ID A0A0N7IRM3_CVH22 Unreviewed; 4092 AA.
AC A0A0N7IRM3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 08-NOV-2023, entry version 47.
DE SubName: Full=Orf1a {ECO:0000313|EMBL:ALJ99895.1};
OS 229E-related bat coronavirus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Duvinacovirus; Human coronavirus 229E.
OX NCBI_TaxID=1739614 {ECO:0000313|EMBL:ALJ99895.1, ECO:0000313|Proteomes:UP000130985};
RN [1] {ECO:0000313|EMBL:ALJ99895.1, ECO:0000313|Proteomes:UP000130985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BtCoV/AT1A-F1/Hip_aba/GHA/2010 {ECO:0000313|EMBL:ALJ99895.1};
RX PubMed=26378164; DOI=10.1128/JVI.01755-15;
RA Corman V.M., Baldwin H.J., Fumie Tateno A., Melim Zerbinati R., Annan A.,
RA Owusu M., Nkrumah E.E., Maganga G.D., Oppong S., Adu-Sarkodie Y., Vallo P.,
RA da Silva Filho L.V., Leroy E.M., Thiel V., van der Hoek L., Poon L.L.,
RA Tschapka M., Drosten C., Drexler J.F.;
RT "Evidence for an Ancestral Association of Human Coronavirus 229E with
RT Bats.";
RL J. Virol. 89:11858-11870(2015).
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; KT253272; ALJ99895.1; -; Genomic_RNA.
DR Proteomes; UP000130985; 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:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039520; P:induction by virus of host autophagy; 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:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; 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; cd21558; alphaCoV-Nsp6; 1.
DR CDD; cd21514; alphaCoV_Nsp2_HCoV-229E-like; 1.
DR CDD; cd21665; alphaCoV_Nsp5_Mpro; 1.
DR CDD; cd21826; alphaCoV_Nsp7; 1.
DR CDD; cd21830; alphaCoV_Nsp8; 1.
DR CDD; cd21897; alphaCoV_Nsp9; 1.
DR CDD; cd21731; alphaCoV_PLPro; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21875; PEDV-like_alphaCoV_Nsp1; 1.
DR CDD; cd21712; TM_Y_alphaCoV_Nsp3_C; 1.
DR Gene3D; 1.10.8.1190; -; 2.
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; 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; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR046443; a/bCoV_NSP1_glob.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
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; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR044385; NSP2_HCoV-229E-like.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044309; NSP5_Mpro_alphaCoV.
DR InterPro; IPR044369; NSP6_alphaCoV.
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; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR Pfam; PF09401; CoV_NSP10; 1.
DR Pfam; PF19212; CoV_NSP2_C; 2.
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; 2.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 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; SSF101816; Replicase NSP9; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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; 2.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
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 IRF3 by virus {ECO:0000256|ARBA:ARBA00022931};
KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01296}; Thiol protease {ECO:0000256|ARBA:ARBA00022807};
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 1934..1957
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2001..2021
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2080..2097
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2104..2122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2501..2523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2738..2757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2763..2780
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2787..2803
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2809..2827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2834..2859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3171..3192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3285..3306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3312..3331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3336..3359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3379..3397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3404..3422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3473..3494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..109
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000259|PROSITE:PS51962"
FT DOMAIN 113..359
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51989"
FT DOMAIN 389..775
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000259|PROSITE:PS51990"
FT DOMAIN 773..897
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51991"
FT DOMAIN 898..993
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51943"
FT DOMAIN 1023..1275
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 1274..1442
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1605..1660
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51944"
FT DOMAIN 1668..1919
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 2387..2491
FT /note="CoV Nsp3 Y"
FT /evidence="ECO:0000259|PROSITE:PS51992"
FT DOMAIN 2878..2973
FT /note="Nsp4C"
FT /evidence="ECO:0000259|PROSITE:PS51946"
FT DOMAIN 2974..3275
FT /note="Peptidase C30"
FT /evidence="ECO:0000259|PROSITE:PS51442"
FT DOMAIN 3554..3636
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51949"
FT DOMAIN 3637..3831
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51950"
FT DOMAIN 3832..3940
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS51951"
FT DOMAIN 3941..4079
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000259|PROSITE:PS51952"
SQ SEQUENCE 4092 AA; 453901 MW; D132FCD1DDA44917 CRC64;
MACNRVTLAV ASDTEISASG CSTVAQAVRR YSEAASNGFR ACRFVSFGLQ DCVVGIADDD
YVMGLHGNQT LFCNIMKFSD RPFMLRGWLV FSNSNYLLEE FDVVFGKRGG GNVTYTDQYL
CGADGKPVIN EDLWQFVDHF GENEEIVING HTYVCAWLTK RKPLDYKRQN NLAIEEINYV
RGDALHTLRN GSVLETAKEV KTSSKVVLSD DLDKLYKVFG SPVMTNGSNI LEAFTKPVFV
SALVQCTCGT KSWSVGDWTG FKSSCCNTLS KKLCVVPGNV KPGDAVVTTQ QAGSGIKYFC
GMTLKFVANI EGVSVWRVIA VQSVDGFVAS ATFVEEEHAN RMDTFCFNVR NSTTDECRLA
MLGAEMTINV RRQVAAGVID ISTGWFDVYD DIFAENKPWF VRKAEDIFGS CWSSLVSVLK
QLKVTTGELM RFVKSICSSA VAVVGGTIQI VASVPEKFLN AFDVFVKAVQ TVFDCAVETS
TIAGKAFDKV FDYVLLDNAL VKFVTTKLKG VRESGLNKVK YATAVVGSTE DVKSSRVERS
TAVLTIANNY PKLSDEGYTA VIGDVAYFVS DGYFRLMAGP TSVLTTAVYK PLFTFNVNVM
GTRPEKFPTT VTCENLEAAV LVVNDKITDS QLDYSVDVID NEIIVKPNIS LCAPLYVRDY
VDKWDDFCRQ YSNESWFEED YKAFTSVLEI TDAVVKAAES KAFIDTIVPP CPSILKIIDG
GKIWNGVIKA VNSVSEWLKS LKLNLTPQGL FGTCAKRFRR WLGILLEAYN AFLDTVVSTV
KIGGLTFKTY AFDKPYIVMR DIVCKVENKT EAEWIELLPR NDRIKSFSTF ESAYMPIAYP
THFDIEEVEL LDAEFVEPGC GGILALIDEH VFYKKDDVYY PSNGTNILPV AFTKSAGGKV
SFSDEVEVKD IAPVYRVKLC FEFEDEKLVD VCEKAIGKKI KHEGDWDSFC KTIQSALSVV
SGYVNLPTYY IYDEEGGTDL SLPVMISEWP LSETDKEEEV QQDQQEDTVV PEVETVVDQV
EEVNSSFDIE VADVKLEVSP FEMPFEELNG LKVLKQVDNN CWVNSVMLQL QLTGLLDDDY
AMQLFKVGRV VKMIERCYVA EKCVRGSPGD VGMCLYRLLK DLHTGFMVMS YKCLCTSGVI
EESGALLFCT PTKNAFAYGV CLNCKAPRMC TIARMQGTMV FVQQEPVPVN PNDLVVKPIC
ASVFRGTASF GHYQTNIYPQ KLCVDGFGVN KIQTWTNDAI NTICIKDADY SAKVAKPVIP
VKNSVDSSPK EATVDVKLNA FLVHNNVAFY QGDVDAVVSG VDFDFIVNAA NENLAHGGGL
AKALDVYTKG KLQRLSKEHI GLAGKVKVGT GVMIECDGLK IFNVVGPRKG KHERDLLIKA
YNTINNEQGT PLTPILSCGI FGVKLETSLE VLLDVCNTKE VKVFVYTDME VCKVKEFVSG
LSTQQVEPLK VEPTPLPLAK DVPKPYKVDG NFSYFTEDLL CVADGKPIVL FTDSVLTLDD
RGLALDNALN GSLSAAIKDC IDTNKAIPSG NLIKFDIGSV VVYMCVVPSE QDKHLDKNVQ
RCTRKLNRLM CDIVCTIPAE HVLPLVLSSL TCNVSFVGEL KAVEAKVITI KVTEDGVNVH
DVTVTTDKSF EQQVGVIADK DKDLSGAVPS DLNTSELLTK AIDVDWVQFY GFRDAVTFAT
VDHSAFAYDS AVVNGIRVLK TSDNNCWVNA VCISLQYLKP HFISQGLDAA WNKFVLGDVE
TFVAFVYYVA GLIKGAKGDA EDTLNKLSKY LANEAQVQLE HYSSCVECEA TFKNSVASIN
SAIVCASVKR DGVQVGYCAH GIKYYSRVRS VSGRAIIVSV EQLEPCAQSR LLSGVAYTAF
SGPADNGHYT VYDTAKKSMY DGDRFVKHDL SLLFVTSVVM VGGYVSPVVE TVKPKPVINQ
LDEKAQKFFD FGDFLVHNFV TFFTWLLSMF TLCKTAVTTG DVKIMAKVPQ RTGVVFKRSL
KYNLKASVAV LRSKWWLLAK FMKLMLLIYT LYSVVLLGVR FGPLNGYFCS ETINGYAKSN
FVKDDYCDGS LGCKMCLFGY QELSQFSHLD VVWKHITDPL FSNMQPFIVM VLLLIFGDNY
LRCFLLYFVA QMISTVGVFL GYKETNWFLH FVPFDVICDE LLVTVIVIKV ISFVRHVLFG
CENPDCIACS KSARLKRFPV NTIVNGVQRS FYVNANGGSK FCKKHRFFCV DCDSYGYGNT
FITAEVSREL GNITKTNVQP TGPAYIMIDK VEFENGFYRL HAGETFWRYN FDITESKYSC
KEVLKNCNVL DDFIVFNNNG TNVTQVKNAS VYFSQLLCRP IKLVDSELLS TLSVDFNGVL
HKAYIDVLRN SFGKDLNANM SLAECKSALG LSISDHEFTS AISNAHRCDV LLSDLSFNNF
VSSYAKPEEK LSAYDLACCM RAGAKVVNAN VLTKDQTPIV WHAKDFNSLS AEGRKYIVKT
SKAKGLTFLL TINENQAITQ IPATSIVAKQ GAGDAGHSST WFWILCGLVC LIQFYLCFFM
PYFMYDTVRS FEGYDFKYIE NGQLKNFEAP LKCVRNVFEN FEDWHYAKFG SVPLNKQSCP
IVVGVSEIVN TVAGIPSNVY LVGKTLIFTL QAAFGNAGVC YDIFGVTTPE KCIFTSACTR
LEGLGGNNVY CYNTDLMKGS LPYSAIQANA YYKYDNGNFI KLPEVIAQGF GFRTVRTITT
KYCRVGECVD SNAGVCFGFD KWFVNDGRVD NGYVCGTGLW NLVFNIFSMF SSSFSVAAMS
GQILLNCALG AFAIFCCFLV TKFRRMFGDL SVGVCTVVMA VLLNNVSYIV TQNLVTMIAY
AVLYFFATRS LRYAWIWCAA YLIAYISFAP WWLCAWYFLA MLTGLLPSLL KLKVSTNLFE
GDKFVGTFES AAAGTFVIDM RSYEKLANSI SPEKLKSYAA SYNRYKYYSG NANEADYRCA
CYAYLAKAML DFSRDHNDIL YTPPTVSYGS TLQAGLRKMA QPSGIVEKCV VRVCYGNTVL
NGLWLGDIVY CPRHVIASNT TSAIDYDHEY SIMRLHNFSI TSGTAFLGVV GATMHGATLK
IKVSQTNMHT PRHSFRTLKS GEGFNILACY DGCAQGVFGV NMRTNWTIRG SFINGACGSP
GYNLKNGEVE FVYMHQIELG SGSHVGSSFD GVMYGGFDDQ PNLQVEFANQ MLTVNVVAFL
YAAILNGCTW WLKGDKLSVE HYNEWAQFNG FTAMNGEDAF SILAAKTGVC VERLLHAIQV
LNNGFGGKQI LGYSSLNDEF SINEVVKQMF GVNLQSGKTT MFKSLSLFAG FFIMFWAELF
VYTTTVWVNP GFLTPFMILL VALSLCLTSV VKHKVLFLQV FLLPSIIVAA IQNCAWDYHV
TKVLAEKFDY NVSVMQMDTQ GFVNIFVCLF VALLHTWRFA KERCTHWCTY LFSLLAVLYT
ALYSYDYVSL LVMLLCAISN EWYIGAIIFR ICRFGVAFLP VEYVSYFGGV KTVLLFYMFL
GFVSCMYYGL LYWINRFCKC TLGVYDFCVS PAEFKYMVAN GLNAPNGPFD ALFLSFKLMG
IGGPRTIKVS TVQSKLTDLK CTNVVLMGIL SNMNIASNSK EWAYCVEMHN KIDLCDDPET
AQDLLLALLA FFLSKHSDFG LGDLVDSYFE NDAILQSVAS SFVGMPSFVA YETARQEYEN
AVANGSSPQI IKQLKKAMNV AKAEFDRESS VQKKINRMAE QAAAAMYKEA RAVNRKSKVV
SAMHSLLFGM LRRLDMSSVD TILNMARNGV VPLSVIPATS ASRLVVVVPD HESFAKMMVD
GFVHYAGVVW TLQEVKDNDG KNVHLKDVTK ENQETLVWPL ILTCERVVKL QNNEIMPGKM
KVKATKAEGD GGVTSEGNAL YNNEGGRAFM YAYVTTKPDM KFVKWEHDSG VVTVELEPPC
RFVVDTPTGP QIKYLYFVKN LNNLRRGAVL GYIGATVRLQ AGKQTEFVSN SHLLTHCSFA
VDPAAAYLDA VKQGAKPVGN CVKMLTNGSG SGQAITSTID SNTTQDTYGG ASVCIYCRAH
VAHPTMDGFC QYKGKWVQVP IGTNDPIRFC LENTVCKVCG CWLNHGCTCD RTAIQSFDNS
YLNESGALVP LD
//
