ID E6ZKW8_SPORE Unreviewed; 1149 AA.
AC E6ZKW8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=sr11837 {ECO:0000313|EMBL:CBQ67971.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ67971.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ67971.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; FQ311430; CBQ67971.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZKW8; -.
DR EnsemblFungi; CBQ67971; CBQ67971; sr11837.
DR VEuPathDB; FungiDB:sr11837; -.
DR eggNOG; KOG4342; Eukaryota.
DR HOGENOM; CLU_003442_0_1_1; -.
DR OrthoDB; 2786490at2759; -.
DR Proteomes; UP000008867; Chromosome 1.
DR GO; GO:0034270; C:Cvt complex; IEA:EnsemblFungi.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
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:0019309; P:mannose catabolic process; IEA:EnsemblFungi.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IEA:EnsemblFungi.
DR CDD; cd10812; GH38N_AMII_ScAms1_like; 1.
DR Gene3D; 2.60.40.2220; -; 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 566..645
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 130647 MW; 7E640516F77C3217 CRC64;
MCQHGRPQAT SKSADYPTHA SAEPRPVRAG LIRSVHERRL EEFVGGQFGD YNLASMLFEA
RTDDPKYVSI QSWTPKAGSK PTFDEAKRQT YLKADKSIKF GPSWTNHWLK LKLTVPKDWV
KKEWLQLEFD PGCEALIYSE DGLPLQGITG GGDKRRVDFP LKPEYRNGIT FYIEVTANGM
FGMPADGTGD PDPNRYFDLA SCDIVVKRPE AWKLMWDFEH LQGCVQNLPR DTELQNRALW
VANQIQNTFR KGDLDSITKC RKLAQEILGK DWDDKIETIY DRDVVEGRED VRIWSLGHSH
IDSAWLWPYS ATQQKVARSW STQIDLMDRF PEHRFTASTA QQYQWLETLY PKLFDKLKKY
VEDGRFQPIG GSWVECDANM PSGEAFARQF LYGQRYFKSR FGKRCDIFWL PDTFGYNAQI
PQLARQSGCD YFFTQKLSWN NINRFPHNTL MWVGLDGTQI IVHMTPVNNY DSRGYVEEIV
RGVKNNTDLW VQPHALMLYG FGDGGGGPSE EMIERMRRAR AVNNNGFKDM PRVHVGRSAK
DFFEHVREVT DNGNRLSTWS GEIYLEFHRG VYTSHGSIKQ WNRRFEAFMQ KLEWLTTLAS
IKASGYKYPK EEIDAIWEPL LLNQFHDCLP GSSIRKVYDD LEEMYADMTI KGKKLWRQAL
NALGVGEEVV ASGNSAYTAI NTLDVPRREL VEVQLSKQMP RAEAIALSHQ SVQLCKAGQT
ALVLLEDVTG RGHATVVDNA NSSFAKSQGV KAVELEHNSF LLQSSAIAVK VAKGRITSIY
DRIADRELIE GGRTAGLAIS EDYPPQFDNW ETELYSLDTE EEIPFTNVRI AEAGPWRASL
ALEAKFGQST VQVSIVLDAV PATTLVGDKD ARPLLRFDTQ IDWWEKHRFL RFNVPTRLRS
DSASFETQFG ITKRPTTRNT SWEAAKFEVC GHRFADLSEE DYGLSILTES KYGYSVEGGL
MRLSLLKAGT YPDAHEDEGL HQFAFALYPH VGGVGRAKVV QVARVFNARF DVDYSREGKI
DIATLERSAG TSGADLQMPI EIVDSTRAGV VIDTIKRAED DFEYYGQKPK DAHSFGIVVR
LYESLGAHAK PTIKIKLPVK EVNLTNLLED VQDDKKEEIA FNTYADEEDS TYVQLDLKPF
EIKTLKISI
//
