ID  P0C6X3;
PN  2'-O-methyltransferase;
GN  rep;
OS  443240;
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. [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. [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. [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. [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. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6X3;
DR  UNIPROT: Q14EB2;
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;
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:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIKTSKYGLGFKWAPEFRWLLPDAAEELASPMKSDEGGLCPSTGQAMESVGFVYDNHVKIDCRCILGQEWHVQSNLIRDI
SQ  FVHEDLHVVEVLTKTAVKSGTAILIKSPLHSLGGFPKGYVMGLFRSYKTKRYVVHHLSMTTSTTNFGEDFLGWIVPFGFM
SQ  PSYVHKWFQFCRLYIEESDLIISNFKFDDYDFSVEDAYAEVHAEPKGKYSQKAYALLRQYRGIKPVLFVDQYGCDYSGKL
SQ  ADCLQAYGHYSLQDMRQKQSVWLANCDFDIVVAWHVVRDSRFVMRLQTIATICGIKYVAQPTEDVVDGAVVIREPVHLLS
SQ  ADAIVLKLPSLMKVMTHMDDFSIKSIYNVDLCDCGFVMQYGYVDCFNDNCDFYGWVSGNMMDGFSCPLCCTVYDSSEVKA
SQ  QSSGVIPENPVLFTNSTDTVNPDSFNLYGYSVTPFGSCIYWSPRPGLWIPIIKSSVKSYDDLVYSGVVGCKSIVKETALI
SQ  THALYLDYVQCKCGNLEQNHILGVNNSWCRQLLLNRGDYNMLLKNIDLFVKRRADFACKFAVCGDGFVPFLLDGLIPRSY
SQ  YLIQSGIFFTSLMSQFSQEVSDMCLKMCILFMDRVSVATFYIEHYVNRLVTQFKLLGTTLVNKMVNWFNTMLDASAPATG
SQ  WLLYQLLNGLFVVSQANFNFVALIPDYAKILVNKFYTFFKLLLECVTVDVLKDMPVLKTINGLVCIVGNKFYNVSTGLIP
SQ  GFVLPCNAQEQQIYFFEGVAESVIVEDDVIENVKSSLSSYEYCQPPKSVEKICIIDNMYMGKCGDKFFPIVMNDKNICLL
SQ  DQAWRFPCAGRKVNFNEKPVVMEIPSLMTVKVMFDLDSTFDDILGKVCSEFEVEKGVTVDDFVAVVCDAIENALNSCKDH
SQ  PVVGYQVRAFLNKLNENVVYLFDEAGDEAMASRMYCTFAIEDVEDVISSEAVEDTIDGVVEDTINDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEEIVTGDNDDQIVVTGDDVDDIESVYDFDTYKALLVFNDVYNDALFVSYGSSVETETYFKVNG
SQ  LWSPTITHTNCWLRSVLLVMQKLPFKFKDLAIENMWLSYKVGYNQSFVDYLLTTIPKAIVLPQGGYVADFAYWFLNQFDI
SQ  NAYANWCCLKCGFSFDLNGLDAVFFYGDIVSHVCKCGHNMTLIAADLPCTLHFSLFDDNFCAFCTPKKIFIAACAVDVNV
SQ  CHSVAVIGDEQIDGKFVTKFSGDKFDFIVGYGMSFSMSSFELAQLYGLCITPNVCFVKGDIINVARLVKADVIVNPANGH
SQ  MLHGGGVAKAIAVAAGKKFSKETAAMVKSKGVCQVGDCYVSTGGKLCKTILNIVGPDARQDGRQSYVLLARAYKHLNNYD
SQ  CCLSTLISAGIFSVPADVSLTYLLGVVDKQVILVSNNKEDFDIIQKCQITSVVGTKALAVRLTANVGRVIKFETDAYKLF
SQ  LSGDDCFVSNSSVIQEVLLLRHDIQLNNDVRDYLLSKMTSLPKDWRLINKFDVINGVKTVKYFECPNSIYICSQGKDFGY
SQ  VCDGSFYKATVNQVCVLLAKKIDVLLTVDGVNFKSISLTVGEVFGKILGNVFCDGIDVTKLKCSDFYADKILYQYENLSL
SQ  ADISAVQSSFGFDQQQLLAYYNFLTVCKWSVVVNGPFFSFEQSHNNCYVNVACLMLQHINLKFNKWQWQEAWYEFRAGRP
SQ  HRLVALVLAKGHFKFDEPSDATDFIRVVLKQADLSGAICELELICDCGIKQESRVGVDAVMHFGTLAKTDLFNGYKIGCN
SQ  CAGRIVHCTKLNVPFLICSNTPLSKDLPDDVVAANMFMGVGVGHYTHLKCGSPYQHYDACSVKKYTGVSGCLTDCLYLKN
SQ  LTQTFTSMLTNYFLDDVEMVAYNPDLSQYYCDNGKYYTKPIIKAQFKPFAKVDGVYTNFKLVGHDICAQLNDKLGFNVDL
SQ  PFVEYKVTVWPVATGDVVLASDDLYVKRYFKGCETFGKPVIWLCHDEASLNSLTYFNKPSFKSENRYSVLSVDSVSEESQ
SQ  GNVVTSVMESQISTKEVKLKGVRKTVKIEDAIIVNDENSSIKVVKSLSLVDVWDMYLTGCDYVVWVANELSRLVKSPTVR
SQ  EYIRYGIKPITIPIDLLCLRDDNQTLLVPKIFKARAIEFYGFLKWLFIYVFSLLHFTNDKTIFYTTEIASKFTFNLFCLA
SQ  LKNAFQTFRWSIFIKGFLVVATVFLFWFNFLYINVIFSDFYLPNISVFPIFVGRIVMWIKATFGLVTICDFYSKLGVGFT
SQ  SHFCNGSFICELCYSGFDMLDTYAAIDFVQYEVDRRVLFDYVSLVKLIVELVIGYSLYTVWFYPLFCLIGLQLFTTWLPD
SQ  LFMLETMHWLIRFIVFVANMLPAFVLLRFYIVVTAMYKVVGFIRHIVYGCNKAGCLFCYKRNCSVRVKCSTIVGGVIRYY
SQ  DITANGGTGFCVKHQWNCFNCHSFKPGNTFITVEAAIELSKELKRPVNPTDASHYVVTDIKQVGCMMRLFYDRDGQRVYD
SQ  DVDASLFVDINNLLHSKVKVVPNLYVVVVESDADRANFLNAVVFYAQSLYRPILLVDKKLITTACNGISVTQTMFDVYVD
SQ  TFMSHFDVDRKSFNNFVNIAHASLREGVQLEKVLDTFVGCVRKCCSIDSDVETRFITKSMISAVAAGLEFTDENYNNLVP
SQ  TYLKSDNIVAADLGVLIQNGAKHVQGNVAKAANISCIWFIDTFNQLTADLQHKLKKACVKTGLKLKLTFNKQEASVPILT
SQ  TPFSLKGGVVLSNLLYILFFISLICFILLWALLPTYSVYKSDIHLPAYASFKVIDNGVVRDISVNDLCFANKFFQFDQWY
SQ  ESTFGSFYYHNSMDCPIVVAVMDEDIGSTMFNVPTKVLRHGFHVLHFLTYAFASDSVQCYTPHIQISYNDFYASGCVLSS
SQ  LCTMFKRGDGTPHPYCYSDGVMKNASLYTSLVPHTRYSLANSNGFIRFPDVISEGIVRIVRTRSMTYCRVGACEYAEEGI
SQ  CFNFNSSWVLNNDYYRSMPGTFCGRDLFDLFYQFFSSLIRPIDFFSLTASSIFGAILAIVVVLVFYYLIKLKRAFGDYTS
SQ  VVVINVIVWCINFLMLFVFQVYPICACVYACFYFYVTLYFPSEISVIMHLQWIVMYGAIMPFWFCVTYVAMVIANHVLWL
SQ  FSYCRKIGVNVCNDSTFEETSLTTFMITKDSYCRLKNSVSDVAYNRYLSLYNKYRYYSGKMDTAAYREAACSQLAKAMET
SQ  FNHNNGNDVLYQPPTASVSTSFLQSGIVKMVSPTSKIEPCIVSVTYGSMTLNGLWLDDKVYCPRHVICLSSNMNEPDYSA
SQ  LLCRVTLGDFTIMSGRMSLTVVSYQMQGCQLVLTVSLQNPYTPKYTFGVVKPGETFTVLAAYNGRPQGAFHVTMRSSYTI
SQ  KGSFLCGSCGSVGYVLTGDSVKFVYMHQLELSTGCHTGTDFTGNFYGPYRDAQVVQLPVKDYVQTVNVIAWLYAAILNNC
SQ  AWFVQNDVCSIEDFNVWAMTNGFSQVKADLVLDALASMTGVSIETLLAAIKRLYMGFQGRQILGSCTFEDELAPSDVYQQ
SQ  LAGVKLQSKTKRFIKETIYWILISTFLFSCIISAFVKWTIFMYINTHMIGVTLCVLCFVSFMMLLVKHKHFYLTMYIIPV
SQ  LCTLFYVNYLVVYKEGFRGLTYVWLSYFVPAVNFTYVYEVFYGCILCVFAIFITMHSINHDIFSLMFLVGRIVTLISMWY
SQ  FGSNLEEDVLLFITAFLGTYTWTTILSLAIAKIVANWLSVNIFYFTDVPYIKLILLSYLFIGYILSCYWGFFSLLNSVFR
SQ  MPMGVYNYKISVQELRYMNANGLRPPRNSFEAILLNLKLLGIGGVPVIEVSQIQSKLTDVKCANVVLLNCLQHLHVASNS
SQ  RLWQYCSILHNEILSTSDLSVAFDKLAQLLIVLFANPAAVDTKCLASIDEVSDDYVQDSTVLQALQSEFVNMASFVEYEV
SQ  AKKNLADAKNSGSVNQQQIKQLEKACNIAKSVYERDKAVARKLERMADLALTNMYKEARINDKKSKVVSALQTMLFSMVR
SQ  KLDNQALNSILDNAVKGCVPLNAIPALAANTLTIIIPDKQVFDKVVDNVYVAYAGSVWHIQTVQDADGINKQLTDISVDS
SQ  NWPLVIIANRYNEVANAVMQNNELMPHKLKIQVVNSGSDMNCNIPTQCYYNNGSSGRIVYAVLSDVDGLKYTKIIKDDGN
SQ  CVVLELDPPCKFSIQDVKGLKIKYLYFIKGCNTLARGWVVGTLSSTIRLQAGVATEYAANSSILSLCAFSVDPKKTYLDY
SQ  IQQGGVPIINCVKMLCDHAGTGMAITIKPEATINQDSYGGASVCIYCRARVEHPDVDGLCKLRGKFVQVPLGIKDPILYV
SQ  LTHDVCQVCGFWRDGSCSCVGSGVAVQSKDLNFLNRVRGTSVNARLVPCASGLSTDVQLRAFDICNTNRAGIGLYYKVNC
SQ  CRFQRIDDDGNKLDKFFVVKRTNLEVYNKEKTYYELTKSCGVVAEHDFFTFDIDGSRVPHIVRKNLSKYTMLDLCYALRH
SQ  FDCNDCSVLCEILCEYADCKESYFSKKDWYDFVENPDIINIYKKLGPIFNRALLNTVSFADTLVKVGLVGVLTLDNQDLY
SQ  GQWYDFGDFIQTAPGFGVAVADSYYSYMMPMLTMCHVLDCELFVNDSYRQFDLVQYDFTDYKLELFNKYFKYWGMKYHPN
SQ  TVDCDNDRCIIHCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYHYKELGVVMNLDVDTHRYRLSLKDLLLYAAD
SQ  PAMHVASASALLDLRTCCFSVAAITSGIKFQTVKPGNFNQDFYEFVKSKGLFKEGSTVDLKHFFFTQDGNAAITDYNYYK
SQ  YNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPASQVIVNNYDKSAGYPFNKFGKARLYYEALSFEEQNEIYAYTKRNVLP
SQ  TLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFYGGWDDMLRHLIKDVDNPVLMGW
SQ  DYPKCDRAMPNILRIVSSLVLARKHEFCCSHGDRFYRLANECAQVLSEIVMCGGCYYVKPGGTSSGDATTAFANSVFNIC
SQ  QAVTANVCSLMACNGHKIEDLSIRNLQKRLYSNVYRTDYVDYTFVNEYYEFLCKHFSMMILSDDGVVCYNSDYASKGYIA
SQ  NISVFQQVLYYQNNVFMSESKCWVENDITNGPHEFCSQHTMLVKIDGDYVYLPYPDPSRILGAGCFVDDLLKTDSVLLIE
SQ  RFVSLAIDAYPLVHHENEEYQKVFRVYLEYIKKLYNDLGNQILDSYSVILSTCDGLKFTDESFYKNMYLKSAVMQSVGAC
SQ  VVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATNHKYVLSVSPYVCNAPNCDVSDVTKLYLGGMSYYCENHKPHYSFKLVM
SQ  NGMVFGLYKQSCTGSPYIDDFNKIASCKWTEVDDYVLANECIERLKLFAAETQKATEEAFKQSYASATIQEIVSDREIIL
SQ  CWETGKVKPPLNKNYVFTGYHFTSTGKTVLGEYVFDKSELTNGVYYRATTTYKLSIGDVFVLTSHSVANLSAPTLVPQEN
SQ  YASIRFSSVYSVPLLFQTNVANYQHIGMKRYCTVQGPPGTGKSHLAIGLAVYYYTARVVYTAASHAAVDALCEKAYKFLN
SQ  INDCTRIIPAKVRVDCYDKFKINDTTCKYVFTTINALPELVTDIVVVDEVSMLTNYELSVINARVKAKHYVYIGDPAQLP
SQ  APRVLLSKGSLEPRHFNSITKIMCCLGPDIFLGNCYRCPKEIVETVSALVYDNKLKAKNDNSSLCFKVYFKGQTTHESSS
SQ  AVNIQQIYLISKFLKANPVWNSAVFISPYNSQNYVAKRILGVQTQTVDSAQGSEYDYVIYSQTAETAHSINVNRFNVAIT
SQ  RAKKGIFCVMSNMQLFESLNFITLPLDKIQNQTLSRLHCTTNLFKDCSKNFLGYHPAHAPSFLSVDDKYKVNEDLAVCLN
SQ  ICEPVLTYSRLISLMGFKLDLTLDGYSKFFITKDEAIKRVRGWVGFDVEGAHATRDNIGTNFPLQIGFSTGVDFVVEATG
SQ  LFAERDCYIFKRTVAKAPPGDNFKHLIPLMSKGQKWDVVRIRIVQMLSDYLLDLSDSVVFITWSASFELTCLRYFAKLGR
SQ  ELNCDVCPNRATCYNSRTGYYGCWRHSYTCDYVYNPLIVDIQQWGYTGSLTSNHDIICNVHKGAHVASSDAIMTRCLAIY
SQ  DCFCKSVNWNLEYPIISNEVSINTSCRLLQRVMLKAAMLCNRYNLCYDIGNPKGIACVKDYEFKFYDASPVVKSVKQLFY
SQ  VYDVHKDNFKDGLCMFWNCNVDKYPSNSIVCRFDTRVLNKLNLPGCNGGSLYVNKHAFHTNPFTRTVFENLKPMPFFYYS
SQ  DTPCVYVDGLESKQVDYVPLRSATCITRCNLGGAVCSKHAEDYCKYLESYNVATTAGFTFWVYKTFDFYNLWNTFTMLQS
SQ  LENVIYNLVNAGHYDGRIGELPCAIMNDKVVVKINNVDTVIFKNNTSLPTNIAVELFTKRSIRHHPELKILRNLNIDICW
SQ  KHVLWDYVKDSLFCSSTYGVCKYTDLNFIENLNVLFDGRDNGALEAFRKARNGVFISTGKLSSLSMIKGPQRADLNGVIV
SQ  DKVGELNVEFWFAMRKDGDDVIFSRADSLSPSHYWSPQGNLGGNCAGNASGNDALARFTIFTQSRVLSTFEPRSDLERDF
SQ  IDMEDSLFIAKYGLEDYAFDHIVYGSFNYKVIGGLHLLIGLFRRLKKSNLVIQEFLQYDSSIHSYFITDQECGSSKSVCT
SQ  VIDLLLDDFVVIVKSLNLNCVSKVVNINVDFKDFQFMLWCNDNKIMTFYPKMQATSDWKPGYSMPVLYKYLNVPLERVSL
SQ  WNYGKAINLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGAGSDKEVAPGSAVLRQWLPSGSILVDNDLNPFVSDS
SQ  LVTYFGDCMTLPFDCHWDLIISDMYDPLTKNIGDYNVSKDGFFTYICYLIRDKLSLGGSVAIKITEFSWNADLYKLMSYF
SQ  AFWTVFCTNVNASSSEGFLIGINYLGKSCFEIDGNVMHANYLFWRNSTTWNGGAYSLFDMSKFSLKLAGTAVVNLRPDQL
SQ  NDLVYSLIERGKLLVRDTRKEIFVGDSLVNTC
//