ID A0A0A0AKZ0_CHAVO Unreviewed; 822 AA.
AC A0A0A0AKZ0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Beta-mannosidase {ECO:0000256|ARBA:ARBA00015707};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE AltName: Full=Lysosomal beta A mannosidase {ECO:0000256|ARBA:ARBA00032581};
DE AltName: Full=Mannanase {ECO:0000256|ARBA:ARBA00033445};
DE Flags: Fragment;
GN ORFNames=N301_12588 {ECO:0000313|EMBL:KGL93700.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL93700.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL93700.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL93700.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose
CC residue from the non-reducing end of all N-linked glycoprotein
CC oligosaccharides. {ECO:0000256|ARBA:ARBA00003150}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC in beta-D-mannosides.; EC=3.2.1.25;
CC Evidence={ECO:0000256|ARBA:ARBA00000829};
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC {ECO:0000256|ARBA:ARBA00004740}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; KL871849; KGL93700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AKZ0; -.
DR STRING; 50402.A0A0A0AKZ0; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR041625; Beta-mannosidase_Ig.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041447; Mannosidase_ig.
DR PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF17753; Ig_mannosidase; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 3.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 286..444
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 645..738
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 742..821
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL93700.1"
FT NON_TER 822
FT /evidence="ECO:0000313|EMBL:KGL93700.1"
SQ SEQUENCE 822 AA; 94623 MW; 98FE3ACB792603E4 CRC64;
DPYYRFNDVM YRWISLDNWT YSRTFKTPFD VRKWQKVNLV FEGVDTVAQI LINNITLGRT
DNMFNRYSFD ITSVIKEVNF VEVRFLSAIS YAAEQSRCHK AYSIPPACPP PVQKGECHAN
FIRKEQCSFS WDWGPSFPTQ GIWKDVRIEA YNHYHLIYFS LTSVFAKSAQ QWSLEIESIF
DVISSKPIAG LVTVNIPKLQ TQQTFSVKLQ PGEGSIVLLV NINKVRSSTV EAWWPNGHGK
QTGYNMTTTF IMEAGYEIEK FSKAYFRTVE LVQEPIPGSL GLSFYFRING RPIFIKGSNW
IPADSFQDRV TYDTLWLLLK SAADANMNAL RVWGGGVYEQ DEFYSICDEL GIMIWQDFMF
ACALYPTDQN YLESVRAEVS HQVRRLKSHP SIILWSGNNE NEAAIASNWF SIPYADREVY
IKDYVMLYVK NIREIVLTED KSRPFIASSP SNGLESVKEG WVSQNPYDTH YGDTHFYDYI
NDCWNWTVYP KTRFASEYGF QSWPSFSTIK KVSSTEDWSY TSNFSLHRQH HENGNDQMLQ
QIGYHFKLPQ STDPIKKFKD MIYLTQVMQA QCIKTETEFY RFSQSEIIKG EGHTMGALYW
QLNDIWQAPS WASLEYGGKW KLLHYFARNF FAPLLPVAYE DKGVLYIYGV SDLHVDHKLT
LRVVVYTWSS LEPVCTLAKD VVTVKAQSAV PIYKESINDF LERCGNCTRK SCVITFCLVG
EDGLQSPTNH HFLSSLKDAV GLEKSHLSAS VSQQDDVYIF ALQTTAVAPF VSLDVGSIKG
RFSDNGFLMT EKKKVVMFYP WEPTSVEELE KSLTLTSLVD II
//
