ID   A0A2G5CNQ0_AQUCA        Unreviewed;      1014 AA.
AC   A0A2G5CNQ0;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=AQUCO_04300019v1 {ECO:0000313|EMBL:PIA32800.1};
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:PIA32800.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA32800.1, 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; PIA32800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5CNQ0; -.
DR   STRING; 218851.A0A2G5CNQ0; -.
DR   InParanoid; A0A2G5CNQ0; -.
DR   OrthoDB; 5474711at2759; -.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   DOMAIN          360..434
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1014 AA;  114803 MW;  1A7592E6049381A0 CRC64;
     MVKMKMKNIL VVVLVLICSV LVLLVESKYI AYNTSQGIVP DKLNVHLVAH THDDVGWLKT
     VDQYYVGSNN SIQGACVRNV LDSLVPALLA DKNRKFIYVE QAFFQRWWRE QSESIQNTVK
     KLVSTGQLDL INGGMCMHDE AAPHYIDMID QTTLGHRFIK QEFNQTPRIG WQIDPFGHSA
     VQAYLLGAEV GFDSLFFGRI DYQDRAKRKD EKTLEFVWQG SKTFGSSAQI FAGAFPAAYE
     PPDNFYFEVN DDSPIVQDNI NLFDYNVQER VNDFITAALS QANITRTNHI MWTMGTDFKY
     QYARTWFREM DKLIHYVNMD GRVNALYSTP SIYTDVKYAA KEEWPLKTDD FFPYADRANA
     YWTGYFTSRP AIKRYVRMMS SYYLAARQLE FLKGRSNLRP NTDYLADALA IAQHHDAVSG
     TEKQHVANDY AKRLSIGYAE AEDLVASSLS CLVESTNKRS CGNTVTKFEQ CPLLNISYCP
     PSEVDLPHGK NLVIVVYNSL GWQREDVVRI PVNSKSVIVR DSSGKEIESQ ILPMVNASMG
     IRNYYVKAYL GKSPSDIPKY WLAFLASVPP LGFSTYIVSG TQPTDSSSTL STTHLSQGSG
     NGTIEIGQGN LKLIYAVNEG KLTQYINKRS SVKEFVDQSY SFYSGNDGSD LDLQASGAYI
     FRPNGSYPLK SESQVSFTVF RGPVLDEVHQ QITPWIYQIT RVYKGKEHVE VEFTVGPIPI
     DDEIGKEVTT QITTTMKTNK TFYTDSNGRD FIKRIRDFRT DWDLQVNQPV AGNYYPINLG
     LYMEDNKTEL SVLVDRSVGG SSLADGQMEL MLHRRLLFDD SRGVAESLDE TVCVDNECQG
     LTIKGNFYLR IDPLGEGAKW RRSFGQEIYS PFLLAFSEQE GDKWSTSHLS TFSAMAPSYS
     LPDNIAMITL QELEDGKVLL RLAHLYEIGE DKDLSVIASV ELKNLFSERK INKVTEMNLS
     ANQERAEMEK KRLVWTVEGG PREEVSAARG KPVDPTKLVV ELEPMEIRTF VVEF
//