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Database: UniProt
Entry: A0A194XJ34_9HELO
LinkDB: A0A194XJ34_9HELO
Original site: A0A194XJ34_9HELO 
ID   A0A194XJ34_9HELO        Unreviewed;      1002 AA.
AC   A0A194XJ34;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   13-FEB-2019, entry version 15.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KUJ20173.1};
GN   ORFNames=LY89DRAFT_682954 {ECO:0000313|EMBL:KUJ20173.1};
OS   Phialocephala scopiformis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Phialocephala.
OX   NCBI_TaxID=149040 {ECO:0000313|EMBL:KUJ20173.1, ECO:0000313|Proteomes:UP000070700};
RN   [1] {ECO:0000313|EMBL:KUJ20173.1, ECO:0000313|Proteomes:UP000070700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 120377 {ECO:0000313|EMBL:KUJ20173.1,
RC   ECO:0000313|Proteomes:UP000070700};
RG   DOE Joint Genome Institute;
RA   Walker A.K., Frasz S.L., Seifert K.A., Miller J.D., Mondo S.J.,
RA   Labutti K., Lipzen A., Dockter R., Kennedy M., Grigoriev I.V.,
RA   Spatafora J.W.;
RT   "Full genome of DAOMC 229536 Phialocephala scopiformis, a fungal
RT   endophyte of spruce producing the potent anti-insectan compound
RT   rugulosin.";
RL   Submitted (OCT-2015) 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; KQ947410; KUJ20173.1; -; Genomic_DNA.
DR   RefSeq; XP_018074528.1; XM_018214608.1.
DR   EnsemblFungi; KUJ20173; KUJ20173; LY89DRAFT_682954.
DR   GeneID; 28824334; -.
DR   KEGG; psco:LY89DRAFT_682954; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000070700; 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:UP000070700};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070700};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1002       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008268301.
FT   DOMAIN      397    577       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1002 AA;  109984 MW;  A8BF08BC36A55DC6 CRC64;
     MNFYTVFAFC IWAVGVAQAQ VQWPLHNDNL TTVVEWDHYS YIINGQRLFI WSGEMHYWRA
     PVPEMWIDIL QKVKAAGFNT VSFYGNWGYH SAKNGSLDFD SGAHNFTKLF ELTKQIGLYV
     LFRPGPYVNA EATAGGFPGW VTTGAYGSLR NNDTRYTDAW TPYFQKISQV VSQHQVTNGG
     SVFIYQIENE YGDQWENVAA KVPDPEAIQY MELLEKCARD AGINVPLTHN NPNMNTKSWS
     KDYDTVGAGG DVDIYGLDHY PSCWSCNTAE CTGTNGNVPE FTVYEYFTNF LQVSPTQPSF
     LAEFQGGSYN PWGGPEGGCV NTTGPDWVNV FYRHNVGQKV TAMNVYMLFG GTSWGGLPMP
     TVATSYDYSA PISESRAIGD KYHETKLFAQ FLRVARDLTK VDLINNGTGY ASTPEIFTNE
     LRNPDTNARF YVTIHTSSPS TNLTAFQLKI STSSGNFTIP QYNQLVLNGR ESKIIVTDFT
     VGKEKLVYST AEIMTVSTQD EKPLVFLWLP EGEDGEFILT GVQSATVLKD DGCANLKTTQ
     RNGGLVVSYT QATGTCVLKF DNGYRFALLD RSTAYYTWVP STSADPYTPE NSTVVVQGPY
     LVRSASNSES ALELTGDISN MTELEVYAPS SVSHITFNGE NIQVSRTSHG SLVGKLNECA
     ETTASIQAKL PALASWKVND GLPERMAEYD DSKWTIANHS STPNPSPPAT YPVLYADEYG
     YHTGNLLWRG RFPGSTATGV HLEVIGGTSS GWSAYLNGIY IGSWLGSTSV TKGSLSLSFS
     NATINSATEN VLLVIQDHMG KDETSGAVNP RGIYNATLLG NSGLNFTSWK LAGNAGGESN
     IDPIRGVYAE GGLHGERMGW HLPGFDDSAW NSSTPETGLT KAGAKWYRTV VPLDIPRGVD
     VSLGFLLGSP TEEKVRAQLY VNGYMFGKYV PYIGNQVVFP VFPGILDYHG QNTIALSIWA
     QDAAGGSVSV DWTVLNVVQS SFDPGFEASY LRPGWSDRSA YY
//
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