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Database: UniProt/TrEMBL
Entry: D2GXB2_AILME
LinkDB: D2GXB2_AILME
Original site: D2GXB2_AILME 
ID   D2GXB2_AILME            Unreviewed;       651 AA.
AC   D2GXB2;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFB15791.1};
DE   Flags: Fragment;
GN   ORFNames=PANDA_001525 {ECO:0000313|EMBL:EFB15791.1};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB15791.1};
RN   [1] {ECO:0000313|EMBL:EFB15791.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; GL192367; EFB15791.1; -; Genomic_DNA.
DR   RefSeq; XP_002913703.1; XM_002913657.3.
DR   AlphaFoldDB; D2GXB2; -.
DR   STRING; 9646.ENSAMEP00000002467; -.
DR   GeneID; 100479145; -.
DR   KEGG; aml:100479145; -.
DR   CTD; 79411; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_7_2_1; -.
DR   InParanoid; D2GXB2; -.
DR   OMA; HERQYLH; -.
DR   OrthoDB; 5489808at2759; -.
DR   TreeFam; TF314816; -.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR048912; BetaGal1-like_ABD1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
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; BETA-GALACTOSIDASE RELATED; 1.
DR   PANTHER; PTHR23421:SF50; BETA-GALACTOSIDASE-1-LIKE PROTEIN; 1.
DR   Pfam; PF21317; BetaGal_ABD_1; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..651
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015088172"
FT   DOMAIN          38..353
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          400..512
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          537..592
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        185
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   NON_TER         651
FT                   /evidence="ECO:0000313|EMBL:EFB15791.1"
SQ   SEQUENCE   651 AA;  73997 MW;  9B31321D7214F355 CRC64;
     MAPEKPLCLP ALLLPLLTLL LPQADTRSFV VDRENDRFLL DGVPFRYVSG SLHYFRVPRV
     LWADRLFKMR MSGLNTVQFY VPWNYHEPEP GVYNFNGSRD LFAFLNEASV ANLLVILRPG
     PYICAEWDMG GLPAWLLQKP DIHLRTSDPD FLAAVDSWFK VLLPRLYPWL YHNGGNIISV
     QVENEYGSYR ACDFGYMRHL AGLFRALLGD RILLFTTDGP EGLKCGSLQG LYTTVDFGPA
     DNMTKIFALL RKYEPHGPLV NSEYYTGWLD YWGQNHSMRS ILAVTTGLEN MLRLGASVNM
     YMFHGGTNFG YWNGADEKGR FLPITTSYDY DAPISEAGDP TPKLFALRNV ISKFQEIPLG
     PLPPPSPKMM LGPLTLHLDG DLLAFLDFLC PQGPIRSILP LPFEAVKQDR GFVLYRTYLT
     YTVSEPTQFW VPNNGVHDRA YVMVDGVFQG VLERNMKHQL FLMGTVGAKL DILLENMGRL
     SFGSNSSDFK GLLEPPILGQ RVLTQWLMFP LKVDKLVKWW FPLQLMKRSH PQVPSGPTFY
     STTFPILGEG RDTFLFLPGW TKGQVWINGF NLGRYWTKRG PQETLYVPRP LLFSRGALNK
     ITLLELENVP PQPQIQFLDR PILNSTLHKT YIYSLSPDTQ SASEPMELSG H
//
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