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
//