ID A0A165MWI3_9APHY Unreviewed; 1117 AA.
AC A0A165MWI3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=DAEQUDRAFT_730564 {ECO:0000313|EMBL:KZT66211.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT66211.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT66211.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT66211.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; KV429093; KZT66211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165MWI3; -.
DR STRING; 1314783.A0A165MWI3; -.
DR OrthoDB; 2786490at2759; -.
DR Proteomes; UP000076727; 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 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:0000313|EMBL:KZT66211.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT DOMAIN 297..550
FT /note="Glycoside hydrolase family 38 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01074"
FT DOMAIN 558..626
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|Pfam:PF09261"
FT DOMAIN 721..940
FT /note="Glycosyl hydrolase family 38 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07748"
FT DOMAIN 1002..1090
FT /note="Glycosyl hydrolases family 38 C-terminal beta
FT sandwich"
FT /evidence="ECO:0000259|Pfam:PF17677"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1117 AA; 124767 MW; 03F8EA099D429DA7 CRC64;
MSHCHHHHHD HGGHASPSVD YPQTNYGTGA KWIKSLTQGR LGTFNGGHYA DVNLSQVLYH
HRVDDSAYIK LQVWSAPGMS KPSFEEAMKQ KFKPAKKGDS FGPSCTFTNH WWKVSVTLPA
YWDQYEVVQF EFDPDCEAMI FTTDGTPLQG ITGGWGGDRR VEFILPPEAR KARKLDFVIE
SSCNGMFGIP WNGDTIEHPD MNRYFRLATA DLVVPNQDAW RLLWDFQTLR EISETLPGNT
SLQNKALVTA NAIMNAFDKD DLGSIARGRK LAESVFGEGW DGKSDKIYEE GPKEAAIWGI
GHCHIDTAWL WPYRVTQQKV ARSWSTQVDL MERYPEHRFT CSQAQQYKWL EQLYPPLFER
VKAQVLAGHF HVVGGSWVEN DSNMPSGEAL ARQFILGQRY FESRFGIRCD TAWLPDSFGL
TGALPQLIRQ AGMKYFFTQK LSCNTFPHST FNWVGIDGTQ VLCHMTPVDT YTAQASVGDV
NKGITNHKNL ESSDTSLLVF GNGDGGGGPL AKMLENLRRI RAAGNNSREL PPVNMGHSVD
EFFEFLAKKS DAGKKAFLAT LASLYRFHKH DYIYPNERIN DCWEKVLLNQ LLPGSAIGMV
YEDAEKLYAE VRKQGDELLE EAWAALLPQS YPFSNTATLS KRGTLLGVNT THLPRRDVVK
VPLGSGATKL KAQVVQAAKD GSHGYALMDC SVGGQYATPT GLFADCMPVS VFTNGSGHFV
LRNSSVQLTI SDGRISSLVD VELGHRWTGY LQRSTELLGC VGYGGPVNFS DHKLLTMLID
VEIHHLETVQ PVEFSNISVV AEGPLRASIK SEFKYRQSTI NVTISLDAIT ASMKKDSRSM
FIFDAVVDWH EKHEFLKFEV PLALHNDMAT YETQFGYVQR PTHNNTTWDM AKFEVCGHKY
ADLSEFGYGV AILSESKYGF SCRGNVLRIS LLRAATAPDE NQDQGLHEFS WAVMPHAGHF
LESDVPQAAQ LFNSPLHMRF VGNDATRPSM LSPFAVEGAR NVFLETVKRG LDDNFESKSG
PVTVVLRIYE AFGGHAQAWL KIAKHIPVAK VLSTNLLEDP EAELSFFEAE DHAYHVVKLN
FHGFEVKTIK IIVGRSDVQA GTEGSDNWIT IDKPSPV
//
