ID A0A182UAA6_9DIPT Unreviewed; 1139 AA.
AC A0A182UAA6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
OS Anopheles melas.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC016781-PA, ECO:0000313|Proteomes:UP000075902};
RN [1] {ECO:0000313|Proteomes:UP000075902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
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 melas CM1001059_A (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEC016781-PA}
RP IDENTIFICATION.
RC STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC016781-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 AlphaFoldDB; A0A182UAA6; -.
DR STRING; 34690.A0A182UAA6; -.
DR EnsemblMetazoa; AMEC016781-RA; AMEC016781-PA; AMEC016781.
DR VEuPathDB; VectorBase:AMEC016781; -.
DR Proteomes; UP000075902; 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; 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; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR041566; AManII_C.
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; ALPHA-MANNOSIDASE 2-RELATED; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF18230; Glyc_hyd_38C_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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 498..578
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT COILED 40..67
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1139 AA; 130150 MW; 59B775E9F4C00AA3 CRC64;
MVRIRRKFAF ILCGVTLFVF LILYVVLNYS VPERARVQDI TYLENKIKQL ENGLSKHRQE
FGDIRKQIDT IRGAVDGGDD AYADSKILDK APLLGDREMM KESVINANGG GAGTCALRTD
IIPQPDVQML NLYEQVSFEN IDGGVWKQGW PIKYHPSEWN SHHKLHVFVV PHSHNDPGWI
QTFDEYYERS TKNIFANMLR HLDENAGMRF IWAEISYFAQ WYDKLVAEQK DIVKRLVKKR
QLEFVTGGWV MPDEANSHWY SMLLQLTEGQ TWLQTRLNVT PVSSWSIDPF GQSATMPYIL
KQSGFENLLI QRTHYIVKKN LALKKQLEFR WRQLWDTRGD TDLFTHMMPF YSYDVPHTCG
PDPKICCQFD FKRLPSMGLS CPWNVPPKPI TDQNVAERAE MIVDQWRKKS VLYRTRNVLI
PLGDDFRYTT SSEWEAQRVN FEQLFNYINN EPSLNVEAKF ATLQDYFDAV RATSGSSGME
QFPSLTGDFF TYADVNQDYW SGYFTSRPYH KRQDRILLHY IRSAEMLHAW NVWEPDSDWK
PLAERLEYAR RQLSLFQHHD GITGTAKDHV MEDYAKRMSR AIEDCKFVMQ QSVYRLLTKP
SVYQPDPAFM YLSIDDSRTV NGSDNVRPTI ILGEELPSKQ VVLHNSLPYT RSEVVEFYVA
SPFVTVLDGN GGTVPSQIAP VWSWHTRPDS ISQPQPSNTK YRLLFRANVP PLGLSVYTIN
SKNNAEESLG VTYTKVIILS KSPFTVNLAA GYPEDIDHAS PTEMSLRFEE GGSTSAAFTS
KGLLKSLTIE NNQATVPVHL EFYRYGMQLS SGKSGAYLFH PAGNATLMTY DQPIVLVMKG
PLETSITAGL PFAVHQTILR DDSVEIRNLV DIGQRDNTEI VMRLQTNINS GATFYTDLNG
MQIIKRKRFQ KLPIQANYYP VPSTMFIEDD NYRLTLLGGQ PLGGSSLSSG EMEIMQDRRL
TRDDDRGLGQ GVQDNLPVLH LFRLVLESRE SCTKPDPDYP TGFLTLPAHA QLQSLLHPLD
KLIYNENDWT GVQMEGFGSR HEPLEQGLEV VAIRQLSHVH FGRTSGALPV GLIVHRTNFE
DCGSEANMEG MLNIKKLLNL DDEHDIYSAR LTLLKPLELV PSDDISLCPM DVKAYIVKR
//