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Database: UniProt
Entry: A0A2B7XM86_9EURO
LinkDB: A0A2B7XM86_9EURO
Original site: A0A2B7XM86_9EURO 
ID   A0A2B7XM86_9EURO        Unreviewed;      1009 AA.
AC   A0A2B7XM86;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   16-JAN-2019, entry version 7.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=AJ80_07625 {ECO:0000313|EMBL:PGH09913.1};
OS   Polytolypa hystricis UAMH7299.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Polytolypa.
OX   NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH09913.1, ECO:0000313|Proteomes:UP000224634};
RN   [1] {ECO:0000313|EMBL:PGH09913.1, ECO:0000313|Proteomes:UP000224634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH09913.1,
RC   ECO:0000313|Proteomes:UP000224634};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from
RT   Ajellomycetaceae.";
RL   Submitted (OCT-2017) 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:PGH09913.1}.
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DR   EMBL; PDNA01000150; PGH09913.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000224634; 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:UP000224634};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224634};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1009       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012270618.
FT   DOMAIN      394    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1009 AA;  111119 MW;  ADB49F2C6A3CC4E5 CRC64;
     MKLCILILAC VVLQSAAASV VHRVRNLDVT DHHEPSKHKL LQDIVKWDNE SLFIHGERLM
     IFSGEVHPYR LPVPSLWLDI FQKIKALGFN CVSFYIDWAL LEGKPGEYSA EGIFALEPFF
     EAATTAGIYL LARPGPYINS EVSGGGFPGW LQRVKGVLRT SAPDYLAATD NYIAHIAATI
     AKAQITNGGP VIMYQPENEY SGACCGVTFP DPDYMQSVID QARDAGIVVP MISNDVYPSG
     HNAPGTGKGE LDIYGHDSYP LGFDCANPSV WPPGNLPTDW RALHLQLSPN TPYSLIEFQA
     GAFDPWGGPG FHKCAELVNH EFERVFYKNN IGFGVTILNL YMTFGGTNWG NLGHPGGYSS
     YDYGSPIAED RNITREKYSE LKLLGNFIKV SPSYINAVPG NLTNSEYTDT SALTVTPLIG
     RLSKSNYFVL RHSDYTSTSS TGYKLSLPTS QGKLTIPQLG GSLTLHGRDS KIHVTDYDVA
     GTNILYSTAE IFTWKQFAES KVLVVYGGMG ERHELAIVTE SKLSVAEGSS EDVNIESADG
     YTIINWDTSS ERRIVTAGDL YIFILDRNSA YDYWVPQLPK KGIHPGFSSA ENTASSIIVK
     AGYLVRAAYL RGSELHIAAD FNATTALEVI GAPKTAKGLY VNGDRVKYGV NEHGFWSASV
     KYDPPKFKIP ALEDLEWKSI DALPELQATY DDSPWTDADE TDSNNSLRAP TTPTSLYSSD
     YGYHTGYLLY RGHFVAKGVE KTLSISIQGG SAFASSVWLN QTYLGSWAGT DKSNDQTSTY
     KLPKLSTGKT YIFTVLIDNM GLDGNWVIGE ETMKNPRGIL DYELSGRDAE DITWKLTGNL
     GGEDYRDRAR GPLNEGGLYI ERQGWHQPQP PSDAWESANP ITDGISSAGV RFFTTKFDLH
     VPKGWDVPLY FTFSNMTSPP TPYRVQLYVN GFQYGKYVSN IGPQTSFPVP QGILNYNGAN
     WLGVTLWALD GEGAKIEGLN LEYRGAVMTA LKDIKLVDAP KFKKRKGAY
//
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