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Database: UniProt
Entry: A0A399G1Z6_9ACTN
LinkDB: A0A399G1Z6_9ACTN
Original site: A0A399G1Z6_9ACTN 
ID   A0A399G1Z6_9ACTN        Unreviewed;       357 AA.
AC   A0A399G1Z6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Peptidase S1 {ECO:0000313|EMBL:RII01706.1};
GN   ORFNames=NI17_15540 {ECO:0000313|EMBL:RII01706.1};
OS   Thermobifida halotolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=483545 {ECO:0000313|EMBL:RII01706.1};
RN   [1] {ECO:0000313|EMBL:RII01706.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44931 {ECO:0000313|EMBL:RII01706.1};
RA   Toth A., Tancsics T.A., Farkas T., Papp P., Olasz F., Balint B.,
RA   Herczeg R., Nagy I., Baka E., Kukolya J.;
RT   "De novo genome project of the cellulose decomposer Thermobifida
RT   halotolerans type strain.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:RII01706.1}.
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DR   EMBL; JRUV01000268; RII01706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399G1Z6; -.
DR   STRING; 483545.GCA_001660385_00158; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..357
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038447938"
FT   DOMAIN          291..343
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          26..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   357 AA;  36266 MW;  4AC184E1BE4C9189 CRC64;
     MLLVVAVVAM ASAGVGGAVS ASLVGNEPPE PQGSNALNNE VPSDVPSRAP DTIAGVAQRV
     SPSVVSIRSA SPQTGGNGSG FVIEGDYVVT NNHVVDAVER TGIEVVYSDG HVSKAEVVGA
     AASSDLAVLR LADPLDVEPL EFGDSDEVTV GDTVIAIGAP LGLEGTVTSG IVSALNRPVT
     VGESGQEAYI SAIQTDAAIN PGNSGGPLVN EQGMVIGVNS AIATMGSLSG EQTGSIGLGF
     AIPSNQASRV VEQLIETGEA PHAVIGAVID LQYREQGALI LEERENGGDT IVRGGPADQA
     GLRPGDVIVE FDGTPVRDGN QLVTLIHTKA PGDRVEIRYE RNGEEHTTVM VLGSSND
//
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