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Database: UniProt
Entry: A0A167ANS0_9PEZI
LinkDB: A0A167ANS0_9PEZI
Original site: A0A167ANS0_9PEZI 
ID   A0A167ANS0_9PEZI        Unreviewed;       987 AA.
AC   A0A167ANS0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 11.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CI238_08968 {ECO:0000313|EMBL:KZL80347.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL80347.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL80347.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL80347.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P.,
RA   Garrido Oter R., Ver Loren van Themaat E., Dallerey J.-F., Damm U.,
RA   Henrissat B., Lespinet O., Thon M., Kemen E., McHardy A.C.,
RA   Schulze-Lefert P., O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely
RT   related pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) 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|RuleBase:RU000675,
CC         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:KZL80347.1}.
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DR   EMBL; LFIW01001910; KZL80347.1; -; Genomic_DNA.
DR   EnsemblFungi; KZL80347; KZL80347; CI238_08968.
DR   Proteomes; UP000076584; 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; IPR019801; Glyco_hydro_35_CS.
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.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000076584};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:KZL80347.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    987       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007883748.
FT   DOMAIN      381    557       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   987 AA;  108895 MW;  82E0D39EFEA3FB03 CRC64;
     MRLFRALTAL ISLLVPGSLA SDNGLTDVVS WDKYSVVIND TRTYILSAEF HYQRLPVPEL
     WPDVLQKFKA NGFNTVSIYF FWSYHSASEG VYDFETGGKN IQRLFDYCKE AGLYVIARAG
     PYCNAETSGG GLALWGSDGR FGKLRSSDER YHAGWLPFIT QVGKIIAANQ ITNGGPVILN
     QVENEYQQTV YQADHTSVIY MEQLKKAFRD AGIVVPLTHN EKGLRSRISW STDYNNVGGA
     VDMYGLDNYP GALSCTDPKV GFNVNRGYYQ WLQNAAFTQP GYLAEFEGGW FSNWGSPTFY
     DECASEHDPA FADVYYKNNI GQRVTLLSIY MSYGGTNWGH SAAPQVYTSY DYSAPLRETR
     EQWTKLFQTK LIGLFTRVSS DLLKADMIGN GTGYSLSSTS AFSWVLRNPD TQAGFTIVQQ
     NSTNSMSPIQ FDVKLDTTAG SITVPNVALN GRQSKILVTD YVFGKHTILY ASADIATYGI
     FDREVLVFYL QEGQTGEFAF KNETDLTFEV FGDTDLKKTT NGDHGAFTWK QAAGSTVVKF
     SNGALVYLLE QKTAWRFWAP PTTSNPAVKP SEQLFVLGPY LVRSASISHG VLHISGDSDR
     ATILEAYVGD KPIETIDWNG KRLAATKTPY GSFTVQIPGA EGRAVTLPEL KNWRAAEALP
     EAAPDYDDFR WAVCNKTTTP NPYVPVTLPV LYSSDYGFYP GAKIYRGYFD GANATSVNIT
     ASGGLAFGWS AWINGQFLGG DVGSASATTT NKTLVFPRGA LRESNNVVTV VVDYHGHDQA
     STAQGINNPR GILGAQLQPG STRTNTGFKL WKLTGAAGGE ANIDPVRGPM NEGGLYPERL
     GWHLPGFAPT GPSWKPETPL DGLSRAGIRF YVTDFTLNID SDLDAPLGLE FSAPAGTIAR
     VMFWINGYQY GKFVPHIGPQ TRFPVPPGVL NNRGRNSLAV SLWAQTDAGA KLDGLKLVRY
     GQYQTDFKFN RDWSYLQPEW KDRQEYA
//
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