ID E2BEA8_HARSA Unreviewed; 1358 AA.
AC E2BEA8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 08-NOV-2023, entry version 46.
DE RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN ORFNames=EAI_07877 {ECO:0000313|EMBL:EFN85953.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN85953.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN85953.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL447768; EFN85953.1; -; Genomic_DNA.
DR RefSeq; XP_011137212.1; XM_011138910.2.
DR STRING; 610380.E2BEA8; -.
DR EnsemblMetazoa; XM_011138910.3; XP_011137212.1; LOC105181861.
DR GeneID; 105181861; -.
DR InParanoid; E2BEA8; -.
DR OMA; DFHYFHA; -.
DR OrthoDB; 942598at2759; -.
DR Proteomes; UP000008237; 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:UP000008237};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1358
FT /note="alpha-1,2-Mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003157259"
FT DOMAIN 650..744
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 1163..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 279
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 373
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 391
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT BINDING 477
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
SQ SEQUENCE 1358 AA; 153926 MW; DF761FD711B6D2B1 CRC64;
MACDTLIWGL LFLGCSIQAL WAMSEDDPLE YMNKEEREAL KEEARDMFYH AYNAYMDNAY
PADELMPLSC KGRYRGSEPN RGDIDSTLGN FSLTLVDTLD TLVVLGDLEE FENAVKLVAR
DVSFDTDVIV SLFETNIRML GGLLSGHILA EYLQQRADIM PWYRGELLDL AKDLGYRFLP
AFNTTTGIPY GRINLKHGMR GVPMEVSRET CTACAGSMIL EMAALSRLTG ESIFEEKAQK
AMDVLWRMRH RGTDLMGSVL NVNSGDWVRR DSGVGAGIDS YYEYCLKAYI LLGDEKYLGR
FNKHYQAVMK YVSQGPMLLD VHMHRPNTNS KNFMDALLAF WPGLQVLKGD IKPAVETHEM
LYQVMQRHNF IPEAFTTDFQ VHWGHHPLRP EFLESTYFLY RATGDHYYLG VGRKVLKSLQ
TYARVPCGYA AVSDVRTNKH DDTMDSFVLS ETFKYLFLLF TEPGELFLDL DEFIFTTEGH
LLPLTLASIR TNISSDFERD IVHVDEFDRT CPNSLHLFPA SVRQPLRNMV EDVCPRRSLK
RRLSASQFQA NNLEHLKMLS DMGITTLTLA DGRVQLLHTF SNAKTPQDSE EGLLFMQEMV
ELSKMQTQQP ETKPQTVTFV KPKTDPPEKV TLLAGPAQFG PELQSFDKIT GKVIFTYPPA
ACTELLNADK LAGKIVIMDR GNCMFIEKAR RIQQAGALAG IVLDNVAGSS AATSPMFAMS
GDGKDVDDVT IPVVFLFFTE AAELMKAINT ANGDLTVTLG IYSSKEEVQL KAPTDLSLFE
RVKGSLRSFL SRHLTPQATT TGSNMDITIP VVESQEYQED TIDFHYFHAE IIKDSLGGEV
RITAPSEDAI IILRPVSTPV EILWHQLKEV FVNQIFLNSK QNKGIRIRSF ILESYYNWVN
KARGVLTKTS LSYKVRWFLS ELLVVAPNSS IRKMGQLLEL TKQKLLKQYL LTNMDTMVLN
LKTVATKLKN MKSVKPDMEQ LLKLSESGIA QVENYSFLRH LLADLFDEED EIVSQHIAFL
DHIHAEVHIT YQEILIDGVQ KHLEKTGEED SSYYDILIAD LQKNLKNVDK GENLLGKTRE
DDLAVAEFIS DCSSGKSELK GRNIKVLDQN MRILKKGREL DIEKLEDFEY FILTEIGKAI
KHSAQNILHK YEGTSDVTKN AVTEGKKDKN SGKSEITLHS PLNQSKGEDR KSRARNSLKE
EIDFLRTTKS ANVKIEETVV KDGQKEKFAD STVNMKASNI GITSTDEENV LLQEIRKDIS
DTQHKQKTDS KAKLSKQKNV VESEIVPTDL LKEFKRPIWA VNEEKDFTEF RKDSQVSEPQ
HSAVESSELK YEKKYINIDK DKEAKPKTHT AKHIDDEL
//