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Database: UniProt
Entry: A0A1L7X8M2_9HELO
LinkDB: A0A1L7X8M2_9HELO
Original site: A0A1L7X8M2_9HELO 
ID   A0A1L7X8M2_9HELO        Unreviewed;       984 AA.
AC   A0A1L7X8M2;
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_11284 {ECO:0000313|EMBL:CZR61388.1};
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:CZR61388.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR61388.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR61388.1,
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; FJOG01000018; CZR61388.1; -; 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     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    984       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012114840.
FT   DOMAIN      365    544       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   984 AA;  107548 MW;  02312426B5C96B36 CRC64;
     MLLFLLVLAL VTWDQHSLIV RGERVMIYSG EFHPFRLPSP GLWLDVFQKI KAMGFTGVSF
     YTDWGLLEGN PGEVVTDGVW SLDQFFSAAS EAGIYLIARP GPYINAETAA GGMPGWALRL
     NGTLRSTAPD YLNATVNYLS IIGKIIADAQ ITNGGPVIMV QPENEYSTWP GESFTQFPEQ
     FNRQLMAFTE DRLRDAGIVV PFAVNDNENK GYFAAGSGLG AVDIYGIDAY PFRYDCAHPY
     VWPTYRFPTG WQTNHTAFSP STPFTIMEFE GGSGDGWGGV GEDMCAILVN NEGIRVLFKN
     NYSFGVTIFN TYMIYGGTNW GNLGYHGGYT SYDYGASITE DRQIWREKYS EMKLQANFFK
     VSPAYLTATA GNVGNGSFVS TPAIAVTPLW GNGMKTNFYV ARHADFTCTG NASYSLTVST
     SIGNVTIPQL SGTLSMIGRD SKIHVTDYDV GGINLIYSTA DIYTWIKTSG SGRVLILYGG
     LNETHEFAIP ISVGKPKLSS GCAATVTKIG SSWVINWEVT AARQVVTIGD LTVYLLWRNE
     AYDIWPLELP AAVPISNYSS ISKSMVIIKA GNLLRSVSID GHNLHLTGDV NCTTTLEVIA
     APSDSLTSIT FNSNPLHTTK SSSGNLVATV GFEPPKTTLP DFSTSSCEWK YHDSLPELSP
     MYDDSLWINC SHTTTTNPWG KRTPTSLYAS DYGFHTGSLI YRGHFTSNGK ESNFLVNITG
     GVGFGYSVWL NSTFLGSWAG SGANQTWAQN FTLPSLQLRE KYVFTILIDH MGQDEEAPGT
     DAIKYPRGLT YFALSGHSNL ADAQWKITGN LGGEQYPDLA RGPRNEGAMY AERMGWHLPS
     PPTQGWENRS PVTDGVDGAG VGFFTTSFEL NMPDGWDVPL SFVFNGTRSG GEGTEGNYRV
     QLFVNGWQFG KYVNNLGPQT AFPVPEGILN YNGRNDVSLT LWSLDADGAK VGGFALVPQA
     IIKSGYSKPS LVESPKWTER KNAF
//
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