ID A0A1A9ZH71_GLOPL Unreviewed; 1089 AA.
AC A0A1A9ZH71;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, 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};
OS Glossina pallidipes (Tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI014614-PA, ECO:0000313|Proteomes:UP000092445};
RN [1] {ECO:0000313|Proteomes:UP000092445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPAI014614-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI014614-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 AlphaFoldDB; A0A1A9ZH71; -.
DR STRING; 7398.A0A1A9ZH71; -.
DR EnsemblMetazoa; GPAI014614-RA; GPAI014614-PA; GPAI014614.
DR VEuPathDB; VectorBase:GPAI014614; -.
DR Proteomes; UP000092445; 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}; Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 24..1089
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5008402927"
FT DOMAIN 373..449
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1089 AA; 126189 MW; 7E3C4BE179A9234A CRC64;
MLSIWRIVAY VCFTAALLHG VELRPQRTEA ELLTNDQCGY ESCPKVQPNM LNVHLIPHTH
DDVGWLKTVD QYYYGSETLI QKAGVQYIID SVIQELLRDP EKRFIYVESA FFFKWWREQN
EELQEQVKML VNEGRLEFIG GAWSMNDEAT THYQSIIDQF AWGLRRLNDT FGKCSRPRIG
WQIDPFGHSR EMASMFAQMG YDGLFFGRLD YQDKSERLLT KTAEMIWRAS ANLGKSSNLF
TGALYNQYQP PPGFCFDILC ADEPIIDGKH SPENNVKRRV DDFFKFVRKQ AQYYRTNQII
ITMGGDFTYQ DANVYYKNLD KLIRYANARQ ANGSEINLLY STPSCYLKAL HDADISWPTK
DDDFFPYASD PHAYWTGYFT SRPTLKRFER VGNHFLQVCK QLTALPPTMY PEWSSHLSFM
RETMGIMQHH DAVTGTEKQK VAYDYAKRLE VAFRACGANT RAALNILTTG DKPKPVEGHK
PRSVKFEFKT CALLNISLCE VSEQSEHFVL TLYNPLSSST AEYIRVPVSD NNYQVLDDKG
VILEVQYVPI PGGLMDLAYR RSKTKYDLVF FADELPPLGY RSYYIKKTKE RPLKPVPDSP
NTSSMTSIGN EYIRLNFDTN GFLAAVTAEG MTRIISQDFL YYEGAVGNNM EFRNRSSGAY
IFRPKNDSMK IITTDLDITV YRGSLVEEVH QKFNDWISQV VRVYSQKNYA EFEWLVGPIP
VDDDIGKEII TRFDTDIKSE GMFFTDSNGR EMIKRLRNHR DTWNLEILEP AAGNYYPITT
KIALEDDRAR VAILTDRAQG GSSLQDGSLE LMVHRRLLHD DAFGVEEALN ETAYGHGLIA
RGTHYLMVGF SQKNDSPTQK ALERFAQLEV TLPTWKFFSK TNYTFEEWMT SFNNSFTGLG
KSLPKNIHLL TLEPWHNGEL LVRFEHILEK DEDPEFSKSV KFNIKEVLKN FDIHDIRETT
LDGNAWLDEH RRMEFVSDPE SIDFVNYATL SEEHQSVHLL RARRPLTKSE YHKEILPDFD
VESKSKQDPK PNTYLNTLRR NRLEQMKLDE KDLKHPREKS NNKYDVELNA MQIRTFVIYL
RQNNSFASE
//