ID A0A2H3IEV7_9EURO Unreviewed; 443 AA.
AC A0A2H3IEV7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 10.
DE SubName: Full=Glycoside hydrolase/deacetylase, beta/alpha-barrel {ECO:0000313|EMBL:PCH00073.1};
GN ORFNames=PENO1_050020 {ECO:0000313|EMBL:PCH00073.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH00073.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH00073.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH00073.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCH00073.1}.
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DR EMBL; NPFK01000127; PCH00073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IEV7; -.
DR STRING; 290292.A0A2H3IEV7; -.
DR OrthoDB; 1768301at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10917; CE4_NodB_like_6s_7s; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR PANTHER; PTHR46471:SF6; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PCH00073.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..443
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013581394"
FT DOMAIN 209..396
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 443 AA; 51206 MW; BCB52D93346BD074 CRC64;
MKLLTVLAYY ILFIIISSAH AMMPLRKRPR DFVIDDFCRS SVNSLDAWHG PGENLPIEYD
QDDDDDCSVR LSPSNPDHNY HTQFSYSCFD LSKHRKMFLH VKYSGSDAFT ISLYQHNGAC
NPWRAPFPGT FDSIEASRYV TDDEGDIYVP LSHFYVDLKR ASSIAFHGFY TSEETILHKV
EIVKHLPDDV DVPRKLPTGT MVLNCKRPNS FAFGIDDGDP ALAQVVMDIL EDEDIKVTFF
VVGRGLRDPD TNFTNLYSEM LERGHQVALH SDTHPKMEGL QTIDEIDDEI TGGQHALKDL
LGVRSRYFRP PYGTVGARMR QRLAAHIDDP YIVNWSVDVE DWLWANTDEP WRQLKAFRRD
VERGGDLVVM HYLTWSTVRY FRDFIDIARR KGRRIMRIDQ CMMDPDAPEL SSLESLQDDG
DESRMLRTQL HSQHEVDVEV EEW
//
