ID   A0A0K0ELU2_STRER        Unreviewed;      1087 AA.
AC   A0A0K0ELU2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0001043000.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0001043000.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361199};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
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DR   AlphaFoldDB; A0A0K0ELU2; -.
DR   STRING; 6248.A0A0K0ELU2; -.
DR   WBParaSite; SSTP_0001043000.1; SSTP_0001043000.1; SSTP_0001043000.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR011682; Glyco_hydro_38_C.
DR   InterPro; IPR015341; Glyco_hydro_38_cen.
DR   InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR   InterPro; IPR000602; Glyco_hydro_38_N.
DR   InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF3; LYSOSOMAL ALPHA-MANNOSIDASE; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF07748; Glyco_hydro_38C; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 1.
DR   SMART; SM00872; Alpha-mann_mid; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW   Hydrolase {ECO:0000256|RuleBase:RU361199};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          421..507
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1087 AA;  127759 MW;  1C76F412DBA89742 CRC64;
     MKYKYNSLNT INTKFYKKCL FFIFIPIVIF IYLYLYFYLP PKQIEYEINN LYFKPQNDEQ
     MLKIYSNISF NKYLEIEKKN YYDVTYNKND MKKINVFLIP HSHDDPGWLK TFEKYYNDDV
     SKILYGMLEY LSKNNEMKFV YVEMSFFELF YSTLSLSNRQ KVKKLLLSEK LEIITGGWVM
     SDEANSHFFS QITELFEGHE FLKNNLQYIP KNHWSIDPFG LSPTMAYIMK ESGFKHMAIQ
     RVHYMVKQYF AEKKLLEFQW RQLWSGGYKN ESQKTDIFTH IFPYGSYTSS ETCGPDKNIC
     DKFNFNKLSN NIISNNDMLE KNVKLIADQF RKKSLLFRGP NIFIPLGTDF SYSNNNEWKN
     VYENYKVIIN NINNSPELNM HVQFGTLNDY FNANDKSINE ENIHIPIITG DFFTYSDRNE
     EYWSGYYTSR PFYKRFDRIL MNYLISAEII YSSIIGKIKS NEMNEFLKLI DYNKLVYARR
     ALSLFQHHDG VTGTSRYDVV LDYGKKLLKA IKNCYLIIEK SIEYDMKKEF FNNTISNNNI
     FNNITSNNNI QVSILEKING TTRMPEIKSI NINKNILIYN VLSKNFDKEL LCTKIENEEI
     FIIDNIDIKN QEIHPIIEKK NNTLIISDKS YLLCYITSLK AFEIQILKLV SSNMFNKKPN
     IAKIFTSKKN IKINKIFNNY EEIIMDNNNF IVSDIHGLKI DKKTGYVTSI NNSPVSIHFE
     YYVETKSQPN SGAYLFTPEG PSKLTNNLNN FYIISKGKIR QEIVVIGPIK GKLIHSIETC
     ITFPYYIDIN NIIDLSNEEE IEIVMKIKTN NGDKNKIIKN RNVFFTDLNG YQIIKRKRLN
     KLPIQGNFYP MPSTIYIEDN KKRLTVLGNQ ALGCSSQEEG SVEIILDRRH FNDDHRGLGH
     GILDNIPTKS KFRILMEDNH IFNYDDQSVT GYLSGNAFIA NQKLQYNIIQ MEVNKNINYK
     LSILKDEFPA NIHIVTLRIL TLPENYGKGG EPDYEYNRIR RKPLKSAALI LQNIGYDKNI
     GENLSNILNI KNGEIYINDY IKNDLIDYYE ECSLTMLYES KNYTNNGYIN IKPMELKTLK
     VNFNKGD
//