POLG_PPVD
ID POLG_PPVD Reviewed; 3141 AA.
AC P13529; A0A0M4HMR7; P89038; Q84929;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1 proteinase;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:P04517};
DE AltName: Full=N-terminal protein;
DE Contains:
DE RecName: Full=Helper component proteinase;
DE Short=HC-pro;
DE EC=3.4.22.45 {ECO:0000250|UniProtKB:P04517};
DE Contains:
DE RecName: Full=Protein P3;
DE Contains:
DE RecName: Full=6 kDa protein 1;
DE Short=6K1;
DE Contains:
DE RecName: Full=Cytoplasmic inclusion protein;
DE Short=CI;
DE EC=3.6.4.-;
DE Contains:
DE RecName: Full=6 kDa protein 2;
DE Short=6K2;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPg;
DE Contains:
DE RecName: Full=Nuclear inclusion protein A;
DE Short=NI-a;
DE Short=NIa;
DE EC=3.4.22.44;
DE AltName: Full=49 kDa proteinase;
DE Short=49 kDa-Pro;
DE AltName: Full=NIa-pro;
DE Contains:
DE RecName: Full=Nuclear inclusion protein B;
DE Short=NI-b;
DE Short=NIb;
DE EC=2.7.7.48;
DE AltName: Full=RNA-directed RNA polymerase;
DE Contains:
DE RecName: Full=Capsid protein;
DE Short=CP;
DE AltName: Full=Coat protein;
OS Plum pox potyvirus (strain D) (PPV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12212;
OH NCBI_TaxID=36596; Prunus armeniaca (Apricot) (Armeniaca vulgaris).
OH NCBI_TaxID=36595; Prunus cerasifera (cherry plum).
OH NCBI_TaxID=3758; Prunus domestica (Garden plum).
OH NCBI_TaxID=105665; Prunus glandulosa.
OH NCBI_TaxID=3760; Prunus persica (Peach) (Amygdalus persica).
OH NCBI_TaxID=88123; Prunus salicina.
OH NCBI_TaxID=114937; Prunus spinosa (Blackthorn) (Prunus domestica var. spinosa).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2602121; DOI=10.1093/nar/17.23.10115;
RA Teycheney P.Y., Tavert G., Delbos R., Ravelonandro M., Dunez J.;
RT "The complete nucleotide sequence of plum pox virus RNA (strain D).";
RL Nucleic Acids Res. 17:10115-10116(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2810-3141, AND PROTEIN SEQUENCE OF
RP 2812-2828.
RA Ravelonandro M., Varveri C., Delbos R., Dunez J.;
RT "Nucleotide sequence of the capsid protein gene of plum pox potyvirus.";
RL J. Gen. Virol. 69:1509-1516(1988).
RN [3]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Le Gall O.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], FUNCTION (6 KDA PROTEIN 1), AND
RP SUBCELLULAR LOCATION (6 KDA PROTEIN 1).
RX PubMed=26962227; DOI=10.1128/jvi.00024-16;
RA Cui H., Wang A.;
RT "Plum Pox Virus 6K1 Protein Is Required for Viral Replication and Targets
RT the Viral Replication Complex at the Early Stage of Infection.";
RL J. Virol. 90:5119-5131(2016).
RN [5]
RP REVIEW.
RX PubMed=11226583; DOI=10.1016/s0168-1702(01)00220-9;
RA Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
RT "Potyvirus proteins: a wealth of functions.";
RL Virus Res. 74:157-175(2001).
RN [6]
RP INTERACTION WITH HOST PLANT EIF(ISO)4E (VIRAL GENOME-LINKED PROTEIN).
RX PubMed=23382802; DOI=10.1371/journal.pone.0050627;
RA Wang X., Kohalmi S.E., Svircev A., Wang A., Sanfacon H., Tian L.;
RT "Silencing of the host factor eIF(iso)4E gene confers plum pox virus
RT resistance in plum.";
RL PLoS ONE 8:e50627-e50627(2013).
CC -!- FUNCTION: [Helper component proteinase]: Required for aphid
CC transmission and also has proteolytic activity. Only cleaves a Gly-Gly
CC dipeptide at its own C-terminus. Interacts with virions and aphid
CC stylets. Acts as a suppressor of RNA-mediated gene silencing, also
CC known as post-transcriptional gene silencing (PTGS), a mechanism of
CC plant viral defense that limits the accumulation of viral RNAs. May
CC have RNA-binding activity. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Cytoplasmic inclusion protein]: Has helicase activity. It
CC may be involved in replication.
CC -!- FUNCTION: [6 kDa protein 1]: Indispensable for virus replication.
CC {ECO:0000269|PubMed:26962227}.
CC -!- FUNCTION: [6 kDa protein 2]: Indispensable for virus replication.
CC {ECO:0000250|UniProtKB:P09814}.
CC -!- FUNCTION: [Viral genome-linked protein]: Mediates the cap-independent,
CC EIF4E-dependent translation of viral genomic RNAs (By similarity).
CC Binds to the cap-binding site of host EIF4E and thus interferes with
CC the host EIF4E-dependent mRNA export and translation (By similarity).
CC VPg-RNA directly binds EIF4E and is a template for transcription (By
CC similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are
CC templates for translation (By similarity).
CC {ECO:0000250|UniProtKB:P18247}.
CC -!- FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and
CC proteolytic activities. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA
CC polymerase that plays an essential role in the virus replication.
CC -!- FUNCTION: [Capsid protein]: Involved in aphid transmission, cell-to-
CC cell and systemis movement, encapsidation of the viral RNA and in the
CC regulation of viral RNA amplification. {ECO:0000250|UniProtKB:P04517}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC restricted by preferences for the amino acids in P6 - P1' that vary
CC with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or
CC Gly) for the enzyme from tobacco etch virus. The natural substrate is
CC the viral polyprotein, but other proteins and oligopeptides
CC containing the appropriate consensus sequence are also cleaved.;
CC EC=3.4.22.44; Evidence={ECO:0000250|UniProtKB:P04517};
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=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in
CC the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the
CC potyviral polyprotein.; EC=3.4.22.45;
CC Evidence={ECO:0000250|UniProtKB:P04517};
CC -!- SUBUNIT: [Viral genome-linked protein]: Interacts with host eIF4E
CC protein (via cap-binding region); this interaction mediates the
CC translation of the VPg-viral RNA conjugates (By similarity). Part of a
CC complex that comprises VPg, RNA, host EIF4E and EIF4G; this interaction
CC mediates the translation of the VPg-viral RNA conjugates (By
CC similarity). Interacts with host eIF(iso)4E both in host nucleus and
CC cytoplasm (PubMed:23382802). {ECO:0000250|UniProtKB:P18247,
CC ECO:0000269|PubMed:23382802}.
CC -!- SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle.
CC Note=Probably colocalizes with 6K2-induced vesicles associated with
CC host chloroplasts. {ECO:0000269|PubMed:26962227}.
CC -!- SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate with
CC host chloroplasts. {ECO:0000250|UniProtKB:P09814}.
CC -!- SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host nucleus
CC {ECO:0000269|PubMed:23382802}. Host cytoplasm
CC {ECO:0000269|PubMed:23382802}. Note=Binds to host plant eIF(iso)4E
CC proteins in both host nucleus and cytoplasm.
CC {ECO:0000269|PubMed:23382802}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Genome polyprotein;
CC IsoId=P13529-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK03-1; Sequence=External;
CC -!- DOMAIN: [Helper component proteinase]: The N-terminus is involved in
CC interaction with stylets. The central part is involved in interaction
CC with virions and the C-terminus is involved in cell-to cell movement of
CC the virus.
CC -!- PTM: [Viral genome-linked protein]: VPg is uridylylated by the
CC polymerase and is covalently attached to the 5'-end of the genomic RNA.
CC This uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.
CC -!- PTM: [Genome polyprotein]: Potyviral RNA is expressed as two
CC polyproteins which undergo post-translational proteolytic processing.
CC Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases
CC resulting in the production of at least ten individual proteins. P3N-
CC PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in
CC the production of three individual proteins. The P1 proteinase and the
CC HC-pro cleave only their respective C-termini autocatalytically. 6K1 is
CC essential for proper proteolytic separation of P3 from CI (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced by conventional
CC translation.
CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC {ECO:0000305}.
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; X16415; CAA34437.1; -; Genomic_RNA.
DR EMBL; D00298; BAA00210.1; -; Genomic_RNA.
DR EMBL; KP998124; ALD08346.1; -; Genomic_RNA.
DR PIR; S06929; GNVSPD.
DR MEROPS; C04.001; -.
DR MEROPS; C06.001; -.
DR MEROPS; S30.001; -.
DR Proteomes; UP000006849; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0019048; P:modulation by virus of host process; ISS:UniProtKB.
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 Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.70.150; -; 1.
DR InterPro; IPR011492; DEAD_Flavivir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001456; HC-pro.
DR InterPro; IPR031159; HC_PRO_CPD_dom.
DR InterPro; IPR042308; HC_PRO_CPD_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002540; Pept_S30_P1_potyvir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001592; Poty_coat.
DR InterPro; IPR001730; Potyv_NIa-pro_dom.
DR InterPro; IPR039560; Potyvirid-P3.
DR InterPro; IPR013648; PP_Potyviridae.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00863; Peptidase_C4; 1.
DR Pfam; PF00851; Peptidase_C6; 1.
DR Pfam; PF01577; Peptidase_S30; 1.
DR Pfam; PF00767; Poty_coat; 1.
DR Pfam; PF08440; Poty_PP; 1.
DR Pfam; PF13608; Potyvirid-P3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR PRINTS; PR00966; NIAPOTYPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51744; HC_PRO_CPD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR PROSITE; PS51871; PV_P1_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW Direct protein sequencing; Helical capsid protein; Helicase;
KW Host cytoplasm; Host cytoplasmic vesicle; Host nucleus;
KW Host-virus interaction; Hydrolase; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; Ribosomal frameshifting;
KW RNA-directed RNA polymerase; Serine protease; Suppressor of RNA silencing;
KW Thiol protease; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..3141
FT /note="Genome polyprotein"
FT /id="PRO_0000420005"
FT CHAIN 1..308
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040315"
FT CHAIN 309..767
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040316"
FT CHAIN 768..1117
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040317"
FT CHAIN 1118..1169
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040318"
FT CHAIN 1170..1804
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040319"
FT CHAIN 1805..1857
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040320"
FT CHAIN 1858..2050
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040321"
FT CHAIN 2051..2293
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040322"
FT CHAIN 2294..2811
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040323"
FT CHAIN 2812..3141
FT /note="Capsid protein"
FT /id="PRO_0000040324"
FT DOMAIN 165..308
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 645..767
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1241..1393
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1412..1571
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2051..2269
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2535..2659
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT MOTIF 360..363
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 619..621
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1343..1346
FT /note="DECH box"
FT MOTIF 1898..1905
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 216
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 225
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 259
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 653
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 726
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2096
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2131
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2201
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1254..1261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 308..309
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 767..768
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1117..1118
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1169..1170
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1804..1805
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1857..1858
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2050..2051
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2293..2294
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2811..2812
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1920
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
FT CONFLICT 98
FT /note="K -> E (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="V -> L (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="V -> T (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="R -> G (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="I -> M (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="S -> W (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="S -> C (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="D -> Y (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="A -> V (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="Missing (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 444..445
FT /note="QQ -> NK (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="I -> T (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="I -> M (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="R -> K (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="T -> S (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="S -> L (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="T -> S (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1073
FT /note="H -> Y (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1293
FT /note="G -> S (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1678
FT /note="V -> A (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1825
FT /note="T -> N (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1853
FT /note="G -> E (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1944
FT /note="D -> N (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 2029
FT /note="I -> V (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 2303
FT /note="R -> K (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 2817
FT /note="D -> G (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 2856
FT /note="L -> F (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 2876
FT /note="P -> S (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 2936
FT /note="K -> R (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
FT CONFLICT 2994
FT /note="I -> V (in Ref. 4; ALD08346)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3141 AA; 355574 MW; 6C3641C404414DBB CRC64;
MSTIVFGSFT CHLDAAIHQD NADRLAKAWT RPENRQVSNV HLLCRRAAKS LINTYESATA
SAWKGLEEKL QPMFAKREFS KTVTKRKGLR CFKESSEKFI EKKLRKQYQE ERERFQFVNG
PDAIVNQISV DKCEASVWVP FPHIIEKPSF ATPSMKKKVV FTKVRMSEAS LQLFMRRVAA
NAKANGQKVE IIGRKRVVGN YTTKSRLTYF RTHVRHLDGS KPRYDLVLDE ATKKILQLFA
NTSRFHHVHK KGEVTPGMSG FVVNPINLSD PMQVYDTDLF IVRGKHNSIL VDSRCKVSKK
QSNEIIHYSD PGKQFSDGFT NSFMQCKLRE TDHQSTSDLD VKECGDVAAL VCQAIIPCGK
ITCLQCAQKY SYMSQQEIRD RFSTVIEQHE KTAMDNYPQF SHVLAFLKRY RELMRVENQN
YEAFKDITHM IGEDRKEAPF SHLQQINELI IKGGMMSAQD YIEASDHLRE LARYQKNRTE
NIRSGSIKAF RNKISSKAHV NMQLMCDNQL DTNGNFVWGQ REYHAKRFFR NYFDVIDVSE
GYRRHIVREN PRGIRKLAIG NLVISTNLAA LRKQLLGEEC IHFEVSKECT SRRGENFVYQ
CCCVTHEDGT PLESEIISPT KNHLVVGNTG DSKYVDLPTA KGGAMFIAKA GYCYINIFLA
MLININEDEA KSFTKTVRDT LVPKLGTWPS MMDLATACHF LAVLYPETRN AELPRILVDH
EAKIFHVVDS FGSLSTGMHV LKANTINQLI SFASDTLDSN MKTYLVGGSE VDKCDEFKNV
KLLIRSIYKP QIMEQVLKEE PYLLLMSVLS PGVLMALFNS GSLEKATQYW ITRSHTLAAI
TSMLSALAAK VSLASTLNAQ MSVIDEHAAV LCDSVFDGTK PYASYMMAVK TLERMKARTE
SDHTLNDLGF SVLRQATPHL VEKSYLQELE QAWKELSWSE KFSAILESQR WRKHIPKPFI
PKDGADLGGR YDISVRSLLG NQYKRLRDVV RRKRDDVVCY THQSMGKLFC KAIGISTSFL
PSTLKMLDML IVFGLLLSIG ATCNSMINEH KHLKQLAADR EDKKRFKRLQ VLHTRLSEKV
GCTPTADEFL EYVGGENPDL LKHAEDLIGD GQVVVHQSKR DSQANLERVV AFVALVMMLF
DSERSDGVYK ILNKLKGIMG SVDQAVHHQS LDDIEDILDE KKLTVDFVLQ SNEVAPTVPF
DSTFEKWWTN QLETGNVIPH YRTEGHFLEF TRENAAHIAN EVMHGSHQDI LIRGAVGSGK
STGLPFHLSK KGHVLLIEPT RPLAENVCKQ LRGQPFNVNP TLRMRGMSTF GSTPITVMTS
GYALHFLANN PTYLDNYKCI IFDECHVHDA SAMAFRCLLS EYSYPGKILK VSATPPGHEV
DFKTQKEVKV IVEESLSFQQ FVSNLGTGCN SDILKHGVNV LVYVASYNEV DTLSKLLTDR
SFKVSKVDGR TMKIGNVEIP TSGTQAKPHF VVATNIIENG VTLDIDVVVD FGLKVVPVLD
IDNRLVRYTK KSISYGERIQ RLGRVGRNKP GAALRIGFTE KGLTQIPPII ATEAAFLCFT
YGLPVMTNGV STSLLAMCTV KQARTMQQFE LSPFYTVALV RFDGTMHQEI FRLLKSYRLR
DSEVILNKLA IPNSNVCGWM SVRDYKRQGC NLDLDENIRV PFYVKDIPET LHERIWQVVE
THKSDAGFGR ICSSSACKIA YTLQTDIHSI PRTIKIIDAL LEQERTKQAH FRAMTSQSCS
SSNFSLSSIT SAIRSKYAKD HTEENIGVLQ MAKSQLLEFK NLNIDPSYPE LVRNFGALEC
VHHQTKEGVS KALQLKGHWN KRLITRDATL MLGVLGGGAW MIFSYLRDSF KEGVVHQGFN
RRQRQKLKFR QARDNRMARE VYGDDSTMED YFGSAYSKKG KSKGKTRGMG TKTRKFVNMY
GYDPTDYNFV RFVDPLTGHT LDEDPLMDIN LVQEHFSQIR NDYIGDDKIT MQHIMSNPGI
VAYYIKDATQ KALKVDLTPH NPLRVCDKTA TIAGFPEREF ELRQTGHPIF VEPNAIPKIN
EEGDEEVDHE SKSLFRGLRD YNPIASSICQ LNNSSGARQS EMFGLGFGGL IVTNQHLFKR
NDGELTIRSH HGEFVVKDTK TLKLLPCKGR DIVIIRLPKD FPPFPKRLQF RTPTTEDRVC
LIGSNFQTKS ISSTMSETSA TYPVDNSHFW KHWISTKDGH CGLPIVSTRD GSILGLHSLA
NSTNTQNFYA AFPDNFETTY LSNQDNDNWI KQWRYNPDEV CWGSLQLKRD IPQSPFTICK
LLTDLDGEFV YTQSKTTHWL RDRLEGNLKA VGACPGQLVT KHVVKGKCTL FETYLLTHPE
EHEFFRPLMG AYQKSALNKD AYVKDLMKYS KPIVVGAVDC DQFERAVDVV ISMLISKGFE
ECNYVTDPDD IFSALNMKAA VGALYSGKKR DYFKNVSDQD KESFVRASCK RLFMGKKGVW
NGSLKAELRP KEKVEANKTR SFTAAPIDTL LGGKVCVDDF NNQFYSLNLH CPWSVGMTKF
RGGWDKLLRA LPEGWIYCDA DGSQFDSSLS PYLINAVLNI RLAFMEEWDI GEQMLSNLYT
EIVYTPIATP DGTIVKKFKG NNSGQPSTVV DNTLMVILAM TYSLLKLGYH PDTHDCICRY
FVNGDDLVLA VHPAYESIYD ELQEHFSQLG LNYTFATKTE NKEELWFMSH KGVLYDDMYI
PKLEPERIVS ILEWDRSNEP IHRLEAICAS MVEAWGYKEL LREIRKFYSW VLEQAPYNAL
SKDGKAPYIA ETALKKLYTD TEASETEIER YLEAFYDDIN DDGESNVVVH QADEREDEEE
VDAGKPIVVT APAATSPILQ PPPVIQPAPR TTAPMLNPIF TPATTQPATK PVSQVPGPQL
QTFGTYGNED ASPSNSNALV NTNRDRDVDA GSIGTFTVPR LKAMTSKLSL PKVKGKAIMN
LNHLAHYSPA QVDLSNTRAP QSCFQTWYEG VKRDYDVTDD EMSIILNGLM VWCIENGTSP
NINGMWVMMD GETQVEYPIK PLLDHAKPTF RQIMAHFSNV AEAYIEKRNY EKAYMPRYGI
QRNLTDYSLA RYAFDFYEMT STTPVRAREA HIQMKAAALR NVQNRLFGLD GNVGTQEEDT
ERHTAGDVNR NMHNLLGVRG V
