ID A0A167DEE0_9PEZI Unreviewed; 726 AA.
AC A0A167DEE0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=CI238_11237 {ECO:0000313|EMBL:KZL83763.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL83763.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL83763.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL83763.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001231};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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:KZL83763.1}.
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DR EMBL; LFIW01001067; KZL83763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167DEE0; -.
DR STRING; 1573173.A0A167DEE0; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06564; GH20_DspB_LnbB-like; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR PANTHER; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KZL83763.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..726
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007885134"
FT DOMAIN 68..148
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 189..513
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
SQ SEQUENCE 726 AA; 78672 MW; 19DC885F88B7D2C4 CRC64;
MRFTLLPISL VLTAAANSLP GLPTVPYTTT GGTLLSTSLT QIIVSSEFAG SVDEAGQTLI
PPTLHSFATT FASDLGSVLS LDIPIKLGAA AEQGSIFLTL GDAELYKDAA GRESSEGYSL
NVTIDGVLIT GASPLGVWWG TRTLLQQLIL GDGELKLGYG TDSPGFPIRG MMPGAGALSS
APDPALVPLD VARHYYPPEF LVEMCAYMSF FKQNTFQLHL SDNLYNNVAI YSRERSLSLY
AAFRLLSDDP SLEGLNKRAN ESYTREVFDD IQTKCAARGV TVLPEIEAPG HALVISQWKP
ELGLESDLSL LNISNPETIP TIKKIWDIFL PWFHTKTVSI GADEYVDPTL SEEALVGEYT
RFVDEMNEYI TSKSGKHVRI WGTFAPSVGG TVNKSVSIQH WANFEANPLY DFVNNGYDVL
NSGEYIYTVG KWSQWYPFEL SLEFIFHGSP DGSAFAPNIF DRENGTNNAA KDSPSLLGHI
APQWNDYGPN ATTVTEGYYQ WRDGLPALAD KQWGGEVAEA DYQGLFSALQ PFAPGQNLDR
RIASRGPTIV EYDFRQRRGS NVTAVEDLSG NKYHATSTCA TSEEGAILTP VCRITTPLVQ
KGRNYTLSFS IKPTSNAKGA IFSGGDSGLW FGNGTVDAVM LFSGESTYAL NYTFPVGSWT
NASLIGRGRQ TFLDVGDGEP MEFLTVLGWN GDRFVWAPIA VEAPLETVGG SGFQGVIGGM
KLVGDA
//
