UniProtKB - Q4WAZ9 (PSOA_ASPFU)
PKS-NRPS hybrid synthetase psoA
NRPS14
Functioni
PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:17722120, PubMed:17464044, PubMed:24082142, PubMed:24939566).
The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566).
The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566).
Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566).
The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566).
Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).
4 Publications: Secondary metabolite biosynthesis Pathwayi
This protein is involved in Secondary metabolite biosynthesis.2 PublicationsView all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 182 | PROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: InterPro
- fatty acid synthase activity Source: GO_Central
- ligase activity Source: UniProtKB-KW
- phosphopantetheine binding Source: InterPro
GO - Biological processi
- fatty acid biosynthetic process Source: GO_Central
- nonribosomal peptide biosynthetic process Source: AspGD
- pseurotin A biosynthetic process Source: AspGD
- secondary metabolic process Source: AspGD
- secondary metabolite biosynthetic process Source: AspGD
Keywordsi
Molecular function | Ligase, Transferase |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:NRPS141 Publication Synonyms:pesO1 Publication ORF Names:AFUA_8G00540 |
Organismi | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Taxonomic identifieri | 330879 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Fumigati › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | FungiDB:Afu8g00540 |
Pathology & Biotechi
Disruption phenotypei
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000416555 | 1 – 4007 | PKS-NRPS hybrid synthetase psoAAdd BLAST | 4007 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2455 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 | |
Modified residuei | 3612 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 |
Keywords - PTMi
Phosphopantetheine, PhosphoproteinProteomic databases
PRIDEi | Q4WAZ9 |
Expressioni
Inductioni
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2418 – 2495 | Carrier 1PROSITE-ProRule annotationAdd BLAST | 78 | |
Domaini | 3576 – 3652 | Carrier 2PROSITE-ProRule annotationAdd BLAST | 77 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 389 | Ketosynthase (KS) domainSequence analysisAdd BLAST | 389 | |
Regioni | 575 – 897 | Malonyl-CoA:ACP transacylase (MAT) domainSequence analysisAdd BLAST | 323 | |
Regioni | 969 – 1147 | Dehydratase (DH) domainSequence analysisAdd BLAST | 179 | |
Regioni | 2131 – 2305 | Ketoreductase (KR) domainSequence analysisAdd BLAST | 175 | |
Regioni | 2513 – 2550 | DisorderedSequence analysisAdd BLAST | 38 | |
Regioni | 2589 – 2885 | Condensation (C) domainSequence analysisAdd BLAST | 297 | |
Regioni | 3076 – 3478 | Adenylation (A) domainSequence analysisAdd BLAST | 403 | |
Regioni | 3696 – 3920 | Reductase (R) domainSequence analysisAdd BLAST | 225 |
Domaini
Sequence similaritiesi
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG1178, Eukaryota KOG1202, Eukaryota |
HOGENOMi | CLU_000022_37_0_1 |
InParanoidi | Q4WAZ9 |
OMAi | GYPPISE |
OrthoDBi | 19161at2759 |
Family and domain databases
Gene3Di | 1.10.1200.10, 2 hits 3.10.129.110, 1 hit 3.30.300.30, 1 hit 3.30.559.10, 1 hit 3.40.366.10, 1 hit 3.40.47.10, 1 hit 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR001227, Ac_transferase_dom_sf IPR036736, ACP-like_sf IPR014043, Acyl_transferase IPR016035, Acyl_Trfase/lysoPLipase IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf IPR023213, CAT-like_dom_sf IPR001242, Condensatn IPR013120, Far_NAD-bd IPR018201, Ketoacyl_synth_AS IPR014031, Ketoacyl_synth_C IPR014030, Ketoacyl_synth_N IPR016036, Malonyl_transacylase_ACP-bd IPR036291, NAD(P)-bd_dom_sf IPR032821, PKS_assoc IPR020841, PKS_Beta-ketoAc_synthase_dom IPR020807, PKS_dehydratase IPR042104, PKS_dehydratase_sf IPR013968, PKS_KR IPR020806, PKS_PP-bd IPR009081, PP-bd_ACP IPR029063, SAM-dependent_MTases IPR016039, Thiolase-like |
Pfami | View protein in Pfam PF00698, Acyl_transf_1, 1 hit PF00501, AMP-binding, 1 hit PF00668, Condensation, 1 hit PF16197, KAsynt_C_assoc, 1 hit PF00109, ketoacyl-synt, 1 hit PF02801, Ketoacyl-synt_C, 1 hit PF08659, KR, 1 hit PF07993, NAD_binding_4, 1 hit PF00550, PP-binding, 2 hits PF14765, PS-DH, 1 hit |
SMARTi | View protein in SMART SM00827, PKS_AT, 1 hit SM00826, PKS_DH, 1 hit SM00825, PKS_KS, 1 hit SM00823, PKS_PP, 2 hits |
SUPFAMi | SSF47336, SSF47336, 2 hits SSF51735, SSF51735, 3 hits SSF52151, SSF52151, 1 hit SSF53335, SSF53335, 1 hit SSF53901, SSF53901, 1 hit SSF55048, SSF55048, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 1 hit PS00606, B_KETOACYL_SYNTHASE, 1 hit PS50075, CARRIER, 2 hits |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MVYTHSPKEP IAIIGTGCRF PGGSTSPSKL WDLLYSPRDL TREVPAESRF
60 70 80 90 100
NPKGFYNVDG EHHGASNATN AYFIEEDPRY FDAGFFSIAP REAESIDPQQ
110 120 130 140 150
RLLLETVYEA MENAGLTLNG MRGSATSAYM GAMSADYTDT QLRDIENVSK
160 170 180 190 200
YMITGTSRAL LANRLSYFFD WKGPSISVDT ACSSSLAAVH LGVQALRAGE
210 220 230 240 250
CTISCVGGSN IILNPDCYLA ATSLHLLSPT GRSQMWDQAA DGYARGEGVC
260 270 280 290 300
VFFMKTLSQA LRDGDRIDAL LRETCVNSDG RTQGIALPSA EAQVSLMRTA
310 320 330 340 350
YKNAGLDLSK AEDRPQYIEA HGTGTQAGDP REAYAIATTF FPPGEDHSHR
360 370 380 390 400
PKLVVGSVKT IIGHTEGCAG IAGILKAVLA MRHKTIPPNQ HFHNLNPSVK
410 420 430 440 450
PSFKHLSIAT SPQPWPVVPP DTPLRASVNG FGSGGTNCHA IVESYVPEIH
460 470 480 490 500
DNGPWGKPKE MTQVPNGVAA PETDFSPIPL IFSASSGTAL RAMLERYQEY
510 520 530 540 550
LERTEVSLLR LAMTLNSHRS TLPVRVSIPG TSKADVLAAI RTQLAKVGSN
560 570 580 590 600
PGAEIGTRSS VPEFDHVRRP KILGVFTGQG AQWAGMGQGL MAKSALFRQV
610 620 630 640 650
IEVMEEAMAQ LPDGPEWSLK EEIMKPPKTS RLGEAEISLP VCAALQVGLV
660 670 680 690 700
KVLRSAGITF SMVVGHSGGE IGSAYAAGKI SEVDAIKIAY YRGVYTKLAI
710 720 730 740 750
GKDGKKGGMI AVGFGYEDGL NFCAMEQFAD RLTVAASNSP KSVTLSGDLD
760 770 780 790 800
AVHEAKELLD AEGVFNRVLR LDTAYHSPHM YPCAAPYLAA IERCGLVAGK
810 820 830 840 850
SNGTAWASSV YDDNRMMTSA QDKDLEAAYW KDNLIGRVLF SQAVERALDE
860 870 880 890 900
GNGDFDLALE IGPHPSLKGP TLETIRHKIG SEIPYSGVLD RKADDILALS
910 920 930 940 950
TALGFSWLTL GSGVVDFAGY VSGFDPSNAS ILNAPALPDL PTYPWDHKKV
960 970 980 990 1000
LYRESRLNKN VRHRVDPPHP LLGSRTPDDT DYEPRWRNFL IMEELPWLRD
1010 1020 1030 1040 1050
HCVQGQIIVP AATYSVMALE AAKVLCRGKH VQSIELSDVA ILRPIVLDEA
1060 1070 1080 1090 1100
SDGTETLFSV RSDLDSNKKH EDEIHAQFTL SAGAMDDRHL RTAATGHIRI
1110 1120 1130 1140 1150
TLAAEAPSSF PNGPRPTELD LLPTSVDRFY ASMDEIGLSY SGPFRAMTSM
1160 1170 1180 1190 1200
KRRLNVASAT VAVDRDLAGT IPVHPTWLDA CFQTFLAAFA APRDGSLWTA
1210 1220 1230 1240 1250
FMPTAIGRMV FSPSSTSQVP GRSVTVDAHI TDFAPGYQVS LPTLTGDMSI
1260 1270 1280 1290 1300
FNSETNQLQI QIEDFVMSSF LPASEKDDRR FYLQNVWGQE MLSGALCAAA
1310 1320 1330 1340 1350
ERCVAPTESE SKIIDTCEKA VHYYLSKLKA AGLLDQWADK NPGLRSLMNE
1360 1370 1380 1390 1400
IEARVTSIPE QSDLVSMLGE VGEHIDLVLV RTIGESLLNS PSEGLGPITP
1410 1420 1430 1440 1450
SPMGALISRW HHEGLGFAQL QRHFVSAAKQ ISHQHANLRI LQVGPSSPGL
1460 1470 1480 1490 1500
VRSVCQELGR SLERYTLVDD SEQTIEEMKS ALAADQLRVD FTTASVENGI
1510 1520 1530 1540 1550
DAVNHLTSAG GFDLVIVHKA FTKQVTALKT VRNLLRPGGF MLMMAATGAQ
1560 1570 1580 1590 1600
LRFPFMLMST LPSLDDERLA QTKFINATRA ETHDLLRQIG FSGVDSIALD
1610 1620 1630 1640 1650
NVPDKHTFSV VVSQALDDHI AFLRSPLTSP SPVPLSGNLL VVGGFSADIA
1660 1670 1680 1690 1700
KLATAIQSLV STVWHGDIIN VRTLAELDDE ASTVEAVLSL TDLDRPVLED
1710 1720 1730 1740 1750
VRAPTFRGLQ RLFSEAKTVL WITHRAKADN PYHNATIGLG RSFQSENPQK
1760 1770 1780 1790 1800
VLQFLDVDTL DGVESAIAET FLKLIGGVNM RNSNPADPTR LWTIEPEVSL
1810 1820 1830 1840 1850
ENGKYLVPRL FPDTERNDRL NALRRKVQTQ VSVETQPISL SRSAQSDQVA
1860 1870 1880 1890 1900
YTAEAVHFHR DLADGATDPV TIQVELCSTE PVIPNIDNED LFCFVGRTSE
1910 1920 1930 1940 1950
GARLVGLSTS NSSVVKVPRE WTIPVDKHTS HDQGAFVLEL RNEIQSLVIA
1960 1970 1980 1990 2000
KSIPPGSTTL IYEPDPHLAA SLQRPGRPAT SSVSFRARST WSIPGSHILI
2010 2020 2030 2040 2050
DPHASRKDIQ AKVPPKTRML IHMEQGPETC EFLALRQALP PYATVVAFND
2060 2070 2080 2090 2100
LAADDVNPRE LLAEALSIIR GDSQSTKVPF DPSSVVKASA LVAGGTREHA
2110 2120 2130 2140 2150
NAAVVDWTGA QSITLSPRPV DTRNLFSPNK TYLLVGLTGH IGQSICRWMV
2160 2170 2180 2190 2200
QGGARHIVVT SRHPEKQGQL WREELLRQGV NIVIEAADVT KEHDLLDLRA
2210 2220 2230 2240 2250
RIVSSMPPVG GIANGAMVLD DKLFIDMPFE SFQAAMKPKV QGSIYLEEVF
2260 2270 2280 2290 2300
SADNLDFFLF FSSISVMTGQ RTQANYVAAN NFMVAMAERR RARGLPASVI
2310 2320 2330 2340 2350
DIGMVVGIGV IQRSQNDKGV SAMENSIRQM DYMPVSETDL HHLLAEAILV
2360 2370 2380 2390 2400
GQRDESPELI TGLETYKPVE GEAPFWHHNV RFSHLITDPD AAQAGADSAG
2410 2420 2430 2440 2450
SAQKSLKEML LSSGGPEEAR KVMENALLQY LASSLKLSRE TIYTDVPIID
2460 2470 2480 2490 2500
LGIDSLVAVQ IRNWTWAEAG YDLPVLKILG GSSVTQICDE VVASLSFDKS
2510 2520 2530 2540 2550
SIAAAKVDSQ AAPAHKLRPW DKPSADTKRT DSIAPVPRSQ IAANGPNGLP
2560 2570 2580 2590 2600
NGALKKASKL AVKVRPLWTT QAGGKDTKKG PRPAPIRIQP LSLGQSRLYF
2610 2620 2630 2640 2650
LSQYMDDDRV LNCTISYALS GKLDVSKLEQ SLIQVVQRHE ALRTSFYTDE
2660 2670 2680 2690 2700
KDGKPMQGLL EKSPFRLRVV PGVSASSDVE TEFNLIRYRP YDLEQADTFA
2710 2720 2730 2740 2750
ATLLSHSPDS HTLICGYHHI IMDGVSWQIF QKDLAMFYNN SGIADSAKHL
2760 2770 2780 2790 2800
PAQYSEFTRK QQEDLSCGAY AERLRFFQDQ FREPVESLPL FPFAKVGTRK
2810 2820 2830 2840 2850
VVKQYAVQEA TTHLNAKVVS AIKQASQTSR TTPFHFYLSA FQVLLHRLLE
2860 2870 2880 2890 2900
TDKMCIGVVD ANRSDQNFVN TIGFFLETIP LWFKVNSEQR FVELLKETRT
2910 2920 2930 2940 2950
KAYAALAQTG VPTEEILRAC GVASSTTETP LFQVCFNYRM GAGRTAALQG
2960 2970 2980 2990 3000
VEMKFLDYVD AQNPFDLVAT VDDLDDGTAM ITLYLQDYLY DQEGAQLLAT
3010 3020 3030 3040 3050
MYANVLQVLA ENPERLVGSV SISNATLEDE GVKLGTGPIL DLVAPSTPTL
3060 3070 3080 3090 3100
SKIFHTWVDK DPHALAVKDT TGKSKTYVQL AERANAIAAS LLNAGAAPSI
3110 3120 3130 3140 3150
PIGVLLDPGV DTIATILAIL RIGAAYVPLD TRSSDAVLSD ILQESQPGIV
3160 3170 3180 3190 3200
IHHSATAPRS QILLKASAKT KLVTLNAVPQ KTIRKIQDVS VPEGLAMILY
3210 3220 3230 3240 3250
TSGSTGSPKG IPLTNANIRT PILGVSERVP LGREVVLQQS GQGFDAAVYQ
3260 3270 3280 3290 3300
IFIALANGGT LIMVDNRDDP AKVAALMAQE SVTCTTHIVS EMQALLKYGY
3310 3320 3330 3340 3350
DELRNCSSWR IAMVAGEAFT VHLLDQFRAL NRPDLKVINA YGPTEASICS
3360 3370 3380 3390 3400
SLGEVSFNRI SSSETSIPIG KAIPNYGTYI VDQHCKPVPL GWPGEVAIAG
3410 3420 3430 3440 3450
PGVASGYLNL GELTQAKFRS AATLGEVFGS DCLYLTGDRG RMLSDGSIVL
3460 3470 3480 3490 3500
SGRVDGDDQV KIRGHRVQLG DVARALVQAS RGVFADAAVI LKGDDTSNPQ
3510 3520 3530 3540 3550
LVAYVVFSRT SNIQDQQTYL RQLNQDLPVP AYMRPAITIP LDTLPVTDRG
3560 3570 3580 3590 3600
KLDSKKLASL PLPSISVDYE EDEQLTPTEA RLRDVWKNVL GDIASSIPIR
3610 3620 3630 3640 3650
RSSDFFSVGG NSLILLALKA EIAQVFGVGL SVSELFQAST LELLAARLDG
3660 3670 3680 3690 3700
TSLLAQINWE EETAPDETQF TLPPPINGIN GHGSSNGHAQ GISVLLTGAT
3710 3720 3730 3740 3750
GFLGGHILRQ LVQLPSVEHV HCVAIRPNKV DVRRQLSVES PKIIRYSGDL
3760 3770 3780 3790 3800
ALPNMGMSES EFSDLFKSID VIVHNGAEVS HMKNYRSLRA ANFLSTVGLA
3810 3820 3830 3840 3850
RAAVSRGIPI HYISTGGVAR LSVADEQPEA SLAAFHPPID GSDGYVASKW
3860 3870 3880 3890 3900
ASEVFLEKVQ RRFQGQVWIH RPSSITGDDV PDNDIAHSLL KFSRELGAVP
3910 3920 3930 3940 3950
ELTGSGFFDF INVETVSNNI AASVVRSSEK SGGGLIYLHQ SGEQVIPVGD
3960 3970 3980 3990 4000
LQKYVEELEG RPLQVLPLKE WVDLSIRKGL DEVLGSYMLA SKGVIRAPLL
QRGPHVE
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AAHF01000014 Genomic DNA Translation: EAL85113.2 |
RefSeqi | XP_747151.2, XM_742058.2 |
Genome annotation databases
EnsemblFungii | EAL85113; EAL85113; AFUA_8G00540 |
GeneIDi | 3504510 |
KEGGi | afm:AFUA_8G00540 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AAHF01000014 Genomic DNA Translation: EAL85113.2 |
RefSeqi | XP_747151.2, XM_742058.2 |
3D structure databases
SMRi | Q4WAZ9 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 746128.CADAFUBP00008381 |
Proteomic databases
PRIDEi | Q4WAZ9 |
Genome annotation databases
EnsemblFungii | EAL85113; EAL85113; AFUA_8G00540 |
GeneIDi | 3504510 |
KEGGi | afm:AFUA_8G00540 |
Organism-specific databases
VEuPathDBi | FungiDB:Afu8g00540 |
Phylogenomic databases
eggNOGi | KOG1178, Eukaryota KOG1202, Eukaryota |
HOGENOMi | CLU_000022_37_0_1 |
InParanoidi | Q4WAZ9 |
OMAi | GYPPISE |
OrthoDBi | 19161at2759 |
Family and domain databases
Gene3Di | 1.10.1200.10, 2 hits 3.10.129.110, 1 hit 3.30.300.30, 1 hit 3.30.559.10, 1 hit 3.40.366.10, 1 hit 3.40.47.10, 1 hit 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR001227, Ac_transferase_dom_sf IPR036736, ACP-like_sf IPR014043, Acyl_transferase IPR016035, Acyl_Trfase/lysoPLipase IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf IPR023213, CAT-like_dom_sf IPR001242, Condensatn IPR013120, Far_NAD-bd IPR018201, Ketoacyl_synth_AS IPR014031, Ketoacyl_synth_C IPR014030, Ketoacyl_synth_N IPR016036, Malonyl_transacylase_ACP-bd IPR036291, NAD(P)-bd_dom_sf IPR032821, PKS_assoc IPR020841, PKS_Beta-ketoAc_synthase_dom IPR020807, PKS_dehydratase IPR042104, PKS_dehydratase_sf IPR013968, PKS_KR IPR020806, PKS_PP-bd IPR009081, PP-bd_ACP IPR029063, SAM-dependent_MTases IPR016039, Thiolase-like |
Pfami | View protein in Pfam PF00698, Acyl_transf_1, 1 hit PF00501, AMP-binding, 1 hit PF00668, Condensation, 1 hit PF16197, KAsynt_C_assoc, 1 hit PF00109, ketoacyl-synt, 1 hit PF02801, Ketoacyl-synt_C, 1 hit PF08659, KR, 1 hit PF07993, NAD_binding_4, 1 hit PF00550, PP-binding, 2 hits PF14765, PS-DH, 1 hit |
SMARTi | View protein in SMART SM00827, PKS_AT, 1 hit SM00826, PKS_DH, 1 hit SM00825, PKS_KS, 1 hit SM00823, PKS_PP, 2 hits |
SUPFAMi | SSF47336, SSF47336, 2 hits SSF51735, SSF51735, 3 hits SSF52151, SSF52151, 1 hit SSF53335, SSF53335, 1 hit SSF53901, SSF53901, 1 hit SSF55048, SSF55048, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 1 hit PS00606, B_KETOACYL_SYNTHASE, 1 hit PS50075, CARRIER, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | PSOA_ASPFU | |
Accessioni | Q4WAZ9Primary (citable) accession number: Q4WAZ9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 18, 2012 |
Last sequence update: | April 17, 2007 | |
Last modified: | February 23, 2022 | |
This is version 114 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families