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Database: UniProt
Entry: A0A0G4PQ15_PENCA
LinkDB: A0A0G4PQ15_PENCA
Original site: A0A0G4PQ15_PENCA 
ID   A0A0G4PQ15_PENCA        Unreviewed;      1013 AA.
AC   A0A0G4PQ15;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   13-FEB-2019, entry version 18.
DE   SubName: Full=Glycoside hydrolase, family 35 {ECO:0000313|EMBL:CRL28517.1};
GN   ORFNames=PCAMFM013_S028g000070 {ECO:0000313|EMBL:CRL28517.1};
OS   Penicillium camemberti FM 013.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1429867 {ECO:0000313|EMBL:CRL28517.1, ECO:0000313|Proteomes:UP000053732};
RN   [1] {ECO:0000313|EMBL:CRL28517.1, ECO:0000313|Proteomes:UP000053732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM 013 {ECO:0000313|Proteomes:UP000053732};
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F.,
RA   Goarin A., Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T.,
RA   Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in
RT   cheese making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
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}.
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DR   EMBL; HG793161; CRL28517.1; -; Genomic_DNA.
DR   EnsemblFungi; CRL28517; CRL28517; PCAMFM013_S028g000070.
DR   Proteomes; UP000053732; 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:UP000053732};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:CRL28517.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053732};
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_5005195862.
FT   DOMAIN      402    583       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1013 AA;  111623 MW;  AE7565F238F5D923 CRC64;
     MARILSFLLV LLACLGASTK ADDQAVTQWP LHDNGINTIV QWDHYSFQVN GQRIFIFSGE
     FHYWRIPVPA LWRDILEKIK AAGFTAFAFY SSWAYHAPNN ATVDFSTGAR DITPIFELAK
     ELGLYIIVRP GPYVNAEANA GGFPLWLTTG EYGTLRNDDT RYTNAWTPYF TEVTEITSRY
     QVTDGHNSIV YQIENEYGNQ WLGDPSLRVP NETAIAYMDL LKANARKNGI TLPLTVNDPN
     MATHSWGKDW SDAGGNVDVS GLDSYPSCWT CDISQCTSTN GAYVPFQVLE YHDYFQESQP
     SMPAFMPEFQ GGSYNPWGGP EGGCPGDIGD DFANLFYRWN IGQRVTAMSL YMMFGGQNHG
     SMAAPVTATS YDYSAPISED RSIWSKYHET KLLALFTRSA KDLTMTELVG NGTQYTDNSA
     VRAYELRNPE TNAAFYATFH SNTSISTNEP FHLKINTSVG VLTVPKYAST IRLNGHQSKI
     IVTDFTFGSK TLLYSTAEVL TYTVFDKKPT LVLWVPTGES GEFSIKGVKK GSIKKCQGCS
     RVKFIKEHGG LTTSFTQSTG TTVLEFDDGV RVIVLDRTSA YDFWAPALTN DPFVPETESV
     LVHGPYLVRD AKLSGSELAI TGDIVNATTL DVFAPNGVKS LTWNGKKVHT HSTEYGSLKG
     SLDAPKSIKL PTFTSWKSKD SLPERFTDYN DSGVAWVDAN HMTTLNPRTP TSLPVLYADQ
     YGFHNGVRLW RGYFNGTATG AFINVQGGSA FGWSAWLNGE FIASYLGNAT ASQGNLTLSF
     TNATLHTNTP NVLLIVHDDT GHDQTTGALN PRGIMDANLL GSDSGFTHWR LAGTAGGESD
     LDPVRGVYNE DGLFAERVGW HLPGFDDSAW GEEESTKDST TSVLSFEGAT VRFFRTTIPL
     DIPAHTDVSI SFVLSTPASV TTKYRAQLFV NGYQYGRYNP YIGNQVVYPV PVGILDYTGE
     NTIGVAVWAQ SEEGASIGID WRVNYLADSS LDVASLDTKD LRPGWTEERV KYA
//
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