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Database: UniProt
Entry: A0A177CET0_9PLEO
LinkDB: A0A177CET0_9PLEO
Original site: A0A177CET0_9PLEO 
ID   A0A177CET0_9PLEO        Unreviewed;      1015 AA.
AC   A0A177CET0;
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_1196129 {ECO:0000313|EMBL:OAG05826.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Massarineae;
OC   Didymosphaeriaceae; Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG05826.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG05826.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG05826.1,
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; KV441552; OAG05826.1; -; Genomic_DNA.
DR   RefSeq; XP_018036191.1; XM_018181439.1.
DR   EnsemblFungi; OAG05826; OAG05826; CC84DRAFT_1196129.
DR   GeneID; 28764925; -.
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     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23   1015       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5008058098.
FT   DOMAIN      394    570       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1015 AA;  111153 MW;  90D4A8AB216704FA CRC64;
     MKVRQYMLRF ALALLGSNVV AARALSGKPS DFIIREERAL QDIVTWDEHS LFVHGKRVNF
     WGGEFHPFRL PVPSLWLDVF QKIRAMGYNG VSFYSAWVLH EPKPGHFQAE GLFDWEPYFA
     AAKKAGIYLV ARPGPYINAE VHGGGFPGWL QRISGNLRTP DADYQAASKH YIESITPILA
     KAQITNGGPI ILFQPENEYS MGMNNVTFPD ADYMNGLMKQ FRDLGIVVPF INNVAWPSGI
     NAPGTDAPVD IYGHNSYPLG MNCSDPKNWV DGALPTDWRK THLEQSPKTP YLLVEYQGGA
     YQPWGGDGFD KCAEFTNHEF ERVFYKNNIA VGATISNFYM TTFGGTNWGN LGHADGYTSY
     DYGAAITEER QVHREKYSEA KLIANFVAAS GDALASATPG FNTTGVYTDN DAVTVTPLVG
     EQTKFYITRQ VKYNSLDSVS YKLAVPTSTG NITIPQLGGT LSLHGRDSKI HVTDYPVGGY
     NLLYSSAEIF TWKKHGSRTT LVVYGGPNER HELAVSKTSG ATAVEGSGVK FANRNGVTIV
     NWDSRPERRV VRIGPSLYII ILDRNSAYDY WTVSTSEGSY SHELTPSSEL IVKAGYLLRT
     ASITDGKIHL TGDINATTIV EVVAGAHEKV KGLTFNSADV KATLDRNGFL KSTTLGFSTP
     QVHLPDLKTL SWKSIDTLPE LQPDYDDSTW PDADHTDTKN TYWPLITPTV LWGAEYGFHA
     GSLLTRGHFV ATGNESIIHL NVSGGSAFGF SAWVNSTFIG SWEGAGDVKI ANLTLPIPKL
     IKGDNYVLTV LSDHMGHNGN WFIGYNEMKT PRGIIGYDFP GHTPPNNGTS RAPDGIKWKI
     TGNLGGEDFH GGRRGSLNEG ALWVERHGYH LPGAPTESWK ASKEPTAALQ KPGVTFYTAT
     FTLSIPSSID VPLSFVFSGD AFNGKGKGWR AQLWVNGYQF GKFANGIGPQ KRFPVPQGIL
     NYSGKNTLGV SIWALEKGGA TPGGFDMVSG MVVESGFGDV ELSPMDGWVE REGAY
//
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