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Database: UniProt
Entry: A0A091SDU6_9GRUI
LinkDB: A0A091SDU6_9GRUI
Original site: A0A091SDU6_9GRUI 
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}.
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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
//
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