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Database: UniProt
Entry: N4V2H2_COLOR
LinkDB: N4V2H2_COLOR
Original site: N4V2H2_COLOR 
ID   N4V2H2_COLOR            Unreviewed;      1030 AA.
AC   N4V2H2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   13-FEB-2019, entry version 28.
DE   SubName: Full=Beta-galactosidase b {ECO:0000313|EMBL:ENH77807.1};
GN   ORFNames=Cob_13225 {ECO:0000313|EMBL:ENH77807.1};
OS   Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 /
OS   LARS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS   lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1213857 {ECO:0000313|EMBL:ENH77807.1, ECO:0000313|Proteomes:UP000014480};
RN   [1] {ECO:0000313|Proteomes:UP000014480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=23252678; DOI=10.1111/nph.12085;
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Comparative genomic and transcriptomic analyses reveal the
RT   hemibiotrophic stage shift of Colletotrichum fungi.";
RL   New Phytol. 197:1236-1249(2013).
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; KB726077; ENH77807.1; -; Genomic_DNA.
DR   ProteinModelPortal; N4V2H2; -.
DR   EnsemblFungi; ENH77807; ENH77807; Cob_13225.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000014480; 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:UP000014480};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014480};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26   1030       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004121365.
FT   DOMAIN      402    583       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1030 AA;  111961 MW;  51B88F30BD8DA3DB CRC64;
     MRFGLKAGAL LWLAASLCGS GGALAQDVDW PIHDNGLNEV VQWDRHSYIV NGERLFVFSG
     EFHYWRIPVP ELWRDLLEKI KAAGFNAFSI YNHWGYHNPK PGVLDFDTGA HNFTSIMTVA
     KEVGIYLIIR PGPYVNAEAN AGGFPLWVTT GEYGALRNDD ERYTQAWTPY WAEISKIIEP
     HLITNGGNVV MFQIENELNG QWKNIPNRVL NPPIANYMQL LQDSARENGI DVPLSHNAPN
     MRGYSWSKDF SDATGNVDVV GVDSYPSCWS CNLSECTGTN GQYTPYLTQN YYDYFTVQSP
     SQPNFMPEFQ GGSYNPWGGP EGGCPSDIGA DFANIFYRDL IYQRVTAISL YMMFGGTNWG
     WLACPVVASS YDYSSPVSEN RIIGSKFYET KLLTLFTRVA KDLTKTERVG NSTSYSSNSA
     IVVGELRNVD NDAAFYVARH AYSPSNTNEA FRLSVNTSEG QLTIPQHGSS IAINGHQAKI
     IPTDFSFGEK TLLYSTAEVL SYIVVDGREI IALWLPEGEA GEFVVTGATS AEVVGEGNVG
     DFQTFAGEGN VTVAYTQKKG ITVVDLGDGS RAVLLDRSAA YLFWVPTLDN DVSAPANKTV
     FVQGPYLVRA AAFNETGRTL ALSGDADRET TITVFASESL CGLTWNGEKL EIASREGNVF
     TATVKGPAGF DIPALGPWKV HDSLPEIATD YEPTSDSWVD ATKTNTSNTV KPASNNPVLY
     VDEYDIHVGN HIYRATFSTT ENPPTGVFLN LTGGLAFGYS VWLNSDYIGS YLGLSYLGAD
     ARSFSFANAT LAEGDDGTNI LVVVMDNSGH DLREAALAPR GITNATLLGP AAAAGGYAFS
     GWKIAGTAGR NDLIDPVRGP INEGGLYAER IGAHLPGFPA DTWEPLASSN TTLSVPGAGI
     RVFRTVVPLA VPSGLDVSIS FRLTAASDTT FAPMEGGYSN RLRALLFVNG YQYGRFNPHI
     GNQVHYPVPA GVLDYGGDNT VAVTVWSQSA EGAELKIEWR ADYVHTSSFD MSFDGGGLRP
     GWDESRLRFA
//
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