ID J9IDC9_9SPIT Unreviewed; 1048 AA.
AC J9IDC9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:EJY72218.1};
GN ORFNames=OXYTRI_06785 {ECO:0000313|EMBL:EJY72218.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY72218.1};
RN [1] {ECO:0000313|EMBL:EJY72218.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY72218.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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:EJY72218.1}.
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DR EMBL; AMCR01015327; EJY72218.1; -; Genomic_DNA.
DR AlphaFoldDB; J9IDC9; -.
DR EnsemblProtists; EJY72218; EJY72218; OXYTRI_06785.
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 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 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 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 345..428
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1048 AA; 122057 MW; 9B83A3690B67698C CRC64;
MFLNDNLKPK KESDYQHKVK DDKIYVHLLP HSHDDIGWLK SVDMYFSGTN ETIARGSVMN
ILDTTVHELL KDPAKKFCYC EVKYLQMWWK YQSDEMKTKV RGLVNNGQLE LVNGGWSSHD
EACTHYEDQL TNMQIGQQFL KQEFGVTPRV GFQIDPFGHS SANQRLYADM GLEAVFIARA
DLNDKARRVQ DREMEWLWRP MFNHLGKQNQ IFTHLMLDGY CPPNYFGYDI RDDTDNDTAF
IDNIDFETFN ADWKTKEFMD LVDRYSKIYR TNHILVPFGC DFHFGNAKQN YRSIDKMIKY
INDRNPNVQL MYSTPSEYLD EVYKAGIEWP TRYDDMFPYA SGTDDFWTGY FSSRQISKRF
IRDGQQNLIS SNKQYAYVMI DQSSSDQDIT LALQASNSMQ DAIGVYQHHD AVTGTSKQFV
ADDYVQRLNK AMIQNKQVYS KFIKSQALKD FGVLAQEDWA MCSVTNATYL ECPVANYSEK
PFLMIVHNPS NSEIYYQKIK MPTDTYNASV WDNTKKQFVD IRSTCFCHKF TYYQSGQQTY
DCNFIIENTI LANSYSLVKI QYNPDPTQGP SQLDPDYKEK ISQFASKIEQ SEGGLNVKPI
HLSLDDMQRG LGKIGYFGDD DNGSKFRVQN SDGVDYYFYL QFRYYNSDNG SDTHKASGHY
FFQPQIDQQE SLKYNVMEGM EALWSNFSQE LYMTYYNYTS ENRRMQLRVR AYEKLPTVEF
ELYMEPIPKK QGSQEVTVTL QPSPRDNAFA NDNIFYTDSN GLEMQRREWN KRPTYIYTTN
STTSSNYYPV ASAVTVLDTN SGSHMQFTVI NDRAQGGSVK SDTSRVELMI NRRIFHLDGE
IQEFLDEGDT PVRTQFWVQI FNRSNENSFQ RQQQMINDEQ PQYFFSSQWT FQEEVELHTN
YQGMSELKLI DKLDADRVHA IKYTLTPLKR HTILVRFQNL DDLFDYEKSA TLNDTVVYID
VDAFAKELYD QVNPQLQAAS VAINEVTLTG TQDYEEMQAK KPRLTGVDDG TIVEPVIPKD
KSKSVIALSA QMIRTFEIIY DPKKTILQ
//