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Database: UniProt
Entry: A0A078ACC2_STYLE
LinkDB: A0A078ACC2_STYLE
Original site: A0A078ACC2_STYLE 
ID   A0A078ACC2_STYLE        Unreviewed;      1086 AA.
AC   A0A078ACC2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Glycosyl hydrolases family 38 protein {ECO:0000313|EMBL:CDW79486.1};
GN   Name=Contig14461.g15406 {ECO:0000313|EMBL:CDW79486.1};
GN   ORFNames=STYLEM_8474 {ECO:0000313|EMBL:CDW79486.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW79486.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW79486.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW79486.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CCKQ01008046; CDW79486.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078ACC2; -.
DR   EnsemblProtists; CDW79486; CDW79486; STYLEM_8474.
DR   InParanoid; A0A078ACC2; -.
DR   OMA; VETEIAM; -.
DR   Proteomes; UP000039865; 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; 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   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; ALPHA-MANNOSIDASE 2-RELATED; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDW79486.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1086
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001729411"
FT   DOMAIN          397..478
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1086 AA;  127942 MW;  5FB89268D90D1DE0 CRC64;
     MMHKYFSYLV TLLISIQVIQ AQLGGQNPSP FSTNIIPRDS DYLRQILAPG GTPKTNQNQQ
     KFSEKPFKYE DQEPFSKLVI HIIPHSHTDP GWLNTPENYY KASVIPILNS VMKYLKEDEN
     TTFIYAEMYF FEQWWNVQNN QTKSDVAQYI KDGRLEIVNG GWVASDEACP LYFDLLENIK
     RGHDFLKKQF GFTPKVAWHA DSFGHSSQTA KLFKELGFEA FFFGRMKDEY KERMIQTQDM
     AFIWNPKFVG IDSDYQAHDG IYSHLTHNIY ATPCDIGIGS PRQLQTFDFD GFIRRNFKVE
     GNKRIIRCLE DFTMGYKTQN ILMMFGDDFA YSDAKVTFNF IDRFTEKIAQ FTDRYVFKYS
     TFSRYLKDLK EELKYRNLKL NAYSGDFLPL KMFHYEHYWN GFYTSRPNHK DQIRQFTQLA
     QYSLNEYVQY QLSQDKLENL EVVYYSQKLM EEWALLMHHD TITGTSIEYV MRQHIDQVKL
     LNYQNTDFLN RQVSGNIYQG LFENLRIDYH NIQDDHDNPL IFGFQTVIYT LIHNPNTYNQ
     FGVRLRVLDV QLHYKVRVWD WTNRQFNDVK IDVLNLKNYE QNDYADLFVA LNIAPFSHEI
     FEITYGLKPF RQLQKFEKNQ LSKLDNQQEY DQTSALIEDE IIIEESSGNE LVFEKPDTNE
     STQETQHQNI HREIGFKDSC LLAVDDANSR EIKFILKDLV HNMTVKLTFQ FKYYSSYVGY
     KDQGGIYVFK TKQSESSYFS DELILIQKQS GDYQTSIQFT YKSRAKNTLS IVTVYLTRNE
     DGCGDIEFDV KRDGLDVNVE ATVNFSSEDI QNNGIFYTDS NGLEYVKRLR RNGLEEIDLK
     STAPANFYPI NTGIFIENNQ KSLQMIVMND RPQAGSGFRD GIIELLFNRR VLTADGLGNP
     ELLNEMNERS EPIRTHNKYF IRFTKSREQA FKAITERTIK TLNPVRMFNA NRFNSEKAQQ
     NDFSRIRQHQ YELSKILNQL DIVDYKLIPD SEFEIVLLWL QQFNHNKSSL KIVNREHAKK
     IIELICKISD KQEVDISMNI LQGNCNQNRN FEFTKSTGQH LKLNEEHQNE YSLYKIITIQ
     IMLNKT
//
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