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Database: UniProt
Entry: A0A177D0L3_9PLEO
LinkDB: A0A177D0L3_9PLEO
Original site: A0A177D0L3_9PLEO 
ID   A0A177D0L3_9PLEO        Unreviewed;      1003 AA.
AC   A0A177D0L3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CC84DRAFT_1227943 {ECO:0000313|EMBL:OAG13056.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Massarineae;
OC   Didymosphaeriaceae; Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG13056.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG13056.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG13056.1,
RC   ECO:0000313|Proteomes:UP000077069};
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; KV441548; OAG13056.1; -; Genomic_DNA.
DR   RefSeq; XP_018043421.1; XM_018183626.1.
DR   EnsemblFungi; OAG13056; OAG13056; CC84DRAFT_1227943.
DR   GeneID; 28767112; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000077069; 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:UP000077069};
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:UP000077069};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25   1003       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5008058837.
FT   DOMAIN      394    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1003 AA;  108799 MW;  DD3EA3D790A70680 CRC64;
     MKHFLNGVSA AALACLTIAA NARAVGYRSP TDFIVPYKRQ ALQDIVTWDK DTIFINGERL
     FLYSGEVHPY RLPVPDLYID IFQKIKALGY NGVSFYVDWA LLEGKPGEYR EEGVFDLKPF
     FDAASEAGIY LIARPGPYIN AEVSGGGYPG WIQRVKGILR TRAEDYLNAT DNYMANVGKT
     LAAAQITNGG PIILVQPENE YTNSKEKPFP DGYYMQYVED QIRNAGVVVP LISNDANNGG
     HNVPGSGEGA VDIYGHDGYP LGFDCSNPEV WGDQQLVTDW YSVHLQQSPN TPYSIMEFQG
     GSYDPWGGPG FDKCLQLVNA AFERVFYKNI YTFGVTIFNI YMTFGGTNWG NLGHPGGYTS
     YDYAAPIAED RQVNREKYSE QKLQANFFKV SPAYLTASRG ARSTTQWTNN PAITVTDATN
     NSTKFYFVRH TTYNTLDSAT YKLTIPTSAF GNTTIPQYNG TSLTLNGRDS KIHVSDYDMG
     GTTLVYSTAE IFTWHKYDDR TVLVVYGGPG ETHELVIGAT GLDVLEGDIK STSTKGYTLL
     NFQADGTRKV AKVGVDKNFI YVYMLDRNSA YNYWSIDQDP HSNADAIILK AGYLVRTASV
     DGSTLALTGD LNATTSLEIL GGAPSPLSKL TFNGAELDFD TTDEGVVTTT LGFTAPSLSL
     PDLSKLSWKY IDSLPEIQSA YDDSAWKAAD LKETYNSHRA LNTPTSLYGS DYGFHTGTLV
     YRGHFTASGA ETSFFIITQG GAAYAASVWL DATFLGSYRG AKGVDFASSN FSIPSTLAGN
     TTHVLTVLVD NQGLDENWTV GDETTKNPRG IMDFALSGRA KSDVAWKITG NLGGEAYVDK
     SRGPLNEGGL FAERHGLHLP GALSASAAAW TNSKGPVADG LSRPGVGFFG AEFDLDIPGG
     WDVPLSFTFT NTTGNAHRVL LYVNGWQYGK YVSNIGPQTK FPVPQGILNH AGTNYLGVAV
     WALEGGETKL GGLSLGADAV IATGLGKVGN VDGDTYEARK GAY
//
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