ID A0A0D2VPM1_CAPO3 Unreviewed; 1249 AA.
AC A0A0D2VPM1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=CAOG_003430 {ECO:0000313|EMBL:KJE92457.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE92457.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) 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; KE346363; KJE92457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2VPM1; -.
DR STRING; 595528.A0A0D2VPM1; -.
DR EnsemblProtists; KJE92457; KJE92457; CAOG_003430.
DR eggNOG; KOG1958; Eukaryota.
DR InParanoid; A0A0D2VPM1; -.
DR OMA; GHQWLKY; -.
DR PhylomeDB; A0A0D2VPM1; -.
DR Proteomes; UP000008743; 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; cd10809; GH38N_AMII_GMII_SfManIII_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 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:UP000008743};
KW Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 27..1249
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5017852919"
FT DOMAIN 541..628
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 36..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1249 AA; 138574 MW; 25448772004A5468 CRC64;
MRVCGRGSRS RVAIFLLALA LIAVASFTLP SLRDDAETGP RGALPDAVPA PADKQASQSQ
TPKPNDSTLD SLSTATSWAY ATVRQVEVNR ANANQPPVPV KRQPVLQEEE HEELRQPEPE
LLRKPIIAHK PMQSVSNDGC AFIAPSTADH EMRDFIESMP FDNLDGGVWK QGWDVQYAAS
EVQTRKLDIY VVPHSHNDPG WIKTFDAYYS QQTKSILDTV VNMLSQNSKR KFIWAEMSYL
QRWWDEQTSD RRELTRRLVD NGQLEIVTGG WVMSDEANAY YYAMIDQLIE GHEWLASTLG
VTPKSGWSID PFGQSSAMPY FLRRTGFESM LIQRTHYSVK KYLARNRGLE FMWRQEWDAE
GTTDILTHMM PFYSYDIPHT CGPEPAVCCQ FDFARLPGQR FSCPWNIPPQ VISTGNVKQR
AQMLVDQYRK KAQLYKSDVV FVPLGDDFRW QGDQEALAQY ENYERLFKEL NGDSKYNVRI
QWGTLSDYFG ALRESLGTAG SAAPPSEFAL AAYGQPHQYA TPTGIQSMTG DFFTYADRDD
HYWSGYFTTR AFYKRADRVL EYTLRSAEIM LSVARAEALT LGVSIAPFLQ TMYPAVVTAR
RNLGLYQHHD GVTGTAKDEV VIDYGARMHS SIGVMQTLMR DLSEFLLATD KHAAAALLAS
GPRRSLNDAA LSNQANDHLV LHLGESAAVH NALPTQEVLK TRPASASWSA GAAEPTRNAN
ARAVVLYNSL GQSRAQTIIL TVATSTSSSN GGVRGTHAPI CVTDSDGTSV LAQTGPLFDR
NGEIVPSTFS LAFEAQIPAV GLATYFVHEV ASDDTRCTRA EPATVQLFNA LQLGSNPVTQ
DHGAFKVTQL SSGPSSGIVL ENSELRVTIE PADGMIQKAV HKNSGKEVLL NENYLKYSTY
RSGAYLFLPN GPAASFVSQQ RPSIRTITGP LLHEAHVVVP TGRLTRVARL YLAPSLPHAV
ERSVIETRIV LDITADNNKE TIVRFSTSVR NGPIFFTDLN GFQMIRRKTQ SKLPLQGNYY
PMPSLAFLED ESIRFSVHSR QALGCASLKE GTFEMMLDRR LSQDDERGLG QGIHDNHENE
LLFHLTLEDF ESPHARGEST GVYFEAPSLL SHLAREELNE PPIVFLAAHL APKEAARLSW
APYSALSSPL PCDVHLVNLR SLSNRDQVAA GLIVQRRGRD CSLRQPDAVF GLCGGQDLGS
ITPYSLLAFA QPKDVTQHTL TLMHPIGQVA RTSPVVLSPM ELYSYVVTF
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