ID   A0A2G5CPN6_AQUCA        Unreviewed;       898 AA.
AC   A0A2G5CPN6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752, ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=AQUCO_04300016v1 {ECO:0000313|EMBL:PIA32797.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA32797.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA32797.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) 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; KZ305060; PIA32797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5CPN6; -.
DR   Proteomes; UP000230069; 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   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; IPR041147; GH38_C.
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:SF60; ALPHA-MANNOSIDASE; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF17677; Glyco_hydro38C2; 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:UP000230069};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   DOMAIN          233..307
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   898 AA;  101208 MW;  16E17D2A00A8F113 CRC64;
     MLSRNGGMCM HDEATPHYID MIDQTTLGHR FIKQEFDQVP RVGWQIDPFG HSAVQAYLLG
     AELGFDSLFF ARIDYQDRKR RKDDKTLEVI WRGSKSLGST SQIFTGVFPR HYDPPDGFTF
     EINDVSEPIQ DDITLFDYNV QERVDDFVAA ALAQANVTRT NHIMWAMGTD FRYQYANTWF
     RQMDKFIHYV NKDGRVNALY STPSIYTDAK YATNESWPVK DDDFFPYADK ENTYWTGYFS
     SRPAFKGYVR MMSGYYLAAR QLEFFKGRSK SGPNTDALAD ALAIAQHHDA VTGTQRQHVA
     SDYAKRLAMG YVEAEELVAS SLACLAESTS KTECGNPMGK LKQCPLLNVS YCPPSEMTLS
     SGKSMVVLVY NSLGWKREDV IRIPVINESI TIHDSSGKEI ESQLIPIANA SLKLRNYYIQ
     AYLGKSPSVT PKYWLAFMAS APPLGFSTYV LSNVKNPGSL TTLSTIYTSL GSDNDTLEVG
     QGNLKLTYAV DKGKLTHYTN SRNLVNADIK QSYVFYSAYA GSDVDPQASG AYIFRPNGTY
     PIKTEQQGLL TVIRGPVLDE VHEQINTWIS QITRIYKGKE HVEVEFMVGP IPIDDGIGKE
     LASQITTAME TNKTFYTDSN GRDFIKRIRD YRTDWELQVN QPVAGNYYPV NLGLYMEDEK
     REFSVLVDRS VGGSSLEDGQ IELMLHRRFL HDDTKGVGEV LNETVCVSEE CTGLTIQGKF
     YFRIDPLGEG AKWRRTVGQE IYSPFLLAFT EQDGDNWTGS HVPTYSFMDP SYSLPDNVAV
     VTLQELEDGK VLLRLAHLYE TGEDKDLSVV ASVELRKLFH GKKISKVTET SLSANQDRVE
     MERKKLRWKI AGAVKDEAEV FRGRPVSSSN LVVELGPMEI RTFIIGFEPS VHGLVLCT
//