ID   A0A0R3SR13_HYMDI        Unreviewed;      1033 AA.
AC   A0A0R3SR13;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=HDID_LOCUS7567 {ECO:0000313|EMBL:VDL59885.1};
OS   Hymenolepis diminuta (Rat tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX   NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000756901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HDID_0000756901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL59885.1, ECO:0000313|Proteomes:UP000274504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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   EMBL; UYSG01010949; VDL59885.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3SR13; -.
DR   STRING; 6216.A0A0R3SR13; -.
DR   WBParaSite; HDID_0000756901-mRNA-1; HDID_0000756901-mRNA-1; HDID_0000756901.
DR   Proteomes; UP000046397; Unplaced.
DR   Proteomes; UP000274504; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274504};
KW   Signal {ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT   CHAIN           19..1033
FT                   /note="Alpha-mannosidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT                   /id="PRO_5033767784"
FT   DOMAIN          372..466
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1033 AA;  117414 MW;  F78976B1C452F223 CRC64;
     MRLHIGLWLL VLLLLVFAGG EECGYSLCPP TKDDHINVHI IPHTHDDVGW LKNIDQYYFG
     DANFYQTAAV QYILDSVIHA LALNPNRKFT YVEMAFFERW WRLQTPAMQE TVHKLVKNGQ
     LEFALGGWSM NDEAVVHYSD SINQLTRGLA FLNATFGECG RPRVAWQIDP FGHARQQARI
     FTEGGFDGVF FQRMDYREKR QRLEEKTMEV LWKVDPTNNK SSLFTHMLYQ SYCSPPGFCF
     DAKCDDPPMI VDPLATNYNA PQRVSQFLEY VRTVSSSYAT NHIFVPMGCD FTYENANLNY
     INMDRLIEHV NAQQQKERSY RTFRLPEITM PVNLLYSSPT CYTKAVNEAF KKQGTIPQRD
     GDFFPYASAP NTFWTGFYTS RPTQKRMVRE ASSLLATCEQ AHLMRPCLGS RYRYPTRSSY
     EFKDGIFQTP DQVVDQLRRA MGMMQHHDAV TGTEKQHVSD DYRQRLTDAM KGCNQLLGAV
     ADTLLGKSYS VQGGGFRACE NLNASVCPPL TSKSLHPDAL IAVYNNLGWD DIQPWLRVPL
     YATKDQLDWL SSFTLTDYTT GETIPFQVVS VPPPILTLPE RRVLHHKGSS ELVFKPNEGL
     KPAGFTLYAL KGEASDGYGK SYRYGYKRPV NQQRFSLEIG PDNLPLFSSK EGHRITMRFM
     NYDANSYYRP TSGAYVFRAL SEAIGFGNFT SEIIRGELVT EVRTTFTPWA YLSARLYADD
     RMEVEWIVGP LPQIGRRVTE IILRYHVEGP GTLPSNPGEF YTDSMGNDLI RRQRLDTEGA
     KNHLVNVVEG SRRNTWNRDS RESSRNHRIE GSYFPVVNRI MIKGVQYAFA VYTDRSEGGS
     SLAEGDLELM LHRATTVDDG LGIVVRGIHR LVLDEVSKVE EMDVRLAQEV SRPLSLFFKD
     RSNDSRSADR SAKFSILTKG LPQFLHLLTV QQWPIEGDLT PKNQLLVRLQ HIGTAAVGPI
     RFDLSGAFTL GSVTKAKEMS ITANQLVENA KANGLTWPEG HEITFKRTMS DNSTQVMLQP
     GEVKTFILDL VKP
//