ID A0A140GL81_9ENTO Unreviewed; 2193 AA. AC A0A140GL81; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 26-FEB-2020, entry version 27. DE RecName: Full=Genome polyprotein {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=P3 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 3AB {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=P2 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=P1 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP0 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=VP4-VP2 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP4 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=P1A {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Virion protein 4 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP2 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=P1B {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Virion protein 2 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP3 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=P1C {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Virion protein 3 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP1 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=P1D {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Virion protein 1 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protease 2A {ECO:0000256|RuleBase:RU364118}; DE Short=P2A {ECO:0000256|RuleBase:RU364118}; DE EC=3.4.22.29 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Picornain 2A {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Protein 2A {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 2B {ECO:0000256|RuleBase:RU364118}; DE Short=P2B {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 2C {ECO:0000256|RuleBase:RU364118}; DE Short=P2C {ECO:0000256|RuleBase:RU364118}; DE EC=3.6.1.15 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 3A {ECO:0000256|RuleBase:RU364118}; DE Short=P3A {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Viral protein genome-linked {ECO:0000256|RuleBase:RU364118}; DE Short=VPg {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Protein 3B {ECO:0000256|RuleBase:RU364118}; DE Short=P3B {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 3CD {ECO:0000256|RuleBase:RU364118}; DE EC=3.4.22.28 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protease 3C {ECO:0000256|RuleBase:RU364118}; DE Short=P3C {ECO:0000256|RuleBase:RU364118}; DE EC=3.4.22.28 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU364118}; DE Short=RdRp {ECO:0000256|RuleBase:RU364118}; DE EC=2.7.7.48 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=3D polymerase {ECO:0000256|RuleBase:RU364118}; DE Short=3Dpol {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Protein 3D {ECO:0000256|RuleBase:RU364118}; DE Short=3D {ECO:0000256|RuleBase:RU364118}; OS Coxsackievirus A16. OC Viruses; Riboviria; Picornavirales; Picornaviridae; Enterovirus; OC Enterovirus A. OX NCBI_TaxID=31704 {ECO:0000313|EMBL:AMN10105.1, ECO:0000313|Proteomes:UP000152758}; RN [1] {ECO:0000313|EMBL:AMN10105.1, ECO:0000313|Proteomes:UP000152758} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CA16-193 {ECO:0000313|EMBL:AMN10105.1}; RX PubMed=27667023; DOI=10.1038/srep34299; RA Sun Y.S., Li Y.J., Xia Y., Xu F., Wang W.W., Yang Z.N., Lu H.J., Chen Z.P., RA Miao Z.P., Liang W.F., Xu Z.Y., Dong H.J., Qiu D.H., Zhu Z.Y., RA van der Veen S., Qian J., Zhou B., Yao P.P., Zhu H.P.; RT "Coxsackievirus A16 induced neurological disorders in young gerbils which RT could serve as a new animal model for vaccine evaluation."; RL Sci. Rep. 6:34299-34299(2016). CC -!- FUNCTION: Capsid protein VP0: Component of immature procapsids, which CC is cleaved into capsid proteins VP4 and VP2 after maturation. Allows CC the capsid to remain inactive before the maturation step. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 CC symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms CC in diameter, composed of 60 copies of each capsid protein and enclosing CC the viral positive strand RNA genome. Capsid protein VP1 mainly forms CC the vertices of the capsid. Capsid protein VP1 interacts with host cell CC receptor to provide virion attachment to target host cells. This CC attachment induces virion internalization. Tyrosine kinases are CC probably involved in the entry process. After binding to its receptor, CC the capsid undergoes conformational changes. Capsid protein VP1 N- CC terminus (that contains an amphipathic alpha-helix) and capsid protein CC VP4 are externalized. Together, they shape a pore in the host membrane CC through which viral genome is translocated to host cell cytoplasm. CC After genome has been released, the channel shrinks. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 CC symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms CC in diameter, composed of 60 copies of each capsid protein and enclosing CC the viral positive strand RNA genome. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 CC symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms CC in diameter, composed of 60 copies of each capsid protein and enclosing CC the viral positive strand RNA genome. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Capsid protein VP4: Lies on the inner surface of the capsid CC shell. After binding to the host receptor, the capsid undergoes CC conformational changes. Capsid protein VP4 is released, Capsid protein CC VP1 N-terminus is externalized, and together, they shape a pore in the CC host membrane through which the viral genome is translocated into the CC host cell cytoplasm. After genome has been released, the channel CC shrinks. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protease 2A: Cysteine protease that cleaves viral polyprotein CC and specific host proteins. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protease 3C: cleaves host DDX58/RIG-I and thus contributes to CC the inhibition of type I interferon production. Cleaves also host CC PABPC1. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 2B: Plays an essential role in the virus replication CC cycle by acting as a viroporin. Creates a pore in the host reticulum CC endoplasmic and as a consequence releases Ca2+ in the cytoplasm of CC infected cell. In turn, high levels of cytoplasmic calcium may trigger CC membrane trafficking and transport of viral ER-associated proteins to CC viroplasms, sites of viral genome replication. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 2C: Induces and associates with structural CC rearrangements of intracellular membranes. Displays RNA-binding, CC nucleotide binding and NTPase activities. May play a role in virion CC morphogenesis and viral RNA encapsidation by interacting with the CC capsid protein VP3. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 3A: Localizes the viral replication complex to the CC surface of membranous vesicles. It inhibits host cell endoplasmic CC reticulum-to-Golgi apparatus transport and causes the dissassembly of CC the Golgi complex, possibly through GBF1 interaction. This would result CC in depletion of MHC, trail receptors and IFN receptors at the host cell CC surface. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 3AB: Localizes the viral replication complex to the CC surface of membranous vesicles. Together with protein 3CD binds the CC Cis-Active RNA Element (CRE) which is involved in RNA synthesis CC initiation. Acts as a cofactor to stimulate the activity of 3D CC polymerase, maybe through a nucleid acid chaperone activity. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 3CD: Is involved in the viral replication complex and CC viral polypeptide maturation. It exhibits protease activity with a CC specificity and catalytic efficiency that is different from protease CC 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context CC of protein 3CD may have an RNA binding activity. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: RNA-directed RNA polymerase: Replicates the viral genomic RNA CC on the surface of intracellular membranes. May form linear arrays of CC subunits that propagate along a strong head-to-tail interaction called CC interface-I. Covalently attaches UMP to a tyrosine of VPg, which is CC used to prime RNA synthesis. The positive stranded RNA genome is first CC replicated at virus induced membranous vesicles, creating a dsRNA CC genomic replication form. This dsRNA is then used as template to CC synthesize positive stranded RNA genomes. ss(+)RNA genomes are either CC translated, replicated or encapsidated. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Viral protein genome-linked: acts as a primer for viral RNA CC replication and remains covalently bound to viral genomic RNA. VPg is CC uridylylated prior to priming replication into VPg-pUpU. The oriI viral CC genomic sequence may act as a template for this. The VPg-pUpU is then CC used as primer on the genomic RNA poly(A) by the RNA-dependent RNA CC polymerase to replicate the viral genome. VPg may be removed in the CC cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved CC off virion genomes because replicated genomic RNA are encapsidated at CC the site of replication. {ECO:0000256|RuleBase:RU364118}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus CC polyprotein. In other picornavirus reactions Glu may be substituted CC for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; CC Evidence={ECO:0000256|RuleBase:RU364118, CC ECO:0000256|SAAS:SAAS01116669}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus CC polyprotein.; EC=3.4.22.29; Evidence={ECO:0000256|RuleBase:RU364118}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; CC Evidence={ECO:0000256|RuleBase:RU364118}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; CC EC=2.7.7.48; Evidence={ECO:0000256|RuleBase:RU364118, CC ECO:0000256|SAAS:SAAS01198479}; CC -!- SUBUNIT: Capsid protein VP1: Interacts with capsid protein VP0, and CC capsid protein VP3 to form heterotrimeric protomers. Five protomers CC subsequently associate to form pentamers which serve as building blocks CC for the capsid. Interacts with capsid protein VP4 in the mature capsid CC (By similarity). Capsid protein VP0: interacts with capsid protein VP1 CC and capsid protein VP3 to form heterotrimeric protomers. Five protomers CC subsequently associate to form pentamers which serve as building blocks CC for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 CC and capsid protein VP3 in the mature capsid (By similarity). Capsid CC protein VP3: interacts with capsid protein VP0 and capsid protein VP1 CC to form heterotrimeric protomers. Five protomers subsequently associate CC to form pentamers which serve as building blocks for the capsid. CC Interacts with capsid protein VP4 in the mature capsid (By similarity). CC Capsid protein VP4: Interacts with capsid protein VP1 and capsid CC protein VP3 (By similarity). Protein 2C: interacts with capsid protein CC VP3; this interaction may be important for virion morphogenesis (By CC similarity). Protein 3AB: interacts with protein 3CD (By similarity). CC Viral protein genome-linked: interacts with RNA-directed RNA polymerase CC (By similarity). Protein 3CD: interacts with protein 3AB and with RNA- CC directed RNA polymerase. RNA-directed RNA polymerase: interacts with CC viral protein genome-linked and with protein 3CD. CC {ECO:0000256|RuleBase:RU364118}. CC -!- SUBCELLULAR LOCATION: Host cytoplasmic vesicle membrane CC {ECO:0000256|SAAS:SAAS00711512}; Peripheral membrane protein CC {ECO:0000256|SAAS:SAAS00711512}; Cytoplasmic side CC {ECO:0000256|SAAS:SAAS00711512}. Virion CC {ECO:0000256|SAAS:SAAS01196568}. CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family. CC {ECO:0000256|RuleBase:RU364118}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KU854873; AMN10105.1; -; Genomic_RNA. DR Proteomes; UP000152758; Genome. DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW. DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW. DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW. DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW. DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW. DR GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IEA:UniProtKB-KW. DR GO; GO:0039540; P:suppression by virus of host RIG-I activity; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR CDD; cd00205; rhv_like; 3. DR Gene3D; 1.10.10.870; -; 1. DR Gene3D; 2.60.120.20; -; 3. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir. DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014838; P3A. DR InterPro; IPR036203; P3A_soluble_dom. DR InterPro; IPR000081; Peptidase_C3. DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR003138; Pico_P1A. DR InterPro; IPR002527; Pico_P2B. DR InterPro; IPR001676; Picornavirus_capsid. DR InterPro; IPR033703; Rhv-like. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR029053; Viral_coat. DR Pfam; PF08727; P3A; 1. DR Pfam; PF00548; Peptidase_C3; 1. DR Pfam; PF02226; Pico_P1A; 1. DR Pfam; PF00947; Pico_P2A; 1. DR Pfam; PF01552; Pico_P2B; 1. DR Pfam; PF00680; RdRP_1; 1. DR Pfam; PF00073; Rhv; 3. DR Pfam; PF00910; RNA_helicase; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50494; SSF50494; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF89043; SSF89043; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51218; SF3_HELICASE_2; 1. PE 3: Inferred from homology; KW Activation of host autophagy by virus {ECO:0000256|RuleBase:RU364118}; KW ATP-binding {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS01198603}; KW Capsid protein {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS01196445}; Coiled coil {ECO:0000256|SAM:Coils}; KW Covalent protein-RNA linkage {ECO:0000256|RuleBase:RU364118}; KW Eukaryotic host gene expression shutoff by virus KW {ECO:0000256|RuleBase:RU364118}; KW Eukaryotic host translation shutoff by virus KW {ECO:0000256|RuleBase:RU364118}; KW Helicase {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS01199809}; KW Host cytoplasm {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711571}; KW Host cytoplasmic vesicle {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711589}; KW Host gene expression shutoff by virus {ECO:0000256|RuleBase:RU364118}; KW Host membrane {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00795395}; KW Host mRNA suppression by virus {ECO:0000256|RuleBase:RU364118}; KW Host-virus interaction {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711757}; KW Hydrolase {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS01198589}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|RuleBase:RU364118}; KW Inhibition of host mRNA nuclear export by virus KW {ECO:0000256|RuleBase:RU364118}; KW Inhibition of host RIG-I by virus {ECO:0000256|RuleBase:RU364118}; KW Inhibition of host RLR pathway by virus {ECO:0000256|RuleBase:RU364118}; KW Ion channel {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS00711528}; KW Ion transport {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711758}; KW Lipoprotein {ECO:0000256|RuleBase:RU364118}; KW Membrane {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS00795440}; KW Myristate {ECO:0000256|RuleBase:RU364118}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS01198580}; KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS01198562}; KW Pore-mediated penetration of viral genome into host cell KW {ECO:0000256|RuleBase:RU364118}; KW Protease {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS01199734}; KW Repeat {ECO:0000256|RuleBase:RU364118}; KW RNA-binding {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS00711776}; KW RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS01198530}; KW T=pseudo3 icosahedral capsid protein {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS01130245}; KW Thiol protease {ECO:0000256|SAAS:SAAS01199735}; KW Transferase {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS01198537}; KW Transport {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS00711554}; KW Viral attachment to host cell {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711583}; KW Viral immunoevasion {ECO:0000256|RuleBase:RU364118}; KW Viral ion channel {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711569}; KW Viral penetration into host cytoplasm {ECO:0000256|RuleBase:RU364118}; KW Viral RNA replication {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS01198628}; KW Virion {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS01196585}; KW Virus endocytosis by host {ECO:0000256|RuleBase:RU364118}; KW Virus entry into host cell {ECO:0000256|RuleBase:RU364118, KW ECO:0000256|SAAS:SAAS00711553}. FT DOMAIN 1216..1374 FT /note="SF3 helicase" FT /evidence="ECO:0000259|PROSITE:PS51218" FT DOMAIN 1958..2074 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1164..1184 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 2193 AA; 243302 MW; B81B96ED25B19D4F CRC64; MGSQVSTQRS GSHENSNSAS EGSTINYTTI NYYKDAYAAS AGRQDMSQDP KKFTDPVMDV IHEMAPPLKS PSAEACGYSD RVAQLTIGNS TITTQEAANI VIAYGEWPEY CPDTDATAVD KPTRPDVSVN RFFTLDTKSW AKDSKGWYWK FPDVLTEVGV FGQNAQFHYL YRSGFCVHVQ CNASKFHQGA LLVAVLPEYV LGTIAGGTGN ENSHPPYATT QPGQVGAVLT HPYVLDAGIP LSQLTVCPHQ WINLRTNNCA TIIVPYMNTV PFDSALNHCN FGLLVIPVVP LDFNTGATSE IPITVTIAPM CAEFAGLRQA VKQGIPTELK PGTNQFLTTD DGVSAPILPG FHPTPPIHIP GEVHNLLEIC RVETILEVNN LKTNETTPMQ RLCFPVSVQS KTGELCAAFR ADPGRDGPWQ STILGQLCRY YTQWSGSLEV TFMFAGSFMA TGKMLIAYTP PGGNVPADRI TAMLGTHVIW DFGLQSSVTL VVPWISNTHY RAHARAGYFD YYTTGIITIW YQTNYVVPIG APTTAYIVAL AAAQDNFTMK LCKDTEDIEQ TANIQGDPIA DMIDQTVNNQ VNRSLTALQV LPTAANTEAS SHRLGTGVVP ALQAAETGAS SNASDKNLIE TRCVLNHHST QETAIGNFFS RAGLVSIITM PTTGTQNTDG YVNWDIDLMG YAQLRRKCEL FTYMRFDAEF TFVVAKPNGE LVPQLLQYMY VPPGAPKPTS RDSFAWQTAT NPSVFVKMTD PPAQVSVPFM SPASAYQWFY DGYPTFGEHL QANDLDYGQC PNNMMGTFSI RTVGTEKSPH SITLRVYMRI KHVRAWIPRP LRNQPYLFKT NPNYKGNDIK CTSTSRDKIT TLGEFGQQSG AIYVGNYRVV NRHLATHNDW ANLVWEDSSR DLLVSSTTAQ GCDTIARCNC QTGIYYCSSK RKHYPVSFTK PSLIFVEASE YYPARYQSHL MLAVGHSEPG DCGGILRCQH GVVGIVSTGG NGLVGFADVR DLLWLDEEAM EQGVSDYIKG LGDAFGMGFT DAVSREVEAL KNHLIGSEGA VEKILKNLVK LISALVIVVR SDYDMVTLTA TLALIGCHGS PWAWIKAKTA SILGIPIVQK QSASWLKKFN DMANAAKGLE WISSKISKFI DWLKEKIIPA AKEKVEFLNN LKQLPLLENQ ISNLEQSAAS QEDLEAMFGN VSYLAHFCRK FQPLYATEAK RVYALEKRMN NYMQFKSKHR IEPVCLIIRG SPGTGKSLAT GIIARAIADK YHSSVYSLPP DPDHFDGYKQ QVVTVMDDLC QNPDGKDMSL FCQMVSTVDF IPPMASLEEK GVSFTSKFVV ASTNASNIVV PTVSDSDAIR RRFYMDCDIE VTDSYKTDLG RLDAGRAAKL CTENNTANFK RCSPLVCGKA IQLRDRKSKV RYSIDTVVSE LIREYNNRSA IGNTIEALFQ GPPKFKPIRI SLEEKPAPDA ISDLLASVDS EEVRQYCREQ GWIIPETPTN VERHLNRAVL VMQSIATVVA VVSLVYVIYK LFAGFQGAYS GAPKQALKKP VLRTATVQGP SLDFALSLLR RNIRQVQTDQ GHFTMLGVRD RLAILPRHSQ PGKTIWVEHK LINVLDAVEL VDEQGVNLEL TLITLDTNEK FRDVTKFIPE TITGASDATL IINTEHMPSM FVPVGDVVQY GFLNLSGKPT HRTMMYNFPT KAGQCGGVVT SVGKIIGIHI GGNGRQGFCA GLKRSYFASE QGEIQWMKPN KETGRLNING PTRTKLEPSV FHDVFEGSKE PAVLTSKDPR LEVNFEQALF SKYVGNTLHE PDEYVTQAAL HYANQLKQLD INTNKMSMEE ACYGTEYLEA IDLHTSAGYP YSALGVKKRD ILDPITRDTT KMKFYMDKYG LDLPYSTYVK DELRSLDKIK KGKSRLIEAS SLNDSVYLRM TFGHLYETFH ANPGTVTGSA VGCNPDVFWS KLPILLPGSL FAFDYSGYDA SLSPVWFRAL EVVLREIGYS EEAVSLIEGI NHTHHVYRNK TYCVLGGMPS GCSGTSIFNS MINNIIIRTL LIKTFKGIDL DELNMVAYGD DVLASYPFPV DCSELARTGK EYGLTMTPAD KSPCFNEVTW ENATFLKRGF LPDYQFPFLI HPTMPMREIH ESIRWTKDAR NTQDHVRSLC LLAWHNGKEE YEKFVSTIRS VPIGKALAIP NFENLRRNWL ELF //