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Database: UniProt
Entry: A1S0E4_THEPD
LinkDB: A1S0E4_THEPD
Original site: A1S0E4_THEPD 
ID   A1S0E4_THEPD            Unreviewed;       311 AA.
AC   A1S0E4;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Peptidase S1 and S6, chymotrypsin/Hap {ECO:0000313|EMBL:ABL78924.1};
GN   OrderedLocusNames=Tpen_1528 {ECO:0000313|EMBL:ABL78924.1};
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408 {ECO:0000313|EMBL:ABL78924.1, ECO:0000313|Proteomes:UP000000641};
RN   [1] {ECO:0000313|Proteomes:UP000000641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5 {ECO:0000313|Proteomes:UP000000641};
RX   PubMed=18263724; DOI=10.1128/JB.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(2008).
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DR   EMBL; CP000505; ABL78924.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1S0E4; -.
DR   STRING; 368408.Tpen_1528; -.
DR   EnsemblBacteria; ABL78924; ABL78924; Tpen_1528.
DR   KEGG; tpe:Tpen_1528; -.
DR   eggNOG; arCOG02833; Archaea.
DR   HOGENOM; CLU_020120_2_2_2; -.
DR   Proteomes; UP000000641; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000000641}.
FT   DOMAIN          233..273
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   311 AA;  32940 MW;  EECC67A7F582F469 CRC64;
     MAEDLQERVI RAYEKVRDSV VSVTAVKVLD FLFVREPVSG LGSGVAVSED GLVATNAHVV
     EGFEEISVTT PGGDHVRAEV VDVDPHYDIA FLRVERARLK PAELGDSDSL RVGQFVVAVG
     NPFGQLLGGP SLTFGVVSGL GRSLRAEGKI YENLIQTDAP VNPGNSGGPL VDLEGRVVGI
     TTAMIPFAQG IGFAIPINEV KYALAQLEKY GRILRPWIGV YGLDVNPAIA YQLGLPRAAG
     VLVLRVVPGS PAARAGVKPG AVILKLDGSE VKGTGDLVSK LRQKEVGEKA VLEVFYAGTL
     RRLQVTVEEA P
//
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