ID A0A016VJD1_9BILA Unreviewed; 1150 AA.
AC A0A016VJD1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN Name=Acey_s0009.g401 {ECO:0000313|EMBL:EYC26873.1};
GN Synonyms=Acey-aman-2 {ECO:0000313|EMBL:EYC26873.1};
GN ORFNames=Y032_0009g401 {ECO:0000313|EMBL:EYC26873.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC26873.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC26873.1}.
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DR EMBL; JARK01001345; EYC26873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016VJD1; -.
DR STRING; 53326.A0A016VJD1; -.
DR Proteomes; UP000024635; 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; cd10809; GH38N_AMII_GMII_SfManIII_like; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000024635};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT DOMAIN 522..602
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT COILED 25..91
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1150 AA; 131105 MW; 3353E3FA341C68F3 CRC64;
MCLYLYHSID TRSIPSESLH HEKTIANMKM NIDQLQNVLK NNRDEISELK KQVADVERRR
NQDWAKQVEK ENEVYDEKAE AEKALEKKVE QIAGDANHKA VEEEEKAVVP EPNRGNKVAI
VHEILKKITT KSSLPVCEMR KDYTNTHTDV QMLDVYNLLT FDNPDGGVWK QGWEVVYDKE
KVAEEKKLEV IVIPHSHCDP GWIKTFEEYY HSQTRNILDL MVKNLYDNKN EMRFIYAEIS
FFELWWQDQT DDVRAKVKQL LASGQLEIVT GGWVMTDEAN SHYFSIIAEL LEGHEWIKNH
LGGFRPTSHW SIDPFGLSPS IPYLMSAANI TNAALQRIHY SVKKHLAKNK QLEFMWRQLW
GSHGRPDMRT HVFPFYSYDV PHTCGPDPKI CCQFDFRRLP GLGHSCPWGI PPEKITENNV
KERAFALYDQ YRKKSQLYKT NVLLVPLGDD FRYDIDAEWT EQYQNYMRLF EEMNKNTEWN
VHARFGTLSD YFTELDRFLR TEQQLLPVFS GDFFTYADRD DHYWSGYFTS RPFYKQMDRV
LQHQLRAAEI AFSLKAMKGE SPTDEVFAKL VLARRALSLF QHHDGITGTA KDHVVVDYGN
KMLAALEATE KVLSEALSAL ISAEVGSTNN LVLDEYRKEQ DTMPVRRSYA IGDFVVLFNT
LSRSRVEPTC IYVTSVHAML KVDSDREIKQ QISPVFVYND GSLTQSSDFE LCFVDELGPF
GISVYEVVES STNEQISTPT ITAKDDIKIS EFKFNRVSGS DFSLANSLFS AHFDTKTGFL
KSVTPNDHKE IEVDLHYVHY GARGHKQLNS GGGDDLSGAY LFLPDGEAKE IPRMDQQFVV
IDGPIMKRVI VAGPPDLKIL QVYSIAYGSP SIEVINEVDI RSKANFELAM RLNTNVQSGD
DLFTDLNGLQ MIRRKRLLSK LPLQAHFYPM SASAYIEDSS TRLSLYTAQA LGVASLKSGQ
LEVMLDRRLN QDDGRGLFQG VFDNHRTLSR FRLLVEPLAS DKVNTADERV GFHSVVGLAQ
DMELLYPTVR MLTKAQPNTE TIGGISQSLP CDVHIVNLRT IAGATNYGGN GMSTPKNEAA
LVLHRPLTDC RSKLQLQSDC MKQENTITPK KLFPNLRSTS EVSLTLLYEG KATDAVALQP
QDVTSVKLTW
//
