Fungal Genomics

at Utrecht University

General Properties

Protein IDOphauB2|4093
Gene name
LocationContig_27:20548..21971
Strand+
Gene length (bp)1423
Transcript length (bp)1251
Coding sequence length (bp)1251
Protein length (aa) 417

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PFAM Domains

PFAM Domain ID Short name Long name E-value Start End
PF00364 Biotin_lipoyl Biotin-requiring enzyme 4.5E-20 35 108
PF02817 E3_binding e3 binding domain 1.8E-07 167 203

Swissprot hits

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Swissprot ID Swissprot Description Start End E-value
sp|O94709|ODPX_SCHPO Probable pyruvate dehydrogenase protein X component, mitochondrial OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN=SPCC1259.09c PE=2 SV=1 5 270 4.0E-45
sp|P16451|ODPX_YEAST Pyruvate dehydrogenase complex protein X component, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=PDX1 PE=1 SV=1 4 233 1.0E-43
sp|Q1RJT3|ODP2_RICBR Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Rickettsia bellii (strain RML369-C) GN=pdhC PE=3 SV=1 36 275 7.0E-28
sp|Q8RWN9|ODP22_ARATH Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial OS=Arabidopsis thaliana GN=At3g13930 PE=2 SV=2 20 331 5.0E-26
sp|O66119|ODP2_ZYMMO Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) GN=pdhC PE=3 SV=2 38 298 7.0E-25
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Swissprot ID Swissprot Description Start End E-value
sp|O94709|ODPX_SCHPO Probable pyruvate dehydrogenase protein X component, mitochondrial OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN=SPCC1259.09c PE=2 SV=1 5 270 4.0E-45
sp|P16451|ODPX_YEAST Pyruvate dehydrogenase complex protein X component, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=PDX1 PE=1 SV=1 4 233 1.0E-43
sp|Q1RJT3|ODP2_RICBR Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Rickettsia bellii (strain RML369-C) GN=pdhC PE=3 SV=1 36 275 7.0E-28
sp|Q8RWN9|ODP22_ARATH Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial OS=Arabidopsis thaliana GN=At3g13930 PE=2 SV=2 20 331 5.0E-26
sp|O66119|ODP2_ZYMMO Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) GN=pdhC PE=3 SV=2 38 298 7.0E-25
sp|Q5M729|ODP23_ARATH Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial OS=Arabidopsis thaliana GN=At1g54220 PE=2 SV=1 22 232 3.0E-24
sp|Q8BKZ9|ODPX_MOUSE Pyruvate dehydrogenase protein X component, mitochondrial OS=Mus musculus GN=Pdhx PE=1 SV=1 18 216 2.0E-23
sp|Q4ULG1|ODP2_RICFE Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) GN=pdhC PE=3 SV=1 36 205 9.0E-23
sp|Q92HK7|ODP2_RICCN Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Rickettsia conorii (strain ATCC VR-613 / Malish 7) GN=pdhC PE=3 SV=1 36 205 2.0E-22
sp|P12695|ODP2_YEAST Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=LAT1 PE=1 SV=1 4 206 3.0E-22
sp|P22439|ODPX_BOVIN Pyruvate dehydrogenase protein X component OS=Bos taurus GN=PDHX PE=1 SV=3 15 203 3.0E-22
sp|O00330|ODPX_HUMAN Pyruvate dehydrogenase protein X component, mitochondrial OS=Homo sapiens GN=PDHX PE=1 SV=3 18 203 3.0E-21
sp|Q9R9N3|ODP2_RHIME Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Rhizobium meliloti (strain 1021) GN=pdhC PE=3 SV=1 35 115 3.0E-21
sp|P20285|ODP2_NEUCR Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) GN=mrp-3 PE=1 SV=2 38 202 5.0E-21
sp|Q9ZD20|ODP2_RICPR Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Rickettsia prowazekii (strain Madrid E) GN=pdhC PE=3 SV=1 36 205 7.0E-21
sp|O59816|ODP2_SCHPO Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN=lat1 PE=3 SV=1 28 202 2.0E-20
sp|Q0WQF7|ODP21_ARATH Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial OS=Arabidopsis thaliana GN=LTA3 PE=2 SV=2 38 206 3.0E-20
sp|Q68WK6|ODP2_RICTY Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Rickettsia typhi (strain ATCC VR-144 / Wilmington) GN=pdhC PE=3 SV=1 36 205 3.0E-19
sp|Q0WQF7|ODP21_ARATH Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial OS=Arabidopsis thaliana GN=LTA3 PE=2 SV=2 38 152 1.0E-18
sp|P36413|ODP2_DICDI Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Dictyostelium discoideum GN=pdhC PE=1 SV=2 33 136 2.0E-18
sp|Q92J43|ODO2_RICCN Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Rickettsia conorii (strain ATCC VR-613 / Malish 7) GN=sucB PE=3 SV=1 36 386 5.0E-18
sp|Q9R9N4|ODPB_RHIME Pyruvate dehydrogenase E1 component subunit beta OS=Rhizobium meliloti (strain 1021) GN=pdhB PE=3 SV=2 35 128 9.0E-18
sp|Q1RHI5|ODO2_RICBR Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Rickettsia bellii (strain RML369-C) GN=sucB PE=3 SV=1 36 386 2.0E-17
sp|O66113|ODPB_ZYMMO Pyruvate dehydrogenase E1 component subunit beta OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) GN=pdhB PE=3 SV=2 38 133 3.0E-17
sp|Q8BMF4|ODP2_MOUSE Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Mus musculus GN=Dlat PE=1 SV=2 35 206 1.0E-16
sp|Q19749|ODP2_CAEEL Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Caenorhabditis elegans GN=F23B12.5 PE=1 SV=1 27 145 4.0E-16
sp|P08461|ODP2_RAT Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Rattus norvegicus GN=Dlat PE=1 SV=3 35 206 6.0E-16
sp|Q4UKI7|ODO2_RICFE Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) GN=sucB PE=3 SV=1 36 386 9.0E-16
sp|P10515|ODP2_HUMAN Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Homo sapiens GN=DLAT PE=1 SV=3 37 206 8.0E-15
sp|Q9ZDY4|ODO2_RICPR Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Rickettsia prowazekii (strain Madrid E) GN=sucB PE=3 SV=1 36 386 1.0E-14
sp|Q68XI8|ODO2_RICTY Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Rickettsia typhi (strain ATCC VR-144 / Wilmington) GN=sucB PE=3 SV=1 36 355 4.0E-14
sp|Q9C8P0|ODP25_ARATH Dihydrolipoyllysine-residue acetyltransferase component 5 of pyruvate dehydrogenase complex, chloroplastic OS=Arabidopsis thaliana GN=EMB3003 PE=2 SV=1 18 116 2.0E-13
sp|P36413|ODP2_DICDI Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Dictyostelium discoideum GN=pdhC PE=1 SV=2 27 206 4.0E-13
sp|Q8BMF4|ODP2_MOUSE Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Mus musculus GN=Dlat PE=1 SV=2 34 120 5.0E-12
sp|P08461|ODP2_RAT Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Rattus norvegicus GN=Dlat PE=1 SV=3 34 120 7.0E-12
sp|P10515|ODP2_HUMAN Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial OS=Homo sapiens GN=DLAT PE=1 SV=3 34 120 4.0E-11
sp|Q23571|ODB2_CAEEL Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial OS=Caenorhabditis elegans GN=ZK669.4 PE=3 SV=1 10 211 4.0E-10
sp|P16263|ODO2_BACSU Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Bacillus subtilis (strain 168) GN=odhB PE=3 SV=2 38 205 7.0E-10
sp|Q9SQI8|ODP24_ARATH Dihydrolipoyllysine-residue acetyltransferase component 4 of pyruvate dehydrogenase complex, chloroplastic OS=Arabidopsis thaliana GN=LTA2 PE=2 SV=1 22 108 9.0E-10
sp|Q8CSL9|ODO2_STAES Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Staphylococcus epidermidis (strain ATCC 12228) GN=odhB PE=3 SV=1 38 308 3.0E-09
sp|Q6GGZ6|ODO2_STAAR Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Staphylococcus aureus (strain MRSA252) GN=odhB PE=3 SV=1 38 186 4.0E-09
sp|Q49XM4|ODO2_STAS1 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) GN=odhB PE=3 SV=1 38 152 5.0E-09
sp|Q5HPC7|ODO2_STAEQ Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) GN=odhB PE=3 SV=1 38 308 7.0E-09
sp|O31550|ACOC_BACSU Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system OS=Bacillus subtilis (strain 168) GN=acoC PE=3 SV=1 33 296 1.0E-08
sp|P37942|ODB2_BACSU Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex OS=Bacillus subtilis (strain 168) GN=bfmBB PE=3 SV=1 31 266 2.0E-08
sp|P0AFG6|ODO2_ECOLI Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Escherichia coli (strain K12) GN=sucB PE=1 SV=2 31 206 3.0E-08
sp|P0AFG7|ODO2_ECO57 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Escherichia coli O157:H7 GN=sucB PE=1 SV=2 31 206 3.0E-08
sp|Q2YY06|ODO2_STAAB Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Staphylococcus aureus (strain bovine RF122 / ET3-1) GN=odhB PE=3 SV=1 38 186 4.0E-08
sp|Q8CT13|ODP2_STAES Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Staphylococcus epidermidis (strain ATCC 12228) GN=pdhC PE=3 SV=1 36 220 5.0E-08
sp|Q5HQ74|ODP2_STAEQ Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) GN=pdhC PE=3 SV=1 36 208 7.0E-08
sp|Q7A5N4|ODO2_STAAN Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Staphylococcus aureus (strain N315) GN=odhB PE=1 SV=1 38 110 8.0E-08
sp|Q99U75|ODO2_STAAM Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) GN=odhB PE=3 SV=1 38 110 8.0E-08
sp|Q8NWR7|ODO2_STAAW Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Staphylococcus aureus (strain MW2) GN=odhB PE=3 SV=1 38 110 8.0E-08
sp|Q6G9E9|ODO2_STAAS Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Staphylococcus aureus (strain MSSA476) GN=odhB PE=3 SV=1 38 110 8.0E-08
sp|Q5HG07|ODO2_STAAC Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Staphylococcus aureus (strain COL) GN=odhB PE=3 SV=1 38 110 8.0E-08
sp|Q2FYM2|ODO2_STAA8 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Staphylococcus aureus (strain NCTC 8325) GN=odhB PE=3 SV=1 38 110 8.0E-08
sp|Q2FH26|ODO2_STAA3 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Staphylococcus aureus (strain USA300) GN=odhB PE=3 SV=1 38 110 8.0E-08
sp|Q6GHZ0|ODP2_STAAR Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Staphylococcus aureus (strain MRSA252) GN=pdhC PE=3 SV=1 36 253 2.0E-07
sp|P65635|ODP2_STAAM Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) GN=pdhC PE=3 SV=1 36 253 2.0E-07
sp|P65636|ODP2_STAAN Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Staphylococcus aureus (strain N315) GN=pdhC PE=1 SV=1 36 253 2.0E-07
sp|Q8NX76|ODP2_STAAW Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Staphylococcus aureus (strain MW2) GN=pdhC PE=3 SV=1 36 253 3.0E-07
sp|Q6GAB9|ODP2_STAAS Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Staphylococcus aureus (strain MSSA476) GN=pdhC PE=3 SV=1 36 253 3.0E-07
sp|Q5HGY9|ODP2_STAAC Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Staphylococcus aureus (strain COL) GN=pdhC PE=3 SV=1 36 253 3.0E-07
sp|Q59821|ODP2_STAAU Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex OS=Staphylococcus aureus GN=pdhC PE=3 SV=1 36 253 3.0E-07
sp|Q89AJ6|ODO2_BUCBP Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) GN=sucB PE=3 SV=1 35 219 7.0E-07
sp|P45302|ODO2_HAEIN Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) GN=sucB PE=3 SV=1 33 202 4.0E-06
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GO

GO Term Description Terminal node
GO:0016746 acyltransferase activity Yes
GO:0003824 catalytic activity No
GO:0016740 transferase activity No
GO:0003674 molecular_function No

SignalP

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SignalP signal predicted Location
(based on Ymax)		 D score
(significance: > 0.45)
No 1 - 24 0.45

Transmembrane Domains

(None)

Transcription Factor Class

(None)

Expression data

No expression data available for this genome

Sequences

Type of sequenceSequence
Locus Download genbank file of locus
The gene with 5 kb flanks (if sufficient flanking sequence is available). For use in cloning design programs. NOTE: features (genes or exons) that are only partially contained within the sequence are completely excluded.
Protein >OphauB2|4093
MASLATTCRVSARLLGRRAATRAFTTSSRCLAAQNFVMPALSPTMTEGNIASWSVSEGQSFSAGDVLLEIETDKA
TMDVEAQEDGVVFKILAEKGAKGVQVGARIAVLAEPGDDLASLEEPRAQASKAPDASPEPKTTETSSTPSRQPDK
DDAATKGQTQHALRRPLLPSVEFLVHEHRIAPADVARIKPTGPGGRLLKGDVLAYLGAIAASSPAAVSSRFAKLA
ALDLSNIKVAAPVAPSQPLEPAPPPTTQLNMPVSLASVLEVQKRIHDSLGVLLPLSTFISRATDVANEALPRVPA
PPTPSELFDQVLGLHSVKAAAGSRGVYQPQISALVPQAQLRPAPRARAAQPSLFDEIVGPRTKTAPRRAGPMTMP
GLSSGDNVFSLVVPKNEEKRGRLFLERCKTILEKEPGRLVL*
Coding >OphauB2|4093
ATGGCGTCACTAGCGACGACATGCCGTGTGTCAGCGCGCCTACTCGGTCGTCGGGCCGCAACTCGAGCCTTTACC
ACGTCGTCTAGATGCCTCGCGGCGCAAAATTTTGTCATGCCTGCGCTATCGCCGACAATGACCGAGGGCAACATT
GCCAGCTGGAGCGTCAGCGAGGGCCAGTCCTTTTCGGCAGGCGACGTGCTGCTGGAGATTGAGACGGACAAGGCG
ACGATGGATGTCGAGGCGCAAGAAGACGGCGTCGTCTTCAAGATTTTGGCGGAAAAGGGCGCAAAGGGCGTGCAG
GTGGGTGCGCGCATCGCCGTCTTGGCCGAGCCGGGAGACGACTTGGCATCGCTCGAGGAGCCGCGCGCGCAGGCC
AGCAAAGCTCCCGACGCGAGTCCCGAGCCCAAGACTACCGAGACGAGCAGCACGCCCTCGCGTCAGCCCGACAAG
GACGACGCCGCCACAAAGGGCCAGACGCAGCACGCGCTCCGGCGGCCCCTTTTGCCGTCTGTCGAGTTTCTAGTC
CACGAGCACCGCATCGCCCCCGCCGACGTGGCGCGTATCAAGCCCACAGGCCCCGGCGGCCGCCTGCTAAAGGGC
GACGTGCTGGCATATCTGGGCGCCATTGCCGCCTCGTCGCCCGCCGCCGTGTCGAGCCGCTTCGCCAAGCTGGCC
GCTCTCGACCTGAGCAACATCAAGGTTGCCGCGCCCGTGGCTCCCTCCCAGCCCCTTGAGCCCGCCCCACCGCCC
ACGACGCAGCTCAACATGCCCGTCTCGCTCGCCAGCGTGCTCGAGGTGCAGAAGCGCATCCACGACTCGCTCGGC
GTCTTGCTCCCGCTCTCAACCTTTATCTCGCGCGCCACCGACGTGGCCAATGAAGCCCTGCCGCGCGTCCCGGCG
CCGCCCACGCCCTCGGAGCTCTTTGACCAGGTCCTTGGCCTGCACAGCGTCAAGGCGGCGGCCGGCTCGCGCGGC
GTCTACCAGCCTCAAATCTCAGCCCTGGTGCCGCAGGCGCAGCTTAGGCCGGCGCCGCGGGCACGTGCTGCGCAG
CCTAGTCTGTTTGACGAAATAGTTGGGCCGCGGACCAAGACTGCGCCCAGACGAGCTGGCCCCATGACCATGCCG
GGCTTGTCGAGCGGTGACAATGTGTTTAGTCTTGTGGTGCCCAAGAATGAGGAGAAGCGAGGCCGGCTTTTCCTC
GAGCGCTGCAAGACCATTTTGGAAAAGGAGCCGGGCCGTCTGGTTCTGTAG
Transcript >OphauB2|4093
ATGGCGTCACTAGCGACGACATGCCGTGTGTCAGCGCGCCTACTCGGTCGTCGGGCCGCAACTCGAGCCTTTACC
ACGTCGTCTAGATGCCTCGCGGCGCAAAATTTTGTCATGCCTGCGCTATCGCCGACAATGACCGAGGGCAACATT
GCCAGCTGGAGCGTCAGCGAGGGCCAGTCCTTTTCGGCAGGCGACGTGCTGCTGGAGATTGAGACGGACAAGGCG
ACGATGGATGTCGAGGCGCAAGAAGACGGCGTCGTCTTCAAGATTTTGGCGGAAAAGGGCGCAAAGGGCGTGCAG
GTGGGTGCGCGCATCGCCGTCTTGGCCGAGCCGGGAGACGACTTGGCATCGCTCGAGGAGCCGCGCGCGCAGGCC
AGCAAAGCTCCCGACGCGAGTCCCGAGCCCAAGACTACCGAGACGAGCAGCACGCCCTCGCGTCAGCCCGACAAG
GACGACGCCGCCACAAAGGGCCAGACGCAGCACGCGCTCCGGCGGCCCCTTTTGCCGTCTGTCGAGTTTCTAGTC
CACGAGCACCGCATCGCCCCCGCCGACGTGGCGCGTATCAAGCCCACAGGCCCCGGCGGCCGCCTGCTAAAGGGC
GACGTGCTGGCATATCTGGGCGCCATTGCCGCCTCGTCGCCCGCCGCCGTGTCGAGCCGCTTCGCCAAGCTGGCC
GCTCTCGACCTGAGCAACATCAAGGTTGCCGCGCCCGTGGCTCCCTCCCAGCCCCTTGAGCCCGCCCCACCGCCC
ACGACGCAGCTCAACATGCCCGTCTCGCTCGCCAGCGTGCTCGAGGTGCAGAAGCGCATCCACGACTCGCTCGGC
GTCTTGCTCCCGCTCTCAACCTTTATCTCGCGCGCCACCGACGTGGCCAATGAAGCCCTGCCGCGCGTCCCGGCG
CCGCCCACGCCCTCGGAGCTCTTTGACCAGGTCCTTGGCCTGCACAGCGTCAAGGCGGCGGCCGGCTCGCGCGGC
GTCTACCAGCCTCAAATCTCAGCCCTGGTGCCGCAGGCGCAGCTTAGGCCGGCGCCGCGGGCACGTGCTGCGCAG
CCTAGTCTGTTTGACGAAATAGTTGGGCCGCGGACCAAGACTGCGCCCAGACGAGCTGGCCCCATGACCATGCCG
GGCTTGTCGAGCGGTGACAATGTGTTTAGTCTTGTGGTGCCCAAGAATGAGGAGAAGCGAGGCCGGCTTTTCCTC
GAGCGCTGCAAGACCATTTTGGAAAAGGAGCCGGGCCGTCTGGTTCTGTAG
Gene >OphauB2|4093
ATGGCGTCACTAGCGACGACATGCCGTGTGTCAGCGCGCCTACTCGGTCGTCGGGCCGCAACTCGAGGTACGATT
ATCACAGAGTCCAAGTCGGAGCGAGTAGAAGGGAAAAAAAAAAAAAAAAAAAAGAGGGCTAGTGCCAAGTCTTTG
CGCCAGAGGAAGAATTTCACAAACATGAAGAAGAAGCCAAGCACCACAGCAAAAGAAGACTAACTGGACCGATTT
CACCCCATAAACAGCCTTTACCACGTCGTCTAGATGCCTCGCGGCGCAAAATTTTGTCATGCCTGCGCTATCGCC
GACAATGACCGAGGGCAACATTGCCAGCTGGAGCGTCAGCGAGGGCCAGTCCTTTTCGGCAGGCGACGTGCTGCT
GGAGATTGAGACGGACAAGGCGACGATGGATGTCGAGGCGCAAGAAGACGGCGTCGTCTTCAAGATTTTGGCGGA
AAAGGGCGCAAAGGGCGTGCAGGTGGGTGCGCGCATCGCCGTCTTGGCCGAGCCGGGAGACGACTTGGCATCGCT
CGAGGAGCCGCGCGCGCAGGCCAGCAAAGCTCCCGACGCGAGTCCCGAGCCCAAGACTACCGAGACGAGCAGCAC
GCCCTCGCGTCAGCCCGACAAGGACGACGCCGCCACAAAGGGCCAGACGCAGCACGCGCTCCGGCGGCCCCTTTT
GCCGTCTGTCGAGTTTCTAGTCCACGAGCACCGCATCGCCCCCGCCGACGTGGCGCGTATCAAGCCCACAGGCCC
CGGCGGCCGCCTGCTAAAGGGCGACGTGCTGGCATATCTGGGCGCCATTGCCGCCTCGTCGCCCGCCGCCGTGTC
GAGCCGCTTCGCCAAGCTGGCCGCTCTCGACCTGAGCAACATCAAGGTTGCCGCGCCCGTGGCTCCCTCCCAGCC
CCTTGAGCCCGCCCCACCGCCCACGACGCAGCTCAACATGCCCGTCTCGCTCGCCAGCGTGCTCGAGGTGCAGAA
GCGCATCCACGACTCGCTCGGCGTCTTGCTCCCGCTCTCAACCTTTATCTCGCGCGCCACCGACGTGGCCAATGA
AGCCCTGCCGCGCGTCCCGGCGCCGCCCACGCCCTCGGAGCTCTTTGACCAGGTCCTTGGCCTGCACAGCGTCAA
GGCGGCGGCCGGCTCGCGCGGCGTCTACCAGCCTCAAATCTCAGCCCTGGTGCCGCAGGCGCAGCTTAGGCCGGC
GCCGCGGGCACGTGCTGCGCAGCCTAGTCTGTTTGACGAAATAGTTGGGCCGCGGACCAAGACTGCGCCCAGACG
AGCTGGCCCCATGACCATGCCGGGCTTGTCGAGCGGTGACAATGTGTTTAGTCTTGTGGTGCCCAAGAATGAGGA
GAAGCGAGGCCGGCTTTTCCTCGAGCGCTGCAAGACCATTTTGGAAAAGGAGCCGGGCCGTCTGGTTCTGTAG

© 2022 - Robin Ohm - Utrecht University - The Netherlands

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