ID A0A1H1YT87_9ACTN Unreviewed; 520 AA.
AC A0A1H1YT87;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Putative serine protease PepD {ECO:0000313|EMBL:SDT24613.1};
GN ORFNames=SAMN04489717_5682 {ECO:0000313|EMBL:SDT24613.1};
OS Actinopolymorpha singaporensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Actinopolymorphaceae; Actinopolymorpha.
OX NCBI_TaxID=117157 {ECO:0000313|EMBL:SDT24613.1, ECO:0000313|Proteomes:UP000198983};
RN [1] {ECO:0000313|EMBL:SDT24613.1, ECO:0000313|Proteomes:UP000198983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22024 {ECO:0000313|EMBL:SDT24613.1,
RC ECO:0000313|Proteomes:UP000198983};
RA de Groot N.N.;
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; LT629732; SDT24613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1YT87; -.
DR STRING; 117157.SAMN04489717_5682; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000198983; Chromosome i.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:SDT24613.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SDT24613.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198983};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 161..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 407..506
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 53839 MW; 99E1606F938C1B6F CRC64;
MTERSEAYEG GRVAPGAQPQ EPRPEQPPRW SAHQPQHAQQ SSPQSSEQAP RFSQAHGPSE
SQSSRPSESA VARQAGPPGQ ATAAPWFAPP PGRQGPSGVP PQRTTRLPGY PTERPDFEPP
PPWARPAARN GVHRAEPGFP QSPADPVGRE GVRGRLPRRN VLIVVGVVLV LLAATLGATA
GVLATLRWGP ALITSEPQAP DDNLGSKGSA FPRPESVANV AKALLPSVVQ ISVTAAQGRA
TGSGFVLRDD GYILTNNHVV ASAAGGNGIK VTTNDGQEAT ATVVGRSPAY DLAVIRVKGV
RNLKPVALGD SDKVRVGEPV VALGSPLGLA GTVTSGIVSA RNRPVTAGGG QSEMSFINAL
QTDAAINPGN SGGPLVNLRA QVIGVNSAIA TISQRSPFSG NEEQGSIGLG FSIPIDQARR
TADQIIRTGH AVYPVVGAVV DVNHQGPGAR LGEIQPNSAA ARAGLQKGDV VKVINGHRVT
GADDLIVQIR SHVPGQRVEL VYDRGGDEHK VIVTLGQETG
//
