ID A0A1M6RK06_PSETH Unreviewed; 818 AA.
AC A0A1M6RK06;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Serine protease, S1-C subfamily, contains C-terminal PDZ domain {ECO:0000313|EMBL:SHK32764.1};
GN ORFNames=SAMN05443637_10532 {ECO:0000313|EMBL:SHK32764.1};
OS Pseudonocardia thermophila.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1848 {ECO:0000313|EMBL:SHK32764.1, ECO:0000313|Proteomes:UP000184363};
RN [1] {ECO:0000313|EMBL:SHK32764.1, ECO:0000313|Proteomes:UP000184363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43832 {ECO:0000313|EMBL:SHK32764.1,
RC ECO:0000313|Proteomes:UP000184363};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FRAP01000005; SHK32764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6RK06; -.
DR STRING; 1848.SAMN05443637_10532; -.
DR Proteomes; UP000184363; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:SHK32764.1};
KW Protease {ECO:0000313|EMBL:SHK32764.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184363}.
FT DOMAIN 725..809
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 83240 MW; C0B386AD2C761DB2 CRC64;
MAMHDREPRG RTEQLPDAPD ADPTDGEGSG AERTWPYGSD DAPKTAPDPA EVGPVSVDEL
LSRGFGPDEP SALDELFDAQ ASLDGDDPLF AELAAQTPSA SVERPQRSDE ARHESPETAA
SPILPQRVPG ERRRVEATPF GNASSSSVDL FADAPADPAA RAATDPGRRS TTYGAAAARF
AQGVAGSERA TSRPATDLFS SGVPEPRTRI GGWTADPWPT PPEGTHRAST DQKSGARPTG
TRDRTNGADG ADGADGARTE HQEPEARGTA PEPAERPRHA RPAEEQDEPD AGGADGRHRS
GPDRASEQAE DRDPEAAEHD VRDAIPAQDR PAERAREKEA EPVVPEAREP VDVEGPTRQH
RGSNGVPRQR SEDDGEAATT TMGVIPAPSP APDDGPATGP TATAPASTAD SATTDPGAVP
HPVPSAGPQP AGTPDGPVAT TEPIFLQQAP PHVVTQQAVP RQAVLQPPPP MPGRPARLAG
RTPGWPVLAA AAAAAAILAG MAGGAIGYSL ASRGPDPAAE ASAGQGTVEQ VAAKVLPSVV
QLRANGASDT TGSAVVLRPD GLLLTNNHVV EQIGSRGLVV QLQDGRTAQA KLVGRDPNSD
LALVQAQGLT GLVPAELGDS SSIAVGQQVV AVGSPLGLGG TVTTGVVSAL DRAVTVGPAQ
GARTQTVLNA VQTDAAINPG NSGGPLVDMA GRVIGINSAI ATTGPRDGSI GVGFAVPINQ
AKRVADELER TGKAARASAG LTVATDSRRT GAVVRTVAAG GPADRAGIAI GDVVVRIDDR
PVLTGDDLQA AIGSRAPGEV VRIELSDRTV EVTLDAAS
//
