GenomeNet

Database: UniProt
Entry: A0A084R4U2_STACH
LinkDB: A0A084R4U2_STACH
Original site: A0A084R4U2_STACH 
ID   A0A084R4U2_STACH        Unreviewed;      1024 AA.
AC   A0A084R4U2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   13-FEB-2019, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFA71227.1};
GN   ORFNames=S40288_03862 {ECO:0000313|EMBL:KFA71227.1};
OS   Stachybotrys chartarum IBT 40288.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Stachybotryaceae;
OC   Stachybotrys.
OX   NCBI_TaxID=1283842 {ECO:0000313|EMBL:KFA71227.1, ECO:0000313|Proteomes:UP000028540};
RN   [1] {ECO:0000313|EMBL:KFA71227.1, ECO:0000313|Proteomes:UP000028540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40288 {ECO:0000313|EMBL:KFA71227.1,
RC   ECO:0000313|Proteomes:UP000028540};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene
RT   clusters in the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; KL658015; KFA71227.1; -; Genomic_DNA.
DR   EnsemblFungi; KFA71227; KFA71227; S40288_03862.
DR   Proteomes; UP000028540; 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:UP000028540};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028540};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1024       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5001780104.
FT   DOMAIN      410    586       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1024 AA;  113745 MW;  33285596B489F506 CRC64;
     MKLSIVFGAV LTLASSDAFR IPRGITEQLL GDRQKRDLLQ DIVTWDAYSL FIHGERGMMF
     SGEVHPFRQP VPSLHLDIFQ KIKALGFNMV SYYVDWALLE GKPGEFRADG IFDFQAFFDA
     ATEAGIYLLA RPGPYINAEV SGGGFPGWLQ RVPALLRTRD PEYLAATENY VANIGAITAR
     AQITNGGPVI LLQVLDLMTM LYRLCKLTSL LPENEYSAAP DIDPFPDTVY FQYLIDQYRN
     ASIVVPTINN DVWPGGNNRP GIGEGEVDIY GHDSYPLGFD CANPDVWGED ALTTTWYQDH
     MRNSPNTPYA IPEFQGGAFD PFGGWGFEQC SELVNHEFER VFYKNNFANG LRIFNIYMTY
     GGTNWGNLGH SGGYTSYDYA ASIREDRRVD REKYSELKLE AQFMKVSPGY LLTIPQTPTT
     GIHSANEEIT ITPLLSNSTG HFFVIRHTDY QNTGSADYTV MLPTSAGDIV IPQLGGQLSL
     HRRDSKFHVT DYPVGDFTLL YSTAEIFTWK AFEDKTVIVV YGGPEELHEF AVKGDFEAEV
     LEGEDVITEV MDDATVIQYT TSPSRSVVKV GDLVVYLLDR NSAYNYWVPD LPGDGQNPAY
     GTSLMNPKSI IVNGGYLVRS VSVEDSSLKL QADFNRTTSL EVIGVPGGIS TLILNGEDLA
     YTISDLGNWI SQPDIELPEI ALPDLSSLDW HYIDSLPEIR SDYDDSGWTV ADHPTTNNTV
     APLRTPVSLY GSDYGYHTGT LIFRGHFTAH GTEEELRLWS QGGSASASAL WLDDEFLGSF
     KGFDYARGSN STYALPTLTR GKRYVLTIVV DNNGIHTNWT PGFDEMKEPR GIIDYAIVSP
     SGCRTRISTW KITGNLGGED YIDKFRGPLN EGGLFFERQG YHQGSPPLDE FSIGNPYEGI
     DHAGVAYYTA KLTLDLPSDK YDIPLSFVFE NTTDSSDYRA LLYVNGFQFG KYLSNIGPQD
     EYPVPEGILN YNGDNWLGLS IWALEDGGAK VPNFAVKAGT AILTGRQPVV LVEGPNYSRR
     QDAY
//
DBGET integrated database retrieval system