ID Q0UUU4_PHANO Unreviewed; 1104 AA.
AC Q0UUU4;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=SNOG_04470 {ECO:0000313|EMBL:EAT88230.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT88230.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; CH445330; EAT88230.1; -; Genomic_DNA.
DR RefSeq; XP_001794887.1; XM_001794835.1.
DR AlphaFoldDB; Q0UUU4; -.
DR STRING; 321614.Q0UUU4; -.
DR EnsemblFungi; SNOT_04470; SNOT_04470; SNOG_04470.
DR GeneID; 5971755; -.
DR KEGG; pno:SNOG_04470; -.
DR VEuPathDB; FungiDB:JI435_044700; -.
DR eggNOG; KOG4342; Eukaryota.
DR HOGENOM; CLU_003442_0_1_1; -.
DR InParanoid; Q0UUU4; -.
DR OMA; GQYWDAW; -.
DR OrthoDB; 2786490at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
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 GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
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:UP000001055}.
FT DOMAIN 558..642
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1104 AA; 124248 MW; 945F8A14D8DC0E7F CRC64;
MGGESHRNMV AASDYPRHAA GPVGKQIHHI YQDRLRQFTD GGQYREQGIV GKLREATASG
PEWVKLSVYS PPNLSRPLFK EATSHEFKDT KVGESFGPSW STHWFKVRLT VPKDMLKKER
LEFVWDANNE GLIWTEDGHT VHGLTGGGER VEWILPDSFR DGKEHTFYIE MACNGMFGNA
PGGDSIQPPD PDRYYQLHTA DIVAVNLEAR ALYFDFWEIS DAAREFPGES VEAHEAQQVA
NRIIDAFIAD GGSNEGIAEG RKIAKGYLGD KIDSHKVYET DNEPIVSGIG YCHIDTCWLW
PFAETKRKVN RSWSSQCDLI ERYPELRFCC TQAQQYKWLE QDYPSTFDRV KKKIKEGSFQ
PIGGSWVEHD TNLPGGESLI RQFLYGQRYF ESRFGQRCKT FWLPDTFGYS TQLPQVCRIS
GMTRFLTQKL SWNNINNFPH TTFNWVALDN SQVICHMPPC ETYTAEADFG DVKRSVSQHK
SLDQDKTSLL VFGKGDGGGG PTWQHLEKLR RCRGMSDKTG LLPRIKLGGS ADDFFDRLEK
KIENGTELVT WYGELYFELH RGTYTTQSNN KRNNRKAEIM LRDIEYLATL ATIKNGFGKK
SAYKYPKKDI DDMWENVLLC QFHDCLPGSS IEMCYDDSDK IYAQVFSTGE RLLSDALSEL
GFDDAKSLTA DSKLVAMNTL PWQRSEIVKL PGAASKAPYG LAHGNGLGPL DVRPLASPYS
ASTAAIKQLS SNEFELRNAQ FIVKVTDGAI TSLYDISADR EVVPRGQKAA QLVIYDDKPL
YWQAWDVEVY HLKSRQELSP SKVTITESSI HRVSLEIETK ISDKSWIKTT LSLPAAVGNA
PTALEIDADI EWHETMKFLK VEFPVDIVNT EASYETQFGV VRRPTHYNTT WDMAKFEVCV
HKWADLSEAT YGVSILNDSK FGFATQGNVM RLSLLRSPKA PDAHADMGHH STRYAIFPHK
GGLDERTVRK AFEFNNPLKI IGHSASVKSP SILNTFAIHN APNLILDTIK RAEDDEDISR
HDLPVKSGHS VILRIYDALG GKSKGVLTWG ALKVKKVVKC NALEDEEESL EVKDVHGGDG
GKEKGVVVGV RAFEIVTLKV VLED
//
