ID A0A2B7X992_9EURO Unreviewed; 1088 AA.
AC A0A2B7X992;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=GX51_02964 {ECO:0000313|EMBL:PGH05440.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH05440.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGH05440.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGH05440.1,
RC ECO:0000313|Proteomes:UP000224080};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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:PGH05440.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDNC01000030; PGH05440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7X992; -.
DR STRING; 2060905.A0A2B7X992; -.
DR OrthoDB; 2786490at2759; -.
DR Proteomes; UP000224080; 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; cd10812; GH38N_AMII_ScAms1_like; 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 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 PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 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 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000224080}.
FT DOMAIN 556..635
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1088 AA; 123309 MW; 65FF8133B8EDAEDC CRC64;
MGGNNKLPST SSYPILASRP VGQQITSIYK DRLRQFTDGG QYSGHNLVAK YYEATNDDEQ
HVKLSVYSVP DLARPSFKDA TSHEFRPTRR GESFGPSWST HWFKIQLTVP EDMRKKERLE
FHWDANNEGM VWTEDGKPLQ GLTGGGERIE WILPDSFRDG KEHIFYIEMA CNGMFGNAPG
GDSIQPPDPN KYYRLNVARI TAVNLQARAL YYDFWMIGDA AREFPSDSWH SHEAQQVANA
IMDAFIEGSG SQESIIKGRQ IAQQYLGNLV DSDAVYKTDK QPIVYGIGNC HIDSCWLWPW
AETKRKVARS WSTQCDLMER YPELRFVCSQ AQQFKWLEQD YPYAFDRVKS WVKKGSFIPI
GGSWVEHDTN MPSGESLVRQ FIYGQRYFES HFGERCTTFW LPDTFGYSSQ IPQLCRLAGM
SRFFTQKLSW NNINKFPHTT FNWVALDGSQ VLCHMTPAET YTASAHFGDV RRSVTQHKSM
DQDNTSLLVF GKGDGGGGPT FEHLEKLRRL RGMSDKGELL PRVTMGSTVD DFFAKLEDKA
ANGTEFVTWY GELYFELHRG TYTTQANNKL YNRKSEFVLR DLELLATLAT LKDPNYKYPK
KDIDDMWESV LLCQFHDCLP GSSIEMCYDD SDKEYAKVFA TGSKLRKEAL KVLGFSSPDS
KDDRGLVAIN TLPWPRSEIV RVDDVRTASK LPKYGLAKGG MGVIAVQPLE LFQSPSVSLK
EVKPGVFRLS NSKLSLEVSN GVITSLVDLD EKREVIAKGG KANQLVIFDD KPLYWQAWDV
EVYHLESRKE LKSETTKIAE VHPHRVSVVT ETKISDKSWV KSTISLTATT GDSTPFVEMT
SEIEWRETMK FLKVEFPVDI VNTEASYETQ YGITRRPTHY NTSWDMAKFE VCCHKWADLS
EAGYGVSILN DSKYGFATCG NLMRLSLLRA AKAPDANADM GRHHIRYAIM PHKGPLDSRT
VRAGYNFNNP LVVQPASGKE SSYLFDAFAL KGSPSLILDT VKRGEDDEDV SRGDFKIRPG
RSIILRIYES LGGKSRGSIV TKLPVKMVWK CNVLEDDLEQ VAVVQKAGVA EVDIELRAFE
VATYRLQL
//