ID   A0A194QC72_PAPXU        Unreviewed;       895 AA.
AC   A0A194QC72;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:KPJ03138.1};
GN   ORFNames=RR46_06296 {ECO:0000313|EMBL:KPJ03138.1};
OS   Papilio xuthus (Asian swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=66420 {ECO:0000313|EMBL:KPJ03138.1, ECO:0000313|Proteomes:UP000053268};
RN   [1] {ECO:0000313|EMBL:KPJ03138.1, ECO:0000313|Proteomes:UP000053268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPJ03138.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPJ03138.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ459193; KPJ03138.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194QC72; -.
DR   STRING; 66420.A0A194QC72; -.
DR   Proteomes; UP000053268; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
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:SF133; ALPHA-GLUCOSIDASE; 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.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        45..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          331..679
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          685..771
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
SQ   SEQUENCE   895 AA;  102886 MW;  A4489041B1427578 CRC64;
     MIPRAEDISQ DSKDKKDEND LIYEYENIKQ ITWYDQLLLN RPLKVVLIVL LVTIAAPLLI
     YQFWFFPSVD APPADGYSTG SCLLQREIRL ACGIGTMNEL NCHPQCCYDV RNRFCFHRLP
     SRFSYILDRE WSENVTLQPR ISTTPYSLQN SIPNLRISVD EITPTHLTLN LYNPQLTTYS
     GSRIENKDYN YSISSPELNI VVNSLQGNIF NTLRGPMIAS RNIWEIAFKI TNESMYGLGE
     IPLKAGTVKV IYNHDQGISS IPLIFAKINE SYHGLLLDSS TPTEVSILAE NQIVVRGITS
     FGLRFHLFTG PKPEHVMRDV MNYIGTFNNF DYWMFGPHIC SVYPGPIDNA FTQFNTFMNS
     VSRQRLPFES TCGPIPIVFK SDHCDNSEND IINRGLRLIR RFNKRFVPHL SPYIRHEVNT
     TIDEEEIDNS TRSCGSTISR YERYLLRDSN NLDPYIGTIG NDSVVYPDYG TITEELIKDL
     WIYNTDVDGI ILENNWPLDE SKKLHNETYL YLPYYNKNFE NALNRTPQWN TSLPNDGGIY
     LFKHNIYGNN FINATHSIFD KTLPKWSSSQ WMNGETVINR QNVDTSWTSL HRELIAMALG
     GISGHWYWSS PVCGDSEDFD IENHSLLCVK WYMAGTFFPI LTIHSKSTPR DPIQFVGTYR
     TYINNALNHR LNLLSYFYTT LQEGPLLRPM FYQYPEVSEL KGVNSQFNVG ENLLIIPNLQ
     PSQTHVHVWM PPGTWYEMYS GLRLNATIGD AVTMTTTDSD FLTLIRGGSI VPLQKDVKAT
     AELTRLESSF AFTIALECTI ESENTNCKAS GHLFMAQNMT IEFKADAENL YITAIGDDYD
     IFCNTTVAIW ANRIQEINIY GLDDEFNNYD NHRRILSSIN LCELKDVHEI YYKYT
//