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Database: UniProt
Entry: A0A0U1NYI7_9BACI
LinkDB: A0A0U1NYI7_9BACI
Original site: A0A0U1NYI7_9BACI 
ID   A0A0U1NYI7_9BACI        Unreviewed;      1227 AA.
AC   A0A0U1NYI7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   31-JUL-2019, entry version 19.
DE   SubName: Full=Subtilisin-like serine protease {ECO:0000313|EMBL:CRK83066.1};
DE   Flags: Precursor;
GN   ORFNames=BN000_03023 {ECO:0000313|EMBL:CRK83066.1};
OS   Bacillus sp. LF1.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1499688 {ECO:0000313|EMBL:CRK83066.1, ECO:0000313|Proteomes:UP000199087};
RN   [1] {ECO:0000313|EMBL:CRK83066.1, ECO:0000313|Proteomes:UP000199087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LF1 {ECO:0000313|EMBL:CRK83066.1,
RC   ECO:0000313|Proteomes:UP000199087};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; CVRB01000003; CRK83066.1; -; Genomic_DNA.
DR   EnsemblBacteria; CRK83066; CRK83066; EBG00005136205.
DR   Proteomes; UP000199087; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034213; S8_Vpr-like.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000199087};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355};
KW   Protease {ECO:0000256|RuleBase:RU003355, ECO:0000313|EMBL:CRK83066.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199087};
KW   Serine protease {ECO:0000256|RuleBase:RU003355};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31   1227       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006712411.
FT   DOMAIN       82    175       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      209    658       Peptidase_S8. {ECO:0000259|Pfam:PF00082}.
FT   DOMAIN      444    530       PA. {ECO:0000259|Pfam:PF02225}.
FT   REGION      243    269       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      545    577       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    246    261       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    545    567       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   1227 AA;  131313 MW;  219F8A1A8CA23541 CRC64;
     MKRKKYGRVF SRLLILTLIF SLFTPIFASA ETGLSPKGTQ VSDESIMKMK ALIAQQESLL
     NQEPSLSPEL KDLEGDNEVG VIVQLSEHPL ALEKGIKKVQ GKSFTSTDRA NVKKKIQSQQ
     DNFEKALGNK GIKHKKGFTF SETFNGMSLK LTAKQLKELL KVNGVVSIEP DSEVHAVGEP
     STDDTVSQMI SSDNQFLGIP DVWAKGYEGQ NVKVAVLDTG IDYYHPEFQG VYKGGYNFVP
     QTSRTDYTRD RADDDPYETS PLDRPAGKAE VDANGRTFYT EHGTHVAGTI AAQGNNPYGI
     KGIAPKVELY SYRVLGAYGS GATSGIIAAI DKAAQQHMDV INLSLGGSNN SSTSADAIAI
     NNAALAGVTA VVATGNSGPN RGTIGSPSTA AFAISVANST IPETTKKGQV NVTLEGSAPA
     NYNLNLMAWK FGVEPADTLT GTYDVVAVPN YGVDADYTGL DVKGKVALIS RGGGVAFVDK
     IAAAKKAGAI ATIIHNNGGT NGNGPAGVFL SDSFAFLPSF DMSTTDGNAL RTAMQTKKAT
     VTFSNFSSSS TGGDDINSSS SRGPSNPNFD LKPDVSAPGT NIMSSVPAYK KDFPDANYTE
     SYERFTGTSM ATPHITGIAA LLKSEHPDWT PFDIKVAISN TAKQLDVTKY DVFAQGPGRV
     QPYQAATTEA LAYAMDKTAF SSKTYDNIKG TITFGNVPTN ANNASTVTKD IKVKNLTGKA
     SDYTVNVQVT KAATGALAGA NVTVDQSKFT LDASGEKALK VTLNVPKGAG STGNEILGYV
     YITNGTTNLT LPFAGNFAPP TGIKDYSIES KVISPNGDGK LDSTTVHYEF YDRQNTTFIE
     LWDAAHQDAG YYHDGYLGYL VASSSTTVGP KSVVFNGGYT EWGTGKKATA PDGVYTIDMS
     TLNLAGTAVA TSAWLGPIYV KSSPSEFVLP AADNIIEDTS FEYKGSIKDK FIDFKPVVEQ
     VFGENYDVND KLTLKYELKD KDGNVIDSKP VKLNQDGSFS IPFAELRSGD YKLKFSISDI
     AQNSSEKEIT ISVKNDPQIA KMVVTNKDID QQIKGNTSVV VLATPAFSKS QNKIRVELPT
     SVLKDLEQSK KSVAFAAPGG VQIMLPTKVM TQLSNSGADK VYLEINRENS SIVPVTGTDE
     AVSDLYQFAF RYEKGRDTTY VTTLDDTVDV RLPVNATAAK GFKKVEAYDF NKDNKSLNLL
     NSLYLSGSIE FKATKLSSFV ALGKNKK
//
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