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Database: UniProt
Entry: A0A1L7XU08_9HELO
LinkDB: A0A1L7XU08_9HELO
Original site: A0A1L7XU08_9HELO 
ID   A0A1L7XU08_9HELO        Unreviewed;      1013 AA.
AC   A0A1L7XU08;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PAC_18411 {ECO:0000313|EMBL:CZR68512.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR68512.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR68512.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR68512.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-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}.
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DR   EMBL; FJOG01000056; CZR68512.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000184330; 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:UP000184330};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184330};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24   1013       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012702043.
FT   DOMAIN      398    578       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1013 AA;  111075 MW;  B54476FDDBAE16BF CRC64;
     MRITNIFVSV VTAFICFFPS STAQILNGGL QEIVTWDSQS IYINGKRVMI LSGEFHPFRL
     PSPSLWLDVF QKIHSLGFNC VSFYINWAQI EGEPGQFRAD GIFALEGFFE SATAANIYLI
     ARPGPYINAE VSGGGFPGWL QPIDGVLRST NDSYLDAAKA YIANISSIIS KAQITNGGPV
     IMVQAENEYT YSNTLEVLEF LASQSPDLVA LKALSDVNLE PQYMADIEQA YLDAGIVVPL
     TVNDAVALGN WAPDTGLGAG DIYGMDAYPF PLSGNCPDPY YWAPGTLPAR TINYTLHLEQ
     SPSTPYSITE FQGGAPSTWG GTLEESCNVW IGPEFERLIY KEVFAQGAKY LNLYMDIQEA
     VNTSYDYGAA ITEERLVSRE KYSELKLQGN FRKVSPAYLL SSPQFMGAGI YTNNQDLFVT
     RVAGEESTTS FYVVRHTDYT SYNSTTYQLS IDTSIGNISI PQLGGNLTLN SRDSKIHVCD
     YDIGGINLIY SSAEIFTWTN SDNKTTLILY GAKGETHEFA FLAELGPPEL SSQCTGIQKQ
     TVSSLVVVQW DVVPSTCVVS FGNAVKVYLL WRNEAYNYWA LDAGINTSVI VKAGYLMRNA
     SITDNALYLN GDINATTTLE IIAAPLQCGQ VFFNGQLIIE DLNLTQQATL QFVPSIFTLP
     DFSSLDWKYI DSLPEIQTGY DDSNWTLCSQ NFSNMARPLT TATSLYAGDY EYYTGSLEYR
     GHFVANGNET IFQIVTQGGD GYGHSIWLND TFIGSWTGTG SDANHNGTYT IGSLVEGSRY
     VITVLIDHMG LEEESFVSDP TAAPQTQGSY YFAPFKTPRG ILDYSLDGHT SQTDVTWKMT
     GNLGGVHYQD LARGPMNEGS MFAERQGYHL PGAPTSTWES RSPLQGIDAA GVGFFATEFE
     LDVPSGYDVP MSFVFGNVTT GNGTAAFRCQ IFVNGYQFGK YVNNIGPQTV YPVPQGVLNH
     NGHNFVALTL WSLDGAGAAL TEFSLEPQAE IMTGYRLIEP APQPGWAQRT GAY
//
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