ID E3LPV2_CAERE Unreviewed; 1148 AA.
AC E3LPV2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN Name=Cre-aman-2 {ECO:0000313|EMBL:EFP05900.1};
GN ORFNames=CRE_27342 {ECO:0000313|EMBL:EFP05900.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361199};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
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DR EMBL; DS268412; EFP05900.1; -; Genomic_DNA.
DR RefSeq; XP_003114562.1; XM_003114514.1.
DR AlphaFoldDB; E3LPV2; -.
DR STRING; 31234.E3LPV2; -.
DR EnsemblMetazoa; CRE27342.1; CRE27342.1; WBGene00052389.
DR GeneID; 9814880; -.
DR KEGG; crq:GCK72_018141; -.
DR CTD; 9814880; -.
DR eggNOG; KOG1958; Eukaryota.
DR HOGENOM; CLU_004690_1_0_1; -.
DR InParanoid; E3LPV2; -.
DR OMA; GHQWLKY; -.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblMetazoa.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR CDD; cd10809; GH38N_AMII_GMII_SfManIII_like; 1.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR PANTHER; PTHR11607:SF3; LYSOSOMAL ALPHA-MANNOSIDASE; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW Hydrolase {ECO:0000256|RuleBase:RU361199};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 518..599
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 75..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 131224 MW; 5381F4F9FCF4D856 CRC64;
MGKRNFYIIL SLGVFLTVSL YLYNGIETGA EAIAKRQQYV DELRRKIGSL EQVAEQNGKT
IDRLEQQVRQ VKVEKSVDFD EDKDKTEEKE KEQEQEQEVA PVPVRGNRGN EGMAHIHQVQ
KHHKPTPPMT DICNIRENIS VAHSDLQMLD LYETWKFENL DGGVWKQGWK IEYDAEKVKA
LPRLEVIVIP HSHCDPGWIM TFDEYYSRQT RNILNGMAKH LGEKDEMRFI YAEISFFETW
WREQSEETRK KVKGYLEAGK LEIVTGGWVM TDEANAHYHS MVTELFEGHE WIQNHLGKNA
IPKSHWSIDP FGLSPSLPHL LTSANITNAV LQRVHYSVKR ELALKKNLEF YWRQLFGSTG
HPDLRSHIMP FYSYDIPHTC GPEPSVCCQF DFRRMPDGGK SCDWGIPPQR ITDENVAERA
QMIYDQYRKK SQLFKNSVIF QPLGDDFRYD IDFEWNSQYE NYKKLFEYMN SKSEWNVHAQ
FGTLSDYFKK LDTAISESGE KLPTLSGDFF TYADRDDHYW SGYFTSRPFY KQLDRVLQHY
LRSAEIAFSL ANIEEEGMME SKVFEKLVTA RRALSLFQHH DGVTGTAKDH VVLDYGQKMI
DALNACEDVL SESLVVLLGI DSTKKMEMDE KRVNENLLPE KLVYKVGQNV VLFNTLSRNR
NEPVCIRVDS VDAGIEAEPP VTKQQISPVI EYNEESKKLV AKDGVFELCF LASLGPMESV
SLKLVKSTTT SKSEIRTNSK IQVDSSFKSS TVGNGDFIVQ NDKVKAEFDG ENGMIKKATS
LVDDKPIDLN SHFVHYGARK ARRKFANGNE DNPAGAYLFL PDGEARELKK EENEWIVIGG
DLVRRVFATP MSDLKILQTY TLYQGLPWID LDNEVDVRSK ENFELALRFS TSISSNDEFF
TDLNGLQMIK RRRQTKLPTQ ANFYPMSAGV YIEDDASRMT IHSAQALGVS SLASGQIEIM
LDRRLSSDDN RGLQQGVRDN KRTVAHFRIV IEPMSPTSSN KKDERVGFHS HVGHLATWSL
HYPVVKMMGE TTPKSIASKN LENELNCDLH VVTFRTLASP TTYEANERST AAEKKAAMVM
HRVVPDCRSR LTLPDTSCLT SGIEIEPLKL ISSLKSARQT SLTNLYEGQK SEQFILQPND
VSSILVSF
//
