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Database: UniProt
Entry: U9W0D1_9CYAN
LinkDB: U9W0D1_9CYAN
Original site: U9W0D1_9CYAN 
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
//
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