ID U4TT01_DENPD Unreviewed; 967 AA.
AC U4TT01;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=D910_01124 {ECO:0000313|EMBL:ERL83857.1};
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:ERL83857.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL83857.1, ECO:0000313|Proteomes:UP000030742}
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).
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; KB630779; ERL83857.1; -; Genomic_DNA.
DR AlphaFoldDB; U4TT01; -.
DR Proteomes; UP000030742; 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; cd10810; GH38N_AMII_LAM_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; 2.
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 InterPro; IPR048534; Man2a1-like_dom.
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 Pfam; PF21260; Laman-like_dom; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT DOMAIN 307..382
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 967 AA; 110400 MW; 8DA7A4E9F73B9826 CRC64;
MKRLFSGNTR NQNAGVQYIL NTVVDSLRKD KNRRFIYVET AFFWKWWIKQ HDIVKSRVRN
LVNNGQLEFI SGGWSMNDEA TTHYHSIIDQ MTWGLRKLND TFGECGRPKL GWQIDPFGHS
KEMANIFAQL GFDGVLLGRI DYQDKQYRWQ TKTPEMVWRG SESLGEASEI FTGVMYNTYG
PPPGFCFDLL CSDEPLIDDK NSFEYNVDSR VNDFFRYLDN VTKVYSTNNV IITMGEDFNY
QDAESWFVNL DKLIYYGNQR QANGSKYNLI YSTPSCYVKA IYDETEGKNA WRLKQDDFFP
YASDPHAFWT GYFTSRPAIK RFERYGNNFL QVCKQLYALA DLGPEDRIDL NALREAMGVM
QHHDAITGTE KQHVAFDYAR HLQKGIDECE IITTAAISKL VSKTNPLFNE STLDLLKVNT
CPLLNISQCA ESETTNKQFI VTVYNPLSRN VDKIVRLPIL GTGYSVHDRV GENITTQIVP
IPEFVKKIPG RTSKADYELL FIARALPPLG WSSYVVTDIS HLQDQREMPY ENSDSESEVF
IDPKTGLITS IVVNDVSVPV SQNFYYYNGF VGDNDDFQNR SSGAYIFRPD GPIVKISEKA
SYKIYSGKIV SEVHQVFNEY VSQVIRVNAI DNYVEFDWVI GPLPQNQQRG IEVVTKYTST
LKSDSIFYTD SNGKENLKRV RNFRPTWELN VSEPIAGNYY PITSQISIRD EDADMDLVVL
VDRAQGGSSL KDGEIEVMLH RVCLHDDAFG VGEALNETAF GKGLVVRGSH YVTVGHRQTN
NSEGIAAITK DIAQRRLLDT WTFITPFTNN DEISNYSQFS GLTQSLPRNV QILTLEPWIG
FSFLLRLEHV FESNEDAELS QPVVVPLANL FTPFEILSAE ETTLGANQWL KDSNRLHFAT
NGSLEDLRYE DYNIVTDFNS AVPKLWTEEN INNRLTRSTV INAFDDPLNI TLSAGQTRTF
IIQVNNK
//