ID K9RHW0_9CYAN Unreviewed; 489 AA.
AC K9RHW0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative protease {ECO:0000313|EMBL:AFY57540.1};
GN ORFNames=Riv7116_5143 {ECO:0000313|EMBL:AFY57540.1};
OS Rivularia sp. PCC 7116.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC Rivularia.
OX NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY57540.1, ECO:0000313|Proteomes:UP000010380};
RN [1] {ECO:0000313|EMBL:AFY57540.1, ECO:0000313|Proteomes:UP000010380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY57540.1,
RC ECO:0000313|Proteomes:UP000010380};
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., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP003549; AFY57540.1; -; Genomic_DNA.
DR RefSeq; WP_015121098.1; NC_019678.1.
DR AlphaFoldDB; K9RHW0; -.
DR STRING; 373994.Riv7116_5143; -.
DR KEGG; riv:Riv7116_5143; -.
DR PATRIC; fig|373994.3.peg.5489; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_023237_0_0_3; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000010380; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000010380};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 169..439
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 436..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 398
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 489 AA; 52235 MW; 672DA8D0CE3D8D5E CRC64;
MTYLSENKEE RVYFEAVLRS ETGESMFAAE TYLAPDNLQQ FAPPPGRAMR AATVLQSLGF
RVQQIGTFSI SADGPRELWE RVFGTRVESR SQTVSPSVGE VTYLSHVAGV PFTIPPELSE
LIERAYPQSP PILFESPLPP RVKYHHLTVP ADVATVCRST PVHKVGITGK GVLVAMVDSG
FYKHSFYKWH GYNYQATLAP DATNVERDES GHGTAEAANI FANAPDIDFI GVKMGGNATL
AFKTASDLHP AVITNSWGYN ICGETLPNSL KPLEAAIIEA VQEQGITVCF SAGNGHAGFP
GMMPEVISVG GVYAHDTLDG DDFLLEASDY SSSFDSQIYP GRHVPDFCGL VGMKPNAIYI
MLPVEPGDQI DRGLGGNGYP SKDETGTDDG WAVISGTSAA SPQIAGICAL LKQVQPGLSP
SLIKSILRSS ARDVKKGNSN GTCLTSREGL PAGNGHDGAT GTGLVDAYAA YKLARSVVIR
NIHDLPSPR
//
