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Database: UniProt
Entry: A0A0G2F2C0_9EURO
LinkDB: A0A0G2F2C0_9EURO
Original site: A0A0G2F2C0_9EURO 
ID   A0A0G2F2C0_9EURO        Unreviewed;      1181 AA.
AC   A0A0G2F2C0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-FEB-2019, entry version 20.
DE   SubName: Full=Putative beta-galactosidase b {ECO:0000313|EMBL:KKY28421.1};
GN   ORFNames=UCRPC4_g00588 {ECO:0000313|EMBL:KKY28421.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae;
OC   Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY28421.1};
RN   [1] {ECO:0000313|EMBL:KKY28421.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY28421.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell
RT   wall degradation and secondary metabolism in the genomes of grapevine
RT   trunk pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY28421.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY28421.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) 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:KKY28421.1}.
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DR   EMBL; LCWF01000013; KKY28421.1; -; Genomic_DNA.
DR   EnsemblFungi; KKY28421; KKY28421; UCRPC4_g00588.
DR   OrthoDB; 179316at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     20     40       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      561    742       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1181 AA;  130321 MW;  646D320653B4F078 CRC64;
     MRFWKLAAER VRDTVFETGF NFSVCVIVIT YLDTLVKYLL HLVSSALQPK REGLFTYNAK
     SAFAVVHKVK ELSTLCAWLD GPFLYFMDAP NQEQSRLDSA FSPVTPGSAV MTCLRFVPLV
     QFNDIMSIDY FGQSVIAFYR LHRNMCIQND PQILRMVTTW KWACCALIAW LSTTAPVTNA
     QNSSAAQWPL HDDGYSDVVQ WDHFSFEVNG KRAFLFAGEM HYWRVPVPEL WGDILQKIKA
     AGCNAFTFYA HWGYHAPNPN TLDFSNGAHN YTRLLELAKE IGLYVFVRTG PYINAEANAG
     GFPLWLTTGA YGTLRNNDTR YTAAWEPYQS ESARLTVPHQ ITEGGNALAN QIENEYGYQW
     TDATAKTPNY TGIAYMELLE QNARSNGITI PLYHNNPNLN SKSWSKDYGA GVGGDVDVYG
     VDSYPACWSC NLAECTSTNG AYVAFQVVKY YDHFQSVAPS QPEFMPEFQG GSYNPWGGPQ
     GGCRNNSDET FANLYYRHNI AERVTAMSLY MFYGGTSWGW FAAPVVATSY DYSAPISEDR
     SIGSKYYETK NLALFTRVAE DLRMTNRLGN STSYTTNSAI LKTELKNPET NAGFYVTAHA
     NSSSDTVESF KLHVSTTLGN LTIPQKATSI VLNGHQSKII VTDFIVGSRS ILYSTAEVLT
     YSIFDGQPTL VLWVPTDESG EFLVEGAKTG SVSTCGGCSN IRFYPEDSGL VVTFTQQAGS
     TVLLIDNELR VVILDRTYAY PFFAPTLSND PLISANETVL VQGPYLVRGA EIEGSVIKIT
     GDSNSATQIE VFAPNSVKSI SWNGKALSTT QTHYGSLTSK IPGPSNFSVP QLGPWKVHDS
     LPEQFANYSD SGPAWVNANR TTTSSVYKPA TYPVLYIDEY GFHNGIHLWR GYFNGSASGV
     FLNVQGGTAF GWSAYLNGNF IGSFLGSSSL EVGNLTLSFS NATINHLGEN ILLVIQDDSG
     HDETTGALNP RGITNATLIS RNYSTTFTKW KVAGTAGGDT YSHTLDPIRS PINEGGLTAE
     RLGWHLPSFD DSSWTASSPS TGFTSATVKF YRTTFPSIDI PTGHDVSLSF RLTTPSSGPL
     SFRALLFVNG YQYGRFNPYI GNQIDFPVPP GILSYASSDD YHDDDEQGNT VGLAVWAQST
     EGAKINVELN AEYVLESGYE FNFGDTRVLR PGWTEERLKY A
//
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