ID   ECDE_ASPRU              Reviewed;         703 AA.
AC   K0E4E1;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Putative glycosyl hydrolase ecdE {ECO:0000303|PubMed:22998630};
DE            EC=3.2.1.- {ECO:0000305|PubMed:22998630};
DE   Flags: Precursor;
GN   Name=ecdE {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; AFT91388.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0E4E1; -.
DR   SMR; K0E4E1; -.
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; -; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001362; Glyco_hydro_32.
DR   InterPro; IPR018053; Glyco_hydro_32_AS.
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; 2.
DR   SMART; SM00640; Glyco_32; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
DR   PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..703
FT                   /note="Putative glycosyl hydrolase ecdE"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003830476"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        641
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   703 AA;  77435 MW;  EB2C6F045F720314 CRC64;
     MKLNIFASAI LLCTSAFPVA ASRLDKPYTE VYRPQYHFSP KENWMNDPNG LVYDTDEGIY
     HIYFQYNPGG TTWGAMSWGH ATSRDLMHWT EHPVALRARG FPDNITEMFF SGTVVVDESN
     TSGFGRKGKV PWVAIYTSYY PMEQVLPSGK RVRKDQQAQS IAYSLDKGMT WTTYDAANPV
     IAEPPAPYHD QHLEFRDPSV FWHVETSRWV AVVSLAKLHK ILIYTSQDLK QWDWVSEFGP
     ANAVGGVWEC PSIFPLTLDG SQQDKWVLML GLNPGGPPGT IGSGTQYIVG DFNGTTFTAD
     ADSIYDGSGP NDGMIFEDFE GDESLAARGW ATTGDFINAS PVRGTLSGQN AVTGFQGQQL
     FNTFLNGDAT TGAITSAPFD ITYKYINFLV GGGNDINETA IRLNVNGKTV HASTGSNDEH
     LTWQSWDVSS LKGQRAVIEI IDNASDGWGH INVDQICFSN TRATNQIANW LDWGPDFYAA
     LSFNGLDRDQ RTILAWMNNW QYGAAIPTDP WRSAMTVPRR LALKTIDGKP SLVQQPAGRW
     RTSGNHGREF SFRAVDGVRP LGRLGKALDI ELTFSSNMSP SNGLGEFGVS IAATKGYQYG
     TRVGYDFATQ QVFVDRSRSG DVSFDATFPG VYHAPLSNSA NGTISLRILL DWSSVEVFGA
     HGEATITSQI FPGPDAVYGQ LFSSGGQTRD VSLQVREIQS TWH