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Database: UniProt
Entry: A0A1F5LHI9_9EURO
LinkDB: A0A1F5LHI9_9EURO
Original site: A0A1F5LHI9_9EURO 
ID   A0A1F5LHI9_9EURO        Unreviewed;      1014 AA.
AC   A0A1F5LHI9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-FEB-2019, entry version 11.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGE52526.1};
GN   ORFNames=PENARI_c010G02136 {ECO:0000313|EMBL:OGE52526.1};
OS   Penicillium arizonense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE52526.1, ECO:0000313|Proteomes:UP000177622};
RN   [1] {ECO:0000313|EMBL:OGE52526.1, ECO:0000313|Proteomes:UP000177622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE52526.1,
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|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:OGE52526.1}.
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DR   EMBL; LXJU01000010; OGE52526.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000177622; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000177622};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000177622};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1014       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5009519602.
FT   DOMAIN      402    582       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1014 AA;  111031 MW;  8955B099C291EC15 CRC64;
     MARILNCLLL LLACLGTSIQ ANDQAVTQWP LQDDGLNTVV QWDHYSFQVN SQRIFIFSGE
     FHYWRIPVPD LWRDILEKIK AAGFTAFAFY SSWAYHAPNN ATIDFTTGAH DITPIFDLAK
     ELGLYIIVRP GPYVNAEASA GGFPLWLTTG EYGTLRNNDT RYTKAWTPYF TEMSQITSRY
     QVTDGHNSIV YQIENEYGNQ WESSASLRVP NETAIHYMEL LEANARANGI TVPLTANDPN
     MNSHSWGSDW SNEGGNVDVA GVDSYPSCWT CDLSQCTSTN GAYVPFQVMD YYSYFEESQP
     NMPGFMPEFQ GGSYNPWGGP EGGCPEDIGD DFANLFYRWN IGQRVTAMSL YMLFGGTNWG
     AIAAPVTASS YDYSAPISED RSIGSKYHET KLLALFTRSA RDLTMTDLVG NGTQYTDNAA
     VKAFELRNPE TNAGFYATFH TNTSISTNEA FHLKVNTSAG LLTIPKHASA LRLNGHQSKI
     IVTDFTFGPK KLLYSTAEVL TYAVFDKTPT LVLWVPTGES AEFSIKGAKS GSVKKCQGCS
     SVQFYKENGG LTAALTQGKG STILDIDGVR VVVLDRSSAY EFWAPALTDD PFVPETEAVL
     VQGPYLVRGA KLTGSKLAIT GDIVNATTLE VFAPKAVKSI TWNGKSIKAK STEYGSLKAS
     LDAPKSIKLP AFSSWKANDS LPERFADYDD SGVAWVDANH MTTLNPRTPT YLPVLYADQY
     GFHNGVRLWR GYFNGTATGA FINVQGGSAF GWSAWLNGAF LGSYLGDANT AQANLTLSFA
     NATLSTTTPN VLLIVHDDTG HDETTGALNP RGIFDASLLN STSGFTHWRL AGTAGGESNL
     DPVRGVWNED GLYGERVGWH LPGFDDSAWK TTSSSKSNSK GKSILSFEGA TVRFFRTTID
     LSLPSEHDIS ISFVLSTPAG TTNAYRAQLF VNGYQYGRYN PFIGNQVVYP VPVGILDYNG
     ENTIAIAVWA QSDEGASIGV EWRVDYLAES SLDVASFETG GLRPRWDKGR VKYA
//
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