ID  P0C6W9;
PN  2'-O-methyltransferase;
GN  rep;
OS  11132;
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: P0C6W9;
DR  UNIPROT: Q66198;
DR  UNIPROT: Q9WQ81;
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: No;
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  MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDIVCSTTAQKLETGGICPENHVMVDCRRLLKQECCVQSSLIREI
SQ  VMNTRPYDLEVLLQDALQSREAVLVTPPLGMSLEACYVRGCNPNGWTMGLFRRRSVCNTGRCAVNKHVAYQLYMIDPAGV
SQ  CFGAGQFVGWVIPLAFMPVQSRKFIVPWVMYLRKCGEKGAYNKDHKRGGFEHVYNFKVEDAYDLVHDEPKGKFSKKAYAL
SQ  IRGYRGVKPLLYVDQYGCDYTGGLADGLEAYADKTLQEMKALFPIWSQELPFDVTVAWHVVRDPRYVMRLQSASTIRSVA
SQ  YVANPTEDLCDGSVVIKEPVHVYADDSIILRQHNLVDIMSCFYMEADAVVNAFYGVDLKDCGFVMQFGYIDCEQDLCDFK
SQ  GWVPGNMIDGFACTTCGHVYETGDLLAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWI
SQ  PILKSSVKSYDGLVYTGVVGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLLNRGVYKPLLENIDYF
SQ  NMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYAGKICHAVVSKSKELLDVSLDSLGAAIHYLNSKIVD
SQ  LAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFVKNIPRYASAVAQAFRSVAKVVLDSLRV
SQ  TFIDGLSCFKIGRRRICLSGSKIYEVERGLLHSSQLPLDVYDLTMPSQVQKTKQKPIYLKGSGSDFSLADSVVEVVTTSL
SQ  TPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDGHVGLLDQAWRVPCAGRCVTFKEQPTVNEIASTPKTIKVFYELD
SQ  KDFNTILNTACGVFEVDDTVDMEEFYAVVIDAIEEKLSPCKELEGVGAKVSAFLQKLEDNSLFLFDEAGEEVLAPKLYCA
SQ  FTAPEDDDFLEESGVEEDDVEGEETDLTVTSAGEPCVASEQEESSEILEDTLDDGPCVETSDSQVEEDVQMSDFVDLESV
SQ  IQDYENVCFEFYTTEPEFVKVLDLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPA
SQ  NIVVPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHVCKCGESMVLIDVDVPFTAHFALKD
SQ  KLFCAFITKRSVYKAACVVDVNDSHSMAVVDGKQIDDHRITSITSDKFDFIIGHGMSFSMTTFEIAQLYGSCITPNVCFV
SQ  KGDIIKVSKRVKAEVVVNPANGHMAHGGGVAKAIAVAAGQQFVKETTDMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPD
SQ  ARTQGKQSYALLERVYKHLNKYDCVVTTLISAGIFSVPSDVSLTYLLGTAKKQVVLVSNNQEDFDLISKCQITAVEGTKK
SQ  LAERLSFNVGRSIVYETDANKLILSNDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVVPEGWRVVNKFYQINGV
SQ  RTVKYFECPGGIDICSQDKVFGYVQQGSFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGESFGKSLGNVFCDGVN
SQ  VTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCSKWQVVFNGKYFTFKQANNNCFVNVSCLML
SQ  QSLNLKFKIVQWQEAWLEFRSGRPARFVSLVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTG
SQ  VDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFKGDKVGHYVHVKCEQSYQL
SQ  YDASNVKKVTDVTGNLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYKPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVY
SQ  TNFKLIGHTVCDILNAKLGFDSSKEFVEYKVTEWPTATGDVVLATDDLYVKRYERGCITFGKPVIWLSHEQASLNSLTYF
SQ  NRPLLVDENKFDVLKVDDVDDGGDISESDAKEPKEINIIKLSGVKKPFKVEDSVIVNDDTSEIKYVKSLSIVDVYDMWLT
SQ  GCRCVVRTANALSRAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPVFNVVKAVRNKISACFNFIKWLFVLLFGWIKISA
SQ  DNKVIYTTEVASKLTCKLVALAFKNAFLTFKWSVVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIAQW
SQ  IKNTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALY
SQ  TAWFYPLFALISIQILTTWLPELFMLSTLHWSVRLLVSLANMLPAHVFMRFYIIIASFIKLFSLFRHVAYGCSKSGCLFC
SQ  YKRNRSLRVKCSTIVGGMIRYYDAMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVT
SQ  DVKQVGCYMRLFYDRDGQRTYDDVNASLFVDYSNLLHSKVKSVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDK
SQ  NLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQICKVLDTFLSCARKSCSIDSDVDTKCLAD
SQ  SVMSAVSAGLELTDESCNNLVPTYLKGDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKAC
SQ  CKTGLKLKLTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFVLSLVCFIGLWCLMPTYTVHKSDFQLPVYASYKVLDNGV
SQ  IRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVVDQDFGSTVFNVPTKVLRYGYHVLHFITHALSADGVQ
SQ  CYTPHSQISYSNFYASGCVLSSACTMFAMADGSPQPYCYTDGLMQNASLYSSLVPHVRYNLANAKGFIRFPEVLREGLVR
SQ  IVRTRSMPYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILA
SQ  VIVVLVFYYLIKLKRAFGDYTSIVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGT
SQ  IMPLWFCLLYISVVVSNHAFWVFSYCRQLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYS
SQ  GKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCIVSVTYGNMTLNGLWLGD
SQ  KVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMQGCMLVLTVTLQNSRTPKYTFGVVKPGETFTV
SQ  LAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVVYVIMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLP
SQ  VQDYIQSVNFVAWLYAAILNNCNWFVQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKHLKNGFQ
SQ  GRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLVKGIVCWIMASTFLFSCIITAFVKWTMFMYVTTNMLSITFCALCV
SQ  ISLTMLLVKHKHLYLTMYIIPVLFTLLYNNYLVVYKQTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLIGMVFVTLRSI
SQ  NQYLFSFIMFVGRVISVVSLWYMGSNLEEEILLMLASLFGTYTWTTALSMAAAKVIAKWVAVNVLYFTDIPQIKIVLVCY
SQ  LFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLT
SQ  DVKCANVVLLNCLQHLHVASNSKLWQYCSTLHNEILATSDLGVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKD
SQ  NTVLQALQSEFVNMASFVEYEVAKKNLDEACSSGSANQQQLKQLEKACNIAKSAYERDRAVARKLERMADLALTNMYKEA
SQ  RINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLTIIVPDKSVYDQVVDNVYVTYAGNVW
SQ  QIQTIQDSDGTNKQLHEISDDCNWPLVIIANRHNEVSATALQNNELMPAKLKTQVVNSGPDQTCNTPTQCYYNNSYNGKI
SQ  VYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDVKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYA
SQ  SNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTSQDSYGGASVCIYCRARVEHPDVDG
SQ  LCKLRGKFVQVPVGIKDPVSYVLTHDVCQVCGFWRDGSCSCVSTDTTVQSKDTNFLNRVRGTSVDARLVPCASGLSTDVQ
SQ  LRAFDICNASVAGIGLHLKVNCCRFQRVDENGDKLDQFFVVKRTDLTIYNREMECYERVKDCKFVAEHDFFTFDVEGSRV
SQ  PHIVRKDLTKYTMLDLCYALRHFDRNDCMLLCDILSIYAGCEQSYFTKKDWYDFVENPDIINVYKKLGPIFNRALVSATE
SQ  FADKLVEVGLVGILTLDNQDLNGKWYDFGDYVIAAPGCGVAIADSYYSYMMPMLTMCHALDCELYVNNAYRLFDLVQYDF
SQ  TDYKLELFNKYFKHWSMPYHPNTVDCQDDRCIIRCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYHYKELGIVM
SQ  NMDVDTHRYRLSLKDLLLYAADPALHVASASALYDLRTCCFSVAAITSGVKFQTVKPGNFNQDFYDFILSKGLLKEGSSV
SQ  DLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPASQVIVNNYDKSAGYPFNKFGKARLY
SQ  YEALSFEEQDEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFY
SQ  GGWDDMLRRLIKDVDNPVLMGWDYPKCDRAMPNILRIVSSLVLARKHEACCSQSDRFYRLANEYAQVLSEIVMCGGCYYV
SQ  KPGGTSSGDATTAFANSVFNICQAVSANVCALMSCNGNKIEDLSIRALQKRLYSHVYRSDMVDSTFVTEYYEFLNKHFSM
SQ  MILSDDGVVCYNSDYASKGYIANISAFQQVLYYQNNVFMSESKCWVENDINNGPHEFCSQHTMLVKMDGDDVYLPYPDPS
SQ  RILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENEEYQKVFRVYLEYIKKLYNELGNQILDSYSVILSTCDGQKF
SQ  TDESFYKNMYLRSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATDHKYVLSVSPYVCNAPGCDVNDVTKL
SQ  YLGGMSYYCEDHKPQYSFKLVMNGMVFGLYKQSCTGSPYIDDFNRIASCKWTDVDDYILANECTERLKLFAAETQKATEE
SQ  AFKQSYASATIQEIVSERELILSWEIGKVKPPLNKNYVFTGYHFTKNGKTVLGEYVFDKSELTNGVYYRATTTYKLSVGD
SQ  VFVLTSHSVANLSAPTLVPQENYSSIRFASVYSVLETFQNNVVNYQHIGMKRYCTVQGPPGTGKSHLAIGLAVYYCTARV
SQ  VYTAASHAAVDALCEKAYKFLNINDCTRIVPAKVRVECYDKFKINDTTRKYVFTTINALPEMVTDIVVVDEVSMLTNYEL
SQ  SVINARIRAKHYVYIGDPAQLPAPRVLLSKGTLEPKYFNTVTKLMCCLGPDIFLGTCYRCPKEIVDTVSALVYENKLKAK
SQ  NESSSLCFKVYYKGVTTHESSSAVNMQQIYLINKFLKANPLWHKAVFISPYNSQNFAARRVLGLQTQTVDSAQGSEYDYV
SQ  IYSQTAETAHSVNVNRFNVAITRAKKGILCVMSNMQLFEALQFTTLTVDKVPQAVETRVQCSTNLFKDCSKSYSGYHPAH
SQ  APSFLAVDDKYKATGDLAVCLGIGDSAVTYSRLTSLMGFKLDVTLDGYCKLFITKEEAVKRVRAWVGFDAEGAHATRDSI
SQ  GTNFPLQLGFSTGIDFVVEATGLFADRDGYSFKKAVAKAPPGEQFKHLIPLMTRGQRWDVVRPRIVQMFADHLIDLSDCV
SQ  VLVTWAANFELTCLRYFAKVGREISCNVCTKRATAYNSRTGYYGCWRHSVTCDYLYNPLIVDIQQWGYIGSLSSNHDLYC
SQ  SVHKGAHVASSDAIMTRCLAVYDCFCNNINWNVEYPIISNELSINTSCRVLQRVMLKAAMLCNRYTLCYDIGNPKAIACV
SQ  KDFDFKFYDAQPIVKSVKTLLYFFEAHKDSFKDGLCMFWNCNVDKYPPNAVVCRFDTRVLNNLNLPGCNGGSLYVNKHAF
SQ  HTKPFSRAAFEHLKPMPFFYYSDTPCVYMDGMDAKQVDYVPLKSATCITRCNLVGAVCLKHAEEYREYLNSYNTATTAGF
SQ  TFWVYKTFDFYNLWNTFTKLQSLENVVYNLVKTGHYTGQAGEMPCAIINDKVVAKIDKEDVVIFINNTTYPTNVAVELFA
SQ  KRSIRHHPELKLFRNLNIDVCWKHVIWDYARESIFCSNTYGVCMYTDLKFIDKLNVLFDGRDNGALEAFKRSNNGVYIST
SQ  TKVKSLSMIRGPPRAELNGVVVDKVGDTDCVFYFAVRKEGQDVIFSQFDSLRVSSNQSPQGNLGSNEPGNVGGNDALATS
SQ  TIFTQSRVISSFTCRTDMEKDFIALDQDVFIQKYGLEDYAFEHIVYGNFNQKIIGGLHLLIGLYRRQQTSNLVIQEFVSY
SQ  DSSIHSYFITDEKSGGSKSVCTVIDILLDDFVALVKSLNLNCVSKVVNVNVDFKDFQFMLWCNDEKVMTFYLRLQAASDW
SQ  KPGYSMPVLYKYLNSPMERVSLWNYGKPVTLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGAGSEKGVAPGSAVL
SQ  RQWLPAGTILVDNDLYPFVSDSVATYFGDCITLPFDCQWDLIISDMYDPITKNIGEYNVSKDGFFTYICHMIRDKLALGG
SQ  SVAIKITEFSWNAELYKLMGYFAFWTVFCTNANASSSEGFLIGINYLGKPKVEIDGNVMHANYLFWRNSTVWNGGAYSLF
SQ  DMAKFPLKLAGTAVINLRADQINDMVYSLLEKGKLLVRDTNKEVFVGDSMVNVI
//