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Database: UniProt
Entry: J9IDC9_9SPIT
LinkDB: J9IDC9_9SPIT
Original site: J9IDC9_9SPIT 
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
//
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