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Database: UniProt
Entry: A0A1A9ZH71_GLOPL
LinkDB: A0A1A9ZH71_GLOPL
Original site: A0A1A9ZH71_GLOPL 
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
//
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