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Database: UniProt
Entry: W1SM91_9BACI
LinkDB: W1SM91_9BACI
Original site: W1SM91_9BACI 
ID   W1SM91_9BACI            Unreviewed;      1411 AA.
AC   W1SM91;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Alpha-1,2-mannosidase {ECO:0000313|EMBL:ETI70215.1};
GN   ORFNames=BAVI_03979 {ECO:0000313|EMBL:ETI70215.1};
OS   Neobacillus vireti LMG 21834.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI70215.1, ECO:0000313|Proteomes:UP000018877};
RN   [1] {ECO:0000313|EMBL:ETI70215.1, ECO:0000313|Proteomes:UP000018877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI70215.1,
RC   ECO:0000313|Proteomes:UP000018877};
RX   PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA   Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT   "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT   potent source and sink for nitric and nitrous oxide under high nitrate
RT   conditions.";
RL   Environ. Microbiol. 16:3196-3210(2014).
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:ETI70215.1}.
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DR   EMBL; ALAN01000026; ETI70215.1; -; Genomic_DNA.
DR   RefSeq; WP_024027012.1; NZ_ALAN01000026.1.
DR   STRING; 220686.AA980_18265; -.
DR   PATRIC; fig|1131730.3.peg.843; -.
DR   eggNOG; COG3537; Bacteria.
DR   OrthoDB; 9804511at2; -.
DR   Proteomes; UP000018877; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 1.20.1050.60; alpha-1,2-mannosidase; 1.
DR   Gene3D; 1.20.1610.10; alpha-1,2-mannosidases domains; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.30.2080.10; GH92 mannosidase domain; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR005887; GH92_a_mannosidase_put.
DR   InterPro; IPR041371; GH92_N.
DR   InterPro; IPR012939; Glyco_hydro_92.
DR   NCBIfam; TIGR01180; aman2_put; 1.
DR   PANTHER; PTHR12143; PEPTIDE N-GLYCANASE PNGASE -RELATED; 1.
DR   PANTHER; PTHR12143:SF43; PUTATIVE SUBFAMILY (AFU_ORTHOLOGUE AFUA_6G13760)-RELATED; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF07971; Glyco_hydro_92; 1.
DR   Pfam; PF17678; Glyco_hydro_92N; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018877};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1411
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039197508"
FT   DOMAIN          76..171
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          1152..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1156..1177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1411 AA;  154975 MW;  7E89ED6BE91304DE CRC64;
     MKKVALKRII SSIVSLAVLA AVPVIQKPSV LAASSASTTS ANTEFFSSFE KNDPQLNWTN
     TVETDANGKK MSSGIDGNVK RDLILGDITD KVVQVTASAN NPPNEIDSKL IDGDPTTKWL
     AFEPTANIVL KLSEPVAVVK YALTSANDAK GRDPKNWTLY GSLDGTNWTA VDTREGEDFK
     DRFQRNMYDL KNTTKYLYYK FDITKNAGDS ITQLAEIALS DGIEVPPPPP GDMKSAIGKG
     PSSSYTAKTN VGWTGLGALN YSGTHLLDGR AYSYNKLYDA DILVTPETEL SYFIAPEFTD
     KNHNDYSSTY VSVDLAFSDG TYLHDLKAVD QYGVGLNPKD QGDSKYLYVN QWNVIRAKIG
     SVAAGKTIKR ILVAYDNPKG PGAFRGSIDD IKITGKPVHK TYGSPIDYVN ILRGTQSNGS
     FSRGNNFPAV AVPHGFNFWT PTTNAGSSWI YQYHESNNAN NLPQIQAFSV SHEPSPWMGD
     RQTFQVMPSA STAATPSANR TSRALEFNHA NEIAQPHYYS VKFENGIRTE MTPTDHAAMF
     KFTFTGATSN LIFDNVDNNG GLTIDANTGE ITGYSDVKSG LSTGATRLFV YAAFDKPVIK
     SGKLTGENRN NVTGYVRFDT TKAEDKVVTM KIATSLISVE QAKKNLEQEI GLTDTFDGLK
     EKAKTEWNKK LGIIEVEGAS EDQLVTLYSN LYRLFLYPNS AFENVGTTTA PVYKYASPYS
     AATGQNTATT TGAKIVDGKT YVNNGFWDTY RTAWPAYSLL TPKIAGELID GFVQQYRDGG
     WIARWSSPGF ANLMPGTSSD VAFADAYLKG VTNFDVQSFY QSAIRNAEAV SPNAGTGRKG
     LTTSIFDGFT NTGTGEGLAW AMDGYINDFG IANLAKALNE KGDKKDPYYA NYAADYQYFL
     NRAQNYVHMF NPSIGFFNGR TANGAWRSTP GNFNPAAWGN DYTETNAWNM AFHVPQDGQG
     LANLYGGKEE LAAKLDQFFS TPETGLFPGS YGGTIHEMRE ARDVRMGMYG HSNQPSHHIA
     YMYDYAGQPW KTQEKVREAL DRLYIGSEIG QGYSGDEDNG EMSAWYILSA MGFYPLKMGT
     PEYAIGAPLF KKATIHLENG KSIVINAPNN SKENKYVQSM KINGKPYTKT SILHADIANG
     AVIDFEMGSK PSKWGSGDQD LPQSITPGST DGTSLSPLPL RDVTDRLVAA DKGAVTVSDE
     GNGQLLFDNT SNTQLSLKSK TPSIVYQFKE GKQNVKMYTL TSSKASQNED PKSWVLKGSN
     DGKSWSVLDQ RKNETFQWRQ YTRAFTIQHP GKYSQYKLEI TENGGAEVTT LAELELLGYD
     DVTNSYQAVN ELMEQFKQSK DLTGPMAVQL TNSLTTSLDH FKKEHKDQAI KHLEDFLKHL
     NNKGLQDRIS PKAKAALSAD ANQLIVLLSR D
//
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