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Database: UniProt
Entry: A0A166KY62_9HOMO
LinkDB: A0A166KY62_9HOMO
Original site: A0A166KY62_9HOMO 
ID   A0A166KY62_9HOMO        Unreviewed;      1005 AA.
AC   A0A166KY62;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-FEB-2018, entry version 11.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:KZV76227.1};
GN   ORFNames=PENSPDRAFT_623303 {ECO:0000313|EMBL:KZV76227.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV76227.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV76227.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV76227.1,
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: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC       {ECO:0000256|SAAS:SAAS00108875}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; KV424466; KZV76227.1; -; Genomic_DNA.
DR   EnsemblFungi; KZV76227; KZV76227; PENSPDRAFT_623303.
DR   Proteomes; UP000077086; 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; -; 1.
DR   Gene3D; 2.60.120.260; -; 3.
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:KZV76227.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1005       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007876557.
FT   DOMAIN      397    574       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1005 AA;  109221 MW;  F59CCE42E4B0AB46 CRC64;
     MNAVIFASAL AALLNILYCY AYIVPSGSPG FYAGNSTSSV TFDEHSILLD GKRVFIFSGE
     MHPWRAPSGG PTWRDVLQKM KAAGFNAVSV YHRWGSSSGR PGELDFGYWR NQTQVYQIAK
     EVGILVIARP GPYINVTAGG YPGWATLLNV TTRSNASEFT DAWKPYIAAA AQFIAPYQYP
     DGPVIAVQVE NEFGPSDPEH PGRSEYFATI EDTLRGNGIT RVPLTSNEAG DSGLFAPEPR
     TYDVGAVDLY TFDAYPQRYA CNDPYTWHEV VTSYPAAHAA DDPDLVWASG EYQAGSQDGW
     GGGGYDGCYE LTNENYVNVF YKNNYASQVM FQNLYMTYGG TNWGNLAEPG VYSSYDYGAA
     IREDRRLTSK YNELKLQAYF LHASRSFLTA EIVSATNLTD SGSEESSGVG ATDGSDVFVT
     SMASDDGGGF YVVRQVTNNI TTPTHFTLDV NTTAGEFTIP RLGGNITLAG RESKILVTNY
     GFGLSTLDYS TAEVLTWFTF DETDYIVLYA LEGQQVEVSL STNTSSADVK GTLMNTTYVD
     GSLIVTGSPS GLTRVDIGND TTLLIVDKVS AYGLWAPRLV HTDGTESYDQ SPDTSSALVS
     GPYFVRNATL KGTSIAMYGD INATTTISLL APSNITSFSW NGAHVDTNVD EFGFLSGLVT
     FDVAEVQLPS LRDAEWWAGD SLPEVLDGFD DSDWVAANLT SVESPYQPYN MGGMYVLYAD
     FYGFHQGNTI YRGHFTGTNA TGVELSVQGG QNFSYGAWIN NRFLGTNPPG GADTSNDTWR
     FEDGDLRDGD NVVTIVLDPT GQEEWYPGDR FKTPRGLRGY GLLGGADFDY WKIAGNLGGE
     HWPDAVRGPM NEGGLSVERI GAHLPGFPAS QHNWTAPSST SSPFSGLGSA GILAYRTNFT
     LDIAANVDAP ISLNFTYTPG SNYRSVIFVN GWQFGRFNGL FGPQTLFPIP QGILNHQGDN
     ELLVTLWSLD PNGAKIEGLE LVSTALISTS KEGFRSWSCR LSRIL
//
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