GenomeNet

Database: UniProt
Entry: N1P6H0_YEASC
LinkDB: N1P6H0_YEASC
Original site: N1P6H0_YEASC 
ID   N1P6H0_YEASC            Unreviewed;      1083 AA.
AC   N1P6H0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE            EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN   ORFNames=CENPK1137D_3305 {ECO:0000313|EMBL:EIW10687.1};
OS   Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=889517 {ECO:0000313|EMBL:EIW10687.1};
RN   [1] {ECO:0000313|EMBL:EIW10687.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CEN.PK113-7D {ECO:0000313|EMBL:EIW10687.1};
RA   Nijkamp J.F., van den Broek M.A., Datema E., de Kok S., Bosman L.,
RA   Luttink M.A., Daran-Lapujade P., Vongsangnak W., Nielsen J., Heijne W.H.M.,
RA   Klaassen P., Platt D., Paddon C.J., Koetter P., van Ham R.C.,
RA   Reinders M.J.T., Pronk J.T., de Ridder D., Daran J.-M.;
RT   "De novo sequencing, assembly and analysis of the genome of the laboratory
RT   strain Saccharomyces cerevisiae CEN.PK113-7D, a model for modern industrial
RT   biotechnology.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001528; EIW10687.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1P6H0; -.
DR   HOGENOM; CLU_003442_0_1_1; -.
DR   Proteomes; UP000013192; Chromosome VII.
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   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          565..645
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1083 AA;  124446 MW;  6817C48C469381FA CRC64;
     MSSEDIIYDP QFKPVQGIYE NRLRQFIDTG GDYHDLNLPK FYDKKRISLD HDHVKVWWYQ
     VSFERGSSPV SPDKRPSWKS IIERDKKGEL EFREANINQP FGPSWSTTWF KVKISLPEDW
     VKSNEQLLFQ WDCSNEGIVI DPKTLIPVTA FSGGERTEYV LPKTSDGKHF FYIEAGNNGM
     FGCGAGSTIN PPDDNRFFHL RKADIVWPDL DARALYIDFW MLGDAARELP GDSWQKHQAR
     QLGNAVMNLF DPNDRSSVRK CRELLQREYF DSFLESSKVY EQGESQVLTN VYGIGNCHID
     TAWLWPFAET RRKIVRSWSS QCTLMDRFPE YKFVASQAQQ FKWLLEDHPE FFNKVLIPKI
     QQSQFFAVGG TWVENDTNIP SGESLARQFF FGQRFFLKHF GLKSKIFWLP DTFGYSSQMP
     QLCRLSGIDK FLTQKLSWNN INSFPHSTFN WAGIDGSQLL THMPPGNTYT ADSHFGDVLC
     TAKQNKTPEY YGSGLMLYGK GDGGGGPTEE MLQKMRRIRS MNNRNGNVIP KLQVGITVDE
     FYDDILKRTN QGHDLPTWSG ELYFEFHRGT YTSQAQTKKL MRLSEIKLHD LEWIAAKTSV
     LYPDSYKYPS KQINELWENV LLCQFHDVLP GSCIEMVYKY EAVPMLHNVV KECTSLIDKT
     VQFLQSQSKA DLVEMRTLTW SKPEKVSEEC SLNGSYTSSV TGYDDYIVLA NGKLKVIICK
     KTGVITSITD ETLGVEYLDT EHGRNKLGAN QFVIYDDKPL GWQAWDTELY SVNQYKYVTK
     PKKVQVSCNT KEKCAVEVIF QISEKCKIKS VISLNATAVT DAKLSKVDIS TTVENWDARN
     KFLKVEFPVN IRNDFASYET QFGITKRPTH YNTSWDVAKF EVCHHKFADY SEYSKGVSIL
     NDCKYGFSTH GNLMRLSLLR SPKAPDAHAD MGTHEIKYAI YPHRGALSSD TVKLAHEFNY
     CFKYKLPKDI GMNFDDIISI SGDENVILSN IKRGEDDSAV KSNYSLNPRD EQSIVVRVYE
     SLGGESFASL NTTLNLKRIE KVDNLEMKVY KSLTATRDES NHAINRIPIK LRPFEIASFR
     LYF
//
DBGET integrated database retrieval system