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Database: UniProt
Entry: U4TT01_DENPD
LinkDB: U4TT01_DENPD
Original site: U4TT01_DENPD 
ID   U4TT01_DENPD            Unreviewed;       967 AA.
AC   U4TT01;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
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; ALPHA-MANNOSIDASE 2-RELATED; 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|ARBA:ARBA00022801, 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
//
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