ID   A0A0V0R5S7_PSEPJ        Unreviewed;       981 AA.
AC   A0A0V0R5S7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Glycoside hydrolase/deacetylase, beta/alpha-barrel {ECO:0000313|EMBL:KRX09712.1};
GN   ORFNames=PPERSA_02584 {ECO:0000313|EMBL:KRX09712.1};
OS   Pseudocohnilembus persalinus (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC   Pseudocohnilembus.
OX   NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX09712.1, ECO:0000313|Proteomes:UP000054937};
RN   [1] {ECO:0000313|EMBL:KRX09712.1, ECO:0000313|Proteomes:UP000054937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=36N120E {ECO:0000313|EMBL:KRX09712.1};
RX   PubMed=26486372; DOI=10.1038/srep15470;
RA   Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA   Miao W.;
RT   "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT   persalinus provides insight into its virulence through horizontal gene
RT   transfer.";
RL   Sci. Rep. 5:15470-15470(2015).
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:KRX09712.1}.
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DR   EMBL; LDAU01000044; KRX09712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0R5S7; -.
DR   EnsemblProtists; KRX09712; KRX09712; PPERSA_02584.
DR   InParanoid; A0A0V0R5S7; -.
DR   OMA; LVEIEWQ; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000054937; 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   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:0000313|EMBL:KRX09712.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..981
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006867718"
FT   DOMAIN          351..436
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   981 AA;  115826 MW;  5DCD62B2135D6CA5 CRC64;
     MVEGIKQVTI LILLCILINT QNDQKTKDQL TIHAIPYSHN DLGWLETPLR YFEGAHQPWG
     EYINIKEIIS SYTLELSKDE RKRFMQVEMG YLKMWWNLQD EDTKKLYQSL IKKGQLEIVQ
     GGWCTHDEAT TYYENIIENM WVGHRFALKT LGVKPQIGWN VDDFGHSLSS ASLFQQMGFN
     GQFFSRIDKQ DKKYRLDQKN MLIMMDQEQY HQCLDYPLYT EVTYNGYYSP TGFDIDAARS
     TKTLPGIDTA KGLEKQSRKL YNYFVEMSKH YQSNTLMHIF GNDNEYRLAN LTFGVQEKLF
     DYINENPSQF NGMKIKWSTP SEYLEVINKE KNFKLKSEQN DFYPYSDQRN AYWTGYFTSR
     VADKKLYRDF GKKVLAFRTY LGLLKFDKMS EICEDKENLI EEIIQQNEET LGMVQHHDAS
     TGTETQRVSN YYKDEVIGAS EKLDDIISQV FNEQIDNQYG MELEDKWINY NWNQTSNEWE
     ILYNNLQNEN ETLLNIYNPT INKEELIELK VPHSKFEIVS LDNNLPQKTE VICRGFQVRP
     DLQKSQNDCK AYFVAKLQGF SINLFQIKYA ENTQNTEELE RQTVDKRLNQ NIVNVSKQKK
     LKIFNPMMEI IYSYFDQKEQ KIVEKEFTLK YLYYTPSTRS PNSGAYLFSP DEKIGPQPYN
     HVLDTYFYKG DIVSNLYLVG DRVQTELSFQ NYDEKLNNII KIQSHADGID NSFKQGAEVV
     LDIFTKIQNK GEFFTDSNGL NMVKRKVDTR FSYEYKKELD VTSNYYPVNS IIQIEDTESK
     QTVSLINDRS QGGTSLFEGQ IQMLIHRRLY RDDNRGLGSR DVLNEIDSKT KKHIDQTFRH
     WLVFGNSGDD NEQIRKIQFD NDLESFTPTL VQNLKQKTKI YFRYYGFNSN DFLLRLHNFD
     HNQQNHFKIN IKTKEIVETT LTANSQLESW KQNKMTWNYD YRSSSQCLRQ QQQQIIDDVI
     NSHHTIDLLP FQIRTFNVTQ I
//