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Database: UniProt
Entry: A0A1H0YW61_9BACI
LinkDB: A0A1H0YW61_9BACI
Original site: A0A1H0YW61_9BACI 
ID   A0A1H0YW61_9BACI        Unreviewed;      1706 AA.
AC   A0A1H0YW61;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Alpha-1,2-mannosidase, putative {ECO:0000313|EMBL:SDQ19086.1};
GN   ORFNames=SAMN05216231_0873 {ECO:0000313|EMBL:SDQ19086.1};
OS   Virgibacillus salinus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=553311 {ECO:0000313|EMBL:SDQ19086.1, ECO:0000313|Proteomes:UP000199444};
RN   [1] {ECO:0000313|EMBL:SDQ19086.1, ECO:0000313|Proteomes:UP000199444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10449 {ECO:0000313|EMBL:SDQ19086.1,
RC   ECO:0000313|Proteomes:UP000199444};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNKD01000001; SDQ19086.1; -; Genomic_DNA.
DR   STRING; 553311.SAMN05216231_0873; -.
DR   Proteomes; UP000199444; 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; 2.60.120.200; -; 1.
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   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR013320; ConA-like_dom_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   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006558; LamG-like.
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   Pfam; PF13385; Laminin_G_3; 1.
DR   SMART; SM00560; LamGL; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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:UP000199444};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1706
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038332326"
FT   DOMAIN          71..215
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          43..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1140..1172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1152..1172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1706 AA;  188599 MW;  2F6624E9119C979F CRC64;
     MRKKFISKLS VILCILMVVS ALPISPVKST MTEAAATSNF NSSFEVNEQQ PTWENTSEVD
     NEGNKMTSGV IGKIPYDSIQ GDITNKVEGV SASNSNPPNE VATNLTDRSA QSKWLAFESS
     AWIEFSFAEP QNLVKYALTS ANDAPGRDPK NWTLVGSNDR ENWVELDTRT DQAFKDRYKR
     KVFEFENNQE YTYYRLKITE NAGDGLTQLA EVALSNGIDV PPPPPSDMKT YVSEGPTSSY
     TAKTRVGWTG TKALTYEGRH EVDGEAYAYN KLFDVNIKVT PEAQLSYYIH PQFVDQDQLD
     YSSTYVSIDL AFTDGSYLSD LGAKDQHGVV LNPQKQGKSE TLYPNQWNHK LADIGSVAEG
     KTIDRILVTY KNPKGPGVFK GSIDDIKIEG NPEPADYTSP VDYVNILRGT NSNGSFSRGN
     NFPAVAVPHG FNFWTPVTDS GSTSWLYSYQ QSNNENNLPE LEAFSLSHET SPWMGDRQTF
     QVMPAKGDNP SADRNERALP FKHKNEIAKP HYYSVEFENG IQTEMTPTNR AAMFNFTFTE
     DTSNLIFDNV NNNGGLTLSS DKQTITGYSD VKSGLSTGAT RMFIYAKVDK PVKDSGKLTG
     EGRDNVTGYL QFDTSGADKT VSMKIATSLI SVEQAKKNLE QDIKADTSFE DLKEKAKELW
     NEKLGIIEIE GATHDELVTF YSNMYRLFTY PNKAYENTGT DTDPVYKYAS PFSEEVGENT
     AMETGANIVE GKPYVNNGFW DTYRTTWPAY TLLTPTQAGE MIDGFVQQYK DGGWISRWSS
     PGYANLMVGT SSDVAFGDAY QKGITNFDVE AYYESALKNA SVASEDQSVG RKGLSTSIFD
     GYTSNSTGEG MSWAMDGYIN DFAIANMAKE LLEKTDKNDP KYEQYQAEHN YYLSRAQNYV
     NMFNPETDFF MGKKASGKWR ATPENYDPRE WGGDYTETNG WNMAFHVPQD GQGLANLYGG
     RDGLANKLDE FFSTPETALH PGHYGGIIHE MREARDVRMG MYGHSNQPSH HIPYMYNLAG
     QPWKTQEKVS EVLSRLYLGS EIGQGYPGDE DNGEMSAWYI FSAAGFYPLQ MGKPEYAIGA
     PFFEKMTIHL ESGKDLVIKA PNVSKKNKYV QSLKVNGKSY NKTTLSHDLL AEGATLEFDM
     GPEPSDWGTS EDALPASITD NATNGSSLLP DPLKDLTNDT NGSTVHSDKG VADRLFDNNS
     ETKVTLESDN PWVQFQFEDG ATRPLMYTIT SGNNDQSDPK SWTLLGSKNA KDWTIVDERT
     DVSFKWREFT KPFSIQNPGE YTYYRLKVTE NGKNGSTSFA ELELLGYGNT DEKFEQVKET
     YEGYRDSGDI KGALIKQFDT KYGQAEDQFE KEHFKQAAKK LDDLLKSLNK KSGNITKDAT
     KVLSADINAL ITSVSRLNSG GNPGKGQWKY KDEVEQVPVF EVSKLAAPTV KPGGDATISV
     IVTNIGLLAG DKQIDFSFDG APVETKTITL EPGESKTVTF TVSDVALGIH QFKINELTGT
     LKALHDGPVL SLDFEDTVQD ASPYGHDGTI HGDVSFVEGK VGNAIKLNGG WVDIPSSKLL
     NGDDEFTIGL WVNLEDPGQD QKIIGKTTIG NGYVLGVDGG LYPEMWDDSG SRFSFNNGSI
     APNEWTHLAL TWKQNGQVTG YIDGEEAASV AAGMNPIAPN DNPLIIGGAP WGPDGLQTKG
     LVDEVRIYKE ALSSEEVKEM YTGNAN
//
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