ID   A0A0R3WZR5_HYDTA        Unreviewed;      1057 AA.
AC   A0A0R3WZR5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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   Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX   NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000630601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TTAC_0000630601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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}.
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   AlphaFoldDB; A0A0R3WZR5; -.
DR   STRING; 6205.A0A0R3WZR5; -.
DR   WBParaSite; TTAC_0000630601-mRNA-1; TTAC_0000630601-mRNA-1; TTAC_0000630601.
DR   Proteomes; UP000046396; Unplaced.
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   CDD; cd10810; GH38N_AMII_LAM_like; 1.
DR   Gene3D; 2.60.40.1360; -; 1.
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; 2.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199}; Signal {ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT   CHAIN           35..1057
FT                   /note="Alpha-mannosidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT                   /id="PRO_5017855467"
FT   DOMAIN          385..479
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1057 AA;  120008 MW;  A22640981F64C177 CRC64;
     LKKLHFRDLQ VGMVLHGALS LGLFLLPLLH VTLAEECGYC LCPPTKDGYI NVHIVPHTHD
     DVGWLKNIDQ YYFGDGKWYQ TASVQYILDS VMHALSLNPS RKFTYVEMAF FERWWRLQDA
     TMQELVHRLV RNGQLEFALG GWTMNDEAVV HYSDSVDQLT RGLAFLNATF GDCGRPRVAW
     QIDPFGHARQ QARIFMDAGF DGVFFQRMDY REKRRRLKDK GMEVLWKVDS IDNTTGLFTH
     MLYQSYCSPP GFCFDSKCDD PPIIVDPLAT NYNVPSRVRQ FLEYVRLVAK SYATNHIFVP
     MGCDFTYESA NENFINLDRL IEHVNAHQSQ EALRSTSWGS STKPVHLLYS SPTCYTKSVN
     EAFKKEGMMP EREGDFFPYA SASNTFWTGF YTSRPSQKFM VRRASSLLAA CEQAHIMKPT
     VGYRCKYPSR PTYDYQKGNF LEPVQVVDQL RRMVGIMQHH DAVTGTEKQH VSDDYRQRLT
     DAMYGCQQLV SSVADSLLET RSHSGGNGFK ACEYLNVSVC LPLTRKHALP DALIAVYNPL
     GWDDLRPWMR LPLHATEGEA DRLHTYTLKE YFTGETVPFQ VVTLPKAVCH LPERGMLSNK
     GHSELVFKPN VGLTPAGFTL YLLTGAASNA YRFGHQHRRR QRRISLKIGQ DNLPVFLTQE
     GQTVTMLLMN YEANTYYKPT SGAYVFRPLR EAVRIGNATS EIIDGELVTE VRTTFSHWAS
     LTARLYADDR MEVEWVVGPL PNIGRRVTEV ILRYRVTGNG ILPATEGEFY TDSMGNDLIK
     RNRVRPGKGR METLEFPDDT GYGLRYWRNW DSRESVQEHL IEGSYFPVVN RILLKGTRYA
     FGVYTDRAEG GSSLAEGELE LMLHRATIVD DGLGVGEPLN ERAFGEGIAV RGVHRLLLDT
     VARVEEMDPR IAQEVSRPPT LVFRDRGNDT LKSSPTIAPS LLTRGLPEGL HLLTVQQWPV
     EGEPSRNQLL VRLQHIGLPG IGAITMELSD AFTVGRVIKA TEMSLTANQL ADVAKRNKLV
     WPSKFERPKG VNYRGESNAT RVVIQPEEIK TLILYMA
//