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Database: UniProt
Entry: A0A1H8EAR0_9BACL
LinkDB: A0A1H8EAR0_9BACL
Original site: A0A1H8EAR0_9BACL 
ID   A0A1H8EAR0_9BACL        Unreviewed;       571 AA.
AC   A0A1H8EAR0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   10-APR-2019, entry version 6.
DE   SubName: Full=Serine protease AprX {ECO:0000313|EMBL:SEN16516.1};
GN   ORFNames=SAMN05444955_106223 {ECO:0000313|EMBL:SEN16516.1};
OS   Lihuaxuella thermophila.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Lihuaxuella.
OX   NCBI_TaxID=1173111 {ECO:0000313|EMBL:SEN16516.1, ECO:0000313|Proteomes:UP000199695};
RN   [1] {ECO:0000313|EMBL:SEN16516.1, ECO:0000313|Proteomes:UP000199695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46701 {ECO:0000313|EMBL:SEN16516.1,
RC   ECO:0000313|Proteomes:UP000199695};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOCQ01000006; SEN16516.1; -; Genomic_DNA.
DR   BioCyc; GCF_900110165:BMW55_RS08815-MONOMER; -.
DR   Proteomes; UP000199695; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR007280; Peptidase_C_arc/bac.
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; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF04151; PPC; 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:UP000199695};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355};
KW   Protease {ECO:0000256|RuleBase:RU003355, ECO:0000313|EMBL:SEN16516.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199695};
KW   Serine protease {ECO:0000256|RuleBase:RU003355};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    571       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5011691839.
FT   DOMAIN       80    134       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      169    434       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
FT   DOMAIN      474    544       PPC. {ECO:0000259|Pfam:PF04151}.
SQ   SEQUENCE   571 AA;  60229 MW;  0DFC696557BE8BEA CRC64;
     MKRMIRVLSL ATALFFGFAT VALAAPPSGK AVKTQAAKEK THRIHKVKGS KLLSNLHERL
     SKASSSEKLP VLISFQSLNQ QANLTKAKAM LQPFTPQHVY KNLPLMSAKL TKQQIQALEA
     SPDVVQIEYD EPVYAFSQTA NYWYGTTKSR TDFGVTGDRD GSPASYSKND VVVAVIDTGI
     DATHADLDGG KVIGWKDFVN NRTTPYDDQG HGTHVASIAA GTGDANAAYK GVAPGAALVG
     VKVLDSQGSG SMSNVTAGID WCITNKNVYG IKVINMSLGT TGSSDGSDAT SQAANRAHDA
     GIVVAVAAGN SGPAQQTIGS PGAAAKSLTV AAMADPGEKG FNIASFSSRG TTADGRIKPD
     IAAPGYNITA AKANSSTQYV TYSGTSMATP FVAGTVALML DANPSLTPDQ VKSNLFTTAT
     DFGPAGQDVD YGWGNLKGYD AVKVSGNLTG TGPALPNHLF AQDTIQTEGY KDEWTFQVNS
     TSAPVSIAMI MPDWSGFWFW TDPDFDVYLY DPSGAEVAKA EGIERQETIT ITPAKTGTYK
     LRVKSYSGTG RYFFDLSSNA SGLTRVLNDQ P
//
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