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Database: UniProt
Entry: A0A1G4AQ33_9PEZI
LinkDB: A0A1G4AQ33_9PEZI
Original site: A0A1G4AQ33_9PEZI 
ID   A0A1G4AQ33_9PEZI        Unreviewed;      1026 AA.
AC   A0A1G4AQ33;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   16-JAN-2019, entry version 8.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CORC01_13482 {ECO:0000313|EMBL:OHE91205.1};
OS   Colletotrichum orchidophilum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHE91205.1, ECO:0000313|Proteomes:UP000176998};
RN   [1] {ECO:0000313|EMBL:OHE91205.1, ECO:0000313|Proteomes:UP000176998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 309357 {ECO:0000313|EMBL:OHE91205.1,
RC   ECO:0000313|Proteomes:UP000176998};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675,
CC         ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OHE91205.1}.
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DR   EMBL; MJBS01000195; OHE91205.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000176998; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000176998};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:OHE91205.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176998}.
FT   DOMAIN      420    596       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1026 AA;  112557 MW;  EF1816D048ACB75E CRC64;
     MLTIVYEPAC SRSVRSRADL ERNAALPGSA PPTRGTAIMR FYQALTALIW LFASGALATD
     NGLTDVVSWD KYSLVINDTR TYILSAEFHY QRTPVPELWP DILQKFKANG FNTVSIYFFW
     SYHSAAEGVY DFETAGKNIQ RLFDYCKEAG LYVIARAGPY CNVQAETNGG GLALWGSDGR
     FGKIRTSDAR YQAGWLPFIT QVGKIIAANQ ITNGGPVILN QVENEYQESV YSPDNTAVIY
     MEQLKKAFHD AGIVVPLTHN EKGMRSRSWS TDYNNVGGAV NVYGLDSYPG ALFCTDPAVG
     FNVVRTYFQW FSNYSFTQPS YLAEFEGGWF SNWGSPTFYD QCASEHDPAF ADVYYKNNIG
     QRVTLLSLYM SYGGTNWGHS AAPQVYTSYD YSAPLRETRE QWTKLFQTKL IGLFTRVSSD
     LLKVEMVGNG TGYGLSSASA FSWVLRNPDT QAGFTVVQQA STKSMTPIQF DVTLNTTAGP
     VTVPNVVLNG RQSKILVTDY VFGKHTLLYA SADIATYGLF DTEVLVFYLQ EGQTGEFAFK
     DAGNLTFEVF GDTDLQETTN GNHSAFTWKQ VAGSTVVKFS NGALIYLLEQ KSAWHFWAPP
     TTPNPTVKPN EQLFIQGPYL VRSASISHGV LHVSGDSDKA TAIEAYVGDE AIETIDWNGQ
     RLAATKTPYG SFTAQIPGAE DRVVTLPELS NWRAADGLPE AAPDFDDSRW TVCNKTTTPS
     PYAPITLPVL YSSDYGFYSG AKVYRGYFDG ANATSVNITA SGGLAFGWSA WVNGQFLGGD
     VGSASATTTN KTLTFPRSAL RESNNVVTVV VDYHGHDQAS TAQGINNPRG ILGAQLQPGS
     TRTNTGFKLW KLAGAAGGEA NIDPVRGPMN EGGLYPERLG WHLPGFAPTG SSWKPESPLV
     GLSGAGIRFY VTDFTLNIDS DLDAPLGIEF SAPAGTTARV LFWINGYQYG KYVPHIGPQT
     RFPVPPGVLN NRGRNILAVS LWAQTDAGAK LDGLKLVQYG QYQTDFKFSR DWSYLQPGWE
     DRQEYA
//
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