ID D7AUA9_NOCDD Unreviewed; 883 AA.
AC D7AUA9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ADH65667.1};
GN OrderedLocusNames=Ndas_0217 {ECO:0000313|EMBL:ADH65667.1};
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:ADH65667.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH65667.1, 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).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP002040; ADH65667.1; -; Genomic_DNA.
DR RefSeq; WP_013151274.1; NC_014210.1.
DR AlphaFoldDB; D7AUA9; -.
DR STRING; 446468.Ndas_0217; -.
DR KEGG; nda:Ndas_0217; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_003559_0_0_11; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000002219; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07489; Peptidases_S8_5; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 2.60.40.1710; Subtilisin-like superfamily; 1.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034187; Peptidases_S8_5.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000002219};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..883
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003092524"
FT DOMAIN 70..133
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 164..586
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 377..456
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 606..707
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 530
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 883 AA; 92062 MW; 199EA8641F6D767C CRC64;
MVPHRTRLAS LAGLTLVAGL VAAAPASADD ASELAPLHPA PSAENGELTH QADGLWFIEL
ESPPTTAGTS SAQVENEHEA FRAEAEESGL EYTERHSFGD LWNGFSVEMD DAQVGTAREI
PGVSAIYPVV TYEVPEGDTS VPDLDTALPM TGSDIAQNEL GLTGEGLRVA VMDTGVDYTH
PDLGGGGFPN DRVVTGYDFV GDDFNAGDPT TVPAPDDDPQ DCHGHGTHVA GIVGARGEVT
GVAPGVDFGA YKVFGCEGST TSDIMIAAME RALADDMDVL NMSIGSAHSW PQYPTAVASD
NLVDEGMVVV ASIGNEGDTG LYSAGAPGLG EDVIGVASYD NTHIRSASAT ANPSGETLAY
MEMGEASPPP ASGETDELVH VGRGCPSLGD ELEADPEGRT ALMVRGACTF AEKYDAAVAA
GATGVVMYNN VPGMFAGGGI VDQGAFSIGI SDTSGAHLLE LLEGDEPVTL SWTGESTTIP
NPTGGLISSF SSFGLSPDLA LKPDIGAPGG LINSTYPMAK GGYATISGTS MSSPHVAGGV
ALLLEARPDL GAHEVRDVLQ NSADPKAWWG DPDAGYTDNV HRQGAGMMDV PGAVLATTAV
TPGKLSLGAT EGEVTETITI ANDGDEEATY TLDHESALGT HGNTFTPGYN DASAEVAFDR
DEVTVAPGGT AEVQVTFTPP AQDFQQMIYG GYVSVAETGG ETYRVPYAAY NGDYQQIEAM
TPITDGSGNV LELPWLTRIT ECGAFSGLEC VGEGGGTFEN QPEGAAYTLE WVDGLPDVPY
VIAHFDHHVT LLEMTVVDER TGRPVHPDRN VGVSVDHVNR SATGTSFFSY AWDGTVLDRH
DRITPVRDGQ YRLEARALKA LGDPDNPDHW ETWTSPVITI DRG
//
