ID A0A1H0VSG5_9PSEU Unreviewed; 535 AA.
AC A0A1H0VSG5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:SDP81158.1};
GN ORFNames=SAMN05192558_11564 {ECO:0000313|EMBL:SDP81158.1};
OS Actinokineospora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=504798 {ECO:0000313|EMBL:SDP81158.1, ECO:0000313|Proteomes:UP000199651};
RN [1] {ECO:0000313|Proteomes:UP000199651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10655 {ECO:0000313|Proteomes:UP000199651};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNJB01000015; SDP81158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0VSG5; -.
DR STRING; 504798.SAMN05421871_104415; -.
DR Proteomes; UP000199651; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05345; He_PIG; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49313; Cadherin-like; 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:UP000199651};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 144..432
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 385
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 535 AA; 53304 MW; 7079A66B35EC0A98 CRC64;
MVTLGQAAAR PDASPAVSRV GDDRSAVTNR LIVTYKSGAR AASVDADAGA QVAALAARMR
HDAKLVRRLG TGAALVDLGA AADARAIREL RDAFAADPEV AAVEREPVFT PDADPNDTYY
PKQWNLAATS AGMNVPAAWP VSTGAGVTVA VIDSGITKHS DLAANSGPGY DFVGDKSRAG
DGDGRDSDPT DEGTWFTDGH CGTGHKAGKS GWHGTMVAGI IGAIGNNAKG IAGVAPRVSI
QSIRVFGSCG AVGGDILDAI TWASGGAVPG VPANPRPAKV ISMSLGWGSR CNTSTQNAID
GALSRGTTVV ASAGNSNVDA TNHSPSGCNG VISVAASDSN GAKASYSNYG GGVSITAPGS
GIWSTTNTST TTPGAEGYRA GSGTSFAAPH IAALAALMLA KNPKLTPSQI QSIMKANARP
LPAGCPPGCG AGLADAAKTV AAVPKPPTGT VTVTNPGTLT AFRGWPVSWQ IKAASSDSTP
VTFRATGLPA GLTISSSGQI NGTPGASGAF TVTVTATNTS GATGKTTFPI QIWGW
//