ID A0A091KM44_9GRUI Unreviewed; 861 AA.
AC A0A091KM44;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=N324_12334 {ECO:0000313|EMBL:KFP40305.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP40305.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP40305.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP40305.1};
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; KK746231; KFP40305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091KM44; -.
DR Proteomes; UP000053330; 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:UP000053330}.
FT DOMAIN 617..704
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 735..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 75
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 222
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 316
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 334
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT BINDING 420
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:KFP40305.1"
FT NON_TER 861
FT /evidence="ECO:0000313|EMBL:KFP40305.1"
SQ SEQUENCE 861 AA; 96565 MW; D3A7C66049D7C7E3 CRC64;
YPADELMPLT CRGRVRGQEP SRGDVDDALG KFSLTLIDTL DTLVVLNKTK EFEEAVKKVI
KDVNLDNDIV VSVFETNIRV LGGLLGGHSV AIMLKEKGEY MQWYNGELLR MAKELGYKLL
PAFNTTSGLP YPRVNLKFGV RHPEARTGTE TDTCTACAGT LILEFAALSR FTGTSIFEEY
ARKALDFIWE KRQRSSNLVG VTINIHTGDW VRKDSGVGAG IDSYYEYLLK AYVLLGDDSF
LERFNTHYDA IMRYISQPPL LLDVHIHKPM LNARTWMDSL LAFFPGLQVL KGDIRPAIET
HEMLYQVIKK HNFLPEAFTT DFRVHWAQHP LRPEFAESTY FLYKATGDPY YLEVGKTLIE
NLNKYARVPC GFAAMKDVRT GSHEDRMDSF FLAEMFKYLY LLFADKEDMI FDIEDYIFTT
EAHLLPLWLS TTNQTISKKN TTTEYTELDD SNFDWTCPNT QILFPNDPMF AQSIREPLKN
VVDKSCPRGI SRAEESFGSG PKPPLRARDF MASNPEHLEI LKKMGVSLIH LKDGRVQLVQ
HAVQAASSLD AEDGLRFMQE MIELSSQQQK EQQLPPRAVQ IVSHPFFGRV VLTAGPAQFG
MDLSKHKAGT RGFVATIKPY NGCSEITNPE AVKEKIALMQ RGQCMFAEKA RNIQKAGAIG
GIVIDDNEGS SSDTAPLFQM AGDGKNTDDI TIPMLFLFNK EGNIILDAIR EYEAVEVLLS
DKAKDRDLEV ENMDQKLSEN DSHKQSSEEA ASASQDAGAI SEEPEEGESP DVPDPDSLSP
AHADSDSVSI SNQDSYVPGT EAAPAPEPAC TQEDNQPQEL KTETESNSKV NWDNKAQPME
SILADWSEDI EAFEMMEKDE L
//