ID  P0C6X8;
PN  2'-O-methyltransferase;
GN  rep;
OS  76344;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [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: P0C6X8;
DR  UNIPROT: Q9PYA2;
DR  UNIPROT: Q9PYA3;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
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: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
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}. [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;
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: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  MAKMGKYGLGFKWAPEFPWMLPNASEKLGSPERSEEDGFCPSAAQEPKTKGKTLINHVRVDCSRLPALECCVQSAIIRDI
SQ  FVDEDPLNVEASTMMALQFGSAVLVKPSKRLSIQAWAKLGVLPKTPAMGLFKRFCLCNTRECVCDAHVAFQLFTVQPDGV
SQ  CLGNGRFIGWFVPVTAIPAYAKQWLQPWSILLRKGGNKGSVTSGHFRRAVTMPVYDFNVEDACEEVHLNPKGKYSRKAYA
SQ  LLKGYRGVKSILFLDQYGCDYTGRLAKGLEDYGDCTLEEMKELFPVWCDSLDNEVVVAWHVDRDPRAVMRLQTLATIRSI
SQ  GYVGQPTEDLVDGDVVVREPAHLLAANAIVKRLPRLVETMLYTDSSVTEFCYKTKLCDCGFITQFGYVDCCGDACDFRGW
SQ  VPGNMMDGFLCPGCSKSYMPWELEAQSSGVIPKGGVLFTQSTDTVNRESFKLYGHAVVPFGSAVYWSPYPGMWLPVIWSS
SQ  VKSYADLTYTGVVGCKAIVQETDAICRSLYMDYVQHKCGNLEQRAILGLDDVYHRQLLVNRGDYSLLLENVDLFVKRRAE
SQ  FACKFATCGDGLVPLLLDGLVPRSYYLIKSGQAFTSMMVNFSHEVTDMCMDMALLFMHDVKVATKYVKKVTGKLAVRFKA
SQ  LGVAVVRKITEWFDLAVDTAASAAGWLCYQLVNGLFAVANGGITFLSDVPELVKNFVDKFKVFFKVLIDSMSVSVLSGLT
SQ  VVKTASNRVCLAGCKVYEVVQKRLSAYVMPVGCNEATCLVGEIEPAVVEDDVVDVVKAPLTYQGCCKPPTSFEKICVVDK
SQ  LYMAKCGDQFYPVVVDNDTIGVLDQCWRFPCAGKKVEFNDKPKVKEIPSTRKIKINFALDATFDSVLSKACSEFEVDKDV
SQ  TLDELLDVVLDAVESTLSPCKEHDVIGTKVCALLNRLAEDYVYLFDEGGEEVIAPKMYCSFSAPDDEDCVAADVVDADEN
SQ  QGDDADDSAALVTDTQEEDGVAKGQVGVAESDARLDQVEAFDIEKVEDPILNELSAELNAPADKTYEDVLAFDAIYSEAL
SQ  SAFYAVPGDETHFKVCGFYSPAIERTNCWLRSTLIVMQSLPLEFKDLEMQKLWLSYKSSYNKEFVDKLVKSVPKSIILPQ
SQ  GGYVADFAYFFLSQCSFKAYANWRCLKCDMDLKLQGLDAMFFYGDVVSHVCKCGTGMTLLSADIPYTLHFGLRDDKFCAF
SQ  YTPRKVFRAACVVDVNDCHSMAVVDGKQIDGKVVTKFNGDKYDFMVGHGMAFSMSAFEIAQLYGSCITPNVCFVKGDVIK
SQ  VLRRVGAEVIVNPANGRMAHGAGVAGAIAKAAGKSFIKETADMVKNQGVCQVGECYESTGGNLCKTVLNIVGPDARGHGK
SQ  QCYSFLERAYQHINKCDDVVTTLISAGIFSVPTDVSLTYLIGVVTKNVILVSNNKDDFDVIEKCQVTSIAGTKALSLQLA
SQ  KNLCRDVKFETNACDSLFSDSCFVSSYDVLQEVELLRHDIQLDDDARVFVQAHMDNLPADWRLVNKFDSVDGVRTVKYFE
SQ  CPGEIFVSSQGKKFGYVQNGSFKVASVSQIRALLANKVDVLCTVDGVNFRSCCVAEGEVFGKTLGSVFCDGINVTKVRCS
SQ  AIHKGKVFFQYSGLSAADLVAVTDAFGFDEPQLLKYYNMLGMCKWPVVVCGNYFAFKQSNNNCYINVACLMLQHLSLKFH
SQ  KWQWQEAWNEFRSGKPLRFVSLVLAKGSFKFNEPSDSTDFMRVVLREADLSGATCDFEFVCKCGVKQEQRKGVDAVMHFG
SQ  TLDKGDLAKGYTIACTCGNKLVHCTQLNVPFLICSNKPEGKKLPDDVVAANIFTGGSLGHYTHVKCKPKYQLYDACNVSK
SQ  VSEAKGNFTDCLYLKNLKQTFSSKLTTFYLDDVKCVEYNPDLSQYYCESGKYYTKPIIKAQFRTFEKVEGVYTNFKLVGH
SQ  SIAEKFNAKLGFDCNSPFTEYKITEWPTATGDVVLASDDLYVSRYSGGCVTFGKPVIWLGHEEASLKSLTYFNRPSVVCE
SQ  NKFNVLPVDVSEPTDKGPVPAAVLVTGALSGAATAPGTAKEQKVCASDSVVDQVVSGFLSDLSGATVDVKEVKLNGVKKP
SQ  IKVEDSVVVNDPTSETKVVKSLSIVDVYDMFLTGCRYVVWMANELSRLVNSPTVREYVKWGMTKIVIPAKLVLLRDEKQE
SQ  FVAPKVVKAKVIACYSAVKWFFLYCFSWIKFNTDNKVIYTTEVASKLTFNLCCLAFKNALQTFNWNVVSRGFFLVATVFL
SQ  LWFNFLYANVILSDFYLPNIGFFPTFVGQIVAWVKTTFGIFTLCDLYQVSDVGYRSSFCNGSMVCELCFSGFDMLDNYDA
SQ  INVVQHVVDRRVSFDYISLFKLVVELVIGYSLYTVCFYPLFGLIGMQLLTTWLPEFFMLETMHWSARFFVFVANMLPAFT
SQ  LLRFYIVVTAMYKIFCLCRHVMYGCSRPGCLFCYKRNRSVRVKCSTVVGGTLRYYDVMANGGTGFCAKHQWNCLNCSAFG
SQ  PGNTFITHEAAADLSKELKRPVNPTDSAYYLVTEVKQVGCSMRLFYERDGQRVYDDVSASLFVDMNGLLHSKVKGVPETH
SQ  VVVVENEADKAGFLNAAVFYAQSLYRPMLLVEKKLITTANTGLSVSQTMFDLYVDSLLGVLDVDRKSLTSFVNAAHNSLK
SQ  EGVQLEQVMDTFIGCARRKCAIDSDVETKSITKSIMSAVNAGVDFTDESCNNLVPTYVKSDTIVAADLGVLIQNNAKHVQ
SQ  ANVAKAANVACIWSVDAFNQLSADLQHRLRKACSKTGLKIKLTYNKQEANVPILTTPFSLKGGAVFSKVLQWLFVVNLIC
SQ  FIVLWALMPTYAVHKSDMQLPLYASFKVIDNGVLRDVTVTDACFANKFIQFDQWYESTFGLVYYRNSRACPVVVAVIDQD
SQ  IGYTLFNVPTKVLRYGFHVLHFITHAFATDSVQCYTPHMQIPYDNFYASGCVLSSLCTMLAHADGTPHPYCYTEGIMHNA
SQ  SLYDSLAPHVRYNLANSNGYIRFPEVVSEGIVRIVRTRSMTYCRVGLCEDAEEGVCFNFNSSWVLNNPYYRAMPGTFCGR
SQ  NAFDLIHQVLGGLVRPIDFFALTASSVAGAILAIIVVLAFYYLIKLKRAFGDYTSVVVINVIVWCINFLMLFVFQVYPTL
SQ  SCLYACFYFYTTLYFPSEISVVMHLQWLVMYGAIMPLWFCIIYVAVVVSNHALWLFSYCRKLGTEVRSDGTFEEMSLTTF
SQ  MITKESYCKLKNSVSDVAFNRYLSLYNKYRYFSGKMDTAAYREAACSQLAKAMETFNHNNGNDVLYQPPTASVTTSFLQS
SQ  GIVKMVFPTSKVEPCVVSVTYGNMTLNGLWLDDKVYCPRHVICSSADMTDPDYSNLLCRVISSDFCVMSGRMSLTVMSYQ
SQ  MQGSLLVLTVTLQNPNTPKYSFGVVKPGETFTVLAAYNGKSQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLTGDSVRFVY
SQ  MHQLELSTGCHTGTDFSGNFYGPYRDAQVVQLPVQDYTQTVNVVAWLYAAILNRCNWFVQSDSCSLEEFNVWAMTNGFSS
SQ  IKADLVLDALASMTGVTVEQILAAIKRLYSGFQGKQILGSCVLEDELTPSDVYQQLAGVKLQSKRTRVVKGTCCWILAST
SQ  LLFCSIISAFVKWTMFMYVTTHMLGVTLCALCFVSFAMLLVKHKHLYLTMFIMPVLCTLFYTNYLVVYKQSFRGLAYAWL
SQ  SHFVPAVDYTYMDEVLYGVVLLVAMVFVTMRSINHDVFSVMFLVGRLVSLVSMWYFGANLEEEVLLFLTSLFGTYTWTTM
SQ  LSLATAKVIAKWLAVNVLYFTDVPQVKLVLLSYLCIGYVCCCYWGVLSLLNSIFRMPLGVYNYKISVQELRYMNANGLRP
SQ  PRNSFEALVLNFKLLGIGGVPVIEVSQIQSRLTDVKCVNVVLLNCLQHLHIASSSKLWQYCSTLHNEILATSDLSVAFDK
SQ  LAQLLVVLFANPAAVDSKCLASIEEVSDDYVRDSTVLQALQSEFVNMASFVEYELAKKNLDEAKASGSANQQQIKQLEKA
SQ  CNIAKSAYERDRAVARKLERMADLALTNMYKEARINDKKSKVVSALQTMLFSMIRKLDNQALNSILDNAVKGCVPLNAIP
SQ  SLTSNTLTIIVPDKQVFDQVVDNVYVTYAGNVWHIQSIQDADGAVKQLNEIDVNITWPLVIAANRHNEVSSVVLQNNELM
SQ  PQKLRTQVVNSGSDMNCNTPTQCYYNTTGMGKIVYAILSDCDGLKYTKIVKEDGNCVVLELDPPCKFSVQDVKGLKIKYL
SQ  YFVKGCNTLARGWVVGTLSSTVRLQAGTATEYASNSAIRSLCAFSVDPKKTYLDYIQQGGAPVTNCVKMLCDHAGTGMAI
SQ  TIKPEATTNQDSYGGASVCIYCRSRVEHPDVDGLCKLRGKFVQVPLGIKDPVSYVLTHDVCQVCGFWRDGSCSCVGTGSQ
SQ  FQSKDTNFLNRVRGTSVNARLVPCASGLDTDVQLRAFDICNANRAGIGLYYKVNCCRFQRADEDGNTLDKFFVIKRTNLE
SQ  VYNKEKECYELTKECGVVAEHEFFTFDVEGSRVPHIVRKDLSKYTMLDLCYALRHFDRNDCSTLKEILLTYAECDESYFQ
SQ  KKDWYDFVENSDIINVYKKLGPIFNRALLNTAKFADTLVEAGLVGVLTLDNQDLYGQWYDFGDFVKTVPGCGVAVADSYY
SQ  SYMMPMLTMCHALDSELFINGTYREFDLVQYDFTDFKLELFNKYFKYWSMTYHPNTCECEDDRCIIHCANFNILFSMVLP
SQ  KTCFGPLVRQIFVDGVPFVVSIGYHYKELGVVMNMDVDTHRYRLSLKDLLLYAADPALHVASASALLDLRTCCFSVAAIT
SQ  SGVKFQTVKPGNFNQDFYEFILSKGLLKEGSSVDLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVNKYFEI
SQ  YDGGCIPATQVIVNNYDKSAGYPFNKFGKARLYYEALSFEEQDEVYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSI
SQ  LSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFYGGWDDMLRRLIKDVDSPVLMGWDYPKCDRAMPNILRIISSLVLARKH
SQ  DSCCSHTDRFYRLANECAQVLSEIVMCGGCYYVKPGGTSSGDATTAFANSVFNICQAVSANVCSLMACNGHKIEDLSIRE
SQ  LQKRLYSNVYRADHVDPAFVNEYYEFLNKHFSMMILSDDGVVCYNSEFASKGYIANISAFQQVLYYQNNVFMSEAKCWVE
SQ  TDIEKGPHEFCSQHTMLVKMDGDEVYLPYPDPSRILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENPEYQNVFR
SQ  VYLEYIKKLYNDLGNQILDSYSVILSTCDGQKFTDETFYKNMYLRSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCA
SQ  YDHVMSTDHKYVLSVSPYVCNSPGCDVNDVTKLYLGGMSYYCEDHKPQYSFKLVMNGMVFGLYKQSCTGSPYIEDFNKIA
SQ  SCKWTEVDDYVLANECTERLKLFAAETQKATEESFKQCYASATIREIVSDRELILSWEIGKVRPPLNKNYVFTGYHFTSN
SQ  GKTVLGEYVFDKSELTNGVYYRATTTYKLSVGDVFILTSHAVSSLSAPTLVPQENYTSIRFASVYSVPETFQNNVPNYQH
SQ  IGMKRYCTVQGPPGTGKSHLAIGLAVYYCTARVVYTAASHAAVDALCEKAYKFLNINDCTRIVPAKVRVDCYDKFKVNDT
SQ  TRKYVFTTINALPELVTDIIVVDEVSMLTNYELSVINSRVRAKHYVYIGDPAQLPAPRVLLNKGTLEPRYFNSVTKLMCC
SQ  LGPDIFLGTCYRCPKEIVDTVSALVYHNKLKAKNDNSSMCFKVYYKGQTTHESSSAVNMQQIYLISKFLKANPSWSNAVF
SQ  ISPYNSQNYVAKRVLGLQTQTVDSAQGSEYDFVIYSQTAETAHSVNVNRFNVAITRAKKGILCVMSSMQLFESLNFSTLT
SQ  LDKINNPRLQCTTNLFKDCSRSYAGYHPAHAPSFLAVDDKYKVGGDLAVCLNVADSAVTYSRLISLMGFKLDLTLDGYCK
SQ  LFITRDEAIRRVRAWVGFDAEGAHATRDSIGTNFPLQLGFSTGIDFVVEATGMFAERDGYVFKKAVARAPPGEQFKHLVP
SQ  LMSRGQKWDVVRIRIVQMLSDHLVDLADSVVLVTWAASFELTCLRYFAKVGKEVVCSVCNKRATCFNSRTGYYGCWRHSY
SQ  SCDYLYNPLIVDIQQWGYTGSLTSNHDLICSVHKGAHVASSDAIMTRCLAVHDCFCKSVNWSLEYPIISNEVSVNTSCRL
SQ  LQRVMFRAAMLCNRYDVCYDIGNPKGLACVKGYDFKFYDASPVVKSVKQFVYKYEAHKDQFLDGLCMFWNCNVDKYPANA
SQ  VVCRFDTRVLNKLNLPGCNGGSLYVNKHAFHTSPFTRAAFENLKPMPFFYYSDTPCVYMEGMESKQVDYVPLRSATCITR
SQ  CNLGGAVCLKHAEDYREYLESYNTATTAGFTFWVYKTFDFYNLWNTFTRLQSLENVVYNLVNAGHFDGRAGELPCAVIGE
SQ  KVIAKIQNEDVVVFKNNTPFPTNVAVELFAKRSIRPHPELKLFRNLNIDVCWSHVLWDYAKDSVFCSSTYKVCKYTDLQC
SQ  IESLNVLFDGRDNGALEAFKKCRDGVYINTTKIKSLSMIKGPQRADLNGVVVEKVGDSDVEFWFAMRRDGDDVIFSRTGS
SQ  LEPSHYRSPQGNPGGNRVGDLSGNEALARGTIFTQSRFLSSFAPRSEMEKDFMDLDEDVFIAKYSLQDYAFEHVVYGSFN
SQ  QKIIGGLHLLIGLARRQQKSNLVIQEFVPYDSSIHSYFITDENSGSSKSVCTVIDLLLDDFVDIVKSLNLNCVSKVVNVN
SQ  VDFKDFQFMLWCNEEKVMTFYPRLQAAADWKPGYVMPVLYKYLESPLERVNLWNYGKPITLPTGCLMNVAKYTQLCQYLN
SQ  TTTLAVPANMRVLHLGAGSDKDVAPGSAVLRQWLPAGSILVDNDINPFVSDSVASYYGNCITLPIACQWDLIISDMYDPL
SQ  TKNIGEYNVSKDGFFTYLCHLIRDKLALGGSVAIKITEFSWNAELYSLMGKFAFWTIFCTNVNASSSEGFLIGINWLNRT
SQ  RTEIDGKTMHANYLFWRNSTMWNGGAYSLFDMSKFPLKVAGTAVVSLKPDQINDLVLSLIEKGKLLVRDTRKEVFVGDSL
SQ  VNVK
//