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Database: UniProt
Entry: A0A074VI15_9PEZI
LinkDB: A0A074VI15_9PEZI
Original site: A0A074VI15_9PEZI 
ID   A0A074VI15_9PEZI        Unreviewed;       988 AA.
AC   A0A074VI15;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   13-FEB-2019, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KEQ60123.1};
GN   ORFNames=M437DRAFT_54931 {ECO:0000313|EMBL:KEQ60123.1};
OS   Aureobasidium melanogenum CBS 110374.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Dothideales; Saccotheciaceae;
OC   Aureobasidium.
OX   NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ60123.1, ECO:0000313|Proteomes:UP000030672};
RN   [1] {ECO:0000313|EMBL:KEQ60123.1, ECO:0000313|Proteomes:UP000030672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ60123.1,
RC   ECO:0000313|Proteomes:UP000030672};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J.,
RA   Zalar P., Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y.,
RA   Lipzen A., 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   -!- 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; KL584844; KEQ60123.1; -; Genomic_DNA.
DR   EnsemblFungi; KEQ60123; KEQ60123; M437DRAFT_54931.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000030672; 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:UP000030672};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030672};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    988       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5001701684.
FT   DOMAIN      378    558       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   988 AA;  108967 MW;  A53C996F71EB7EA0 CRC64;
     MRLCFNTLIY TFLLAVLVLA TDNGLTTQVT WDPYSLMVNG KRLFLFSGEF AYERMPVPEM
     WSDIFQKFRA NGFNAVSLYF FWSYHSASRD VFDFKSGGKD IQRVIDAAAE AGLYIIARPG
     PYANAETNGG GLALWTSDAP GNYRTSDQTY YEAWEPWMRE VNKILVKNQI TMGGPIILYQ
     IENELQETVH KANNTLVTYM EQLKKSVKDS GIVIPLTHNE KGQRSQSWST DYQDVGGAVN
     IYGLDSYPGG LSCTNIDSGF NLVRNYYQWF QNYSYTRPEF WPEFEAGYFT SWHGVFYDSC
     LAEHDPAFAD VYYKNNIGQR GTLMSLYMTM GGTNWGNLAA PVVYTSYDYS APMRETRELQ
     LKMSQTKLIA LFTRVSQDLL YTNMESNGTG NAVSTQDIWT WVLRNPNTTA GFYVTQHSKS
     SSRAVTDFSI NLQTSLGLIT VPGVQLNGRQ SKIAVTDYHF EKHTLLYSSV DILTYGLFDT
     TSVLVLYLEA GQVGEFAFPG NVSSTSYGNT SVTTCRMKAN GTSYYTKFVY KQTTGKTAIQ
     MSNGVMVYLL DVSTAWSFWA PVTTSDPNVA ADEQIFAIGP YLVRNASVSS NVVSVNGDNT
     NSTTLEVFVG NANVDTIAWN GKRLATKKTA YGALTADLTS VLDRKVTMPI LSGWQVADSL
     PEVARDYDDS SWAVCNKTTT LAPVRPLSLP VLYSSDYGYY AGVKVYRGYF DGKTAVSANL
     TAQGGSAAGW SAWLNGKLVG GHPGNASLLS TSDVLDLTRA TLFDKDNVLT VVTDYTGHDE
     TSTGKGAANP RGLLGAVLKS SENATVDFKQ WKIQGNAGGS ANIDPVRGPL NEGGLYGERL
     GWHLPGFKLS GNGWSVGSPA EGLNSSGIRW YLTTFELGID LDLDVPIGLE LSAPSGTVAS
     VQIYLNGYQY GKYIPHIGPQ TRFPFPPGVI NNQGRNTLAL SVWAETDAGA KLDNVSLFAY
     NVYETSFNFA QDWTYLQPEW TSERLQYA
//
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