ECDF_ASPRU
ID ECDF_ASPRU Reviewed; 508 AA.
AC K0E681;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Putative glycosyl hydrolase ecdF {ECO:0000303|PubMed:22998630};
DE EC=3.2.1.- {ECO:0000305|PubMed:22998630};
DE Flags: Precursor;
GN Name=ecdF {ECO:0000303|PubMed:22998630};
OS Aspergillus rugulosus (Emericella rugulosa).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41736;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 58397 / NRRL 11440;
RX PubMed=22998630; DOI=10.1021/ja307220z;
RA Cacho R.A., Jiang W., Chooi Y.H., Walsh C.T., Tang Y.;
RT "Identification and characterization of the echinocandin B biosynthetic
RT gene cluster from Emericella rugulosa NRRL 11440.";
RL J. Am. Chem. Soc. 134:16781-16790(2012).
RN [2]
RP CLUSTER REVISION.
RX PubMed=27502607; DOI=10.1186/s12864-016-2885-x;
RA Huettel W., Youssar L., Gruening B.A., Guenther S., Hugentobler K.G.;
RT "Echinocandin B biosynthesis: a biosynthetic cluster from Aspergillus
RT nidulans NRRL 8112 and reassembly of the subclusters Ecd and Hty from
RT Aspergillus pachycristatus NRRL 11440 reveals a single coherent gene
RT cluster.";
RL BMC Genomics 17:570-570(2016).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC -!- CAUTION: EcdB, ecdC, ecdD, ecdE and ecdF have previously been
CC identified as being part of the echinocandin B biosynthetic cluster,
CC but it was later realized that this was due to a genome misassembly and
CC these 5 proteins are now considered as artifacts and not part of the
CC cluster. {ECO:0000269|PubMed:27502607}.
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DR EMBL; JX421684; AFT91384.1; -; Genomic_DNA.
DR AlphaFoldDB; K0E681; -.
DR SMR; K0E681; -.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..508
FT /note="Putative glycosyl hydrolase ecdF"
FT /evidence="ECO:0000255"
FT /id="PRO_5013130535"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 508 AA; 54821 MW; 24E4E153F8819E6A CRC64;
MFLHILCLLA GQALADDYRP VFHFVPEKNW MNEPNGLIKI GSTWHLFYQH NPTANVWGNL
NWGHATSSDL VHWTHEPLAI TSENGIEAFT GTSYYDAENT SGLGTSDNPP YLAWYTGYFP
SNGTQDQRLA FSIDAGETWT KFEGNPVISA AQEAPHDATG GLETRDPKVF FHADSGKWIM
VLAHGGQNKM SFWTSVDAKR WSWASDLTST QVPGLPSAVK GWEVPDMFEV PVHGTDKTTW
VLIFTPAEGS PAGGNGVLAL TGSFDGTVFH PNPVNVSTLW LDYGRDFDGA LSWENLPDSD
GHRILAAISN SYGANPPTNT WKGMLSFPRT LSLHQSQTGQ YFLQQPVSNL DTVSTPLVSV
KNQTIAPGQV LLSSVRGTAL DIRIAFSANA GTVLSLAVRK AGSQETVIQY RQSDATLSVD
RTTSGLTSYD PAAGGVHTAP LRPDASGVVQ IRALVDTCSV EVFGGQGEVV ISDLIFPDET
SDGLALQVIG GTAVLRSLEK FPRLGAVL