ID   K9IUJ0_DESRO            Unreviewed;       972 AA.
AC   K9IUJ0;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
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};
DE   Flags: Fragment;
OS   Desmodus rotundus (Vampire bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC   Desmodontinae; Desmodus.
OX   NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA52975.1};
RN   [1] {ECO:0000313|EMBL:JAA52975.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:JAA52975.1};
RA   Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA   Ribeiro J.M.C.;
RT   "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT   and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT   Desmodus rotundus.";
RL   Submitted (NOV-2012) 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; GABZ01000550; JAA52975.1; -; mRNA.
DR   AlphaFoldDB; K9IUJ0; -.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
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   InterPro; IPR048534; Man2a1-like_dom.
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   Pfam; PF21260; Laman-like_dom; 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   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW   Hydrolase {ECO:0000256|RuleBase:RU361199, ECO:0000313|EMBL:JAA52975.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   DOMAIN          334..413
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
FT   REGION          532..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAA52975.1"
SQ   SEQUENCE   972 AA;  109955 MW;  EACC2DFF0B05A272 CRC64;
     QTCPMVQPDM LNVHLVAHTH DDVGWLKTVD QYFYGIYNSI QHAGVQYILD SIISSLLAEP
     TRRFVYVEMA FFSRWWHQQT NATQDVVRDL VRQGRLEFAN GGWVMNDEAA THYGAIIDQM
     TLGLRFLEDT FGNDGRPRVA WHIDPFGHSR EQASLFAQMG FDGFFFGRLD YQDKWVRKKN
     LEMEQVWRAS ASLKPPAADL FTSVLPNMYN PPEHLCWDVL CADKPIVEDP RSPEYNAKEL
     VDYFLDLAAA QGQLYRTNHT VMTMGSDFQY ENANIWFKNL DKLIKLVNAQ QANGSRVNVL
     YSTPACYLWE LNKANLTWSV KQDDFFPYAD GPHQFWTGFF SSRPALKRYE RLSYNFLQVC
     NQLEALAGPA ANVGPYGSGD SAPLNEAMAV LQHHDAVSGT SKQHVADDYA RQLAAGWGPC
     EVLLSNALAQ LSGSKEKFSF CRNLNISLCP LSQTAKSFQV TIYNPLGRKV DWMVRLPVSK
     HTFLVKDPSG TVVPSDVVVM PSSDRQELLF SASVPALGFS IYSVTQVPGQ SPQALTYQPR
     PQKSSSHIKP LSRIKSSSRI KPSSRDLTIQ NEHIWARFDP DTGLLVEIKN LDQDLLLPVH
     QAFYWYNASI GNSLSTQASG AYIFRPNQQE PLLVSHWAQT RLVKTALVQE VHQNFSAWCS
     QVVRLYPGQR HLELEWTVGP IPVGDNWGKE VISRFDTPLE TKGLFFTDSN GREILERRWN
     YRPTWELNQT EPVAGNYYPV NSRIYITDGN VQLTVLTDRS QGGSSLRDGS VELMVHRRLL
     KDDERGVGEP LLEKGLGLWV RGRHLVLLDK ARTAAVGHRL QAEKELLAPQ VVLAPGGGIP
     YHPEVAPRKQ FSGLRRELPL NVHLLTLARW GRKMLLLRLE HQFAVGEDKG GNLSSPVTLD
     LRDLFSTFTI INLKETTLAA NQLWASASRL QWMPNTGPTL KRFPSRLDPA SITLQPMEIR
     TFLASVQWKE DS
//