ID B3C6V5_9BACE Unreviewed; 1072 AA.
AC B3C6V5;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Glycosyl hydrolase family 38 C-terminal domain protein {ECO:0000313|EMBL:EDV07079.1};
GN ORFNames=BACINT_00645 {ECO:0000313|EMBL:EDV07079.1};
OS Bacteroides intestinalis DSM 17393.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV07079.1, ECO:0000313|Proteomes:UP000004596};
RN [1] {ECO:0000313|EMBL:EDV07079.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV07079.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides intestinalis (DSM 17393).";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDV07079.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV07079.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2008) 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:EDV07079.1}.
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DR EMBL; ABJL02000006; EDV07079.1; -; Genomic_DNA.
DR AlphaFoldDB; B3C6V5; -.
DR STRING; 471870.BACINT_00645; -.
DR eggNOG; COG0383; Bacteria.
DR Proteomes; UP000004596; 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 Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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 InterPro; IPR013780; Glyco_hydro_b.
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:EDV07079.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1072
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002785325"
FT DOMAIN 301..379
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 1040..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1057
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 119810 MW; E70A772EF32578CB CRC64;
MMKKLIFPLL FVLGISTHVD AQKPYKAYMV SNTHLDTQWL WTVQTTIDHY LYRTLTQNFW
LIDHYPGYIF NFEGAVRYQW AKEYYPTEYE RLKNYIKAGR WNISGSSWDS TDPNIPSPES
FFRNLLYGQE FFKKEFGKKS NDIFLPDCFG FGYTLPTIAA HSGIIGFSTQ KLQHRKLPFY
GDHKLPFMFG LWEGIDGARI MAVPHAQDYV SRFDGQELSN NGKLVDLAKN GLNNTVYHYY
GAGDRGGSPT IASVRSVETG MKGEGPVQII SARSGQLFDD YYPFEKHPEL LVFKGELLMD
VHATGCYTSQ AAMKLFNRRN ELLADAAERA SVVAEWLGGA AYPEEPLRES WQRFLWHQFH
DDLTGTSIPV AYTFSWNDEL IAQSEFAEIT TGAVGAVSRA LDTRTRGISV VVYNPVAQSR
CDIVTATVDM ASQPKDIVAV APNGKKVFGQ LLSWQNGKAT VLFPVDMDPV SFSVYDVRSG
KISGTKQLKA ESNILENSIY KVVLDKNGDI ASITDKRNGR ELVEPGKAFR LALFTPSESR
TWPAWELFKK TIDQTPLPVN GNVEISVAEN GPVRASLKVK RTYGTSNFVQ YITLTEGGQD
DRIDIRNEID WNERNTLLKA EFPMNVSNEI ATYDLGIGYI GRGSNTDNKY EVVAQQWADI
TSADGSYGIS VMNDSKYGWD KPDNHTLRLT LLNTPAVGKD PNMAHQEHLD MGHHTFSYSI
YGHKSDIAEA GTAWKAEAFN QLLLSFTTPK HAGTLGRKLS FVKTNMPGIA IKAVKKAEDG
KSYIVRVNEI YGKDFENAEI IFASAVESAC EVNGIEEYVG ETKYEGDKIV FSGTAFQPRT
FSVRLKENAC LEIPENHSID IECNATALTA DEFSMSGNFD GEGNSFAAEL MPDVVEAEGV
TFRMENNPAD YNYIRCDGQT IPLPEKHGYT KCYLLVTSSH GDRKASFQVD GKDYSVNVPF
YSGFIGQWGW TGESEGYMKD ASIAYIGTHR HSSRVGGNES YIYTYLYKIC LDIAPDAKAL
TLPKDAGVAL FAVTLSDNSN DDTKPATEMR ALPHETAKVE YTTEPVAASR RR
//
