ID A0A091SDU6_9GRUI Unreviewed; 882 AA.
AC A0A091SDU6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
DE Flags: Fragment;
GN ORFNames=N332_06623 {ECO:0000313|EMBL:KFQ38420.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ38420.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ38420.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ38420.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 ---------------------------------------------------------------------------
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; KK816462; KFQ38420.1; -; Genomic_DNA.
DR RefSeq; XP_010186456.1; XM_010188154.1.
DR AlphaFoldDB; A0A091SDU6; -.
DR GeneID; 104543522; -.
DR KEGG; mui:104543522; -.
DR CTD; 80267; -.
DR OrthoDB; 942598at2759; -.
DR Proteomes; UP000053369; 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 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:UP000053369}.
FT DOMAIN 635..722
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 747..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 93
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 240
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 334
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 352
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ38420.1"
FT NON_TER 882
FT /evidence="ECO:0000313|EMBL:KFQ38420.1"
SQ SEQUENCE 882 AA; 98949 MW; 94F8D0C8CECBFF8E CRC64;
NQVLEMFDHA YSNYMEHAYP ADELMPLTCR GRVRGQEPSR GDVDDALGKF SLTLIDTLDT
LVVLNKTKQF EEAVKKVIKD VNLDNDIVVS VFETNIRVLG GLLGGHSVAI MLKEKGEYMQ
WYNGELLHMA KELGYKLLPA FNTTSGLPYP RVNLKFGVRH PEARTGTETD TCTACAGTLI
LEFAALSRFT GTSIFEEYAR KALDFIWEKR QRSSNLVGVT INIHTGDWVR KDSGVGAGID
SYYEYLLKAY VLLGDDSFLE RFNTHYDAIM RYISQPPLLL DVHIHKPMLN ARTWMDSLLA
FFPGLQVLKG DIRPAIETHE MLYQVIKKHN FLPEAFTTDF RVHWAQHPLR PEFAESTYFL
YKATGDPYYL EVGKTLIENL NKYARVPCGF AAMKDVRTGS HEDRMDSFFL AEMFKYLYLL
FADKEDMIFD IEDYIFTTEA HLLPLWLSTT NQTISKKNTT TEYMELDDSN FDWTCPNTQI
LFPNDPMFAQ SIREPLKNVV DKSCPRGISR AEENLGSGPK PPLRARDFMA SNPEHLEILK
KMGVSLIHLK DGRVQLVQHA VQAASSLDAE DGLRFMQEMI ELSSQQQKEQ QLPPRAVQIV
SHPFFGRVVL TAGPAQFGMD LSKHKAGTRG FVATIKPYNG CSEITNPEAV KEKIALMQRG
QCMFAEKARN IQKAGAIGGI VIDDNEGSSS DTAPLFQMAG DGKNTDDITI PMLFLFNKEG
NIILDAIREY EAVEVLLSDK AKDRDLEMEN TDQKLSDNDS HKQNSEEATS ASQDVGAVSD
EPEEGGSSDV TDPEPLSPAD ADSDSVSISN QDSSVPGTDE AGAPEPACTA CTQGDNRPQE
QKTETESDSK VNWDNKVQPM ESILADWNED IEAFEMMEKD EL
//