ID D7B6J8_NOCDD Unreviewed; 506 AA.
AC D7B6J8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Peptidase S1 and S6 chymotrypsin/Hap {ECO:0000313|EMBL:ADH69285.1};
GN OrderedLocusNames=Ndas_3888 {ECO:0000313|EMBL:ADH69285.1};
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).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH69285.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH69285.1, 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};
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).
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DR EMBL; CP002040; ADH69285.1; -; Genomic_DNA.
DR AlphaFoldDB; D7B6J8; -.
DR STRING; 446468.Ndas_3888; -.
DR MEROPS; S01.494; -.
DR KEGG; nda:Ndas_3888; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_3_7_11; -.
DR Proteomes; UP000002219; Chromosome 1.
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:UP000002219}.
FT DOMAIN 441..493
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..147
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 506 AA; 49986 MW; 4E7E9C6C206D657A CRC64;
MNLDPGPGEQ PGAPRSDQAS AHPVGGGFPG SANPSGPAVY GASAANPGSG DPSGSTAHTS
FANPSGPGHP GIGGPSGPAN PMNPGAPSAP GQHTGHTGQS AAHGGYATAF QAGHAAPGPG
APPPGVPGPH TTGPHSAPQP PAPKRPRRGV PVWMALSGML VVALIAGGAG GVAGNLLDGS
STDEAAQEEG PVMNEPPPEA PRRDPDTIAG VAQRVSPSVV FIHSADPTIP SSGSGFVIDG
NYVVTNDHVS AGLEADGIVV EYSDGSLSSA SVVGSDPSSD LAVLSLDDPI DVEPLQFGDS
EQVIVGDEVI AIGAPLGLSG TVTQGIISAV NRPVSSGEGE NASRFYALQT DAAINPGNSG
GPLVDLEGRV IGVNSMIVTM SSMGEPTGNI GLGFAIPSVE AERVVNRLVE YGETSYADIG
AEIDLDSPVA GAVIADGGGA VESGGPADEA GLEPGDVILS LDGRPVNSGQ ELLAMLRSRS
PGEEVEVEFD RDGRRDTVTV TLGSSD
//
