ID  P29846;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  31645;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: P29846;
DR  UNIPROT: A7YCU9;
DR  PDB: 1N64;
DR  PDB: 2ZJO;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (PubMed:12208879). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF- induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000269|PubMed:12208879, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (PubMed:9557650). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2, ECO:0000269|PubMed:9557650}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
DE  Interaction: O43889; IntAct: EBI-909649; Score: 0.59
DE  Interaction: P29846; IntAct: EBI-9303365; Score: 0.54
DE  Interaction: P61978; IntAct: EBI-8849316; Score: 0.64
DE  Interaction: P36941; IntAct: EBI-9099695; Score: 0.62
DE  Interaction: P08107; IntAct: EBI-9293903; Score: 0.62
DE  Interaction: P11142; IntAct: EBI-9293821; Score: 0.35
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0043433;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNGKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTWERSQPRGRRQPIPKARQPEGRAWAQPG
SQ  YPWPLYGNEGLGWAGWLVSPRGSRPNWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGVARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVHNVSGIYHVTNDCSNSSIVYEAADMIMHTPGCVPCVRENNSSRCWV
SQ  ALTPTLAARNNSVPTATIRRHVDLLVGAAAFCSAMYVGDLCGSVFLVSQLFTFSPRRYETVQDCNCSIYPGHVTGHRMAW
SQ  DMMMNWSPTTALVVSQLLRIPQAVVDMVGGAHWGVLAGLAYYSMVGNWAKVLIVMLLFAGVDGSTIVSGGTVARTTHSLA
SQ  SLFTQGASQKIQLINTNGSWHINRTALNCNDSLQTGFLASLFYAHRFNASGCPERMASCRSIDKFDQGWGPITYTEADIQ
SQ  DQRPYCWHYAPRPCGIVPASQVCGPVYCFTPSPVVVGTTDRFGAPTYSWGENETDVLILNNTRPPQGNWFGCTWMNSTGF
SQ  TKTCGGPPCNIGGGGNNTLVCPTDCFRKHPEATYTKCGSGPWLTPRCMVDYPYRLWHYPCTVNFTIFKVRMYVGGVEHRL
SQ  NAACNWTRGERCDLEDRDRSELSPLLLSTTEWQILPCSFTGLPALSTGLIHLHQNVVDVQYLYGIGSAVVSFAIKWEYIL
SQ  LLFLLLADARVCACLWMMLLIAQAEAALENLVVFNAASVAGMHGTLSFLVFFCAAWYIKGRLVPGAAYALYGVWPLLLLL
SQ  LALPPRAYAMDREMAASCGGAVFVGLVLLTLSPHYKMFLARLIWWLQYFITRAEAHLQVWIPPLNVRGGRDAIILLTCAA
SQ  YPELIFDITKILLAILGPLMVLQAGLTRIPYFVRAQGLIRACMLVRKAAGGHYVQMALMKLAALTGTYVYDHLTPLQDWA
SQ  HTGLRDLAVAVEPVVFSDMETKIITWGADTAACGDIILGLPVSARRGREILLGPADSLEGRGWRLLAPITAYAQQTRGLF
SQ  GCIITSLTGRDKNQVEGEVQVVSTATQSFLATCINGVCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWHAPQGARSL
SQ  TPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPSGHVVGIFRAAVCTRGVAKAVDFVPVES
SQ  METTMRSPVFTDNSSPPAVPQAFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGVDPNIRT
SQ  GVRTITTGAPITYSTYGKFLADGGCSGGAYDIIMCDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHP
SQ  NIEEIALSNTGEIPFYGKAIPIETIKGGRHLIFCHSKKKCDELAAKLSALGIHAVAYYRGLDVSVIPASGNVVVVATDAL
SQ  MTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTMPQDAVSRSQRRGRTSRGRRGIYRFVTPGERPSGMFDSSVLCEC
SQ  YDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAP
SQ  PPSWDQMWKCLTRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSV
SQ  VIVGRIILSGKPAVVPDREVLYQEFDEMEECASHLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESKWRTLEAF
SQ  WANDMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLTTQSTLLFNILGGWVAAQLAPPGAASAFVGAGIAGAAVG
SQ  SIGLGKVLVDMVAGYGAGVAGALVAFKVMSGEMPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVDPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDAAARVTQILSGLTITQLLRRLHQWINEDCSTPCSGSWLRDVWDWICTVLADFKTWLQSKLL
SQ  PRLPGVPFFSCQRGYKGVWRGDGIMQTTCPCGAQLTGHVKNGSMRIWGPKTCSNTWHGTFPINAYTTGPCTPSPAPNYSR
SQ  ALWRVAAEEYVEVRRVGDFHYVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPACKPLLREEVSFQVGLNQYVVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSALSLKAACTTRHTPPDADLIEANLLWRQEMGGN
SQ  ITRVESENKVVILDSFDPLRAEEDEREVSVPAEILRKSRKFPPALPVWARPDYNPPLLEPWKDPDYVPPVVHGCPLPPVK
SQ  APPIPPPRRKRTVVLTESTVSSALAELATKTFGSSESSAAGSGTATAPPDQPSDDGDAGSDVESCSSMPPLEGEPGDPDL
SQ  SDGSWSTVSEEDGEGVICCSMSYTWTGALITPCAAEESKLPINALSNSLLRHHNMVYATTSRSASQRQKKVTIDRLQVLD
SQ  DHYRDVLKEMKAKASTVKAKLLSVEEACKLTPPHSARSKFGYGAKDVRNLSGKAINHIRSVWKDLLEDTETPIDTTIMAK
SQ  NEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGSSYGFQYSPGQRVEFLVNAWKSKKCPMGFSYDT
SQ  RCFDSTVTESDIRVEESIYQCCDLAPEARQAIRSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKASA
SQ  ACRAAKLQDCTMLVCGDDLVVICESAGTQEDAASLRVFTEAMTRYSAPPGDLPQPEYDQELITSCSSNVSVAHDASGKRV
SQ  YYLTRDPTTPLARAAWATARHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQ
SQ  IIERLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRAWRHRARSVRAKLLSQGGRAATCGRYLFNWAVKTKLKLTPIPA
SQ  ASQLDLSKWFVAGYGGGDIYHSLSRARPRWFMLCLLLLSVGVGIYLLPNR
//