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Database: UniProt
Entry: A0A2H3IC40_9EURO
LinkDB: A0A2H3IC40_9EURO
Original site: A0A2H3IC40_9EURO 
ID   A0A2H3IC40_9EURO        Unreviewed;      1008 AA.
AC   A0A2H3IC40;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-FEB-2019, entry version 7.
DE   SubName: Full=Glycoside hydrolase, family 35 {ECO:0000313|EMBL:PCG94192.1};
GN   ORFNames=PENO1_079720 {ECO:0000313|EMBL:PCG94192.1};
OS   Penicillium occitanis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG94192.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCG94192.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCG94192.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A.,
RA   Gargouri A., Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant
RT   Pathogen Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PCG94192.1}.
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DR   EMBL; NPFK01000288; PCG94192.1; -; Genomic_DNA.
DR   Proteomes; UP000218381; 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:UP000218381};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:PCG94192.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1008       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5013668954.
FT   DOMAIN      397    585       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1008 AA;  111425 MW;  79E4F55E6653F110 CRC64;
     MTQLFTKLLI YFLLFASPLL ADQWPLHNDS LNDVVQWDHY SFELNGQRLF VFAGEWHYWR
     IPVPELWIDI LEKIKAAGFT AFAMYVNWAY HAPNNHTVDF LTGAHDITPI LEMAKDVGLY
     VLLRPGPYIN AEVNAGGFPL WVTTGEYGSL RNNDSRYTAA WEPYFTKLSE ITSKYQISNG
     GNVITYQIEN EFGDQWTGSP SLRVEYEPAA KYMELLEANA RQNGIDIPLI ANEPNMRAIS
     WGKDWSNSSA NVDVVGLDSY PSCWSCDLSV CTGTNGEYIA YEVVDYYDYF QETQPTMPSF
     LAEFQGGSFN PWGGPVGGCP GDIGPDFANL FYRWNIGQRV TAINLYMLFG GTNWGAIAAP
     VVATSYDYSS PISENRTIGA KYYETKLLTM FTRAAKDLTV TDLVGNGTQY STNTAVQAYV
     IQNPNTNCTF YVTIHTTSSS STDETFQMHI QTSFGVLSVP RYGNSIRLNG HQSKIIVTDF
     QFGSHKLLYS TAEVLTYAIL DGMPTLALWV PTGESGEFSV LGSKWASVQR CEGCSGVGFY
     PGQDTSNQTA SELTISFTQD QGMSVIELDT GVRVVLLDRE SAYHFWAPAL NTDPSVPEDQ
     SVLVQGPHLV RSARIVGSTI RLQGDSAQAN PIEVFAPKQV QVIFWNGKEL KTSRTSYGSL
     QASLPQPPSV KLPSLGPWKY NNSLPEKAQD YKDTSVAWIS ADHMSTSNPS RPATYPVLYA
     DEYGFHNSIR IWRGYFTGNA TGVVLSVQGG YAFGYSAWLN GQLLGSYLGE PNVEQSNLTL
     PFNISHVSTS SENVLVIVHD DTGHDETSGA LNPRGILGAT LMSDSSSVNF SQWRVTGTAG
     GETNLDPMRG PYNEGGLYAE RMGWHLPGFK DNAWVDAGSQ LNFTGADIKF YRTVTPLSIP
     EGVDVSISFE LSACGTTNAF RAQLFVNGYQ MGRFNPYVGN QIEFPVPPGI LDYKGDNTIG
     FSLWAQTEAG ACASVDWKIN YVLESSLDVT FDGEYLRPGW TSERLQYS
//
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