ID A0A074Y257_AURPU Unreviewed; 898 AA.
AC A0A074Y257;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:KEQ80981.1};
GN ORFNames=M438DRAFT_303173 {ECO:0000313|EMBL:KEQ80981.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ80981.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ80981.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ80981.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; KL584994; KEQ80981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074Y257; -.
DR STRING; 1043002.A0A074Y257; -.
DR HOGENOM; CLU_006501_0_1_1; -.
DR OrthoDB; 1847696at2759; -.
DR Proteomes; UP000030706; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR048229; GalB-like.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR NCBIfam; NF041463; GalB; 1.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..898
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001702940"
FT DOMAIN 114..241
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 253..367
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 375..529
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 719..778
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 791..893
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 898 AA; 100090 MW; 4D5304ED954B79FC CRC64;
MFFFTICGLL LPALIYQVNA SPHNAQPKYR LGREQINLNS DWKFRRWEEN PDGLIYDYRQ
DLENLTDVSI LKPWILPSGN DFIKDSSKHY QRPEGNPGSN VTFVQNDFDD QCWTSVTLPH
DWAIAGPFYT EPDGEAIVGG GMGRLPVFGV GWYRRKLHIS NDDKNKQIQL ELGGAMSYAM
VWLNGKLIGG WPYPYNSFQL DLTPHLQFGQ DNQIAIRLDN PVDSARWYPG GGLYRDVWLT
KTEHTHVNQW GTRFTTRDVS DDSAVIDLQL SLGNTANYTS KVSVVTEIYR SNTVTGQQGR
MAASFPATTV EIEANDKTSI NQTLLLSSPQ LWGPPPTQTP NTYIGVTRLL NEAGIQVDVY
ETRFGIRKFE YTGDDGLRVN GERVRVQGVN EHHDLGALGA AFNVRAAERK LEILRELGVN
AIRMAHNPPA SELLDLTDKM GFLVFDEVFD SWERNKTAND FHLIFSDWHE QDLRAMIRRD
ANHPSIMVWS IGNEVGEQNY TQELTEIATT LYAIAHDEDP TRPVTASMNF AQPGNNGAPF
PDILDVLSIN YQGEGIRDTP NYAVTKGITT KPAYPLFHED QPDKLIWTSE SASTVSTRGT
YFFPVTDDGG APVNDSSGGN TTLAQVSAYE LYSANFGSSP DKVFATQDQN TYVGGEFVWT
GFDYIGEPTP YYTSRSSYSG IIDLAGFKKD RFYLYQARWR PDLPMVHILP HWNWAGREGQ
VTPVHVFTSG DEAELFLNNV SMGRQHLDQY EYRLRWDKIT YEPGELHVES YKAGKLWAEA
TVRTTGPAVS LRLTADRQSI SADGVDLSYI TADVLDSQGS VVPTANPEIE FSVSGSGGII
ATDNGDPADL VAFTSTNRKA FSGKALAIVK ASKRNGTISV VAKSEGLTSG EITLNLLT
//
