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Database: UniProt
Entry: A0A1V6NE22_9EURO
LinkDB: A0A1V6NE22_9EURO
Original site: A0A1V6NE22_9EURO 
ID   A0A1V6NE22_9EURO        Unreviewed;      1013 AA.
AC   A0A1V6NE22;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   13-FEB-2019, entry version 11.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQD62696.1};
GN   ORFNames=PENPOL_c011G01609 {ECO:0000313|EMBL:OQD62696.1};
OS   Penicillium polonicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60169 {ECO:0000313|EMBL:OQD62696.1, ECO:0000313|Proteomes:UP000191408};
RN   [1] {ECO:0000313|EMBL:OQD62696.1, ECO:0000313|Proteomes:UP000191408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 4502 {ECO:0000313|EMBL:OQD62696.1,
RC   ECO:0000313|Proteomes:UP000191408};
RA   Nielsen J.C., Nielsen J.;
RT   "Uncovering the secondary metabolism of Penicillium species provides
RT   insights into the evolution of 6-MSA pathways.";
RL   Submitted (AUG-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|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:OQD62696.1}.
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DR   EMBL; MDYM01000011; OQD62696.1; -; Genomic_DNA.
DR   Proteomes; UP000191408; 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:UP000191408};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191408};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1013       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5013139283.
FT   DOMAIN      402    583       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1013 AA;  111449 MW;  925143BC2A69A366 CRC64;
     MTRISNFLLV LLACLGASTK ADDQAVTQWP LHDNGISTIV QWDHYSFQVN GQRIFIFSGE
     FHYWRIPVPA LWRDILEKIK AAGFTAFAFY SSWAYHAPNN ATVDFSTGPR DITPIFELAK
     ELGLYIIVRP GPYVNAEANA GGFPLWLTTG EYGTLRNDDN RYTNAWTPYF TEVTEITSRY
     QVTDGHNSIV YQIENEYGNQ WLGDPSLRVP NETAIAYMDL LKANARKNGI TLPLTVNDPN
     MASHSWGKDW SDAGGNVDVA GLDSYPSCWT CDISQCTSTN GAYVPFQVLE YHDYFQESQP
     SMPAFMPEFQ GGSYNPWGGP EGGCPGDIGD DFANLFYRWN IGQRVTAMSL YMMFGGQNHG
     SMAAPVTATS YDYSAPISED RSIWSKYHET KLLALFTRSA KDLTMTELVG NGTQYTDNSA
     VRAYELRNPE TNAAFYATFH SNTSISTNEP FHLKVNTSVG VLTVPKYAST IRLNGHQSKI
     IVTDFAFGSK TLLYSTAEVL TYTVFDKKPT LVLWVPTGES GEFSIKGAKK GSIKKCQGCS
     RVKFIKEHGG LTTSFTQSTG TTVLEFDDGV RVIVLDRTSA YDFWAPALTN DPFVPETESV
     LVQGPYLVRD AKLSGSELAI TGDVVNATTL DVFAPNGVKS VTWNGKKVHT HSTEYGSLAG
     SLDAPKSIKL PTFTSWKSKD SLPERFTDYN DSGVAWVDAN HMTTLNPRTP TSLPVLYADQ
     YGFHNGVRLW RGYFNGTATG AFINVQGGSA FGWSAWLNGE FIASYLGNAT TPQGNLTLSF
     TNATLHTDTP NVLLIIHDDT GHDQTTGALN PRGIMDANLL GSDSGFTHWR LAGTAGGESD
     LDPVRGVYNE DGLFAERVGW HLPGFDDSAW GEEGSTKDST KSVLSFEGAT VRFFRTTIPL
     DIPAHTDVSI SFVLSTPAGV TTKYRAQLFV NGYQYGRYNP YIGNQVVYPV PVGILDYTGE
     NTIGVAVWAQ SEEGASIGID WRVNYLADSS LDVASLDTKD LRPGWTEERV KYA
//
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