ID   EBDG_ARTBC              Reviewed;         882 AA.
AC   D4AUH1;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Exo-beta-D-glucosaminidase ARB_07888 {ECO:0000305};
DE            EC=3.2.1.165 {ECO:0000250|UniProtKB:Q4R1C4};
DE   Flags: Precursor;
GN   ORFNames=ARB_07888;
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).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- FUNCTION: Hydrolyzes chitosan and chitooligosaccharides with retention
CC       of anomeric configuration (By similarity).
CC       {ECO:0000250|UniProtKB:Q4R1C4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of chitosan or chitosan oligosaccharides to remove
CC         successive D-glucosamine residues from the non-reducing termini.;
CC         EC=3.2.1.165; Evidence={ECO:0000250|UniProtKB:Q4R1C4};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q4R1C4}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; ABSU01000011; EFE33136.1; -; Genomic_DNA.
DR   RefSeq; XP_003013776.1; XM_003013730.1.
DR   AlphaFoldDB; D4AUH1; -.
DR   SMR; D4AUH1; -.
DR   STRING; 663331.D4AUH1; -.
DR   EnsemblFungi; EFE33136; EFE33136; ARB_07888.
DR   GeneID; 9526967; -.
DR   KEGG; abe:ARB_07888; -.
DR   eggNOG; KOG2230; Eukaryota.
DR   HOGENOM; CLU_005015_2_4_1; -.
DR   OMA; VDWNPYP; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052761; F:exo-1,4-beta-D-glucosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR043534; EBDG/EBM.
DR   InterPro; IPR028829; Exo-b-D-glucosamin.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR041351; Ig_GlcNase.
DR   InterPro; IPR041447; Mannosidase_ig.
DR   PANTHER; PTHR43536; PTHR43536; 1.
DR   PANTHER; PTHR43536:SF1; PTHR43536:SF1; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF18368; Ig_GlcNase; 1.
DR   Pfam; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF49303; SSF49303; 3.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..31
FT                   /evidence="ECO:0000250|UniProtKB:Q4R1C4"
FT                   /id="PRO_0000434659"
FT   CHAIN           32..882
FT                   /note="Exo-beta-D-glucosaminidase ARB_07888"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434660"
FT   ACT_SITE        466
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q56F26"
FT   ACT_SITE        538
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q56F26"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        442
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        688
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        773
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        816
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   882 AA;  99868 MW;  6B4C4A147B1C9878 CRC64;
     MWFVFRPAAI PALLLTLGVS ALSPLRPLVS TAGQHEVIPG WYLQSERHVS SSIFSLSFPG
     ADVSSWYRMG PRGTVMAGLL ENGVYNETHL FFSDNFKSLP DADFRDVSWL YREEFTLQPG
     SGQHFTLHTH GISSRGDIYL NGHRVASKDV QAGSYAGYQY DVTKHVLKGG NCLLIKAYPT
     NYLRDLALGF VDWNPYPPDN GTGIWRHVEL SQSGPIRLSS PRVTTDFVPG VRVNDTNLTV
     KTDVHNIGQE TIRGSIKGFI EGAQNQRQPI SAPFTLKPGE QQTIEMNTTI QNPSVWWPAS
     WGDQPLYTAR ISAFVGKIKS DGPKRRKFGI RHIESRVNDQ DTVEFKVNGK PFFVMGAGYS
     SDIFLRFTVE RITTIFQYVL DMGMNTVRLE GKQEHPELYD IADKMGIMII SGWECCDHWE
     GWKYNTEGFG QPWTDVDYPI ANSSMLHEAR MMQTHPSILA FLIGSDYWPN DQATNIYVDA
     LRRMDWNAAI ISSAAKRGFP KLLGPSGMKM DGPYDWVPPS YWFGDRLGAA GAGGFGSELG
     SGVGTPEIRS LKKFLSEEDM KDLWTKPNKV LYHMSAGVSQ FRDRSIYNKA LYARYGKPNS
     LDDYSLKAQL MDYEATRSEY EAYAAYKSHS NPTTGLIYWM LNPAWPNLHW ALFDYYLKPM
     ASYFGTKTGA RIEHAIYDYR EQAVYLINHS NSRSGARSVT VDLINIDGKS LSHSTMKADT
     TPLMSQKLSK VSGLDKNRDV SFLRLILKDD AGKVLSRNVY WLPQREDVLD WGNSTWYHTP
     VTEYADLTPL SKLRKADVRV DINIQGRTKT RVSLQNKSNH PAFFIRLNLL DKASGDEVTP
     VFWEDNYVTL WPHERIELGV TYPQTHRVEL EVSGYNVEKK MV