ID   CRH12_ARTBC             Reviewed;         365 AA.
AC   D4B4J2;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 2.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Probable extracellular glycosidase ARB_03382 {ECO:0000305};
DE            EC=3.2.-.- {ECO:0000305};
DE   AltName: Full=Allergen Asp f 9 homolog {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_03382;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: Extracellular glycosidase which plays an important role in
CC       fungal pathogenesis. Involved in cell wall assembly and regeneration,
CC       filamentation, and adherence to host cells.
CC       {ECO:0000250|UniProtKB:Q5AFA2}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALLERGEN: May cause an allergic reaction in human. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. CRH1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE30040.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000034; EFE30040.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003010680.1; XM_003010634.1.
DR   AlphaFoldDB; D4B4J2; -.
DR   SMR; D4B4J2; -.
DR   STRING; 663331.D4B4J2; -.
DR   EnsemblFungi; EFE30040; EFE30040; ARB_03382.
DR   GeneID; 9524793; -.
DR   KEGG; abe:ARB_03382; -.
DR   eggNOG; ENOG502QVQI; Eukaryota.
DR   HOGENOM; CLU_027506_1_1_1; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Allergen; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..365
FT                   /note="Probable extracellular glycosidase ARB_03382"
FT                   /id="PRO_0000434919"
FT   TOPO_DOM        26..302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..365
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          50..243
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        125
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P27051"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P27051"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   365 AA;  40761 MW;  8F74E6B1CC0A52C8 CRC64;
     MMASRRISVL SSLGLFACLL SPVVAQTFTY CNPLEKDDCP NAPALGQNYT TYLNSSLNPD
     VWNATSGLVE ISDAGSNFTI HKALDSPTIQ SFFYIFFGTV EVHMKAATGR GVVSSIVIQS
     EVLDEIDWEW VGSEPDKVQT NYFGKGNTTS YDRGKTFDIK GAMDDFHNYT VNWTPEKIEW
     YIDTVLVRTL KYEEALGGKN FPQTPSTVRL GIWPGGDPQN KKGVIEWAGG EIDYEKTPYI
     MSVKELKVVD AHKGKEYSYS DRSGDWQSIK VIDGVSDIAN EINKPPPKSL AQRWRELPTA
     AKIAIFASIG GLVILGMAII AFCCVKQRRA GRREFSMENS KFVEDQNNVM AMRTQWNHKY
     KPVGS