ID B5YMF0_THAPS Unreviewed; 296 AA.
AC B5YMF0;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
DE Flags: Fragment;
GN ORFNames=THAPS_263092 {ECO:0000313|EMBL:ACI64796.1};
OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=35128 {ECO:0000313|EMBL:ACI64796.1, ECO:0000313|Proteomes:UP000001449};
RN [1] {ECO:0000313|EMBL:ACI64796.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:ACI64796.1};
RX PubMed=15459382; DOI=10.1126/science.1101156;
RA Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA Wilkerson F.P., Rokhsar D.S.;
RT "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT metabolism.";
RL Science 306:79-86(2004).
RN [2] {ECO:0000313|EMBL:ACI64796.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:ACI64796.1};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
RN [3] {ECO:0000313|EMBL:ACI64796.1, ECO:0000313|Proteomes:UP000001449}
RP GENOME REANNOTATION.
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:ACI64796.1};
RG Diatom Consortium;
RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA Schmutz J., Lindquist E., Shapiro H., Lucas S., Glavina del Rio T.,
RA Bruce D., Pitluck S., Rokhsar D., Armbrust V.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds, and a preference for a large uncharged residue in P1.
CC Hydrolyzes peptide amides.; EC=3.4.21.62;
CC Evidence={ECO:0000256|ARBA:ARBA00023529};
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; CP001160; ACI64796.1; -; Genomic_DNA.
DR RefSeq; XP_002296079.1; XM_002296043.1.
DR AlphaFoldDB; B5YMF0; -.
DR STRING; 35128.B5YMF0; -.
DR PaxDb; 35128-Thaps263092; -.
DR EnsemblProtists; ACI64796; ACI64796; THAPS_263092.
DR GeneID; 7448963; -.
DR KEGG; tps:THAPS_263092; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_15_0_1; -.
DR InParanoid; B5YMF0; -.
DR OMA; ETYSEME; -.
DR Proteomes; UP000001449; Chromosome 7.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 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:UP000001449};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 31..276
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 37
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 69
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACI64796.1"
FT NON_TER 296
FT /evidence="ECO:0000313|EMBL:ACI64796.1"
SQ SEQUENCE 296 AA; 31564 MW; 21A633F4F4A00E2C CRC64;
EIQQYGLDLI QAPLVWEAIE SNTKKYTNTP VKVCIIDTGY DYGNEDLPTD DVTSTETKYG
DAFIDGDGHG THCAGVIGAI GDNDRGVIGV NPDPTKFSLH ISKALNAQGI GTASSLIQAI
EGCMESGSKI ISMSLGGGPN SDIFREIYKE AYDEGILIFG AAGNQGSTDH DYPASFPHVV
SVGAVNQNGK RAPFSNFNDQ VELMAPGVEV LSTYPNDSYF TLSGTSMATP YVAGVAALVW
GYFPECSNHQ IRNVLALTAK TMSKNNFTCD FKNGYGLVQA KDAFDMLEEY GCDAGG
//