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Database: UniProt
Entry: A0A180H2V7_PUCT1
LinkDB: A0A180H2V7_PUCT1
Original site: A0A180H2V7_PUCT1 
ID   A0A180H2V7_PUCT1        Unreviewed;       629 AA.
AC   A0A180H2V7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   ORFNames=PTTG_09171 {ECO:0000313|EMBL:OAV99134.1};
OS   Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=630390 {ECO:0000313|EMBL:OAV99134.1};
RN   [1] {ECO:0000313|EMBL:OAV99134.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV99134.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OAV99134.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV99134.1};
RA   Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA   Young S., Zeng Q., Fellers J.;
RT   "Comparative analysis highlights variable genome content of wheat rusts and
RT   divergence of the mating loci.";
RL   Submitted (MAY-2016) 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         ECO:0000256|PIRNR:PIRNR001093};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285, ECO:0000256|PIRNR:PIRNR001093}.
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:OAV99134.1}.
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DR   EMBL; ADAS02000004; OAV99134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A180H2V7; -.
DR   STRING; 630390.A0A180H2V7; -.
DR   VEuPathDB; FungiDB:PTTG_09171; -.
DR   OrthoDB; 178991at2759; -.
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   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR029019; HEX_eukaryotic_N.
DR   PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF14845; Glycohydro_20b2; 1.
DR   PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 2.
DR   PRINTS; PR00738; GLHYDRLASE20.
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, ECO:0000256|PIRNR:PIRNR001093};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..629
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008110602"
FT   DOMAIN          18..193
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          243..576
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   REGION          198..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        402
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   629 AA;  69069 MW;  1DFF4C3822AE96EC CRC64;
     MMRLLLVLLA LLRPASALWP LPQHLEQQHT AVRLAANLSI HLPGDHPAPP DIHQAIAATL
     ALIRNDRHQP MAVDRGDALY HALAQPTHAH QLSLLTIHLA PPPALPTACP QQQPAAAADL
     LCAHPFTNAS YPPPAHAAPS ILAEMQQPLQ TRSEAYELTI HRPGQHAQEE YAAVLSASSA
     LGVLRGLQTF AQLVYTLTPP HPHDPSAPRK QQPLGGGAPG QPAGGAPIRF LYGPLLIKDR
     PAFPYRGLLL DTSRNFYSLA SIRKTIETMS WAKLNLLHWH IVDAQSWPLH LPAHPQLSRH
     GAYAAHQTYS LEDLKELARF ANARGVEILL EVDTPGHTAV VGEAYPDLVA CKDKTPWSNY
     AAEPPAGQLR IADERALALV NEIFATLTTQ VPGTLFSSGG DEVNKRCYEE DGPTQTRLRQ
     QNQTLSQALA SFVQATHATI RRAGKVPVVW EELVLDEAIP LPVDHTLVAV WRNSSMVEKV
     VQKGYSIIHG ASDYSYLDCG LGGWLGNSVN GTSWCDPYKT WQKIYSFDPY KNVAPAQHHQ
     VLGGQALLWS EQTDEQNMDA IIWPRALATA EVYWTGNTGR ARSVTEALPR MHDMRYRIVQ
     RGVRAAPLQP HWCAVRPGLC DLPAGTQEN
//
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