ID A0A182MB09_9DIPT Unreviewed; 1046 AA.
AC A0A182MB09;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
OS Anopheles culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA013891-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA013891-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA013891-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 EMBL; AXCM01004170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182MB09; -.
DR STRING; 139723.A0A182MB09; -.
DR EnsemblMetazoa; ACUA013891-RA; ACUA013891-PA; ACUA013891.
DR VEuPathDB; VectorBase:ACUA013891; -.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000075883; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 352..428
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 993..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1046 AA; 119633 MW; 7DF0640604CA3DC5 CRC64;
MNTKTVNIYF SKANNSTQPF QSCPKPKKNM LNVHLVPHTH DDVGWLKTVD QYYYGSKTTI
QKAGVQYILD SVIQSLLSDP ERKFIYVESA FFFKWFNEQT VELQQQVRML VDEGRLEFIG
GAWSMNDEAA AHYHSVVDQF TWGLRKLNET FGECGRPRIG WQIDPFGHSR EQASLFAQMG
YDGLFFGRLD YQDKRERMTH KRAEMIWKTS ANLDDADLFT GVLYNLYQAP PGFCFDILCS
DEPFMDGAYS AENNVKAKVD KFLYYVNLQA ESYRTNNIVL TMGGDFTYMD ANVYFKNMDK
LIKYTNARQT NGSNVNVFYS TPSCYLKALH DVGITWPTKS DDFFPYASDP HSFWTGYYTS
RPTSKRFERV GNHFLQVCKQ LTTLAPTREP HMEPHLNILR EAMGVMQHHD AITGTEKQHV
ANDYARMLNV AVKACSANTK AVLNQIVDPK YKRSLRAAGL PIEHVTPYPE YTFAFQSCHL
LNVSKCELTE TKDSFTITLY NPLAHAGHEY VRVPVTGGRY IVRDYRNVEV SSQLVPIPES
VLNLSYRFSN ATSELVFLAN ELPPLGFKSY FVTRAIDSLD DFLHEVPAAV PASADQPEGP
PTTHWQSEEV TIGNKYLNVS FDSNGFMSSI TIDGVTNRLR QTFVYYEGAL GNNEEFRNRS
SGAYIFRPNG TEKTVTENVQ LKVVKGPTVQ EVHQVFNEWM SQVVRIYADE SHVELEWMVG
PIPVDDGVGK EIVSRFYTAA QSSGVFWTDA NGREMIKRVR NHRDTWDLDL MEKISGNYYP
VTAKIALEDE NLRLAVLNDR AQGGSSLEDG SLELMVHRRL LHDDAFGVEE ALNEKAFGKG
LVARGKHWIV FGAKKPVSPT PEARERFLQN RVLLPNWIFF SDVSEFKYED WQKQYTNIYS
ALSLSLPLNV HLLTFEPWTD NSILVRFEHL LEKGEDPLYS KPVRFNVQDV FRQFSIEEIR
ETSLGANQLK EDSKRLKFKP DPDYIVYSSV KRDVSGEHPS PSPPNVQSGS SPLLQNLERD
GGDDGYEILL KPMQIRTFIF QLEYKP
//
