ID A0A1V9ZEF2_9STRA Unreviewed; 959 AA.
AC A0A1V9ZEF2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=THRCLA_07309 {ECO:0000313|EMBL:OQR96352.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQR96352.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQR96352.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQR96352.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR96352.1}.
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DR EMBL; JNBS01001975; OQR96352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9ZEF2; -.
DR STRING; 74557.A0A1V9ZEF2; -.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000243217; 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:UP000243217};
KW Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 17..959
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5017848514"
FT DOMAIN 352..423
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 959 AA; 108504 MW; 897F1307E4F479B3 CRC64;
MRVLSVLAAI SMGISAKKLP SCEHWTPVGP HGGHYNTSAA LSDEKLNVHL IPHTHDDPGW
LITVDQYYTQ EVDYILESVV TELLKNPNRR FMYVEQSFFQ RWWREQSHEM KKIIKQLVKE
GRLDLSVNGG WVMHDEATAH YSVMIDQTSF GHAFLLHEFN VKPRIGWQID PFGHSSTQGS
LLSSGVNFDA LYFARIDYQD YDKRKNNKDL EFMWEASPSR GEKIFTGMIQ DGYGAPHNFQ
FEENSPIKDD PYLHDFNVCE EVKSFVDQSL ERAKHTKGNH IFWPMGTDFT YQNGLKWFKN
MDKIIHYANQ EGRVNVFYST LGHYTDLKLA DKSLQWAVKT DDFFPYADRA YAYWTGYFTS
RPGLKRFARV ANGVLQNMRH VEIHTATSSK LMHLTATVGL TQHHDGISGT EKQHVADDYA
QRMQEGLDAA VKQLNKVLGS EKSPYSLCLL ANVSICEPST SSKEFEVLVY NNFPHASTFG
LNIPIDTTNA EVNLVSNDAP VVSSVVPYVP VHAKAKAAAH TLLIKADVPP LSFQRYRIKK
TTTADDISAE DVSTLENDHI KATFDLKSGS LSSLLDKATK TELPIKTSFG YYQSYSNGND
VNSGAYIFRP NTSTLHSLPK LKDHGCTIAK LLKSCWFRFG DWGALSYQLH PWDKSLTVEW
TVGPIPIDDH QGKEVILRFD TNLASNKRWY TDSNGLEFVE RVRDYRETWN LTLHNDEEHV
AANYVPITTG VYLRDDKIQL NILTDRAQGS ASLKDGQVDV MVHRRLLGDD HRGVDEALNE
TETILLENNK LHTQGLTVRG QFSLNVAPQT LAMERLRKEM YQTYVPPLVA YRAGSGAIKE
LPYSKDITWP ANVGLIAFHW THPHCHLIRL SHLFAVNEHP EFSKPASVDL LQLVKVASGQ
HVVVKELTLS GNAVKSLAST TVTLKAMEVK SFELCIISGV PVYDFDIKSL SSSDEQLDF
//