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Database: UniProt
Entry: A0A238YVU0_9ACTN
LinkDB: A0A238YVU0_9ACTN
Original site: A0A238YVU0_9ACTN 
ID   A0A238YVU0_9ACTN        Unreviewed;       382 AA.
AC   A0A238YVU0;
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, subtilisin family {ECO:0000313|EMBL:SNR74693.1};
GN   ORFNames=SAMN06265355_106242 {ECO:0000313|EMBL:SNR74693.1};
OS   Actinomadura mexicana.
OC   Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC   Actinomadura.
OX   NCBI_TaxID=134959 {ECO:0000313|EMBL:SNR74693.1, ECO:0000313|Proteomes:UP000198420};
RN   [1] {ECO:0000313|EMBL:SNR74693.1, ECO:0000313|Proteomes:UP000198420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44485 {ECO:0000313|EMBL:SNR74693.1,
RC   ECO:0000313|Proteomes:UP000198420};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZNP01000006; SNR74693.1; -; Genomic_DNA.
DR   BioCyc; GCF_900188105:CHC11_RS17620-MONOMER; -.
DR   Proteomes; UP000198420; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd04077; Peptidases_S8_PCSK9_Proteinase; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
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   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:UP000198420};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355};
KW   Protease {ECO:0000256|RuleBase:RU003355, ECO:0000313|EMBL:SNR74693.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198420};
KW   Serine protease {ECO:0000256|RuleBase:RU003355};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    382       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5013394213.
FT   DOMAIN       60    105       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      146    361       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
SQ   SEQUENCE   382 AA;  38564 MW;  E41DF75526C98EF8 CRC64;
     MKKPLFTAVA AASLLAVSAA PAPAVTLPAP LTLAVSGQGI AGQYIVTLKP GVSIGATVSK
     HGIKTMYRYG RVLNGFAAKL NSKKLAKLRG AAGVARIEQD AVVHADGTQQ NPPSWGIDRI
     DQTALPLSRS YTYNSTGAGV YAYIIDSGIY TPHPEFGGRA ANVYDALGGS GADCNGHGTH
     VAGTVGSTSY GVAKNVYLRG VRVLNCQGSG STSGVIAGMN WVAGNRSRPA VANMSLGGGY
     SSTVNSAADN LASSGVFLAA AAGNDGRNAC NYSPGSAANA TTVAASTITD ARASYSNYGA
     CVDLYAPGSS ITSTWLNGGT NTISGTSMAT PHVTGVAALY KATYGDASYG TVRGWLISNA
     VSGVISGNPA GTPNRLLNKR DL
//
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