ID A0A1I5WHH3_9PSEU Unreviewed; 509 AA.
AC A0A1I5WHH3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Serine protease, S1-C subfamily, contains C-terminal PDZ domain {ECO:0000313|EMBL:SFQ19069.1};
GN ORFNames=SAMN05421810_105107 {ECO:0000313|EMBL:SFQ19069.1};
OS Amycolatopsis arida.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=587909 {ECO:0000313|EMBL:SFQ19069.1, ECO:0000313|Proteomes:UP000198727};
RN [1] {ECO:0000313|Proteomes:UP000198727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5579 {ECO:0000313|Proteomes:UP000198727};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; FOWW01000005; SFQ19069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5WHH3; -.
DR STRING; 587909.SAMN05421810_105107; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000198727; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:SFQ19069.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SFQ19069.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198727};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 407..497
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 51457 MW; 356B3ADFB8541F90 CRC64;
MNQPNSDQPD QEDPAARERR LGPRPIERPA VDPALAATFG RPRGVAGAFD RLPAPGTRSG
NGVAAPPPPE SLAEAFGRPP GAEDVVLQRP QDDIAPAETT EPEAPLWAEP TDPWRDPGAG
AVLGGPAVPA EERDDDSAGR PRGPLLSLPE VLFGRRVKPT ALALLGVVAL LVGAAGGLVG
WAIAGAGDSL TGELNIAEAT AAKERPAGSV ADVAGRVAPA VVSVEVKAGQ SGGVGSGVVL
DRQGYVVTNH HVVSQAVKDP ETEITAVFTD GTRSQARVVG TDPKTDLAVL KVNVANPVVI
QVSKSADLAP GDTVIAVGSP FGLENTVTQG IVSALHRPVT APGENGDPPV TYDAIQTDAA
INPGNSGGAL VDATGALVGI NSLIRTVGGD GEGGSIGLGF AIPVDQVVRI SESLIRDGHV
KHADLGVNAA SVAANTSEGA QIQNVVAGGP ADRAGIAEGD VVTRVGDRAV RNAAELVVAV
REHEIGDVVP VRIVRQGTPL TVDVTLGSD
//
