ID F4JKD9_ARATH Unreviewed; 354 AA. AC F4JKD9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 18-JAN-2017, entry version 49. DE SubName: Full=Aspartyl protease family protein {ECO:0000313|EMBL:AEE84544.1}; GN OrderedLocusNames=At4g22050 {ECO:0000313|EMBL:AEE84544.1, GN ECO:0000313|TAIR:AT4G22050}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702 {ECO:0000313|EMBL:AEE84544.1, ECO:0000313|Proteomes:UP000006548}; RN [1] {ECO:0000313|EMBL:AEE84544.1, ECO:0000313|Proteomes:UP000006548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RX PubMed=10617198; DOI=10.1038/47134; RG EU; RG CSHL and WU Arabidopsis Sequencing Project; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] {ECO:0000313|Proteomes:UP000006548} RP GENOME REANNOTATION. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the peptidase A1 family. CC {ECO:0000256|PROSITE-ProRule:PRU01103, CC ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00640153}. CC -!- SIMILARITY: Contains 1 peptidase A1 domain. {ECO:0000256|PROSITE- CC ProRule:PRU01103}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01103}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002687; AEE84544.1; -; Genomic_DNA. DR RefSeq; NP_193936.2; NM_118326.3. DR UniGene; At.2110; -. DR ProteinModelPortal; F4JKD9; -. DR SMR; F4JKD9; -. DR STRING; 3702.AT4G22050.1; -. DR MEROPS; A01.A33; -. DR PaxDb; F4JKD9; -. DR EnsemblPlants; AT4G22050.1; AT4G22050.1; AT4G22050. DR GeneID; 828294; -. DR Gramene; AT4G22050.1; AT4G22050.1; AT4G22050. DR KEGG; ath:AT4G22050; -. DR TAIR; AT4G22050; -. DR eggNOG; KOG1339; Eukaryota. DR eggNOG; ENOG410XNV7; LUCA. DR InParanoid; F4JKD9; -. DR KO; K01379; -. DR OMA; WLAKTEN; -. DR OrthoDB; EOG0936179B; -. DR Proteomes; UP000006548; Chromosome 4. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0030163; P:protein catabolic process; IBA:GO_Central. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR Gene3D; 2.40.70.10; -; 2. DR InterPro; IPR001461; Aspartic_peptidase_A1. DR InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR033121; PEPTIDASE_A1. DR InterPro; IPR021109; Peptidase_aspartic_dom. DR PANTHER; PTHR13683; PTHR13683; 1. DR Pfam; PF00026; Asp; 1. DR PRINTS; PR00792; PEPSIN. DR SUPFAM; SSF50630; SSF50630; 1. DR PROSITE; PS00141; ASP_PROTEASE; 2. DR PROSITE; PS51767; PEPTIDASE_A1; 1. PE 3: Inferred from homology; KW Aspartyl protease {ECO:0000256|PROSITE-ProRule:PRU01103, KW ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00629219}; KW Complete proteome {ECO:0000313|Proteomes:UP000006548}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01103, KW ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00629231}; KW Protease {ECO:0000256|PROSITE-ProRule:PRU01103, KW ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00629201, KW ECO:0000313|EMBL:AEE84544.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006548}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 354 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003315478. FT DOMAIN 46 350 Peptidase A1. {ECO:0000259|PROSITE: FT PS51767}. FT ACT_SITE 64 64 {ECO:0000256|PROSITE-ProRule:PRU01103}. FT ACT_SITE 251 251 {ECO:0000256|PROSITE-ProRule:PRU01103}. SQ SEQUENCE 354 AA; 39230 MW; 8F12917A9F28A05C CRC64; MYTSIFFIFS FLSVSEALVR IPLQIDHALS TNNDGVQLKN VKDFLYYGKI QIGNPGQTFT VLFDTGSSSL WVPSENWLAK TENPRNRYIS SASRTFKENG TKAELKYGKG SLTGFLSVDT VTVGGISITS QTFIEGVKTP YKEFFKKMPF DGILGLRFTD PLNFGTSVWH SMVFQGKIAK NVFSIWLRRF SNSGEINGGE VVFGGIIPAH FSGDHTYVDV EGPGNFFAMS NIWVGGKNTN ICSSGCKAIV DSGSSNINVP MDSADEIHRY IGVEPNCNNF ETLPDVTFTI GGKAFVLTPL DYIRRSRSQC TSKFVGKTNR SHWTLGIPFM RVFHTVFDYQ NTLAVKVGFA KSTD //