ID N6TR79_DENPD Unreviewed; 1118 AA.
AC N6TR79;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
DE Flags: Fragment;
GN ORFNames=YQE_12490 {ECO:0000313|EMBL:ENN70826.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ENN70826.1};
RN [1] {ECO:0000313|EMBL:ENN70826.1, ECO:0000313|Proteomes:UP000019118}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
RN [2] {ECO:0000313|EnsemblMetazoa:ENN70826}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JAN-2017) to UniProtKB.
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; APGK01057855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; APGK01057856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; APGK01057857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB741282; ENN70826.1; -; Genomic_DNA.
DR AlphaFoldDB; N6TR79; -.
DR EnsemblMetazoa; ENN70826; ENN70826; YQE_12490.
DR HOGENOM; CLU_004690_1_0_1; -.
DR OMA; WRQNWDM; -.
DR Proteomes; UP000019118; Unassembled WGS sequence.
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; 2.60.40.1360; -; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT DOMAIN 489..575
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ENN70826.1"
SQ SEQUENCE 1118 AA; 128239 MW; D1BE7279AF2FF241 CRC64;
MKLKRAVIIC GFLLTLVVVF TIYSAKELTL SVRKTSITQD YKDNQWLHFE DRIKQLEDDL
SRHHNAVAEI KVAMQNILSS STNAARKSPV NYIPLETPQV STMIYNSSCP ISKFYRPKVD
IQMLDLYNTL TFDNPDGGVW KQGWRIQIDE KEWNRQNKLK VFVVPHSHND AGWTRTLLEY
YSTQTKHILN NMLQKLPEDP RRKFIWAEIS FFSMWWAELD NGNKEAVKRL IKNNQLEIVT
GGWVMNDEAS SHYISIIHQL TEGHQWLKKH LNYTPISHWS IDPFGLSSTQ PALLKSSGLQ
NMLIQRVHYS VKKHLAKTRN LEFRWRQLWA DSDNTDIFCH LMPFYGYDIP HTCGPDPKVC
CQFDFKRLPN HGLQCPWKVP PVKITDENVA ARAELLLDQY RKKSKLYQTN VVLAPLGDDF
RYDHITEWDV QYNNYQKLFD YMNKKLDLHV QAQFGTLSDY FAAVQKEKEL TKFPVLSGDF
FTYADRDDHY WSGYYTSRPF YKRMDRVLLS YIRAAETIEA LTYHSGKRMS WDNKEATGLG
HFLVSSRQEL SLFQHHDGIT GTAKDHVMVD YGKRMLLAIH DCQRIIQHCV NVLLEGPGSQ
QSLKDDVTHY NFDDVWHSHN TLPEKMQITI GVPDLPSKKI VIYNSLAFAR HEVVTFNINT
QFIEVSPIFE YGSTMSTTKY EISFIASIPA FGTVSYTINS VYQENLPQET SFADVKIYNQ
YGDVTALRGF KVNVSERAEE FTFQNARIVA SFNKLGLLKA VKIGSSIVPV HLDFAKYGVA
ARPVDRSGAY LFLPDGEASE LKIENTVVNV VEGPVISSLT VQLPYVLHKA TLYNSPGADG
LSVELTNTVD IEETNNFELV MRMATNIDSQ DEFFTDANGY QLVKRRRFKK LPLQANYYPM
PTKAYIEDKD TRLTVLSSSP LGCSSLTGGE IEIMLDRRLN QDDNLGLGQA VLDNHPTKHI
FRVLVEKRPP GCETSVSDHP SGFPTVSASV ASESLLNPLF KLIKMKDDEE NKVEFYAPNF
QLGVDLLIPT FKTNVFMKGT YHTGLVLHRQ FLDTCFLDEA LIKDFPLSEG KVNLRGLFPH
QQSTSLYQAT LSFLKTEKIL HVDDDISLCP MEMKAFYI
//
