POLG_RHDVF
ID POLG_RHDVF Reviewed; 2344 AA.
AC P27410;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Genome polyprotein;
DE AltName: Full=p254;
DE Contains:
DE RecName: Full=Protein p16;
DE Contains:
DE RecName: Full=Protein p23;
DE Contains:
DE RecName: Full=NTPase;
DE EC=3.6.1.15;
DE AltName: Full=2C-like protein;
DE AltName: Full=P2C;
DE AltName: Full=p37;
DE Contains:
DE RecName: Full=Precursor p41;
DE Contains:
DE RecName: Full=Protein p29;
DE Contains:
DE RecName: Full=Protein p23/2;
DE Contains:
DE RecName: Full=Protein p18;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPg;
DE AltName: Full=p13;
DE Contains:
DE RecName: Full=3C-like protease;
DE Short=3CLpro;
DE EC=3.4.22.66;
DE AltName: Full=Calicivirin;
DE AltName: Full=Thiol protease P3C;
DE AltName: Full=p15;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=3Dpol;
DE AltName: Full=p58;
DE Contains:
DE RecName: Full=Capsid protein VP60;
GN ORFNames=ORF1;
OS Rabbit hemorrhagic disease virus (strain Rabbit/Germany/FRG/1989)
OS (Ra/LV/RHDV/GH/1989/GE) (RHDV-FRG).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Lagovirus.
OX NCBI_TaxID=314536;
OH NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1840711; DOI=10.1016/0042-6822(91)90436-f;
RA Meyers G., Wirblich C., Thiel H.-J.;
RT "Rabbit hemorrhagic disease virus -- molecular cloning and nucleotide
RT sequencing of a calicivirus genome.";
RL Virology 184:664-676(1991).
RN [2]
RP FUNCTION OF VPG.
RX PubMed=1887589; DOI=10.1016/0042-6822(91)90437-g;
RA Meyers G., Wirblich C., Thiel H.-J.;
RT "Genomic and subgenomic RNAs of rabbit hemorrhagic disease virus are both
RT protein-linked and packaged into particles.";
RL Virology 184:677-686(1991).
RN [3]
RP MUTAGENESIS OF HIS-1135; ASP-1152; ASP-1175; CYS-1212 AND HIS-1227.
RX PubMed=8083986; DOI=10.1128/jvi.68.10.6487-6495.1994;
RA Boniotti B., Wirblich C., Sibilia M., Meyers G., Thiel H.J., Rossi C.;
RT "Identification and characterization of a 3C-like protease from rabbit
RT hemorrhagic disease virus, a calicivirus.";
RL J. Virol. 68:6487-6495(1994).
RN [4]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=7474137; DOI=10.1128/jvi.69.11.7159-7168.1995;
RA Wirblich C., Sibilia M., Boniotti M.B., Rossi C., Thiel H.-J., Meyers G.;
RT "3C-like protease of rabbit hemorrhagic disease virus: identification of
RT cleavage sites in the ORF1 polyprotein and analysis of cleavage
RT specificity.";
RL J. Virol. 69:7159-7168(1995).
RN [5]
RP SUBGENOMIC ORIGIN OF VP60.
RX PubMed=7637026; DOI=10.1128/jvi.69.9.5812-5815.1995;
RA Sibilia M., Boniotti M.B., Angoscini P., Capucci L., Rossi C.;
RT "Two independent pathways of expression lead to self-assembly of the rabbit
RT hemorrhagic disease virus capsid protein.";
RL J. Virol. 69:5812-5815(1995).
RN [6]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=9557747; DOI=10.1128/jvi.72.5.4492-4497.1998;
RA Konig M., Thiel H.J., Meyers G.;
RT "Detection of viral proteins after infection of cultured hepatocytes with
RT rabbit hemorrhagic disease virus.";
RL J. Virol. 72:4492-4497(1998).
RN [7]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=11040126; DOI=10.1006/viro.2000.0545;
RA Meyers G., Wirblich C., Thiel H.J., Thumfart J.O.;
RT "Rabbit hemorrhagic disease virus: genome organization and polyprotein
RT processing of a calicivirus studied after transient expression of cDNA
RT constructs.";
RL Virology 276:349-363(2000).
RN [8]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=10644847; DOI=10.1099/0022-1317-81-2-481;
RA Joubert P., Pautigny C., Madelaine M.-F., Rasschaert D.;
RT "Identification of a new cleavage site of the 3C-like protease of rabbit
RT haemorrhagic disease virus.";
RL J. Gen. Virol. 81:481-488(2000).
RN [9]
RP CHARACTERIZATION OF RNA-DIRECTED RNA POLYMERASE.
RX PubMed=11266218; DOI=10.1007/s007050170191;
RA Lopez Vazquez A.L., Martin Alonso J.M., Parra F.;
RT "Characterisation of the RNA-dependent RNA polymerase from Rabbit
RT hemorrhagic disease virus produced in Escherichia coli.";
RL Arch. Virol. 146:59-69(2001).
RN [10]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=12504575; DOI=10.1006/viro.2002.1660;
RA Thumfart J.O., Meyers G.;
RT "Rabbit hemorrhagic disease virus: identification of a cleavage site in the
RT viral polyprotein that is not processed by the known calicivirus
RT protease.";
RL Virology 304:352-363(2002).
RN [11]
RP FUNCTION OF CAPSID PROTEIN VP60.
RX PubMed=15063122; DOI=10.1016/j.virol.2004.01.021;
RA Barcena J., Verdaguer N., Roca R., Morales M., Angulo I., Risco C.,
RA Carrascosa J.L., Torres J.M., Caston J.R.;
RT "The coat protein of Rabbit hemorrhagic disease virus contains a molecular
RT switch at the N-terminal region facing the inner surface of the capsid.";
RL Virology 322:118-134(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1252-1767.
RX PubMed=11677245; DOI=10.1074/jbc.m109261200;
RA Ng K.K.S., Cherney M.M., Vazquez A.L., Machin A., Martin-Alonso J.M.,
RA Parra F., James M.N.G.;
RT "Crystal structures of active and inactive conformations of a caliciviral
RT RNA-dependent RNA polymerase.";
RL J. Biol. Chem. 277:1381-1387(2002).
CC -!- FUNCTION: NTPase presumably plays a role in replication. {ECO:0000250}.
CC -!- FUNCTION: Viral genome-linked protein is covalently linked to the 5'-
CC end of the positive-strand, negative-strand genomic RNAs and subgenomic
CC RNA. Acts as a genome-linked replication primer. May recruit ribosome
CC to viral RNA thereby promoting viral proteins translation (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: 3C-like protease processes the polyprotein: 3CLpro-RdRp (p72)
CC is first released by autocleavage, then all other proteins are cleaved.
CC {ECO:0000250}.
CC -!- FUNCTION: RNA-directed RNA polymerase replicates genomic and
CC antigenomic RNA by recognizing replications specific signals.
CC Transcribes also a subgenomic mRNA by initiating RNA synthesis
CC internally on antigenomic RNA. This sgRNA codes for structural
CC proteins. Catalyzes the covalent attachment VPg with viral RNAs (By
CC similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}.
CC -!- FUNCTION: Capsid protein VP60 self assembles to form an icosahedral
CC capsid with a T=3 symmetry, about 35 nm in diameter, and consisting of
CC 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm
CC might be capsid proteins assembled as icosahedron with T=1 symmetry.
CC The capsid encapsulate VP2 proteins and genomic or subgenomic RNA.
CC Attaches virion to target cells by binding histo-blood group antigens,
CC inducing endocytosis of the viral particle. Acidification of the
CC endosome induces conformational change of capsid protein thereby
CC injecting virus genomic RNA into host cytoplasm (By similarity).
CC {ECO:0000250}.
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=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=Endopeptidase with a preference for cleavage when the P1
CC position is occupied by Glu-|-Xaa and the P1' position is occupied by
CC Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01242};
CC -!- SUBUNIT: Binds to histo-blood group antigens at surface of target
CC cells. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP60]: Virion. Host cytoplasm
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=Genome polyprotein;
CC IsoId=P27410-1; Sequence=Displayed;
CC Name=Subgenomic capsid protein VP60; Synonyms=VP1;
CC IsoId=P27410-2; Sequence=VSP_034381;
CC -!- PTM: Specific enzymatic cleavages by its own cysteine protease yield
CC mature proteins. The protease cleaves itself from the nascent
CC polyprotein autocatalytically. Precursor p41 can be cleaved by viral
CC 3CLpro into protein p19 and VPg, or cleaved by host protease into
CC protein p23/2 and protein p18. {ECO:0000269|PubMed:10644847,
CC ECO:0000269|PubMed:11040126, ECO:0000269|PubMed:12504575,
CC ECO:0000269|PubMed:7474137, ECO:0000269|PubMed:9557747}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently attached
CC to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This
CC uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Two different RNAs lead the expression of the capsid
CC protein. One arises from the cleavage of the polyprotein translated
CC from the genomic RNA and the other from the translation of a subgenomic
CC RNA derived from the (-)RNA template. Capsid protein expressed from the
CC subgenomic mRNA is produced in much larger amounts than the cleaved one
CC (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced from the genomic
CC RNA.
CC -!- MISCELLANEOUS: [Isoform Subgenomic capsid protein VP60]: Produced from
CC the subgenomic RNA. {ECO:0000305}.
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DR EMBL; M67473; AAA47285.1; -; Genomic_RNA.
DR PIR; A41039; RRWWRH.
DR RefSeq; NP_062875.1; NC_001543.1.
DR PDB; 1KHV; X-ray; 2.50 A; A/B=1252-1767.
DR PDB; 1KHW; X-ray; 2.70 A; A/B=1252-1767.
DR PDB; 6M24; X-ray; 2.29 A; C=2271-2279.
DR PDB; 6M2J; X-ray; 2.20 A; C=2308-2316.
DR PDB; 6M2K; X-ray; 2.59 A; C=2106-2114.
DR PDBsum; 1KHV; -.
DR PDBsum; 1KHW; -.
DR PDBsum; 6M24; -.
DR PDBsum; 6M2J; -.
DR PDBsum; 6M2K; -.
DR SMR; P27410; -.
DR MEROPS; C24.001; -.
DR PRIDE; P27410; -.
DR GeneID; 1491968; -.
DR KEGG; vg:1491968; -.
DR BRENDA; 3.4.22.B15; 5265.
DR EvolutionaryTrace; P27410; -.
DR Proteomes; UP000000413; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C: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:0017111; F:nucleoside-triphosphatase activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; 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 CDD; cd00205; rhv_like; 1.
DR Gene3D; 2.60.120.20; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004005; Calicivirus_coat.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR000317; Peptidase_C24.
DR InterPro; IPR009003; Peptidase_S1_PA.
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 Pfam; PF00915; Calici_coat; 1.
DR Pfam; PF03510; Peptidase_C24; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00916; 2CENDOPTASE.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51894; CV_3CL_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; Alternative promoter usage; ATP-binding; Capsid protein;
KW Covalent protein-RNA linkage; Disulfide bond; Helicase; Host cytoplasm;
KW Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW Protease; Reference proteome; RNA-directed RNA polymerase; Thiol protease;
KW Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2344
FT /note="Genome polyprotein"
FT /id="PRO_0000341645"
FT CHAIN 1..143
FT /note="Protein p16"
FT /id="PRO_0000036959"
FT CHAIN 144..339
FT /note="Protein p23"
FT /id="PRO_0000036960"
FT CHAIN 340..718
FT /note="NTPase"
FT /id="PRO_0000036961"
FT CHAIN 719..1108
FT /note="Precursor p41"
FT /id="PRO_0000341646"
FT CHAIN 719..993
FT /note="Protein p29"
FT /id="PRO_0000036962"
FT CHAIN 719..936
FT /note="Protein p23/2"
FT /id="PRO_0000341647"
FT CHAIN 937..1108
FT /note="Protein p18"
FT /id="PRO_0000341648"
FT CHAIN 994..1108
FT /note="Viral genome-linked protein"
FT /id="PRO_0000036963"
FT CHAIN 1109..1251
FT /note="3C-like protease"
FT /id="PRO_0000036964"
FT CHAIN 1252..1767
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000036965"
FT CHAIN 1768..2344
FT /note="Capsid protein VP60"
FT /id="PRO_0000036967"
FT DOMAIN 492..653
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1109..1244
FT /note="Peptidase C24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT DOMAIN 1495..1619
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1770..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1135
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1152
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1212
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT BINDING 522..529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 143..144
FT /note="Cleavage; by 3CLpro"
FT SITE 339..340
FT /note="Cleavage; by 3CLpro"
FT SITE 718..719
FT /note="Cleavage; by 3CLpro"
FT SITE 936..937
FT /note="Cleavage; by host"
FT SITE 993..994
FT /note="Cleavage; by 3CLpro"
FT SITE 1108..1109
FT /note="Cleavage; by 3CLpro"
FT SITE 1251..1252
FT /note="Cleavage; by 3CLpro"
FT SITE 1767..1768
FT /note="Cleavage; by 3CLpro"
FT MOD_RES 1014
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT DISULFID 1584..1591
FT VAR_SEQ 1..1765
FT /note="Missing (in isoform Subgenomic capsid protein VP60)"
FT /evidence="ECO:0000305"
FT /id="VSP_034381"
FT MUTAGEN 1135
FT /note="H->N: Complete loss of 3CLpro activity in vitro."
FT /evidence="ECO:0000269|PubMed:8083986"
FT MUTAGEN 1152
FT /note="D->E: Partial loss of 3CLpro activity in vitro."
FT /evidence="ECO:0000269|PubMed:8083986"
FT MUTAGEN 1152
FT /note="D->G,N: Complete loss of 3CLpro activity in vitro."
FT /evidence="ECO:0000269|PubMed:8083986"
FT MUTAGEN 1175
FT /note="D->G,E: Complete loss of 3CLpro activity in vitro."
FT /evidence="ECO:0000269|PubMed:8083986"
FT MUTAGEN 1175
FT /note="D->N: Partial loss of 3CLpro activity in vitro."
FT /evidence="ECO:0000269|PubMed:8083986"
FT MUTAGEN 1212
FT /note="C->G: Complete loss of 3CLpro activity in vitro."
FT /evidence="ECO:0000269|PubMed:8083986"
FT MUTAGEN 1212
FT /note="C->S: Partial loss of 3CLpro activity in vitro."
FT /evidence="ECO:0000269|PubMed:8083986"
FT MUTAGEN 1227
FT /note="H->L,N: Complete loss of 3CLpro activity in vitro."
FT /evidence="ECO:0000269|PubMed:8083986"
FT STRAND 1257..1263
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1266..1271
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1282..1287
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1293..1295
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1300..1302
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1305..1307
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1315..1324
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1325..1327
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1337..1353
FT /evidence="ECO:0007829|PDB:1KHV"
FT TURN 1354..1356
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1364..1370
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1373..1376
FT /evidence="ECO:0007829|PDB:1KHW"
FT STRAND 1379..1381
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1385..1387
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1391..1393
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1396..1410
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1418..1423
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1440..1444
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1446..1465
FT /evidence="ECO:0007829|PDB:1KHV"
FT TURN 1466..1469
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1470..1472
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1482..1493
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1495..1502
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1505..1508
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1511..1522
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1529..1539
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1543..1545
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1547..1551
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1564..1586
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1594..1597
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1600..1603
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1606..1611
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1613..1617
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1619..1628
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1633..1637
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1647..1649
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1655..1660
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1663..1668
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1670..1678
FT /evidence="ECO:0007829|PDB:1KHV"
FT STRAND 1679..1689
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1698..1712
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1716..1729
FT /evidence="ECO:0007829|PDB:1KHV"
FT TURN 1730..1732
FT /evidence="ECO:0007829|PDB:1KHV"
FT HELIX 1740..1750
FT /evidence="ECO:0007829|PDB:1KHV"
SQ SEQUENCE 2344 AA; 257068 MW; 1454C248F81E9212 CRC64;
MAAMSRLTGM TTAILPEKKP LDFFLDLRDK TPPCCIRATG RLAWPVFPGQ NGKEGPLETC
NKCGKWLNGF GNFGLEDLGD VCLCSIAQQK HKFGPVCLCN RVYIHDCGRW RRRSRFLKHY
KALNKVIPCA YQFDESFPTP IFEGEVDDLF VELGAPTSMG FMDKKLLKKG KKLMDKFVDV
DEPCLTSRDT SLLDSIASDN TIRAKLEEEY GVEMVQAARD RKDFMKNLRL ALDNRPANPV
TWYTKLGNIT EKGKQWAKKV VYGARKVTDP LKTLASILLV GLHNVIAVDT TVMLSTFKPV
NLLAILMDWN NDLTGFITTL VRLLELYGVV QATVNLIIEG VKSFWDKVVC ATDRCFDLLK
RLFDTFEDSV PTGPTAGCLI FMAFVFSTVV GYLPNNSVIT TFMKGAGKLT TFAGVVGAIR
TLWITINQHM VAKDLTSVQQ KVMTVVKMAN EAATLDQLEI VSCLCSDLET TLTNRCTLPS
YNQHLGILNA SQKVISDLHT MVLGKINMTK QRPQPVAVIF KGAPGIGKTY LVHRIARDLG
CQHPSTINFG LDHFDSYTGE EVAIADEFNT CGDGESWVEL FIQMVNTNPC PLNCDKAENK
NKVFNSKYLL CTTNSNMILN ATHPRAGAFY RRVMIVEARN KAVESWQATR HGSKPGKSCY
SKDMSHLTFQ VYPHNMPAPG FVFVGDKLVK SQVTPREYKY SELLDLIKSE HPDVASFEGA
NKFNFVYPDA QYDQALLMWK QYFVMYGCVA RLAKNFVDDI PYNQVHISRA SDPKIEGCVE
YQCKFQHLWR MVPQFVLGCV NMTNQLGTPL TQQQLDRITN GVEGVTVTTV NNILPFHSQT
TLINPSFIKL IWAVRKHLKG LSGVTKVAQF IWRVMTNPVD AYGTLVRTLT GAATFSDDPV
STTIICSNCT IQLHSCGGLL VRYSRDPVPV ASDNVDRGDQ GVDVFTDPNL ISGFSWRQIA
HLFVEVISHL CANHLVNLAT MAALGAVATK AFQGVKGKTK RGRGARVNLG NDEYDEWQAA
RREFVNAHDM TAEEYLAMKN KAAMGSDDQD SIMFRSWWTR RQLRPEEDQV TIVGRSGVRN
EVIRTRVRQT PRGPKTLDDG GFYDNDYEGL PGFMRHNGSG WMIHIGNGLY ISNTHTARSS
CSEIVTCSPT TDLCLVKGES IRSVAQIAEG TPVCDWKKSP ISTYGIKKTL SDSTKIDVLA
YDGCTQTTHG DCGLPLYDSS GKIVAIHTGK LLGFSKMCTL IDLTITKGVY ETSNFFCGEP
IDYRGITAHR LVGAEPRPPV SGTRYAKVPG VPDEYKTGYR PANLGRSDPD SDKSLMNIAV
KNLQVYQQEP KLDKVDEFIE RAAADVLGYL RFLTKGERQA NLNFKAAFNT LDLSTSCGPF
VPGKKIDHVK DGVMDQVLAK HLYKCWSVAN SGKALHHIYA CGLKDELRPL DKVKEGKKRL
LWGCDVGVAV CAAAVFHNIC YKLKMVARFG PIAVGVDMTS RDVDVIINNL TSKASDFLCL
DYSKWDSTMS PCVVRLAIDI LADCCEQTEL TKSVVLTLKS HPMTILDAMI VQTKRGLPSG
MPFTSVINSI CHWLLWSAAV YKSCAEIGLH CSNLYEDAPF YTYGDDGVYA MTPMMVSLLP
AIIENLRDYG LSPTAADKTE FIDVCPLNKI SFLKRTFELT DIGWVSKLDK SSILRQLEWS
KTTSRHMVIE ETYDLAKEER GVQLEELQVA AAAHGQEFFN FVCRELERQQ AYTQFSVYSY
DAARKILADR KRVVSVVPDD EFVNVMEGKA RAAPQGEAAG TATTASVPGT TTDGMDPGVV
ATTSVITAEN SSASIATAGI GGPPQQVDQQ ETWRTNFYYN DVFTWSVADA PGSILYTVQH
SPQNNPFTAV LSQMYAGWAG GMQFRFIVAG SGVFGGRLVR AVIPPGIEIG PGLEVRQFPH
VVIDARSLEP VTITMPDLRP NMYHPTGDPG LVPTLVLSVY NNLINPFGGS TSAIQVTVET
RPSEDFEFVM IRAPSSKTVD SISPAGLLTT PVLTGVGNDN RWNGQIVGLQ PVPGGFSTCN
RHWNLNGSTY GWSSPRFGDI DHRRGSASYS GSNATNVLQF WYANAGSAID NPISQVAPDG
FPDMSFVPFN GPGIPAAGWV GFGAIWNSNS GAPNVTTVQA YELGFATGAP GNLQPTTNTS
GAQTVAKSIY AVVTGTAQNP AGLFVMASGI ISTPNASAIT YTPQPDRIVT TPGTPAAAPV
GKNTPIMFAS VVRRTGDVNA TAGSANGTQY GTGSQPLPVT IGLSLNNYSS ALMPGQFFVW
QLTFASGFME IGLSVDGYFY AGTGASTTLI DLTELIDVRP VGPRPSKSTL VFNLGGTANG
FSYV
