ID U5LR11_9BETC Unreviewed; 4454 AA.
AC U5LR11;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=ORF 1a {ECO:0000313|EMBL:AGX27798.1};
GN Name=ORF 1a {ECO:0000313|EMBL:AGX27798.1};
OS Betacoronavirus Erinaceus/VMC/DEU/2012.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Merbecovirus; Hedgehog coronavirus 1.
OX NCBI_TaxID=1385427 {ECO:0000313|EMBL:AGX27798.1, ECO:0000313|Proteomes:UP000101546};
RN [1] {ECO:0000313|EMBL:AGX27798.1, ECO:0000313|Proteomes:UP000101546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ErinaceusCoV/2012-174/GER/2012 {ECO:0000313|EMBL:AGX27798.1};
RX PubMed=24131722; DOI=10.1128/JVI.01600-13;
RA Corman V.M., Kallies R., Philipps H., Gopner G., Muller M.A., Eckerle I.,
RA Brunink S., Drosten C., Drexler J.F.;
RT "Characterization of a novel betacoronavirus related to middle East
RT respiratory syndrome coronavirus in European hedgehogs.";
RL J. Virol. 88:717-724(2014).
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 -!- SUBCELLULAR LOCATION: Host cytoplasm, host perinuclear region
CC {ECO:0000256|ARBA:ARBA00004407}. Host membrane
CC {ECO:0000256|ARBA:ARBA00004301}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004301}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000256|ARBA:ARBA00008087, ECO:0000256|PROSITE-ProRule:PRU01294}.
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DR EMBL; KC545383; AGX27798.1; -; Genomic_RNA.
DR Proteomes; UP000101546; Genome.
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:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0002151; F:G-quadruplex RNA binding; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by symbiont of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039579; P:suppression by virus of host ISG15-protein conjugation; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR CDD; cd21901; alpha_betaCoV_Nsp10; 1.
DR CDD; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR CDD; cd21827; betaCoV_Nsp7; 1.
DR CDD; cd21831; betaCoV_Nsp8; 1.
DR CDD; cd21898; betaCoV_Nsp9; 1.
DR CDD; cd21732; betaCoV_PLPro; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21878; MERS-CoV-like_Nsp1; 1.
DR CDD; cd21815; MERS-CoV-like_Nsp3_betaSM; 1.
DR CDD; cd21823; MERS-CoV-like_Nsp3_NAB; 1.
DR CDD; cd21523; SUD_C_MERS-CoV_Nsp3; 1.
DR CDD; cd21716; TM_Y_MERS-CoV-like_Nsp3_C; 1.
DR CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR Gene3D; 1.10.8.1190; -; 1.
DR Gene3D; 2.60.120.1680; -; 1.
DR Gene3D; 3.10.20.350; -; 1.
DR Gene3D; 3.10.20.540; -; 1.
DR Gene3D; 6.10.140.2090; -; 1.
DR Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 1.10.1840.10; main proteinase (3clpro) structure, domain 3; 1.
DR Gene3D; 3.40.220.20; Nsp3, SUD-M subdomain; 1.
DR Gene3D; 1.10.8.370; nsp7 replicase; 1.
DR Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1.
DR Gene3D; 2.40.10.250; Replicase NSP9; 1.
DR Gene3D; 3.40.50.11020; Replicase polyprotein, nucleic acid-binding domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR046443; a/bCoV_NSP1_glob.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR047573; CoV_NSP2_M.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR047566; CoV_NSP3_Y3.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR022733; DPUP_SUD_C_bCoV.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR021590; NSP1_glob_bCoV.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR024375; NSP3_bCoV.
DR InterPro; IPR047567; NSP3_G2M_bCoV.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR InterPro; IPR044382; NSP3_SUD_C_MERS-CoV.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038083; NSP3A-like.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044367; NSP6_betaCoV.
DR InterPro; IPR043610; NSP6_CoV.
DR InterPro; IPR014828; NSP7_CoV.
DR InterPro; IPR037204; NSP7_sf_CoV.
DR InterPro; IPR014829; NSP8_CoV.
DR InterPro; IPR037230; NSP8_sf_CoV.
DR InterPro; IPR014822; NSP9_CoV.
DR InterPro; IPR036499; NSP9_sf_CoV.
DR InterPro; IPR013016; Peptidase_C16_CoV.
DR InterPro; IPR008740; Peptidase_C30_CoV.
DR InterPro; IPR043477; Peptidase_C30_dom3_CoV.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043177; PLpro_N_sf_CoV.
DR InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR Pfam; PF16251; bCoV_NAB; 1.
DR Pfam; PF11501; bCoV_NSP1; 1.
DR Pfam; PF11633; bCoV_SUD_M; 1.
DR Pfam; PF09401; CoV_NSP10; 1.
DR Pfam; PF19212; CoV_NSP2_C; 1.
DR Pfam; PF19211; CoV_NSP2_N; 1.
DR Pfam; PF19218; CoV_NSP3_C; 1.
DR Pfam; PF16348; CoV_NSP4_C; 1.
DR Pfam; PF19217; CoV_NSP4_N; 1.
DR Pfam; PF19213; CoV_NSP6; 1.
DR Pfam; PF08716; CoV_NSP7; 1.
DR Pfam; PF08717; CoV_NSP8; 1.
DR Pfam; PF08710; CoV_NSP9; 1.
DR Pfam; PF08715; CoV_peptidase; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF144246; Coronavirus NSP10-like; 1.
DR SUPFAM; SSF140367; Coronavirus NSP7-like; 1.
DR SUPFAM; SSF143076; Coronavirus NSP8-like; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF159936; NSP3A-like; 1.
DR SUPFAM; SSF101816; Replicase NSP9; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51942; BCOV_NSP3C_C; 1.
DR PROSITE; PS51941; BCOV_NSP3C_M; 1.
DR PROSITE; PS51994; BCOV_NSP3E_G2M; 1.
DR PROSITE; PS51945; BCOV_NSP3E_NAB; 1.
DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51962; COV_NSP1; 1.
DR PROSITE; PS51991; COV_NSP2_C; 1.
DR PROSITE; PS51990; COV_NSP2_M; 1.
DR PROSITE; PS51989; COV_NSP2_N; 1.
DR PROSITE; PS51992; COV_NSP3_Y3; 1.
DR PROSITE; PS51943; COV_NSP3A_UBL; 1.
DR PROSITE; PS51944; COV_NSP3D_UBL; 1.
DR PROSITE; PS51946; COV_NSP4C; 1.
DR PROSITE; PS51949; COV_NSP7; 1.
DR PROSITE; PS51950; COV_NSP8; 1.
DR PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
DR PROSITE; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050};
KW Decay of host mRNAs by virus {ECO:0000256|ARBA:ARBA00022616};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Eukaryotic host gene expression shutoff by virus
KW {ECO:0000256|ARBA:ARBA00023247};
KW Eukaryotic host translation shutoff by virus
KW {ECO:0000256|ARBA:ARBA00022809};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host mRNA suppression by virus {ECO:0000256|ARBA:ARBA00022557};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022632};
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 Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023208};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Modulation of host ubiquitin pathway by viral deubiquitinase
KW {ECO:0000256|ARBA:ARBA00022876};
KW Modulation of host ubiquitin pathway by virus
KW {ECO:0000256|ARBA:ARBA00022662}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000101546};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01289}; 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 Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00444}.
FT TRANSMEM 2240..2261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2363..2383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2403..2427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2819..2840
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3087..3112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3124..3155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3175..3201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3622..3641
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3647..3674
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3681..3701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3732..3750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3757..3773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3793..3815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3827..3849
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..151
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000259|PROSITE:PS51962"
FT DOMAIN 202..482
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51989"
FT DOMAIN 488..721
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000259|PROSITE:PS51990"
FT DOMAIN 723..859
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51991"
FT DOMAIN 863..972
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51943"
FT DOMAIN 1180..1346
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1348..1474
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51941"
FT DOMAIN 1474..1546
FT /note="DPUP"
FT /evidence="ECO:0000259|PROSITE:PS51942"
FT DOMAIN 1551..1606
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51944"
FT DOMAIN 1620..1889
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 1903..2016
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000259|PROSITE:PS51945"
FT DOMAIN 2032..2154
FT /note="G2M"
FT /evidence="ECO:0000259|PROSITE:PS51994"
FT DOMAIN 2699..2802
FT /note="CoV Nsp3 Y"
FT /evidence="ECO:0000259|PROSITE:PS51992"
FT DOMAIN 3214..3310
FT /note="Nsp4C"
FT /evidence="ECO:0000259|PROSITE:PS51946"
FT DOMAIN 3311..3616
FT /note="Peptidase C30"
FT /evidence="ECO:0000259|PROSITE:PS51442"
FT DOMAIN 3909..3991
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51949"
FT DOMAIN 3992..4190
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51950"
FT DOMAIN 4191..4300
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS51951"
FT DOMAIN 4301..4440
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000259|PROSITE:PS51952"
FT REGION 1042..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4454 AA; 494009 MW; C09D6E3E292865C8 CRC64;
MSSATGEGSQ GARATYRAAL NNEKRHDHVA LTVPCCGTEA KVTALSPWFM DGMLAYETVK
EMLLKGEQLL FAPSNLSGYI KFLPGPRVYL VERLTGGTYS EPFIVNQLAF SDEQDGPMMG
TTLQGKPIGF FFPFDEELVT GTYTFKLRKN GLGGQLFREV PWFENHDFHG IEGFSQIVED
LQEDPKGKFS NKLYKKLCGG DVIPVDQYMC GFDGSPIKPY LDLANKEGLT KLADVEADVC
SRVDKQGFLI FKGTTYRVVW FTERKDVDYS KQTLFTVICV MQRNGVHDIP AHPFTLGSKV
EQLKPHVAKG NLVGLTLKAK ILYTMYGEDA VEEPSYIYHS AFVDCVKCNE GKWCTGNAVA
GFACECGAAY TAKQVLLQSS GLVKSNALFC ATCPFAQGDR CSLDCKHTVP QVVSYLSEKC
VVFPSGKSFV LAFGGALYTY MGCAEGTMYF VPRAKSVVSR IGTACFTGCV GAWDKVQQVA
NLFTQKAQQQ LNFVNEFVVS DVVLAILTGT TSTLDELRSL LQGITFEKMR DYCVKHGIKV
TMGDYVDSAI NVGGASVRSA AINAPFVVLS ALGESFKKIA AVPFKVGSSF LKTWEYLSDC
IVYRVLPYEL EDVSDFVQLL FNCVEISAAS MYFASVVIRE KVNTMFNALP LSVQTAAKNF
IDVCLRATLC TVKFLNDLLS LVKLVVYKAF VYTSAGFVST LEKTSPAAQK LLDVLSKAFK
LLHKKVSWAG SKVHAVIYEG KDALVFSSGT YHCVTAPGSV VGAHLEATIP GEVVKKQLSM
LTATNYSTTV DVRPKTRNVE LVYGQLETTN MHSPDVVVGD YVIVSDKVFV RSEEDGRLAF
YPMCTNGKAV PCMFTLKGGA PIKKVSFGND EIHEIDAVRT VTVEYNIHPV LDTLLSNTEL
KTFVVDKDLT VSEFALVVQE AVADLLAKLL RGIALDDFDL EDFIDTKVYV FNLDGDEVWK
STMIFSVHPV DCDDEEIDDA LEEDDSFNEE EEPDSWAEMV DAIFPLSDEA EGDVVVEEQS
LVDDAGVVSP SAAAEKIVPM HDVSDDSASN NEESLSADVE PKGVAPPVEE VIVETKVPTT
LILEESDNPV LADADSSQQS DCVKHVVLGT TNTSEVCVDV EHCVVDQISE EVPKGAAPPV
MEEEKPSQEV SGSPEPSLKE DKPHKDCQKQ LAGNDDQIDP LKNYKHKVLS GNVTIVLADA
IKLARCFSSS VLVNAANSHL KHAGGIAHAI DSASKGAVQR ESDDYIKNNG ALQVGDTVLL
KGHGLAKHIL HVVGPDARQG QDVTLLSKCY KAMNAHPLVV TPLVSAGIFG VDPKVSLQML
QQVAKTRVLV CVNSANIYEA LTEVVVPQGL TFSFEGMKSA VAKAKEYGFT MFICVDNKQN
VKLLKTLGVK ADKKQSTVNG VRYYCYTSED TVPNLVAVAN KQKGIVALPL GYVTHGFDLM
QAAAIVKMVT VPYVCLLANK EQLAILQGDV LKSTPFEEFV TGIKKNGYAH WQLVQGEILV
NGVSYSKLLQ WSDQTVVYSS NKLFVLKNGN LLPFTSVEQC RSYLNSRTTQ QLNVEVLATV
DGVNFRTVIL NNKNTFRSQL GTVFLDGVDV SDTIPSVDKN GASVYIADNF SKEELAAVKE
MYGVEDPTFL YKYYSIRAKV VKWKMAMCED APSLCLNSNN CYLNAAVMML DCLRDIKFNI
PALQAAYMKF KGGDFGDFIS LLMAYGNCTY GQPDDASMLL HTALSKAELL VSARMVWREW
CDHCGVKDVV ITGIKACVYV GVQSLDELRE CNHHICQCGG VRFRQLVECV TPWLLLSGPP
NEELVANPDF VAFNVFIGHE AGVGHFVHAR VKKGLLYKYD SGTLTKASDW KCKVTDKLYP
GQKYTAECEI VVYSLDGNQK AEKQPNFSAY YVKDGKYYTN KPSLEFTPAT VSSGVVYTNS
CFIVNDGDAI GSAFNKLLGF DKNKPASKQL TYSLLPNEDG DVLLAEFKSY DPMYKNGAAY
KGKPILWVNN GLYDSKLNKY NRASLRQIFD IQPVETNNRF APLKVEEVDE RPTSHVQEET
LVSEKSELKV VKCKGLSKPF VKNGFSFISD DKGILTVEYL TKEDMHTLYV NPKSQIIVLK
DNWLSGLFQM HTVQSGDLNV VASSGSLTKK VKLLFKTSSM CKEFLSRTFV ATKCVNSVVS
ATVRKLCCNK DVFVKLFSFI KMLCFIPLRH FNKQKECVNV DVKTLSIAGV VTGNVIKQCC
STGFYLFKQK LRRIDWKSSL RWLLFMLTTV LMLLSLYHLY VFNAVLTSDV IKEVNTGIKG
VYYRISSYLG VTSVCDGFSN NYRNVSFNRD DYCEKFGYVC HWCLMGQDSL THYSAIQIVQ
TNLSHYVLSI DWMWFWIELS VAYLMYTPAF NWVLLVCTLQ YFFSQTNHII NWRSYNFVMS
GVYLLTTYIP LCGLLRVYNV LATLWYLRRF YNHVINGCKD TACMLCYKRN RLTRVEASTV
VCGVKRTFYI TANGGISFCS RHNWNCVDCD TTGLGHTFIC EEVANDLTTS LRRLVKPTDR
SHYYVESVEV KNSVVQLNYT RDGQLCYERV PLCNFSNIDK FKFKEVCKST TGIPEFNFVI
YDSTDRGQEN LARSACVYYS QVLCKSILLV DSNLMNTVGD SSAIAIRLLD SFINSFASLY
NVSRDKLEKL ISTAKDCVKR GEDLQSVLKT FIQAARVHAN VESDVETASI VDGIQYAHKN
DIELVTDSFN NYIPSYVKPD SIATVDLGCL IDLKAASVNP ASMRNANGAC VWNIDAYLKL
SDSLKRQIRV ACRKCSLNFK LTTSKLRAQD NILSVKFSVT KFVGGSLNSK LGSFLFKMYA
GFTICLVILA ILMYCILPTF NMAKVDFNND RILGYKVLDN GIVRDIGIDD KCFVNKYNTF
DAWYQQEFGN SYDNDYNCPV VVAVIAGISG ERVPGVPTSL IWAGNQILFF VSRVFATNNN
ICYTPHMEIA YERFSDSGCV LSAECTLFKD AVGSMVPYCY DANVLPGAVP YDTMLPHVRY
DLYDSNMFIK FPEVIVEGTL RVVKTLKTQY CRLGSCEWSE AGICVSTNGS WMLNNEHYAS
KPGVYCGSDY LDMVRRSFMS VFQPITYFQL TTSLFMGLCL CLGIVVIFYY VNKFKRAFAD
YTQCVLIAVM ATGLNGLCLC FVASNPFLIV PYSAFYYYST FYVTNEPAVV MHASWLIMFL
PVASVWVVCS YLAAICFRHC FWVLAYFSRK KVDVFTDGKL NCTFQEAAAN IFVVNRDTYV
ALRNAISQDA YNKYLGMFNK YKYFSGVMDT AAYREASAAH LAKALQVFSE NGSDLLYQPP
NCSLASSVLQ SGLVKMAHPS GAVEQCIVQV TCGSMTLNGL WLDNIVYCPR HVMCPQDQLV
DPNYDALLNS MTNHSFTIQR HGRSTANLRC TGHAMHGTLL KLTVDSANPE TPAYTFTTIK
QGSSFSVLAC YNGRPSGTYT VVMRPNSTIK GSFLCGSCGS VGYVKEGNVI NFCYMHQMEL
SNGTHTGSSF DGNMYGNFQD RQIYQAQLSD KHCTINVVAW LYAAVLNGCN WFVKPNKTGV
AAFNEWALSN QFTEFVSTQA LELLAVKTGV QIEQLLYSIQ QLNNGFQGNV ILGSAMLEDE
YTPEDVNMQM MGVVMQSSVR KITYGLTHWL LATCVLTYVV ILQLTKFTIW NFLFNVIPLQ
LTPIMFVVLA LAMLCVKHKH AFLTTFLLPG ALCLTYANLV YEPNTPVSSF LIMCVNWLNP
DGTYMRTTHM DLGVYVSLCL ALLVVVRRLY KPSVTNCAFA LTSLVMWFYS YSIGDASSPI
VYLQFVTAAT SDYMVTVFLA VNVAKCLTYL TSMYFTTLSV VVPEVKIVLL MYICIGFICT
MYFGVFSFLN LKMRAPMGVY SYEVSTQEFR YMNANGLRAP RNSWDAMVLN FKLLGVGGVP
CIKIASVQSK LTDLKCTSVV LLSVLQQLHL EANSKAWSHC VKLHNDILST SDPSEAFEKF
VALLATLMSF SGSVDLEALA SELLDNISVL QSTLTEFSHL ASYAELETAQ KSYQEAVASG
DASPQMLKAL QKAVNVAKNT YEKDKSIARK LERMAEQAMT SMYKQARAED KKSKIVSAMQ
TMLFGMIKKL DNDVLNGIIS NARNGCVPLS IIPLCASNKL RVVIPDMQIW KQVVTYPVLS
YAGALWDITL INNVDGEVVR PSDVIDTNEG LTWPLLLECT RAVASAVKLQ NNEIKPTGLK
TMVVAAGQEQ NSCTVKSVAY YEPVQGRKML MGILSEDAHL KWARVEGQDG FITIELQPPC
KFLIAGSKGP EVRYLYFVKN LNNLHRGQLL GHIAATVRLQ AGSNTEYASN SSVLSLVNFA
VDPAKAYTDY VNAGGAPLTN CVKMLTPKTG TGIAISVKPE SNLDQETYGG ASVCLYCRAH
IEHPDVSGVC KFKGKFVQIP AQCTRDPVGF CLANVQCNVC QYWVGYGCNC DSLRENTMLH
SKDTNFLNES GVLL
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