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Database: UniProt
Entry: A0A0F0H0V6_9ACTN
LinkDB: A0A0F0H0V6_9ACTN
Original site: A0A0F0H0V6_9ACTN 
ID   A0A0F0H0V6_9ACTN        Unreviewed;      1010 AA.
AC   A0A0F0H0V6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:KJK47288.1};
GN   ORFNames=UK14_21135 {ECO:0000313|EMBL:KJK47288.1};
OS   Streptomyces sp. NRRL F-4428.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609137 {ECO:0000313|EMBL:KJK47288.1, ECO:0000313|Proteomes:UP000033569};
RN   [1] {ECO:0000313|EMBL:KJK47288.1, ECO:0000313|Proteomes:UP000033569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-4428 {ECO:0000313|EMBL:KJK47288.1,
RC   ECO:0000313|Proteomes:UP000033569};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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:KJK47288.1}.
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DR   EMBL; JYJI01000179; KJK47288.1; -; Genomic_DNA.
DR   RefSeq; WP_045323104.1; NZ_JYJI01000179.1.
DR   AlphaFoldDB; A0A0F0H0V6; -.
DR   PATRIC; fig|1609137.3.peg.4872; -.
DR   OrthoDB; 9772207at2; -.
DR   Proteomes; UP000033569; Unassembled WGS sequence.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
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; cd10789; GH38N_AMII_ER_cytosolic; 1.
DR   Gene3D; 2.60.40.2220; -; 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   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR041147; GH38_C.
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   PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR   PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF17677; Glyco_hydro38C2; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033569}.
FT   DOMAIN          516..595
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1010 AA;  111735 MW;  AD5C8B03F0CAC952 CRC64;
     MHDDRSITEH RLRRVLHERI RPAVHSSPLP LTVERWDAPG EPVPVAEGLA APYEPCAPGD
     TWGPAWGTTW FKVTGTVPAA WAGRTVEAVL DLGFDRMMPG FQCEGLVHRA DGTGIKALNP
     YNDWVRVADR AEGGERIEWY VEAAANPVLV DHRATYEGDL RTSGDRPLYR LARMDLTLFE
     TEVWELVQDL DVLYELMTQL DTGDARRYEI LRALGAALDA VDLSDVPGTA AAARAHLADV
     LAAPANASAH RISAVGHAHI DSAWLWPLRE TVRKVARTVS NMVNLMDGHP DLVFAMSQAQ
     QLDWIKTHRP ELFERVKKKV ADGQFVPVGG MWVESDTNMV GGEAMARQFL YGKKFFLDEF
     GIDTHNVWLP DSFGYTAAMP QLVRLSGSRW FLTQKICWSQ VNDFPHHTFW WEGIDGSRVF
     THFPPVDTYN SDLGGAQMAH AARNYREKGW GSRSLVPFGW GDGGGGPTRE HLARARRQRD
     LEGSPRIEIE RPDAFFEKAR AEYEDAPVWA GELYLELHRG TYTSQAKTKQ GNRRSESLLR
     EAELWAATAA VRVPGYAYPY EDLERIWKTV LLHQFHDILP GSSIAWVHRE ARETYGRVAQ
     ELRDITLAAQ RALAGEGTEE LVFNCAPHAR RGIPAGGAGR PAQPPEPVTV EERHGGGHVL
     ANGLLVVEID ARGLIVSVHD LRARREAVAP GRAANLLQIH PDFPNMWDAW DVDEFYRNNV
     TDLDDLDGLD GLEVAESGPR SATVRVTRSF GRSRAVQQIT LRAGAKTLDI VTDVDWHETE
     KFLKAAFPLD VKADRTASET QFGHVYRATH TNTSWEAAKF EICAHRWIHA EEPGWGVALL
     NDSTYGHDVT RDVRPDGGQT TTVRLSLLRA PRYPDPETDQ GAHTLRFSLA PGAGIGDAVR
     EGHALNLPER TVPGAGPVAP LLAVDSDAVV VEAVKLAEDR GGDVIVRLYE SRGGRATATL
     TASFPITGAV ESDLLERPLA GSAVGVPTPA DTVPLTLRPF QIVTLRLRRP
//
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