ID A0A2N6NFJ2_BEABA Unreviewed; 1079 AA.
AC A0A2N6NFJ2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:PMB66065.1};
GN ORFNames=BM221_008266 {ECO:0000313|EMBL:PMB66065.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB66065.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB66065.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB66065.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
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:PMB66065.1}.
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DR EMBL; MRVG01000009; PMB66065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NFJ2; -.
DR OMA; GQYWDAW; -.
DR Proteomes; UP000235728; 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:UP000235728}.
FT DOMAIN 552..631
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1079 AA; 122004 MW; 6AAA573B7306B108 CRC64;
MGGGHDHNSR GAYPVYADKP VGVAKTSILQ GRIEPFYKPG QYEKVNLLAN MYNARYSGEP
NVKLAVWSAP GQDRPSFQEA VSHEFKEAHI GDVFGPSWTT HWFHVTITIP RALHDEEFVI
LEWDANNEGM IWNDDGMPLQ GLTGNGDRIE WVIPDEFRDG KEHVIYIEMA CNGMFGNAPN
GTNDNTPPDP NRYFTISKAN IAAVNYQARM LLFDIWQIGD AARELPGDSA EQNKALAVAM
KIIDTFQVDN QDSILKCRKI AQQVVGPDVD SHRVYEVGKE PTVFGIGHCH IDSCWLWPFA
ETKRKVARSW SSQCDLMDRY PEAHFACSQA QQFKWLKTLY PRAFERVKAK VREGQFHPIG
GSWVEHDTNM PSGESLLRQF FYGQRFFESE FGSRSRTFWL PDTFGYSSQL PQLCRLAGMD
RFMTQKLSWN NINTFPHTTF MWVSPDGSQV ICHMPPSETY TSEANLSDLR KSISKHKTMR
TDSSSLLVFG KGDGGGGPTW QHLEKLRRCA GISNTIGGIP KLKLGLSVDD FFDRLTAKAD
DFPTWYGELY FELHRGTYTT QANNKYYNRK AEVMLRDIEQ LATIASIKNK SYKYPTEDID
DMWETVLLCQ FHDCLPGSSI EMCYDDTDKL YAEVFKTGHT LLKEIYQSLN ISDVRSPSAH
ETVVLNTLPW HRKEIVEISE TEVGVACGDG QLLPVRAFKT QGTEPAVTLR QVSKDQFVLQ
NEHFRVEVEG GCITSLHDRL NDREIVEKGG KANKYVIFDD IPIYWDAWDV EVYHLNTKKN
LQYGETRVHE IKPHRVTLVT DIQISKESSI KAYISLSASL KGQPSWIECS AEVDWHESSK
FLKVEFPVNI VNNEASYETA YSITKRPTHY NTSWDMAKFE VCCHKFADLS EHNYGVSILN
DSKYGFATAG KVMRLSLLRS PKSPDEHADM GKHSIRWAIF PHKGALSSAT VRAGYAFNTP
LKVLSAPKAA VDNLGSAPIR LVNVDESASL ILDTIKRGHD DEDVSRRQGL CVNPGKSVIV
RVYESLGGHS RGTIETTFDV KRVSKCNLLE DESDDVSFSG GKFAIKLRPF EVATFKLQL
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