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Database: UniProt
Entry: A0A1J9RKI8_9PEZI
LinkDB: A0A1J9RKI8_9PEZI
Original site: A0A1J9RKI8_9PEZI 
ID   A0A1J9RKI8_9PEZI        Unreviewed;      1034 AA.
AC   A0A1J9RKI8;
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=Beta-galactosidase b {ECO:0000313|EMBL:OJD29039.1};
GN   ORFNames=BKCO1_9600016 {ECO:0000313|EMBL:OJD29039.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetes incertae sedis; Botryosphaeriales;
OC   Botryosphaeriaceae; Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD29039.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD29039.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD29039.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible
RT   with a hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-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:OJD29039.1}.
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DR   EMBL; MNUE01000096; OJD29039.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000183809; 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:UP000183809};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183809};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1034       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012317760.
FT   DOMAIN      395    574       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1034 AA;  111177 MW;  DA7FA903ED2B91EF CRC64;
     MLRLRHLLAL SSALLPLAAT AQEWPVQDSG YTDAVQWDHY SFIVNGKRVY LFGGEMHPFR
     LPVPELWQDI VQKTKALGFN TFSFYTNWFF HNPHPNQTDF ETAAHDISRL LEYAKDAGLF
     VAVRPGPYVN AELNAGGFPL WVTTGAYGEL RDDNATYEAA WTPYQDGIAK VVAPYQIHKN
     GTVISYQLEN EYGEQWLDSA TKTPNQPAIN YMEELNANAR RNGIEVPTTH NSPNLQDFSW
     SKDQDTVGAG GNVNVLGLDN YPLCWSCDQS ECTGVSNDYN LVEYYSWFQN NTPHQPSLMP
     EFQGGRYNPL DGDAGQCLEP MGPEFRNLFY RHNIDQKVTA QILYTLFGGT NWGWMAAPFI
     GTSYDYAAPI AEDRSLRDSW YETKSLALFT RVAEDLREAD RVGNSTAYTT NDEVTATELR
     NKATGGAFYI ARHADSVTGK PVSFKLHVDT SIGSLTIPQK AAEIELNARE AKIVPTDFRF
     SGQKLLYSTA EVFTYVELDG KPTVALWVPG GEGGEFLLEG AANMSAKAVP ADAVSFHQSQ
     HGLIVSFANQ TGTTVVDTDK ARFVILDRTD AWKTFAPVLT PDPHAPVNET ILVQGPHLVR
     TAAISGDTLI LTGDTSSDTT LDVFAPAAVK TVTWNGEPLS TTPTAHGSLS ASLPGPLAVT
     LPPLSNLTWR SAPSLPEIAP NYTLSPAVWK PANATTTPSQ YTSATTPYLY IDALGFHVGH
     HLYRATFAGS PALTGLFLAL QGGTGFGWSA YLNGRFLHAE PGSSPAALEA TNATIPFPAN
     SSALLPGTDN VLVVLMDNSG HEQRAEALEV RGITNATLLS SSSSSAPAAF SSWHVAGTAA
     SADATTTLLD PVRGPYNEGG LHGERAGWHL PGFDDSAWSI ASPTSGSSSG AVLRAGGGST
     TAESDVTFHR ATVAALDIPR AHDGTVHFSL GVPEGGSEDV RALLFVNGYQ FGRYRPGVST
     ATDFPVPPGV LDFSAGGENT LVVAVWAVGG REVGVEIGWR VEGVVRGGLG VGFESGGEGG
     YLRPGWGVER GVFA
//
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