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Database: UniProt
Entry: A0A139H166_9PEZI
LinkDB: A0A139H166_9PEZI
Original site: A0A139H166_9PEZI 
ID   A0A139H166_9PEZI        Unreviewed;       985 AA.
AC   A0A139H166;
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=Uncharacterized protein {ECO:0000313|EMBL:KXS96174.1};
GN   ORFNames=AC578_2652 {ECO:0000313|EMBL:KXS96174.1};
OS   Mycosphaerella eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Mycosphaerella.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS96174.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXS96174.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS96174.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana
RT   suggests a link between parallel evolutionary changes in
RT   Pseudocercospora fijiensis and Pseudocercospora eumusae and increased
RT   virulence on the banana host.";
RL   Submitted (JUL-2015) 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:KXS96174.1}.
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DR   EMBL; LFZN01000184; KXS96174.1; -; Genomic_DNA.
DR   EnsemblFungi; KXS96174; KXS96174; AC578_2652.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000070133; 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:UP000070133};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    985       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007806216.
FT   DOMAIN      378    556       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   985 AA;  109081 MW;  6BBEF1C74ADE710D CRC64;
     MYMLIRLVWL LSVAYLALGI DDGFTKAVTW DKYSLMINGS RVFIQAGEFH YARLPVPEMW
     RDVLQKFKSN GLNAVSIYFF WSYHSPKPGI FDFESPGKDI QKLFDMCKEI GLWVIARPGP
     YCNAETNGGG LALYGSDGSF GKLRTSDETY HQAWLPWMKA VGTIIAKNQI TKGGPVILYQ
     IENELQEISH EVNNTLVLYM EQVESASRDV GIDVPFFSNE KGMRSQSWST DYEDVGGSVN
     IYGLDSYPGG LSCTDPDAGF KVVRTYYQWF HNYSFTQPSF VPEFEAGYFQ PWGGKFFDTC
     LAMHDPQFAD VFYKNNIGQR VTLQSLYLAF GGTNWGNLAA PVVYTSYDYS APMNEKREVT
     TKFKQTKLVA LFTRASAELL KTEMESNGTG NVVSTADVWT WVLRNADTHA GFYVLQHDNT
     SSRATTTFDI NLNTSKGNVT VKGLELKGRQ SKIVTTDYHL GTNYNILFCT ADVLTWVTLG
     NATMLILYAD IGQSANFAIE TKAKYEVFGD TKLISDADDH EAYTRYSYTQ GAGSTIVRFE
     DDLVVWLLDT ETAWDFYAIP LSTDPFASSN NQILALGPYN IRSASIEGSA VAMIGDNENT
     TTLEVFAGPY VSSITWNGQD LATAVTEYGS LKATVRGSDA VLSVPSLLWK AANSLPELSS
     SYDDSGWKIC NKTATLSPVA PLTLPVLFSS EYGYFAGIKI YRGYFISKSA RSANITIQGG
     RASGFTAWLN GMFVGHTFGN ATSTSPASAL LDFSNATLGD ENVLTVVTDY TGHDETSTGP
     AGVENPRGIL GAWLYDGDGN ELPYTTWKIR GSAMDEKEKL DPVRGPMNED GLHGTRLGWH
     LPGFEANGPE WIDEFPTVGL NKSGVRWYVS NFELEFPKDI DAPVSFDLEA VGGTTASMEL
     FVNGYQFGKS LPHFGPQTRF PFPPGIINNR GNNTIALVIW AMTDAGAKLA KAELVVDRTY
     QTGFDFNQDW SMLQPRWTPD RLQYA
//
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