ID R6VZD0_9BACT Unreviewed; 1197 AA.
AC R6VZD0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative glycosylhydrolase {ECO:0000313|EMBL:CDC97336.1};
GN ORFNames=BN576_02138 {ECO:0000313|EMBL:CDC97336.1};
OS Alistipes sp. CAG:268.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1262693 {ECO:0000313|EMBL:CDC97336.1, ECO:0000313|Proteomes:UP000018329};
RN [1] {ECO:0000313|EMBL:CDC97336.1, ECO:0000313|Proteomes:UP000018329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:268 {ECO:0000313|Proteomes:UP000018329};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDC97336.1}.
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DR EMBL; CBGE010000107; CDC97336.1; -; Genomic_DNA.
DR AlphaFoldDB; R6VZD0; -.
DR STRING; 1262693.BN576_02138; -.
DR Proteomes; UP000018329; 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; 2.60.120.260; Galactose-binding domain-like; 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; IPR000421; FA58C.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; PF00754; F5_F8_type_C; 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; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000313|EMBL:CDC97336.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018329};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1197
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004422429"
FT DOMAIN 1046..1197
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1197 AA; 133718 MW; D55B3BD33ADE76CB CRC64;
MKRTLLGLLA LCMLTPVGAQ ERDKAYLVSN AHFDSQWNWD VQRSILEYIP KTLNQNLHLL
SQYPDYVFNF EGGIKYQWMK EYYPHQYELI KRYIREGRWH ITGSTWDATD PNIPSAESFT
RNILYGQHFY RSEFGVEGTD IFLPDCFGFG WTLPTIAAHS GLIGFSTQKL MWRHRPFYGS
SKIPFEIGLW QGIDGSRIMA VMDAHNYTTK WRYEDLSQSD YLSGITSKSP IRTVYHYYGT
GDTGGAPTIE SVRAVEAGVH GDGPVKIISA TSDQLFKDYL PYDAHPELPV WDGELLMDVH
ATGCYTSQAA MKLYNRRNEL LADAAERSAV AADWLGGVSY PRELLTEAWK RVIWHQFHDD
LTGTSIPRAY EFSWNDELLS LQQFAGVLTT SVGSVTRSLR TDVKGTPVVV YNAAGFPVRN
LVEATVPSRS DRVTVYDARG ERVPHQILGF ENGLLHVLFS AEVPAAGYAV YEVRGGGSRT
VASGLKAEDR TLENSIYRLT LDANGDICSI EDKRSGRELV EKGKSIRLAL FTKNESFSWP
AWEILKKTLD ADPEPICGDV KIRVAEQGPV RASLCVERTH GESTFRQYIT LTEGGQDDRI
DIVNEVDWAS TDALLKAEFP LSVSNPKATY DLGVGSVARG NNTDTAYEVY AQQWADLTAE
DGSYGVSVLN DCKYGWDKPD DHTLRLTLLH TPSTRGGYSY QNRQDYGHHI FTYSIVGHDG
DFRRGGTVRK AEVLNQPLRA FVAPKHRGTL GRSFSFVESL NEHVALRALK QAEDSEDYVV
RFYETSGQAP QQAVVRFAGE IVEAEELNGN EAPIGGASFS GRELRFTAAP FSMKTFRVKL
AAPAQAVAPA ACRPVALPYN LKTASYNPYR SDANFDGKGN SYAAELFPSK IECRGIGFEF
GSPEAENGVK CRRDTIALPS GDYDKLYLVV ASTRHDNRAV FTVDGEEHEV LVPYYGGFIG
QWGHTGHTEG YLKRADVLFC GTHKHDMIAN RDVPYEFTYL FCTSIDIPKG ARELILPDDP
RIVVFAATVA SDPNNAVTPA CDLLRVSLPE KGADEGEQAN RNLAFDRLVI ARSGEVSSEE
RAECALDDNA ETKWCDVSGA RPKYITVDLG KVQPIRGWYV MHAGLESLDY ITKEYSLEVC
TTPDGDWQRV DTVRDNTSLE TDRLLATPVE ARYVRLLVTK PDQSEGSTTR IYEFSVY
//
