ID A0A0V1A4J5_9BILA Unreviewed; 968 AA.
AC A0A0V1A4J5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Sucrase-isomaltase, intestinal {ECO:0000313|EMBL:KRY19404.1};
DE Flags: Fragment;
GN Name=SI {ECO:0000313|EMBL:KRY19404.1};
GN ORFNames=T12_15906 {ECO:0000313|EMBL:KRY19404.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY19404.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY19404.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY19404.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00779}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY19404.1}.
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DR EMBL; JYDQ01000036; KRY19404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1A4J5; -.
DR STRING; 990121.A0A0V1A4J5; -.
DR Proteomes; UP000054783; 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 CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR CDD; cd14752; GH31_N; 1.
DR CDD; cd00111; Trefoil; 1.
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; 2.
DR Gene3D; 4.10.110.10; Spasmolytic Protein, domain 1; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
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 InterPro; IPR000519; P_trefoil_dom.
DR InterPro; IPR044913; P_trefoil_dom_sf.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF168; P-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR Pfam; PF00088; Trefoil; 1.
DR SMART; SM00018; PD; 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; PS51448; P_TREFOIL_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361185};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 43..90
FT /note="P-type"
FT /evidence="ECO:0000259|PROSITE:PS51448"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY19404.1"
SQ SEQUENCE 968 AA; 110488 MW; 3388123AF03304AE CRC64;
LKRMNTQELL KRRWVPYALL AFAALVILII LLAVYVPSGT QLPELEQIDE QVRVDCHPDP
NPTEDACHRR GCVWLLATGN WSAPSCYYPT SFGYAVTSEQ PGLLTLTRRE ILGEVSPLSK
PVKQLQVQYE FFNDQIVHVK ITDATVARYE VPVPLWPKGK PQAQISSNRL QFVVLGNHPT
FAFAIHDQQR TLFNTSIGGL VYADQFLQIA TYLSSWNLYG FGENLHTNLK HDLSTFRTWP
MFSRDQPPVA DPPTAGNLYG VHPFYMQMND DGSSHGVLFF NSGAQEYTTG PGPSLVYRTI
GGILDMYFFV GPQPGQVIQQ YQTLIGYPAM PAYWSLGFQL CRYGYHNTSE VEELVKRMRA
LEIPQDVQYV DIDYMDKNKD FTIDSENFKD LPELVNKTKE NGLRWIFILD PAINVASEQY
PAFHQGKQSN VFVTWPDEKY VPPLNANYTT TVGTKIMLGT VWPFDNVAFP DFLNPKTHSW
WKQQIVTFHN VLNFDGIWID MNEPANFGTN EDTPWYVIDP NLKHLQQLRC PNNTYDTPPY
ATQAAYYWKT TLNDKTICMI GEHSDGVRKY RHYDVHSLYG WSETKPTIEA VQKATGKRGV
VITRSTFPTS GQFSGHWLGD NFSKWADLAA SIIGILEFNM FGIPYVGADI CGFEEDADEE
MCARWQQLGA FYPFSRNHNG KNRRSQDPTQ WQSVAEATKA SLKLRYYFLP YLYTLFYKAH
TKGETVVRPL FFEFPNDPNT HHIDKQFLWG PAVLITPVLQ AGVVHTEAYF PTAQWYNVYE
AEIAGALQQP GRVTISSPRY GCVPVHVRGG YILPRQKPAL NTRDSRTNPL DLLITVDKNN
NTSVGELFWD NGESIMINES NSYFFHIQYI VRPTNAKIQI TVKHAPHADY LDTIALPTLD
RIEIFGAEHS VDLKAEINLD GMPISLTDSN VQFNVNLKKL IIQKDNFWDL KNSTAGQIRT
LSWQHKLR
//
