ID A0A084VFG6_ANOSI Unreviewed; 961 AA.
AC A0A084VFG6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=ZHAS_00003860 {ECO:0000313|EMBL:KFB36710.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB36710.1};
RN [1] {ECO:0000313|EMBL:KFB36710.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC003860-PA}
RP IDENTIFICATION.
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; ATLV01012389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ATLV01012390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE524787; KFB36710.1; -; Genomic_DNA.
DR STRING; 74873.A0A084VFG6; -.
DR EnsemblMetazoa; ASIC003860-RA; ASIC003860-PA; ASIC003860.
DR VEuPathDB; VectorBase:ASIC003860; -.
DR VEuPathDB; VectorBase:ASIS014261; -.
DR OMA; WIYQINR; -.
DR Proteomes; UP000030765; 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 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 23..961
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5010759815"
FT DOMAIN 371..447
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 961 AA; 110011 MW; 51F2E44D390E8507 CRC64;
MVGQRLVIFG LSVFSVILAA HGSPRWYSHS ARKEAGCGYE ACPVPKEGMI NVHLVPHSHD
DVGWLKTVDQ YYYGSRNNIQ KAGVQYILDS VVQELLKDPN RRFVYVESAF MHKWYMEQTV
ELQQQVKMLV DEGRLEFIGG AWSMNDEAAV HYQSVVDQFT WGLRFLNDTF GECGRPRIGW
QIDPFGHSRE QASLFAQMGY DGLFFARLDY QDKNHRMQTR TPEMVWHTSG SLGDSDLFTS
VLYNHYSAPP GFCFDILCND DPMIDDKGST DYNVKNRIDT FITWLEKMAE SYRSNNLILS
MGDDFNYMDA IMNFKNMDKL IKYTNERQAE GSKINAFYST PSCYVKAVHS ANIDWPTKSD
DFFPYESDYH SFWTGYYTSR PTQKRYEREG NHFLQVCKQL SAIAPSKESF YEDHLTALRD
AMGVMQHHDA ITGTEKQHVA DDYARMLYXX XXXXXSSTGA TNSDNNVVLL YNPLGHSSDD
FVRLPVKEGH YVVRNDRGQT VPSTLIPIPS SVLDLPFRNS AATHELVFHA ESIAPVGYRS
FYVSKEEEQK DVSSGIATIR QEKTSITVDG ATHPLKQNFL FYEGAYGNNE EFRNRSSGAY
IFRPNGTEKA VTEVVELQVV KSELVQEVHQ IFNEWISQVI RVYAGKDHVE LEWLVGPIPI
DDGTGKEIVS RFESDVASEG VFWTDSNGRE MLRRVRNKRE TWDLDLLEPV SGNYYPITAK
LALEDDHFRM SLLNDRAQGG SSLQDGQLEL MVHRRLLRDD AFGVGEALNE TQYGAGLVAR
GKHWLYFGSS QKDVSPTLHA KERFLQNKVL LPSWTFVNPV DSVLSYDDYL SNFRNIYSAI
AQQLPPNVNL LTLEPWKDGT VLVRFEHLFE INEDPVYSQA VRFNVRNVLF ALNIESIHET
TLGANQWKED SVRLQFSMES TANEVSENVF ETENIPIVDE STDFDIELQP MEIRTFVVKR
R
//
