ID A0A024UMW7_9STRA Unreviewed; 961 AA.
AC A0A024UMW7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=H310_01796 {ECO:0000313|EMBL:ETW07207.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW07207.1};
RN [1] {ECO:0000313|EMBL:ETW07207.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW07207.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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; KI913954; ETW07207.1; -; Genomic_DNA.
DR RefSeq; XP_008863300.1; XM_008865078.1.
DR AlphaFoldDB; A0A024UMW7; -.
DR STRING; 157072.A0A024UMW7; -.
DR EnsemblFungi; H310_01796-t26_1; H310_01796-t26_1-p1; H310_01796.
DR EnsemblProtists; ETW07207; ETW07207; H310_01796.
DR GeneID; 20078846; -.
DR VEuPathDB; FungiDB:H310_01796; -.
DR eggNOG; KOG1959; Eukaryota.
DR OrthoDB; 5474711at2759; -.
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}; Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 20..961
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5017853503"
FT DOMAIN 356..428
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 961 AA; 106988 MW; 6CB119A5631398D4 CRC64;
MAKVWTALAA AAVVAQGHGE VPRFKCDNWT PSYPHNGHYN TSATISTEKL NVHLIPHTHD
DPGWLITVDQ YFTQEVDYIL DTVVTELQKD PKRRFMYVEQ SFFQRWWREQ SKETKKVVKK
LVKNGQLDLS ANGGWVMHDE ATPHYTTMLD QTAFGHKFLL DEFGVRPRIG WQIDPFGHSS
TQGSLLSSGV GFDALYFARM DYQDYGKRKD EKNLEFLWKP SASRNDSVFT GMLQDGYGGP
GGFYFENDAP IKDDPYLHDN NVCERIKTFV DQSLERAKHT KGNHIFWPMG TDFQYQNALR
WFKNLDKLIH YANQEGRVNM FYSTLAAYTD LKLQDKSIQW SVKTDDFFPY ADQPNGYWSG
YFSSRPALKR YVRVANSVLQ SVRQLEVWAG ASASRVHHLA ATVGLSLHHD GISGTEKQKV
SDDYAQRLGE GVGNGNWRVN DLLAAPVDFC FMANVSICHR SASADLFTFL VYNPLAVAHT
YTIELPLTAS NAAVKLANGT AVASVVVPFT PVYAHPIQHA APNQLVVQAN VPPLSWLVYH
VTPTSTGANA IESWAVVRDA IVAADNEFVH VEVDTATGSL VSLTEKRSNS TVAVKSSLLY
YQAYGKPGDS CSSGAYLFHP NTSAVHALPA ITSHKCYRTR LVASCAFRFG AWGALEYKLH
VWDKSIVVEW TVGPIPIDDG QGKEVILRFD TSVQSEKTWY TDSNGLEFVK RVAANYVPIT
IATYLRDAST QFNVVTDRAQ GVASLNDVGS VEIMVHRRLL QDDNKGVDEH LNETETLSLA
NNQQLTQGLT VRGSFALSVG PLDAAMAQLR AEMSRRYLNP LVALTAHNTS LTPPTTAWTP
RLPFNVGLIS LEVVDAHTIR LRLTHLFAIR EHPVWSHDAT VDLTVLLGSP WSTAHHLRVT
ELSLSGNRVL RSIPRTTVTL KAMHVRAFEI TTMQGPAASI FDPTVTNLAD GGGDNEASLD
F
//
