ID A0A168IY37_9ACTN Unreviewed; 539 AA.
AC A0A168IY37;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Putative serine protease PepD {ECO:0000313|EMBL:OAA20263.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:OAA20263.1};
GN ORFNames=UG55_10806 {ECO:0000313|EMBL:OAA20263.1};
OS Frankia sp. EI5c.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=683316 {ECO:0000313|EMBL:OAA20263.1, ECO:0000313|Proteomes:UP000077018};
RN [1] {ECO:0000313|EMBL:OAA20263.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA20263.1,
RC ECO:0000313|Proteomes:UP000077018};
RX PubMed=27389275;
RA D'Angelo T., Oshone R., Abebe-Akele F., Simpson S., Morris K., Thomas W.K.,
RA Tisa L.S.;
RT "Permanent Draft Genome Sequence for Frankia sp. Strain EI5c, a Single-
RT Spore Isolate of a Nitrogen-Fixing Actinobacterium, Isolated from the Root
RT Nodules of Elaeagnus angustifolia.";
RL Genome Announc. 4:e00660-16(2016).
RN [2] {ECO:0000313|EMBL:OAA20263.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA20263.1,
RC ECO:0000313|Proteomes:UP000077018};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA20263.1}.
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DR EMBL; LRTK01000080; OAA20263.1; -; Genomic_DNA.
DR STRING; 683316.UG55_10806; -.
DR PATRIC; fig|683316.3.peg.4911; -.
DR Proteomes; UP000077018; 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; 2.40.10.10; 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; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OAA20263.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OAA20263.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077018}.
FT DOMAIN 429..499
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..141
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 53039 MW; 863E24BB44DEFE7A CRC64;
MDPRSQDPQG PPGRQDAPXA GSPAPASRPA GSEPSGAYPA PYPPGPPAYG PPPGAGNPGA
PGAPGVHQPA EHQSGYPRTG GTQPAPTRPT GPYAPPTGQS GGREQTGGWW NPSGPSWGAP
VPPGGTPGQP AGFPGSPGSP GSPGGPDGYG RYTPATPTPP PLRRRRLVAA AVALALVSGG
IGGGVGALVA SNESPAAVVS TDSGLRQSTD GSGGVSAAAD NTVSAAAQAI LPSVVTIAEE
SGQGAGTGSG TIIRADGYIL TNNHVVSGAA NGGTLTVTMQ DGRTFDAKIK ATDPSADLAV
IKVEATGLPA ATFXDSAALQ VGELVVAVGS PLGLNGTVTS GIVSALHRPV RTGDATVRDQ
TNTVLDAIQT DAPIXXGNSG GPLVNSRGEI IGVNTAIATV GGTSSPFGET QQSGNIGVGF
AIPGSYAQKV ASQLIESGTA RHPYLGVSAF TAGENXRSTA ASGTGAQIRS LVNGGPADKA
GLXTGDVITK VGDRAITDVD SLIAAVRSHD IGNQXEVTYL RDGQTNTVQV TLLEQPPNS
//
