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Database: UniProt
Entry: A0A2A2KCJ3_9BILA
LinkDB: A0A2A2KCJ3_9BILA
Original site: A0A2A2KCJ3_9BILA 
ID   A0A2A2KCJ3_9BILA        Unreviewed;      1402 AA.
AC   A0A2A2KCJ3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-FEB-2019, entry version 8.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PAV71736.1};
GN   ORFNames=WR25_20793 {ECO:0000313|EMBL:PAV71736.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV71736.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV71736.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV71736.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual
RT   nematode.";
RL   Curr. Biol. 0:0-0(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|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:PAV71736.1}.
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DR   EMBL; LIAE01008931; PAV71736.1; -; Genomic_DNA.
DR   Proteomes; UP000218231; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
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; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR010905; Glyco_hydro_88.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR008000; Rham/fucose_mutarotase.
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   Pfam; PF07470; Glyco_hydro_88; 1.
DR   Pfam; PF05336; rhaM; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000218231};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218231}.
FT   DOMAIN      446    621       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
FT   COILED     1042   1062       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1402 AA;  153608 MW;  C2EE9CB1488B7536 CRC64;
     MAEEYRRRHD AIWPDLAEAL REAGIYDYSI FLDEETNVLF AVLRLHPDDK RDALPAKPVM
     QRCLAAALLL AGATAPQIAP PTEVPRVTFD SRSLRIDGKP TLIWSSEFHP FRLPSPDLWR
     DILQKMKASG FNTVAIYIDW GFHSPKKGVY DFTGIRDIDR LLSMAQEEGL YVITRAGPYV
     NAELSRGGFP GWLVNQPGKA RTDDPEYLAA VDEWLDRINP IIARHQLGRG GSVILHQIEN
     ELALTTPAQS RYMQHLYDKA RADGITVPMF HNDQGRNGYW VPKSSGVPLT VPGPQELYAF
     DGYPGGVCGV DNKPTRGAPA PDWGLYGPGG AKGGASASPN TPGFIAEFGG GWFDYWGSNG
     MYPCNAIQRG SGYQRVFYGT NIANGIAIQS IYMGYGGTSW GWLPAPVVYT SYDYGSAIDE
     ARNLRPKALE LKQIGQFLAA VPDLARLEKA PPVAITGSEA VQVYHDRNPD TDARLLFVAP
     KPSNATGDAR FTITADLPDG RYSFASELHG RDAKLLVAGV NLERQRLVYS TSELQTTIRH
     GAEDVALFYG RAGEPGETVL RYTSAPKVTV IDGQVSSAFD AAKGDLRLTY IHQGLARVRI
     EGGGRAPLLL LIGDIAAGQS FFRQDGLLER GPALVRHATV RGATLDLTGD TETATPLEVW
     GPVRSVRWNG QSVSVTHSVS GSLIARRPLP APQPLALPDL TAATWRYAEG SPEARRDFDD
     SAWATAGSAR NVATIRPPTG QPNLGADSYG FHDGDVWYRG RFTGSADAQT VTVHYGAGGA
     GMLQLFLDGK LIGQHELAGG LPRPITTGVA EFPLPPEAQA PGEHVLAAMV RVNGHNWDLD
     VDDAHKEPRG LISVSLARPG GDSFAVPIAW KIQGRVGGED LKDVARGPSN NGGLYGERMG
     WPLPGFPDGA WAGRKLADAR PYTGTSWYRT AFDLSVPKGD DATIGVQIGD PTTPRSPGRY
     RVLIFVNGWN MGQFVANVGP QRVFPIPDGI LHHRGRNTLA LAVTSDGAPG NAIEPVKLVT
     LHHAHGGVAT LPVAALNHDI PRAEVTAQIA KLIDNLVNIK DETGEFLLRL EDGRVIDTKG
     WNDWEWTHGI GLFGLYRYWE QTGDQAAWDV MLKWFEDRFA AGTPTKNINT MSPFLTLANL
     YEHTGDQTYL PYLDIWAEWL MADDGLPKTE EGGFQHIVFN DENPQEMWDD TLMMSVLPLA
     RIGQILGRPH YIEEAKRQFL IHIKYLFDRQ TGLWYHGWTF DGRHNFAGAL WARGNCWVTI
     AIPEIIEMLD LPPGDAFRTF LIDTLAAQVK TLAEHQDDSG LWHTLIVDPT SYLEASATAG
     FAYGILKAVR KGYLPRHYEA VGIKAIRAVL ANIDDKGELK QVSFGTAMGD TMQFYKDIAL
     TSMPYGQSLA ICALGEFLRT YI
//
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