ID A0A1V4JFH2_PATFA Unreviewed; 1013 AA.
AC A0A1V4JFH2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN Name=MAN2B2 {ECO:0000313|EMBL:OPJ70896.1};
GN ORFNames=AV530_017235 {ECO:0000313|EMBL:OPJ70896.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ70896.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ70896.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ70896.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ70896.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OPJ70896.1}.
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DR EMBL; LSYS01007721; OPJ70896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JFH2; -.
DR STRING; 372326.A0A1V4JFH2; -.
DR Proteomes; UP000190648; 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; cd10811; GH38N_AMII_Epman_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; 1.
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:SF28; EPIDIDYMIS-SPECIFIC ALPHA-MANNOSIDASE; 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW Hydrolase {ECO:0000256|RuleBase:RU361199};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 20..1013
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5017845147"
FT DOMAIN 352..435
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1013 AA; 115428 MW; 404BBE1C23B1FB62 CRC64;
MGTPLLLLLL FSLPLRAGGR GGLRVFVVAH SHMDVGWIYT VQESMHAYAA NVYSTVVEEL
MNGKQRKFIA VEQEFFRLWW DGVATDKHKK EVHQLLQEGR LEFVIGGQVM HDEAVTLIDD
QILQLTEGHG FLYETFGIRP QFSWHVDPFG ASATTPTLFA LAGFNAHLIS RIDYDLKDDM
QKNKKLQFVW QGSPSLSEKQ EIFTHVMDQY SYCTPPRLPF SDRSGFYWNG IAVFPDPPKD
GVYPDMSLPV TDTNIHLYAQ AMVANIKERA AWFRTSDVLW PWGCDKQFFN ASVQYSNMDL
LLDYINKHSD ELGVTVQYAT VGDYFQAVYN RNLTWEIRDS QDFLPYSTEA FQAWTGFYTS
RSALKGIARR ASSLLYAGES FFTMYVQKHP AGPICKYRAL KQLQSLRWAV SEVQHHDGIT
GTESPKVKDM YTDNLIYGMF NVKKLMASII FDMNNAKKDG EVYSSVYNKH SRIPGATGVD
QYVVVYNPLA WNITTFVTVS VSHSAMGVYD ELGHSVPAQV QSSVESRSAY DLYILVEISG
LSYRKYNVKP LNGKQSAFIG RLVKYKRKDI TRADQKSQQF LPVVNNCYQV LFDPNTNLMR
SITERETNQT VQLTQEFLEY HVNGDVAKGP ISDNYFFAPN GSAVPVSKAV GLEVVSGKLM
TEIRQYFYSN VTAQNYTYAV YTRIYTVPEG YDGNMLCHRI EQEYRVGPLE INREAVLRTT
TNLNTEQLLY TDNNGYQIQK RPFKAYVDNP VARNYYPMVQ TAYIEDNTTR LMLLTERAHG
VSSQGNGQVE VMLHRRLWNN HQWDVSNNLT LNDSSVVRPV IWLILGTKAV SNILYRTSAL
ALEHRPIVMF GALSGDKPKL PRQLQQHSVH ESSVTLPPNL HLQTLSIPGW RYSSDHAEQV
HNVHVGKQKQ GDADFSRVLL RIRHLYEVGE DPVLSQPVTV NLKSLLQGLG SVKQVEERSL
TGTWDVNTLT RWKWKTVKSP SKGFSNSSET SENCTVTIHP KEIRTFFVYF QGQ
//
