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Database: UniProt
Entry: A0A084R2C0_STAC4
LinkDB: A0A084R2C0_STAC4
Original site: A0A084R2C0_STAC4 
ID   A0A084R2C0_STAC4        Unreviewed;      1020 AA.
AC   A0A084R2C0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   13-FEB-2019, entry version 20.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFA70355.1};
GN   ORFNames=S40285_01720 {ECO:0000313|EMBL:KFA70355.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Stachybotryaceae;
OC   Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA70355.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA70355.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA70355.1,
RC   ECO:0000313|Proteomes:UP000028524};
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}.
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DR   EMBL; KL659203; KFA70355.1; -; Genomic_DNA.
DR   EnsemblFungi; KFA70355; KFA70355; S40285_01720.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000028524; 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:UP000028524};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028524};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1020       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5001780112.
FT   DOMAIN      398    578       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1020 AA;  113717 MW;  F804268922D5C1E5 CRC64;
     MRAILGLAAL AASAGLVLGQ ETPAEWPVLD NGLNTVVQWD HYSYYVNGQR LFVFSGEFHP
     WRYPVPELWR DLLEKIKAGG FNAFSIYESW NYHSANPDHL DFENGAHDFT SILTLAKELG
     MYVIIRPGPY VNAEENAGGF PMWLTTGAYG ALRNDDERYT EAWTPYWEEI SRLIEPHLVT
     NGGNVIMFQI ENELNGQWSN IQQRILYPPT ANYMQALQDS ARDQGIDVPL SHNAPNMRGW
     SWSKDFSNAT GNVDVVGVDS YPSCWSCNLS ECTGTNGEYV PYQVVNYYDY FTAWAPRQPK
     FVPEFQGGSY NPWGGPRGGC PADIAEDFAN MFYRNLIFQR ITAISLYMLF GGTNWGWHAC
     PVVATSYDYS SPVSENRLLW DKFYETKLLT LFTRVAKDLA HTDRLGNDTT YTDNDAITTS
     ELRNPDTNGA FYVVMHAESS SGTRETFQLR VNTTQGELTI PRNGGDITIN GHQAKILVTD
     FSFGSKHLLY STAEVLSYAI IDGWETIALW LPEGEAGEFA IQGVESAEIL QGSAVDSFEA
     QSADGQITVS YVQRRGMTVL DLAGTRVLLL DREAAYHFWV PTLDNNPFAP PNSTVFVQGS
     YLVRSAVHNK EEHALYLTGD EEESSTLTVF APRGLCSIYW NDQRVTVESS GGGIYEIQVE
     GPAEFELPEL GPWTSVDSLP EIQEDYSPES IAWVVANNTE TTNPTKPADN NPVLYVDDYD
     IHVGNHIYRA TFPSTDEPPT GVLLDMIGGL AFGWSVWLNS EYIGSYHGWS WIGDAAATFS
     FENATLRDEG DNVLVILMDN SGHGLRELAI EPRGITEATL VGPSDEYKFS EWRIAGTAGR
     DENIDPMRGP LNEGGLYAER LGMHLPGYPD DDWEEASAAG ATLVVPSAGV RVFRTTAPLH
     VPSGLDVSIS FRLTSTNDDT FEPSDPTYSN RLRALLFVNG YQYGRFNPHI GHQIDYPVPP
     GILNYDGDNT IAVTVWSQDA QGVELKVEWM VNYVHTSSFD MLFDSAELRP GWTEDRLQYA
//
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