ID A0A067BYM9_SAPPC Unreviewed; 950 AA.
AC A0A067BYM9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=SPRG_15416 {ECO:0000313|EMBL:KDO19426.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO19426.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO19426.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO19426.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361199};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
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DR EMBL; KK583351; KDO19426.1; -; Genomic_DNA.
DR RefSeq; XP_012209852.1; XM_012354462.1.
DR AlphaFoldDB; A0A067BYM9; -.
DR EnsemblProtists; KDO19426; KDO19426; SPRG_15416.
DR GeneID; 24137147; -.
DR KEGG; spar:SPRG_15416; -.
DR VEuPathDB; FungiDB:SPRG_15416; -.
DR OMA; LEFIWRP; -.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
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; cd10810; GH38N_AMII_LAM_like; 1.
DR Gene3D; 2.60.40.1360; -; 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; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
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 InterPro; IPR013780; Glyco_hydro_b.
DR PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR PANTHER; PTHR11607:SF3; LYSOSOMAL ALPHA-MANNOSIDASE; 1.
DR Pfam; PF09261; Alpha-mann_mid; 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, ECO:0000256|RuleBase:RU361199};
KW Hydrolase {ECO:0000256|RuleBase:RU361199};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..950
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013062483"
FT DOMAIN 346..417
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 950 AA; 106092 MW; 080AE80FD0791F11 CRC64;
MGLRLLATTL ALATAKQLPS CGAWQPTGPV GGHYNTSADL SGAKLNVHLV PHTHDDPGWL
RTVDEYYTEE VDYILESVIT ELLKNPTRRF MYVEQSFFQR WWREQTHEMK TIVKKLVKEG
RFDLSVNGGW VMHDEATCHY SVMVDQTALG HAFLLHEFGV KPRIGWQIDP FGHSSTQGSL
LSAGVNFDAL YFARIDYQDY EKRKANKDLA VAVARRKIFT GMIQDGYGAP REFQFEENAP
IKDDPYLHDF NVCNEVKMFV EQSLERAKHT KGNHIFWPMG TDFTYQNGLK WFKNMDKLIH
YANQEGRVNV FYSTLGHYTD LKLADKSLQW STKTDDFFPY ADRAFAYWTG YFTSRPGLKR
YARVANGILQ TMRQLEVHSA TSSKLMHLTA SVGVTQHHDG ITGTEKQHVS NDYAQRLSEG
LASAETQLNH LLGASKSPFA TCLLANVSLC EPTTSAAETF EVVVYNPLPF AHTFGVSLPI
DTPSADVALA STNAQVPSTV VPYVPVHVDA EAAPHTLLLQ ADVPALSLQR FRVTKTKAAT
TSTAADVSTL ENDHIKATLD VTKGSLASLL DKATQTQVSM ATKFGYYQSY SNGDDVNSGA
YIFRPNTSTL HDFPSVSSHG CDVVPLLQSC WFRFGNMGVL SYQLRPWDTS LVVEWTVGPI
PIDDHQGKEV ILRFDSNVAS NKRWYTDSNG LEYVERVRDF RETWNLTLHN DEEHVAANYV
PITTGAYLRD DKVQLNVLTD RAQGCASLKD GQLDVMVHRR LLGDDHRGVD EALNETETIQ
LTNNQPRIQG LTVRGQFYLS VGPHEAAIER LRTTTYAQFV PPLVALRAGS GGFVEMKPLG
DLKWPANIGL TALHWAHPHC RLVRLSHLFA IHEHSEWSKP ASVDLLQLVP GAEHVVVKEL
TLSANAVKGP SPTTVTLQPM QVKSFELCVE GKRAPVYDAG RASLVDSLDF
//
