ID A0A366RMI4_9HYPO Unreviewed; 1080 AA.
AC A0A366RMI4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=FIESC28_06114 {ECO:0000313|EMBL:RBR18341.1};
OS Fusarium coffeatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR18341.1, ECO:0000313|Proteomes:UP000253153};
RN [1] {ECO:0000313|EMBL:RBR18341.1, ECO:0000313|Proteomes:UP000253153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR18341.1,
RC ECO:0000313|Proteomes:UP000253153};
RA Gardiner D.M.;
RT "Fusarium incarnatum-equiseti species complex species 28.";
RL Submitted (JUN-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:RBR18341.1}.
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DR EMBL; QKXC01000126; RBR18341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366RMI4; -.
DR OrthoDB; 2786490at2759; -.
DR Proteomes; UP000253153; 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}.
FT DOMAIN 553..632
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1080 AA; 122605 MW; 33347C76471A0707 CRC64;
MGGGSEPKGN DSSYPLFAER PVGVPKTSIL KGRIEPFYKS GQYYKVNLQA NMYNARYSGK
PHVQLFVWDA PDLSRPTFEE AVSHEFRETH TGTSFGPSWS THWFKVVLRI PKNIKDEELI
ELHWDASNEG TIWTEDGVPI QGLTGSGERI EWIIPDSFCD GEEHTIYIEM ACNGMFGNAP
NGTTTIAPPD PNRRFNLSKA DIVAVNVPAR KLHIDIWEIG DAARELPENS AEQNHALAVA
MKIINTFEVD NQDSILKCRE IAREILGPDV DSHKVYEVGK DPVVFGIGHC HIDSCWLWPW
AETKRKVVRS WTNQCDLMDR YPEANFACSQ AQQYKWLKTY YPAAYKRVKQ KVKEGQFHPI
GGSWVEHDTN LPSGESLVRQ FFYGQRFFET EFGSRCRTFW LPDTFGYSSQ LPQLCRLADM
DRFLTQKLSW NNINNFPHTT FMWVSPDGSQ VICHMPPSET YTANADFGDL KRSIEKHKTM
RVDSTSLLVF GKGDGGGGPT WQHFEKLRRC AGISNTIGGI PKIKMGSTVD DYFDRLNQKA
TEFPTWYGEL YFELHRGTYT TQANNKYYNR KAEVMLRDIE QLATFASIKN KKYKYPTKDL
DDMWEAVLLC QFHDCLPGSS IEMCYDDSDK VYAEVFETGK RLMNELYDSL NVASQFSSCL
NESVAINTLP WHRKELVELS DSEVGVACGD GQLLALRTFK VQEEKPAVTV MEQSTDVYVL
QNDQLRVVVE NGVITSIYDI DNDREVIEKG GEANKFVIFD DIPLYWQAWD VEVYHLDARR
KVEYGKTKIF EQKAHRVTLV TEIKISENSS IKSYTTLSAA LKGQPSQIDV RADVNWHEDS
KFLKVEFPVN VVNTEASYET AFSITKRPTH YNTSWDMAKF EVCCHKFADL SENNYGVSIL
NDCKYGFATA GKMMRLSLLR SPKAPDANAD MGRHTIRWAI LPHKGSLSSA TVKAAYAFNN
PLKPVTASKA ALESVSSAPI KLVNTDESQS LVLDTIKRGQ DDEDVTRNEG LRVNKGQSII
LRVYESLGGR SRGTIETSFN VKHVTKTNIL EDDLEKIEME DGKIPITLRP FEVATFKLQL
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