Gene_locus Report for: emeni-q5avd3

Emericella nidulans (Aspergillus nidulans) Putative uncharacterized protein

Comment

Other strains: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

Relationship

Family	\|	LIDHydrolase
Block	\|	X
Position in NCBI Life Tree	\|	Emericella nidulans

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Fungi: N E > Dikarya: N E > Ascomycota: N E > saccharomyceta: N E > Pezizomycotina: N E > leotiomyceta: N E > Eurotiomycetes: N E > Eurotiomycetidae: N E > Eurotiales: N E > Aspergillaceae: N E > Aspergillus: N E > Aspergillus nidulans: N E

There are 38 a/b hydrolases in Emericella nidulans view in a: Table

6_AlphaBeta_hydrolase : emeni-q5ax50Emericella nidulans (Aspergillus nidulans) Aspergillus nidulans FGSC A4 Putative uncharacterized protein, emeni-q5b5j7Emericella nidulans (Aspergillus nidulans) Putative uncharacterized protein, emeni-q5b938Emericella nidulans (Aspergillus nidulans) Aspergillus nidulans FGSC A4 Putative uncharacterized protein, emeni-q5ba78Emericella nidulans (Aspergillus nidulans) Aspergillus nidulans FGSC A4 Putative uncharacterized protein.
A85-IroE-IroD-Fes-Yiel : emeni-AnEstB

Emericella nidulans (Aspergillus nidulans) siderophore-degrading esterase AnEstB, emeni-q5av79

Emericella nidulans (Aspergillus nidulans) siderophore-degrading esterase AnEstA.
ABHD11-Acetyl_transferase : emeni-c8vu15Emericella nidulans (Aspergillus nidulans). Alpha/beta hydrolase, putative (AFU_orthologue AFUA_1G02390).
Acidic_Lipase : emeni-q5b446Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR 194 / M139) (Aspergillus nidulans) Triglyceride lipase-cholesterol esterase, putative (AFU_orthologue; AFUA_5G08960), emeni-q5bcd2Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR 194 / M139) (Aspergillus nidulans) Ab-hydrolase associated lipase, putative (AFU_orthologue; AFUA_2G14600).
Arb2_domain : emend-q7z8l7Emericella nidulans (Aspergillus nidulans). Putative histone deacetylase Arb2 domain.
BD-FAE : emeni-q5az32Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR 194 / M139) (Aspergillus nidulans) Polyketide synthase, putative (JCVI).
Carboxypeptidase_S10 : emeni-CBPYAEmericella nidulans (Aspergillus nidulans) carboxypeptidase.
Duf_726 : emeni-q5azl2Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) Putative uncharacterized protein, emeni-q5b602Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) Putative uncharacterized protein.
Duf_829 : emeni-q5b1v2Emericella nidulans (Aspergillus nidulans) Putative uncharacterized protein, emeni-q5bar0Emericella nidulans (Aspergillus nidulans) Putative uncharacterized protein, emeni-q5beh9Emericella nidulans (Aspergillus nidulans) Putative uncharacterized protein, emeni-q5bgk7Emericella nidulans (Aspergillus nidulans) Putative uncharacterized protein.
Duf_1100-S : emeni-q5ara9Aspergillus nidulans FGSC A4 Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR 194 / M139) (Aspergillus nidulans) hypothetical protein.
Esterase_phb : emeni-axe1Emericella nidulans (Aspergillus nidulans) AN6093-2 Acetylxylan esterase A.
FaeC : emeni-faecEmericella nidulans (Aspergillus nidulans) AN5267.2 Ferulic acid esterase C.
FSH1 : emeni-afocEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans). Asperfuranone biosynthesis protein B, emeni-dbaeEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans). Derivative of benzaldehyde biosynthesis cluster protein E.
Fungal-Bact_LIP : emeni-q5ay57Aspergillus nidulans FGSC A4 hypothetical protein, emeni-q5bcd1Aspergillus nidulans, Emericella nidulans, hypothetical protein.
Fusarinine_C_esterase_sidJ : emeni-q5ay37Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR 194 / M139) (Aspergillus nidulans) Esterase, putative (AFU_orthologue; AFUA_7G00330).
Homoserine_transacetylase : emeni-CYSCEmericella nidulans (Aspergillus nidulans) putative homoserine o-acetyltransferase, emeni-met2Emericella nidulans (Aspergillus nidulans).
Hormone-sensitive_lipase_like : emeni-stciEmericella nidulans (and Aspergillus nidulans FGSC A4) stcI gene in sterigmatocystin biosynthetic cluster.
Kynurenine-formamidase : emeni-q5bdv9Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans). N-formylkynurenine formamidase.
Lipase_3 : emeni-atg15Emericella nidulans (Aspergillus nidulans) putative lipase atg15 (EC 3.1.1.3) (autophagy-related protein 15).
MpaH : emeni-q5b719Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans). Toxin biosynthesis protein, putative (AFU_orthologue AFUA_4G12320).
Prolylcarboxypeptidase : emeni-q5awu9Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR 194 / M139) (Aspergillus nidulans) Hypothetical serine carboxypeptidase (Eurofung).
Thioesterase : emeni-acvsEmericella nidulans (Aspergillus nidulans) Aspergillus nidulans FGSC A4 acv synthetase (acvs) Thioesterase domain, emeni-q4j6a7Emericella nidulans (Aspergillus nidulans) acv synthetase (fragment), emeni-stcaEmericella nidulans (Aspergillus nidulans) Aspergillus nidulans FGSC A4 putative sterigmatocystin biosynthesis polyketide synthase (pks)Thioesterase domain.
Thiohydrolase : emeni-q5ax97Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans). DltD N-terminal domain protein (AFU_orthologue AFUA_8G00380)

Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data

Molecular evidence		Database
No mutation No structure No kinetic No Substrate No inhibitor		1 Genbank : AACD01000132 1 UniProt : Q5AVD3 1 UniProt : Q5AVD3 1 Interpro : Q5AVD3 1 Pfam : Q5AVD3 1 PIRSF : Q5AVD3 1 SUPERFAM : Q5AVD3

Sequence

Peptide

Graphical view for this peptide sequence: emeni-q5avd3
Colored MSA for LIDHydrolase (raw)
MSVCNWFVVLAWIAHSHGGSGPALDSRQVTYSLSKLSPAQLQSLEDITSS SPRVQNDHFKPEPKSTYFIYTTFIHRVSSTPTTLPLYNQDRNDPARTPHR RRQFLPQNTITRRLISYYHVFLSLLSKNIASSQLACHNGVHIVGYSLAGF ELETGAVQNEDGRQIYDLEEQICFVQRRLRENMRRLRADPTVSKHHDLGS DAATETETPKPKVILIGHSVGTYIAMEILRRHLERQSTPSDDDDVAVDFE IAGGIMLFPTVLDIAKSPSGQKLTFLLRIIPQLALMVSIFAWVLTTVLPD GLLRSLVRCVMRSPPEDAVDATTRFLKSRRGVREALHMAADEMRTITSDK WSDDVWGVSRATHKSDAHLTSKPPIQLLFYFGRNDHWVAEKTREEILAAR GGMRTGHGPKMVVCEESVPHAFCLRHNEIMARKVADMVQEVLN
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA
MSVCNWFVVLAWIAHSHGGSGPALDSRQVTYSLSKLSPAQLQSLEDITSS
SPRVQNDHFKPEPKSTYFIYTTFIHRVSSTPTTLPLYNQDRNDPARTPHR
RRQFLPQNTITRRLISYYHVFLSLLSKNIASSQLACHNGVHIVGYSLAGF
ELETGAVQNEDGRQIYDLEEQICFVQRRLRENMRRLRADPTVSKHHDLGS
DAATETETPKPKVILIGHSVGTYIAMEILRRHLERQSTPSDDDDVAVDFE
IAGGIMLFPTVLDIAKSPSGQKLTFLLRIIPQLALMVSIFAWVLTTVLPD
GLLRSLVRCVMRSPPEDAVDATTRFLKSRRGVREALHMAADEMRTITSDK
WSDDVWGVSRATHKSDAHLTSKPPIQLLFYFGRNDHWVAEKTREEILAAR
GGMRTGHGPKMVVCEESVPHAFCLRHNEIMARKVADMVQEVLN

Reference

Title:

Galagan JE, Calvo SE, Cuomo C, Ma LJ, Wortman JR, Batzoglou S, Lee SI, Basturkmen M, Spevak CC and Birren BW <40 more author(s)>

Ref:

438

PubMed

Other Papers

Send your questions or comments to :Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.

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