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Database: UniProt
Entry: A0A0L0C6C3_LUCCU
LinkDB: A0A0L0C6C3_LUCCU
Original site: A0A0L0C6C3_LUCCU 
ID   A0A0L0C6C3_LUCCU        Unreviewed;      1145 AA.
AC   A0A0L0C6C3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=FF38_06141 {ECO:0000313|EMBL:KNC27938.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC27938.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC27938.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC27938.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC27938.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
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:KNC27938.1}.
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DR   EMBL; JRES01000835; KNC27938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0C6C3; -.
DR   STRING; 7375.A0A0L0C6C3; -.
DR   EnsemblMetazoa; KNC27938; KNC27938; FF38_06141.
DR   OMA; GHQWLKY; -.
DR   Proteomes; UP000037069; 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; LYSOSOMAL ALPHA-MANNOSIDASE; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   DOMAIN          495..572
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
FT   REGION          65..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1145 AA;  132646 MW;  134530D99E4E1928 CRC64;
     MLRIRRRFAL VLCAVFVAIF LAVYFLINYA APAEDNKKPN FMNLDNIEAL KQKMDLPKVL
     ETNNLENNNV GEKPQRQTEH FKKSGQGVKR KEGDGDELKI EQNMISENKD DTCDFDPQQV
     PQPNIQMLDL YGKMKFDNPD GGVWKQGWNI KYDPLQYNDH HKLKVFVVPH SHNDPGWIKT
     FDDYYDHETK HILSNALRHL RENPEMKFIW AEISYFAKFY QDLGESNKQE IKKLVANGQL
     EFVTGGWVMP DEANSHWHNI LLQLTEGQHW LKKYLNVTPT SSWAIDPFGH SASMPYILKK
     SGFTNSLIQR THYSVKKELA LKRNLEFYWR QLWDDTGSTD LFTHMMPFYS YDIPHSCGPD
     PKICCQFDFK RVPNFGLMCP WKVPPQTIDD HNVAQRAELI IDQWKKKAEL YRTNVVLFPL
     GDDFRYSQST EWEVQRVNYE NLFNHINSER KYFVEAKFGT LQEYFDAVHQ EQKEKQRDFP
     TLSGDFFTYA DRNDNYWSGY YTSRPYHKRM DRVLMHYIRS AEILSSWDKW DESSKFDEML
     QDARRQLSLF QHHDGITGTA KTHVVEDYNR RMMDAIKSCR FVMQQAIYRL LTKPSIYNAD
     NNFNYFFMDD SRWPGPDDSR TTIILGEELP QKHLVFHNSL PQWREDIVDF YIASPYVSVV
     DFNNNPVDIQ ISPVWTWHKH TLTNTITPQA STTKYRLIFK AKVPPLGLST YIVKVETPET
     IKPNYITFAS NLILTKNPIT TQLGDYPKEV KFGKHREISL KVGSGPTVAF SAEGMMKSIQ
     IKESEAHTPV RVQFFKYGVR QKGEYSGAYL FLPNGFASQI TNAQQPVVLV TKGPLESSIS
     VGLSFGVHHT ILRDGEAPEI RNNIDINDMD DTEIVMRFQT RIHNDETFYT DLNSLQLIKR
     QRFTKIPLQG NYYPIPSAIY IEDDTLRLTV VSAQPLGGSS LADGEVEIMQ DRRLTHDDER
     GLGQGVLDNQ PVLHIFRVLL ERIDNCEKLA DNHPSGILTL PAYRNLKSIL DPIDKFIFTE
     NDWLGVMPEF GSSHTALGED MEIVVMRNLP ASSAIPAIAR DRKPHMQQNT GLIIHRTNLM
     QCSGLQAQNT GELNLHHLLQ WGSQNVSAVY KTNLTFLKRL SSQKIDEDIT LCPMDSLAFI
     LQRHS
//
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