ID   A0A0N4TQN4_BRUPA        Unreviewed;      1104 AA.
AC   A0A0N4TQN4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=BPAG_LOCUS10876 {ECO:0000313|EMBL:VDN92062.1};
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0001091401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BPAG_0001091401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN92062.1, ECO:0000313|Proteomes:UP000278627}
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}.
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; UZAD01013203; VDN92062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4TQN4; -.
DR   STRING; 6280.A0A0N4TQN4; -.
DR   WBParaSite; BPAG_0001091401-mRNA-1; BPAG_0001091401-mRNA-1; BPAG_0001091401.
DR   Proteomes; UP000038020; Unplaced.
DR   Proteomes; UP000278627; 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:SF69; 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; 2.
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:UP000278627};
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        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          432..513
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1104 AA;  127960 MW;  F74F48BB35D6DCF0 CRC64;
     MAKIKITPFL SAHTKRYVFM AGFCVFFIFL IEFRIILLTI SFIFNLLKFD DEEQSDGATF
     QCTQTYPIKT KTEFNTFDVL QQIIGLRQKS KQHYTVRKKS ILDVTEVYVL PFTHVDPGWL
     RTFNNYLNDT NAILDNMLVF MQNHPRMRFM WCEIVFLERW WIKQNESVKS LTRKLIENKQ
     LEIVSGSWVM TDEATTYFPS IVDNIIEGQQ YVNNELNVQA EVMWSNDPFG YGPSVPYLYT
     KTGVKRGVIN RIHHGLKAFL RYHGAIPFRW QQFFDVNDEN EMYMHVLPYS HYDILNSCGP
     DPDVCCQYDF KRINHFTCSN AAPVPITDSN IRKRALKLEK AFLKMSLQQG SNIVLSVWGD
     DFRYAELEEW YQQYDNLILL FDYINKNSKR TKIRFGTLME YFDALERSNK IKNIIPATLS
     GDFFPYQCSA GDYWTGYYTT RPFYKRQERE LHSFIRASDL LTANALINLS TKSRQIIQQQ
     LTIARRNLAL FQHHDAITGT SKNHVMKDYS ERIFASIKIA ENMLRISLNA LLRSNNFEID
     NIPLVYNESS SKKMVIVEQP RTILIYNNQP HGRMELIELQ ISDPNVVVIG TNGPIQAQIE
     PYFDTVSGKL TKSYLLVFSA YLKALSFVHF TIQKNHAATT EITQILTPLK SLRMTKYISS
     NFHVKTISKN EFFLQTQRIL VELNPKNGLL EVPPTETLLR LLLASAKVVF NKDSPSLKAR
     GDVYKEQERK RSREIIAIPD PDHEGFSRDG TKRLRCKQEF SYYKSIFSGA YIMALQDAEV
     IKLKMTEAET FIVSGPLRQI AYTLSRFVKQ RLSVNNISGA EENRLHMQLR IDIRKMSDAE
     LVTKFATDMI ADDVEYYTDS NGLQLIKRAE YDASNRPEMN YYPMPTAMIL QDRSKRLSVL
     SNVPHGVRTF NKINLEIMLD RRLSTDDGKG LGFNDDGLPV DNLPVNMAFT FVIEQMTVAD
     NKQQRQQRRF AYNTLNAHLA LQSLIYQPNI FIISGILENS PLYHLQSLPC DVQLLTIRPL
     TYDINRRLMI LHRAGIDCTT LNSSICHGNE LDSALKKLMQ SFGVTTVQKT LLNGIKQISE
     EMPYQMMTFI LEPADFATYL IRFN
//