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Database: UniProt
Entry: A0A139HJQ2_9PEZI
LinkDB: A0A139HJQ2_9PEZI
Original site: A0A139HJQ2_9PEZI 
ID   A0A139HJQ2_9PEZI        Unreviewed;       728 AA.
AC   A0A139HJQ2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755};
DE            EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755};
GN   ORFNames=AC578_10701 {ECO:0000313|EMBL:KXT02607.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT02607.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT02607.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT02607.1,
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 suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased 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 alpha-D-galactose
CC         residues in alpha-D-galactosides, including galactose
CC         oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00001255};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT02607.1}.
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DR   EMBL; LFZN01000040; KXT02607.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HJQ2; -.
DR   OrthoDB; 2584938at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   CDD; cd14791; GH36; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.70.98.60; alpha-galactosidase from lactobacil brevis; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR038417; Alpga-gal_N_sf.
DR   InterPro; IPR002252; Glyco_hydro_36.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43053:SF3; ALPHA-GALACTOSIDASE C-RELATED; 1.
DR   PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 1.
DR   Pfam; PF02065; Melibiase; 1.
DR   PRINTS; PR00743; GLHYDRLASE36.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133}.
SQ   SEQUENCE   728 AA;  82329 MW;  D532D592FD3994D4 CRC64;
     MSSQFKPNIR VELPLKQHGI SVHAVSDIRW IRWRPSALDV DLMIDGDAHV WIHSIRPKDA
     HVKEYNTDTE LAHALPIVQI RLLGEGSTYG TSERLVFSAT PQRLSYVSHT EWQDGHSHFL
     KIEMHDKTAD IAVQTQFGVF FNVPVLRSTV FVKNEGRHNV FLQAVASLSL GYLNRGHDEW
     WKEYEVWFAN STNFREAQWK AFEPGDLGMD YVGASDFHKP GTRASIVKSN LGTFSTCGSL
     PMGALSRKDG KQCYMWQIEH SGSWRWELGN ILHGLYVIAG GPNDQDHQWT KKLEPGEEFE
     SVSTALAVIS GKTEDAFDAF TRYRRGIRRR HADNQTLPVV FNDYMNCLDG DPNEQKVLAL
     IQPARRLGAE YFCIDAGWYA DVDDWWDCVG EWKPSRVRFP RGLNFVLDTI KDAGMKPGLW
     MEPEVIGIKS PVAAALPDGA FFQRLGRRVV EQSRYHLDFR HTAVTTRLNN IIDGLVNDLG
     VQYFKFDANI DVTHGTDFNA SSPGDGMLEH RRAYMAWINR LYDRFPDLVI ESCSSGGQRL
     DYHTLATHSI QSTSDQTNPV IYSAISANIL TALTPEQSAS WALPAPEYDD DTIALCMVNS
     LMGRLYISGR IDLLTDSQLQ LVIEASDVYK SIRADIPNSV PFWPIGLHAW HQDWLVLGLK
     TVSAMYLAVW RRGGLDSFSF QLLEAQEHAN FSALYPKRLI TVLKWHAAKK QLSVTIPTFP
     SARLISVA
//
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