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Database: UniProt
Entry: A0A166CZ13_9HOMO
LinkDB: A0A166CZ13_9HOMO
Original site: A0A166CZ13_9HOMO 
ID   A0A166CZ13_9HOMO        Unreviewed;       984 AA.
AC   A0A166CZ13;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-FEB-2019, entry version 14.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:KZV66862.1};
GN   ORFNames=PENSPDRAFT_584749 {ECO:0000313|EMBL:KZV66862.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV66862.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV66862.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV66862.1,
RC   ECO:0000313|Proteomes:UP000077086};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV424589; KZV66862.1; -; Genomic_DNA.
DR   EnsemblFungi; KZV66862; KZV66862; PENSPDRAFT_584749.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000077086; 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:UP000077086};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:KZV66862.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077086}.
FT   DOMAIN      353    523       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   984 AA;  107672 MW;  AC19610E1622807C CRC64;
     MKPNSTGRTD AVQWDGYSLI LRGQRVFIHS GEFHQWRLPV PALWRDVLTK FRAAGLNAVS
     IYTHWGLIEP SRGQISFSGI NALKPFFELC QELGLWVVVR PGPYINAETT AGGIAHWVTT
     EVPGRLRTNE SEWWESWQGY VKAIIEETAP YQISEGGPVI AVQLDNEYAQ TPDGAAYFQA
     LVDAFKNSPI VVPLTYNDPH AGENFINGTG AVDIYGLDAY PQRFDCSRPD VWNPVDDTYH
     DYHMRVNPGQ PWYMPEFQAG AFDPYGPSAP GYDKCRELTN AGFESVFYKS AWGANAKMMS
     YYMVYGGTSW GGLPFPEVYT SYDYGAAISE PRTLTSKYDE LKAQGLFLRS SVNFTKTEWI
     GNSTNGVVDV TNPDVLVVEL RNPESGSGFY IARQLNSSST DTVKFNMTIN TIEGPLPIPQ
     TTDGIVLGGR EAKVIVTDYF YGTLGYLYYS TAEIFFSGNI GDRDVLLAYG RSDQEHEIGV
     FGGHMLNIPP MSSASDGLTG LRAIFDVPGM LVLFADVPTA HTFFAPPLSG PPEDPFANFW
     GFGTNASVLV GGPYLVREAV IGEDKVIALT GDIEKDTIIT VIGPEDMAGV TWNGEPVGCD
     PEAGERISNT GVCIGGLRLS PVVSKITVPK LEGWRYADSL PERALDFDDD DWIIADKTTT
     NAWRPPVYGD GRVLYGCDYG FCENVVLWRG HFEATGEEAS VSLLINGGDA FAASVFLNGV
     FLGTAYGNST NNLNIIAEVD AEYKFPNGVL QSGRDNVITI VQDNMGLEES GDEWEVDILR
     SPRGVRGFQL NPSGNFSDWK VQGKLGGYRA FPDKMRTITN EGGLFGEREG WHLPGFDTSA
     WVERALSDGL PDAHAGVGFF STTFDLEIPE GFDVMLSFVF DDGVGETGVP YRALLFVNGW
     MMGKRVANLG PQAKFPVHEG ILDYGGTNTV VVALWALEDQ QVSPSLVLVV DKVFQGGVGR
     IATNNPTYSE LRSVITLAPV LGAC
//
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