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Database: UniProt
Entry: A0A1J9RQQ8_9PEZI
LinkDB: A0A1J9RQQ8_9PEZI
Original site: A0A1J9RQQ8_9PEZI 
ID   A0A1J9RQQ8_9PEZI        Unreviewed;       997 AA.
AC   A0A1J9RQQ8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-FEB-2019, entry version 9.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:OJD34859.1};
GN   ORFNames=BKCO1_2000097 {ECO:0000313|EMBL:OJD34859.1};
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:OJD34859.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD34859.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD34859.1,
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:OJD34859.1}.
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DR   EMBL; MNUE01000020; OJD34859.1; -; 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   ECO:0000313|EMBL:OJD34859.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183809};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    997       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012905027.
FT   DOMAIN      370    551       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   997 AA;  108071 MW;  3EE0399813409E64 CRC64;
     MRAVAILLFL LGAVISLASA QRDNGYTDVV QWDENSLFIN GERVYIYSGE FHYARLPVPE
     LWRDVIQNVY FFWSYHSPSK GVFDFESPGK DIQKLFDMAK EEGVYIIARP GPYCNAETSA
     GGYGLYLTDG SGGDIRTNDE TYHAQWLAWV DAVMPIIARN QITEGGPVIL VQVENELTES
     RHVADDPLVL YMEQLKQAFR DHGIVVPFTS NEKGMRGQSW SVDYQDVGGA VDIYGLDSYA
     GGLSCSNIDT GFTVLRTYYQ WFQNYSFTQP EYTPEFKAGW FQPWGGYFFD ECVSEHDTAY
     PDVFYKNNIA QRMTLQNMYM TYGGTNWGHL AAPVVYTSYD YGAPLRETRE VWDKFKHIKL
     ISLFTRVSDG LLNTRMESNG TGNAVNDTAI FTWVLRNPET EARFYFTQHD NSRSRANTAF
     SLDVATSAGA ITIPSLDLQG RQSRIVVTDY PVGDYTLLYS SAEVLTYGLF DVPVLVFYLN
     EGQVGELAFK GSDLQTANFT THGATTDFAA SAAGNGTSAA FKYTQTKGAT VVKFARGPVL
     YLLERWAAYT FFAPATTSDP HVAPDEQVFV LGPYLVRSAS ISGSTVSLSG DHLNATSIDV
     YAGGSDAASA VDTISWNGVA LATTRSAYGS LQASLPGIVD RAVPLPALAG WKVADGLPEA
     AAAYDDSRWA VANKTTTLSP VAPATLPVLY GSDYGFYAGA LIYRGHFDND DGGVTGANVT
     VQGGAAAGWS AWLNGALVGG HPGNASLVST SAVLDFAGAG GNATSSLAAE GNVLTVVTDY
     TGHDQDSQGP YGPLNPRGII AASLLGDGTA TNATAPSFKQ WKLQGNAGGG AGYVDPVRGP
     LNEGGLHGER LGWHLPGFDA SAWDDGDPRE GFGGAGIRWY TTEFELDVDE DLDAPIGLEL
     GMPEGTVARV QVFVNGYQYG KYLPHIGPQT KFPFPPGVLN NRGSNTLSLS VWAQSEDGAA
     FDKVELVLYG KYQSDFGFSR DWSDLQPGWS EDRLQYA
//
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