ID   D3A928_9CLOT            Unreviewed;       809 AA.
AC   D3A928;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Glycosyl hydrolase family 38 N-terminal domain protein {ECO:0000313|EMBL:EFD01704.1};
GN   ORFNames=CLOSTHATH_00098 {ECO:0000313|EMBL:EFD01704.1};
OS   Hungatella hathewayi DSM 13479.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX   NCBI_TaxID=566550 {ECO:0000313|EMBL:EFD01704.1, ECO:0000313|Proteomes:UP000004968};
RN   [1] {ECO:0000313|EMBL:EFD01704.1, ECO:0000313|Proteomes:UP000004968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13479 {ECO:0000313|EMBL:EFD01704.1,
RC   ECO:0000313|Proteomes:UP000004968};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2010) 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:EFD01704.1}.
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DR   EMBL; ACIO01000009; EFD01704.1; -; Genomic_DNA.
DR   RefSeq; WP_006770664.1; NZ_GG667607.1.
DR   AlphaFoldDB; D3A928; -.
DR   HOGENOM; CLU_003442_1_1_9; -.
DR   Proteomes; UP000004968; 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; 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:0000313|EMBL:EFD01704.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          268..346
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   809 AA;  91500 MW;  1A8F3F1AAEE19C4B CRC64;
     MEKDKKLYMI GNAHIDVVWL WQWQEGLQEV KATFKSVLDR MKEYDDFIFT GSSAAYYEWV
     EENDPSMFEE IRSRVKEGRW VIVGGWWTEP DCNAPCGESF VRQGLYGQRY FEEKFGVKAV
     CGYNVDSFGH NGNLPQILKK CGMDSYVFMR PGRHEKGIAG ENFVWKSADG SAVNAFRLPF
     EYCTWPDQIE EHVRRCAGEI KNSDGGIMCF YGVGNHGGGP TKKNIDSIHR MNARPDMPEL
     QLSSPNEYFE DVKKRGRDLP VVCGGLFHHS SGCYSVESRV KALNRAAEMR LLMAERVSVM
     AGLLTGIRYP AEEYQKAWKS VLFNQFHDIL AGTSLRESYE DAAEDYGYAL HAAGRGLNSA
     VQSLSWQINI PMEEGMKPLV VVNPNAFNTK AEVQAESWTL KEGTVLLDEN GNQIPCQLVQ
     SSAALQGRCR ICFVADLPSL GWRTYRFAVR EKAETFPEVA VSECSAENRW FKLTLDPETG
     YIASLLKKND GTEYFSGPAA VPVVIRDESD TWSHAVRIFD EVIGRFKAVS VRTVENGPVK
     CVIRVTSVWG NSRIIQDFSV FQDLDYIAVK TTVDWHEKQA MLKLQFPMNM NYLRTSWEIP
     YGMEQREPDG EEYPMQMWLD LEGTNPGMET SMNGLSILNE GKFAGSATGK TASLTVLRSP
     VYTHHEPYQL QENLEYVYID QGTQTFTYGL YPHDGSWENA ATVRRAKVMN CRPIALFETY
     HEGRLEQTGS LMEVNQENIV VEVLKKAEDG SGDLILRAYE TAGRAVKAEL TIGVLEQTIE
     ADFQPFEIKT LRLPGQKGGE AVWTDMLEE
//