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Protein G1-like6 (OsG1L6) (Protein ABNORMAL FLOWER AND DWARF 1) (Protein BEAK LIKE SPIKELET 1) (Protein BEAK-SHAPED GRAIN 1) (Protein TRIANGULAR HULL 1)

 G1L6_ORYSJ              Reviewed;         248 AA.
Q6K5X1; A0A0P0VR07;
19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
02-JUN-2021, entry version 96.
RecName: Full=Protein G1-like6 {ECO:0000303|PubMed:19901325};
Short=OsG1L6 {ECO:0000303|PubMed:19901325};
AltName: Full=Protein ABNORMAL FLOWER AND DWARF 1 {ECO:0000303|PubMed:26486996};
AltName: Full=Protein BEAK LIKE SPIKELET 1 {ECO:0000303|Ref.9};
AltName: Full=Protein BEAK-SHAPED GRAIN 1 {ECO:0000303|PubMed:23526395};
AltName: Full=Protein TRIANGULAR HULL 1 {ECO:0000303|PubMed:22203474};
Name=G1L6 {ECO:0000303|PubMed:19901325};
Synonyms=AFD1 {ECO:0000303|PubMed:26486996}, BLS1 {ECO:0000303|Ref.9},
BSG1 {ECO:0000303|PubMed:23526395}, TH1 {ECO:0000303|PubMed:22203474};
OrderedLocusNames=Os02g0811000 {ECO:0000312|EMBL:BAS81516.1},
LOC_Os02g56610 {ECO:0000305};
ORFNames=OJ1116_E04.14 {ECO:0000312|EMBL:BAD21590.1},
OsJ_08822 {ECO:0000312|EMBL:EAZ25035.1},
P0016F11.6 {ECO:0000312|EMBL:BAD22027.1};
Oryza sativa subsp. japonica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39947;
[1]
NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
STRAIN=cv. Nipponbare;
PubMed=19901325; DOI=10.1073/pnas.0907896106;
Yoshida A., Suzaki Y., Tanaka W., Hirano H.-Y.;
"The homeotic gene long sterile lemma (G1) specifies sterile lemma identity
in the rice spikelet.";
Proc. Natl. Acad. Sci. U.S.A. 106:20103-20108(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16100779; DOI=10.1038/nature03895;
International rice genome sequencing project (IRGSP);
"The map-based sequence of the rice genome.";
Nature 436:793-800(2005).
[3]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=18089549; DOI=10.1093/nar/gkm978;
The rice annotation project (RAP);
"The rice annotation project database (RAP-DB): 2008 update.";
Nucleic Acids Res. 36:D1028-D1033(2008).
[4]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=24280374; DOI=10.1186/1939-8433-6-4;
Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
"Improvement of the Oryza sativa Nipponbare reference genome using next
generation sequence and optical map data.";
Rice 6:4-4(2013).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
"The genomes of Oryza sativa: a history of duplications.";
PLoS Biol. 3:266-281(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Nipponbare;
PubMed=12869764; DOI=10.1126/science.1081288;
The rice full-length cDNA consortium;
"Collection, mapping, and annotation of over 28,000 cDNA clones from
japonica rice.";
Science 301:376-379(2003).
[7]
DNA-BINDING, AND GENE FAMILY.
PubMed=23146749; DOI=10.1186/1745-6150-7-39;
Iyer L.M., Aravind L.;
"ALOG domains: provenance of plant homeotic and developmental regulators
from the DNA-binding domain of a novel class of DIRS1-type retroposons.";
Biol. Direct 7:39-39(2012).
[8]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=22203474; DOI=10.1007/s11103-011-9868-8;
Li X., Sun L., Tan L., Liu F., Zhu Z., Fu Y., Sun X., Sun X., Xie D.,
Sun C.;
"TH1, a DUF640 domain-like gene controls lemma and palea development in
rice.";
Plant Mol. Biol. 78:351-359(2012).
[9]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
DOI=10.1007/s11105-012-0480-0;
Ma X., Cheng Z., Wu F., Jin M., Zhang L., Zhou F., Wang J., Zhou K., Ma J.,
Lin Q., Lei C., Wan J.;
"BEAK LIKE SPIKELET1 is required for lateral development of lemma and palea
in rice.";
Plant Mol. Biol. Rep. 31:98-108(2013).
[10]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=23526395; DOI=10.1007/s11427-013-4449-5;
Yan D., Zhou Y., Ye S., Zeng L., Zhang X., He Z.;
"Beak-shaped grain 1/TRIANGULAR HULL 1, a DUF640 gene, is associated with
grain shape, size and weight in rice.";
Sci. China Life Sci. 56:275-283(2013).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25224972; DOI=10.1266/ggs.89.61;
Sato D.S., Ohmori Y., Nagashima H., Toriba T., Hirano H.Y.;
"A role for TRIANGULAR HULL1 in fine-tuning spikelet morphogenesis in
rice.";
Genes Genet. Syst. 89:61-69(2014).
[12]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=26486996; DOI=10.1111/jipb.12441;
Ren D., Rao Y., Wu L., Xu Q., Li Z., Yu H., Zhang Y., Leng Y., Hu J.,
Zhu L., Gao Z., Dong G., Zhang G., Guo L., Zeng D., Qian Q.;
"The pleiotropic ABNORMAL FLOWER AND DWARF1 affects plant height, floral
development and grain yield in rice.";
J. Integr. Plant Biol. 58:529-539(2016).
[13]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
MUTAGENESIS OF ARG-80; GLY-124 AND HIS-129.
PubMed=29057928; DOI=10.1038/s41598-017-14146-w;
Peng P., Liu L., Fang J., Zhao J., Yuan S., Li X.;
"The rice TRIANGULAR HULL1 protein acts as a transcriptional repressor in
regulating lateral development of spikelet.";
Sci. Rep. 7:13712-13712(2017).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=30725309; DOI=10.1186/s12284-019-0265-2;
Wang J., Zhang Q., Wang Y., Huang J., Luo N., Wei S., Jin J.;
"Analysing the rice young panicle transcriptome reveals the gene regulatory
network controlled by TRIANGULAR HULL1.";
Rice 12:6-6(2019).
-!- FUNCTION: Transcription factor required for lateral development of the
lemma and palea (PubMed:22203474, Ref.9, PubMed:23526395,
PubMed:25224972, PubMed:26486996, PubMed:29057928, PubMed:30725309).
Involved in the regulation of grain hull development (PubMed:23526395).
Possesses transactivation activity in yeast, and may determine grain
shape and size by modifying gene expression in the grain hull
(PubMed:23526395). Regulates the expression of cell proliferation and
expansion related genes (PubMed:26486996). Acts as transcriptional
repressor and regulates cell expansion during the lateral development
of spikelet (PubMed:29057928). May act upstream of hormone-related
genes and starch and sucrose metabolism-related genes, which may be
responsible for lemma and palea development, and grain filling,
respectively (PubMed:30725309). Does not seem to function at stages of
floral-organ initiation and patterning (Ref.9).
{ECO:0000269|PubMed:22203474, ECO:0000269|PubMed:23526395,
ECO:0000269|PubMed:25224972, ECO:0000269|PubMed:26486996,
ECO:0000269|PubMed:29057928, ECO:0000269|PubMed:30725309,
ECO:0000269|Ref.9}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29057928}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22203474,
ECO:0000269|PubMed:23526395, ECO:0000269|PubMed:26486996,
ECO:0000269|PubMed:29057928, ECO:0000269|Ref.9}.
-!- TISSUE SPECIFICITY: Expressed in lemma, palea, rachis branches, flag
leaves and young embryos (PubMed:22203474). Highly expressed in lemmas
and paleas of young spikelets (Ref.9, PubMed:23526395,
PubMed:26486996). Expressed in stamens, pistil and leaf sheaths
(Ref.9). {ECO:0000269|PubMed:22203474, ECO:0000269|PubMed:23526395,
ECO:0000269|PubMed:26486996, ECO:0000269|Ref.9}.
-!- DISRUPTION PHENOTYPE: Triangular hull with tortuous lemma and palea
(PubMed:22203474, PubMed:29057928). Defects in development of lemma and
palea, which have a beak-like form (Ref.9, PubMed:25224972,
PubMed:30725309). Beak-shaped grains of decreased width, thickness and
weight with a loosely interlocked lemma and palea that are unable to
close tightly (PubMed:23526395, PubMed:26486996, PubMed:29057928). Poor
grain filling (PubMed:22203474, Ref.9, PubMed:23526395,
PubMed:25224972, PubMed:26486996, PubMed:29057928, PubMed:30725309).
{ECO:0000269|PubMed:22203474, ECO:0000269|PubMed:23526395,
ECO:0000269|PubMed:25224972, ECO:0000269|PubMed:26486996,
ECO:0000269|PubMed:29057928, ECO:0000269|PubMed:30725309,
ECO:0000269|Ref.9}.
-!- SIMILARITY: Belongs to the plant homeotic and developmental regulators
ALOG protein family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; AB512495; BAI52984.1; -; mRNA.
EMBL; AP004081; BAD21590.1; -; Genomic_DNA.
EMBL; AP005303; BAD22027.1; -; Genomic_DNA.
EMBL; AP008208; BAF10387.1; -; Genomic_DNA.
EMBL; AP014958; BAS81516.1; -; Genomic_DNA.
EMBL; CM000139; EAZ25035.1; -; Genomic_DNA.
EMBL; AK111446; BAG99260.1; -; mRNA.
RefSeq; XP_015624971.1; XM_015769485.1.
SMR; Q6K5X1; -.
STRING; 4530.OS02T0811000-01; -.
PaxDb; Q6K5X1; -.
PRIDE; Q6K5X1; -.
EnsemblPlants; Os02t0811000-01; Os02t0811000-01; Os02g0811000.
GeneID; 4331099; -.
Gramene; Os02t0811000-01; Os02t0811000-01; Os02g0811000.
KEGG; osa:4331099; -.
eggNOG; ENOG502QT0B; Eukaryota.
HOGENOM; CLU_071168_3_0_1; -.
InParanoid; Q6K5X1; -.
OMA; ASPQFIM; -.
OrthoDB; 1383354at2759; -.
Proteomes; UP000000763; Chromosome 2.
Proteomes; UP000007752; Chromosome 2.
Proteomes; UP000059680; Chromosome 2.
Genevisible; Q6K5X1; OS.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0009299; P:mRNA transcription; ISS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0090698; P:post-embryonic plant morphogenesis; ISS:UniProtKB.
GO; GO:0080050; P:regulation of seed development; IMP:UniProtKB.
GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
InterPro; IPR040222; ALOG.
InterPro; IPR006936; ALOG_dom.
PANTHER; PTHR31165; PTHR31165; 1.
Pfam; PF04852; DUF640; 1.
PROSITE; PS51697; ALOG; 1.
1: Evidence at protein level;
Developmental protein; DNA-binding; Nucleus; Reference proteome; Repressor;
Transcription; Transcription regulation.
CHAIN 1..248
/note="Protein G1-like6"
/id="PRO_0000425308"
DOMAIN 80..207
/note="ALOG"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01033"
REGION 1..35
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 50..84
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 198..248
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 205..210
/note="Nuclear localization signal"
/evidence="ECO:0000255"
COMPBIAS 1..15
/note="Basic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 50..80
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MUTAGEN 80
/note="R->W: Loss of homodimerization."
/evidence="ECO:0000269|PubMed:29057928"
MUTAGEN 124
/note="G->Q: Loss of homodimerization."
/evidence="ECO:0000269|PubMed:29057928"
MUTAGEN 129
/note="H->Y: Triangular hull 1 phenotype; loss of
homodimerization."
/evidence="ECO:0000269|PubMed:29057928"
SEQUENCE 248 AA; 25886 MW; A31CC55FC87E3577 CRC64;
MDRHHHHHHH HHHHMMSGGG QDPAAGDGGA GGATQDSFFL GPAAAAMFSG AGSSSSGAGT
SAGGGGGGPS PSSSSPSLSR YESQKRRDWN TFGQYLRNHR PPLSLSRCSG AHVLEFLKYM
DQFGKTKVHT PVCPFYGHPN PPAPCPCPLR QAWGSLDALI GRLRAAYEEN GGTPEMNPFG
ARAVRLYLRE VRETQARARG ISYEKKKRKK PSSAGAGAGP SSEGSPPPPG GSASGGGDTS
ASPQFIIP


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[Cyp6g1 CYP6-like DDT-R Rst(2)DDT CG8453] Cytochrome P450 6g1 (EC 1.14.-.-) (CYPVIG1) (Cyp6-like protein)
[pep NCU02549] Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (Complex III subunit I) (Core protein I) (Cytochrome b-c1 complex subunit 1, mitochondrial) (Processing enhancing protein) (Ubiquinol-cytochrome c oxidoreductase core protein 1) (Ubiquinol-cytochrome c reductase complex 50 kDa protein)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)
[gag] Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag]
[ABC1K1 ACDO1 BDR1 PGR6 At4g31390 F3L17.6] Protein ACTIVITY OF BC1 COMPLEX KINASE 1, chloroplastic (ABC1-LIKE KINASE 1) (EC 2.7.-.-) (EC 2.7.11.1) (Protein ABC1-LIKE KINASE RELATED TO CHLOROPHYLL DEGRADATION AND OXIDATIVE STRESS 1) (AtACDO1) (Protein BLEACHING AND DWARF IN RED LIGHT 1) (Protein PROTON GRADIENT REGULATION 6)
[] Core protein precursor (EC 2.7.7.48) (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Envelope glycoprotein E1) (Envelope glycoprotein E2) (Genome polyprotein) (Gp32) (Hepacivirin) (Mature core protein) (NS1) (NS3 helicase) (NS3 protease) (NS3P) (NS5B) (Non-structural protein 4A) (Non-structural protein 4B) (Non-structural protein 5A) (Protease NS2) (RNA-directed RNA polymerase) (Serine protease/helicase NS3) (Viroporin p7) (Viroporin p70) (gp35) (gp68) (gp70) (p21) (p23) (p27) (p56/58) (p68) (p8)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[orf1ab ORF1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[fes-1 NCU06606] Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 7.1.1.8) (Complex III subunit 5) (Complex III subunit V) (Rieske iron-sulfur protein) (RISP) (Ubiquinol-cytochrome c oxidoreductase iron-sulfur subunit) (Ubiquinol-cytochrome c reductase complex 25 kDa protein)
[Gnai3] Guanine nucleotide-binding protein G(i) subunit alpha-3 (G(i) alpha-3)
[egsA APE_0519.1] Glycerol-1-phosphate dehydrogenase [NAD(P)+] (G1P dehydrogenase) (G1PDH) (Gro1PDH) (EC 1.1.1.261) (Enantiomeric glycerophosphate synthase) (sn-glycerol-1-phosphate dehydrogenase)
[cox-1 coi cox1 NCM025 NCU16016] Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide I) (Cytochrome c oxidase subunit Cox1)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)
[] 49 kDa proteinase (EC 2.7.7.48) (EC 3.4.22.44) (EC 3.4.22.45) (6 kDa protein 1) (6 kDa protein 2) (Capsid protein) (Coat protein) (Cytoplasmic inclusion protein) (Genome polyprotein) (Helper component proteinase) (N-terminal protein) (NIa-pro) (Nuclear inclusion protein A) (Nuclear inclusion protein B) (P1 proteinase) (RNA-directed RNA polymerase) (VPg) (Viral genome-linked protein) (protein P3)
[] Core protein precursor (EC 2.7.7.48) (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Envelope glycoprotein E1) (Envelope glycoprotein E2) (Genome polyprotein) (Gp32) (Hepacivirin) (Mature core protein) (NS1) (NS3 helicase) (NS3 protease) (NS3P) (NS5B) (Non-structural protein 4A) (Non-structural protein 4B) (Non-structural protein 5A) (Protease NS2) (RNA-directed RNA polymerase) (Serine protease/helicase NS3) (Viroporin p7) (Viroporin p70) (gp35) (gp68) (gp70) (p21) (p23) (p27) (p56/58) (p68) (p8) (Fragment)

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