ID A0A0Q4LNZ7_9SPHI Unreviewed; 517 AA.
AC A0A0Q4LNZ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KQN38105.1};
GN ORFNames=ASE92_01285 {ECO:0000313|EMBL:KQN38105.1};
OS Pedobacter sp. Leaf41.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1736218 {ECO:0000313|EMBL:KQN38105.1, ECO:0000313|Proteomes:UP000051488};
RN [1] {ECO:0000313|Proteomes:UP000051488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf41 {ECO:0000313|Proteomes:UP000051488};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf41 {ECO:0000313|Proteomes:UP000051488};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQN38105.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMLE01000001; KQN38105.1; -; Genomic_DNA.
DR RefSeq; WP_056848306.1; NZ_LMLE01000001.1.
DR AlphaFoldDB; A0A0Q4LNZ7; -.
DR STRING; 1736218.ASE92_01285; -.
DR Proteomes; UP000051488; 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; -; 2.
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; PF00595; PDZ; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KQN38105.1}.
FT DOMAIN 306..398
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 517 AA; 54130 MW; B5065BFAC942A3A2 CRC64;
MKKILGITVL AAFIGGAAAI GGYKLFERNQ TGSTISEKQN LYFANNPLKV SSAGTADFTQ
AAAAVAPGVV HIKTTYEAKS GGGSRNSSPF DMFDDFFGGG GRQMQRQPRA ASGSGVIISQ
DGYIVTNNHV VENASKVEVV LTDRRKVEAK VIGRDPNTDL ALIKVNATGL PVVKMGNSDN
VQVGEWVLAV GFPLDLQTTV TAGIVSAKNR SIGIIGREQQ GNEITEEEYR EYQRTGKRPQ
APANTSIESF IQTDAAINPG NSGGALVNAT GELVGINSAI ASQSGYNQGY GFAIPVNLAR
KIVDDFMKYG MVKRGYIGVN FYPLSGDEKP EGITTSEVSG LYVSDVVAGG GGAAAGIKKG
DIIKKVDGVV INDSPDLQER IGRMNPGDKV KLSVLRDGSL KDITVTLKGE SSIGLTANNA
ATKNVEVSKL GATFAPATQA QKTKFGINSG VVVTSVVTGK AFDNIGVEKG LIITKVNGQP
VNSVADVQKA LPQGRNNMIS ISGVGEQGTY NFSFPAQ
//
