ID A6DIB6_9BACT Unreviewed; 1041 AA.
AC A6DIB6;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Glycoside hydrolase family 38 central domain-containing protein {ECO:0000259|SMART:SM00872};
GN ORFNames=LNTAR_09374 {ECO:0000313|EMBL:EDM28770.1};
OS Lentisphaera araneosa HTCC2155.
OC Bacteria; Lentisphaerota; Lentisphaeria; Lentisphaerales; Lentisphaeraceae;
OC Lentisphaera.
OX NCBI_TaxID=313628 {ECO:0000313|EMBL:EDM28770.1, ECO:0000313|Proteomes:UP000004947};
RN [1] {ECO:0000313|EMBL:EDM28770.1, ECO:0000313|Proteomes:UP000004947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM28770.1,
RC ECO:0000313|Proteomes:UP000004947};
RX PubMed=20363947; DOI=10.1128/JB.00208-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Morris R.M., Giovannoni S.J.;
RT "Genome sequence of Lentisphaera araneosa HTCC2155T, the type species of
RT the order Lentisphaerales in the phylum Lentisphaerae.";
RL J. Bacteriol. 192:2938-2939(2010).
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:EDM28770.1}.
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DR EMBL; ABCK01000004; EDM28770.1; -; Genomic_DNA.
DR RefSeq; WP_007277647.1; NZ_ABCK01000004.1.
DR AlphaFoldDB; A6DIB6; -.
DR STRING; 313628.LNTAR_09374; -.
DR eggNOG; COG0383; Bacteria.
DR OrthoDB; 9772207at2; -.
DR Proteomes; UP000004947; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000004947}.
FT DOMAIN 528..606
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT COILED 1001..1028
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1041 AA; 118979 MW; 15635C1D9BD8AD32 CRC64;
MLLTQKTLQK IERIVSTYEE KIFNPLSEIK SFELFECQEH LRSVPDQSSE NIALPHQWGS
VWNNSWFKTE FTISKDHIGK KLYLQPKTEG RETMLWVNNE AKGIISKELE VGARGYHHTL
FIGDNYSEGK NIALALECYA GHPCIGCHPG DERESTTFTK EEYIHTFQSC FIVERDELIK
DFVFDLKTLL QIVQHLPEES FRKGTVAACL EKVFLLISQS PVDTQSKQLR NSLKVARSVM
APELEKKNSP SAPIAGIIGH SHMDTAWLWT TQETQRKCAR TFSNALNLME QYPEYMFLQS
SVLHLEDIKT NYPNIFKQIK QRVAEGRWEP NGASYVEADG NITGGEAQIR QFTRGMKFLK
DEFDYTPDSY WLPDTFGYNA ALPQIIKGCG LKYFLTTKLS WNESNTFPYD SFKWQGIDGS
EVVAHFNETH CWPDPQTLLS RLNGLEEGKY TGNKFSIRHK DVTDKRYIAY GFGDGGGGPM
YEMLEMARRC EDLEGVPKAQ HMTLSQFMDN MVETSPQLPE HRGELYLELH RGTLTHQHKI
KRYNRKLEVA MRLLEYLDVQ SKLSGGDGIA KETLDALWKT LLVNQFHDIL PGTSIPEVHD
LAIEQYEQAM EACRELAEIP QSYGSGEYSL LNTLNWNRND YFSIAVDSTK LSMKNLASEP
YNDLYGTDHL LIKSDVDGLS TRNIEIVKNS KIENSSPFSI KEKVSTPYYE FKLTPDGEIK
DLISLKHQRR LTKESQAFNE FLIGEDIPAL WDSWDIDFDQ QVKMQVSAQH IKTKIVNQGQ
LHLRIRSKYS IGNASHIQQD IVFYAESARI DFETLVDWNE DHKLLQTSFD LDVFSNSIKC
EIPFGYIERP THNNSMVDRA CFEFSQHKYS DISETRFGVA FLNDGKYAID ANGSRVKLSL
LKSGGHPDPR GDKGQHFMVY SLLPHDGQLS SEEVICPAYE LNHPPVLLPA NQMTNDSLCE
VSESNIIIES IKWADDNSGY VLRLYEAEGT ASQCQLKLSS AGSAIHECNM LEEELNELEQ
TEKGITLHFR AFEIKTLKVS L
//
