTML DIIKALGTCR
FNIPAGTNLV FPPPSRSGPW VRVLAGGWCP GRNSYLDEAA YCNHLDVLRL LSKTPLTCLG
DFRQLTPVGF ESHCFAFDLM PRTQLTTIWR FGQNICQAIQ SEYEKELLSH ARHTRVVHVQ
KPVWYGQVLT PYHKDRENGA ITIDSSQGAT FDVVTIHLPT PGSLNRPRAL VALTRARHAV
FIYDPHDQMG QFFSVPAEQT PCNIVVPRDG NLVVLDRHNK ECTVAEALGN GDKFRVTDKF
AVDTLRTVCA DLEGSASPLP KVARNLGFYF SPDLPQFAKL PEDLAPHWPV VTCRNEPRWP
DRLVASMRPL CSQSRACVGA GYMVGPSTFL GIPGVVSYYL THYAKGEPQQ LPDTIFSTGR
LEIDCREYLD EREKEIAALF PHAFIGETTG TQVGGCHHVT SKYLPRNLPR ESVAIVGVSS
PGKAAKALCT LTDRVLPDLL PYLSPETQSK CWKLSLDFKP CRLMVWKDKT AYFQLEGKYF
SWYELAAYAQ YIQVPPKATV FLDPCMGPAE VNRAVVGSTD WNCQLSITPY DYGARAVLTS
CDVWDMPPCY RLVGCAGFVC NDPVLGDSNV RFAHLYFRTE NDWEDFNQEA FSAQVNTSYR
TRLNEPRYLF PSGDCIRPVL GATRD
//
