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
//