ID U9W0D1_9CYAN Unreviewed; 395 AA.
AC U9W0D1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Trypsin-like serine protease with c-terminal pdz domain protein {ECO:0000313|EMBL:ESA38384.1};
GN ORFNames=N836_02465 {ECO:0000313|EMBL:ESA38384.1};
OS Leptolyngbya sp. Heron Island J.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya.
OX NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA38384.1, ECO:0000313|Proteomes:UP000017515};
RN [1] {ECO:0000313|EMBL:ESA38384.1, ECO:0000313|Proteomes:UP000017515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Heron Island J {ECO:0000313|EMBL:ESA38384.1,
RC ECO:0000313|Proteomes:UP000017515};
RX PubMed=24503993;
RA Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA Fromme P.;
RT "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL Genome Announc. 2:e01166-e01113(2014).
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:ESA38384.1}.
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DR EMBL; AWNH01000013; ESA38384.1; -; Genomic_DNA.
DR AlphaFoldDB; U9W0D1; -.
DR STRING; 1385935.N836_02465; -.
DR PATRIC; fig|1385935.3.peg.787; -.
DR eggNOG; COG0265; Bacteria.
DR OrthoDB; 9807133at2; -.
DR Proteomes; UP000017515; 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; IPR048172; HhoA_HhoB_HtrA-like.
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 NCBIfam; NF041521; HhoA_HhoB_HtrA; 1.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ESA38384.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017515};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..395
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004691913"
FT DOMAIN 279..378
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 395 AA; 42157 MW; D61B5BB14EF8536A CRC64;
MSKPMSKLRF FSLRFAKSLA IYGFIAACST TAAVLTTARL MPTTAQQVPS SGSGRLLTGS
SFIASVADQV GPAVVRIDSS RTVTRQSGPF NDPFFREFFG DMWEQPSSRV ERGQGSGFVV
EADGVIWTNA HVVEGADTVT VTLRDGREFS GQVVGEDPLT DVAVIKVEAQ DLPTVTLGNS
EQLRPGEWAI AIGNPLGLDN TVTAGIISAT GRTSAQIRVP DKRVQFIQTD AAINPGNSGG
PLLNERGEVI GINTAIIGGA QGLGFAIPIN SAQRLAQELI EKGRVEHAYL GIQMRTLTND
LRQQINRDPR SNLRLSADEG VIILGLMRNS PAVEAGLEVG DVIVAMNGNS ITEAEQVQQV
VQDVGVGESI ELEIDRAGRP VSLDVQTKAL PQQRR
//