ID E2A0Q9_CAMFO Unreviewed; 1539 AA. AC E2A0Q9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 22-FEB-2023, entry version 42. DE RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193}; DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361193}; GN ORFNames=EAG_11254 {ECO:0000313|EMBL:EFN72962.1}; OS Camponotus floridanus (Florida carpenter ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea; OC Formicidae; Formicinae; Camponotus. OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311}; RN [1] {ECO:0000313|EMBL:EFN72962.1, ECO:0000313|Proteomes:UP000000311} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311}; 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the CENP-L/IML3 family. CC {ECO:0000256|ARBA:ARBA00011060}. CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS6 family. CC {ECO:0000256|ARBA:ARBA00009512}. 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; GL435626; EFN72962.1; -; Genomic_DNA. DR STRING; 104421.E2A0Q9; -. DR InParanoid; E2A0Q9; -. DR OMA; DFHYFHA; -. DR Proteomes; UP000000311; Unassembled WGS sequence. DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-KW. DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. 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:0019843; F:rRNA binding; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:1904380; P:endoplasmic reticulum mannose trimming; IEA:InterPro. DR GO; GO:1904382; P:mannose trimming involved in glycoprotein ERAD pathway; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:InterPro. DR CDD; cd15465; bS6_mito; 1. DR Gene3D; 1.50.10.10; -; 2. DR Gene3D; 3.30.70.60; -; 1. DR Gene3D; 3.50.30.30; -; 1. DR InterPro; IPR012341; 6hp_glycosidase-like_sf. DR InterPro; IPR025204; CENP-L. 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; IPR000529; Ribosomal_S6. DR InterPro; IPR035980; Ribosomal_S6_sf. DR InterPro; IPR036026; Seven-hairpin_glycosidases. DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6. 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; PF13092; CENP-L; 1. DR Pfam; PF01532; Glyco_hydro_47; 2. DR Pfam; PF02225; PA; 1. DR Pfam; PF01250; Ribosomal_S6; 1. DR PRINTS; PR00747; GLYHDRLASE47. DR SUPFAM; SSF52025; PA domain; 1. DR SUPFAM; SSF54995; Ribosomal protein S6; 1. DR SUPFAM; SSF48225; Seven-hairpin glycosidases; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR601382-2}; KW Centromere {ECO:0000256|ARBA:ARBA00023328}; KW Chromosome {ECO:0000256|ARBA:ARBA00022454}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Glycosidase {ECO:0000256|RuleBase:RU361193}; KW Hydrolase {ECO:0000256|RuleBase:RU361193}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR601382-2}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Reference proteome {ECO:0000313|Proteomes:UP000000311}; KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274}; KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..1539 FT /note="alpha-1,2-Mannosidase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003156797" FT DOMAIN 536..629 FT /note="PA" FT /evidence="ECO:0000259|Pfam:PF02225" FT REGION 1100..1122 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 362 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR601382-2" SQ SEQUENCE 1539 AA; 175667 MW; 3E8FAED49EA0AA13 CRC64; MACDALIWGL LFVGCVQILW AMSEDDPLEY MSKEEREALK EEARDMFYHA YNAYMENAYP ADELMPLSCK GRYRGSEPNR GDIDSTLGNF SLTLVDTLDT LVVLGDLEEF ENAVKLVARN EKAQKAMDVL WRMRHRGTDL MGSVLNVNSG DWVRRDSGVG AGIDSYYEYC LKAYILLGDE KYLGRFNKHY QAVMKYVSQG PMLLDVHMHR PNTNSKNFMD ALLAFWPGLQ VLKGDIKPAV ETHEMLYQVI QRHNFIPEAF TTDFQVHWGH HPLRPEFLES TYFLYRATGD HYYLGVGRKV LKSLQTYARV PCGYAAVSDV RTNKHDDTMD SFVLSETFKY LFLLFAEPGE LILELDEFIF TTEGHLLPLT LASIRTNISS DFERDIVYVD EFDRTCPNSL HLFPASVRQP LRNMVEDVCP RRSIKRRLSA SQFQANNLEH LKILSDMGIT TLTLADGRIQ LLHTFSNAKT TQDSEEGLLF MQEMVELSKM QMQQPETKPQ TVTFIRPNTD PLEKVTLLAG PAQFGPDLQN FDKISGKVIF TYPPAACTDL HNADKLAGKI AIVNRGNCMF IEKARRIQKA GALAGIVLDN IAGSSAATSP MFAMSGDGKE IDDVTIPVVF LFFTEAAELM KAINAADGDL TVTLGIYSSK EEIQLKAPTD LSLFERVKGS LKSFLSRHVT PQATTIGSSL DITIPVIESQ EDQEDVVDFH YFHAEIIKDS LNGEVKITAT SEAAIIILRP VSTPTEILWH QLKEVFVNQI FLNRKQNKGI RIRSFILESY YNWVNKERGL LTKTSLSYKV RWFLSELLVV APNSSIKKMG QLLELNKQKL LKQYLLTNMD TMVLNLKTVA TKLKSIKSVR PKMEQLLKIS ESGITQVEYY SFLRHLLVDL FDEEDEIINR HIALLDHIHA EVHSIYQEIL IDGVHRHLEK LGEEDHSYYD ILIADLQKNL KNVDKEENLL GKIKENDLAV AEFISDSNGG KGDIETKNIN ILKKDKKSST NEIKDFEYFI LTEIEKAVKY SEQNTLEKYD DVNSELKNVV IQDKKNKDAV KSDDIILFSK NQSEGDDRKN EVQSLQKKLG LQATKAVDVK FEKVTIQEKQ EEKSSTDSIS DTNKNVRSSG IMYTPRTPQM RERQRFNLTI RPDNEEDDVS GLEDLVGQTW NVYAVSALFG FQQDDIHFKL YSKRLREEIA STLSHEDVTY DAKFSIMENV VLKPNHENHP AIKIEVLAKN NDTEKEKSLY QGILLSWDIT QSEQSKENLI RLPLLLCRGT STGIDAVHAT IIRMFDCSII VLPAKECDLS WLVPIIIMTN KEEPVVSGEI QMVYTVPELP ITDTITVKFQ TGDLRKILSA IITNQNDENV FLNREHIEIF FEALHKQMLI LGGLKLGLCT LHRINLPGIT IMENRPELVA TLKRATSTIF NTGGFIRKIE NWGVKPLPCK AVAHGQVHRE ANHFLIYFDV PPRELDKIVD ECNRDIDIVK LQVFKQMEPK KWNCTFHEEM LPPPYRPGVQ KLMELAKRRN NNKYQFKYNS GLNYYPFNK //