ID A0A2G5SN69_9PELO Unreviewed; 931 AA.
AC A0A2G5SN69;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 08-NOV-2023, entry version 17.
DE RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN Name=Cnig_chr_X.g22950 {ECO:0000313|EMBL:PIC16296.1};
GN ORFNames=B9Z55_022950 {ECO:0000313|EMBL:PIC16296.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC16296.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR601382-2};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family.
CC {ECO:0000256|ARBA:ARBA00007658, ECO:0000256|RuleBase:RU361193}.
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:PIC16296.1}.
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DR EMBL; PDUG01000006; PIC16296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5SN69; -.
DR STRING; 1611254.A0A2G5SN69; -.
DR Proteomes; UP000230233; Chromosome x.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02126; PA_EDEM3_like; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR044674; EDEM1/2/3.
DR InterPro; IPR037322; EDEM3_PA.
DR InterPro; IPR001382; Glyco_hydro_47.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR036026; Seven-hairpin_glycosidases.
DR PANTHER; PTHR45679; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR45679:SF2; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 3; 1.
DR Pfam; PF01532; Glyco_hydro_47; 1.
DR Pfam; PF02225; PA; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF48225; Seven-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR601382-2};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosidase {ECO:0000256|RuleBase:RU361193};
KW Hydrolase {ECO:0000256|RuleBase:RU361193};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601382-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..931
FT /note="alpha-1,2-Mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013633537"
FT DOMAIN 666..760
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 268
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 362
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 380
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
SQ SEQUENCE 931 AA; 106416 MW; 1B8D4E7DF0247BBD CRC64;
MFYTRWKVFL LLAVWFLTIG GEELDKKKLQ KEAYDMFMHG YNSYMNYAFP ADELMPLSCK
GRIRGLTPSR GDVDDVLGNY SVTLLDSLDT LVVLNELDEF ERAVDLVIKQ VRFDSDHVVS
VFETNIRVLG GLISAHVLAE LIKEKYPERM QTYEGQLLKM ATEVGNRLLP AFNTTSGLPY
SRINLKHGMQ DHLKRQKDTC TACGGTMILE FAALTRLTGD PIYEKKARKA MDFLWQQRHR
SSDLMGTVLN VHSGDWTRRE SGIGAGIDSY YEYTLKAYIL LGDESYLDRF NKHYDAIKRY
ITKGPIFVDV HMHRPTVATR GFMDSLLAFW PGLQVLKGDV KEAIEIHEML FQVIQKHKFL
PEAFTHDFQV HWAEHPIRPE FVESTYFLYR ATKDPHYLHV AKQIMDSINK YVKVPCGFAA
LKDIRTMVKE DQMESFVLSE TFKYLYLIFT DPEDLVFDPD HFVLTTEAHF LPLSIGHTEP
VENVGNPRRM VLRSDEPKQK NYVCANPIDF TKLPTEQEEA RLIRERTKVV LGELRNGMTG
GSGGQSGSCE SPAERMRAWH FSTSNQDHIK QLGQMGIELV NLNDGRLHLS HTSANALSPI
FARWGHEFMQ EMQEYVETLE KNPHFADGSE RLVQILSHPY YGKTILQASP AQFGRDLATT
IRPVYGPAVI SIPYRACDEI VNKDEMIGKI AIVERSGCVF QEKARRVQQA GAIGMIVIDT
EENTKFASGR PPFSMASDKD GKDDIEIPSL FLFRLEGDKL LHAMEKNKET VIAMTSQRVS
TNATIGELLK KGRMFNFPTI PQCGLRDGDI VWHSLKYPEI ILNLRFNGIN QDSDPRMHQE
VVERHVTELK KYLLFGDSDY EFQFYEFFRT VAYGALDLNV DNPKLLSVIS AISTLKKDPV
PPSVYQRLPG EITRVRCIPR GEHMSCSRIS L
//
