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Database: UniProt
Entry: W3WG96_PESFW
LinkDB: W3WG96_PESFW
Original site: W3WG96_PESFW 
ID   W3WG96_PESFW            Unreviewed;       998 AA.
AC   W3WG96;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   16-JAN-2019, entry version 27.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PFICI_15325 {ECO:0000313|EMBL:ETS72933.1};
OS   Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Xylariomycetidae; Xylariales; Sporocadaceae;
OC   Pestalotiopsis.
OX   NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS72933.1, ECO:0000313|Proteomes:UP000030651};
RN   [1] {ECO:0000313|Proteomes:UP000030651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for
RT   synthesis of natural products.";
RL   BMC Genomics 16:28-28(2015).
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}.
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DR   EMBL; KI912125; ETS72933.1; -; Genomic_DNA.
DR   RefSeq; XP_007842097.1; XM_007843906.1.
DR   EnsemblFungi; ETS72933; ETS72933; PFICI_15325.
DR   GeneID; 19280338; -.
DR   KEGG; pfy:PFICI_15325; -.
DR   OMA; GGEDYVD; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000030651; 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:UP000030651};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    998       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004834620.
FT   DOMAIN      390    568       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   998 AA;  109358 MW;  42D040C6EE7BB656 CRC64;
     MYTRVFHLSF FIWSCLSFVA FTVGSFQQNL KVRPYARDPL QDVVTWDEHS IFVNGERVLF
     FSGEFHAFRL PVPSLWLDIL QKIRSLGFTG VSFYVDWALL EGKPGEYSAE GVFALEPLFE
     AASKAGIYLL ARPGPYINAE VSGGGYPGWL QRVEGYLRTN ATDYLATTEN YMTSVLKSIS
     NAQITNGGPV ILVQPENEYS QAVSGIPFPN ADYMEYVEDQ FRKNGIVVPL ISNDASPYGH
     NAPGQPAPVD IYGHDGYPLG FDCSNPSRWT SFNTNFRTLH LEQSPSTPYS IVEFQGGAFD
     PWGGVGFDKC LSLVNYEFER VYYKNNYGFG VTIYNLYMIF GGSNWGNLGH PGGYTSYDYG
     ATIAEDRSVA REKYSEMKLQ ANFLVASPAY LTVTPGTPST TQYTTSSDVY VTPLKSNETQ
     FYVVRHSLFN STEATTYKLR LDGSSSGNIT VPQLGGSLTL NGRDSKIHVS DYDLGGTTLL
     YSTAEIFTWQ KYGNGTVLVV YGGPGEQHEL AVSQIGISSS EINASLDVLV NSTETSVIVN
     WLTSATAQYV TIGDLQVYIV DRNTAYNFWV IPSGNSLYTN TEDVNIVAKS GYLLRTANVT
     ETSLDITGDL NATSPLWIVG GAPKNLKTLT FNGQEVEFSV DENGAISSNL TYIAPEFAVP
     TLKDLQWYYI DSLPEIQGDY DDDAWTLASF ATTNNTSRAL TTPTSLYASD YGYHAGSLIY
     RGKFTAKGNE TTFKVETQGG TAYGASIFLD SSFLGSTVGN KSAASANATF ALPQLGADEV
     HTFTILIDHM GLDEEWTVGS NTMRSPRGVL NYDLAGHDQS DVTWKLTGNL GGEDYVDHVR
     GPLNEGALYA ERQGYHLPSP PVETWTKGLS PIDGISSAGV GFFTTSVDLD FPSGYDIPLS
     IRLPAINFTS TIRVQLYVNG WQFGKYVSNI GPQTQYPVPE GIWNYNGQNW LAVSLWALEA
     AGGSIASIEL VASEAVQSGR EQVQVVESPA WSQRAEAY
//
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