ID  P0C6W5;
PN  2'-O-methyltransferase;
GN  rep;
OS  694006;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W5;
DR  UNIPROT: A3EXG5;
DR  PDB: 5UTV;
DR  Pfam: PF11501;
DR  Pfam: PF11633;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:19264783}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UNP9; IntAct: EBI-29486867; Score: 0.44
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGVPDPPKLKSMVVTTLKWCDPFANPNVTGWDIPIEEALEYAKQQLRTPEPQLVFVPYYLSHAPGISGDRVVITDSIWY
SQ  ATNFGWQPIRELAMDKDGVRYGRGGTHGVLLPMQDPSFIMGDIDIQIRKYGIGANSPPDVLPLWDGFSDPGPDVGPYLDF
SQ  PDNCCPTKPKAKRGGDVYLSDQYGFDNNGILVEPVMKLLGVIKSDFTLEQLLAALGKYRTEDGYDLPDGYVKVAIKVGRK
SQ  AVPVLKQSIFTVVGVTEQLVPGYYYPFSTSSVVEHTKPTRGGPVGKTVEAVMLSLYGTNNYNPATPVARLKCSYCDYYGW
SQ  TPLKDIGTVNCLCGAEFQLTSSCVDAESAGVIKPGCVMLLDKSPGMRLIPGNRTYVSFGGAIWSPIGKVNGVTVWVPRAY
SQ  SIVAGEHSGAVGSGDTVAINKELVEYLIEGIRVDADTLDNPTCATFIANLDCDTKAPVVHTVESLQGLCLANKIMLGDKP
SQ  LPTDEFHPFIVGLAYHVQRACWYGALASRTFEAFRDFVRTEEERFAQFFGKVCAPINGCVYLAYTTGRVTLFSAYQVLNT
SQ  AIAKSKDAFGGVAAIVVDMLKPILEWVLKKMSIAKGAWLPYAEGLLALFKAQFTVVKGKFQFLRASLNSKCHSLCDLLTT
SQ  IMSKLLTSVKWAGCKVDALYTGTYYYFSRKGVLTEVQLCAKRLGLLLTPKQQKMEVEVLDGDFDAPVTLTDLELEECTGV
SQ  LEEVFGASDVKLVKGTLVSLASKLFVRTEDGFLYRYVKSGGVLGKAFRLRGGGVSKVTFGDEEVHTIPNTVTVNFSYDVC
SQ  EGLDAILDKVMAPFQVEEGTKLEDLACVVQKAVYERLSDLFSDCPAELRPINLEDFLTSECFVYSKDYEKILMPEMYFSL
SQ  EDAVPVDDEMVDDIEDTVEQASDSDDQWLGDEGAEDCDNTIQDVDVATSMTTPCGYTKIAEHVYIKCADIVQEARNYSYA
SQ  VLVNAANVNLHHGGGVAGALNRATNNAMQKESSEYIKANGSLQPGGHVLLSSHGLASHGILHVVGPDKRLGQDLALLDAV
SQ  YAAYTGFDSVLTPLVSAGIFGFTVEESLCSLVKNVACTTYVVVYDRQLYERALATSFDVPGPQSSVQHVPAIDWAEAVEV
SQ  QESIVDQVETPSLGAVDTVDSNADSGLNETARSPENVVGSVPDDVVADVESCVRDLVRQVVKKVKRDKRPPPIVPQQTVE
SQ  QQPQEISSPGDCNTVLVDVVSMSFSAMVNFGKEKGLLIPVVIDYPAFLKVLKRFSPKEGLFSSNGYEFYGYSRDKPLHEV
SQ  SKDLNSLGRPLIMIPFGFIVNGQTLAVSAVSMRGLTVPHTVVVPSESSVPLYRAYFNGVFSGDTTAVQDFVVDILLNGAR
SQ  DWDVLQTTCTVDRKVYKTICKRGNTYLCFDDTNLYAITGDVVLKFATVSKARAYLETKLCAPEPLIKVLTTVDGINYSTV
SQ  LVSTAQSYRAQIGTVFCDGHDWSNKNPMPTDEGTHLYKQDNFSSAEVTAIREYYGVDDSNIIARAMSIRKTVQTWPYTVV
SQ  DGRVLLAQRDSNCYLNVAISLLQDIDVSFSTPWVCRAYDALKGGNPLPMAEVLIALGKATPGVSDDAHMVLSAVLNHGTV
SQ  TARRVMQTVCEHCGVSQMVFTGTDACTFYGSVVLDDLYAPVSVVCQCGRPAIRYVSEQKSPWLLMSCTPTQVPLDTSGIW
SQ  KTAIVFRGPVTAGHYMYAVNGTLISVYDANTRRRTSDLKLPATDILYGPTSFTSDSKVETYYLDGVKRTTIDPDFSKYVK
SQ  RGDYYFTTAPIEVVAAPKLVTSYDGFYLSSCQNPQLAESFNKAINATKTGPMKLLTMYPNVAGDVVAISDDNVVAHPYGS
SQ  LHMGKPVLFVTRPNTWKKLVPLLSTVVVNTPNTYDVLAVDPLPVNNETSEEPISVKAPIPLYGLKATMVLNGTTYVPGNK
SQ  GHLLCLKEFTLTDLQTFYVEGVQPFVLLKASHLSKVLGLRVSDSSLHVNHLSKGVVYAYAATRLTTRVTTSLLGGLVTRS
SQ  VRKTADFVRSTNPGSKCVGLLCLFYQLFMRFWLLVKKPPIVKVSGIIAYNTGCGVTTCVLNYLRSRCGNISWSRLLKLLR
SQ  YMLYIWFVWTCLTICGVWLSEPYAPSLVTRFKYFLGIVMPCDYVLVNETGTGWLHHLCMAGMDSLDYPALRMQQHRYGSP
SQ  YNYTYILMLLEAFFAYLLYTPALPIVGILAVLHLIVLYLPIPLGNSWLVVFLYYIIRLVPFTSMLRMYIVIAFLWLCYKG
SQ  FLHVRYGCNNVACLMCYKKNVAKRIECSTVVNGVKRMFYVNANGGTHFCTKHNWNCVSCDTYTVDSTFICRQVALDLSAQ
SQ  FKRPIIHTDEAYYEVTSVEVRNGYVYCYFESDGQRSYERFPMDAFTNVSKLHYSELKGAAPAFNVLVFDATNRIEENAVK
SQ  TAAIYYAQLACKPILLVDKRMVGVVGDDATIARAMFEAYAQNYLLKYSIAMDKVKHLYSTALQQISSGMTVESVLKVFVG
SQ  STRAEAKDLESDVDTNDLVSCIRLCHQEGWEWTTDSWNNLVPTYIKQDTLSTLEVGQFMTANAKYVNANIAKGAAVNLIW
SQ  RYADFIKLSESMRRQLKVAARKTGLNLLVTTSSLKADVPCMVTPFKIIGGHRRIVSWRRVLIHVFMLLVVLNPQWFTPWY
SQ  IMRPIEYNVVDFKVIDNAVIRDITSADQCFANKFSAFENWYSNRYGSYVNSRGCPMVVGVVSDIVGSLVPGLPARFLRVG
SQ  TTLLPLVNYGLGAVGSVCYTPHYAINYDVFDTSACVLAATCTLFSSASGERMPYCADAALIQNASRYDMLKPHVMYPFYE
SQ  HSGYIRFPEVISAGVHIVRTMAMEYCKVGRCDVSEAGLCMSLQPRWVVNNAYFRQQSGVYCGTSAFDLFMNMLLPIFTPV
SQ  GAVDITTSILMGALLAVVVSMSLYYLLRFRRAFGDYSGVIFTNILAFVLNVIVLCLEGPYPMLPSIYAMVFLYATCYFGS
SQ  DIACMMHVSFLIMFAGVVPLWVTVLYIVVVLSRHILWFASLCTKRTVQVGDLAFHSFQDAALQTFMLDKEVFLRLKREIS
SQ  SDAYFKYLAMYNKYKYYSGPMDTAAYREAACSHLVMALEKYSNGGGDTIYQPPRCSVASAALQAGLTRMAHPSGLVEPCL
SQ  VKVNYGSMTLNGIWLDNFVICPRHVMCSRDELANPDYPRLSMRAANYDFHVSQNGHNIRVIGHTMEGSLLKLTVDVNNPK
SQ  TPAYSFIRVSTGQAMSLLACYDGLPTGVYTCTLRSNGTMRASFLCGSCGSPGFVMNGKEVQFCYLHQLELPNGTHTGTDF
SQ  SGVFYGPFEDKQVPQLAAPDCTITVNVLAWLYAAVLSGENWFLTKSSISPAEFNNCAVKYMCQSVTSESLQVLQPLAAKT
SQ  GISVERMLSALKVLLSAGFCGRTIMGSCSLEDEHTPYDIGRQMLGVKLQGKFQSMFRWTLQWFAIIFVLTILILLQLAQW
SQ  TFVGALPFTLLLPLIGFVAVCVGFVSLLIKHKHTYLTVYLLPVAMVTAYYNFQYTPEGVQGYLLSLYNYVNPGRIDVIGT
SQ  DLLTMLIISVACTLLSVRMVRTDAYSRIWYVCTAVGWLYNCWTGSADTVAISYLTFMVSVFTNYTGVACASLYAAQFMVW
SQ  VLKFLDPTILLLYGRFRCVLVCYLLVGYLCTCYFGVFNLINRLFRCTLGNYEYVVSSQELRYMNSHGLLPPTNSWQALML
SQ  NIKLAGIGGIPIYRVSTIQSNMTDLKCTSVVLLSVLQQLRVESSSKLWALCVKLHNEILASNSPTEAFEAFVSLLSVLLS
SQ  LPGAINLDELCSSILENNSVLQAVASEFSNLSSYVDYENAQKAYDTAVATGAPASTVNALKKAMNVAKSVLDKDVATTRK
SQ  LERMSELAMTAMYKQARAEDRRSKVTAAMQTMLFNMIRRLDSDALSNILNNARNGVVPLGVIPRTAANKLLLVVPDFSVY
SQ  TATITMPTLTYAGSAWDVMQVADADGKTVNATDITRENSVNLAWPLVVTAQRQQATSPVKLQNNELMPQTVKRMNVVAGV
SQ  SQTACVTDAVAYYNATKEGRHVMAILADTDGLAFAKVEKSTGDGFVILELEPPCKFMVDTPKGPALKYLYFTKGLKNLCR
SQ  GTVLGTLACTVRLHAGSATEVASNSSILSLCSFSVDPEATYKDYLDNGGSPIGNCVKMLTPHTGTGLAITAKPDANIDQE
SQ  SFGGASCCLYCRCHIEHPGASGVCKYKGKFVQIPLVGVNDPIGFCIRNVVCAVCNMWQGYGCPCSSLREINLQARDECFL
SQ  NRVRGTSGVARLVPLGSGVQPDIVLRAFDICNTKVAGFGLHLKNNCCRYQELDADGTQLDSYFVVKRHTESNYLLEQRCY
SQ  EKLKDCGVVARHDFFKFNIEGVMTPHVSRERLTKYTMADLVYSLRHFDNNNCDTLKEILVLRGCCTADYFDRKDWYDPVE
SQ  NPDIIRVYHNLGETVRKAVLSAVKMADSMVEQGLIGVLTLDNQDLNGQWYDFGDFIEGPAGAGVAVMDTYYSLAMPVYTM
SQ  TNMLAAECHVDGDFSKPKRVWDICKYDYTQFKYSLFSKYFKYWDMQYHPNCVACADDRCILHCANFNILFSMVLPNTSFG
SQ  PLVQKIYVDGVPFVVSTGYHYRELGVVMNQDIRQHAQRLSLRELLVYAADPAMHVAASNALADKRTVCMSVAAMTTGVTF
SQ  QTVKPGQFNEDFYNFAVKCGFFKEGSTISFKHFFYAQDGNAAISDYDYYRYNLPTMCDIKQLLFSLEVVDKYFDCYDGGC
SQ  LQASQVVVANYDKSAGFPFNKFGKARLYYESLSYADQDELFAYTKRNVLPTITQMNLKYAISAKNRARTVAGVSIASTMT
SQ  NRQFHQKMLKSIAAARGASVVIGTTKFYGGWNRMLRTLCEGVENPHLMGWDYPKCDRAMPNLLRIFASLILARKHATCCN
SQ  ASERFYRLANECAQVLSEMVLCGGGFYVKPGGTSSGDSTTAYANSVFNICQAVSANLNTFLSIDGNKIYTTYVQELQRRL
SQ  YLGIYRSNTVDNELVLDYYNYLRKHFSMMILSDDGVVCYNADYAQKGYVADIQGFKELLYFQNNVFMSESKCWVEPDITK
SQ  GPHEFCSQHTMLVDMKGEQVYLPYPDPSRILGAGCFVDDLLKTDGTLMMERYVSLAIDAYPLTKHPDPEYQNVFWCYLQY
SQ  IKKLHEELTGHLLDTYSVMLASDNASKYWEVEFYENMYMESATLQSVGTCVVCNSQTSLRCGGCIRRPFLCCKCCYDHVV
SQ  STTHKLVLSVTPYVCNNPSCDVADVTQLYLGGMSYYCRDHRPPISFPLCANGQVFGLYKNICTGSPDVADFNSLATCDWS
SQ  NSKDYVLANTATERLKLFAAETLRATEENAKQAYASAVVKEVLSDRELVLSWETGKTRPPLNRNYVFTGFHITKNSKVQL
SQ  GEYIFEKGDYGDVVNYRSSTTYKLQVGDYFVLTSHSVQPLSSPTLLPQERYTKLVGLYPAMNVPESFASNVVHYQRVGMS
SQ  RYTTVQGPPGTGKSHLSIGLALYYPSAKIVYTACSHAAVDALCEKAHKNLPINRCSRIVPAKARVECFSKFKVNDVGAQY
SQ  VFSTINALPETTADILVVDEVSMCTNYDLSMINARVRAKHIVYVGDPAQLPAPRTLLTKGTLAPEHFNSVCRLMVAVGPD
SQ  IFLATCYRCPKEIVDTVSALVYDKKLKANKVTTGECYKCYYKGSVTHDSSSAINKPQLGLVKEFLIKNPKWQSAVFISPY
SQ  NSQNSVARRMLGLQTQTVDSSQGSEFDYVIYCQTSDTAHALNVNRFNVAITRAKKGILCVMSDSTLYESLEFTPLDVNDY
SQ  VKPKMQSEVTVGLFKDCAKAEPLGPAYAPTFVSVNDKFKLNESLCVHFDTTELQMPYNRLISKMGFKFDLNIPGYSKLFI
SQ  TREQAIREVRGWVGFDVEGAHACGPNIGTNLPLQIGFSTGVNFVVTPSGYIDTESGSRLANVVSKAPPGDQFKHLIPLMR
SQ  KGEPWSVVRKRIVEMLCDTLDGVSDTVTFVTWAHGFELTTLHYFAKVGPERKCFMCPRRATLFSSVYGAYSCWSHHRHIG
SQ  GADFVYNPFLVDVQQWGYVGNLQVNHDNVCDVHKGAHVASCDAIMTRCLAIHDCFCGEVNWDVEYPIIANELAINRACRS
SQ  VQRVVLKAAVKALHIETIYDIGNPKAIKVYGVNVNNWNFYDTNPVVEGVKQLHYVYDVHRDQFKDGLAMFWNCNVDCYPH
SQ  NALVCRFDTRVLSKLNLAGCNGGSLYVNQHAFHTDAFNKNAFVNLKPLPFFYYSDTACENATGVSTNYVSEVDYVPLKSN
SQ  VCITRCNLGGAVCKKHADEYRNFLESYNTMVSAGFTLWVDKTFDVFNLWSTFVKLQSLENVAYNVLKSGHFTAVAGELPV
SQ  AILNDRLYIKEDGADKLLFTNNTCLPTNVAFELWAKRSVNVVPEVKLLRNLGVTCTYNLVIWDYESNAPLVPNTVGICTY
SQ  TDLTKLDDQVVLVDGRQLDAYSKFCQLKNAIYFSPSKPKCVCTRGPTHASINGVVVEAPDRGTAFWYAMRKDGAFVQPTD
SQ  GYFTQSRTVDDFQPRTQLEIDFLDLEQSCFLDKYDLHDLGLEHIVYGQFDGTIGGLHLLIGAVRRKRTAHLVMETVLGTD
SQ  TVTSYAVIDQPTASSKQVCSVVDIILDDFIALIKAQDRSVVSKVVQCCLDFKVFRFMLWCKGGKISTFYPQLQAKQDWKP
SQ  GYSMPALYKVQNAVLEPCLLHNYGQAARLPSGTLMNVAKYTQLCQYLNTCSLAVPAKMRVMHFGAGSDKGVCPGTAVLKQ
SQ  WLPADAYLVDNDLCYCASDADSTYVGSCETFFSVNKWDFIFSDMYDARTKNTSGDNTSKEGFFTYLTGFIRSKLALGGSI
SQ  AIKITEHSWSADLYAIMGHFNWWTCFCTSVNSSSSEAFLIGVNYIGVGALLDGWQMHANYVFWRNSTVMQLSSYSLYDLQ
SQ  RFPLRLKGTPVMSLKEDQLNELVLNLIRAGRLIVRDAVDIGVRGVACSGV
//