ID A0A369JCT5_HYPMA Unreviewed; 1170 AA.
AC A0A369JCT5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN Name=ams1 {ECO:0000313|EMBL:RDB17533.1};
GN ORFNames=Hypma_001244 {ECO:0000313|EMBL:RDB17533.1};
OS Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Hypsizygus.
OX NCBI_TaxID=39966 {ECO:0000313|EMBL:RDB17533.1, ECO:0000313|Proteomes:UP000076154};
RN [1] {ECO:0000313|EMBL:RDB17533.1, ECO:0000313|Proteomes:UP000076154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=51987-8 {ECO:0000313|EMBL:RDB17533.1,
RC ECO:0000313|Proteomes:UP000076154};
RA Choi I.-G., Min B., Kim J.-G., Kim S., Oh Y.-L., Kong W.-S., Park H.,
RA Jeong J., Song E.-S.;
RT "Whole genome sequencing of Hypsizygus marmoreus.";
RL Submitted (APR-2018) 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:RDB17533.1}.
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DR EMBL; LUEZ02000110; RDB17533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369JCT5; -.
DR STRING; 39966.A0A369JCT5; -.
DR InParanoid; A0A369JCT5; -.
DR OrthoDB; 2786490at2759; -.
DR Proteomes; UP000076154; 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:UP000076154}.
FT DOMAIN 574..656
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1170 AA; 130754 MW; 404E228710021FDF CRC64;
MSCQHGQRGD GYPELNSSAG AKWIKHLTKD RLGNFIGGHF SNVNLSSVLF THRIDNVEHV
KLQVWSAPGL TKPTFEQAMK HKFKPAKKGD SFGPSWVNIL LSRPCQTATL ITYQTNHWWK
VAVTIPGYWQ QYDRVQFEFD PGCEAMIYTT DGVPLQGITG GFGGDRRVEY IIPEAERKQG
RHDFVIESSC NGMFGVPWNG DTIAPPDMNR YFSLKSADLV VPNMEAWGLL WDFTTLHELI
DTLPGNTPLQ NKALVVANEI MNVFSKGDAT AIRGARKLAE DIFGEGWEGK GFQANSCASC
ADHLAGHCHI DTAWLWPYRV TQQKVARSWS TQVDLMERYP EHRFTCSSAQ QYKWLEQLYP
PLFDRVKEKV LEGKFHPVGG AWVEHDGNMP SGEALVRQFV FGQKYFESRF GKRCDTAWLP
DSFGLTGALP QLIRGAGMNY FFTQKLSWNN INVFPHSTFN WVGIDGSQVL CHMTPVDTYT
AQATVGDIYK GQTNHKNLES SQSALLVFGN GDGGGGPLAQ MLENLRRIRG VTNTHRELPP
VSMGYSVDEF FDELLKDSKA GKTLPNWHGE LYLEFHRGTY TSHGSIKKGN RHSEILLRDV
EHVATLASLY KLHKKDYFYP KEKIDDSWEK VLLNQFHDVL PGSAIGMVYE DAEILYAEVQ
KDGDALLEEA FNVLFPDSVA LTRSANPKSF PASSKIVGFN TTFFRRSDII EVPLIGASSS
LKSQILQTSN DGKVGYGVMN SSGGGCVGCL CTPETGLHAQ IVPVSVFTNG SDNFILRNSS
VQLTISKGRI SSLVDVKLGR ELIPKGSTGG LVIFEDRPNY WDAWDVEIHH LETAKQLEFS
NISVVAQGPL RGSVRAEVKY DKSTIIVDIS LDAITASTKE NSRSLFRFDA VVDWHQRHEF
LKFELPLNIH NDNATYETQF GHVQRPTHKN TTWDMAKFEV CGHKFADLSE YGYGVAILSE
SKYGFSCQGH LLRISLLRAA TAPDAEQDQG EHHFSWAVMP HEGHFLESDV PMAAYLFNSP
IRVRCVPSNG DAAMASLDSP FTIEGGRNVI LETVKRGESD HFGGKQSDVS KKMTVILRLY
EAFGGHAQTK LRIAGHLSVS KAYTTNLLED DDDELNVTPV DGGATVILDF RGFEVKTVKL
VLEHAGISQS EDRREDRRES WINIDRLAIY
//