ID T1KZW3_TETUR Unreviewed; 954 AA.
AC T1KZW3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur29g00310.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur29g00310.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAEY01000758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1KZW3; -.
DR STRING; 32264.T1KZW3; -.
DR EnsemblMetazoa; tetur29g00310.1; tetur29g00310.1; tetur29g00310.
DR eggNOG; KOG2430; Eukaryota.
DR HOGENOM; CLU_003818_4_0_1; -.
DR OMA; NYVCANP; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
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 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; 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:UP000015104}.
FT DOMAIN 694..778
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 800..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 109
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 255
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 350
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 369
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
SQ SEQUENCE 954 AA; 108085 MW; F3807FE05422EE73 CRC64;
MCLIQCMSNE EIQSLRDEVK EMFYHGYNSY MEKAYPADEL MPLSCRGRYR DREPNRGDID
DALGNFSLTL VDTLDTLVIF NNISEFERGV ALLVKDLNFD TDVVVSVFET NIRVLGGLLS
GHIFSNYIKD RWKDHLQWYK NELLLLAQDL GYRLLPAFNT STGIPHPRIN LKFGMRSPQI
INVRETCTSC AGTMILEFAA LSRLTGEPIF EIAARKAMDY LWNQRHRSSD LVGTVLNIHN
GDWVRRDSGV GAGIDSYYEY LLKGYILLGD ETYLQRFNQH YKGIMKYVSQ GPLLVDVHMH
RPKSNAKNFM DSLLAFWPGL QVLKGDIKPA IATHEMLYQV AQRHNFLIPE AFSINDFEAH
WSGYFLRPEF IESTYFLFKA TGDHHYLEVG KQVMEGLQKY TRTECGFAAV KDVRTRTKED
RMDSFFLTET LKYLYLLFAT KKDLIVDLDQ FVFTTEAHFL PLSLSSMQLD EISKISEKAD
ALSPPPSSFL TFVDEEKDGS MQYFRHCPNV KYLIKKDLKV DYVRDIRETL KGYIANSRDA
SLKYARSSSQ STSTPSLNLA SSTCSMSYND HGDLSEKRLS LQPQDFSATN KEHLEIIKKM
GINVGFTTDG RIQLIHSAAT AENVDKGVEG ALFMQEMLRL SKQQVNQFNS KHQWLSFISP
STGSMLKFKS GIAQFGLQLK QPLSGKVSIA DPIKACSELL PESNSAISGK IAIVERGECT
FVQKARVVQK AGAIGCIVID DVIGTTEETL PMFAMSGDGK DDVSIPVTFL YYQQGHSLMW
FLKQKDDLVI EINAADSKDN NLDFSSSKPS EPSNNEDKDG SYEDDSEVMS PVEAYAEITD
ITQQIIGGNG EDTERGMKVV EAVLNSFHHD LTLKYQQYVK NNFNSIVEGT ILQDMFSSLQ
SSLKNMKTVF ESEGEPLLAR SKRKRNLMSL RTCNTLTYEH LISTYTICPR VNTD
//