ID A0A164X4C8_9AGAM Unreviewed; 1183 AA.
AC A0A164X4C8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=SISNIDRAFT_452270 {ECO:0000313|EMBL:KZS95622.1};
OS Sistotremastrum niveocremeum HHB9708.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS95622.1, ECO:0000313|Proteomes:UP000076722};
RN [1] {ECO:0000313|EMBL:KZS95622.1, ECO:0000313|Proteomes:UP000076722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB9708 {ECO:0000313|EMBL:KZS95622.1,
RC ECO:0000313|Proteomes:UP000076722};
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; KV419401; KZS95622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164X4C8; -.
DR STRING; 1314777.A0A164X4C8; -.
DR OrthoDB; 2786490at2759; -.
DR Proteomes; UP000076722; 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:UP000076722}.
FT DOMAIN 564..645
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 1108..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1183 AA; 130479 MW; 271CEDA71CF7C893 CRC64;
MAHHHHHHHP PPETVQTAAS YAELNLKPGA KWVKSLTQGR LDQFVGGHYS SVNLSSALFT
HRLDDEKHVK LQVWSAPGLT KPSFDEAVKQ KFKPAKKGDR FGPSWSNHWW KVTVHIPSDW
TKYERVQFEF DPGCEAMIFS TEGTPLQGIT GGYGGDRRVE YIIPLSDRKK GTHEFVIESS
CNGMFGVPWN GDTIEPPDMN RYYTLDSADL VVPNQEAWHL LWDFQTLKEL TQSLPGNSII
QNKALKVANE ILNIFDSGDL KSVGKARKAA EQVFGEGWAE KGAKVYDEGE KTAQVWGIGH
CHIDTAWLWP YSSTQQKVAR SWSTQVDLME RYPEHRFTCS SAQQFKWLEQ LYPKLFEKVK
EKIISGQFQP VGGAWVEHDG NMPSGEAFAR QMIFGQRYFE SRFGKRCETA WLPDSFGLNG
ALPQIIRSAG MKHFFTQKLS CNVFPHSTFN WVGIDGTQIL CHMTPVDTYT AQATVGDIQK
GIHNHKNLES SQTSLLVFGN GDGGGGPLSK MLENLRRIRA ATNESRELPV VNMGYSVDDF
FDHLDESSKA GKVLPNWHGE LYLEFHRGTY TSHGSIKKGN RKSEILLRDV EHVATLASLF
GKEGYIYPKS KIDDAWEKVL LNQSMNSVLP GSAIGMVYDD AEKLYAEVSK AGHQILEEAF
QALFPSSISL PFSPSSSSLP ESSDKGSIIG YNTLPFARRA VIGLPLGTGV KGNGMRGEAV
QISKDGNVGY YLMDSSASEG AGVVAPRGLF ADIKPASAWT EGDKFVLGNS NVQLTIEEGR
ITSLIDVVLG RELIPDGESG GLIWYNDRPN YWDAWDIEIH HLETPHPIAF SNISIAENGP
VRASLIAEAS YGGTTISITV PTLKENSRSF FTFDAKVDWH QRHECLKFEI PLNIHNDNAT
YEVPWGHVSR PTHKNTALDM AKFEVCGHKY ADLSEYGYGV ALLSESKYGF ACHGNVLSMS
LLRGATAPDA EQDQGKHEFA WAVMPHVGSF LESDVPIAAH FFNSPLHVRF IPATTTPNTQ
SMNAKNVPFK VEGAPNVILE TIKRGDDDFD TYSLQEKGGE KSVVLRLYEA YGGHASARLR
VSGRVGVKKV FVTGLLEDEE GEGVRLLASS AGGSSIGQGS GAGAEGRREG RTRGTDGDSV
DYDGSGSGDA VYEIPFRGFQ VVTVKLIVDT SSTSSGTTES SDR
//
