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Database: UniProt
Entry: K9SS16_9SYNE
LinkDB: K9SS16_9SYNE
Original site: K9SS16_9SYNE 
ID   K9SS16_9SYNE            Unreviewed;       580 AA.
AC   K9SS16;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Putative protease with the C-terminal PDZ domain {ECO:0000313|EMBL:AFY73028.1};
GN   ORFNames=Syn7502_00908 {ECO:0000313|EMBL:AFY73028.1};
OS   Synechococcus sp. PCC 7502.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1173263 {ECO:0000313|EMBL:AFY73028.1, ECO:0000313|Proteomes:UP000010385};
RN   [1] {ECO:0000313|EMBL:AFY73028.1, ECO:0000313|Proteomes:UP000010385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7502 {ECO:0000313|EMBL:AFY73028.1,
RC   ECO:0000313|Proteomes:UP000010385};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Synechococcus sp. PCC 7502.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003594; AFY73028.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9SS16; -.
DR   STRING; 1173263.Syn7502_00908; -.
DR   KEGG; synp:Syn7502_00908; -.
DR   PATRIC; fig|1173263.3.peg.934; -.
DR   eggNOG; COG3975; Bacteria.
DR   HOGENOM; CLU_022755_0_1_3; -.
DR   OrthoDB; 9778516at2; -.
DR   Proteomes; UP000010385; Chromosome.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.60.40.3650; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR024191; Peptidase_M61.
DR   InterPro; IPR007963; Peptidase_M61_catalytic.
DR   InterPro; IPR040756; Peptidase_M61_N.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF05299; Peptidase_M61; 1.
DR   Pfam; PF17899; Peptidase_M61_N; 1.
DR   PIRSF; PIRSF016493; Glycyl_aminpptds; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AFY73028.1};
KW   Protease {ECO:0000313|EMBL:AFY73028.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010385}.
FT   DOMAIN          460..539
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   580 AA;  67115 MW;  1E78FB3EAC7EE747 CRC64;
     MSQPWQYVVS MPQPENHLFN VQLTISEWIE EFIDLHLPVW SPGSYLVREY AKHLQNFNAI
     NLDGKNLNWQ KITKNHWRVH TSKQPCQISY QIFAHELTVR TNHLDASHGY FNGAATFMFV
     PHHEDHSFTV EIVLPSENWQ IATALPHFEY QPSVFFADRY DTLADSPFEI GIHTQVKFEV
     QGKPHELIIW GEGNLDMAQV ETDTKAIITT EADLFGGLPY DHYVFILHLS NAYGGLEHRN
     CCSLIYPRFN FRGDQYLKFM NLVAHEFFHT WNVKRIRPKA LEKYDYDQEN YTTSLWFAEG
     ATSYYDQIIP LRARVYGKEQ FLKNLGETIT RLQNTPGRQV QSLYESSFDT WIKLYRPDAN
     SPNSQISYYL KGELVSLLLD LAIRISSNHA RSLDDVMRSL WQKFGNPDGN LNSEAEIGYT
     EADLYEVIAT VAGSNLQDFL EKHIYTTDEL DYNYYFEPFG IELYSGYAQK SVYTGISVRS
     NNGTAVVKSV DANSPAQLVG IDPNDEILAI NNFRVTPESF SDRLQDFQAN TEITITLFKQ
     DQLKQVLLKL ENPRCDRFLV SQIKKPNLIQ QENLRGWLGE
//
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