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Database: UniProt
Entry: A0A2H3IPK3_9EURO
LinkDB: A0A2H3IPK3_9EURO
Original site: A0A2H3IPK3_9EURO 
ID   A0A2H3IPK3_9EURO        Unreviewed;       988 AA.
AC   A0A2H3IPK3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   16-JAN-2019, entry version 6.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PENO1_057250 {ECO:0000313|EMBL:PCG98627.1};
OS   Penicillium occitanis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG98627.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCG98627.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCG98627.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A.,
RA   Gargouri A., Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant
RT   Pathogen Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
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:PCG98627.1}.
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DR   EMBL; NPFK01000157; PCG98627.1; -; Genomic_DNA.
DR   Proteomes; UP000218381; 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:UP000218381};
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:PCG98627.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    988       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5013642030.
FT   DOMAIN      379    553       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   988 AA;  108559 MW;  8D87A3668DFE84A2 CRC64;
     MLIPYSSIAC LATLVAGTVA NFDRTSSDVV IRQTPNSQLP LQKNVTWDSQ SLSVNGERMM
     IFSGEFHPFR LPSPSLWLDV FQKVKALGFN TVSFYVDWAL LEGKPGEFRA EGVFALEPFF
     EAATQAGIYL IARPGPYINA EVSGGGFPGW LQRLNVTLRS YNTSYLEATD NYVSHVAGSI
     AKAQITNGGP VILYQPENEY SGACCGALFP DPNYMQYVED QARKAGVTVP FINNDAWQGG
     HNAPGTGLGQ VDIYGFDNYP LGFDCGNPYT WPGSNGMAED FYSTHLRLSP NTPLSLDEKF
     QGGAFDPWGG SGFAGCASLL GPEFERVIYG GMNWGNLGHP GGYSSYDYGA AISESRNVTR
     EKYSELKLLG NFLKVSSSYL TASPESASSG IYTDTTDLTT IPVVGSTTAY FVVRHNNYTN
     QSSISYKLKL PTSTGNLTIP QTGGFLSLNG RDSKIHVVDY DVGGTNLLYS TAEIFTWKNF
     TSGKVLVLYG GPGEHHELAI SSTSTTSVLE GLARTETMGQ TTIVSWDVSS TRQIVLIGDM
     KILLLDRNSA YNYWAPECPT EGISPGLSSQ ETTASSIIVK ADYLVRTAYL QGDNLHLTAD
     FNATSTIEVI GVPKGARNLF VNSRKVPFKV DKHGFWVAEI PYVPPKIELM DFKALDWKYV
     DTLPELSPTY DDSAWRDADF PHSTNTFQPL NTSTSLFGSD YGFNTGYLLF RGHFTAEGTE
     TDFFIETQGG TAFGSSVWLN NTYLGSFAGN SIDENSNQTY ILPPLESGKH YTITVVIDQT
     GLMENWVIGL DDMKDPRGII SYQLFGRNDT AITWKVTGNL GGEDYVDKVR GPLNEGGLYC
     ERQGFHQPQP PSDSWEASSP FEGISKPGIA FYSARFDLDM PDGWDIPLYF QFGNKTSPPP
     KYRAMLFVNG YQFGKYINHI GPQTLFHVPQ GILNYQGTNW IAVTIWAQQA SGAKLDDFQL
     IKETPVMSAL TGIKSVEQPW YSARMGAY
//
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