ID D7B820_NOCDD Unreviewed; 514 AA.
AC D7B820;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Peptidase S1 and S6 chymotrypsin/Hap {ECO:0000313|EMBL:ADH70328.1};
GN OrderedLocusNames=Ndas_4945 {ECO:0000313|EMBL:ADH70328.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OG Plasmid pNDAS01 {ECO:0000313|Proteomes:UP000002219}.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH70328.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH70328.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RC PLASMID=Chromosome 2 {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; CP002041; ADH70328.1; -; Genomic_DNA.
DR RefSeq; WP_013155935.1; NC_014211.1.
DR AlphaFoldDB; D7B820; -.
DR STRING; 446468.Ndas_4945; -.
DR KEGG; nda:Ndas_4945; -.
DR eggNOG; COG5640; Bacteria.
DR HOGENOM; CLU_526671_0_0_11; -.
DR Proteomes; UP000002219; Chromosome 2.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00190; Tryp_SPc; 1.
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 Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002219};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..514
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003092797"
FT DOMAIN 27..260
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 378..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 53702 MW; 3B04060C44337246 CRC64;
MRSRTLLPAL VLAVTATVVT AVPAHAIVGG NPSTQSYEFM GSFQPDYPAP PRPDGHGCGV
VVLAPQWVLT ASHCAGKNPT NARTGVPRGW SVRVGSPDSD SGGEVAEVDH YYRLATSGDE
GGFWGRDLAL MHLERPVEAQ PLPIASASPP PGTPVRIMGW GMTCDDAGNP DCFPTRLREA
DTVVQPPSAC LGQAVEGELC VGSRDGSVAA ANMDSGGPAL VREDGAWALA GVVSGPSGEG
APTLFTDATR HTGWIDGVVS GTDVPPDDEI PDVEGMVDLQ GCVGSVVRTP ASEPDAPALM
LTNGHCVRED WPAPGEALVD RPADLEVPVA DPRGYPRVTA RAERLVYATM TGTDVALYRL
DRTYEQLASQ GAKTFELGTT PVRPGDEVTM VSPGTRSDCS VEAVPAHLRE GGYQQDDPIR
YASGEGCLPY PGMSGSVLLA PDGSTVVGVH NTHNRDGEEC TDDNPCEVDA DGNVTFERGR
GYGQQVHTVP ACLTDRSELD LSRRGCSLTG AGSA
//
