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Database: UniProt
Entry: A0A1F5LNX3_9EURO
LinkDB: A0A1F5LNX3_9EURO
Original site: A0A1F5LNX3_9EURO 
ID   A0A1F5LNX3_9EURO        Unreviewed;      1255 AA.
AC   A0A1F5LNX3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-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=PENARI_c005G11908 {ECO:0000313|EMBL:OGE54817.1};
OS   Penicillium arizonense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE54817.1, ECO:0000313|Proteomes:UP000177622};
RN   [1] {ECO:0000313|EMBL:OGE54817.1, ECO:0000313|Proteomes:UP000177622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE54817.1,
RC   ECO:0000313|Proteomes:UP000177622};
RX   PubMed=27739446; DOI=10.1038/srep35112;
RA   Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA   Workman M., Frisvad J.C.;
RT   "Penicillium arizonense, a new, genome sequenced fungal species,
RT   reveals a high chemical diversity in secreted metabolites.";
RL   Sci. Rep. 6:35112-35112(2016).
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:OGE54817.1}.
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DR   EMBL; LXJU01000005; OGE54817.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000177622; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:UP000177622};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000177622};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1255       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5009519747.
FT   TRANSMEM   1102   1124       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      396    576       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1255 AA;  135948 MW;  E1491144182D30E2 CRC64;
     MKLSSTWAIA CLAVQAAGAA ISHQLNGLTI TEHPDPVKRA LLQKYVTWDE KSIFVNGERI
     MLFSGEVHPF RLPVPSLWID VFQKVKALGF NCVSFYVDWN LLEGKPGQYS AEGIFALEPF
     FDAAKEAGIY LLARPGPYIN AEASGGGFPG WLQRVNGTLR TSDEAYLKST DNYIANVAAT
     IAKGQITEGG PIILYQPENE YSGACCGYNG FPDAVYMQYV EDQARNAGVV VPLISNDAWA
     GGHNAPSTGK GAVDIYGHDS YPLGFDCANP STWPSGNLPT GWYQTHMKQS PATPYSLVEF
     QGGAFDPWGG VGFTKCAALL NHEFERVFYK NNLSFRVAFL NLYMIFGGTN WGNLGHPGGY
     TSYDYGSPIT ESRNITREKY SELKLIGNFA KASPAYLLAT PGALTTSTYT TSSDIAVTPL
     LGGNSTASSF FVVRHNDYTS QASVDYKLKV TTSAGSVTIP QLGGSLTLSG RDSKIHVVDY
     DVAGTNILYS SAEVFTWNKV GKSKVLVLYG GPGEHHELAV TSTSKASVVE GSSSGITTKQ
     VGTAVVIGWD VSTTRRIVEV GDLKVLLLDR NSAYNYWVPQ VPASGTSPGY STQNAAASAV
     IVKAGYLVRT AYLKGSDLHL TADFNATTPI EVIGAPSTAK NLVINGKKAQ VKVDKNGIWS
     SSVAYSAPKI KLPTLKSLNW KAIDTLPEIQ NTYDDSKWVA ADHASTKNNV HALQTPTSLY
     SSDYGFHTGT LIYRGHFTAT GDEKTFFVQT QGGLAFGSSV WLNETHIGSW GGISINSNYN
     ATYTLPTLTK GKTYVFTVVV DNMGLNEDWT VGSEEMKLPR GIIDYNLSGQ PADAITWKLT
     GNLGGEDYID KVRGPLNEGG LYAERQGFHQ PSAPTKDWKS GSPFDGLSAP GIKFYSTSFD
     LDIEKGWDVP LYFNFGNSTA SPAAYRAQLY VNGYQYGKYV NNIGPQTSYP VPEGILNYRG
     SNYIALSLWA QEKDGAKVES LELVYTTPVS TALDEVEAAG QPNISPSKRP SAYTDSSTRS
     NYNTNLTSDS HKQSSKLNPY LEPKPKPIKS KQTKAMTFNS TLTTEPNDLT SHLLTSHQKR
     YTTISIPSTY GHLHDSPAAG TVVGIVLGSV AGFVLLMYVL FLAVNPGGIA RGASSGPAPT
     VSSSLSMDEE EIVDVRASRR PSRRRHSDNT IEVMEERETF RDSYRRRPSS RHDRIVVEES
     LATSTSGGGD VVEVLEEESS VPSDVSPRPA RRSRRGVSHV DPLAYGGGSQ YSRRS
//
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