GenomeNet

Database: UniProt
Entry: A0A443RPS0_9ACAR
LinkDB: A0A443RPS0_9ACAR
Original site: A0A443RPS0_9ACAR 
ID   A0A443RPS0_9ACAR        Unreviewed;      1035 AA.
AC   A0A443RPS0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=B4U79_08075 {ECO:0000313|EMBL:RWS17228.1};
OS   Dinothrombium tinctorium.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC   Trombidioidea; Trombidiidae; Dinothrombium.
OX   NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS17228.1, ECO:0000313|Proteomes:UP000285301};
RN   [1] {ECO:0000313|EMBL:RWS17228.1, ECO:0000313|Proteomes:UP000285301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UoL-WK {ECO:0000313|EMBL:RWS17228.1};
RA   Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA   Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT   "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT   transferred genes associated with secondary metabolism.";
RL   Gigascience 0:0-0(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RWS17228.1}.
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; NCKU01000106; RWS17228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443RPS0; -.
DR   STRING; 1965070.A0A443RPS0; -.
DR   Proteomes; UP000285301; Unassembled WGS sequence.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
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   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   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:UP000285301};
KW   Signal {ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT   CHAIN           17..1035
FT                   /note="Alpha-mannosidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT                   /id="PRO_5018814492"
FT   DOMAIN          346..421
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1035 AA;  119862 MW;  5CCC6B7750CEAC86 CRC64;
     MKSCALLLLL FHFAKNEYIY PRKANCGYKS CPVTKPGLLN VHIVCHTHLD TGWVETYDEY
     YFRYVRDILD SVVNNLYQDP NRKFIFVETS FFSRWWDEQN DVIKNRVFWL VQTGQLEFIS
     GGWSMNDEAT PRYQAIIDQM TIGHRWLNNV FGECGKPKIG WQIDPFGHSR EQASIFAQMG
     FDGLFLGRID FQDKFIREKT KTMEFIWKSS PSLGKKADIL TGVLPNVYWP PSGFCFDVNC
     FDEQIYEFNA ERRAQEFIRL MKQQASHYST NHTIVTMGMD FYYRDANKWY TNLDRLMAAV
     NKIGNQEGIH VFYSSPSCYL KSLYESRRQW PVKLDDFFPY ADKFNSYWSG YYTSRPALKY
     HIEYANNIMQ AAKQLTVLAN LAESYRKKLT PLQEALAILQ HHDAITGTAK QYVTDDYTNM
     LSVGVKSAEE VITEALHRIW LADGIIPTSS LHFCNNLNVS ECFVTEMINQ TTDAVVTIYN
     PIAHSVKSYI KLPVIGSGFR VRDSFGAVIT SQMVPNHYAV NQLPERASRS HSTLVFRAML
     PPLGFTSFAI DKIDTNTIPM PNQMSQIYES PQFYEEATIS NGRVSVIVDG QSGLLKSVIL
     KDGRKVDITQ NFFIYQAESR FSGEKPSGAY AFNPTETQPL PVSEIASFKV IRGPLVEEIH
     QNFSPWVSQT IRIYQHVDYI EFDWIVGPIP IENWSFDAGQ EVVSRFNTNF NTNGTFFTDS
     NGRETLRRIR DHRPTWELDT TEKVASNYYP VTSWAFIRDY KLDLQLTILP DRAQGGSSLK
     DGSLELMIHR RLLQDDGFGV DEALNEPGVD KKGLVVRGKH RVFVNDIQES VRQMRIMSKS
     LNNKPIFAFR KRSVPALQRH RSSLLQASKN NDRSTFVGLN RKLPANIHLL TLEPWDDNRV
     LLRLEHFFEI NEDPKYSRPR RVALRDLFTP FRIVEVIEMN LSANTEKKYL EYRRLQWQPQ
     YDPYANYTNV LDQVDIEDLE LVTNTTSSNS DISGPSFVIT IHPMEIRTFL VRTDARENCK
     PNILNRYNRY RGRYC
//
DBGET integrated database retrieval system