ID A0A0U5CHA5_9EURO Unreviewed; 1015 AA.
AC A0A0U5CHA5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 13-FEB-2019, entry version 15.
DE SubName: Full=Putative Beta-galactosidase (Eurofung) {ECO:0000313|EMBL:CEL10108.1};
GN ORFNames=ASPCAL13233 {ECO:0000313|EMBL:CEL10108.1};
OS Aspergillus calidoustus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=454130 {ECO:0000313|EMBL:CEL10108.1, ECO:0000313|Proteomes:UP000054771};
RN [1] {ECO:0000313|EMBL:CEL10108.1, ECO:0000313|Proteomes:UP000054771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaenicke S.;
RL Submitted (DEC-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}.
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DR EMBL; CDMC01000017; CEL10108.1; -; Genomic_DNA.
DR EnsemblFungi; CEL10108; CEL10108; ASPCAL13233.
DR OrthoDB; 179316at2759; -.
DR Proteomes; UP000054771; 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:UP000054771};
KW Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW Reference proteome {ECO:0000313|Proteomes:UP000054771};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}.
FT CHAIN 28 1015 {ECO:0000256|SAM:SignalP}.
FT /FTId=PRO_5006855725.
FT DOMAIN 406 587 BetaGal_dom2. {ECO:0000259|SMART:
FT SM01029}.
SQ SEQUENCE 1015 AA; 112045 MW; 953DCD3CAF33E138 CRC64;
MTLSPLTKVL AALASVLSFA TIPHSLASDT EWPIRDTGLG DKTVQWDHYS LIYNGERLFS
FGGEFHPFRI PVPELWVDIM EKIKASGMNT MSFYNHWGFH MPTSDPGSLD FESGAHDLGR
LYEIAKELGL FVHSRPGPYI NAELNAGGMP LWITTGEYGA LRDNNTAWEA KWKPYMDRVA
EITAPYQVTR NGTVILFQIE NEFPQQWADV EAKTPNPVPI AYMEELFEQM QARGIDIPLT
HNMPGQRYKS WSVDYDTVGA GGNVHIYGLD NYPSCWSCMP EDCSTSNPSF TLMDYTAHFN
EVSPKQPSMM PEFQGGAMNP WDGPAGGCEA KTDDAFVNFY YRDNVAQRVT ILGLYMFYGG
TNWGWLAAPF VPTSYGYSAA IAENRAIGAK FYEIKSLALF TRSATDLTKT DLVGNSTLYT
NNEAVTTIEL RNPDTDAGIY AIRHTDPTSN DEQTFRLSVR TSVGNFTLPT LEQGTIGLNG
HIQKILVTDF RFGNRNLIYS TAEVLTYGIF DKEPTLALWV PNGEGGEFFV QGAKSGKVVA
GGKAEVKFSR SREGLIVNFK EQQGMTVLML DDDARVIVMD RDTVHLFWAP ALTSDPRVPA
NQVAFVQGPY LVRSAKLDRH TISLRGDSSQ ATELEVFTES RVHTVKWNGK TLATHKTKYN
SLKAKIDGPR RFSAPSFRSW KAQDSLPERF ANYSDSGPAW ANADHMTTVS KYKDATKPYL
YADEYGFHAG VQLWRGYFNG SAGGVNLKVQ GGIAHGWSAW LNGAFIGSFL GDLGSSSGSK
ELEFPTESLK ADGQNVLLVL QDNSGHDQGS ASLNVRGIIN ATLIDSESGG FNSWKVAGTA
GGASGTTIDP VRTYYNEGGL TAERLGWHLP GFDDSEWSTS TPSDGFAGAG AKFYRGILPL
DTPAGHDVAL SVKISFEDKS SESSNFRAYL YVNGYQYGRY YPYINSAVNT FPVPPGIWEY
SGDNVVGLAV WNQGSGEVRV DIKLQVDYVL ASALNVKFDG EYLRPGWDES RTQYV
//