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Database: UniProt
Entry: A0A135TYB0_9PEZI
LinkDB: A0A135TYB0_9PEZI
Original site: A0A135TYB0_9PEZI 
ID   A0A135TYB0_9PEZI        Unreviewed;      1017 AA.
AC   A0A135TYB0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-FEB-2019, entry version 14.
DE   SubName: Full=Glycosyl hydrolase family 35 {ECO:0000313|EMBL:KXH53072.1};
GN   ORFNames=CSAL01_09817 {ECO:0000313|EMBL:KXH53072.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH53072.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH53072.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH53072.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-2014) 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}.
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:KXH53072.1}.
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DR   EMBL; JFFI01001846; KXH53072.1; -; Genomic_DNA.
DR   EnsemblFungi; KXH53072; KXH53072; CSAL01_09817.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000070121; 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:UP000070121};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:KXH53072.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26   1017       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007804411.
FT   DOMAIN      402    583       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1017 AA;  111218 MW;  5566CA25113514C1 CRC64;
     MRFGLKAGGL LWLAASLCGT QSALAQDVDW PIHDNGLNEV VQWDHHSYIV NGERLFVFSG
     EFHYWRIPVP ELWRDLLEKV KAAGFNAFSI YNHWGYHNPT PGVLDFETGA HNFTSIMTVA
     KELGIYLIIR PGPYVNAETN AGGFPLWATT GAYGDLRNDD ERYTAAWTPF WSEISKVIKP
     HLITNGGNVI MFQIENELNG QWKDIAKRTL NPPIANYMQL LQDSARENGI DVPLSHNAPN
     MRGFSWSKDF SNATGNVDVV GVDSYPSCWS CNLSECTGTN GAYIPYLTQD YYSYFTVQSP
     SQPNFLPEFQ GGSYNPWGGP EGGCPSDIGA DFANIFYRDL IYQRVTAISL YMMFGGTNWG
     WLACPVVASS YDYSSPVSEN RIIGSKFHET KLLTLFTRVA KDLTKTERVG NGTGYTTNSA
     ITVSELRNVD NNAAFYVARH AYSPSNTNEA FKLSVNTSQG ALTIPQHGSS IAINGHQAKI
     LVTDFPFGEK TLLYSTAEVL SYTILDGQEV IALWLPEGEA GEFTVTGVNS AKLVGDGNVG
     DFNVYPGESN VTIAYTQKKG ITLVDLGDGS RAVLLDRTAA YLFWVPVLDN DPFAPANKTV
     FVQGPYLVRH AAFNETGRSL ALSGDADQET TITVFASESI CGITWNGKKL ELLSREGNVF
     TAKIEGPAKF EVPALGPWKL HDSLPEIATD YEATSDSWVA ANKVNTSNTV KPASNNPVLY
     VDEYDIHVGN HIYRATFPTS ESAPTGVFLN VTGGLAFGYS VWLNSEYVGS YLGLSYLGAD
     ASEFSFANAT LSKTGDNVLV VIMDNSGHDL REAALAPRGI TNATLLGPDA ANYKFSEWKI
     AGTAGRNDLI DPVRGPINEG GLYAERVGAH LPGYPDADWV SFDAANGSLS VPDAGIRIFR
     TVVPLDVPAG LDVSISFRLT AAADQTNRLR ALLFVNGYQY GRFNPYIGNQ VQFPVPNGIL
     NYNGDNTIAV TVWSQAAEGV ALSVEWQADY VHTSSFDMSF DSKSLRPEWD ESRWAFA
//
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