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Database: UniProt
Entry: A0A101U9D3_9ACTN
LinkDB: A0A101U9D3_9ACTN
Original site: A0A101U9D3_9ACTN 
ID   A0A101U9D3_9ACTN        Unreviewed;      1004 AA.
AC   A0A101U9D3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:KUO06627.1};
GN   ORFNames=AQJ67_01325 {ECO:0000313|EMBL:KUO06627.1};
OS   Streptomyces caeruleatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=661399 {ECO:0000313|EMBL:KUO06627.1, ECO:0000313|Proteomes:UP000053429};
RN   [1] {ECO:0000313|EMBL:KUO06627.1, ECO:0000313|Proteomes:UP000053429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24802 {ECO:0000313|EMBL:KUO06627.1,
RC   ECO:0000313|Proteomes:UP000053429};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces caeruleatus NRRL B-24802, type
RT   strain for the species Streptomyces caeruleatus.";
RL   Submitted (OCT-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:KUO06627.1}.
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DR   EMBL; LMWY01000001; KUO06627.1; -; Genomic_DNA.
DR   RefSeq; WP_062716081.1; NZ_KQ948924.1.
DR   AlphaFoldDB; A0A101U9D3; -.
DR   STRING; 661399.AQJ67_01325; -.
DR   OrthoDB; 9772207at2; -.
DR   Proteomes; UP000053429; 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:UP000053429}.
FT   DOMAIN          519..597
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
FT   REGION          634..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1004 AA;  111188 MW;  77EA75B593026C58 CRC64;
     MHDDRSLVEA RLKRVLDERV RPAVYPESVP LDVAVWHAPG EPVPVAEGLA AEPEAIEVGA
     RWGAPWGTSW FRVTGTVPEA WAGKTVEALL DLGFDENMPG FQCEGLVYRP DGTPVKGLNP
     RNQWVRIGAP VEGGEEVCLH IEAASNPVIL DYHPFLPTQL GDKETAGSEP QYTLTRMDLA
     VFDETVWQLV LDLEVLGELM AELPVESARR WEILRAVEKA LDAIDLQDVG GTAARARSRL
     TRVLATPAVP SAHRISAVGH AHIDSAWLWP LRETVRKVAR TTSNMTALIE DEPDFVFAMS
     QAQQWAWVKE HRPEVWARVK KAVADGRFVP AGGMWVESDT NMPGSEAMAR QFVHGKRFFL
     DEFGIENDEA WLPDTFGFAA GLPQIIKAAG SKWLLTQKIS WSQTNKFPHH TFQWEGIDGT
     RIFTHFPPVD TYNCSMKGSE IAHAARNFKD KGRARHSLAP TGWGDGGGGT TREMVAKAAR
     LRDLEGSATV VWETPDAFFR KAEAEYPEPP VWVGELYLEL HRATLTSQAR TKQGNRRSEH
     LLREAELWAA TAAVRAGFPY PYDELDRIWK TVLLHQFHDI LPGSSIAWVH REARKTYEQV
     AEELTGIIRA AQRALAGDGE RILLFNSAPH TRAGVPAGGV GTPETQGRTR VTPRPDGGHV
     LDNGLLRVEV DGRGLVVSVY DIDADRETIA PGGAANLLQL HSDFPNMWDA WDVDEFYRNT
     VTDLTDARIV DESGDGVRVV RAFGSSRVTQ RLSLAPGDKR LLVDTVVDWH ETEKFLKLAF
     PLDVHAERYA SETQFGHFHR PTHTNTSWEA AKFEACNHRF VHLAEPGWGV AVVNDSTYGH
     DVTRTVRTDG DRGTTTTVRV SLLRAPRFPD PETDQGVHRF RHALVPGAGI GDAVREGWRI
     NLPERRVSGG VDEVAPLVTV DQDAVVVTAV KLADDGSGDV VVRLHEAHGG RVRATLTAGF
     EVADVVATDL LERALPEAPA YDGRRVALRL RPFELVTLRL RRAL
//
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