GenomeNet

Database: UniProt
Entry: L5KQE8_PTEAL
LinkDB: L5KQE8_PTEAL
Original site: L5KQE8_PTEAL 
ID   L5KQE8_PTEAL            Unreviewed;       966 AA.
AC   L5KQE8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Neutral alpha-glucosidase AB {ECO:0000313|EMBL:ELK13445.1};
GN   ORFNames=PAL_GLEAN10011478 {ECO:0000313|EMBL:ELK13445.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK13445.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; KB030625; ELK13445.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5KQE8; -.
DR   STRING; 9402.L5KQE8; -.
DR   eggNOG; KOG1066; Eukaryota.
DR   InParanoid; L5KQE8; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06603; GH31_GANC_GANAB_alpha; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR030459; Glyco_hydro_31_CS.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF162; NEUTRAL ALPHA-GLUCOSIDASE AB; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR   PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..966
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003969443"
FT   DOMAIN          89..346
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          409..736
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          744..832
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   REGION          210..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   966 AA;  108950 MW;  F20A9D4166840909 CRC64;
     MAAVPAVAAR RRRSRAGLVL ACLGVCLGIT LAVDRSNFKT CEESSFCRRQ RSIRPGLSPY
     RALLDSLQLG PDALTVHLIN EVTKVLLVLE LQGLQKNMTR IRIDELEPRR PRYRVPDVLV
     ADPPTARLSV SGRDDNSVEL TVAEGPYKII LTARPFRLDL LEDRSLLLSV NARGLLAFEH
     QRAPRVSFSD KVSLTLGSIW DKIKNLFSRQ GSKDPAEGDG AQPEETPGDG DKAKETQGKA
     EKDEPGAWEE TFKTHTDTKP YGPTSVGLDF SLPGMEHVYG IPEHADNLRL KVTEGGEPYR
     LYNLDVFQYE LYNPMALYGS VPVLLGHSPH RDLGIFWLNA AETWVDISSN TAGKTLFGKM
     LDYLQGSGET PQTDVRWMSE SGIIDVFLLL GPSVFDIFRQ YASLTGTQAL PPLFSLGYHQ
     SRWNYRDEAD VLEVSQGFDD HNLPCDVIWL DIEHADGKRY FTWDSSRFPQ PLTMLEHLAS
     KKRKLVAIVD PHIKVDSGYR IHEELQSLHL YVKTRDGFDY EGWCWPGAAS YPDFTNPTMR
     AWWANMFSFD NYEGSAPNLY VWNDMNEPSV FNGPEVTMLK DAKHYGGWEH RDVHNIYGLY
     VHMATAEGLV LRSGGVERPF VLSRAFFSGS QRYGAVWTGD NTAEWDHLKI SIPMCLSLGL
     VGISFCGADV GGFFKNPAPE LLVRWYQMGA YQPFFRAHAH LDTGRREPWL LPSQYQDIIR
     DALDQRYALL PFWYTLLYQA HREGIPVMRP LWVHYPQDVT TFSIDDQFLL GDALLVHPVS
     DSGAHGVQVY LPGQGEVWYD VHSYQKHHGP QTLYLPVTLS SIPAFQRGGT IIPRWMRVRR
     SSECMKEDPI TLFVALSPQG TAQGELYLDD GHTFNYQTRH EFLLRRFSFS GNTLVSSSAD
     PKGHFETPVW IERVVIIGAG KPAAVVLQTK GSPESHLSFQ HDPETSVLIL RKPGVNVASD
     WSIHLR
//
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