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Database: UniProt
Entry: A0A177D281_ALTAL
LinkDB: A0A177D281_ALTAL
Original site: A0A177D281_ALTAL 
ID   A0A177D281_ALTAL        Unreviewed;      1011 AA.
AC   A0A177D281;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CC77DRAFT_950910 {ECO:0000313|EMBL:OAG13488.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Alternaria; Alternaria alternata group.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG13488.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG13488.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG13488.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L.,
RA   Chaput D.L., Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; KV441510; OAG13488.1; -; Genomic_DNA.
DR   RefSeq; XP_018378909.1; XM_018535344.1.
DR   EnsemblFungi; OAG13488; OAG13488; CC77DRAFT_950910.
DR   GeneID; 29120938; -.
DR   KEGG; aalt:CC77DRAFT_950910; -.
DR   Proteomes; UP000077248; 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:UP000077248};
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:UP000077248};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5008058901.
FT   DOMAIN      394    572       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  110192 MW;  2938B362DE72B020 CRC64;
     MKSFLKLGGA VALGCFAVES AARAVGYSPK EFIKPYRREA LQDIVTWDED SLFVHGERIF
     LYSGEVHPYR LPVPDLYADL FQKIKALGYN GVSFYVDWAL LEGKPGVYRE EGVFDLQPFF
     DAAQEAGIYL LARPGPYINA EVSGGGFPGW IQRVNGTLRT RAPDFLEATD NYMKNVLAKI
     KPAQITEGGP IILIQPENEY TQATSAIKPF PDPVYMQYVE DQIRDAGIVV PLISNDASAK
     GNNAPGQPAA VDIYGHDGYP LGFDCANPTT WPDGNLPTNW HQLHEQQSPT TPYSIVEFQS
     GSFDPWGGPG FDKCGILVGA EFNRVFYKQL YSFGVTILNL YMTYGGTNWG NLGHPGGYTS
     YDYAAPIKED RQVDREKYSE LKLQANFLKV SPAYLTAARG NASNSTWTTS TDLSVTPATN
     EKTTFYFLRH SKYNSLESTT YKLHVTTSVF GNITVPQMNG TSLTLNGRDS KVHVSDYDIG
     GATLVYSTAE VFTWHKYDDK TVLVVYGGAG ETHELALDVT GLEVVEGDVA STTAKGTTIL
     NFKVDGTRKI AKVGADSPVY VYMLDRGEAF NYWAIDQAPH DSSNPVIVKA GYLMRTAKVT
     GDTIALVGDL NATTTVEVIG GASSEVSKMT FNGKDIDFTT SEQGTLSASI EFTKPDISIP
     KLSELEWKFV DSLPEIQPGY DDSEWTAADL KKTYNSLRPL TTPVSLYSSD YGYHTGTLLF
     RGTFTASGNE STFYLSTQGG SAFGSSAWIG DQFLGSWRGY DAAMNGNTTF TMPNLTKGKT
     YTITVVVDNQ GLDENWTIGT ETMKNPRGIL DYKLSGHDAS DIAWKLTGNL GGEDYRDISR
     GPLNEGGLYV ERQGLHLPGA LTATDAKWQA SAGPVADGIS APGIGFFATE FDLNMPSGYD
     IPLSFTFTNG TSSSNSSSGS SVPAYRVQLY VNGWQYGKYV SNVGPQVKFP VTEGILNYNG
     TNYLGVSLWG LDGGSTKVDG LELEVDAEIW SGMKSVATVM GSEYEKREGA Y
//
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