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Database: UniProt
Entry: A0A150V5K0_9PEZI
LinkDB: A0A150V5K0_9PEZI
Original site: A0A150V5K0_9PEZI 
ID   A0A150V5K0_9PEZI        Unreviewed;       992 AA.
AC   A0A150V5K0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-FEB-2019, entry version 13.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:KYG45818.1};
GN   ORFNames=M433DRAFT_66443 {ECO:0000313|EMBL:KYG45818.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales;
OC   Capnodiales incertae sedis; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG45818.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG45818.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG45818.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z.,
RA   LaButti K., Lapidus A., Lipzen A., Chen C., Johnson J.,
RA   Lindquist E.A., Pan C., Hettich R.L., Grigoriev I.V., Singer S.W.,
RA   Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
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:KYG45818.1}.
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DR   EMBL; JPDO01000144; KYG45818.1; -; Genomic_DNA.
DR   EnsemblFungi; KYG45818; KYG45818; M433DRAFT_66443.
DR   Proteomes; UP000075602; 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:UP000075602};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:KYG45818.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    992       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007571419.
FT   DOMAIN      377    565       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   992 AA;  109183 MW;  9DD6BFB83D94C8A0 CRC64;
     MKWAQSIALL LATAVAVFAT NDGLTTAVTW DPYSLMINGE RVFIFSGEFH YERLPVPELW
     RDVLQKYKAN GLNAVSIYFF MSYHSPRRDV FDFETPGRDL QNLLDIAKEV GLFVIARPGP
     YCNAETNGGG LALWGSDGSM GDLRTSDETY YQSWLPWITN VGKILAQNQW PHGNVILDQI
     ENELQETDHS PTNTLVIYME QIENATRNAG VVIPFSSNEK GERSESWSTD YEDVGGAVNV
     YGLDSYPGGL SCTNINSGFN VVRNYYQWFQ NYSYTQPEFL PEFEAGWLEG WGTYWYGQCV
     EEHDPAFADV YYKNNIGQRV TLMNLYMAYG GTNWGNLAAP VVYTSYDYSA PLKETREIEA
     KFQQTKLIAL FTRVSQDLLE TYMESNGSGN AVSTDEIYSW VIQNPYNGAR FYTLQQTSTP
     SRSVVTFSAY FNTSLGTVTV PNVQLNGRQS KIATTDYHFG QYTLLYCSSD ILTWGDFDGS
     TVLVLYLDIG QAGEFAFKDV PSHLSYQTYG SSNVSSSSGT VNGTSSDTSS PFTKYTWTQT
     AGPTVVKFSN GVTVYLLDLD TAWTFFAPAT TSNPHILPDE QVFVLGPYLV RDVTVMGGTI
     ELQGDNANTT SLEVYAVHAD TVIWNGRRLA TKRTPYGSLI AYVTGANDVE VTLPTLSWVV
     ANSLPEAERD YDDSKWVICN NSTTLSPVSP LTLPVLFSSD YGYYSGVKLY RGYFDGTGAT
     SANITVQGGA AAGWSAYLNG KYVGSNTGNP SLWATSGVLD FSNATKYNTS NVLTVVTDYT
     GHDETSTGPM GVENPRGILG AYLYAGSNQI NFTQWKIQGN AGGPANIDPV RGCLNEDGIH
     GTRLGWHLPG FDPTGPAWST GSPLQGLNQS GINWYISHFK LDIDSDLDVP LGIELNAPAG
     TEASVQIYMN GYQYGKYIPQ IGPQTRFPIP PGIINNQGEN TLALSLWAQT DAGAKLSNVT
     LFAYNKFQTS FDFANIGGGL QPGWTPSRLQ YM
//
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