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Database: UniProt
Entry: K5VXC5_PHACS
LinkDB: K5VXC5_PHACS
Original site: K5VXC5_PHACS 
ID   K5VXC5_PHACS            Unreviewed;      1005 AA.
AC   K5VXC5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   13-FEB-2019, entry version 34.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:EKM56228.1};
GN   ORFNames=PHACADRAFT_95998 {ECO:0000313|EMBL:EKM56228.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus)
OS   (Peniophora carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM56228.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM56228.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM56228.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa
RT   and P. chrysosporium, to elucidate the genetic basis of the distinct
RT   wood types they colonize.";
RL   BMC Genomics 13:444-444(2012).
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; JH930472; EKM56228.1; -; Genomic_DNA.
DR   RefSeq; XP_007396519.1; XM_007396457.1.
DR   EnsemblFungi; EKM56228; EKM56228; PHACADRAFT_95998.
DR   GeneID; 18920913; -.
DR   KEGG; pco:PHACADRAFT_95998; -.
DR   InParanoid; K5VXC5; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000008370; 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:UP000008370};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:EKM56228.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23   1005       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003885113.
FT   DOMAIN      396    568       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1005 AA;  108076 MW;  E5E56D186E4A103B CRC64;
     MTLLAFVLAA LLFLVTPHVV HTAVTDGPRI LAEPPRHSTG LTDAVQWDNY TLWIEGQRVF
     LHSGEFHTFR LPVPDLWLDI FQKMVAAGLN GVRCALTASI YIHWALTNPA PGVLDFNDWR
     DLQPVFKAAE QAGIFIVLRP GPYINAETTA GGLALWTTSL TTSELRTNAT DIEESWMPYV
     QRIINESKPN QVSDGGSLIA VQVDNEYSQS PIQRAEYFAQ LEATYTSNGI VVPLTYNDPG
     EGLNFINGTG AVDIYGLDSY PQGFDCSNPT RWSPVVTNYH SYHEEADPGT VWYMPEFQGG
     SFDPWGGPGY DACEVLTGPD FQDVFYKQNW ASNVKMISYY MLYGGTNWGG IAAPVVYTSY
     DYGSTLRENR ALSPKFDELK RQGLFLRSSP EFRKTDWIGD SSTGVSVTST NNASFVTLLR
     NPDTGAQFVI VRQADSTSTS NIAFNLTLST SAGTLTIPRT LSSGIQLDGR QSKVVLADYT
     FGSPAHSNKL LYSTAAVLFA GSIGGIDTVF LYGDTNQGHE FAFSSGSSQP TTVAFAPGFK
     TGLQVVSSPK STASPLVLWA DTQTASTFFA PAVSTGAATF TNYWQFGTNE TVLVGGPMLV
     RNATVSGSRL ALRGDLNAST PLTLLVPSSV STVSWNGANV AVKSLSGAPT LPGAKLLEGQ
     LSFSLGKGSV SVPALTGWKF KDSLPEVQSG FDDANWTVAD HTTTNITTKP LFGDGRVLYE
     CDYGFCENVV LWRGHFNGIG SETSVNLTIN GGNAFGASVF LNDVFLGTTN GSASVEQTNA
     LYSFPDGAVK TGTDNVITVV QDHMGNDEDP NERSPRGIPG FQLNSGNFTT WKVQGKLGGY
     TNYPDKVRGI LNEGGLFGER EGWHLPGFDT SSWASRSLSS GLPNDTAGVG FFVTTFNLAV
     PQGVDAMFSF VFDNNTAVPA GQAYRALLFV NGWQYGKRVA NIGPQAKFPV PSGILDHSGK
     NTVAIALWAL ENAAVSPTLE LVLDEAVEGG VGQVAVNNPA WTPRE
//
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