POLG_HPE1H
ID POLG_HPE1H Reviewed; 2180 AA.
AC Q66578; Q90062;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Capsid protein VP0;
DE AltName: Full=P1AB;
DE AltName: Full=Virion protein 0;
DE Contains:
DE RecName: Full=Capsid protein VP3;
DE AltName: Full=P1C;
DE AltName: Full=Virion protein 3;
DE Contains:
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=P1D;
DE AltName: Full=Virion protein 1;
DE Contains:
DE RecName: Full=Protein 2A;
DE Short=P2A;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Short=P2C;
DE EC=3.6.1.15;
DE Contains:
DE RecName: Full=Protein 3A;
DE Short=P3A;
DE Contains:
DE RecName: Full=Protein 3B;
DE Short=P3B;
DE AltName: Full=VPg;
DE Contains:
DE RecName: Full=Protease 3C;
DE Short=P3C;
DE EC=3.4.22.28;
DE EC=3.4.22.29;
DE AltName: Full=Picornain 3C;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase 3D-POL;
DE Short=P3D-POL;
DE EC=2.7.7.48;
OS Human parechovirus 1 (strain Harris) (HPeV-1) (Echovirus 22).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Parechovirus.
OX NCBI_TaxID=103911;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9539; Macaca (macaques).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PROTEIN SEQUENCE OF 29-61; 67-80;
RP 290-297 AND 543-551.
RX PubMed=1528901; DOI=10.1073/pnas.89.18.8847;
RA Hyypiae T., Horsnell C., Maaronen M., Khan M., Kalkkinen N., Auvinen P.,
RA Kinnunen L., Stanway G.;
RT "A distinct picornavirus group identified by sequence analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8847-8851(1992).
RN [2]
RP PROTEIN SEQUENCE OF 6-22; 29-61; 67-80 AND 118-131.
RX PubMed=7966616; DOI=10.1128/jvi.68.12.8232-8238.1994;
RA Stanway G., Kalkinnen N., Roivainen M., Ghazi F., Khan M., Smyth M.,
RA Meurman O., Hyppiae T.;
RT "Molecular and biological characteristics of echovirus 22, a representative
RT of a new picornavirus group.";
RL J. Virol. 68:8232-8238(1994).
RN [3]
RP FUNCTION OF CAPSID PROTEINS.
RX PubMed=11160695; DOI=10.1128/jvi.75.4.1958-1967.2001;
RA Joki-Korpela P., Marjomaki V., Krogerus C., Heino J., Hyypia T.;
RT "Entry of human parechovirus 1.";
RL J. Virol. 75:1958-1967(2001).
RN [4]
RP INTERACTION WITH HOST ACBD3.
RX PubMed=23572552; DOI=10.1128/mbio.00098-13;
RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.;
RT "ACBD3 interaction with TBC1 domain 22 protein is differentially affected
RT by enteroviral and kobuviral 3A protein binding.";
RL MBio 4:E00098-E00098(2013).
CC -!- FUNCTION: Capsid proteins VP0, VP2, VP3 form a closed capsid enclosing
CC the viral positive strand RNA genome. Capsid proteins interact with
CC host alpha-V/beta-3 integrin heterodimer to provide virion attachment
CC target cell. This attachment induces virion internalization
CC predominantly through clathrin-mediated endocytosis.
CC {ECO:0000269|PubMed:11160695}.
CC -!- FUNCTION: [Protein 2A]: Is not a protease. {ECO:0000250}.
CC -!- FUNCTION: [Protein 2B]: Affects membrane integrity and cause an
CC increase in membrane permeability. {ECO:0000250}.
CC -!- FUNCTION: [Protein 2C]: Associates with and induces structural
CC rearrangements of intracellular membranes. It displays RNA-binding,
CC nucleotide binding and NTPase activities (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane
CC anchor. {ECO:0000250}.
CC -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC proteins from the precursor polyprotein. In addition to its proteolytic
CC activity, it binds to viral RNA, and thus influences viral genome
CC replication. RNA and substrate bind cooperatively to the protease (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and
CC antigenomic RNA by recognizing replications specific signals.
CC {ECO:0000255|PROSITE-ProRule:PRU00539}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus
CC polyprotein.; EC=3.4.22.29;
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 -!- 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:0000255|PROSITE-ProRule:PRU01222};
CC -!- SUBUNIT: [Protein 3A]: Interacts with host ACBD3.
CC {ECO:0000269|PubMed:23572552}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250}. Host
CC cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250}. Host
CC cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Protein 3B]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase 3D-POL]: Host
CC cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes
CC to the surface of intracellular membrane vesicles that are induced
CC after virus infection as the site for viral RNA replication. These
CC vesicles are derived from the endoplasmic reticulum (By similarity).
CC {ECO:0000250}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently linked to
CC the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC peptide primer for the polymerase (By similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages yield mature proteins. All cleavages
CC are catalyzed by P3C.
CC -!- PTM: The N-terminus of VP0 is blocked.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000305}.
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DR EMBL; L02971; AAA72291.1; -; Genomic_RNA.
DR EMBL; S45208; AAB23363.1; -; Genomic_RNA.
DR PIR; A46182; A46182.
DR PDB; 4UDF; EM; 20.00 A; 12/16/1A/1E/1I/1M/1Q/1U/1Y/22/26/2A/2E/2I/2M/2Q/2U/2Y/32/36/3A/3E/3I/3M/3Q/3U/3Y/42/46/4A=360-542, 13/17/1B/1F/1J/1N/1R/1V/1Z/23/27/2B/2F/2J/2N/2R/2V/2Z/33/37/3B/3F/3J/3N/3R/3V/3Z/43/47/4B=61-289.
DR PDB; 4Z92; X-ray; 3.10 A; A=543-776, B=290-542, C=1-289.
DR PDB; 5MJV; X-ray; 3.09 A; A=543-776, B=290-542, C=1-289.
DR PDBsum; 4UDF; -.
DR PDBsum; 4Z92; -.
DR PDBsum; 5MJV; -.
DR SMR; Q66578; -.
DR ELM; Q66578; -.
DR IntAct; Q66578; 1.
DR MEROPS; C03.023; -.
DR PRIDE; Q66578; -.
DR ABCD; Q66578; 1 sequenced antibody.
DR Proteomes; UP000002496; Genome.
DR Proteomes; UP000232771; 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:UniProtKB-EC.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:RHEA.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
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; 2.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR007053; LRAT_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
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 InterPro; IPR009419; VPP_parechovir_P3A.
DR InterPro; IPR009407; VPP_parechovir_P3B.
DR Pfam; PF06344; Parecho_VpG; 1.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF06363; Picorna_P3A; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51934; LRAT; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Capsid protein;
KW Clathrin-mediated endocytosis of virus by host;
KW Covalent protein-RNA linkage; Direct protein sequencing; Helicase;
KW Host cytoplasm; Host cytoplasmic vesicle; Host membrane;
KW Host-virus interaction; Hydrolase; Ion channel; Ion transport; Lipoprotein;
KW Membrane; Myristate; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
KW T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
KW Transport; Viral attachment to host cell; Viral ion channel;
KW Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW Virus endocytosis by host; Virus entry into host cell.
FT CHAIN 1..289
FT /note="Capsid protein VP0"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039730"
FT CHAIN 290..542
FT /note="Capsid protein VP3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039731"
FT CHAIN 543..776
FT /note="Capsid protein VP1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039732"
FT CHAIN 777..923
FT /note="Protein 2A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039733"
FT CHAIN 924..1045
FT /note="Protein 2B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039734"
FT CHAIN 1046..1374
FT /note="Protein 2C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039735"
FT CHAIN 1375..1491
FT /note="Protein 3A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039736"
FT CHAIN 1492..1511
FT /note="Protein 3B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039737"
FT CHAIN 1512..1711
FT /note="Protease 3C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039738"
FT CHAIN 1712..2180
FT /note="RNA-directed RNA polymerase 3D-POL"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039739"
FT DOMAIN 787..881
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT DOMAIN 1160..1318
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1518..1708
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1945..2059
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT MOTIF 764..766
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 1558
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1596
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1670
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2045
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1185..1192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 776..777
FT /note="Cleavage; by protease 2A"
FT /evidence="ECO:0000255"
FT MOD_RES 1494
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:5MJV"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 241..252
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:5MJV"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 400..406
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 412..418
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 428..435
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 441..450
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 463..469
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 497..508
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 515..525
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 570..573
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 610..613
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 618..627
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 631..635
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 642..648
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 650..652
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 654..663
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 668..674
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:5MJV"
FT HELIX 685..688
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 691..694
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 698..703
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 708..716
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 719..727
FT /evidence="ECO:0007829|PDB:5MJV"
FT STRAND 735..746
FT /evidence="ECO:0007829|PDB:5MJV"
SQ SEQUENCE 2180 AA; 245844 MW; 3A5F1DAC43C12DEE CRC64;
METIKSIADM ATGVVSSVDS TINAVNEKVE SVGNEIGGNL LTKVADDASN ILGPNCFATT
AEPENKNVVQ ATTTVNTTNL TQHPSAPTMP FSPDFSNVDN FHSMAYDITT GDKNPSKLVR
LETHEWTPSW ARGYQITHVE LPKVFWDHQD KPAYGQSRYF AAVRCGFHFQ VQVNVNQGTA
GSALVVYEPK PVVTYDSKLE FGAFTNLPHV LMNLAETTQA DLCIPYVADT NYVKTDSSDL
GQLKVYVWTP LSIPTGSANQ VDVTILGSLL QLDFQNPRVF AQDVNIYDNA PNGKKKNWKK
IMTMSTKYKW TRTKIDIAEG PGSMNMANVL CTTGAQSVAL VGERAFYDPR TAGSKSRFDD
LVKIAQLFSV MADSTTPSEN HGVDAKGYFK WSATTAPQSI VHRNIVYLRL FPNLNVFVNS
YSYFRGSLVL RLSVYASTFN RGRLRMGFFP NATTDSTSTL DNAIYTICDI GSDNSFEITI
PYSFSTWMRK TNGHPIGLFQ IEVLNRLTYN SSSPSEVYCI VQGKMGQDAR FFCPTGSVVT
FQNSWGSQMD LTDPLCIEDD TENCKQTMSP NELGLTSAQD DGPLGQEKPN YFLNFRSMNV
DIFTVSHTKV DNLFGRAWFF MEHTFTNEGQ WRVPLEFPKQ GHGSLSLLFA YFTGELNIHV
LFLSERGFLR VAHTYDTSND RVNFLSSNGV ITVPAGEQMT LSAPYYSNKP LRTVRDNNSL
GYLMCKPFLT GTSTGKIEVY LSLRCPNFFF PLPAPKVTSS RALRGDMANL TNQSPYGQQP
QNRMMKLAYL DRGFYKHYGI IVGDHVYQLD SDDIFKTALT GKAKFTKTKL TSDWVIEEEC
ELDYFRIKYL ESAVDSEHIF SVDKNCETIA KDIFGTHTLS QHQAIGLVGT ILLTAGLMST
IKTPVNAVTI KEFFNHAIDG DEQGLSLLVQ KCTTFFSSAA TEILDNDLVK FIVKILVRIL
CYMVLYCHKP NILTTACLST LLIMDVTSSS VLSPSCKALM QCLMDGDVKK LAEIVAESMS
NTDDDEVKEQ ICDTVKYTKT ILSNQGPFKG FNEVSTAFRH IDWWIHTLLK IKDMVLSVFK
PSIESKAIQW LERNKEHVCS ILDYASDIIV ESKDQSKMKT QDFYQRYSDC LAKFKPIMAI
CFRSCHNSIS NTVYRLFQEL ARIPNRISTN NDLIRIEPIG IWIQGEPGQG KSFLTHTLSR
QLQKSCKLNG VFTNPTASEF MDGYDNQDIH LIDDLGQTRK EKDIEMLCNC ISSVPFIVPM
AHLEEKGKFY TSKLVVATTN KSDFSSTVLQ DSGALKRRFP YIMHIRAAKA YSKAGKLNVS
QAMATMSTGE CWEVSKNGRD WETLKLKDLV DKITIDYNER VKNYNAWKQQ LENQTLDDLD
DAVSYIKHNF PDAIPYVDEY LNIEMSTLIE QMEAFIEPKP SVFKCFANKI GSKISKASRE
VVDWFSDKIK SMLSFVERNK AWLTVVSAVT SAISILLLVT KIFKKEESKD ERAYNPTLPV
AKPKGTFPVS QREFKNEAPY DGQLEHIISQ MAYITGSTTG HMTHCAGYQH DEIILHGHSI
KYLEQEDELT LHYKNKVFPI EQPSVTQVTL GGKPMDLAIL KCKLPFRFKK NSKYYTNKIG
TESMLIWMTE QGIITKEVQR VHHSGGIKTR EGTESTKTIS YTVKSCKGMC GGLLISKVEG
NFKILGMHIA GNGEMGVAIP FNFLKNDMSD QGIVTEITPI QPMYINTKTQ IHKSPVYGAV
EVKMGPAVLS KSDTRLEEPV ECLIKKSASK YRVNKFQVNN ELWQGVKACV KSKFREIFGM
NGIVDMKTAI LGTSHVNSMD LSTSAGYSFV KSGYKKKDLI CLEPFSVAPL LERLVQDKFH
NLLKGNQITT TFNTCLKDEL RKLDKIASGK TRCIEACEVD YCIVYRMIMM EIYDKIYQTP
CYYSGLAVGI NPYKDWHFMI NALNDYNYEM DYSQYDGSLS SMLLWEAVEV LAYCHDSPDL
VMQLHKPVID SDHVVFNERW LIHGGMPSGS PCTTVLNSLC NLMMCIYTTN LISPGIDCLP
IVYGDDVILS LDKEIEPEKL QSIMADSFGA EVTGSRKDEP PSLKPRMEVE FLKRKPGYFP
ESTFIVGKLD TENMIQHLMW MKNFSTFKQQ LQSYLMELCL HGKDTYQHYI KILEPYLQEW
NITVDDYDVV ITKLMPMVFD
