ID F2T9U0_AJEDA Unreviewed; 667 AA.
AC F2T9U0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 2.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:EGE80003.2};
GN ORFNames=BDDG_02944 {ECO:0000313|EMBL:EGE80003.2};
OS Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE80003.2};
RN [1] {ECO:0000313|EMBL:EGE80003.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE80003.2};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease.;
RA Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; GG749417; EGE80003.2; -; Genomic_DNA.
DR AlphaFoldDB; F2T9U0; -.
DR HOGENOM; CLU_005732_2_0_1; -.
DR Proteomes; UP000007802; 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; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR018954; Betagal_dom2.
DR InterPro; IPR037110; Betagal_dom2_sf.
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:SF122; BETA-GALACTOSIDASE A-RELATED; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..667
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005346482"
FT DOMAIN 357..512
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 667 AA; 74201 MW; DD9866AC5B93BC9A CRC64;
MRFLSACAIA CLALQSAAVV VVDRKLGGFT VIEHPDPAKR DLLQDIVKWD NESLFINGER
IMIFSAEFHP FRYSFMGLII RCGLPVPSLW LDIFQKIKAL GFNCVSFYTN WALTEGKPGE
YTAEGIFAWE PFFEAATEAG IYLLARPGPC INAEVSGGGF PGWLQRVRGQ FRTSDKDYLA
ATDNYIAHIA SPVAKAQITN GGPVILYQPE NEHTLSLRIH DFPDGDYMQY VIDQARKAGI
VVPMISNDAW AAGNNAPGTG KGEVDIYGHD KYPPIPTSSL LDFCPPIGGS STSSKVPSHL
TPLSSFGNVF LNLYMGHPGG YTSYDYGAPI SEDRNITREK YGELKLIGNF MKASPSFMNA
VPGHWSISKF TTTPTLTVTS LIGRLSDSSF FVLRHSEYSS KASTNYKLKL PTSVGRLIMP
QLNGTLTLNG RDSKIHVTDY DVAGTKYFLF DCRDIHMEEV WGPQGLLVEG PSHDMTIKKV
DDYVVLNWET MRERRIVDIG DLSVFILDLE SLELRRASPL RRKAVLGLGI QHGSMGVTLD
PGRARAILGA SSTNIYSFPK LKAGEKYVFT MLVDNMSLGQ DYVIGADSTK NPRGIQHYKL
FGRLQSRVTW KLAGNLGGED YQDRFRGPLN EGGLYIERQG WHQPNPPHPV LEVCKPHYRR
RCGWVRE
//