ID   A0A239QT32_9MICO        Unreviewed;      1064 AA.
AC   A0A239QT32;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:SNU01767.1};
GN   ORFNames=SAMN06298212_11649 {ECO:0000313|EMBL:SNU01767.1};
OS   Ruaniaceae bacterium KH17.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Ruaniaceae.
OX   NCBI_TaxID=1945888 {ECO:0000313|EMBL:SNU01767.1, ECO:0000313|Proteomes:UP000214750};
RN   [1] {ECO:0000313|EMBL:SNU01767.1, ECO:0000313|Proteomes:UP000214750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH17 {ECO:0000313|EMBL:SNU01767.1,
RC   ECO:0000313|Proteomes:UP000214750};
RA   Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; FZQV01000016; SNU01767.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239QT32; -.
DR   Proteomes; UP000214750; 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:UP000214750}.
FT   DOMAIN          509..582
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
FT   REGION          692..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1064 AA;  118733 MW;  C9B9ACC9BCC1F37F CRC64;
     MTGHYAWSMR DAESFLGAVA RQPARFRQLK RIRTQVFTTV VQLDAQIVRS AEPIPFAELS
     DYPWEPLRAG AAWGRKLDCA WIHVTGSFDP AAIAGRTASV LFGLRGEALI HSPDGALLDG
     VNSVWIEREL PDAHGKWRPI RNLDLSTGRV DFFADAAYNG FLIYDVGRAV FHGATVAIRD
     DDAHDLYYDY LTLVVLADQT DDTHLAAEIW TALDKADDAV GRKDHTAARA ELAPLLARPS
     ESEFAYKAIG HGHLDMAWLW PLRETRRKAA RTYTRQLNSI GERPDFIYGT SQPQQLAWMK
     AEHPELYARI KEAVAGGRIE LQGAFWVEPD TNLPSGESLV RQALIGRRFL EEEFGIDEMR
     LCWLPDTFGY SGNLPQILKK SGMDWFQTIK LSWNKTNTFP HRSFHWRGID GSQVLVHMPP
     EGNYNSRADA ESLLVGVTQY PEAELGTALL AYGFGDGGGG PGEFHHESLA RVKNLRGLPR
     VEFSSAADFF RDLETRGVSH VHDGELYLEL HQGTYTTQAA GKRHNRVVER MLHEIEALSA
     ITGEDSRSAL EGVWREVLLL QFHDILPGSS IGRVYREAND SYESIERELA EYSAKLLARL
     PRGTSAPTRR VREPHAPEVP DLRTVGPTAL NLTSFPRSEY LKHDGEWFRA EVAPYAAAKL
     TEFSSFCAEG EARSRRTQGI VAAPELDPAT PRRMTHRSIS AGGATPRWLS EESETSEIET
     IAREYHHGLD SVPLRSTHEL ANDRLALAFG ANGEITSCRS LDTGEEIAGA GLNRLVLHKD
     NYQFPWDAWD VDEGYLDREP RPLRLVRAET FRDGPTLVRR QLLGLSGVVV DQRVVLTEGS
     PVVEFQTRVN WKATHRMLRA EFRPTHYGPT AKCEIQFGHI ERVTTERDSI EKAQFEICAH
     KWIATEDATG GFAVLNDSKY GHRAKNGLLS LNLLRAPTFP DKRADRGVHH FTYAFMPFTD
     LADVVREGYR LNNPLIVDEG VAFGSVASSS NPGVVIETIK PAEDGNGVIL RLYESLGTPC
     TTALATTLPH GTARFTNLLE HDEDPADLGA LTFSPFEIKT VRLS
//