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Database: UniProt
Entry: A0A178E4M8_9PLEO
LinkDB: A0A178E4M8_9PLEO
Original site: A0A178E4M8_9PLEO 
ID   A0A178E4M8_9PLEO        Unreviewed;      1011 AA.
AC   A0A178E4M8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   13-FEB-2019, entry version 12.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAL50073.1};
GN   ORFNames=IQ07DRAFT_539901 {ECO:0000313|EMBL:OAL50073.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Cucurbitariaceae; Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL50073.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL50073.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL50073.1,
RC   ECO:0000313|Proteomes:UP000077535};
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|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; KV441645; OAL50073.1; -; Genomic_DNA.
DR   EnsemblFungi; OAL50073; OAL50073; IQ07DRAFT_539901.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000077535; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000077535};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     27       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        28   1011       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008085082.
FT   DOMAIN      409    590       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  110382 MW;  CD12F3B9806EEBCF CRC64;
     MRGLSGLSWL SLLSTLSSFS NVVGSDAQSI TTPSQWPLHD NGLNDVVQWD HYSFKINGKR
     LFVFSGEIHY WRIPVPEVWE DLLEKIKAAG FTAFAFYGNW AYHSANNQTL DFTTGAHDFT
     KLFEIAERVG LYIITRPGPY VNAEANAGGF PLWLTTGAYG SLRNDDPRYL KALDPYFSKY
     SELTSKHLVT KGGNVFVYQI ENEYGEQWKD RTKKIPNDSA ARYMAALEDS ARANGIDVPL
     IHNDPNMNTK SWSKDYAPGA VGNVDVAGLD SYPSCWSCNL DECTGTNGEY VAYQVIDYYD
     HFEEVSPTQP SFFPEFQGGS YNPWGGPEGG CPADIGADFA NIFYRNLISQ RVTALSLYMV
     FGGTNWGALA APVTATSYDY SSPISENRKI DSKYYETKNL ALFTRVAEDL TVTDRIGNSS
     VYTSNSAVEA SELRNPLTNA AFYVTIHSYS PSSTKESFKL HVSTSIGNLT IPQHEGSIVL
     NGHQSKILVT DFAMGNHTLT YSTAEVLTYA LIDKKPVVVL WAGVGESVEF HIKGAKKGHQ
     VSKNKGFNAT FHAESHGVTT NIQQVSGLSV LDFDNGVKVI VADKPTAYLF WAPNLSKDPF
     APVDQSVLVQ GPYLVRHASE KGGVLSLTGD VTNQTAIEVF TSHRVKSLTW NGKKLHASRT
     PYGSLKATVG AFSGKIDLPS LSEWKVQDGL PEKLPSYKDS SAAWITADRL TTTNPTKPDT
     LPVLYVDEYG FHNSFHLFRG SFVGSATGVK LSVQGGLAFG WSAWLNGDFV GSFLGNSSVG
     SGNATLSFAN ATLHANSTNV LLVAQDNTGH DLRSDAVKPR GILHASLEGG ANFTSWKIAG
     EAGGESTLID PVRGPLAEGG LTAERLGWHL PGFDDSAWNS SSPSTGFSDA GIQFYRTTIP
     LNIPEGVDAS FAFVLNSLGS QAVRVQLFVN GYQYARFNPY VGNEKKFPVP PGILNYRGDN
     VIGVSVWAQS EEGAKVDVQL VNEYVVESSW SSNFDSEYLR PGWTKERLAY A
//
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