ID Q139M5_RHOPS Unreviewed; 234 AA.
AC Q139M5;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Peptidase S1 and S6, chymotrypsin/Hap {ECO:0000313|EMBL:ABE39214.1};
GN OrderedLocusNames=RPD_1979 {ECO:0000313|EMBL:ABE39214.1};
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE39214.1, ECO:0000313|Proteomes:UP000001818};
RN [1] {ECO:0000313|EMBL:ABE39214.1, ECO:0000313|Proteomes:UP000001818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE39214.1,
RC ECO:0000313|Proteomes:UP000001818};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000283; ABE39214.1; -; Genomic_DNA.
DR AlphaFoldDB; Q139M5; -.
DR STRING; 316057.RPD_1979; -.
DR KEGG; rpd:RPD_1979; -.
DR eggNOG; COG5640; Bacteria.
DR HOGENOM; CLU_079867_0_0_5; -.
DR BioCyc; RPAL316057:RPD_RS09935-MONOMER; -.
DR Proteomes; UP000001818; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
FT DOMAIN 1..226
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 234 AA; 23762 MW; 68FBE590E3CDEFF7 CRC64;
MVGGARESDD GIGRAVVTIV GSRGNFCSGA LIAPDLVLSA AHCVGPGANY KIVQLDAERR
PQLRDIRRVA AHPQFDRRAI EANRASADVA LLQLAAPLPG KTPLPIGAPG DPLAAGQSFT
IAGIGVAQRG DGRSGGVVRS AQLIATGRPG RLQIRLVDPA TNNARDGLGA CTGDSGGPAL
QEQNGRAVII GVVSWSTGAA NASGCGGLTG VTPLTLYRDW IVSTARIWGA ALPP
//
