ID A0A196SJS6_BLAHN Unreviewed; 966 AA.
AC A0A196SJS6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=AV274_0963 {ECO:0000313|EMBL:OAO17303.1};
OS Blastocystis sp. subtype 1 (strain ATCC 50177 / NandII).
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=478820 {ECO:0000313|EMBL:OAO17303.1, ECO:0000313|Proteomes:UP000078348};
RN [1] {ECO:0000313|EMBL:OAO17303.1, ECO:0000313|Proteomes:UP000078348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50177 / NandII {ECO:0000313|Proteomes:UP000078348};
RA Gentekaki E., Curtis B., Stairs C., Eme L., Herman E., Klimes V.,
RA Arias M.C., Elias M., Hilliou F., Klute M., Malik S.-B., Pightling A.,
RA Rachubinski R., Salas D., Schlacht A., Suga H., Archibald J., Ball S.G.,
RA Clark G., Dacks J., Van Der Giezen M., Tsaousis A., Roger A.;
RT "Nuclear genome of Blastocystis sp. subtype 1 NandII.";
RL Submitted (MAY-2016) 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}.
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:OAO17303.1}.
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DR EMBL; LXWW01000036; OAO17303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A196SJS6; -.
DR STRING; 478820.A0A196SJS6; -.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000078348; 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; cd00451; GH38N_AMII_euk; 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; 1.
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:UP000078348};
KW 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..966
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5017848888"
FT DOMAIN 369..450
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 966 AA; 109272 MW; 087A0ADFBAAB6F6A CRC64;
MKRIASILAL AAIVATAMGL GMKDELNAKL SNTYTEPNPV NINGTINVWI HAHTHDDPGW
LVKADQYYVK QVRYILDTVI GALALNPARK FTYVEQGFFQ RWWREQDEHV KALVHKLVDN
GQFEFNMGGW VMSDEAAANY EDIINEMTLG AKFIYDEFGV RPTVAWSIDP FGHSKEVEAM
YAAMGFDAFG INRVHYADKE QRTKNQKLEF VWRGSASEGA KSDMFIHMMD NHYCSPKECD
FFSNSSGDCM YWKDDNEWFQ DNAELPTFKV NMEEKAQAFV NMVKTRATYY DNGNNLLITW
GCDFTFLSAP VSYDNMDKLI KYVNANEERF GVHVQYAVFS DYIKAVHQHK KQWDVYEGDF
MPYASDPDAY WTGYYTSRGR TKGISRRVMN ELAAAELYLS LAKVYELPVD LPAVFDKVMK
LRKAEGEFQH HDAITGTEKQ AVADDYTVQM EDGSFFANEA TATVLGAILN VRLTHNLTLA
WEQMDKGKLL GAVLVNDQAQ ALHTVVRAVV PVSALEVTDA RGNALPFQIN AIPDWSVERA
NGTHVVYVEV TVPALGFTTV YFSPRMTAAT VPRGGIARDD FIENEAYRLT FENGALATVE
LKKEGVVVPF TDSLLQYEGR FGNSRSSGAY SFIPARNEPD AVAEKAELTV VKGELVEEAR
LVYRAGYQEV LRLYRAAGEL GEVIEVVHDM GPTDDGREII ARFASPFLKN GRVIHTDGNG
LEDIERVYRE DPVMPVSANY YPISNRVWMA GEEHDLRLSV VVDRAHGVAS VVDGALEVML
KRRTLGDDWF GVDEPLKEND HYQQTMWLHL GAKKAAVALH KRLDTMLTHR PVDFFFVGEA
RVAKGEASLL KKDLPANVQL MNFQLNALAD NDYLLRFHHR FMKGEETELA SVVSFDVNDY
LDGFKVTEMK EYGLSGMFSR EQIDKERMTW DINPAMKQEV EETVDEGTKV TLGPMAFKTY
RVKVAH
//
