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Database: UniProt
Entry: A0A0N4ZBQ4_PARTI
LinkDB: A0A0N4ZBQ4_PARTI
Original site: A0A0N4ZBQ4_PARTI 
ID   A0A0N4ZBQ4_PARTI        Unreviewed;      1039 AA.
AC   A0A0N4ZBQ4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-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   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000496300.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000496300.1}
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}.
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DR   AlphaFoldDB; A0A0N4ZBQ4; -.
DR   STRING; 131310.A0A0N4ZBQ4; -.
DR   WBParaSite; PTRK_0000496300.1; PTRK_0000496300.1; PTRK_0000496300.
DR   Proteomes; UP000038045; 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   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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   DOMAIN          379..465
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1039 AA;  120762 MW;  E7F9789A7F9A191F CRC64;
     MIKYSIPTSD KQMFKLYDEI DFKNYSNNFF HSYYDINYEK NNEKDMRQLN VYIIPHSHCD
     PGWLKTFEDY YNDDVSSILS GMLKHLNDKK NTIKFVYAEM SFFELFYSTL NKEKREIVEN
     LLNNNKLEIL TGGWVMSDEA NSFFVSQIVE LFEGHEFVKN QLNYIPKNHW SIDPFGLSPT
     MAYLIKQCGF KHMAIQRVHY IVKEYLAQNR LLEFQWRQLW SGGYGSTKND TDIFTHVFPY
     GSYSYKETCG PNKYICEEIS DRIINGYEFY PNKSDIIKND SLILADQFRK KSLLFKGSNI
     FVPFGDDFKY RLEDEWVNVN KEYTLIMNEI NKNKDLKMNV QFGTLNDYFK KNDENLIEEK
     INISTVSGDF FTYADGDQDY WSGYYTSRPF YKRFDRVLMD ALRTAEIIFG NVLSKIEKNE
     QNLFLQNIDY NKLVYARRAL SLFQHHDGIS GTSKDFVVID FGKKMFKAIQ YCYEIIEKCV
     QYGLDGYISD HAKVSILNKV NSFNKSSRVN AITINNNIII FNPLSRDVKR ELICTKVKSE
     KLFVIDGIDI NDQEVHPNIK MEKKNNIIRV SSESYILCYI TSIKAFDIKI FKLIDLEKSL
     VKVKMAKIYT SDVMIETNHL FSKYINISTV ANNSTFIFSK IHGVSINTKT GYIKSIGNYP
     VSYDFVYYSM KQHGPKSGAY LFHPAGKPKK LNSNENTYII TQGQLYNKAI VIGPEKIKLL
     HKIECKISSP EYVDISNSVD ISRRRNFEVA MKIKTNNEKN DMMIKNGNVF YTDLNGYQII
     KRKRLKSLPI QGNFYPMPST TFIQDNYKRL TLLSNQPLGC SSQEEGSIEV ILDRTSSYDD
     NRGLGSGVID NIQTVSKFRI LIEDRKNKFV KIDNMFNFEG KIGTGYLSKN ALMASQSLHY
     NLIQMEASKN IKDENNQFSF LKNELPLNIH IVYLRTSSDI VDYGNGGEPD NEYIRNKRQP
     VRNAALILQN IIFDGTVGVE ETCGAIKYEL SINNYIKDGR IKSYQDSSLT LLYNLGNQTT
     DKNVIIRPME LKTLKIHFN
//
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