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Database: UniProt
Entry: A0A162Q789_PHYB8
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ID   A0A162Q789_PHYB8        Unreviewed;      1035 AA.
AC   A0A162Q789;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-FEB-2019, entry version 16.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:OAD80706.1};
GN   ORFNames=PHYBLDRAFT_76826 {ECO:0000313|EMBL:OAD80706.1};
OS   Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 /
OS   NBRC 33097 / NRRL 1555).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX   NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD80706.1, ECO:0000313|Proteomes:UP000077315};
RN   [1] {ECO:0000313|EMBL:OAD80706.1, ECO:0000313|Proteomes:UP000077315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J.,
RA   Gutierrez G., Heitman J., Henrissat B., Iturriaga E.A., Lang B.F.,
RA   Lavin J.L., Lee S., Li W., Lindquist E., Lopez-Garcia S., Luque E.M.,
RA   Marcos A.T., Martin J., Mccluskey K., Medina H.R., Miralles-Duran A.,
RA   Miyazaki A., Munoz-Torres E., Oguiza J.A., Ohm R., Olmedo M.,
RA   Orejas M., Ortiz-Castellanos L., Pisabarro A.G., Rodriguez-Romero J.,
RA   Ruiz-Herrera J., Ruiz-Vazquez R., Sanz C., Schackwitz W., Schmutz J.,
RA   Shahriari M., Shelest E., Silva-Franco F., Soanes D., Syed K.,
RA   Tagua V.G., Talbot N.J., Thon M., De Vries R.P., Wiebenga A.,
RA   Yadav J.S., Braun E.L., Baker S., Garre V., Horwitz B.,
RA   Torres-Martinez S., Idnurm A., Herrera-Estrella A., Gabaldon T.,
RA   Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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; KV440971; OAD80706.1; -; Genomic_DNA.
DR   RefSeq; XP_018298746.1; XM_018443192.1.
DR   GeneID; 29004098; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000077315; 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; 2.60.120.260; -; 2.
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; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000077315};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:OAD80706.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077315};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     31       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        32   1035       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007838500.
FT   DOMAIN       58    431       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      896    988       BetaGal_dom4_5. {ECO:0000259|Pfam:
FT                                PF13364}.
SQ   SEQUENCE   1035 AA;  117574 MW;  B6A4ABEC82D1CDF7 CRC64;
     MSDMTPIYSF FAILPLLLSA FVLFCHQRTH GTLNITTESV AYDRALYNTT LDWNKHTLIV
     DGEETMILSG EFHYWRVPDR SRWEPILKQY KSAGLNTIRI YFHWGYHSPD ENIYRFDGNR
     DIDHLLGLCE RLKLFVLAAP GPYICAETQA GGYPAWLIAK RELNIRHNAM MLWRTYDPMF
     AAYEVQWLQA LLPIIARHQV TTNPRGCVLA VQIDNELFEK MAGILPVGLR DQMRVLAKAS
     RDAGTTVPLF TNDGFEEGGW VPRPENAGKG GWWDSNQFGI DLYGFDKYVV FAPSSSPKSW
     LIDGDYSLSE WGTWDPKSIE HSIDKLEKTV RGFGGGAKES PMFIPELQGG WFNHYQLKHT
     YDQIYDFFGD QYTKTLFDST LAQGVTMANV YMIYGGTNWG ALGDPDVYTS YDYSACIREF
     GKMSMRGRNL RKTLLFAQSF APYFSKTERV NPSASSSVEN TINTQRVAVG ADQPVEFTFF
     RNFDRKQRTT FDVTHSSPSG VFTLECKLAY KTSFIGLGQY TAQNGLRLLL STLPIHLRMV
     HPDTNEEIWI VEPNEVGSLA FESSEIQVSG NMQNNVLHRE GPASILSFTK QTGHTTLTTL
     KGRLHLIGLL PEQVSTLFAD FEAGHWNPDK QRSMPVVAWG ADTFYYNHHE KTLEVQYDRS
     QDTVNVISFK KPTDKRMRAL VAPDALPFVH SFVFQEHAHE QFPLPVLVLL EQWKTRAVDF
     RGMKWHALLT NNNKPVWDSL DYLYTSGHSL YRTNFITPSA TRPKVTLEFN ARNRATVLVN
     GRIVGGHTTY SRQLFSPGAK IGPDPWFLGT HTYDLSPYVN RQDNLENEVI VLVDSFGLNR
     QAFIMNDVRN PRGIINARLN GINSTAVWEI TGVDVRLLDQ PYNTTGFPDE NTEAVWSSTH
     TKIVAADKKY SFLVKASDGP FWVRTKFDHG LKNAVDSLSV PLRLHLDGTM TANVFLNDVL
     IGRYYGNGDG PQHDFYIPDG LVHKDGNELK MLIYSWEDTE AHVSIEGWPV DPDSGNLVQD
     GSVEEYMVWK DSILL
//
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