Entry
stringlengths
6
10
Entry Name
stringlengths
5
11
Sequence
stringlengths
2
35.2k
EC number
stringlengths
7
118
Cofactor
stringlengths
38
1.77k
Gene Ontology (biological process)
stringlengths
18
11.3k
Gene Ontology (cellular component)
stringlengths
17
1.75k
Gene Ontology (molecular function)
stringlengths
24
2.09k
Pfam
stringlengths
8
232
Gene3D
stringlengths
10
250
Protein families
stringlengths
9
237
Post-translational modification
stringlengths
16
8.52k
Subcellular location [CC]
stringlengths
29
6.18k
Catalytic activity
stringlengths
64
35.7k
Kinetics
stringlengths
69
11.7k
Pathway
stringlengths
27
908
pH dependence
stringlengths
64
955
Temperature dependence
stringlengths
70
1.16k
Function [CC]
stringlengths
17
15.3k
Organism
stringlengths
8
196
O64644
SAP18_ARATH
MAEAARRQGGGRPLPPPPRGVNQQPPRPKPEPVDREKTCPLLLRVFTKSGGHHTSEDYAVRGKEPKDEVQIYTWKDASLRELTDLVKEVSVAARRRNARLSFAFVYPNNKGGYNVREVGETMAYPNRKQPDDSKTLSELPFEIGDYLDVAIY
null
null
response to abscisic acid [GO:0009737]; response to salt stress [GO:0009651]
cytosol [GO:0005829]; nucleolus [GO:0005730]
transcription corepressor activity [GO:0003714]
PF06487;
3.10.20.550;
SAP18 family
null
null
null
null
null
null
null
FUNCTION: Links the histone deacetylase complex to transcriptional repressors bound to chromatin. Involved in the tethering of the SIN3 complex to core histone proteins. {ECO:0000269|PubMed:16429262}.
Arabidopsis thaliana (Mouse-ear cress)
O64645
SOC1_ARATH
MVRGKTQMKRIENATSRQVTFSKRRNGLLKKAFELSVLCDAEVSLIIFSPKGKLYEFASSNMQDTIDRYLRHTKDRVSTKPVSEENMQHLKYEAANMMKKIEQLEASKRKLLGEGIGTCSIEELQQIEQQLEKSVKCIRARKTQVFKEQIEQLKQKEKALAAENEKLSEKWGSHESEVWSNKNQESTGRGDEESSPSSEVETQLFIGLPCSSRK
null
null
cell differentiation [GO:0030154]; flower development [GO:0009908]; maintenance of inflorescence meristem identity [GO:0010077]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of flower development [GO:0009911]; positive regulation of transcription by RNA polymerase II [GO:0045944]...
cytoplasm [GO:0005737]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF01486;PF00319;
3.40.1810.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:18466303, ECO:0000269|PubMed:31540691}. Cytoplasm {ECO:0000269|PubMed:18466303}. Note=Translocation from the cytoplasm to the nucleus in the presence of AGL24.
null
null
null
null
null
FUNCTION: Transcription activator active in flowering time control. May integrate signals from the photoperiod, vernalization and autonomous floral induction pathways. Can modulate class B and C homeotic genes expression. When associated with AGL24, mediates effect of gibberellins on flowering under short-day condition...
Arabidopsis thaliana (Mouse-ear cress)
O64647
TCP9_ARATH
MATIQKLEEVAGKDQTLRAVDLTIINGVRNVETSRPFQVNPTVSLEPKAEPVMPSFSMSLAPPSSTGPPLKRASTKDRHTKVEGRGRRIRMPATCAARIFQLTRELGHKSDGETIRWLLENAEPAIIAATGTGTVPAIAMSVNGTLKIPTTTNADSDMGENLMKKKRKRPSNSEYIDISDAVSASSGLAPIATTTTIQPPQALASSTVAQQLLPQGMYPMWAIPSNAMIPTVGAFFLIPQIAGPSNQPQLLAFPAAAASPSSYVAAVQQASTMARPPPLQVVPSSGFVSVSDVSGSNLSRATSVMAPSSSSGVTTGSSSS...
null
null
negative regulation of leaf senescence [GO:1900056]; regulation of cell size [GO:0008361]; regulation of DNA-templated transcription [GO:0006355]; root development [GO:0048364]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
PF03634;
null
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
null
Arabidopsis thaliana (Mouse-ear cress)
O64682
PID_ARATH
MLRESDGEMSLGTTNSPISSGTESCSSFSRLSFDAPPSTIPEEESFLSLKPHRSSDFAYAEIRRRKKQGLTFRDFRLMRRIGAGDIGTVYLCRLAGDEEESRSSYFAMKVVDKEALALKKKMHRAEMEKTILKMLDHPFLPTLYAEFEASHFSCIVMEYCSGGDLHSLRHRQPHRRFSLSSARFYAAEVLVALEYLHMLGIIYRDLKPENILVRSDGHIMLSDFDLSLCSDSIAAVESSSSSPENQQLRSPRRFTRLARLFQRVLRSKKVQTLEPTRLFVAEPVTARSGSFVGTHEYVAPEVASGGSHGNAVDWWAFGVF...
2.7.11.1
null
auxin polar transport [GO:0009926]; auxin-activated signaling pathway [GO:0009734]; cotyledon development [GO:0048825]; phosphorylation [GO:0016310]; phyllome development [GO:0048827]; positive gravitropism [GO:0009958]; response to auxin [GO:0009733]; root hair elongation [GO:0048767]; root hair initiation [GO:0048766...
cell surface [GO:0009986]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
PTM: Autophosphorylated. Phosphorylated by PDK1.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16731587, ECO:0000269|PubMed:17889649, ECO:0000269|PubMed:20040538}. Note=Targeted to the cell periphery.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase involved in the regulation of auxin signaling. Acts as a positive regulator of cellular auxin efflux and regulates organ development by enhancing polar auxin transport. Phosphorylates conserved serine residues in the PIN auxin efflux carriers. Phosphorylation of PIN proteins is...
Arabidopsis thaliana (Mouse-ear cress)
O64722
ZHD3_ARATH
MEIASQEDPIPINTSYGNSGGGHGNMNHHHHANSAPSSLNITTSNPLLVSSNSNGLGKNHDHSHHHHVGYNIMVTNIKKEKPVVIKYKECLKNHAATMGGNAIDGCGEFMPSGEEGSIEALTCSVCNCHRNFHRRETEGEEKTFFSPYLNHHQPPPQQRKLMFHHKMIKSPLPQQMIMPIGVTTAGSNSESEDLMEEEGGGSLTFRQPPPPPSPYSYGHNQKKRFRTKFTQEQKEKMISFAERVGWKIQRQEESVVQQLCQEIGIRRRVLKVWMHNNKQNLSKKSNNVSNNVDLSAGNNDITENLASTNP
null
null
glucosinolate metabolic process [GO:0019760]; regulation of developmental process [GO:0050793]
nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; transcription cis-regulatory region binding [GO:0000976]
PF04770;
1.10.10.60;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Note=Interactions with MIF proteins prevent nuclear subcellular location and leads to a scattered repartition throughout the cytoplasm. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Putative transcription factor. {ECO:0000250}.
Arabidopsis thaliana (Mouse-ear cress)
O64728
STI_ARATH
MSGSRVSDLSKLHLKKELTQIRKAGRVLRDPGTTSSWKSPLDSSRSVALLETPASRNGGSSSQFPIRGESSTNRRGKEKKVFLYNWKTQKSSSEKSGLAKNGKEEEEEEEDASSWTQASVNDDDDVSDARNGGDSYRREIQSASMGFRCRDTNLASQGVSKMRKSNVGSCKKKSKKKISSSRLDCLSKYQPRDDIVARNCNAGSDDTEEELSNSEDLRKVTGASPLLLKLKQKNWSRSSSRLLRANNRKEDSSCTYNSTPALSTSSYNMYAVRNPSTVGSWDGTTTSVNDGDDELDDNLDLPGRQGCGIPCYWTKKAMKH...
null
null
DNA repair [GO:0006281]; DNA-templated DNA replication [GO:0006261]; trichome branching [GO:0010091]; trichome differentiation [GO:0010026]
DNA polymerase III complex [GO:0009360]; DNA replication factor C complex [GO:0005663]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA clamp loader activity [GO:0003689]; DNA-directed DNA polymerase activity [GO:0003887]
PF13177;PF12169;
1.10.8.60;1.20.272.10;3.40.50.300;
DnaX/STICHEL family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Acts as a key regulator of trichome branching through an endoreduplication-independent pathway. {ECO:0000269|PubMed:10572032, ECO:0000269|PubMed:12586888, ECO:0000269|PubMed:18477400, ECO:0000269|PubMed:22210898, ECO:0000269|PubMed:9367433}.
Arabidopsis thaliana (Mouse-ear cress)
O64743
BBE15_ARATH
MAFAISKRNATLFLVTLLLISVPLSSSTLQQDFVKCLVDNSDVSFPITASFFSPDQNATLFKEELESTAQNLRYLTPSNPKPVFIFEPLYETHVQAAVVCAKKLQLHLRLRSGGHDYEGLSFVAEDETPFVIVDLSKLRQVDVDLDSNSAWAHAGATIGEVYYRIQEKSQTHGFPAGLCSSLGIGGHLVGGAYGSMMRKFGLGADNVLDARIVDANGQILDRAAMGEDVFWAIRGGGGGSFGVILAWKIKLVPVPATVTVFTVTKTLEQDGTKVLYKWEQIADKLDDDLFIRVIISPASKTTKPGNRTISMSYQAQFLGD...
1.1.99.-
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:26037923}; Note=Binds 1 FAD per subunit in a bicovalent manner. {ECO:0000269|PubMed:26037923};
embryo development ending in seed dormancy [GO:0009793]; polar nucleus fusion [GO:0010197]
extracellular region [GO:0005576]; plant-type cell wall [GO:0009505]; plasmodesma [GO:0009506]
cinnamyl-alcohol dehydrogenase activity [GO:0045551]; coniferyl-alcohol dehydrogenase activity [GO:0050268]; FAD binding [GO:0071949]; sinapyl alcohol dehydrogenase activity [GO:0052747]
PF08031;PF01565;
3.30.465.10;3.40.462.20;3.30.43.10;
Oxygen-dependent FAD-linked oxidoreductase family
PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage. {ECO:0000269|PubMed:26037923}.
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000303|PubMed:26037923}.
CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl alcohol + A = (E)-4-coumaraldehyde + AH2; Xref=Rhea:RHEA:76451, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:28353, ChEBI:CHEBI:64555; Evidence={ECO:0000269|PubMed:26037923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76452; Evidence={ECO:0000305|PubMed:260379...
null
null
null
null
FUNCTION: Required for endosperm development and polar nuclei fusion (PubMed:15634699). Mediates oxidation of p-hydroxylated derivatives of cinnamyl alcohol (i.e. the monolignols p-coumaryl-, coniferyl-, and sinapyl alcohol) to their corresponding aldehydes. Can also use the beta-O-glycosylated form of coniferyl alcoho...
Arabidopsis thaliana (Mouse-ear cress)
O64750
PSA2_ARATH
MAASSSHLFALPSPASPFLSAPNRNRVRVLAKSCPENQSFDSNDSDSSSETTHKAQGDQKSVSRRQWMTACVCASAALISNSYTFVSVQSAAALDKKPGGSCRNCQGSGAVLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLVCPVCLGTGLPNNKGLLRRPGARELLEKMYNGRLLPDS
null
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q6A662}; Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000250|UniProtKB:Q6A662};
megagametogenesis [GO:0009561]; photosystem I assembly [GO:0048564]; thylakoid membrane organization [GO:0010027]
chloroplast [GO:0009507]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid lumen [GO:0009543]; chloroplast thylakoid membrane [GO:0009535]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]
metal ion binding [GO:0046872]; protein-disulfide reductase (NAD(P)) activity [GO:0047134]
null
2.10.230.10;
DnaJ family
null
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:27047527}.
null
null
null
null
null
FUNCTION: Involved in female gametophyte development. Required for embryo sac development (PubMed:15634699). Nuclear genome-encoded factor required for the accumulation of photosystem I (PSI) during plant development (PubMed:25228689). Required for light acclimation and chloroplast development (PubMed:27047527). {ECO:0...
Arabidopsis thaliana (Mouse-ear cress)
O64752
JMJ15_ARATH
MEPFSAAQNKEDKDTSVEPPRRRCHRKNKGTNVEPPSSPYHPKVLARWDPANEKRPDIGEAPVFHPTSEEFEDTLAYIEKIRPLAESFGICRIVPPSNWSPPCRLKGDSIWKNKNFPTRVQFVDLLQNRGPVKKKTPKGRKRKRGKYSRTVAPKKRNGSVSKSVSTPKATEEENFGFESGPEFTLEKFEKYAQDFKDSYFERKDNVGDPSVEEIEGEYWRIIEKETNEVKVLYGTDLENPILGSGFSKGVKIPTRRNDMDKYISSGWNLNNLARLQGSLLSFEDCEISGVQVPWLYVGMCFSTFCWHVEDNHLYSLNYHH...
1.14.11.-
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q8GUI6}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8GUI6};
embryo development ending in seed dormancy [GO:0009793]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression, epigenetic [GO:0045814]; pollen development [GO:0009555]; positive regulation of response to salt stress [GO:1901002]; regulation of DNA-templated transcripti...
chromatin [GO:0000785]; nucleus [GO:0005634]
histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; metal ion binding [GO:0046872]
PF05965;PF05964;PF02373;PF02375;PF02928;
3.30.160.360;2.60.120.650;
JARID1 histone demethylase family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000255|PROSITE-ProRule:PRU00768}.
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + succinate; Xref=Rhea:RHEA:60212, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,...
null
null
null
null
FUNCTION: Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a specific activity for H3K4me3 (PubMed:22555401). No activity on H3K4me2, H3K4me1, H3K9me3/2, H3K27me3/2 and H3K36me3/2 (PubMed:22555401). Involved in the control of flowering time by demethylating H3K4me3 at the FLC locus and repressi...
Arabidopsis thaliana (Mouse-ear cress)
O64763
ATL9_ARATH
MAILDTKSSRWIPHNLLFLLLLLLLQSVPYGFGQTQTTPPGTTKTKPNDPVVVVITVLFLVIFFMVFGSIFCRRSNAQFSRSSIFRSTDADAESQVVRIRRLTARGLDAEAIETFPTFLYSEVKAVRIGKGGVECAVCLCEFEDDETLRLMPPCCHVFHADCVDVWLSEHSTCPLCRADLVLNQQGDDDDSTESYSGTDPGTISSSTDPERGMVLESSDAHLLDAVTWSNSNITPRSKSTGLSSWQITGILFPRSHSTGHSLIQPAGNLDRFTLRLPDDVRRQLMKTSRTMGHVALLPQARSSRSGYRSGSVGSERSAFP...
2.3.2.27
null
defense response to fungus [GO:0050832]; protein ubiquitination [GO:0016567]; response to chitin [GO:0010200]
membrane [GO:0016020]
metal ion binding [GO:0046872]; ubiquitin-protein transferase activity [GO:0004842]
PF13639;
3.30.40.10;
RING-type zinc finger family, ATL subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:15644464};
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: E3 ubiquitin-protein ligase able to catalyze polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8 in vitro. May be involved in the early steps of the plant defense signaling pathway. {ECO:0000269|PubMed:15644464, ECO:0000269|PubMed:15923325}.
Arabidopsis thaliana (Mouse-ear cress)
O64765
UAP2_ARATH
MKEPTTEIEIETSAVATILPPPLPPTASPHQALVERLKDYGQEDVFSLWDELSPEERDLLLRDIENLDLPRIDRIIRCSLHSQGLPVAAIEPVPENCVSTVEERTKEDREKWWKMGLKAIYEGKLGVVLLSGGQGTRLGSSDPKGCYNIGLPSGKSLFQIQAERILCVQRLASQAMSEASPTRPVTIQWYIMTSPFTHEPTQKFFKSHKYFGLEPDQVTFFQQGTLPCISKDGKFIMETPFSLSKAPDGNGGVYTALKSSRLLEDMASRGIKYVDCYGVDNVLVRVADPTFLGYFIDKSAASAAKVVRKAYPQEKVGVFV...
2.7.7.23; 2.7.7.83; 2.7.7.9
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20557289}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20557289};
embryo development ending in seed dormancy [GO:0009793]; embryo sac development [GO:0009553]; pollen development [GO:0009555]; UDP-glucose metabolic process [GO:0006011]; UDP-N-acetylgalactosamine metabolic process [GO:0019276]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048]; UDP-N-acetylglucosamine metaboli...
cytoplasm [GO:0005737]
UDP-N-acetylgalactosamine diphosphorylase activity [GO:0052630]; UDP-N-acetylglucosamine diphosphorylase activity [GO:0003977]; UTP:glucose-1-phosphate uridylyltransferase activity [GO:0003983]
PF01704;
null
UDPGP type 1 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000269|PubMed:20557289}; CATALYTIC ACTIVIT...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=180 uM for GlcNAc-1-P {ECO:0000269|PubMed:20557289}; KM=203 uM for UTP {ECO:0000269|PubMed:20557289}; KM=65 uM for UDP-GlcNAc {ECO:0000269|PubMed:20557289}; KM=808 uM for UDP-GalNAc {ECO:0000269|PubMed:20557289};
PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
null
null
FUNCTION: Uridylyltransferase involved in the biosynthesis of UDP-glucosamine, an essential precursor for glycoprotein and glycolipid synthesis. Can use UDP-glucosamine, the 4-epimer UDP-galactosamine and UDP-glucose as substrates (PubMed:20557289). Acts redundantly with GLCNAC1PUT1. Required for gametogenesis and embr...
Arabidopsis thaliana (Mouse-ear cress)
O64768
RAF24_ARATH
MDQAKGYEHVRYTAPDPRDEGLGSINQRFSHDSSTNVNTYVRPPDYGVSTPARPVLNYSIQTGEEFAFEFMRDRVIMKPQFIPNVYGEHSGMPVSVNLSALGMVHPMSESGPNATVLNIEEKRQSFEHERKPPSRIEDKTYHELVQSAPVISSKNDTGQRRHSLVSSRASDSSLNRAKFLCSFGGKVIPRPRDQKLRYVGGETRIIRISKTISFQELMHKMKEIFPEARTIKYQLPGEDLDALVSVSSDEDLQNMMEECIVFGNGGSEKPRMFLFSSSDIEEAQFVMEHAEGDSEVQYVVAVNGMDLSSRRSSLGLSPPG...
2.7.11.1
null
cellular response to auxin stimulus [GO:0071365]; phosphorylation [GO:0016310]; regulation of auxin mediated signaling pathway [GO:0010928]; response to auxin [GO:0009733]; signal transduction [GO:0007165]
cytoplasm [GO:0005737]
ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]
PF00564;PF07714;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
PTM: Hyperphosphorylated in response to auxin in an ABP1- and TMK1-dependent manner. {ECO:0000269|PubMed:38128538}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:38128538}. Note=Broadly distributed to both membrane-associated and intracellular punctate structures. {ECO:0000269|PubMed:38128538}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027}; ...
null
null
null
null
FUNCTION: RAF-like protein kinase acting, together with RAF20, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming (PubMed:38128538). Required for general growth and developmenta...
Arabidopsis thaliana (Mouse-ear cress)
O64782
SD129_ARATH
MGMVLFACLLLLIIFPTCGYAAINTSSPLSIRQTLSSPGGFYELGFFSPNNTQNQYVGIWFKKIVPRVVVWVANRDTPVTSSAANLTISSNGSLILLDGKQDVIWSTGKAFTSNKCHAELLDTGNFVVIDDVSGNKLWQSFEHLGNTMLPQSSLMYDTSNGKKRVLTTWKSNSDPSPGEFSLEITPQIPTQGLIRRGSVPYWRCGPWAKTRFSGISGIDASYVSPFSVVQDTAAGTGSFSYSTLRNYNLSYVTLTPEGKMKILWDDGNNWKLHLSLPENPCDLYGRCGPYGLCVRSDPPKCECLKGFVPKSDEEWGKGNW...
2.7.12.1
null
detection of lipopolysaccharide [GO:0032497]; innate immune response [GO:0045087]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; pattern recognition receptor signaling pathway [GO:0002221]; protein autophosphorylation [GO:0046777]; recognition of pollen [GO:0048544]
plasma membrane [GO:0005886]
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; carbohydrate binding [GO:0030246]; pattern recognition receptor activity [GO:0038187]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine ki...
PF01453;PF11883;PF08276;PF07714;PF00954;
2.90.10.10;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
PTM: Autophosphorylated at Tyr-600 (PubMed:31922267). Autophosphorylation at Tyr-600 is required for downstream phosphorylation of the receptor-like cytoplasmic kinase PBL34, PBL35 and PBL36, and activation of plant immunity (PubMed:31922267). {ECO:0000269|PubMed:31922267}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25729922, ECO:0000269|PubMed:31922267}; Single-pass type I membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000269|PubMed:31922267}; Physiolog...
null
null
null
null
FUNCTION: S-domain receptor protein kinase involved in lipopolysaccharide (LPS) sensing (PubMed:25729922, PubMed:29431629, PubMed:31922267). Specifically detects LPS of Pseudomonas and Xanthomonas species (PubMed:25729922). LPS are major components of the outer membrane of Gram-negative bacteria and are important micro...
Arabidopsis thaliana (Mouse-ear cress)
O64816
CSK2P_ARATH
MALRPCTGFTISSLRNASAANNNLFSLLSFSSSSPAKRNLLLSSLQDNLRRFASSASLYRQHLRNQQQQHQQQQQSRVKEKSETLAQKIGKSIRRAGAPSKARVYADVNVVRPKDYWDYESLAVQWGVQDDYEVVRKVGRGKYSEVFEGIHATDNEKCVIKILKPVKKKKIKREIKILQNLCGGPNIVKLLDIVRDQQSKTPSLIFEHVNNKDFKVLYPTLSDYDVRYYIFELLKALDFCHSRGIMHRDVKPHNVMIDHEQRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDLQDYDYSLDLWSLGCMFAGMIF...
2.7.11.1
null
cellular response to abscisic acid stimulus [GO:0071215]; chloroplast-nucleus signaling pathway [GO:0010019]; DNA damage response [GO:0006974]; negative regulation of seed germination [GO:0010187]; phosphorylation [GO:0016310]; regulation of cell cycle [GO:0051726]; regulation of growth [GO:0040008]; regulation of phot...
chloroplast [GO:0009507]; cytosol [GO:0005829]; nucleus [GO:0005634]; protein kinase CK2 complex [GO:0005956]
ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, CK2 subfamily
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:16926165}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr...
null
null
null
null
FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site (By similarity). Involved in the regulation of various developmental processes (PubMed:26025542). Involved in the regulation of plant growth ...
Arabidopsis thaliana (Mouse-ear cress)
O64817
CSK23_ARATH
MSKARVYTDVNVVRPKEYWDYESLVVQWGHQDDYEVVRKVGRGKYSEVFEGKNVNTNERCVIKILKPVKKKKIKREIKILQNLCGGPNIVKLYDIVRDEHSKTPSLVFEFVNSVDFKVLYPTLTDYDIRYYIYELLKALDFCHSQGIMHRDVKPHNVMIDHQLRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDLQDYDYSLDMWSLGCMFAGMIFRKEPFFYGHDNHDQLVKIAKVLGTNELDHYLNKYQLDLDPQLEALVGRHVPKPWSKFINADNQHLVSPEAIDFLDKLLQYDHQDRLTAREAMDHPYFA...
2.7.11.1
null
chromatin organization [GO:0006325]; circadian rhythm [GO:0007623]; DNA repair [GO:0006281]; phosphorylation [GO:0016310]; regulation of cell cycle [GO:0051726]; regulation of circadian rhythm [GO:0042752]; response to gamma radiation [GO:0010332]; response to UV-C [GO:0010225]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; protein kinase CK2 complex [GO:0005956]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, CK2 subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16926165, ECO:0000269|PubMed:21735091}. Nucleus, nucleolus {ECO:0000269|PubMed:16926165}. Cytoplasm {ECO:0000269|PubMed:21735091}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr...
null
null
null
null
FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site. The tetrameric holoenzyme CK2 is composed of two alpha and two beta subunits (By similarity). Acts as a circadian clock component that maint...
Arabidopsis thaliana (Mouse-ear cress)
O64825
LYK4_ARATH
MISFSFHLLVFILLSLSSFATAQQPYVGISTTDCSVSDNTTSVFGYSCNGLNKTCQAYVIFRSTPSFSTVTSISSLFSVDPSLVSSLNDASPSTSFPSGQQVIIPLTCSCTGDDSQSNITYTIQPNDSYFAIANDTLQGLSTCQALAKQNNVSSQSLFPGMRIVVPIRCACPTAKQINEDGVKYLMSYTVVFEDTIAIISDRFGVETSKTLKANEMSFENSEVFPFTTILIPLVNPPANTNSLIPPPPPPPPQSVSPPPLSPDGRKSKKKTWVYALAGVLGGALVLSVIGAAIFCLSKKKTKTQTQEETGNLDSFMGKKP...
2.7.11.1
null
cellular response to chitin [GO:0071323]; cellular response to molecule of bacterial origin [GO:0071219]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]
plasma membrane [GO:0005886]
ATP binding [GO:0005524]; chitin binding [GO:0008061]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF01476;PF07714;
3.10.350.10;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
PTM: Autophosphorylated; induced by chitin and derivatives. {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22744984}; Single-pass membrane protein {ECO:0000269|PubMed:22744984}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr...
null
null
null
null
FUNCTION: Lysin motif (LysM) receptor kinase that functions as a cell surface receptor in chitin elicitor (chitooligosaccharides) signaling leading to innate immunity. Recognizes microbe-derived N-acetylglucosamine (NAG)-containing ligands. Involved in the resistance to the pathogenic fungus Alternaria brassicicola and...
Arabidopsis thaliana (Mouse-ear cress)
O64827
SUVR5_ARATH
MEVKMDELVLDVDVEEATGSELLVKSEPEADLNAVKSSTDLVTVTGPIGKNGEGESSPSEPKWLQQDEPIALWVKWRGKWQAGIRCAKADWPLTTLRGKPTHDRKKYCVIFFPHTKNYSWADMQLVRSINEFPDPIAYKSHKIGLKLVKDLTAARRYIMRKLTVGMFNIVDQFPSEVVSEAARDIIIWKEFAMEATRSTSYHDLGIMLVKLHSMILQRYMDPIWLENSFPLWVQKCNNAVNAESIELLNEEFDNCIKWNEVKSLSESPMQPMLLSEWKTWKHDIAKWFSISRRGVGEIAQPDSKSVFNSDVQASRKRPKL...
2.1.1.-
null
chromatin remodeling [GO:0006338]; methylation [GO:0032259]; negative regulation of gene expression, epigenetic [GO:0045814]
chromosome [GO:0005694]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; histone H3 methyltransferase activity [GO:0140938]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270]
PF05033;PF00856;PF18868;
3.30.160.60;2.170.270.10;
Class V-like SAM-binding methyltransferase superfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17224141}. Chromosome {ECO:0000250|UniProtKB:Q5DW34}. Note=Associates with euchromatic regions. {ECO:0000250|UniProtKB:Q5DW34}.
CATALYTIC ACTIVITY: Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:000026...
null
null
null
null
FUNCTION: Histone methyltransferase that functions together with its binding partner LDL1/SWP1 as one of the regulators of flower timing in Arabidopsis (PubMed:17224141). Mediates H3K9me2 deposition and regulates gene expression in a DNA methylation-independent manner. Binds DNA through its zinc fingers and represses t...
Arabidopsis thaliana (Mouse-ear cress)
O64879
BGL15_ARATH
MRGNYLSLLVVLIVLASNDVLANNNSSTPKLRRSDFPEDFIFGSATSAYQVEGGAHEDGRGPSIWDTFSEKYPEKIKDGSNGSVADNSYHLYKEDVALLHQIGFNAYRFSISWSRILPRGNLKGGINQAGIDYYNNLINELLSKGIKPFATMFHWDTPQALEDAYGGFRGAEIVNDFRDYADICFKNFGDRVKHWMTLNEPLTVVQQGYVAGVMAPGRCSKFTNPNCTDGNGATEPYIVGHNLILSHGAAVQVYREKYKASQQGQVGIALNAGWNLPYTESPKDRLAAARAMAFTFDYFMEPLVTGKYPVDMVNNVKGRL...
3.2.1.21
null
carbohydrate metabolic process [GO:0005975]; kaempferol O-glucoside metabolic process [GO:0033329]; quercetin O-glucoside metabolic process [GO:0033302]
apoplast [GO:0048046]; Golgi apparatus [GO:0005794]; plant-type cell wall [GO:0009505]; plasmodesma [GO:0009506]
beta-glucosidase activity [GO:0008422]; scopolin beta-glucosidase activity [GO:0102483]
PF00232;
3.20.20.80;
Glycosyl hydrolase 1 family
null
SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:25468534}.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; Evidence={ECO:0000269|PubMed:25468534};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=51 uM for kaempferol 3-O-beta-glucoside-7-O-alpha-rhamnoside {ECO:0000269|PubMed:25468534}; KM=36 uM for quercetin 3-O-beta-glucoside-7-O-alpha-rhamnoside {ECO:0000269|PubMed:25468534}; KM=60 uM for kaempferol 3-O-beta-glucoside {ECO:0000269|PubMed:25468534}; KM=52...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:25468534};
null
FUNCTION: Beta-glucosidase involved in the rapid degradation of flavonol 3-O-beta-glucoside-7-O-alpha-rhamnosides during abiotic stress recovery. No activity with quercetin 3-O-alpha-rhamnoside, quercetin 3-O-beta-galactoside and rutin. {ECO:0000269|PubMed:25468534}.
Arabidopsis thaliana (Mouse-ear cress)
O64883
BGL26_ARATH
MAHLQRTFPTEMSKGRASFPKGFLFGTASSSYQYEGAVNEGARGQSVWDHFSNRFPHRISDSSDGNVAVDFYHRYKEDIKRMKDINMDSFRLSIAWPRVLPYGKRDRGVSEEGIKFYNDVIDELLANEITPLVTIFHWDIPQDLEDEYGGFLSEQIIDDFRDYASLCFERFGDRVSLWCTMNEPWVYSVAGYDTGRKAPGRCSKYVNGASVAGMSGYEAYIVSHNMLLAHAEAVEVFRKCDHIKNGQIGIAHNPLWYEPYDPSDPDDVEGCNRAMDFMLGWHQHPTACGDYPETMKKSVGDRLPSFTPEQSKKLIGSCDY...
3.2.1.21
null
carbohydrate metabolic process [GO:0005975]; defense response by callose deposition in cell wall [GO:0052544]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; glucosinolate metabolic process [GO:0019760]; indole glucosinolate catabolic process [GO:0042344]; induced systemic resistan...
chloroplast envelope [GO:0009941]; membrane [GO:0016020]; peroxisome [GO:0005777]
beta-glucosidase activity [GO:0008422]; scopolin beta-glucosidase activity [GO:0102483]; thioglucosidase activity [GO:0019137]
PF00232;
3.20.20.80;
Glycosyl hydrolase 1 family
null
SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16293760}.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; Evidence={ECO:0000269|PubMed:19095900};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=722 uM for indol-3-yl-methylglucosinolate {ECO:0000269|PubMed:19095900}; KM=150 uM for 4-methyl-umbelliferyl-beta-D-glucoside {ECO:0000269|PubMed:19095900}; Vmax=7.5 umol/min/mg enzyme with indol-3-yl-methylglucosinolate as substrate {ECO:0000269|PubMed:19095900}; ...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:19095900};
null
FUNCTION: Possesses beta-glucosidase activity toward 4-methyl-umbelliferyl-beta-D-glucoside in vitro. Possesses myrosinase activity toward indol-3-yl-methylglucosinolate (I3M) and 4-methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) in vivo (PubMed:19095900). Component of an inducible preinvasion resistance mechanism tha...
Arabidopsis thaliana (Mouse-ear cress)
O64884
OFT20_ARATH
MALSKNSNSNSFNKKKVSYISVPSQIINSLSSSSLQSLLVSPKKSSRSTNRFSFSYRNPRIWFFTLFLVSLFGMLKLGFNVDPISLPFSRYPCSTTQQPLSFDGEQNAASHLGLAQEPILSTGSSNSNAIIQLNGGKNETLLTEGDFWKQPDGLGFKPCLGFTSQYRKDSNSILKNRWKYLLVVVSGGMNQQRNQIVDAVVIARILGASLVVPVLQVNVIWGDESEFADIFDLEHFKDVLADDVHIVSSLPSTHVMTRPVEEKRTPLHASPQWIRAHYLKRINRERVLLLRGLDSRLSKDLPSDLQKLRCKVAFQALRFS...
2.4.1.-
null
cell wall organization [GO:0071555]; fucose metabolic process [GO:0006004]
Golgi membrane [GO:0000139]
glycosyltransferase activity [GO:0016757]
PF10250;
null
Glycosyltransferase GT106 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|Ref.11}; Single-pass type II membrane protein {ECO:0000305|Ref.11}.
null
null
PATHWAY: Glycan metabolism. {ECO:0000305}.
null
null
FUNCTION: May play a role in the biosynthesis of matrix polysaccharides and contribute to the biomechanics and development of the plant cell wall. {ECO:0000269|Ref.11}.
Arabidopsis thaliana (Mouse-ear cress)
O64903
NDK2_ARATH
MVGATVVSKWTPLCVASPPERNSASLNPHCSPARVNFRTALAAFRPQFRLFSRNSASRRRLRASSSAESGIFLPHLVASMEDVEETYIMVKPDGIQRGLVGEIISRFEKKGFKLIGLKMFQCPKELAEEHYKDLSAKSFFPNLIEYITSGPVVCMAWEGVGVVASARKLIGKTDPLQAEPGTIRGDLAVQTGRNIVHGSDSPENGKREIGLWFKEGELCKWDSALATWLRE
2.7.4.6
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
auxin-activated signaling pathway [GO:0009734]; CTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; phosphorylation [GO:0016310]; red, far-red light phototransduction [GO:0009585]; response to hydrogen peroxide [GO:0042542]; response to UV [GO:0009411]; UTP biosynthetic process [GO:0006228]
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plastid [GO:0009536]; thylakoid [GO:0009579]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleoside diphosphate kinase activity [GO:0004550]
PF00334;
3.30.70.141;
NDK family
PTM: Autophosphorylated. {ECO:0000269|PubMed:12506203}.
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18431481}.
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleosid...
null
null
null
null
FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. May activate MPK3 and MPK6. May be involved in the regulation of cellular redox state and hydroge...
Arabidopsis thaliana (Mouse-ear cress)
O64948
LONP2_ARATH
MAETVELPSRLAILPFRNKVLLPGAIIRIRCTSHSSVTLVEQELWQKEEKGLIGILPVRDDAEGSSIGTMINPGAGSDSGERSLKFLVGTTDAQKSDAKDQQDLQWHTRGVAARALHLSRGVEKPSGRVTYVVVLEGLSRFNVQELGKRGPYSVARITSLEMTKAELEQVKQDPDFVALSRQFKTTAMELVSVLEQKQKTGGRTKVLLETVPIHKLADIFVASFEMSFEEQLSMLDSVDLKVRLSKATELVDRHLQSIRVAEKITQKVEGQLSKSQKEYLLRQQMRAIKEELGDNDDDEDDVAALERKMQAAGMPSNIWK...
3.4.21.53
null
lateral root development [GO:0048527]; protein import into peroxisome matrix, docking [GO:0016560]; protein processing [GO:0016485]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; protein targeting to peroxisome [GO:0006625]
intracellular organelle lumen [GO:0070013]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; serine-type endopeptidase activity [GO:0004252]
PF00004;PF05362;PF02190;
1.10.8.60;1.20.5.5270;1.20.58.1480;3.30.230.10;2.30.130.40;3.40.50.300;
Peptidase S16 family
null
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000255|HAMAP-Rule:MF_03121, ECO:0000269|PubMed:19329564}.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; Evidence={ECO:0000255|HAMAP-Rule:MF_03121};
null
null
null
null
FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix (By similarity). Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import. {ECO:0000255|HAMAP-...
Arabidopsis thaliana (Mouse-ear cress)
O64961
TPS9_SOLLC
MAASSADKCRPLANFHPSVWGYHFLSYTHEITNQEKVEVDEYKETIRKMLVETCDNSTQKLVLIDAMQRLGVAYHFDNEIETSIQNIFDASSKQNDNDNNLYVVSLRFRLVRQQGHYMSSDVFKQFTNQDGKFKETLTNDVQGLLSLYEASHLRVRNEEILEEALTFTTTHLESIVSNLSNNNNSLKVEVGEALTQPIRMTLPRMGARKYISIYENNDAHHHLLLKFAKLDFNMLQKFHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVLNLTSIIDDTFDAYATFDELVTFNDAIQ...
4.2.3.-; 4.2.3.113; 4.2.3.15; 4.2.3.60
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:9482865}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:9482865}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000305|PubMed:9482865};
diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114]
cytoplasm [GO:0005737]
germacrene C synthase activity [GO:0102904]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; terpene synthase activity [GO:0010333]
PF01397;PF03936;
1.10.600.10;1.50.10.130;
Terpene synthase family, Tpsa subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + germacrene C; Xref=Rhea:RHEA:28302, ChEBI:CHEBI:33019, ChEBI:CHEBI:61478, ChEBI:CHEBI:175763; EC=4.2.3.60; Evidence={ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:9482865}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28303; Evidence={E...
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:9482865}.
null
null
FUNCTION: Involved in the biosynthesis of germacrene C, one of the most abundant sesquiterpene in the leaf oil of tomato (PubMed:11090225). Produces mainly germacrene C, but also smaller amounts of germacrene A, B and D when used with farnesyl diphosphate (FPP) as substrate; able to use both (2E,6E)-farnesyl diphosphat...
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
O64973
RPS5_ARATH
MGGCFSVSLPCDQVVSQFSQLLCVRGSYIHNLSKNLASLQKAMRMLKARQYDVIRRLETEEFTGRQQRLSQVQVWLTSVLIIQNQFNDLLRSNEVELQRLCLCGFCSKDLKLSYRYGKRVIMMLKEVESLSSQGFFDVVSEATPFADVDEIPFQPTIVGQEIMLEKAWNRLMEDGSGILGLYGMGGVGKTTLLTKINNKFSKIDDRFDVVIWVVVSRSSTVRKIQRDIAEKVGLGGMEWSEKNDNQIAVDIHNVLRRRKFVLLLDDIWEKVNLKAVGVPYPSKDNGCKVAFTTRSRDVCGRMGVDDPMEVSCLQPEESWD...
null
null
cell death [GO:0008219]; defense response [GO:0006952]; defense response to bacterium [GO:0042742]; plant-type hypersensitive response [GO:0009626]
plasma membrane [GO:0005886]
ADP binding [GO:0043531]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; nucleotide binding [GO:0000166]; signaling receptor activity [GO:0038023]
PF13855;PF00931;
1.10.8.430;3.40.50.300;3.80.10.10;1.10.10.10;
Disease resistance NB-LRR family
null
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor {ECO:0000269|PubMed:22046960, ECO:0000269|PubMed:22331412}.
null
null
null
null
null
FUNCTION: Disease resistance (R) protein that specifically recognizes the avrPphB type III effector avirulence protein from Pseudomonas syringae. Also confers resistance against Hyaloperonospora parasitica (downy mildew). Resistance proteins guard the plant against pathogens that contain an appropriate avirulence prote...
Arabidopsis thaliana (Mouse-ear cress)
O64989
C90B1_ARATH
MFETEHHTLLPLLLLPSLLSLLLFLILLKRRNRKTRFNLPPGKSGWPFLGETIGYLKPYTATTLGDFMQQHVSKYGKIYRSNLFGEPTIVSADAGLNRFILQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRDMRSISLNFLSHARLRTILLKDVERHTLFVLDSWQQNSIFSAQDEAKKFTFNLMAKHIMSMDPGEEETEQLKKEYVTFMKGVVSAPLNLPGTAYHKALQSRATILKFIERKMEERKLDIKEEDQEEEEVKTEDEAEMSKSDHVRKQRTDDDLLGWVLKHSNLSTEQILDLILSLLFAGHETSSVAI...
1.14.14.178
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798};
brassinosteroid biosynthetic process [GO:0016132]; jasmonic acid mediated signaling pathway [GO:0009867]; leaf development [GO:0048366]; leaf shaping [GO:0010358]; response to brassinosteroid [GO:0009741]; response to jasmonic acid [GO:0009753]; sterol metabolic process [GO:0016125]; unidimensional cell growth [GO:0009...
endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]
fatty acid alpha-hydroxylase activity [GO:0080132]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; steroid 22-alpha hydroxylase activity [GO:0010012]
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=a C27-steroid + O2 + reduced [NADPH--hemoprotein reductase] = a (22S)-22-hydroxy C27-steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70059, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.35 uM for campesterol (at pH 7.25 and 30 degrees Celsius) {ECO:0000269|PubMed:16460510}; KM=3 uM for campestanol (at pH 7.25 and 30 degrees Celsius) {ECO:0000269|PubMed:16460510}; Note=kcat is 1.8 min(-1) for campesterol (at pH 7.25 and 30 degrees Celsius) (PubMe...
PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis. {ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746}.
null
null
FUNCTION: Catalyzes the C22-alpha-hydroxylation step in brassinosteroids biosynthesis (PubMed:16460510, PubMed:9490746). Converts campesterol (CR) to (22S)-22-hydroxycampesterol (22-OHCR, 22-hydroxyCR), campestanol (CN) to 6-deoxycathasterone (6-deoxoCT), and 6-oxocampestanol (6-oxoCN) to cathasterone (CT) (PubMed:1646...
Arabidopsis thaliana (Mouse-ear cress)
O65020
ETO1_ARATH
MRSLKLAEGCKGTQVYALNPSAPTPPPPPGNSSTGGGGGGGSGGGTGGVGDKLLQHLSDHLRVNSVRSKSSRTYPPPTQPNAVVSPEFLLPCGLPVTDLLEPQIDPCLKFVDLVEKMAQVYRRIENCSQFEKSGAYLEQCAIFRGISDPKLFRRSLRSSRQHAVDVHAKVVLASWLRFERREDELIGTTSMDCCGRNLECPKATLVSGYDPESVYDPCVCSGASRSEMMNEDECSTSQEVDYDMSFCIGDEEVRCVRYKIASLSRPFKAMLYGGFREMKRATINFTQNGISVEGMRAAEIFSRTNRLDNFPPNVVLELLK...
null
null
ethylene-activated signaling pathway [GO:0009873]; negative regulation of ethylene-activated signaling pathway [GO:0010105]; protein ubiquitination [GO:0016567]
null
null
PF13181;
1.25.40.10;
ETO1 family
null
null
null
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: Essential regulator of the ethylene pathway, which acts by regulating the stability of 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes. May act as a substrate-specific adapter that connects ACS enzymes, such as ACS5, to ubiquitin ligase complexes, leading to proteasomal degradation of ACS enzymes. {E...
Arabidopsis thaliana (Mouse-ear cress)
O65039
CYSEP_RICCO
MQKFILLALSLALVLAITESFDFHEKELESEESLWGLYERWRSHHTVSRSLHEKQKRFNVFKHNAMHVHNANKMDKPYKLKLNKFADMTNHEFRNTYSGSKVKHHRMFRGGPRGNGTFMYEKVDTVPASVDWRKKGAVTSVKDQGQCGSCWAFSTIVAVEGINQIKTNKLVSLSEQELVDCDTDQNQGCNGGLMDYAFEFIKQRGGITTEANYPYEAYDGTCDVSKENAPAVSIDGHENVPENDENALLKAVANQPVSVAIDAGGSDFQFYSEGVFTGSCGTELDHGVAIVGYGTTIDGTKYWTVKNSWGPEWGEKGYIR...
3.4.22.-
null
proteolysis involved in protein catabolic process [GO:0051603]
cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]; lysosome [GO:0005764]
cysteine-type endopeptidase activity [GO:0004197]
PF08246;PF00112;
3.90.70.10;
Peptidase C1 family
PTM: The potential N-glycosylation site at Asn-115 is not glycosylated.
SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:11296243}. Note=The pro-endopeptidase accumulates in the ricinosomes.
null
null
null
null
null
FUNCTION: Involved in programmed cell death. Shows a pronounced preference for hydrophobic residues in the P2 position and no obvious preference in the P1 position of the cleavage site. Accepts proline at the P1 and P1' positions.
Ricinus communis (Castor bean)
O65041
UBA3_ARATH
MADLDVPPQVPQSKTRDLDKLLLRHGNLVDPGFVPGPGLRDDIRDYVRILVIGAGGLGCELLKDLALSGFRNLEVIDMDRIEVTNLNRQFLFRIEDVGKPKAEVAAKRVMERVSGVEIVPHFSRIEDKEIEFYNDFNIIALGLDSIEARKYINGVACGFLEYNEDDTPKRETIKPMVDGGTEGFKGHARVILPGVTPCFECTIYLFPPQVKFPLCTLAETPRNAAHCIEYAHLIQWETVHRGKTFDPDEPEHMKWVYDEAIRRAELFGIPGVTYSLTQGVVKNIIPAIASTNAIISAACALETLKIVSACSKTLVNYLTY...
6.2.1.64
null
protein neddylation [GO:0045116]
cytosol [GO:0005829]; nucleus [GO:0005634]
ATP binding [GO:0005524]; NEDD8 activating enzyme activity [GO:0019781]; protein heterodimerization activity [GO:0046982]
PF08825;PF00899;
3.40.50.720;1.10.10.520;3.10.290.20;
Ubiquitin-activating E1 family, UBA3 subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine.; EC=6.2.1.64;
null
PATHWAY: Protein modification; protein neddylation.
null
null
FUNCTION: Catalytic subunit of the dimeric ECR1-AXR1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-ECR1 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cys...
Arabidopsis thaliana (Mouse-ear cress)
O65201
ACOX2_ARATH
MESRREKNPMTEEESDGLIAARRIQRLSLHLSPSLTPSPSLPLVQTETCSARSKKLDVNGEALSLYMRGKHIDIQEKIFDFFNSRPDLQTPIEISKDDHRELCMNQLIGLVREAGVRPFRYVADDPEKYFAIMEAVGSVDMSLGIKMGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYTGCFAMTELHHGSNVQGLQTTATFDPLKDEFVIDTPNDGAIKWWIGNAAVHGKFATVFARLILPTHDSKGVSDMGVHAFIVPIRDMKTHQTLPGVEIQDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDVSRDGTYTS...
1.3.3.6
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O65202}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O65202};
fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; lipid homeostasis [GO:0055088]; long-chain fatty acid metabolic process [GO:0001676]
peroxisome [GO:0005777]
acyl-CoA oxidase activity [GO:0003997]; FAD binding [GO:0071949]; fatty acid binding [GO:0005504]
PF01756;PF00441;PF02770;
2.40.110.10;1.20.140.10;
Acyl-CoA oxidase family
null
SUBCELLULAR LOCATION: Peroxisome {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6; Evidence={ECO:0000269|PubMed:10571860}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960; Evidence={ECO:0000269|Pu...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.4 uM for C18:1-CoA {ECO:0000269|PubMed:10571860};
null
null
null
FUNCTION: Catalyzes the desaturation of long-chain acyl-CoAs to 2-trans-enoyl-CoAs. Active on substrates longer than C14 and mostly with C18-CoA. Activity on long-chain mono-unsaturated substrates is double than with the corresponding saturated substrates. {ECO:0000269|PubMed:10571860}.
Arabidopsis thaliana (Mouse-ear cress)
O65202
ACOX1_ARATH
MEGIDHLADERNKAEFDVEDMKIVWAGSRHAFEVSDRIARLVASDPVFEKSNRARLSRKELFKSTLRKCAHAFKRIIELRLNEEEAGRLRHFIDQPAYVDLHWGMFVPAIKGQGTEEQQKKWLSLANKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHTPTQTASKWWPGGLGKVSTHAVVYARLITNGKDYGIHGFIVQLRSLEDHSPLPNITVGDIGTKMGNGAYNSMDNGFLMFDHVRIPRDQMLMRLSKVTREGEYVPSDVPKQLVYGTMVYVRQTIVADASNALSRAVCIATRYSAVRRQFGAHNGGI...
1.3.3.6
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15581893}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:15581893};
ascaroside biosynthetic process [GO:1904070]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; jasmonic acid biosynthetic process [GO:0009695]; lipid homeostasis [GO:0055088]; long-chain fatty acid metabolic process [GO:0001676]; response to fungus [GO:0009620]; res...
cytosol [GO:0005829]; peroxisome [GO:0005777]; plasmodesma [GO:0009506]
acyl-CoA oxidase activity [GO:0003997]; FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; palmitoyl-CoA oxidase activity [GO:0016401]
PF01756;PF02770;PF14749;
1.10.540.10;2.40.110.10;1.20.140.10;
Acyl-CoA oxidase family
null
SUBCELLULAR LOCATION: Peroxisome {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6; Evidence={ECO:0000269|PubMed:10571860}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960; Evidence={ECO:0000269|Pu...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.3 uM for C14-CoA;
null
null
null
FUNCTION: Catalyzes the desaturation of both long- and medium-chain acyl-CoAs to 2-trans-enoyl-CoAs. Most active with C14-CoA. Activity on long-chain mono-unsaturated substrates is 40% higher than with the corresponding saturated substrates. Seems to be an important factor in the general metabolism of root tips. May be...
Arabidopsis thaliana (Mouse-ear cress)
O65258
BAM2_ARATH
MAIRLNHSVIPVSVKLGAPTRVSARSSLPFSVGDWRGVSTFSGARPLVLAKVKLRAESTEEDRVPIDDDDDSTDQLVDEEIVHFEERDFAGTACVPVYVMLPLGVIDMNSEVVEPEELLDQLRTLKSVNVDGVMVDCWWGIVESHTPQVYNWSGYKKLFQMIRELGLKIQVVMSFHECGGNVGDDVHIQIPEWVREIGQSNPDIYFTDSAGRRNTECLTWGIDKQRVLRGRTALEVYFDYMRSFRVEFDEFFEEKIIPEIEVGLGPCGELRYPSYPAQFGWKYPGIGEFQCYDKYLMNSLKEAAEVRGHSFWGRGPDNTE...
3.2.1.2
null
polysaccharide catabolic process [GO:0000272]
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]
amylopectin maltohydrolase activity [GO:0102229]; beta-amylase activity [GO:0016161]
PF01373;
3.20.20.80;
Glycosyl hydrolase 14 family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:18431481}.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.; EC=3.2.1.2;
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:19664588};
null
FUNCTION: Low beta-amylase activity. Interacts poorly with starch or other alpha-1,4-glucan. {ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:19664588}.
Arabidopsis thaliana (Mouse-ear cress)
O65272
KEA2_ARATH
MDFASSVQRQSMFHGGADFASYCLPNRMISAKLCPKGLGGTRFWDPMIDSKVRSAIRSKRNVSYRSSLTLNADFNGRFYGHLLPAKPQNVPLGFRLLCQSSDSVGDLVGNDRNLEFAEGSDDREVTFSKEEKDTREQDSAPSLEELRDLLNKATKELEVASLNSTMFEEKAQRISEVAIALKDEAASAWNDVNQTLNVVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAEGYNTSEESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVANIMVL...
null
null
abscisic acid-activated signaling pathway [GO:0009738]; calcium-mediated signaling [GO:0019722]; plastid gene expression [GO:0140899]; plastid rRNA transcription [GO:0042794]; potassium ion transport [GO:0006813]; primary root development [GO:0080022]; reactive nitrogen species metabolic process [GO:2001057]; regulatio...
chloroplast [GO:0009507]; chloroplast inner membrane [GO:0009706]; membrane [GO:0016020]
potassium ion transmembrane transporter activity [GO:0015079]; potassium:proton antiporter activity [GO:0015386]; proton transmembrane transporter activity [GO:0015078]
PF00999;PF02254;
1.20.1530.20;3.40.50.720;
Monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family, KEA (TC 2.A.37.1) subfamily
PTM: Acetylated at Lys-170 by the stromal acetyltransferase enzyme NSI. {ECO:0000269|PubMed:29967049, ECO:0000269|PubMed:31865509}.
SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:22551943, ECO:0000269|PubMed:24794527, ECO:0000269|PubMed:33485149}; Multi-pass membrane protein {ECO:0000255}. Plastid inner membrane {ECO:0000269|PubMed:33485149}; Multi-pass membrane protein {ECO:0000255}. Note...
CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:24278440, ECO:0000269|PubMed:31296940, ECO:0000269|PubMed:33111995};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.8. {ECO:0000269|PubMed:24278440};
null
FUNCTION: Electroneutral K(+)/H(+) efflux antiporter modulating monovalent cation and pH homeostasis in plastids, especially during plastid division and thylakoid membrane formation (PubMed:22551943, PubMed:24278440, PubMed:27443603, PubMed:31296940, PubMed:33111995). Transports K(+) and Cs(+) preferentially relative t...
Arabidopsis thaliana (Mouse-ear cress)
O65282
CH20_ARATH
MAATQLTASPVTMSARSLASLDGLRASSVKFSSLKPGTLRQSQFRRLVVKAASVVAPKYTSIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGKNKIDITVPTGAQIIYSKYAGTEVEFNDVKHLILKEDDIVGILETEDIKDLKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKGKDGSNYIALRASDVMAILS
null
null
chaperone cofactor-dependent protein refolding [GO:0051085]; negative regulation of abscisic acid-activated signaling pathway [GO:0009788]; positive regulation of superoxide dismutase activity [GO:1901671]; protein heterotetramerization [GO:0051290]; response to cold [GO:0009409]
apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; chloroplast thylakoid membrane [GO:0009535]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; plastid [GO:0009536]; thylakoid [GO:0009579]
ATP binding [GO:0005524]; copper ion binding [GO:0005507]; protein folding chaperone [GO:0044183]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
PF00166;
2.30.33.40;
GroES chaperonin family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:10205903}.
null
null
null
null
null
FUNCTION: Seems to function only as a co-chaperone, along with CPN60, and in certain cases is essential for the discharge of biologically active proteins from CPN60 (PubMed:17178727, PubMed:23057508). Required to activate the iron superoxide dismutases (FeSOD) (PubMed:23057508). {ECO:0000269|PubMed:17178727, ECO:000026...
Arabidopsis thaliana (Mouse-ear cress)
O65312
MEDEA_ARATH
MEKENHEDDGEGLPPELNQIKEQIEKERFLHIKRKFELRYIPSVATHASHHQSFDLNQPAAEDDNGGDNKSLLSRMQNPLRHFSASSDYNSYEDQGYVLDEDQDYALEEDVPLFLDEDVPLLPSVKLPIVEKLPRSITWVFTKSSQLMAESDSVIGKRQIYYLNGEALELSSEEDEEDEEEDEEEIKKEKCEFSEDVDRFIWTVGQDYGLDDLVVRRALAKYLEVDVSDILERYNELKLKNDGTAGEASDLTSKTITTAFQDFADRRHCRRCMIFDCHMHEKYEPESRSSEDKSSLFEDEDRQPCSEHCYLKVRSVTEAD...
2.1.1.356
null
heterochromatin formation [GO:0031507]; methylation [GO:0032259]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of endosperm development [GO:2000014]; response to absence of light [GO:0009646]; seed morphogenesis [GO:0048317]
nucleus [GO:0005634]; PcG protein complex [GO:0031519]
chromatin binding [GO:0003682]; histone H3K27 trimethyltransferase activity [GO:0140951]; sequence-specific DNA binding [GO:0043565]
PF18264;PF00856;
2.170.270.10;
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, EZ subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11114524}. Note=Excluded from the nucleolus.
CATALYTIC ACTIVITY: Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEB...
null
null
null
null
FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of some PcG multiprotein complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target genes. Required to prevent the proliferation of the central cell of the female gametophyte by repressing target genes before f...
Arabidopsis thaliana (Mouse-ear cress)
O65351
SBT17_ARATH
MSSSFLSSTAFFLLLCLGFCHVSSSSSDQGTYIVHMAKSQMPSSFDLHSNWYDSSLRSISDSAELLYTYENAIHGFSTRLTQEEADSLMTQPGVISVLPEHRYELHTTRTPLFLGLDEHTADLFPEAGSYSDVVVGVLDTGVWPESKSYSDEGFGPIPSSWKGGCEAGTNFTASLCNRKLIGARFFARGYESTMGPIDESKESRSPRDDDGHGTHTSSTAAGSVVEGASLLGYASGTARGMAPRARVAVYKVCWLGGCFSSDILAAIDKAIADNVNVLSMSLGGGMSDYYRDGVAIGAFAAMERGILVSCSAGNAGPSSS...
3.4.21.-
null
mucilage extrusion from seed coat [GO:0080001]; mucilage metabolic process involved in seed coat development [GO:0048359]; proteolysis [GO:0006508]; seed coat development [GO:0010214]
apoplast [GO:0048046]; extracellular region [GO:0005576]; secretory vesicle [GO:0099503]
serine-type endopeptidase activity [GO:0004252]
PF17766;PF05922;PF02225;PF00082;
2.60.40.2310;3.50.30.30;3.30.70.80;3.40.50.200;
Peptidase S8 family
null
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:12413398, ECO:0000269|PubMed:9188482}. Note=Intracellular spaces and cell wall.
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:12413398};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius. Thermostable. {ECO:0000269|PubMed:12413398};
FUNCTION: Serine protease. Has a substrate preference for the hydrophobic residues Phe and Ala and the basic residue Asp in the P1 position, and for Asp, Leu or Ala in the P1' position (PubMed:12413398). Essential for mucilage release from seed coats. Triggers the accumulation and/or activation of cell wall modifying e...
Arabidopsis thaliana (Mouse-ear cress)
O65355
GGH2_ARATH
MWSYVWLPLVALSLFKDSIIMAKAATILLPSQTGFDISRSPVCSAPDPNLNYRPVIGILSHPGDGASGRLSNATDASSIAASYVKLAESGGARVIPLIFNEPEEILFQKLELVNGVILTGGWAKEGLYFEIVKKIFNKVLERNDAGEHFPIYAICLGFELLTMIISQNRDIFEKMDARNSASSLQFVENVNIQGTIFQRFPPELLKKLGTDCLVMQNHRFGISPQSFEGNIALSNFFKIVTTCVDDNGKVYVSTVQSTKYPVTGFQWHPEKNAFEWGSSKIPHSEDAIQVTQHAANHLVSEARKSLNRPESKKVLSNLIY...
3.4.19.9
null
tetrahydrofolylpolyglutamate metabolic process [GO:0046900]
extracellular space [GO:0005615]; plant-type cell wall [GO:0009505]; plant-type vacuole [GO:0000325]; vacuole [GO:0005773]
gamma-glutamyl-peptidase activity [GO:0034722]; omega peptidase activity [GO:0008242]
PF07722;
3.40.50.880;
Peptidase C26 family
null
SUBCELLULAR LOCATION: Vacuole {ECO:0000305|PubMed:21070406}. Secreted, extracellular space {ECO:0000250}. Secreted, cell wall {ECO:0000250}. Note=Extracellular or cell-wall bound.
CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate; Xref=Rhea:RHEA:56784, Rhea:RHEA-COMP:14738, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:141005; EC=3.4.19.9;
null
null
null
null
FUNCTION: Cleaves the polyglutamate sidechains of folate polyglutamates in the vacuole. Is important for polyglutamyl tail length determination before vacuolar exit. Plays a role on folate stability and intracellular folate content. Has endopeptidase activity against 4-amino-10-methylpteroyl penta-, tetra-, tri- and di...
Arabidopsis thaliana (Mouse-ear cress)
O65359
SYP41_ARATH
MATRNRTLLFRKYRNSLRSVRAPLSSSSLTGTRSGGVGPVIEMASTSLLNPNRSYAPISTEDPGTSSKGAITVGLPPAWVDVSEEISVNIQRARTKMAELGKAHAKALMPSFGDGKEDQHNIESLTQEITFLLKKSEKQLQRLSASGPSEDSNVRKNVQRSLATDLQLLSMELRKKQSTYLKRLRQQKEDGMDLEMNLSRNRYRPEEDDFGDMLNEHQMSKIKKSEEVSVEREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKAERTQRHGGMVKCASVLVILCFIMLLLLILKEI...
null
null
chloroplast organization [GO:0009658]; defense response to fungus [GO:0050832]; Golgi organization [GO:0007030]; Golgi to plasma membrane protein transport [GO:0043001]; Golgi to vacuole transport [GO:0006896]; intracellular protein transport [GO:0006886]; salicylic acid mediated signaling pathway [GO:0009863]; trans-G...
SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]
SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]
PF05739;
1.20.58.70;
Syntaxin family
null
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:10888666, ECO:0000269|PubMed:11739776, ECO:0000269|PubMed:15342965, ECO:0000269|PubMed:15743878, ECO:0000269|PubMed:22307646}; Single-pass type IV membrane protein {ECO:0000255}. Note=SYP41 is found in a different region of the TGN ...
null
null
null
null
null
FUNCTION: Contributes to the regulation of secretory and vacuolar transport pathways in the post-Golgi network, and to the maintenance of the Golgi apparatus and trans-Golgi network (TGN) morphologies (PubMed:22307646). Together with VTI12, required for membrane fusion (PubMed:15919093). Vesicle trafficking protein tha...
Arabidopsis thaliana (Mouse-ear cress)
O65375
LRX1_ARATH
MLFPPLRSLFLFTLLLSSVCFLQIKADHDDESDLGSDIKVDKRLKFENPKLRQAYIALQSWKKAIFSDPFNFTANWNGSDVCSYNGIYCAPSPSYPKTRVVAGIDLNHADMAGYLASELGLLSDLALFHINSNRFCGEVPLTFNRMKLLYELDLSNNRFVGKFPKVVLSLPSLKFLDLRYNEFEGKIPSKLFDRELDAIFLNHNRFRFGIPKNMGNSPVSALVLADNNLGGCIPGSIGQMGKTLNELILSNDNLTGCLPPQIGNLKKVTVFDITSNRLQGPLPSSVGNMKSLEELHVANNAFTGVIPPSICQLSNLENFT...
null
null
cell wall organization [GO:0071555]; trichoblast differentiation [GO:0010054]; unidimensional cell growth [GO:0009826]
extracellular region [GO:0005576]; plant-type cell wall [GO:0009505]; plasmodesma [GO:0009506]
structural constituent of cell wall [GO:0005199]
PF00560;PF08263;
3.80.10.10;
null
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat. {ECO:0000250}.; PTM: O-glycosylated on hydroxyprolines. {ECO:0000250}.
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:11331608}. Note=Specifically localized in the wall of the root hair proper.
null
null
null
null
null
FUNCTION: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization. Together with LRX2, component of the extracellular mechanism regulating root hair morphogenesis and elongation. {ECO:0000269|PubMed:11331608, ECO:0000269|PubMed:12834403}.
Arabidopsis thaliana (Mouse-ear cress)
O65390
APA1_ARATH
MKIYSRTVAVSLIVSFLLCFSAFAERNDGTFRVGLKKLKLDSKNRLAARVESKQEKPLRAYRLGDSGDADVVVLKNYLDAQYYGEIAIGTPPQKFTVVFDTGSSNLWVPSSKCYFSLACLLHPKYKSSRSSTYEKNGKAAAIHYGTGAIAGFFSNDAVTVGDLVVKDQEFIEATKEPGITFVVAKFDGILGLGFQEISVGKAAPVWYNMLKQGLIKEPVFSFWLNRNADEEEGGELVFGGVDPNHFKGKHTYVPVTQKGYWQFDMGDVLIGGAPTGFCESGCSAIADSGTSLLAGPTTIITMINHAIGAAGVVSQQCKTV...
3.4.23.-
null
lipid metabolic process [GO:0006629]; proteolysis [GO:0006508]
extracellular region [GO:0005576]; plant-type vacuole [GO:0000325]; plasmodesma [GO:0009506]; secretory vesicle [GO:0099503]; vacuole [GO:0005773]
aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175]
PF00026;PF05184;PF03489;
2.40.70.10;1.10.225.10;
Peptidase A1 family
null
SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:17012602}. Note=Located in protein storage vacuoles (PSV) of the embryo.
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0-6.0 with insulin B chain as substrate and at 37 degrees Celsius. {ECO:0000269|PubMed:20079503};
null
FUNCTION: Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles (By similarity). Possesses aspartic protease activity in vitro. {ECO:0000250, ECO:0000269|PubMed:20079503}.
Arabidopsis thaliana (Mouse-ear cress)
O65396
GCST_ARATH
MRGGSLWQLGQSITRRLAQSDKKVVSRRYFASEADLKKTALYDFHVAHGGKMVPFAGWSMPIQYKDSIMDSTVNCRENGSLFDVAHMCGLSLKGKDCVPFLETLVVADVAGLAPGTGSLTVFTNEKGGAIDDSVITKVTDEHIYLVVNAGCRDKDLAHIEEHMKAFKSKGGDVSWHIHDERSLLALQGPLAAPVLQHLTKEDLSKLYFGNFQILDINGSTCFLTRTGYTGEDGFEISVPDEHAVDLAKAILEKSEGKVRLTGLGARDSLRLEAGLCLYGNDMEQHISPVEAGLTWAIGKRRRAEGGFLGADVILQQLKDG...
2.1.2.10
null
glycine catabolic process [GO:0006546]
apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; chloroplast thylakoid [GO:0009534]; cytosolic ribosome [GO:0022626]; extracellular region [GO:0005576]; mitochondrion [GO:0005739]
aminomethyltransferase activity [GO:0004047]; mRNA binding [GO:0003729]; transaminase activity [GO:0008483]
PF01571;PF08669;
2.40.30.110;3.30.70.1400;4.10.1250.10;
GcvT family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:2...
null
null
null
null
FUNCTION: The glycine decarboxylase (GDC) or glycine cleavage system catalyzes the degradation of glycine. {ECO:0000250}.
Arabidopsis thaliana (Mouse-ear cress)
O65398
GLX1_ARATH
MAEASDLLEWPKKDNRRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETSNFVVELTYNYGVSSYDIGTGFGHFAISTQDVSKLVENVRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFELIQRGPTPEPFCQVMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEEYESIVLELTYNYDVTEYTKGNAYAQIAIGTDDVYKSGEVIKIVNQELGGKITREAGPLPGLGTKIVSFLDPDGWKTVLVDNKDFLKELE
4.4.1.5
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9CPU0}; Note=Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits. {ECO:0000250|UniProtKB:Q9CPU0};
methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]
chloroplast envelope [GO:0009941]; cytosol [GO:0005829]; extracellular region [GO:0005576]; peroxisome [GO:0005777]; plant-type vacuole [GO:0000325]; secretory vesicle [GO:0099503]
dioxygenase activity [GO:0051213]; lactoylglutathione lyase activity [GO:0004462]; metal ion binding [GO:0046872]
PF00903;
3.10.180.10;
Glyoxalase I family
PTM: Phosphorylated by SnRK2.8. {ECO:0000269|PubMed:17404219}.
null
CATALYTIC ACTIVITY: Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal; Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=4.4.1.5; Evidence={ECO:0000250|UniProtKB:Q04760};
null
PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2. {ECO:0000250|UniProtKB:Q04760}.
null
null
FUNCTION: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. {ECO:0000250|UniProtKB:Q04760}.
Arabidopsis thaliana (Mouse-ear cress)
O65440
BAME3_ARATH
MADKIFTFFLILSSISPLLCSSLISPLNLSLIRQANVLISLKQSFDSYDPSLDSWNIPNFNSLCSWTGVSCDNLNQSITRLDLSNLNISGTISPEISRLSPSLVFLDISSNSFSGELPKEIYELSGLEVLNISSNVFEGELETRGFSQMTQLVTLDAYDNSFNGSLPLSLTTLTRLEHLDLGGNYFDGEIPRSYGSFLSLKFLSLSGNDLRGRIPNELANITTLVQLYLGYYNDYRGGIPADFGRLINLVHLDLANCSLKGSIPAELGNLKNLEVLFLQTNELTGSVPRELGNMTSLKTLDLSNNFLEGEIPLELSGLQK...
2.7.11.1
null
cell differentiation [GO:0030154]; floral organ development [GO:0048437]; maintenance of root meristem identity [GO:0010078]; phloem development [GO:0010088]; phosphorylation [GO:0016310]; regulation of cell differentiation [GO:0045595]; regulation of meristem growth [GO:0010075]
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; peptide binding [GO:0042277]; peptide receptor activity [GO:0001653]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00560;PF08263;PF00069;
3.80.10.10;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28607033}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:28607033}; Single-pass type I membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159}; ...
null
null
null
null
FUNCTION: Necessary for male gametophyte development, as well as ovule specification and function (PubMed:16367950). Required for the development of high-ordered vascular strands within the leaf and a correlated control of leaf shape, size and symmetry (PubMed:16367950). LRR-rich receptor-like kinase (LRR-RLK) involved...
Arabidopsis thaliana (Mouse-ear cress)
O65493
XCP1_ARATH
MAFSAPSLSKFSLLVAISASALLCCAFARDFSIVGYTPEHLTNTDKLLELFESWMSEHSKAYKSVEEKVHRFEVFRENLMHIDQRNNEINSYWLGLNEFADLTHEEFKGRYLGLAKPQFSRKRQPSANFRYRDITDLPKSVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDTTFNSGCNGGLMDYAFQYIISTGGLHKEDDYPYLMEEGICQEQKEDVERVTISGYEDVPENDDESLVKALAHQPVSVAIEASGRDFQFYKGGVFNGKCGTDLDHGVAAVGYGSSKGSDYVIVKNSWG...
3.4.22.-
null
programmed cell death involved in cell development [GO:0010623]; proteolysis involved in protein catabolic process [GO:0051603]
extracellular space [GO:0005615]; lysosome [GO:0005764]; nucleus [GO:0005634]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]
cysteine-type endopeptidase activity [GO:0004197]
PF08246;PF00112;
3.90.70.10;
Peptidase C1 family
PTM: Autocleaves.
SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:11788755}. Cell membrane {ECO:0000269|PubMed:11788755}. Note=Predominantly vacuolar. May be associated to plasma membrane.
null
null
null
null
null
FUNCTION: Cysteine protease involved in xylem tracheary element (TE) autolysis during xylogenesis in roots. Participates in micro autolysis within the intact central vacuole before mega autolysis is initiated by tonoplast implosion. {ECO:0000269|PubMed:18573193}.
Arabidopsis thaliana (Mouse-ear cress)
O65502
HC244_ARATH
MASLRLPAQLVTRGNLIHHNSSSSSSGRLSWRRSLTPENTIPLFPSSSSSSLNRERSIVVPVTCSAAAVNLAPGTPVRPTSILVVGATGTLGRQIVRRALDEGYDVRCLVRPRPAPADFLRDWGATVVNADLSKPETIPATLVGIHTVIDCATGRPEEPIKTVDWEGKVALIQCAKAMGIQKYVFYSIHNCDKHPEVPLMEIKYCTEKFLQESGLNHITIRLCGFMQGLIGQYAVPILEEKSVWGTDAPTRVAYMDTQDIARLTLIALRNEKINGKLLTFAGPRAWTTQEVITLCERLAGQDANVTTVPVSVLRVTRQLT...
null
null
photosystem II assembly [GO:0010207]
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; photosystem II [GO:0009523]; plasma membrane [GO:0005886]; thylakoid membrane [GO:0042651]
translation initiation factor activity [GO:0003743]
PF05368;
3.40.50.720;
NmrA-type oxidoreductase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:23027666}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:23027666}; Peripheral membrane protein {ECO:0000269|PubMed:23027666}; Stromal side {ECO:0000269|PubMed:23027666}. Note=Predominantly present at thylakoid membranes. {ECO:0000269|P...
null
null
null
null
null
FUNCTION: Auxiliary factor required, together with HCF173, for the biogenesis of photosystem II (PSII), especially for the synthesis of the reaction center proteins (e.g. D1), via the regulation of the corresponding mRNA (e.g. psbA) translation initiation (ribosomal loading) and stabilization (PubMed:29930106). Forms a...
Arabidopsis thaliana (Mouse-ear cress)
O65508
NAC76_ARATH
MESVDQSCSVPPGFRFHPTDEELVGYYLRKKVASQKIDLDVIRDIDLYRIEPWDLQESCRIGYEERNEWYFFSHKDKKYPTGTRTNRATMAGFWKATGRDKAVYDKSKLIGMRKTLVFYKGRAPNGQKTDWIMHEYRLESDENAPPQEEGWVVCRAFKKKPMTGQAKNTETWSSSYFYDELPSGVRSVTEPLNYVSKQKQNVFAQDLMFKQELEGSDIGLNFIHCDQFIQLPQLESPSLPLTKRPVSLTSITSLEKNKNIYKRHLIEEDVSFNALISSGNKDKKKKKTSVMTTDWRALDKFVASQLMSQEDGVSGFGGHH...
null
null
cell wall organization [GO:0071555]; positive regulation of secondary cell wall biogenesis [GO:1901348]; regulation of DNA-templated transcription [GO:0006355]; xylem vessel member cell differentiation [GO:0048759]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
PF02365;
2.170.150.80;
Plant vascular related NAC-domain protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9C8W9, ECO:0000255|PROSITE-ProRule:PRU00353}.
null
null
null
null
null
FUNCTION: Transcription activator that binds to the secondary wall NAC binding element (SNBE), 5'-(T/A)NN(C/T)(T/C/G)TNNNNNNNA(A/C)GN(A/C/T)(A/T)-3', in the promoter of target genes (By similarity). Involved in xylem formation by promoting the expression of secondary wall-associated transcription factors and of genes i...
Arabidopsis thaliana (Mouse-ear cress)
O65517
SRS2_ARATH
MAGIFSLGGNNNNNGDEEEENQQQQKTNWVWYRSNANTNNINPSSSQQVWQIPPEQMLMHHHSHPQQQSLDLYPGHQIDVSDLATSSRSITISCRDCGNQAKKDCTHMRCRTCCKSRGFDCSTHVRSTWIPVARRRERQQQLHMSTSGGGGGSGSGGAGGGGSSIPKRHRDPTLPGTSSSSRLPSHSAGLEMGEASFPGEVSSDALFRCVKMSGVDDGGDGQYAYQTTVNIGGHLFKGILYDQGPESSYMSGGSGGSDHQSSSAGGGGGGHPFNPPVVTDGGGGVSSAMFVDPNSGGYYSSNMTTSVFMPPGTQFYQNPP...
null
null
anther development [GO:0048653]; auxin biosynthetic process [GO:0009851]; auxin-activated signaling pathway [GO:0009734]; pollen development [GO:0009555]; positive regulation of DNA-templated transcription [GO:0045893]
nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]
PF05142;
null
SHI protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Transcription activator that binds DNA on 5'-ACTCTAC-3' and promotes auxin homeostasis-regulating gene expression (e.g. YUC genes), as well as genes affecting stamen development, cell expansion and timing of flowering. Synergistically with other SHI-related proteins, regulates gynoecium, stamen and leaf devel...
Arabidopsis thaliana (Mouse-ear cress)
O65554
CIPK6_ARATH
MVGAKPVENGSDGGSSTGLLHGRYELGRLLGHGTFAKVYHARNIQTGKSVAMKVVGKEKVVKVGMVDQIKREISVMRMVKHPNIVELHEVMASKSKIYFAMELVRGGELFAKVAKGRLREDVARVYFQQLISAVDFCHSRGVYHRDLKPENLLLDEEGNLKVTDFGLSAFTEHLKQDGLLHTTCGTPAYVAPEVILKKGYDGAKADLWSCGVILFVLLAGYLPFQDDNLVNMYRKIYRGDFKCPGWLSSDARRLVTKLLDPNPNTRITIEKVMDSPWFKKQATRSRNEPVAATITTTEEDVDFLVHKSKEETETLNAFHI...
2.7.11.1
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
basipetal auxin transport [GO:0010540]; hyperosmotic salinity response [GO:0042538]; phosphorylation [GO:0016310]; response to calcium ion [GO:0051592]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414]; signal transduction [GO:0007165]
endoplasmic reticulum [GO:0005783]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF03822;PF00069;
3.30.310.80;1.10.510.10;
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
PTM: Autophosphorylated.
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:21445098}. Note=Targeted to the cell membrane when interacting with CBL4 and ATK2.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr...
null
null
null
null
FUNCTION: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Downstream of CBL1, CBL2, CBL3 and CBL9, regulates by phosphorylation the K(+) conductance and uptake of A...
Arabidopsis thaliana (Mouse-ear cress)
O65570
VILI4_ARATH
MSVSMRDLDPAFQGAGQKAGIEIWRIENFIPTPIPKSSIGKFFTGDSYIVLKTTALKTGALRHDIHYWLGKDTSQDEAGTAAVKTVELDAALGGRAVQYREVQGHETEKFLSYFKPCIIPQEGGVASGFKHVVAEEHITRLFVCRGKHVVHVKEVPFARSSLNHDDIYILDTKSKIFQFNGSNSSIQERAKALEVVQYIKDTYHDGTCEVATVEDGKLMADADSGEFWGFFGGFAPLPRKTANDEDKTYNSDITRLFCVEKGQANPVEGDTLKREMLDTNKCYILDCGIEVFVWMGRTTSLDDRKIASKAAEEMIRSSER...
null
null
actin crosslink formation [GO:0051764]; actin filament capping [GO:0051693]; actin filament depolymerization [GO:0030042]; actin filament organization [GO:0007015]; actin filament severing [GO:0051014]; cytoplasmic streaming [GO:0099636]; root hair elongation [GO:0048767]
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886]
actin filament binding [GO:0051015]; mRNA binding [GO:0003729]
PF00626;PF02209;
3.40.20.10;1.10.950.10;
Villin/gelsolin family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21275995}.
null
null
null
null
null
FUNCTION: Binds actin and actin filament bundles in a Ca(2+)-insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Involved in root hair growth through regulating actin organization in a Ca(2+)-dependent manner. {ECO:0000269|PubMed:21275995, ECO:0000269|...
Arabidopsis thaliana (Mouse-ear cress)
O65572
CCD1_ARATH
MAEKLSDGSSIISVHPRPSKGFSSKLLDLLERLVVKLMHDASLPLHYLSGNFAPIRDETPPVKDLPVHGFLPECLNGEFVRVGPNPKFDAVAGYHWFDGDGMIHGVRIKDGKATYVSRYVKTSRLKQEEFFGAAKFMKIGDLKGFFGLLMVNVQQLRTKLKILDNTYGNGTANTALVYHHGKLLALQEADKPYVIKVLEDGDLQTLGIIDYDKRLTHSFTAHPKVDPVTGEMFTFGYSHTPPYLTYRVISKDGIMHDPVPITISEPIMMHDFAITETYAIFMDLPMHFRPKEMVKEKKMIYSFDPTKKARFGVLPRYAKD...
1.14.99.n4
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
carotene catabolic process [GO:0016121]; carotenoid catabolic process [GO:0016118]; xanthophyll catabolic process [GO:0016124]
chloroplast stroma [GO:0009570]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
9-cis-epoxycarotenoid dioxygenase activity [GO:0045549]; metal ion binding [GO:0046872]
PF03055;
null
Carotenoid oxygenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12834401, ECO:0000269|PubMed:16507088}. Note=On the exterior surface of the plastids.
CATALYTIC ACTIVITY: Reaction=all-trans-zeaxanthin + 2 O2 = 2 (3R)-hydroxy-beta-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial; Xref=Rhea:RHEA:26393, ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:53171, ChEBI:CHEBI:53173; EC=1.14.99.n4; Evidence={ECO:0000269|PubMed:11316814};
null
null
null
null
FUNCTION: Cleaves a variety of carotenoids symmetrically at both the 9-10 and 9'-10' double bonds. Active on beta,beta-carotene, lutein, zeaxanthin, all-trans-violaxanthin, 9-cis-violaxanthin and 9'-cis-neoxanthin. With most substrates, the carotenoid is symmetrically cleaved. Probably not involved in abscisic acid bio...
Arabidopsis thaliana (Mouse-ear cress)
O65583
UKL4_ARATH
MGSKSVVDMIEAASRAHFSGLHVNGHMNGLEPSALKETTSASEDIQRQPFVIGVAGGAASGKTTVCDMIIQQLHDQRVVLINLDSFYHNLTEEELARVHEYNFDHPDAFDTEHLLSCMEKLRQGQAVDIPKYDFKTYRSSVFRRVNPTDVIILEGILLFHDPRVRKLMNMKIFVCTDADVRLARRIKRDTVENGRDIGTVLDQYSKFVKPAFDDFILPTKKYADIIIPRGGDNHVAIDLIVQHICTKLGQHDLCKIYPNLYVIHSTFQIRGMHTLIRDSQTTKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVITPTGCVY...
2.4.2.9; 2.7.1.48
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP. {ECO:0000250};
CTP salvage [GO:0044211]; phosphorylation [GO:0016310]; UMP salvage [GO:0044206]
cytoplasm [GO:0005737]
ATP binding [GO:0005524]; cytidine kinase activity [GO:0043771]; GTP binding [GO:0005525]; uracil phosphoribosyltransferase activity [GO:0004845]; uridine kinase activity [GO:0004849]
PF00485;PF14681;
3.40.50.2020;3.40.50.300;
Uridine kinase family; UPRTase family
null
null
CATALYTIC ACTIVITY: Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019, ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9; CATALYTIC ACTIVITY: Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674, ChEBI:CHEBI:15378, ChEBI:C...
null
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.; PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1.
null
null
FUNCTION: Involved in the pyrimidine salvage pathway. The uracil phosphoribosyltransferase (UPRT) activity, that catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate, is unsure. {ECO:0000269|PubMed:19563437}.
Arabidopsis thaliana (Mouse-ear cress)
O65639
CSP1_ARATH
MASEDQSAARSTGKVNWFNASKGYGFITPDDGSVELFVHQSSIVSEGYRSLTVGDAVEFAITQGSDGKTKAVNVTAPGGGSLKKENNSRGNGARRGGGGSGCYNCGELGHISKDCGIGGGGGGGERRSRGGEGCYNCGDTGHFARDCTSAGNGDQRGATKGGNDGCYTCGDVGHVARDCTQKSVGNGDQRGAVKGGNDGCYTCGDVGHFARDCTQKVAAGNVRSGGGGSGTCYSCGGVGHIARDCATKRQPSRGCYQCGGSGHLARDCDQRGSGGGGNDNACYKCGKEGHFARECSSVA
null
null
cold acclimation [GO:0009631]; DNA duplex unwinding [GO:0032508]; response to cold [GO:0009409]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414]; RNA secondary structure unwinding [GO:0010501]
cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
double-stranded DNA binding [GO:0003690]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697]; zinc ion binding [GO:0008270]
PF00313;PF00098;
2.40.50.140;4.10.60.10;
Cold shock protein (CSP) family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
null
null
null
null
null
FUNCTION: Chaperone that binds to RNA, single- (ssDNA) and double-stranded (dsDNA) DNA, and unwinds nucleic acid duplex. Exhibits a DNA melting activity. May be involved in cold resistance. Prevents seed germination under dehydration or salt stress conditions. {ECO:0000269|PubMed:17169986, ECO:0000269|PubMed:19258348, ...
Arabidopsis thaliana (Mouse-ear cress)
O65660
PLAT1_ARATH
MARRDVLLPFLLLLATVSAVAFAEDDPDCVYTFYLRTGSIWKAGTDSIISARIYDKDGDYIGIKNLQAWAGLMGPDYNYFERGNLDIFSGRAPCLPSPICALNLTSDGSGDHHGWYVNYVEITTAGVHAQCSTQDFEIEQWLATDTSPYELTAVRNNCPVKLRDSVSRVGSEIRKKLSWVV
null
null
response to cold [GO:0009409]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414]
chloroplast thylakoid membrane [GO:0009535]; endoplasmic reticulum [GO:0005783]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plastoglobule [GO:0010287]; secretory vesicle [GO:0099503]; thylakoid [GO:0009579]
null
PF01477;
2.60.60.20;
null
null
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:25396746}. Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:22274653}. Note=Localizes to rod shaped ER structures that resemble ER bodies. {ECO:0000269|PubMed:25396746}.
null
null
null
null
null
FUNCTION: Positive regulator of abiotic stress tolerance involved in the regulation of plant growth. May be a downstream target of the abscisic acid (ABA) signaling pathway. {ECO:0000269|PubMed:25396746}.
Arabidopsis thaliana (Mouse-ear cress)
O65683
BZP11_ARATH
MESSSSGTTSSTIQTSSGSEESLMEQRKRKRMLSNRESARRSRMKKQKLLDDLTAQVNHLKKENTEIVTSVSITTQHYLTVEAENSVLRAQLDELNHRLQSLNDIIEFLDSSNNNNNNNMGMCSNPLVGLECDDFFVNQMNMSYIMNQPLMASSDALMY
null
null
negative regulation of translation [GO:0017148]; positive regulation of DNA-templated transcription [GO:0045893]; response to sucrose [GO:0009744]; sucrose induced translational repression [GO:0080149]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; protein heterodimerization activity [GO:0046982]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
PF00170;
1.20.5.170;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:15047879}.
null
null
null
null
null
FUNCTION: Transcription factor that binds to the DNA sequence 5'-ACTCAT-3' in target gene promoters. Promotes POX1/PRODH1 expression in response to hypoosmolarity stress (PubMed:15047879). Positively regulates the expression of ASN1 and POX2/PRODH2 genes, which are involved in amino acid metabolism (PubMed:18088315). R...
Arabidopsis thaliana (Mouse-ear cress)
O65686
RS16A_ARATH
MTVKIRLARLGCKHRPFYRVVVADEKSRRDGKQIEVLGFYDPLQGKEDADRVSLKFDRIKYWLSVGAQPTDTVESMLFRAGLIPPKPMVVVGSKNGQKSTSQHVSPITGEILN
null
null
embryo development ending in seed dormancy [GO:0009793]; mitochondrial translation [GO:0032543]
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; plasma membrane [GO:0005886]; plastid [GO:0009536]; ribosome [GO:0005840]; small ribosomal subunit [GO:0015935]
mRNA binding [GO:0003729]; protein domain specific binding [GO:0019904]; structural constituent of ribosome [GO:0003735]
PF00886;
3.30.1320.10;
Bacterial ribosomal protein bS16 family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18453549}. Note=Not seen to be targeted to mitochondria. {ECO:0000269|PubMed:18453549}.
null
null
null
null
null
null
Arabidopsis thaliana (Mouse-ear cress)
O65717
CNGC1_ARATH
MNFRQEKFVRFQDWKSDKTSSDVEYSGKNEIQTGIFQRTISSISDKFYRSFESSSARIKLFKRSYKSYSFKEAVSKGIGSTHKILDPQGPFLQRWNKIFVLACIIAVSLDPLFFYVPIIDDAKKCLGIDKKMEITASVLRSFTDVFYVLHIIFQFRTGFIAPSSRVFGRGVLVEDKREIAKRYLSSHFIIDILAVLPLPQMVILIIIPHMRGSSSLNTKNMLKFIVFFQYIPRFIRIYPLYKEVTRTSGILTETAWAGAAFNLFLYMLASHVFGAFWYLFSIERETVCWKQACERNNPPCISKLLYCDPETAGGNAFLNE...
null
null
null
plasma membrane [GO:0005886]
calmodulin binding [GO:0005516]; cAMP binding [GO:0030552]; cGMP binding [GO:0030553]; monoatomic ion channel activity [GO:0005216]
PF00027;PF00520;
1.10.287.70;1.10.287.630;2.60.120.10;
Cyclic nucleotide-gated cation channel (TC 1.A.1.5) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Acts as a cyclic nucleotide-gated ion channel. Can be activated by cyclic AMP which leads to an opening of the cation channel. May be responsible for cAMP-induced calcium entry in cells and thus should be involved in the calcium signal transduction. Could transport K(+), Na(+) and Pb(2+). {ECO:0000269|PubMed:...
Arabidopsis thaliana (Mouse-ear cress)
O65718
CNGC2_ARATH
MPSHPNFIFRWIGLFSDKFRRQTTGIDENSNLQINGGDSSSSGSDETPVLSSVECYACTQVGVPAFHSTSCDQAHAPEWRASAGSSLVPIQEGSVPNPARTRFRRLKGPFGEVLDPRSKRVQRWNRALLLARGMALAVDPLFFYALSIGRTTGPACLYMDGAFAAVVTVLRTCLDAVHLWHVWLQFRLAYVSRESLVVGCGKLVWDPRAIASHYARSLTGFWFDVIVILPVPQAVFWLVVPKLIREEKVKLIMTILLLIFLFQFLPKIYHCICLMRRMQKVTGYIFGTIWWGFALNLIAYFIASHVAGGCWYVLAIQRVA...
null
null
calcium ion import [GO:0070509]; defense response [GO:0006952]; nitric oxide mediated signal transduction [GO:0007263]; plant-type hypersensitive response [GO:0009626]
plasma membrane [GO:0005886]
calcium channel activity [GO:0005262]; calmodulin binding [GO:0005516]; cAMP binding [GO:0030552]; cGMP binding [GO:0030553]; intracellularly cAMP-activated cation channel activity [GO:0005222]; intracellularly cyclic nucleotide-activated monoatomic cation channel activity [GO:0005221]; inward rectifier potassium chann...
PF00027;
1.10.287.70;1.10.287.630;2.60.120.10;
Cyclic nucleotide-gated cation channel (TC 1.A.1.5) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Acts as a cyclic nucleotide-gated ion channel. Permeable to potassium and calcium in a cyclic nucleotide-dependent fashion (cAMP or cGMP). Could also transport lithium, cesium and rubium and displays a strong selectivity against sodium. Seems to directly participate in pathogen-induced calcium influx. May fun...
Arabidopsis thaliana (Mouse-ear cress)
O65719
HSP7C_ARATH
MAGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPINTVFDAKRLIGRRFTDSSVQSDIKLWPFTLKSGPAEKPMIVVNYKGEDKEFSAEEISSMILIKMREIAEAYLGTTIKNAVVTVPAYFNDSQRQATKDAGVIAGLNVMRIINEPTAAAIAYGLDKKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKNKKDISGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGIDFYAPITRARFEELNIDLFRKCM...
null
null
response to heat [GO:0009408]; response to virus [GO:0009615]
apoplast [GO:0048046]; chloroplast [GO:0009507]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; Golgi apparatus [GO:0005794]; nuclear matrix [GO:0016363]; plant-type cell wall [GO:0009505]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]; vacuole [GO:0005773]
ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; mRNA binding [GO:0003729]; protease binding [GO:0002020]
PF00012;
1.20.1270.10;3.30.30.30;3.30.420.40;
Heat shock protein 70 (TC 1.A.33) family, DnaK subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14505352}. Nucleus matrix {ECO:0000269|PubMed:14505352}.
null
null
null
null
null
FUNCTION: In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions. {ECO:0000305}.
Arabidopsis thaliana (Mouse-ear cress)
O65782
C83B1_ARATH
MDLLLIIAGLVAAAAFFFLRSTTKKSLRLPPGPKGLPIIGNLHQMEKFNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMKRFIDILYETQALLGTLFFSDLFPYFGFLDNLTGLSARLKKAFKELDTYLQELLDETLDPNRPKQETESFIDLLMQIYKDQPFSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPE...
1.14.14.45
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242};
adventitious root development [GO:0048830]; defense response by callose deposition in cell wall [GO:0052544]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; indole glucosinolate biosynthetic process [GO:0009759]; indoleacetic acid biosynthetic process [GO:0009684]; induced systemic...
endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=(E)-(indol-3-yl)acetaldehyde oxime + glutathione + O2 + reduced [NADPH--hemoprotein reductase] = (E)-1-(glutathione-S-yl)-2-(1H-indol-3-yl)acetohydroximate + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52180, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 uM for indole-3-acetaldoxime {ECO:0000269|PubMed:11158532, ECO:0000269|PubMed:11553739, ECO:0000269|PubMed:12970475}; KM=65 uM for p-hydroxyphenylacetaldoxime {ECO:0000269|PubMed:12970475}; KM=188 uM for phenylacetaldoxime {ECO:0000269|PubMed:12970475}; Note=kc...
null
null
null
FUNCTION: Involved in the metabolism of aromatic oximes. Catalyzes the oxime metabolizing step in indole glucosinolate biosynthesis by converting indole-3-acetaldoxime into indole-3-S-alkyl-thiohydroximate. Probably required for glucosinolate activation in response to pathogens. Functions in auxin homeostasis because i...
Arabidopsis thaliana (Mouse-ear cress)
O65797
ADS1_ARATH
MSLSASEKEENNKKMAADKAEMGRKKRAMWERKWKRLDIVKAFASLFVHFLCLLAPFNFTWPALRVALIVYTVGGLGITVSYHRNLAHRSFKVPKWLEYFFAYCGLLAIQGDPIDWVSTHRYHHQFTDSDRDPHSPNEGFWFSHLLWLFDTGYLVEKCGRRTNVEDLKRQWYYKFLQRTVLYHILTFGFLLYYFGGLSFLTWGMGIGVAMEHHVTCLINSLCHVWGSRTWKTNDTSRNVWWLSVFSFGESWHNNHHAFESSARQGLEWWQIDISWYIVRFLEIIGLATDVKLPSESQRRRMAMVR
1.14.19.-
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:O00767};
unsaturated fatty acid biosynthetic process [GO:0006636]; very long-chain fatty acid biosynthetic process [GO:0042761]
chloroplast membrane [GO:0031969]; endoplasmic reticulum membrane [GO:0005789]
16:0 monogalactosyldiacylglycerol desaturase activity [GO:0009979]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water [GO:0016717]
PF00487;
null
Fatty acid desaturase type 1 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23175755}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000305|PubMed:27062193}; Multi-pass membrane protein {ECO:0000255}.
null
null
PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000305}.
null
null
FUNCTION: Involved in delta-9 desaturation of fatty acids (Probable) (PubMed:15240892, PubMed:17156034). Involved in the production of very-long-chain fatty acids (VLCFAs) (PubMed:23175755). May desaturate chloroplastic monogalactosyl diacylglycerol (MGDG) and alter chloroplast membrane fluidity, which is required to p...
Arabidopsis thaliana (Mouse-ear cress)
O65896
CDA1_ARATH
MDKPSFVIQSKEAESAAKQLGVSVIQLLPSLVKPAQSYARTPISKFNVAVVGLGSSGRIFLGVNVEFPNLPLHHSIHAEQFLVTNLTLNGERHLNFFAVSAAPCGHCRQFLQEIRDAPEIKILITDPNNSADSDSAADSDGFLRLGSFLPHRFGPDDLLGKDHPLLLESHDNHLKISDLDSICNGNTDSSADLKQTALAAANRSYAPYSLCPSGVSLVDCDGKVYRGWYMESAAYNPSMGPVQAALVDYVANGGGGGYERIVGAVLVEKEDAVVRQEHTARLLLETISPKCEFKVFHCYEA
3.5.4.5
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:10024464}; Note=Binds 1 zinc ion per subunit. {ECO:0000305|PubMed:10024464};
cytidine catabolic process [GO:0006216]; cytidine deamination [GO:0009972]
cytosol [GO:0005829]; mitochondrion [GO:0005739]
cytidine deaminase activity [GO:0004126]; deoxycytidine deaminase activity [GO:0047844]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270]
PF00383;PF08211;
3.40.140.10;
Cytidine and deoxycytidylate deaminase family
null
null
CATALYTIC ACTIVITY: Reaction=cytidine + H(+) + H2O = NH4(+) + uridine; Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5; Evidence={ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3}; PhysiologicalDirection=left-to-r...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 uM for cytidine (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:10024464}; KM=250 uM for cytidine (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:10469156}; KM=226.1 uM for cytidine (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|Ref.3}; KM=75 uM ...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3};
null
FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. Functions as a conventional cytidine deaminase. Has no affinity for RNA and is not involved in RNA-editing by C-to-U deamination. {ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3}.
Arabidopsis thaliana (Mouse-ear cress)
O65934
ABC1_MYCTU
MPMSQPAAPPVLTVRYEGSERTFAAGHDVVVGRDLRADVRVAHPLISRAHLLLRFDQGRWVAIDNGSLNGLYLNNRRVPVVDIYDAQRVHIGNPDGPALDFEVGRHRGSAGRPPQTTSIRLPNLSAGAWPTDGPPQTGTLGSGQLQQLPPATTRIPAAPPSGPQPRYPTGGQQLWPPSGPQRAPQIYRPPTAAPPPAGARGGTEAGNLATSMMKILRPGRLTGELPPGAVRIGRANDNDIVIPEVLASRHHATLVPTPGGTEIRDNRSINGTFVNGARVDAALLHDGDVVTIGNIDLVFADGTLARREENLLETRVGGLD...
7.-.-.-
null
transmembrane transport [GO:0055085]
cytosol [GO:0005829]; membrane [GO:0016020]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]
PF01061;PF00005;PF00498;
2.60.200.20;3.40.50.300;
ABC transporter superfamily; ABC-2 integral membrane protein family
PTM: Phosphorylated by PknF. Can probably be phosphorylated in vivo by other kinases when PknF is missing. {ECO:0000269|PubMed:15135525, ECO:0000269|PubMed:15987910, ECO:0000269|PubMed:21622570}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Involved in the translocation of an unknown substrate across the membrane. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for virulence. {ECO:0000269|PubMed:15135525, ECO:0000269|PubMed:16040957}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O66200
CH60_ENTAG
MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGIDKAVASAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQA...
5.6.1.7
null
chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial unfolded protein response [GO:0034514]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of T cell activation [GO:0050870]; positive regulation of ...
GroEL-GroES complex [GO:1990220]
ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; isomerase activity [GO:0016853]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
PF00118;
3.50.7.10;1.10.560.10;3.30.260.10;
Chaperonin (HSP60) family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00600};
null
null
null
null
FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. {ECO:0000255|HAMAP-Rule:...
Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
O66465
MRAY_AQUAE
MLYQLALLLKDYWFAFNVLKYITFRSFTAVLIAFFLTLVLSPSFINRLRKIQRLFGGYVREYTPESHEVKKYTPTMGGIVILIVVTLSTLLLMRWDIKYTWVVLLSFLSFGTIGFWDDYVKLKNKKGISIKTKFLLQVLSASLISVLIYYWADIDTILYFPFFKELYVDLGVLYLPFAVFVIVGSANAVNLTDGLDGLAIGPAMTTATALGVVAYAVGHSKIAQYLNIPYVPYAGELTVFCFALVGAGLGFLWFNSFPAQMFMGDVGSLSIGASLATVALLTKSEFIFAVAAGVFVFETISVILQIIYFRWTGGKRLFKR...
2.7.8.13
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000269|PubMed:23990562, ECO:0000269|PubMed:27088606, ECO:0000269|PubMed:29459785}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:23990562};
cell cycle [GO:0007049]; cell division [GO:0051301]; cell wall macromolecule biosynthetic process [GO:0044038]; cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]
plasma membrane [GO:0005886]
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phospho-N-acetylmuramoyl-pentapeptide-transferase activity [GO:0008963]; phosphotransferase activity, for other substituted phosphate groups [GO:0016780]; UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecapre...
PF00953;PF10555;
null
Glycosyltransferase 4 family, MraY subfamily
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00038}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00038}.
CATALYTIC ACTIVITY: Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP; Xref=Rhe...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=190 uM for UDP-MurNAc-pentapeptide {ECO:0000269|PubMed:27088606};
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00038}.
null
null
FUNCTION: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ...
Aquifex aeolicus (strain VF5)
O66490
KAD_AQUAE
MILVFLGPPGAGKGTQAKRLAKEKGFVHISTGDILREAVQKGTPLGKKAKEYMERGELVPDDLIIALIEEVFPKHGNVIFDGFPRTVKQAEALDEMLEKKGLKVDHVLLFEVPDEVVIERLSGRRINPETGEVYHVKYNPPPPGVKVIQREDDKPEVIKKRLEVYREQTAPLIEYYKKKGILRIIDASKPVEEVYRQVLEVIGDGN
2.7.4.3
null
AMP salvage [GO:0044209]; CDP biosynthetic process [GO:0046705]; nucleoside diphosphate metabolic process [GO:0009132]; nucleoside monophosphate metabolic process [GO:0009123]; phosphorylation [GO:0016310]; UDP biosynthetic process [GO:0006225]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]
adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; UMP kinase activity [GO:0033862]
PF00406;
3.40.50.300;
Adenylate kinase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}.
CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00235};
null
PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}.
null
null
FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-Rule:MF_00235}.
Aquifex aeolicus (strain VF5)
O66663
KDTA_AQUAE
MQFEVLKRFFPKESLKNCKGALWVHTASIGEFNTFLPILKELKREHRILLTYFSPRAREYLKTKSDFYDCLHPLPLDNPFSVKRFEELSKPKALIVVEREFWPSLIIFTKVPKILVNAYAKGSLIEKILSKKFDLIIMRTQEDVEKFKTFGAKRVFSCGNLKFICQKGKGIKLKGEFIVAGSIHTGEVEIILKAFKEIKKTYSSLKLILVPRHIENAKIFEKKARDFGFKTSFFENLEGDVILVDRFGILKELYPVGKIAIVGGTFVNIGGHNLLEPTCWGIPVIYGPYTHKVNDLKEFLEKEGAGFEVKNETELVTKLT...
2.4.99.12
null
lipid A biosynthetic process [GO:0009245]; lipopolysaccharide core region biosynthetic process [GO:0009244]
plasma membrane [GO:0005886]
Kdo transferase activity [GO:0043842]; transferase activity [GO:0016740]
PF04413;
3.40.50.11720;3.40.50.2000;
Glycosyltransferase group 1 family, Glycosyltransferase 30 subfamily
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:22474366}; Peripheral membrane protein {ECO:0000305|PubMed:22474366}; Cytoplasmic side {ECO:0000305|PubMed:22474366}.
CATALYTIC ACTIVITY: Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+); Xref=Rhea:RHEA:28066, ChEBI:CHEBI:15378, ChEBI:CHEBI:58603, ChEBI:CHEBI:60364, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; EC=2.4.99.12; Evidence={ECO:0000269|PubMed:19546212, ECO:0000...
null
PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
null
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly thermostable. Does not lose activity after 16 hours at 70 or 80 degrees Celsius, but incubation of the enzyme at 90 and 99 degrees Celsius for 1 hour results in gradual loss of activity. {ECO:0000269|PubMed:19546212};
FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of a single 3-deoxy-D-manno-octulosonate (Kdo) residue from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Is strictly monofunctional, i.e. is capable of adding only a single Kdo residue to the...
Aquifex aeolicus (strain VF5)
O66990
PYRC_AQUAE
MLKLIVKNGYVIDPSQNLEGEFDILVENGKIKKIDKNILVPEAEIIDAKGLIVCPGFIDIHVHLRDPGQTYKEDIESGSRCAVAGGFTTIVCMPNTNPPIDNTTVVNYILQKSKSVGLCRVLPTGTITKGRKGKEIADFYSLKEAGCVAFTDDGSPVMDSSVMRKALELASQLGVPIMDHCEDDKLAYGVINEGEVSALLGLSSRAPEAEEIQIARDGILAQRTGGHVHIQHVSTKLSLEIIEFFKEKGVKITCEVNPNHLLFTEREVLNSGANARVNPPLRKKEDRLALIEGVKRGIIDCFATDHAPHQTFEKELVEFA...
3.5.2.3
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000269|PubMed:15381710, ECO:0000269|PubMed:15826652, ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009}; Note=Binds 1 Zn(2+) ion per subunit (PubMed:15381710, PubMed:15826652, PubMed:19128030, PubMed:24314009). Fully f...
'de novo' UMP biosynthetic process [GO:0044205]; purine nucleobase catabolic process [GO:0006145]
cytoplasm [GO:0005737]
allantoinase activity [GO:0004038]; dihydroorotase activity [GO:0004151]; zinc ion binding [GO:0008270]
PF01979;
3.20.20.140;2.30.40.10;
Metallo-dependent hydrolases superfamily, DHOase family, Class I DHOase subfamily
null
null
CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000269|PubMed:15381710, ECO:0000269|PubMed:24314009};
null
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305}.
null
null
FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000269|PubMed:15381710, ECO:0000269|PubMed:24314009}.
Aquifex aeolicus (strain VF5)
O67049
AROE_AQUAE
MINAQTQLYGVIGFPVKHSLSPVFQNALIRYAGLNAVYLAFEINPEELKKAFEGFKALKVKGINVTVPFKEEIIPLLDYVEDTAKEIGAVNTVKFENGKAYGYNTDWIGFLKSLKSLIPEVKEKSILVLGAGGASRAVIYALVKEGAKVFLWNRTKEKAIKLAQKFPLEVVNSPEEVIDKVQVIVNTTSVGLKDKDPEIFNYDLIKKDHVVVDIIYKETKLLKKAKEKGAKLFDGLPMLLWQGIEAFKIWNGCEVPYSVAERSVRDLRG
1.1.1.25
null
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; shikimate metabolic process [GO:0019632]
cytosol [GO:0005829]
NADP binding [GO:0050661]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]
PF18317;PF01488;PF08501;
3.40.50.10860;3.40.50.720;
Shikimate dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:17649975};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=42.4 uM for shikimate (at pH 9 and 25 degrees Celsius) {ECO:0000269|PubMed:17649975}; KM=42.4 uM for NADP (at pH 9 and 25 degrees Celsius) {ECO:0000269|PubMed:17649975}; Note=kcat is 55.5 sec(-1) for dehydrogenase activity (at pH 9 and 25 degrees Celsius). {ECO:000...
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_00222}.
null
null
FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:17649975}.
Aquifex aeolicus (strain VF5)
O67082
RNC_AQUAE
MKMLEQLEKKLGYTFKDKSLLEKALTHVSYSKKEHYETLEFLGDALVNFFIVDLLVQYSPNKREGFLSPLKAYLISEEFFNLLAQKLELHKFIRIKRGKINETIIGDVFEALWAAVYIDSGRDANFTRELFYKLFKEDILSAIKEGRVKKDYKTILQEITQKRWKERPEYRLISVEGPHHKKKFIVEAKIKEYRTLGEGKSKKEAEQRAAEELIKLLEESE
3.1.26.3
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11738048, ECO:0000269|PubMed:15016361, ECO:0000269|PubMed:16439209, ECO:0000269|PubMed:18047582, ECO:0000269|PubMed:21138964}; Note=Binds 2 Mg(2+) per subunit. Mn(2+) also supports catalytic activity. {ECO:0000269|PubMed:11738048, ECO:0000269|P...
mRNA processing [GO:0006397]; pre-miRNA processing [GO:0031054]; regulation of gene expression [GO:0010468]; RNA processing [GO:0006396]; rRNA processing [GO:0006364]; siRNA processing [GO:0030422]; tRNA processing [GO:0008033]
cytoplasm [GO:0005737]; RISC complex [GO:0016442]
deoxyribonuclease I activity [GO:0004530]; double-stranded RNA binding [GO:0003725]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; ribonuclease III activity [GO:0004525]
PF00035;PF14622;
3.30.160.20;1.10.1520.10;
Ribonuclease III family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=98 nM for 16S-u-hp RNA {ECO:0000269|PubMed:21138964};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:21138964};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70-85 degrees Celsius. {ECO:0000269|PubMed:21138964};
FUNCTION: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Probably processes pre-crRNA and tracrRNA of type II CRISPR loci if pr...
Aquifex aeolicus (strain VF5)
O67233
CARB2_AQUAE
MSKKVVILGSGPNRIGQGIEFDYACVHAVFSLQEEGYYAVMVNCNPETVSTDYDTADKLYFEPIVFEHVMDIIEREKPEGVILQFGGQTPLKLALPLQKNGVKILGTKPESIDKAEDRELFRELIIELGLKQPPSGTARTKEEALKIAKEIGFPVLVRPSYVLGGRAMRIVYDEEELKEYLEEAVSVSHERPVLIDKFLDNSIELDVDAVSDGKDVLIGAVMEHIEEAGVHSGDSATSIPPYSLSKEIVEEVKEQTRKLAVALEVKGLINVQYAVQNNEVYVLEVNPRASRTVPFVSKSIGYPLAKIATKVAIGKSLREI...
6.3.4.16; 6.3.5.5
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00968}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P00968}; Note=Binds 2 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000305};
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; arginine biosynthetic process [GO:0006526]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; UTP biosynthetic process [GO:0006228]
cytosol [GO:0005829]
aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; metal ion binding [GO:0046872]
PF02786;PF02142;
3.40.50.20;3.30.470.20;3.40.50.1380;
CarB family
null
null
CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI...
null
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000250|UniProtKB:P00968}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000250|UniProtKB:P00968}.
null
null
FUNCTION: Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and...
Aquifex aeolicus (strain VF5)
O67496
ISPG_AQUAE
MIQKRKTRQIRVGNVKIGGDAPIVVQSMTSTKTHDVEATLNQIKRLYEAGCEIVRVAVPHKEDVEALEEIVKKSPMPVIADIHFAPSYAFLSMEKGVHGIRINPGNIGKEEIVREIVEEAKRRGVAVRIGVNSGSLEKDLLEKYGYPSAEALAESALRWSEKFEKWGFTNYKVSIKGSDVLQNVRANLIFAERTDVPLHIGITEAGMGTKGIIKSSVGIGILLYMGIGDTVRVSLTDDPVVEVETAYEILKSLGLRRRGVEIVACPTCGRIEVDLPKVVKEVQEKLSGVKTPLKVAVMGCVVNAIGEAREADIGLACGRG...
1.17.7.3
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:20932974}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:20932974};
isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway [GO:0019288]; terpenoid biosynthetic process [GO:0016114]
null
4 iron, 4 sulfur cluster binding [GO:0051539]; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity [GO:0046429]; iron ion binding [GO:0005506]
PF04551;
3.20.20.20;3.30.413.10;
IspG family
null
null
CATALYTIC ACTIVITY: Reaction=(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + reduced [flavodoxin]; Xref=Rhea:RHEA:43604, Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:10623, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEB...
null
PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 5/6. {ECO:0000255|HAMAP-Rule:MF_00159}.
null
null
FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:20932974}.
Aquifex aeolicus (strain VF5)
O67648
LPXC_AQUAE
MGLEKTVKEKLSFEGVGIHTGEYSKLIIHPEKEGTGIRFFKNGVYIPARHEFVVHTNHSTDLGFKGQRIKTVEHILSVLHLLEITNVTIEVIGNEIPILDGSGWEFYEAIRKNILNQNREIDYFVVEEPIIVEDEGRLIKAEPSDTLEVTYEGEFKNFLGRQKFTFVEGNEEEIVLARTFCFDWEIEHIKKVGLGKGGSLKNTLVLGKDKVYNPEGLRYENEPVRHKVFDLIGDLYLLGSPVKGKFYSFRGGHSLNVKLVKELAKKQKLTRDLPHLPSVQAL
3.5.1.108
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:11148046};
lipid A biosynthetic process [GO:0009245]
null
metal ion binding [GO:0046872]; UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity [GO:0008759]; UDP-3-O-acyl-N-acetylglucosamine deacetylase activity [GO:0103117]
PF03331;
3.30.230.20;3.30.1700.10;
LpxC family
null
null
CATALYTIC ACTIVITY: Reaction=a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate; Xref=Rhea:RHEA:67816, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:137740, ChEBI:CHEBI:173225; EC=3.5.1.108; Evidence={ECO:0000255|HAMAP-Rule:MF_00388, ECO:...
null
PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6. {ECO:0000255|HAMAP-Rule:MF_00388}.
null
null
FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:11148046}.
Aquifex aeolicus (strain VF5)
O67869
CARB1_AQUAE
MPKRTDIKKILIIGSGPIVIGQAAEFDYSGTQACKALKQEGYEVILVNSNPATIMTDPEMADKTYIEPLTADILEEIIKKERPDALLPTLGGQTGLNLAVELYENGVLERYGVELIGANYEAIKKGEDRELFKETMESIGLKVPESAVVRSVEEGLKAVEKIGFPVILRPAFTLGGTGSSVAYNVEEFKEKLKVALETSPIHEVLLDKSLIGWKEIEFEVVRDKADNVIIVCAIENFDPMGVHTGDSITVAPTQTLTDKEYQMLRDAAIAVIRAIGVDTGGSNIQFALSPESGDFYVIEMNPRVSRSSALASKATGFPIA...
6.3.4.16; 6.3.5.5
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00968}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P00968}; Note=Binds 2 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000305};
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; arginine biosynthetic process [GO:0006526]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; UTP biosynthetic process [GO:0006228]
cytosol [GO:0005829]
aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; metal ion binding [GO:0046872]
PF02786;PF02787;
3.40.50.20;3.30.470.20;1.10.1030.10;
CarB family
null
null
CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI...
null
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000250|UniProtKB:P00968}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000250|UniProtKB:P00968}.
null
null
FUNCTION: Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and...
Aquifex aeolicus (strain VF5)
O67911
CATNT_AQUAE
MENIEIVSSGKHTLHGLNFYLSYFDDVAKVLPREHYCFIVGGWVRDRILGEPVGYNIDVDFLTTADPVELAKNFAKRIGGHFFVFEKRGFLIKRPTIASVVLHLPPYRYRFDFSPLKGKDLEKALIEDLKERDFTANAIAVNLDDVLSIGAKQTIVYDPTGGIKDLEQGLLRPVSIENLKRDPVRVLRGFRIAIEKNLQLTEDFYEFVKEDPRIVLKSAVERITHELFKIMKEKTAHKVIRELYEYGVLEAIIPEIGRLREVKDQGEHHIYPLDEHTLKTLEYLEQVIEDRAKYLSAELLENFGKKRVLGEFTDVELLKW...
2.7.7.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24389024};
RNA 3'-end processing [GO:0031123]; tRNA processing [GO:0008033]
null
CTP:tRNA cytidylyltransferase activity [GO:0052927]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; tRNA binding [GO:0000049]
PF01966;PF01743;PF12627;
1.10.246.80;3.30.460.10;1.10.3090.10;
TRNA nucleotidyltransferase/poly(A) polymerase family
null
null
CATALYTIC ACTIVITY: Reaction=a tRNA precursor + 2 CTP = a tRNA with a 3' CC end + 2 diphosphate; Xref=Rhea:RHEA:60008, Rhea:RHEA-COMP:10465, Rhea:RHEA-COMP:15488, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74896, ChEBI:CHEBI:83069; Evidence={ECO:0000269|PubMed:11701927, ECO:0000269|PubMed:24389024}; Physiologica...
null
null
null
null
FUNCTION: tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the two cytidine residues to tRNA. {ECO:0000269|PubMed:11701927, ECO:0000269|PubMed:24389024}.
Aquifex aeolicus (strain VF5)
O67931
SQRD_AQUAE
MAKHVVVIGGGVGGIATAYNLRNLMPDLKITLISDRPYFGFTPAFPHLAMGWRKFEDISVPLAPLLPKFNIEFINEKAESIDPDANTVTTQSGKKIEYDYLVIATGPKLVFGAEGQEENSTSICTAEHALETQKKLQELYANPGPVVIGAIPGVSCFGPAYEFALMLHYELKKRGIRYKVPMTFITSEPYLGHFGVGGIGASKRLVEDLFAERNIDWIANVAVKAIEPDKVIYEDLNGNTHEVPAKFTMFMPSFQGPEVVASAGDKVANPANKMVIVNRCFQNPTYKNIFGVGVVTAIPPIEKTPIPTGVPKTGMMIEQM...
1.8.5.4
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:19487671}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:19487671};
aerobic electron transport chain [GO:0019646]
membrane [GO:0016020]
identical protein binding [GO:0042802]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]; nucleotide binding [GO:0000166]; quinone binding [GO:0048038]; sulfide:quinone oxidoreductase activity [GO:0070224]
PF07992;
3.50.50.100;
SQRD family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10816041, ECO:0000269|PubMed:19487671}; Peripheral membrane protein {ECO:0000269|PubMed:10816041, ECO:0000269|PubMed:19487671}.
CATALYTIC ACTIVITY: Reaction=n a quinone + n H(+) + n hydrogen sulfide = n a quinol + n sulfur; Xref=Rhea:RHEA:30239, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:26833, ChEBI:CHEBI:29919, ChEBI:CHEBI:132124; EC=1.8.5.4; Evidence={ECO:0000303|PubMed:10816041, ECO:0000303|PubMed:19487671};
null
null
null
null
FUNCTION: Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur. {ECO:0000303|PubMed:10816041, EC...
Aquifex aeolicus (strain VF5)
O68008
BACC_BACLI
MKTKVEKIYPLSNMQKGMLFHAMKDEASHAYFEQFIIELKGDVDERMFEESLNEVMKRHEILRASFHHRLDEPLHVIIKDRHMKFDYLDIRGRHDQDGVLERYLAEDRQKGFDLAKDTLMRACLIRMSDDSYQFVWTYHHILLDGWCLGIILDELLTIYEMKRKGQNHQLEDPRPYSDYIKWLEDQDKEEAQSYWESYLSGYDQKNSLPKLRTPSETGFKRREKTIECSKELTNRLIKLANRNHVTINTVLQSIWGVILAKYNNSEDVVFGTVVSGRDAEVEGIETMVGVFINTIPTRIRLDKDKLFKDVLRQTQADALE...
5.1.1.11; 5.1.1.13
COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000305}; Note=Binds 5 phosphopantetheines covalently. {ECO:0000305};
amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; antibiotic biosynthetic process [GO:0017000]; carboxylic acid metabolic process [GO:0019752]; secondary metabolite biosynthetic process [GO:0044550]
cytosol [GO:0005829]
aspartate racemase activity [GO:0047689]; ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; ligase activity [GO:0016874]; phenylalanine racemase (ATP-hydrolyzing) activity [GO:0047462]; phosphopantetheine binding [GO:0031177]
PF00501;PF13193;PF00668;PF00550;PF00975;
3.30.300.30;3.40.50.980;1.10.1200.10;3.40.50.1820;3.30.559.10;1.10.287.490;3.30.559.30;
ATP-dependent AMP-binding enzyme family
null
null
CATALYTIC ACTIVITY: Reaction=L-aspartate = D-aspartate; Xref=Rhea:RHEA:14973, ChEBI:CHEBI:29990, ChEBI:CHEBI:29991; EC=5.1.1.13; CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-phenylalanine = AMP + D-phenylalanine + diphosphate + H(+); Xref=Rhea:RHEA:20201, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHE...
null
PATHWAY: Antibiotic biosynthesis; bacitracin biosynthesis.
null
null
FUNCTION: Induces peptide synthesis, activates and incorporates five amino acids, forms a thiazoline ring between the first two amino acids and incorporates a D-glutamine in the fourth position.
Bacillus licheniformis
O68252
PCEA_SULMU
MEKKKKPELSRRDFGKLIIGGGAAATIAPFGVPGANAAEKEKNAAEIRQQFAMTAGSPIIVNDKLERYAEVRTAFTHPTSFFKPNYKGEVKPWFLSAYDEKVRQIENGENGPKMKAKNVGEARAGRALEAAGWTLDINYGNIYPNRFFMLWSGETMTNTQLWAPVGLDRRPPDTTDPVELTNYVKFAARMAGADLVGVARLNRNWVYSEAVTIPADVPYEQSLHKEIEKPIVFKDVPLPIETDDELIIPNTCENVIVAGIAMNREMMQTAPNSMACATTAFCYSRMCMFDMWLCQFIRYMGYYAIPSCNGVGQSVAFAVE...
1.21.99.5
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:29378885, ECO:0000269|PubMed:8663199}; Note=Binds 2 [4Fe-4S] clusters. {ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:29378885, ECO:0000269|PubMed:8663199}; COFACTOR: Name=corrinoid; Xref=ChEBI:CHEBI:339...
null
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]
PF13486;PF13484;
3.30.70.20;
PceA family
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000255|PROSITE-ProRule:PRU00648}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16802174, ECO:0000269|PubMed:8663199, ECO:0000269|PubMed:9696761}. Cell inner membrane {ECO:0000269|PubMed:16802174}; Peripheral membrane protein {ECO:0000269|PubMed:16802174}; Cytoplasmic side {ECO:0000269|PubMed:16802174}. Cell inner membrane {ECO:0000269|PubMed:168...
CATALYTIC ACTIVITY: Reaction=A + chloride + H(+) + trichloroethene = AH2 + tetrachloroethene; Xref=Rhea:RHEA:20353, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:16602, ChEBI:CHEBI:17300, ChEBI:CHEBI:17499, ChEBI:CHEBI:17996; EC=1.21.99.5; Evidence={ECO:0000269|PubMed:11976751, ECO:0000269|PubMed:12420164, ECO:0000...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for tetrachloroethene (with reduced methyl viologen as electron donor) {ECO:0000269|PubMed:8663199}; KM=200 uM for tetrachloroethene (with reduced methyl viologen as electron donor) {ECO:0000269|PubMed:11976751}; KM=0.24 mM for trichloroethene (with reduced ...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 8.0. {ECO:0000269|PubMed:8663199};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 42 degrees Celsius. {ECO:0000269|PubMed:8663199};
FUNCTION: Catalyzes the reductive dechlorination of tetrachloroethene (PCE) to trichloroethene (TCE) and of trichloroethene to cis-1,2-dichloroethene (DCE) (PubMed:11976751, PubMed:12420164, PubMed:24433392, PubMed:28671181, PubMed:8663199). In addition, trans-1,3-dichloropropene, 1,1,3-trichloropropene and 2,3-dichlor...
Sulfurospirillum multivorans (Dehalospirillum multivorans)
O68691
SCTF_YERPE
MSNFSGFTKGTDIADLDAVAQTLKKPADDANKAVNDSIAALKDKPDNPALLADLQHSINKWSVIYNINSTIVRSMKDLMQGILQKFP
null
null
protein secretion by the type III secretion system [GO:0030254]
cell surface [GO:0009986]; extracellular region [GO:0005576]; type III protein secretion system complex [GO:0030257]
null
PF09392;
1.20.58.90;
SctF family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16135236, ECO:0000269|PubMed:28196868, ECO:0000269|PubMed:29458689}. Cell surface {ECO:0000269|PubMed:16135236, ECO:0000269|PubMed:29458689}. Note=Targeted to the T3SS apparatus via the combined action of an N-terminal secretion signal and the YscE-YscG chaperone. {ECO...
null
null
null
null
null
FUNCTION: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:16135236). YscF/SctF forms the external needle filament that protrudes from the bacterial surface (PubMed:16135236, PubMed:19968786, PubMed:2819686...
Yersinia pestis
O68900
PET_ECO44
MNKIYSIKYSAATGGLIAVSELAKKVICKTNRKISAALLSLAVISYTNIIYAANMDISKAWARDYLDLAQNKGVFQPGSTHVKIKLKDGTDFSFPALPVPDFSSATANGAATSIGGAYAVTVAHNAKNKSSANYQTYGSTQYTQINRMTTGNDFSIQRLNKYVVETRGADTSFNYNENNQNIIDRYGVDVGNGKKEIIGFRVGSGNTTFSGIKTSQTYQADLLSASLFHITNLRANTVGGNKVEYENDSYFTNLTTNGDSGSGVYVFDNKEDKWVLLGTTHGIIGNGKTQKTYVTPFDSKTTNELKQLFIQNVNIDNNTA...
3.4.21.-
null
proteolysis [GO:0006508]
cell outer membrane [GO:0009279]; cell surface [GO:0009986]; extracellular region [GO:0005576]; periplasmic space [GO:0042597]
serine-type endopeptidase activity [GO:0004252]
PF03797;PF13018;PF02395;
2.160.20.20;2.40.10.120;2.40.128.130;
null
PTM: Cleaved to release the mature protein from the outer membrane.
SUBCELLULAR LOCATION: [Serine protease pet autotransporter]: Periplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Serine protease pet]: Secreted. Cell surface.; SUBCELLULAR LOCATION: [Serine protease pet translocator]: Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=The cleaved C-terminal...
null
null
null
null
null
FUNCTION: Serine protease with enterotoxic and cytotoxic activity. Internalization into the host cell is required for the induction of cytopathic effects. However, the serine activity is not necessary for secretion and internalization into the host cell. {ECO:0000269|PubMed:10225873, ECO:0000269|PubMed:10496914, ECO:00...
Escherichia coli O44:H18 (strain 042 / EAEC)
O69054
PTXD_STUST
MLPKLVITHRVHDEILQLLAPHCELMTNQTDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLAMADRLQGWGATLQYHEAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEDWARADRPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAGAR...
1.20.1.1
null
null
cytosol [GO:0005829]
glycerate dehydrogenase activity [GO:0008465]; glyoxylate reductase (NADP+) activity [GO:0030267]; hydroxypyruvate reductase activity [GO:0016618]; NAD binding [GO:0051287]; phosphonate dehydrogenase activity [GO:0050609]
PF00389;PF02826;
3.40.50.720;
D-isomer specific 2-hydroxyacid dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + phosphonate = H(+) + NADH + phosphate; Xref=Rhea:RHEA:13173, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16215, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.20.1.1; Evidence={ECO:0000269|PubMed:11278981};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.25-7.75.;
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius.;
FUNCTION: Catalyzes phosphite (phosphonate) oxidation. {ECO:0000269|PubMed:11278981}.
Stutzerimonas stutzeri (Pseudomonas stutzeri)
O69078
CSRA_PSEAE
MLILTRRVGETLMVGDDVTVTVLGVKGNQVRIGVNAPKEVAVHREEIYQRIQKEKDQEPNH
null
null
mRNA catabolic process [GO:0006402]; negative regulation of translational initiation [GO:0045947]; positive regulation of translational initiation [GO:0045948]; protein secretion by the type III secretion system [GO:0030254]; protein secretion by the type VI secretion system [GO:0033103]; quorum sensing [GO:0009372]; r...
cytosol [GO:0005829]
mRNA 5'-UTR binding [GO:0048027]
PF02599;
2.60.40.4380;
CsrA/RsmA family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}.
null
null
null
null
null
FUNCTION: A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UT...
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
O69174
ENO_STAAU
MPIITDVYAREVLDSRGNPTVEVEVLTESGAFGRALVPSGASTGEHEAVELRDGDKSRYLGKGVTKAVENVNEIIAPEIIEGEFSVLDQVSIDKMMIALDGTPNKGKLGANAILGVSIAVARAAADLLGQPLYKYLGGFNGKQLPVPMMNIVNGGSHSDAPIAFQEFMILPVGATTFKESLRWGTEIFHNLKSILSQRGLETAVGDEGGFAPKFEGTEDAVETIIQAIEAAGYKPGEEVFLGFDCASSEFYENGVYDYSKFEGEHGAKRTAAEQVDYLEQLVDKYPIITIEDGMDENDWDGWKQLTERIGDRVQLVGDDL...
4.2.1.11
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26627653}; Note=Binds a second Mg(2+) ion via substrate during catalysis. {ECO:0000255|HAMAP-Rule:MF_00318};
glycolytic process [GO:0006096]
cell surface [GO:0009986]; extracellular region [GO:0005576]; phosphopyruvate hydratase complex [GO:0000015]
magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]
PF00113;PF03952;
3.20.20.120;3.30.390.10;
Enolase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15158195}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15158195}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15158195}. Note=Fractions of enolase are present in both the cytoplasm and on the cel...
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26627653}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; Evidence={ECO...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.37 mM for 2-phosphoglycerate by octamer {ECO:0000269|PubMed:26627653}; Note=kcat is 83 sec(-1) for octamer. {ECO:0000269|PubMed:26627653};
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00318}.
null
null
FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP) (PubMed:26627653). It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:26627653}.; FUNCTION: 'Moonlights' as a laminin receptor. Binds laminin w...
Staphylococcus aureus
O69199
CYAB_AERHY
MSSQHFQGRFEVEFKYRLSDVDAFTCALAALNPEVMLEDNQEQDSYFDTPEHSLAAEGKSLVIRTMQPSGIQLWIVKGPEADRCEAVNITDADKAASMLRTLGYRQVLAISKRRSIYFVGPFHVTRDHLEGIGDFAELAIMTDDEALLPDYRQQLQDLATRLGLSSAQLETRSYRTLCEQSLTLNSEKVPS
4.6.1.1
null
cAMP biosynthetic process [GO:0006171]
cytoplasm [GO:0005737]
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]
PF01928;
2.40.320.10;
Adenylyl cyclase CyaB family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000269|PubMed:22984449};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5. {ECO:0000269|PubMed:9642185};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius. {ECO:0000269|PubMed:9642185};
FUNCTION: In vitro, CyaB catalyzes the biosynthesis of cyclic AMP (cAMP) from ATP. It seems that under the physiological conditions CyaB has no function in cAMP processes. In vitro, it is also able to hydrolyze substrates such as thiamine triphosphate (ThTP) and inorganic triphosphate (PPPi) at a low rate. It has a sli...
Aeromonas hydrophila
O69652
CDS1_MYCTU
MSGGACIAVRSLSRSWTDNAIRLIEADARRSADTHLLRYPLPAAWCTDVDVELYLKDETTHITGSLKHRLARSLFLYALCNGWINENTTVVEASSGSTAVSEAYFAALLGLPFIAVMPAATSASKIALIESQGGRCHFVQNSSQVYAEAERVAKETGGHYLDQFTNAERATDWRGNNNIAESIYVQMREEKHPTPEWIVVGAGTGGTSATIGRYIRYRRHATRLCVVDPENSAFFPAYSEGRYDIVMPTSSRIEGIGRPRVEPSFLPGVVDRMVAVPDAASIAAARHVSAVLGRRVGPSTGTNLWGAFGLLAEMVKQGRS...
4.4.1.1
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00868, ECO:0000269|PubMed:34439535};
cell redox homeostasis [GO:0045454]; cysteine biosynthetic process [GO:0019344]; hydrogen sulfide biosynthetic process [GO:0070814]; L-cysteine catabolic process to pyruvate [GO:0019450]; positive regulation of cellular respiration [GO:1901857]; regulation of sulfur metabolic process [GO:0042762]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]
lyase activity [GO:0016829]; pyridoxal phosphate binding [GO:0030170]
PF00291;
3.40.50.1100;
Cysteine synthase/cystathionine beta-synthase family, Cds1 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) + pyruvate; Xref=Rhea:RHEA:24931, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919, ChEBI:CHEBI:35235; EC=4.4.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00868, ECO:0000269|PubMed:34439535}; Physio...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.26 mM for cysteine {ECO:0000269|PubMed:34439535}; Note=kcat is 78.71 sec(-1). {ECO:0000269|PubMed:34439535};
null
null
null
FUNCTION: A cysteine desulfhydrase that generates hydrogen sulfide, H(2)S. The H(2)S produced by this enzyme stimulates respiration in M.tuberculosis, mediated primarily via cytochrome bd with a lesser contribution from cytochrome bc1/aa3. H(2)S modulates the balance between respiration and glycolysis, and also contrib...
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O69711
NMTR_MYCTU
MGHGVEGRNRPSAPLDSQAAAQVASTLQALATPSRLMILTQLRNGPLPVTDLAEAIGMEQSAVSHQLRVLRNLGLVVGDRAGRSIVYSLYDTHVAQLLDEAIYHSEHLHLGLSDRHPSAG
null
null
null
null
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]
PF01022;
1.10.10.10;
null
null
null
null
null
null
null
null
FUNCTION: Represses transcription of ctpJ/nmtA, by binding to its promoter region. {ECO:0000269|PubMed:12163508}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O69729
TCRY_MYCTU
MGITAATEMALRRHLVAQLDNQLGGTSYRSVLMYPEKMPRPPWRHETHNYIRSGPGPRFLDAPGQPAGMVAAVVSDGTTVAAGYLTGSGSRAALTSTGRSQLERIAGSRTPLTLDLDGLGRYRVLAAPSRNGHDVIVTGLSMGNVDATMLQMLIIFGIVTVIALVAATTAGIVIIKRALAPLRRVAQTASEVVDLPLDRGEVKLPVRVPEPDANPSTEVGQLGSALNRMLDHIAAALSARQASETCVRQFVADASHELRTPLAAIRGYTELTQRIGDDPEAVAHAMSRVASETERITRLVEDLLLLARLDSGRPLERGPV...
2.7.13.3
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:19962420};
phosphorelay signal transduction system [GO:0000160]; protein autophosphorylation [GO:0046777]
cytosol [GO:0005829]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; magnesium ion binding [GO:0000287]; phosphorelay sensor kinase activity [GO:0000155]; protein homodimerization activity [GO:0042803]
PF00672;PF02518;PF00512;
1.10.287.130;6.10.340.10;3.30.565.10;
null
PTM: Autophosphorylated.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3;
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mM for ATP {ECO:0000269|PubMed:19962420};
null
null
null
FUNCTION: Member of the two-component regulatory system TcrY/TcrX. Activates TcrX by phosphorylation. {ECO:0000269|PubMed:12595424, ECO:0000269|PubMed:19962420}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O69762
HCHL_PSEFL
MSTYEGRWKTVKVEIEDGIAFVILNRPEKRNAMSPTLNREMIDVLETLEQDPAAGVLVLTGAGEAWTAGMDLKEYFREVDAGPEILQEKIRREASQWQWKLLRMYAKPTIAMVNGWCFGGGFSPLVACDLAICADEATFGLSEINWGIPPGNLVSKAMADTVGHRQSLYYIMTGKTFGGQKAAEMGLVNESVPLAQLREVTIELARNLLEKNPVVLRAAKHGFKRCRELTWEQNEDYLYAKLDQSRLLDTEGGREQGMKQFLDDKSIKPGLQAYKR
4.1.2.61
null
isoprenoid catabolic process [GO:0008300]
null
trans-feruloyl-CoA hydratase activity [GO:0050548]; vanillin synthase activity [GO:0050547]
PF00378;
6.10.250.2850;
Enoyl-CoA hydratase/isomerase family
null
null
CATALYTIC ACTIVITY: Reaction=(E)-feruloyl-CoA + H2O = acetyl-CoA + vanillin; Xref=Rhea:RHEA:62412, ChEBI:CHEBI:15377, ChEBI:CHEBI:18346, ChEBI:CHEBI:57288, ChEBI:CHEBI:87305; EC=4.1.2.61; Evidence={ECO:0000269|PubMed:10222033, ECO:0000269|PubMed:9461612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62413; Evid...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.8 uM for feruloyl-CoA {ECO:0000269|PubMed:18479250}; KM=2.4 uM for feruloyl-CoA {ECO:0000269|PubMed:10222033}; KM=5.3 uM for 4-coumaroyl-CoA {ECO:0000269|PubMed:10222033}; KM=1.6 uM for caffeoyl-CoA {ECO:0000269|PubMed:10222033}; Vmax=36.5 nmol/sec/mg enzyme wit...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9.5. {ECO:0000269|PubMed:10222033};
null
FUNCTION: Catalyzes the hydration of the acyl-CoA thioester of ferulic acid and the subsequent retro-aldol cleavage of the hydrated intermediate to yield vanillin (4-hydroxy-3-methoxy-benzaldehyde) (PubMed:10222033, PubMed:9461612). The enzyme is also active with caffeoyl-CoA and 4-coumaroyl-CoA producing 3,4-dihydroxy...
Pseudomonas fluorescens
O70126
AURKB_MOUSE
MAQKENAYPWPYGSKTSQSGLNTLSQRVLRKEPATTSALALVNRFNSQSTAAPGQKLAENKSQGSTASQGSQNKQPFTIDNFEIGRPLGKGKFGNVYLAREKKSRFIVALKILFKSQIEKEGVEHQLRREIEIQAHLKHPNILQLYNYFYDQQRIYLILEYAPRGELYKELQKSRTFDEQRTATIMEELSDALTYCHKKKVIHRDIKPENLLLGLQGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEMVDLWCIGVLCYELMVGNPPFESPSHSETYRRIVKVDLKFPSSVPSGAQDLISKLLKHNPWQR...
2.7.11.1
null
abscission [GO:0009838]; cell cycle G2/M phase transition [GO:0044839]; cellular response to UV [GO:0034644]; cleavage furrow formation [GO:0036089]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; mitotic cytokinesis checkpoint signaling [GO:0044878]; mitotic spindle midzone assembly [GO:0051256]; m...
chromocenter [GO:0010369]; chromosome [GO:0005694]; chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; condensed chromosome, centromeric region [GO:0000779]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; mitotic spindl...
ATP binding [GO:0005524]; histone H3S28 kinase activity [GO:0044022]; kinase binding [GO:0019900]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily
PTM: The phosphorylation of Thr-237 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism. Thr-237 phosphorylation is indispensable for the AURKB kinase activity. {ECO:0000250|UniProtKB:Q96GD4}.; PTM: Acetylated at Lys-220 by KAT5 at kinetochores, increasing AURKB activity and promoting...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96GD4}. Chromosome {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96GD4}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96GD4}. Midbody {ECO:0000250|UniPro...
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:24034696}; CATALYTIC...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis (By similarity). The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced micr...
Mus musculus (Mouse)
O70127
ABCBB_RAT
MSDSVILRSVKKFGEENHAFESDGSHNNDKKSRLQDKMKEGDIRVGFFELFRFSSSKDIWLMLMGGVCALLHGMAQPGILIIFGIMTDIFIKYDIERQELEIPGKACVNNTIVWINSSFHQNMTNGTVCGLVDIESEMIKFSGIYAGVGMTVLILGYFQIRLWVITGARQIRRMRKIYFRRIMRMEIGWFDCTSVGELNSRFADDIEKINDAIADQLAHFLQRMSTAMCGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSIAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYEKNLVFAQRWGIWKGM...
7.6.2.-
null
bile acid and bile salt transport [GO:0015721]; bile acid metabolic process [GO:0008206]; bile acid signaling pathway [GO:0038183]; canalicular bile acid transport [GO:0015722]; cellular response to xenobiotic stimulus [GO:0071466]; cholesterol homeostasis [GO:0042632]; fatty acid metabolic process [GO:0006631]; lipid ...
apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; endosome [GO:0005768]; Golgi membrane [GO:0000139]; intercellular canaliculus [GO:0046581]; intracellular canaliculus [GO:0046691]; membrane [GO:0016020]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recy...
ABC-type bile acid transporter activity [GO:0015432]; ABC-type oligopeptide transporter activity [GO:0015421]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; bile acid transmembrane transporter activity [GO:0015125]; canalicular bile acid transmemb...
PF00664;PF00005;
1.20.1560.10;3.40.50.300;
ABC transporter superfamily, ABCB family, Multidrug resistance exporter (TC 3.A.1.201) subfamily
PTM: Ubiquitinated; short-chain ubiquitination regulates cell-Surface expression of ABCB11. {ECO:0000269|PubMed:18829893}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:O95342}.
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11113123, ECO:0000269|PubMed:17082223, ECO:0000269|PubMed:9545351}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:11113123, ECO:0000269|PubMed:15121884}; Multi-pass membrane protein {ECO:0000255}. Endosome {ECO:0...
CATALYTIC ACTIVITY: Reaction=ATP + cholate(in) + H2O = ADP + cholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50048, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:9545351}; PhysiologicalDirectio...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.7 uM for taurocholate {ECO:0000269|PubMed:16332456}; KM=25.7 uM for glycocholate {ECO:0000269|PubMed:16332456}; KM=10.2 uM for taurochenodeoxycholate {ECO:0000269|PubMed:16332456}; KM=5.6 uM for glycochenodeoxycholate {ECO:0000269|PubMed:16332456}; KM=22.2 uM for...
null
null
null
FUNCTION: Catalyzes the transport of the major hydrophobic bile salts, such as taurine and glycine-conjugated cholic acid across the canalicular membrane of hepatocytes in an ATP-dependent manner, therefore participates in hepatic bile acid homeostasis and consequently to lipid homeostasis through regulation of biliary...
Rattus norvegicus (Rat)
O70129
C5AR1_CAVPO
MMVTVSYDYDYNSTFLPDGFVDNYVERLSFGDLVAVVIMVVVFLVGVPGNALVVWVTACEARRHINAIWFLNLAAADLLSCLALPILLVSTVHLNHWYFGDTACKVLPSLILLNMYTSILLLATISADRLLLVLSPIWCQRFRGGCLAWTACGLAWVLALLLSSPSFLYRRTHNEHFSFKVYCVTDYGRDISKERAVALVRLLVGFIVPLITLTACYTFLLLRTWSRKATRSAKTVKVVVAVVSSFFVFWLPYQVTGILLAWHSPNSATYRNTKALDAVCVAFAYINCCINPIIYVVAGHGFQGRLLKSLPSVLRNVLTE...
null
null
chemotaxis [GO:0006935]; inflammatory response [GO:0006954]; mRNA transcription by RNA polymerase II [GO:0042789]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of epithelial cell prolife...
apical part of cell [GO:0045177]; basolateral plasma membrane [GO:0016323]; cytoplasmic vesicle [GO:0031410]
complement component C5a receptor activity [GO:0004878]; G protein-coupled receptor activity [GO:0004930]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: Sulfation plays a critical role in the association of C5aR with C5a, but no significant role in the ability of the receptor to transduce a signal and mobilize calcium in response to a small peptide agonist. {ECO:0000250|UniProtKB:P21730}.; PTM: Phosphorylated on serine residues in response to C5a binding, resultin...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9576615}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21730}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P21730}. Note=Phosphorylated C5aR colocalizes with ARRB1 and ARRB2 in cytoplasmic vesicles. {ECO:0000250|UniProtKB:P21730}.
null
null
null
null
null
FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a (PubMed:9576615). The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events. Receptor acti...
Cavia porcellus (Guinea pig)
O70131
NINJ1_MOUSE
MESGTEEYELNGDLRPGSPGSPDALPPRWGLRNRPINVNHYANKKSAAESMLDIALLMANASQLKAVVEQGNDFAFFVPLVVLISISLVLQIGVGVLLIFLVKYDLNNPAKHAKLDFLNNLATGLVFIIVVVNIFITAFGVQKPVMDVAPRQ
null
null
angiogenesis [GO:0001525]; behavior [GO:0007610]; cell adhesion [GO:0007155]; heterotypic cell-cell adhesion [GO:0034113]; hyaloid vascular plexus regression [GO:1990384]; inflammatory response [GO:0006954]; killing of cells of another organism [GO:0031640]; leukocyte chemotaxis involved in inflammatory response [GO:00...
extracellular region [GO:0005576]; filopodium membrane [GO:0031527]; plasma membrane [GO:0005886]; synaptic membrane [GO:0097060]
cell adhesion mediator activity [GO:0098631]; cell-cell adhesion mediator activity [GO:0098632]; lipopolysaccharide binding [GO:0001530]; membrane destabilizing activity [GO:0140912]
PF04923;
null
Ninjurin family
PTM: [Ninjurin-1]: Cleaved by MMP9 protease to generate the Secreted ninjurin-1 form. {ECO:0000269|PubMed:23142597, ECO:0000269|PubMed:32883094}.; PTM: [Ninjurin-1]: N-linked glycosylation is required for homooligomerization. {ECO:0000269|PubMed:28067406}.
SUBCELLULAR LOCATION: [Ninjurin-1]: Cell membrane {ECO:0000269|PubMed:24917672, ECO:0000269|PubMed:27815839, ECO:0000269|PubMed:31091274, ECO:0000269|PubMed:33472215}; Multi-pass membrane protein {ECO:0000255}. Synaptic cell membrane {ECO:0000269|PubMed:27815839}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR...
null
null
null
null
null
FUNCTION: [Ninjurin-1]: Effector of necroptotic and pyroptotic programmed cell death that mediates plasma membrane rupture (cytolysis) (PubMed:19557008, PubMed:33472215, PubMed:36468682, PubMed:37196676, PubMed:37198476). Acts downstream of Gasdermin (GSDMA, GSDMB, GSDMC, GSDMD, or GSDME) or MLKL during pyroptosis or n...
Mus musculus (Mouse)
O70132
FEV_RAT
MRQSGTSQPLLINMYLPDPVGDGLFKEGKSPSWGPLSPAVQKGSGQIQLWQFLLELLADRANAGCIAWEGGHGEFKLTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMSKVHGKRYAYRFDFQGLAQACQPPPAHAHAAAAAAAAAAAAQDGALYKLPAGLAPLPFPGLSKLNLMAASAGVAPAGFSYWPGPNATAAAAATAALYPTPGLQPPPGPFGAVAAASHLGGHYH
null
null
maternal behavior [GO:0042711]; neuron fate specification [GO:0048665]; neuron maturation [GO:0042551]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcriptio...
nuclear speck [GO:0016607]; nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; RNA polymerase II cis-regulatory region sequence-sp...
PF00178;
1.10.10.10;
ETS family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
null
null
null
null
null
FUNCTION: Functions as a transcriptional regulator. May function as a transcriptional repressor. Functions in the differentiation and the maintenance of the central serotonergic neurons. May play a role in cell growth. {ECO:0000269|PubMed:10575032, ECO:0000269|PubMed:9468386}.
Rattus norvegicus (Rat)
O70133
DHX9_MOUSE
MGDIKNFLYAWCGKRKMTPAYEIRAVGNKNRQKFMCEVRVEGFNYAGMGNSTNKKDAQSNAARDFVNYLVRINEVKSEEVPAVGIVPPPPILSDTSDSTASAAEGLPAPMGGPLPPHLALKAEENNSGVESSGYGSPGPTWDRGANLKDYYSRKEEQEVQATLESEEVDLNAGLHGNWTLENAKARLNQYFQKEKIQGEYKYTQVGPDHNRSFIAEMTIYIKQLGRRIFAREHGSNKKLAAQSCALSLVRQLYHLGVIEAYSGLTKKKEGERVEPYKVFLSPDLELQLQNVVQELDLEIVPPPVDPSMPVILNIGKLAHF...
3.6.4.13
null
alternative mRNA splicing, via spliceosome [GO:0000380]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to heat [GO:0034605]; cellular response to tumor necrosis factor [GO:0071356]; circadian rhythm [GO:0007623]; CRD-mediated mRNA stabilization [GO:0070934]; DNA duplex unwinding [GO:0032508]; DNA...
actin cytoskeleton [GO:0015629]; centrosome [GO:0005813]; CRD-mediated mRNA stability complex [GO:0070937]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nuclear stress granule [GO:0097165]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; ...
3'-5' DNA helicase activity [GO:0043138]; 3'-5' DNA/RNA helicase activity [GO:0033679]; 3'-5' RNA helicase activity [GO:0034458]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; DNA replication origin bindi...
PF00270;PF00035;PF21010;PF04408;PF00271;PF07717;
1.20.120.1080;3.30.160.20;3.40.50.300;
DEAD box helicase family, DEAH subfamily
PTM: Methylated. PRMT1-mediated methylation of undefined Arg residues in the nuclear transport domain (NTD) is required for nuclear import of DHX9. {ECO:0000250|UniProtKB:Q08211}.; PTM: Phosphorylated by PRKDC; phosphorylation occurs in a RNA-dependent manner. Phosphorylated by EIF2AK2/PKR; this phosphorylation reduces...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17303075}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q08211}. Nucleus, nucleolus {ECO:0000269|PubMed:10413677}. Cytoplasm {ECO:0000250|UniProtKB:Q08211}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q08211}. Note=Nucleoplas...
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q08211};
null
null
null
null
FUNCTION: Multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and that plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation and RNA-mediated gene silencing. Requires a 3'-singl...
Mus musculus (Mouse)
O70137
ALX3_MOUSE
MDPERCAPFSVGPAAGPYAAAGDEAPGPQGTPDAAPHLHPAPPRGPRLSRFPACGPLEPYLPEPAKPPAKYLQDLGPGPVLNGGHFYEGSAEAEEKASKAASFPQLPVDCRGGPRDGPSNVQASPGPCLASLSVPLSPGLPDSMELAKTKSKKRRNRTTFSTFQLEELEKVFQKTHYPDVYAREQLALRTDLTEARVQVWFQNRRAKWRKRERYGKMQEGRNPFTTAYDISVLPRTDSHPQLQNSLWPSPGSGSPGGPCLMSPEGIPSPCMSPYSHSHGNVAGFMGVPASPAAHPGIYSIHGFPPALGGHSFEPSPDGDY...
null
null
embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:0035116]; embryonic skeletal system morphogenesis [GO:0048704]; pattern specification process [GO:0007389]; regulation of apoptotic process [GO:0042981]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcriptio...
nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
PF00046;
1.10.10.60;
Paired homeobox family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
null
null
null
null
null
FUNCTION: Transcriptional regulator with a possible role in patterning of mesoderm during development.
Mus musculus (Mouse)
O70138
MMP8_MOUSE
MFRLKTLPLLIFLHTQLANAFPVPEHLEEKNIKTAENYLRKFYNLPSNQFRSSRNATMVAEKLKEMQRFFSLAETGKLDAATMGIMEMPRCGVPDSGDFLLTPGSPKWTHTNLTYRIINHTPQLSRAEVKTAIEKAFHVWSVASPLTFTEILQGEADINIAFVSRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDSEETWTQDSKNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYGPSDNPIQPTGPSTPKACDPHLRFDATTTLRGEIYFFKDKYFWRRHPQLRTVDLNFISL...
3.4.24.34
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
cellular response to lipopolysaccharide [GO:0071222]; collagen catabolic process [GO:0030574]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; positive regulation of microglial cell activation [GO:1903980]; positive regulation of neuroinflammatory response [GO:0150078]; pos...
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; tumor necrosis factor binding [GO:0043120]; zinc ion binding [GO:0008270]
PF00045;PF00413;PF01471;
3.40.390.10;2.110.10.10;
Peptidase M10A family
null
SUBCELLULAR LOCATION: Cytoplasmic granule. Secreted, extracellular space, extracellular matrix. Note=Stored in intracellular granules and released during inflammatory conditions.
CATALYTIC ACTIVITY: Reaction=Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.; EC=3.4.24.34;
null
null
null
null
FUNCTION: Can degrade fibrillar type I, II, and III collagens. May play a role in the degradation of collagen fibers during uterine involution.
Mus musculus (Mouse)
O70143
SHC3_RAT
MLPRTKYNRFRNDSVTSVDDLLHSLSVSGSGGKVSAEPAASPYLVSGEALRKAPDDGPGSLGHLLHKVSHLKLSSSGLRGLSSAARERAGARLSGSCSAPSLAAPDGGSATPGSRAPAASMSATRKSRASDEPLPRPPRGAPHASDQVLGSGVTYVVKYLGCIEVLRSMRSLDFSTRTQVTREAISRVCEAVPGAKGAFKKRKPPSKMLSSILGKSNLQFAGMSISLTISTASLNLRTPDSKQIISNHHMRSISFASGGDPDTTDYVAYVAKDPVNRRACHILECCDGLAQDVIGSIGQAFELRFKQYLQCPSKIPALQD...
null
null
intracellular signal transduction [GO:0035556]; learning or memory [GO:0007611]; synaptic transmission, glutamatergic [GO:0035249]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
cytosol [GO:0005829]; plasma membrane [GO:0005886]; synapse [GO:0045202]
phosphotyrosine residue binding [GO:0001784]; protein tyrosine kinase activity [GO:0004713]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor binding [GO:0005102]
PF00640;PF00017;
2.30.29.30;3.30.505.10;
null
PTM: Tyrosine phosphorylated. {ECO:0000250}.
null
null
null
null
null
null
FUNCTION: Signaling adapter that couples activated growth factor receptors to signaling pathway in neurons. Involved in the signal transduction pathways of neurotrophin-activated Trk receptors in cortical neurons (By similarity). {ECO:0000250}.
Rattus norvegicus (Rat)
O70145
NCF2_MOUSE
MSLAEAIRLWNEGVLAADKKDWKGALEAFSEVQDPHSRICFNIGCVNTILENLQAAEQAFTKSINRDKHSAVAYFQRGMLYYRMEKYDLAIKDLKEALTQLRGNQLIDYKILGLQFKLFACEVLYNIALMHAKKEEWKKAEEQLALATNMKSEPRHSKIDKAMESIWKQKLFEPVVIPVGRLFRPNERQVAQLAKKDYLGKATVVASVVHQDNFSGFAPLQPQSAEPPPRPKTPEIFRALEGEAHRVLFGFVPETPEELQVMPGNIVFVLKKGSDNWATVMFNGQKGLVPCNYLEPVELRIHPQSQPQEDTSPESDIPPP...
null
null
cellular response to hormone stimulus [GO:0032870]; NADP catabolic process [GO:0006742]; phagocytosis [GO:0006909]; positive regulation of blood pressure [GO:0045777]; positive regulation of neuron apoptotic process [GO:0043525]; regulation of reactive oxygen species biosynthetic process [GO:1903426]; respiratory burst...
acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; NADPH oxidase complex [GO:0043020]
small GTPase binding [GO:0031267]; superoxide-generating NADPH oxidase activator activity [GO:0016176]
PF00564;PF00018;PF00515;PF13181;
2.30.30.40;1.25.40.10;
NCF2/NOXA1 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19878}.
null
null
null
null
null
FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). {ECO:0000250|UniProtKB:P19878}.
Mus musculus (Mouse)
O70146
TESK1_MOUSE
MAGERPPLRGPGPGEAPGEGPGGAGGGPGRGRPSSYRALRSAVSSLARVDDFDCAEKIGAGFFSEVYKVRHRQSGQVMVLKMNKLPSNRSNTLREVQLMNRLRHPNILRFMGVCVHQGQLHALTEYMNGGTLEQLLSSPEPLSWPVRLHLALDIAQGLRYLHAKGVFHRDLTSKNCLVRREDRGFTAVVGDFGLAEKIPVYREGTRKEPLAVVGSPYWMAPEVLRGELYDEKADVFAFGIVLCELIARVPADPDYLPRTEDFGLDVPAFRTLVGNDCPLPFLLLAIHCCSMEPSTRAPFTEITQHLEQILEQQPEATPLA...
2.7.12.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
actin cytoskeleton organization [GO:0030036]; establishment of vesicle localization [GO:0051650]; negative regulation of cilium assembly [GO:1902018]; negative regulation of phosphorylation [GO:0042326]; negative regulation of protein autophosphorylation [GO:0031953]; phosphorylation [GO:0016310]; podocyte cell migrati...
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase...
PF07714;
1.10.510.10;
Protein kinase superfamily, TKL Ser/Thr protein kinase family
PTM: Autophosphorylated on serine and tyrosine residues. {ECO:0000250|UniProtKB:Q63572}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15569}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63572}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15569}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q63572}. Note=Colocalizes with SPRY4 in v...
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr...
null
null
null
null
FUNCTION: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues (By similarity). Regulates the cellular cytoskeleton by enhancing actin stress fiber formation via phosphorylation of cofilin and by preventing mic...
Mus musculus (Mouse)
O70150
KCC1B_RAT
MLLLKKQTEDISSVYEIREKLGSGAFSEVMLAQERGSAHLVALKCIPKKALRGKEALVENEIAVLRRISHPNIVALEDVHESPSHLYLAMELVTGGELFDRIMERGSYTEKDASHLVGQVLGAVSYLHSLGIVHRDLKPENLLYATPFEDSKIMVSDFGLSKIQAGNMLGTACGTPGYVAPELLEQKPYGKAVDVWALGVISYILLCGYPPFYDESDPELFSQILRASYEFDSPFWDDISESAKDFIRHLLERDPQKRFTCQQALQHLWISGDAALDRDILGSVSEQIQKNFARTHWKRAFNATSFLRHIRKLGQSPEGE...
2.7.11.17
null
phosphorylation [GO:0016310]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein serine kinase activity [GO:0106310]
PF00069;
1.10.510.10;
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily
PTM: Isoform 1 and isoform 2 are phosphorylated by CAMKK1. {ECO:0000305}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p...
null
null
null
null
FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro, isoform 1 and isoform 2 phosphorylate CREB1, SYN1/synapsin I. Phosphorylates and activates CAMK1. {ECO:0000269|PubMed:9405489}.
Rattus norvegicus (Rat)
O70152
DPM1_MOUSE
MASTGASRSLAASPRPPQGRSSRQDKYSVLLPTYNERENLPLIVWLLVKSFSESAINYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPREKKLGLGTAYIHGIKHATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFITQILLRPGASDLTGSFRLYRKEVLQKLIEKCVSKGYVFQMEMIVRARQMNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT
2.4.1.83
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q8U4M3}; Note=Binds 1 divalent metal cation. {ECO:0000250|UniProtKB:Q8U4M3};
dolichol metabolic process [GO:0019348]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; GDP-mannose metabolic process [GO:0019673]; GPI anchor biosynthetic process [GO:0006506]; protein mannosylation [GO:0035268]; protein O-linked mannosylation [GO:0035269]
dolichol-phosphate-mannose synthase complex [GO:0033185]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
alcohol binding [GO:0043178]; dolichyl-phosphate beta-D-mannosyltransferase activity [GO:0004582]; dolichyl-phosphate-mannose-protein mannosyltransferase activity [GO:0004169]; mannose binding [GO:0005537]; metal ion binding [GO:0046872]
PF00535;
null
Glycosyltransferase 2 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum.
CATALYTIC ACTIVITY: Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683, ChEBI:CHEBI:58189, ChEBI:CHEBI:58211; EC=2.4.1.83; Evidence={ECO:0000305|PubMed:9535917};
null
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:9535917}.
null
null
FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose...
Mus musculus (Mouse)
O70156
OLR1_RAT
MAFDDKMKPVNGQPDQKSCGKKPKGLHLLSSTWWCPAAVTLAILCLVLSVTLIVQQTQLLQVSDLLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAANSSGPCPQDWIWHKENCYLFHGPFNWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHSTSPFWMGLHRKNPNHPWLWENGSPLSFQFFRT...
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immune system process [GO:0002376]; inflammatory response [GO:0006954]; leukocyte cell-cell adhesion [GO:0007159]; lipoprotein metabolic process [GO:0042157]; negative regulation of gene expression [GO:0010629]; response to hydrogen peroxide [GO:0042542]
extracellular region [GO:0005576]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
carbohydrate binding [GO:0030246]; identical protein binding [GO:0042802]; low-density lipoprotein particle receptor activity [GO:0005041]
PF00059;
3.10.100.10;
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PTM: N-glycosylated. {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Membrane raft {ECO:0000250}. Secreted {ECO:0000250}. Note=A secreted form also exists. Localization to membrane rafts requires palmitoylation (By similarity). {...
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FUNCTION: Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-ox...
Rattus norvegicus (Rat)