ID B8C847_THAPS Unreviewed; 336 AA.
AC B8C847;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=THAPSDRAFT_36297 {ECO:0000313|EMBL:EED90219.1};
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:EED90219.1, ECO:0000313|Proteomes:UP000001449};
RN [1] {ECO:0000313|EMBL:EED90219.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED90219.1};
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:EED90219.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED90219.1};
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).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CM000645; EED90219.1; -; Genomic_DNA.
DR RefSeq; XP_002292244.1; XM_002292208.1.
DR AlphaFoldDB; B8C847; -.
DR STRING; 35128.B8C847; -.
DR PaxDb; 35128-Thaps36297; -.
DR EnsemblProtists; EED90219; EED90219; THAPSDRAFT_36297.
DR GeneID; 7449326; -.
DR KEGG; tps:THAPSDRAFT_36297; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_1_0_1; -.
DR InParanoid; B8C847; -.
DR OMA; KYDHDAS; -.
DR Proteomes; UP000001449; Chromosome 9.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000001449}.
FT DOMAIN 24..333
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 42
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 227
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 261..294
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 336 AA; 36236 MW; 2304E9F0AAA77C61 CRC64;
MTSVDVGEGK SENVIIKDYS NAQYYGEVMI GTPPQKFTVV FDTGSSNLWV PKVNCQNCGY
WFIHGGKNKF DNSQSTSYKA DGSDFHIQYG SGDVQGYFSV DTVTLADDIV ITDQKFAEVS
NAGGLGVGYI MGQFDGILGL GFEGLSLGGA KTVFKNAIDQ KVVAQPVFAF SLGDNADGEL
TLGGYDDSKF KGDITWIPLS EPKYWQIDIE DITAGSYSSG TTNGIVDSGT SLITGPSTSI
IKIALSVGAM PNIMGQYTID CAKVPNLPDL EFKINGQVWK VPGKDLVIES AGTCLFAMMG
MDIPTGPQWI LGDVFMRKFY TIFDYENQKV GLAEPN
//