ID   A0A0T6AVM3_9SCAR        Unreviewed;       663 AA.
AC   A0A0T6AVM3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=AMK59_8291 {ECO:0000313|EMBL:KRT79199.1};
OS   Oryctes borbonicus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC   Scarabaeidae; Dynastinae; Oryctes.
OX   NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT79199.1, ECO:0000313|Proteomes:UP000051574};
RN   [1] {ECO:0000313|EMBL:KRT79199.1, ECO:0000313|Proteomes:UP000051574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OB123 {ECO:0000313|EMBL:KRT79199.1};
RC   TISSUE=Whole animal {ECO:0000313|EMBL:KRT79199.1};
RA   Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA   Roedelsperger C.;
RT   "Draft genome of the scarab beetle Oryctes borbonicus.";
RL   Submitted (SEP-2015) 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   -!- 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:KRT79199.1}.
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DR   EMBL; LJIG01022696; KRT79199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6AVM3; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000051574; 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   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, ECO:0000313|EMBL:KRT79199.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051574};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   DOMAIN          185..260
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   663 AA;  75294 MW;  D97FAD65E95041AA CRC64;
     MASIFAQMGF DGILLGRIDY QDKQHRFYTK TPEFIWQSSA SLGNKTDIFT SIMYNTYSPP
     PGFCFDILCM DEPIVDDINS FAYNVDRKVN TFFAYLNNVT KAYATNHVII TMGEDFNYQA
     AHTWYKNLDK LILYANKRQK EGSKYNLLYS TPSCYLKAVQ DAAKGKIKWS VKTDDFFPYA
     SDSHAFWTGY FTSRPTLKRY ERFGNNFLQV CKQLYSLTDL GPEDWADLNA LREAMGIMQH
     HDAVTGTEKQ HVAFDYARLL SKGFDECEFV TRTALSKLVS GKPLPYKHEY PAPEVNFQSC
     LLANISQCKI TEASKKFVVT VYNPLSRNVT HYVRLPVTGT AYSVLDYNGN PVPTQLMPIP
     NTILNIPGRV SASTVELIFV AKDVPPLGFL SFYVTQTTGN HVMKPKHLHS IVYQSQIGID
     PDTGKVNKIK INDQLIPMDQ DFYYYRGAVG NNSNVDYRSS GAYIFRPNKT APFQISERTN
     YELFEGEIVG ELRQVFNEWT SQIVRAYKDE VFIEFDWLIG PIPIDDINGK EVITRYSTDL
     KTDSTFYTDS NGREMLQRIK DYRPTWDITL LEGVAGNYYP VTSKMVLQDP HRNLEVAVLT
     DRAQGGTSLN DGEVELMLHR TCLHDDAFGV DEELLEKAFG TGLVARGSHY LIAGPISGTE
     GNE
//