entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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O64728
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STI_ARATH
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Protein STICHEL
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MSGSRVSDLSKLHLKKELTQIRKAGRVLRDPGTTSSWKSPLDSSRSVALLETPASRNGGSSSQFPIRGESSTNRRGKEKKVFLYNWKTQKSSSEKSGLAKNGKEEEEEEEDASSWTQASVNDDDDVSDARNGGDSYRREIQSASMGFRCRDTNLASQGVSKMRKSNVGSCKKKSKKKISSSRLDCLSKYQPRDDIVARNCNAGSDDTEEELSNSEDLRKVTGASPLLLKLKQKNWSRSSSRLLRANNRKEDSSCTYNSTPALSTSSYNMYAVRNPSTVGSWDGTTTSVNDGDDELDDNLDLPGRQGCGIPCYWTKKAMKHRGGCRSCCSPSFSDTLRRTGSSILCGSQSVYRRHNRHSSGGYSKQKIACRSAQGVLPLLSYGGDGRGGSSLGTGLSDDELSTNYGELDLEAQSRLDGRRWSTSYRSQDGLEAVALDGEEEEGSTPETIRSFSQKYRPMFFEELIGQSIVVQSLMNAVKRSRIAPVYLFQGPRGTGKTSTARIFSAALNCVATEEMKPCGYCKECNDFMSGKSKDFWELDGANKKGADKVRYLLKNLPTILPRNSSMYKVFVIDECHLLPSKTWLSFLKFLENPLQKVVFIFITTDLENVPRTIQSRCQKFLFDKLKDSDIVVRLKKIASDENLDVDLHALDLIAMNADGSLRDAETMLEQLSLLGKRITTALVNELVGVVSDEKLLELLELALSSDTAETVKRARELLDLGADPIVLMSQLASLIMDIIAGTYKVVDEKYSNAFFDGRNLTEADMEGLKHALKLLSEAEKQLRVSNDRSTWFTATLLQLGSMPSPGTTHTGSSRRQSSRATDDDPASVSREVMAYKQRIGGLHFSKSASPASVIKRNGNHSHEAKPFSRVIDNNCYKSSSSSQMIESEGSIASHENSIASTMMLNQRSSEKLNDIWRKCIERCHSKTLRQLLYTHGKLISISEVEGILVAYIAFGENDIKLRAERFLSSITNSIEMVLRRSVEVRIILLPETELLVVPHQTRKPEMTNKSGHLNNIAGLNAETDVEVGSSVESRSKLPMQRIESIIREQRLETAWLQTADKDTPGSIIRVKPERNQILPQEDTYRQTNVASAISSSGLTTHQWVDELNNEVKLLKIGDNGELQENLTGTRGQHCPLSPSLLHDTNFGNNKDNLGGYESGSGRVGCNILFCWNTKKTQRRSKSKQVKGTPVRSRRNRKSRFSLFNGCAKPRKAEGNIRR
|
Acts as a key regulator of trichome branching through an endoreduplication-independent pathway.
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O64743
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BBE15_ARATH
|
Monolignol oxidoreductase AtBBE-like 15 (EC 1.1.99.-) (Berberine bridge enzyme-like 15) (AtBBE-like 15) (Protein EMBRYO SAC DEVELOPMENT ARREST 28) (Protein MATERNAL EFFECT EMBRYO ARREST 23)
|
MAFAISKRNATLFLVTLLLISVPLSSSTLQQDFVKCLVDNSDVSFPITASFFSPDQNATLFKEELESTAQNLRYLTPSNPKPVFIFEPLYETHVQAAVVCAKKLQLHLRLRSGGHDYEGLSFVAEDETPFVIVDLSKLRQVDVDLDSNSAWAHAGATIGEVYYRIQEKSQTHGFPAGLCSSLGIGGHLVGGAYGSMMRKFGLGADNVLDARIVDANGQILDRAAMGEDVFWAIRGGGGGSFGVILAWKIKLVPVPATVTVFTVTKTLEQDGTKVLYKWEQIADKLDDDLFIRVIISPASKTTKPGNRTISMSYQAQFLGDSNRLLQVMQKSFPELGLTKKDCTEMSWIKSVMYIAGFPNSAAPEALLAGKSLFKNHFKAKSDFVKEPIPVEGLEGLWERFLEEDSPLTIWNPYGGMMSRISESEIPFPHRNGTLFKIQWLSTWQDGKVSEERHMKWIREMYSYMEQYVSKNPRQAYVNYRDLDLGTNEGETDAREWGAKYYKGNFERLVKIKGEFDPDNFFRHEQSVPTKIG
|
Required for endosperm development and polar nuclei fusion. 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 alcohol (coniferin) as substrate, but is much less efficient towards cinnamyl alcohol. The electron acceptor required for these reactions is not known, but does not seem to be dioxygen.
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O64750
|
PSA2_ARATH
|
Protein PHOTOSYSTEM I ASSEMBLY 2, chloroplastic (AtPSA2) (Protein EMBRYO SAC DEVELOPMENT ARREST 3)
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MAASSSHLFALPSPASPFLSAPNRNRVRVLAKSCPENQSFDSNDSDSSSETTHKAQGDQKSVSRRQWMTACVCASAALISNSYTFVSVQSAAALDKKPGGSCRNCQGSGAVLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLVCPVCLGTGLPNNKGLLRRPGARELLEKMYNGRLLPDS
|
Involved in female gametophyte development. Required for embryo sac development. Nuclear genome-encoded factor required for the accumulation of photosystem I (PSI) during plant development. Required for light acclimation and chloroplast development.
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O64752
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JMJ15_ARATH
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Lysine-specific demethylase JMJ15 (EC 1.14.11.-) (Jumonji domain-containing protein 15) (AtJMJ15) (Protein JUMONJI 15) (Lysine-specific histone demethylase JMJ15) (Protein MATERNAL EFFECT EMBRYO ARREST 27) ([histone H3]-trimethyl-L-lysine(4) monodemethylase JMJ15)
|
MEPFSAAQNKEDKDTSVEPPRRRCHRKNKGTNVEPPSSPYHPKVLARWDPANEKRPDIGEAPVFHPTSEEFEDTLAYIEKIRPLAESFGICRIVPPSNWSPPCRLKGDSIWKNKNFPTRVQFVDLLQNRGPVKKKTPKGRKRKRGKYSRTVAPKKRNGSVSKSVSTPKATEEENFGFESGPEFTLEKFEKYAQDFKDSYFERKDNVGDPSVEEIEGEYWRIIEKETNEVKVLYGTDLENPILGSGFSKGVKIPTRRNDMDKYISSGWNLNNLARLQGSLLSFEDCEISGVQVPWLYVGMCFSTFCWHVEDNHLYSLNYHHFGEPKVWYGVPGSHATGLEKAMRKHLPDLFDEQPDLLHELVTQFSPTILKNEGVPVYRAVQNAGEYVLTFPRAYHSGFNCGFNCAEAVNVAPVDWLAHGQNAVEIYSQETRKTSLSHDKILLGAAFEAVKSLSAHGEDNTKRFSWKRFCGKDGIITKAIEARLRMEEKRIEALGNGFSLVKMDKDFDSNCERECISCFSDLHLSATGCKNCSSLEEYGCTKHDICSCEGKDRFIFLRYTIDELSSLVRALEGESDDLKAWLSKVMEGCSETQKGESSGIIVKEKQVQEECFDLNGECNKSSEICEDASIMDLAAYHVEPINLGFLVVGKLWCNKHAIFPKGFKSRVKFYNVQDPMRISYYVSEIVDAGLLGPLFKVTLEESQDESFSYASPQKCWEMVLLRVKEEIMRRSNQKQDVHMLESIDGLKMFGFRSPFIVQATEALDPNHGQVEYWNHKNEKDSLEMKDCFMSNSSQSLSKARLFGVDLN
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Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a specific activity for H3K4me3. No activity on H3K4me2, H3K4me1, H3K9me3/2, H3K27me3/2 and H3K36me3/2. Involved in the control of flowering time by demethylating H3K4me3 at the FLC locus and repressing its expression. The repression of FLC level and reduction in H3K4me3 at the FLC locus results in induction of the flowering activator FT, which is a downstream target of FLC. Promotes salt tolerance by down-regulating the expression of several transcriptions factors involved in stress responses via H3K4me3 and H3K4me2 demethylation.
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O64763
|
ATL9_ARATH
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E3 ubiquitin-protein ligase ATL9 (EC 2.3.2.27) (RING-H2 finger protein ATL9) (RING-type E3 ubiquitin transferase ATL9)
|
MAILDTKSSRWIPHNLLFLLLLLLLQSVPYGFGQTQTTPPGTTKTKPNDPVVVVITVLFLVIFFMVFGSIFCRRSNAQFSRSSIFRSTDADAESQVVRIRRLTARGLDAEAIETFPTFLYSEVKAVRIGKGGVECAVCLCEFEDDETLRLMPPCCHVFHADCVDVWLSEHSTCPLCRADLVLNQQGDDDDSTESYSGTDPGTISSSTDPERGMVLESSDAHLLDAVTWSNSNITPRSKSTGLSSWQITGILFPRSHSTGHSLIQPAGNLDRFTLRLPDDVRRQLMKTSRTMGHVALLPQARSSRSGYRSGSVGSERSAFPYGRKSNNNNRRLHSLSFSFSFRSGSVRSTFSGDAPKNLPTSIEAGERSFERLRPDERV
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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.
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O64765
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UAP2_ARATH
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UDP-N-acetylglucosamine diphosphorylase 2 (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridylyltransferase 2) (UDP-N-acetylgalactosamine diphosphorylase 2) (EC 2.7.7.83) (UTP--glucose-1-phosphate uridylyltransferase 2) (EC 2.7.7.9)
|
MKEPTTEIEIETSAVATILPPPLPPTASPHQALVERLKDYGQEDVFSLWDELSPEERDLLLRDIENLDLPRIDRIIRCSLHSQGLPVAAIEPVPENCVSTVEERTKEDREKWWKMGLKAIYEGKLGVVLLSGGQGTRLGSSDPKGCYNIGLPSGKSLFQIQAERILCVQRLASQAMSEASPTRPVTIQWYIMTSPFTHEPTQKFFKSHKYFGLEPDQVTFFQQGTLPCISKDGKFIMETPFSLSKAPDGNGGVYTALKSSRLLEDMASRGIKYVDCYGVDNVLVRVADPTFLGYFIDKSAASAAKVVRKAYPQEKVGVFVRRGKGGPLTVVEYTELDQSMASATNQQTGRLQYCWSNVCLHMFTLDFLNQVANGLEKDSVYHLAEKKIPSINGDIVGLKLEQFIFDCFPYAPSTALFEVLREEEFAPVKNANGSNYDTPESARLLVLRLHTRWVIAAGGFLTHSVPLYATGVEVSPLCSYAGENLEAICRGRTFHAPCEISL
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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. Acts redundantly with GLCNAC1PUT1. Required for gametogenesis and embryo development.
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O64782
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SD129_ARATH
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G-type lectin S-receptor-like serine/threonine-protein kinase SD1-29 (EC 2.7.12.1) (Protein LIPOOLIGOSACCHARIDE-SPECIFIC REDUCED ELICITATION) (S-domain-1 (SD1) receptor kinase 29) (SD1-29)
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MGMVLFACLLLLIIFPTCGYAAINTSSPLSIRQTLSSPGGFYELGFFSPNNTQNQYVGIWFKKIVPRVVVWVANRDTPVTSSAANLTISSNGSLILLDGKQDVIWSTGKAFTSNKCHAELLDTGNFVVIDDVSGNKLWQSFEHLGNTMLPQSSLMYDTSNGKKRVLTTWKSNSDPSPGEFSLEITPQIPTQGLIRRGSVPYWRCGPWAKTRFSGISGIDASYVSPFSVVQDTAAGTGSFSYSTLRNYNLSYVTLTPEGKMKILWDDGNNWKLHLSLPENPCDLYGRCGPYGLCVRSDPPKCECLKGFVPKSDEEWGKGNWTSGCVRRTKLSCQAKSSMKTQGKDTDIFYRMTDVKTPDLHQFASFLNAEQCYQGCLGNCSCTAFAYISGIGCLVWNGELADTVQFLSSGEFLFIRLASSELAGSSRRKIIVGTTVSLSIFLILVFAAIMLWRYRAKQNDAWKNGFERQDVSGVNFFEMHTIRTATNNFSPSNKLGQGGFGPVYKGKLVDGKEIGVKRLASSSGQGTEEFMNEITLISKLQHRNLVRLLGYCIDGEEKLLIYEFMVNKSLDIFIFDPCLKFELDWPKRFNIIQGIARGLLYLHRDSRLRVIHRDLKVSNILLDDRMNPKISDFGLARMFQGTQYQDNTRRVVGTLGYMSPEYAWAGLFSEKSDIYSFGVLMLEIISGKRISRFIYGDESKGLLAYTWDSWCETGGSNLLDRDLTDTCQAFEVARCVQIGLLCVQHEAVDRPNTLQVLSMLTSATDLPVPKQPIFAVHTLNDMPMLQANSQDFLSVNEMTESMIQGR
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S-domain receptor protein kinase involved in lipopolysaccharide (LPS) sensing. Specifically detects LPS of Pseudomonas and Xanthomonas species. LPS are major components of the outer membrane of Gram-negative bacteria and are important microbe-associated molecular patterns (MAMPs) that trigger biphasic production of reactive oxygen species (ROS) and immune responses in plants. Seems to be only partially associated with the second LPS-triggered ROS burst. Mediates defense signaling in response to the medium-chain 3-hydroxy fatty acid 3-OH-C10:0, a pathogen-associated molecular pattern (PAMP) which induces autophosphorylation at Tyr-600. Autophosphorylation at Tyr-600 is required for downstream phosphorylation of the receptor-like cytoplasmic kinase PBL34, PBL35 and PBL36, and activation of plant immunity. (Microbial infection) Targeted by the bacterial type III effector protein tyrosine phosphatase HopAO1 from Pseudomonas syringae. HopAO1 dephosphorylates Tyr-600, which suppresses the immune response.
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O64816
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CSK2P_ARATH
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Casein kinase II subunit alpha-4, chloroplastic (CK2-alpha4) (EC 2.7.11.1) (Plastid-targeted casein kinase 2 alpha) (cpCK2alpha)
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MALRPCTGFTISSLRNASAANNNLFSLLSFSSSSPAKRNLLLSSLQDNLRRFASSASLYRQHLRNQQQQHQQQQQSRVKEKSETLAQKIGKSIRRAGAPSKARVYADVNVVRPKDYWDYESLAVQWGVQDDYEVVRKVGRGKYSEVFEGIHATDNEKCVIKILKPVKKKKIKREIKILQNLCGGPNIVKLLDIVRDQQSKTPSLIFEHVNNKDFKVLYPTLSDYDVRYYIFELLKALDFCHSRGIMHRDVKPHNVMIDHEQRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDLQDYDYSLDLWSLGCMFAGMIFRKEPFFYGHDNYDQLVKIAKVLGTDELNAYLNKYRIELDPNLTSLVGRHSRKPWTKFINSENQHLAVPEAVDFVDKLLRYDHQERPTAKEAMAHPYFYPIRNAESSRTPRSQ
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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. Involved in the regulation of plant growth and flowering time. Involved in retrograde signaling in plant responses to abscisic acid (ABA) and heat stress. May act as an enhancing factor in abiotic stress signaling through modulation of the expression of some molecular players in retrograde signaling. Phosphorylates RuBisCo activase (RCA) at Thr-78.
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O64817
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CSK23_ARATH
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Casein kinase II subunit alpha-3 (CK II) (EC 2.7.11.1)
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MSKARVYTDVNVVRPKEYWDYESLVVQWGHQDDYEVVRKVGRGKYSEVFEGKNVNTNERCVIKILKPVKKKKIKREIKILQNLCGGPNIVKLYDIVRDEHSKTPSLVFEFVNSVDFKVLYPTLTDYDIRYYIYELLKALDFCHSQGIMHRDVKPHNVMIDHQLRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDLQDYDYSLDMWSLGCMFAGMIFRKEPFFYGHDNHDQLVKIAKVLGTNELDHYLNKYQLDLDPQLEALVGRHVPKPWSKFINADNQHLVSPEAIDFLDKLLQYDHQDRLTAREAMDHPYFAQVKAAESSRLRTQ
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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 circadian clock component that maintains the correct period length through phosphorylation of CCA1.
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O64825
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LYK4_ARATH
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LysM domain receptor-like kinase 4 (LysM-containing receptor-like kinase 4) (EC 2.7.11.1)
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MISFSFHLLVFILLSLSSFATAQQPYVGISTTDCSVSDNTTSVFGYSCNGLNKTCQAYVIFRSTPSFSTVTSISSLFSVDPSLVSSLNDASPSTSFPSGQQVIIPLTCSCTGDDSQSNITYTIQPNDSYFAIANDTLQGLSTCQALAKQNNVSSQSLFPGMRIVVPIRCACPTAKQINEDGVKYLMSYTVVFEDTIAIISDRFGVETSKTLKANEMSFENSEVFPFTTILIPLVNPPANTNSLIPPPPPPPPQSVSPPPLSPDGRKSKKKTWVYALAGVLGGALVLSVIGAAIFCLSKKKTKTQTQEETGNLDSFMGKKPPMSDQEFDPLDGLSGMVVESLKVYKFHELQSATSDFTSSSSIGGSGYIGKINGDGAMIKKIEGNASEEVNLLSKLNHLNIIRLSGFCFHEGDWYLVYEHASNGSLSEWIHTTKSLLSLTQKLQIALDIATGLNYLHNFADPPYVHRDLNSNNVFLDLEFRAKIGSLGSARSTTEDFVLTKHVEGTRGYLAPEYLEHGLVSTKLDVYAFGVVLLEIVTGKEASELKKEIDEGKAIDEILIHGRLLPEGLTSFVERLVVDCLKKDHLNRPSMDENVMSLSKILAATQNWEESSY
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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 to the bacterial pathogen the bacterial pathogen Pseudomonas syringae pv tomato DC3000, probably by sensing microbe-associated molecular pattern (MAMP) and pathogen-associated molecular patterns (PAMP). May play a role in detecting peptidoglycans (e.g. PGNs) during bacterial growth.
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O64827
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SUVR5_ARATH
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Histone-lysine N-methyltransferase SUVR5 (EC 2.1.1.-) (C2H2 zinc finger-SET histone methyltransferase) (Protein C2H2 SET) (Protein SET DOMAIN GROUP 6) (Suppressor of variegation 3-9-related protein 5) (Su(var)3-9-related protein 5)
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MEVKMDELVLDVDVEEATGSELLVKSEPEADLNAVKSSTDLVTVTGPIGKNGEGESSPSEPKWLQQDEPIALWVKWRGKWQAGIRCAKADWPLTTLRGKPTHDRKKYCVIFFPHTKNYSWADMQLVRSINEFPDPIAYKSHKIGLKLVKDLTAARRYIMRKLTVGMFNIVDQFPSEVVSEAARDIIIWKEFAMEATRSTSYHDLGIMLVKLHSMILQRYMDPIWLENSFPLWVQKCNNAVNAESIELLNEEFDNCIKWNEVKSLSESPMQPMLLSEWKTWKHDIAKWFSISRRGVGEIAQPDSKSVFNSDVQASRKRPKLEIRRAETTNATHMESDTSPQGLSAIDSEFFSSRGNTNSPETMKEENPVMNTPENGLDLWDGIVVEAGGSQFMKTKETNGLSHPQDQHINESVLKKPFGSGNKSQQCIAFIESKGRQCVRWANEGDVYCCVHLASRFTTKSMKNEGSPAVEAPMCGGVTVLGTKCKHRSLPGFLYCKKHRPHTGMVKPDDSSSFLVKRKVSEIMSTLETNQCQDLVPFGEPEGPSFEKQEPHGATSFTEMFEHCSQEDNLCIGSCSENSYISCSEFSTKHSLYCEQHLPNWLKRARNGKSRIISKEVFVDLLRGCLSREEKLALHQACDIFYKLFKSVLSLRNSVPMEVQIDWAKTEASRNADAGVGEFLMKLVSNERERLTRIWGFATGADEEDVSLSEYPNRLLAITNTCDDDDDKEKWSFSGFACAICLDSFVRRKLLEIHVEERHHVQFAEKCMLLQCIPCGSHFGDKEQLLVHVQAVHPSECKSLTVASECNLTNGEFSQKPEAGSSQIVVSQNNENTSGVHKFVCKFCGLKFNLLPDLGRHHQAEHMGPSLVGSRGPKKGIRFNTYRMKSGRLSRPNKFKKSLGAVSYRIRNRAGVNMKRRMQGSKSLGTEGNTEAGVSPPLDDSRNFDGVTDAHCSVVSDILLSKVQKAKHRPNNLDILSAARSACCRVSVETSLEAKFGDLPDRIYLKAAKLCGEQGVQVQWHQEGYICSNGCKPVKDPNLLHPLIPRQENDRFGIAVDAGQHSNIELEVDECHCIMEAHHFSKRPFGNTAVLCKDISFGKESVPICVVDDDLWNSEKPYEMPWECFTYVTNSILHPSMDLVKENLQLRCSCRSSVCSPVTCDHVYLFGNDFEDARDIYGKSMRCRFPYDGKQRIILEEGYPVYECNKFCGCSRTCQNRVLQNGIRAKLEVFRTESKGWGLRACEHILRGTFVCEYIGEVLDQQEANKRRNQYGNGDCSYILDIDANINDIGRLMEEELDYAIDATTHGNISRFINHSCSPNLVNHQVIVESMESPLAHIGLYASMDIAAGEEITRDYGRRPVPSEQENEHPCHCKATNCRGLLS
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Histone methyltransferase that functions together with its binding partner LDL1/SWP1 as one of the regulators of flower timing in Arabidopsis. Mediates H3K9me2 deposition and regulates gene expression in a DNA methylation-independent manner. Binds DNA through its zinc fingers and represses the expression of a subset of stimulus response genes. May represent a novel mechanism for plants to regulate their chromatin and transcriptional state, which may allow for the adaptability and modulation necessary to rapidly respond to environment or developmental cues.
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O64879
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BGL15_ARATH
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Beta-glucosidase 15 (AtBGLU15) (EC 3.2.1.21)
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MRGNYLSLLVVLIVLASNDVLANNNSSTPKLRRSDFPEDFIFGSATSAYQVEGGAHEDGRGPSIWDTFSEKYPEKIKDGSNGSVADNSYHLYKEDVALLHQIGFNAYRFSISWSRILPRGNLKGGINQAGIDYYNNLINELLSKGIKPFATMFHWDTPQALEDAYGGFRGAEIVNDFRDYADICFKNFGDRVKHWMTLNEPLTVVQQGYVAGVMAPGRCSKFTNPNCTDGNGATEPYIVGHNLILSHGAAVQVYREKYKASQQGQVGIALNAGWNLPYTESPKDRLAAARAMAFTFDYFMEPLVTGKYPVDMVNNVKGRLPIFTAQQSKMLKGSYDFIGINYYSSTYAKDVPCSTKDVTMFSDPCASVTGERDGVPIGPKAASDWLLIYPKGIRDLVLYAKYKFKDPVMYITENGRDEFSTNKIFLKDGDRIDYYARHLEMVQDAISVGANVKGFFAWSLLDNFEWAMGYTVRFGLVYVDFKDGCKRYPKKSAEWFRKLLNEKKND
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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.
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O64883
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BGL26_ARATH
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Beta-glucosidase 26, peroxisomal (AtBGLU26) (EC 3.2.1.21) (Protein PENETRATION 2)
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MAHLQRTFPTEMSKGRASFPKGFLFGTASSSYQYEGAVNEGARGQSVWDHFSNRFPHRISDSSDGNVAVDFYHRYKEDIKRMKDINMDSFRLSIAWPRVLPYGKRDRGVSEEGIKFYNDVIDELLANEITPLVTIFHWDIPQDLEDEYGGFLSEQIIDDFRDYASLCFERFGDRVSLWCTMNEPWVYSVAGYDTGRKAPGRCSKYVNGASVAGMSGYEAYIVSHNMLLAHAEAVEVFRKCDHIKNGQIGIAHNPLWYEPYDPSDPDDVEGCNRAMDFMLGWHQHPTACGDYPETMKKSVGDRLPSFTPEQSKKLIGSCDYVGINYYSSLFVKSIKHVDPTQPTWRTDQGVDWMKTNIDGKQIAKQGGSEWSFTYPTGLRNILKYVKKTYGNPPILITENGYGEVAEQSQSLYMYNPSIDTERLEYIEGHIHAIHQAIHEDGVRVEGYYVWSLLDNFEWNSGYGVRYGLYYIDYKDGLRRYPKMSALWLKEFLRFDQEDDSSTSKKEEKKESYGKQLLHSVQDSQFVHSIKDSGALPAVLGSLFVVSATVGTSLFFKGANN
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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. Component of an inducible preinvasion resistance mechanism that prevents penetration of the nonhost fungal species B.graminis and E.pisi. Involved in indole glucosinolate (IGS) activation during pattern-triggered immunity (PTI). Functions as myrosinase for the breakdown of flg22-triggered IGS. Required for both callose deposition and glucosinolate activation during pathogen-triggered resistance. During fungal attack, required for IGS activation that mediates broad-spectrum antifungal defense.
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O64884
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OFT20_ARATH
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O-fucosyltransferase 20 (O-FucT-20) (EC 2.4.1.-) (O-fucosyltransferase family protein)
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MALSKNSNSNSFNKKKVSYISVPSQIINSLSSSSLQSLLVSPKKSSRSTNRFSFSYRNPRIWFFTLFLVSLFGMLKLGFNVDPISLPFSRYPCSTTQQPLSFDGEQNAASHLGLAQEPILSTGSSNSNAIIQLNGGKNETLLTEGDFWKQPDGLGFKPCLGFTSQYRKDSNSILKNRWKYLLVVVSGGMNQQRNQIVDAVVIARILGASLVVPVLQVNVIWGDESEFADIFDLEHFKDVLADDVHIVSSLPSTHVMTRPVEEKRTPLHASPQWIRAHYLKRINRERVLLLRGLDSRLSKDLPSDLQKLRCKVAFQALRFSPRILELGNKLASRMRNQGQYLSLHLRMEKDVWVRTGCLPGLTPEYDEIVNSERERHPELLTGRSNMTYHERKLAGLCPLTALEVTRLLKALEAPKDARIYWAGGEPLGGKEVLEPLTKEFPQFYNKHDLALPGELEPFANKASVMAAIDYIVCEKSDVFIPSHGGNMGHALQGQRAYAGHKKYITPNKRQMLPYFMNSSLPESDFNRIVKDLHRESLGQPELRMSKAGKDVTKHPVPECMCSDRQQQEQQSDA
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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}.
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O64903
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NDK2_ARATH
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Nucleoside diphosphate kinase II, chloroplastic (NDK II) (NDP kinase II) (NDPK II) (NDPK Ia) (EC 2.7.4.6)
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MVGATVVSKWTPLCVASPPERNSASLNPHCSPARVNFRTALAAFRPQFRLFSRNSASRRRLRASSSAESGIFLPHLVASMEDVEETYIMVKPDGIQRGLVGEIISRFEKKGFKLIGLKMFQCPKELAEEHYKDLSAKSFFPNLIEYITSGPVVCMAWEGVGVVASARKLIGKTDPLQAEPGTIRGDLAVQTGRNIVHGSDSPENGKREIGLWFKEGELCKWDSALATWLRE
|
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 hydrogen peroxide-mediated MAP kinase signaling.
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O64948
|
LONP2_ARATH
|
Lon protease homolog 2, peroxisomal (EC 3.4.21.53)
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MAETVELPSRLAILPFRNKVLLPGAIIRIRCTSHSSVTLVEQELWQKEEKGLIGILPVRDDAEGSSIGTMINPGAGSDSGERSLKFLVGTTDAQKSDAKDQQDLQWHTRGVAARALHLSRGVEKPSGRVTYVVVLEGLSRFNVQELGKRGPYSVARITSLEMTKAELEQVKQDPDFVALSRQFKTTAMELVSVLEQKQKTGGRTKVLLETVPIHKLADIFVASFEMSFEEQLSMLDSVDLKVRLSKATELVDRHLQSIRVAEKITQKVEGQLSKSQKEYLLRQQMRAIKEELGDNDDDEDDVAALERKMQAAGMPSNIWKHAQRELRRLKKMQPQQPGYNSSRVYLELLADLPWDKASEEHELDLKAAKERLDSDHYGLAKVKQRIIEYLAVRKLKPDARGPVLCFVGPPGVGKTSLASSIAAALGRKFVRLSLGGVKDEADIRGHRRTYIGSMPGRLIDGLKRVGVCNPVMLLDEIDKTGSDVRGDPASALLEVLDPEQNKSFNDHYLNVPYDLSKVVFVATANRVQPIPPPLLDRMELIELPGYTQEEKLKIAMRHLIPRVLDQHGLSSEFLKIPEAMVKNIIQRYTREAGVRSLERNLAALARAAAVMVAEHEQSLPLSKDVQKLTSPLLNGRMAEGGEVEMEVIPMGVNDHEIGGTFQSPSALVVDETMLEKILGPPRFDDSEAADRVASAGVSVGLVWTTFGGEVQFVEATSMVGKGEMHLTGQLGDVIKESAQLALTWVRARASDFKLALAGDMNVLDGRDIHIHFPAGAVPKDGPSAGVTLVTALVSLFSQKRVRADTAMTGEMTLRGLVLPVGGIKDKILAAHRYGIKRVILPQRNSKDLVEVPAAVLSSLEVILAKRMEDVLENAFEGGCPWRNNYSKL
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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-Rule:MF_03121, ECO:0000269|PubMed:19748917}.
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O64961
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TPS9_SOLLC
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Sesquiterpene synthase 9 (SlTPS9) (Terpene synthase 9) (Beta-myrcene synthase TPS9) (EC 4.2.3.15) (Germacrene C synthase TPS9) (EC 4.2.3.60) (Limonene synthase TPS9) (EC 4.2.3.-) (Sesquiterpene synthase 1) (Terpinolene synthase TPS9) (EC 4.2.3.113)
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MAASSADKCRPLANFHPSVWGYHFLSYTHEITNQEKVEVDEYKETIRKMLVETCDNSTQKLVLIDAMQRLGVAYHFDNEIETSIQNIFDASSKQNDNDNNLYVVSLRFRLVRQQGHYMSSDVFKQFTNQDGKFKETLTNDVQGLLSLYEASHLRVRNEEILEEALTFTTTHLESIVSNLSNNNNSLKVEVGEALTQPIRMTLPRMGARKYISIYENNDAHHHLLLKFAKLDFNMLQKFHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVLNLTSIIDDTFDAYATFDELVTFNDAIQRWDANAIDSIQPYMRPAYQALLDIYSEMEQVLSKEGKLDRVYYAKNEMKKLVRAYFKETQWLNDCDHIPKYEEQVENAIVSAGYMMISTTCLVGIEEFISHETFEWLMNESVIVRASALIARAMNDIVGHEDEQERGHVASLIECYMKDYGASKQETYIKFLKEVTNAWKDINKQFFRPTEVPMFVLERVLNLTRVADTLYKEKDTYTNAKGKLKNMINSILIESVKI
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Involved in the biosynthesis of germacrene C, one of the most abundant sesquiterpene in the leaf oil of tomato. 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 diphosphate ((EE)-FPP) and (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP). No or low activity with geranylgeranyl diphosphate (GGPP). Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, limonene and terpinolene.
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O64973
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RPS5_ARATH
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Disease resistance protein RPS5 (Resistance to Pseudomonas syringae protein 5) (pNd3/pNd10)
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MGGCFSVSLPCDQVVSQFSQLLCVRGSYIHNLSKNLASLQKAMRMLKARQYDVIRRLETEEFTGRQQRLSQVQVWLTSVLIIQNQFNDLLRSNEVELQRLCLCGFCSKDLKLSYRYGKRVIMMLKEVESLSSQGFFDVVSEATPFADVDEIPFQPTIVGQEIMLEKAWNRLMEDGSGILGLYGMGGVGKTTLLTKINNKFSKIDDRFDVVIWVVVSRSSTVRKIQRDIAEKVGLGGMEWSEKNDNQIAVDIHNVLRRRKFVLLLDDIWEKVNLKAVGVPYPSKDNGCKVAFTTRSRDVCGRMGVDDPMEVSCLQPEESWDLFQMKVGKNTLGSHPDIPGLARKVARKCRGLPLALNVIGEAMACKRTVHEWCHAIDVLTSSAIDFSGMEDEILHVLKYSYDNLNGELMKSCFLYCSLFPEDYLIDKEGLVDYWISEGFINEKEGRERNINQGYEIIGTLVRACLLLEEERNKSNVKMHDVVREMALWISSDLGKQKEKCIVRAGVGLREVPKVKDWNTVRKISLMNNEIEEIFDSHECAALTTLFLQKNDVVKISAEFFRCMPHLVVLDLSENQSLNELPEEISELASLRYFNLSYTCIHQLPVGLWTLKKLIHLNLEHMSSLGSILGISNLWNLRTLGLRDSRLLLDMSLVKELQLLEHLEVITLDISSSLVAEPLLCSQRLVECIKEVDFKYLKEESVRVLTLPTMGNLRKLGIKRCGMREIKIERTTSSSSRNKSPTTPCFSNLSRVFIAKCHGLKDLTWLLFAPNLTFLEVGFSKEVEDIISEEKAEEHSATIVPFRKLETLHLFELRGLKRIYAKALHFPCLKVIHVEKCEKLRKLPLDSKSGIAGEELVIYYGEREWIERVEWEDQATQLRFLPSSRWRWRET
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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 protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Requires PBS1 to trigger the defense reaction against avrPphB. In case of infection by Pseudomonas syringae, AvrPphB triggers RPS5-mediated defense mechanism via the cleavage of PBS1, suggesting that the cleavage of PBS1 could trigger an exchange of ADP for ATP, thereby activating RPS5. May function as a fine-tuned sensor of alterations in the structure of the effector target PBS1.
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O64989
|
C90B1_ARATH
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Steroid (22S)-hydroxylase (EC 1.14.14.178) ((22S)-22-hydroxycampesterol synthase) (6-deoxycathasterone synthase) (Cathasterone synthase) (Cytochrome P450 90B1) (AtCYP90B1) (Protein DWARF 4) (Dwarf4) (Steroid 22-alpha-hydroxylase)
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MFETEHHTLLPLLLLPSLLSLLLFLILLKRRNRKTRFNLPPGKSGWPFLGETIGYLKPYTATTLGDFMQQHVSKYGKIYRSNLFGEPTIVSADAGLNRFILQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRDMRSISLNFLSHARLRTILLKDVERHTLFVLDSWQQNSIFSAQDEAKKFTFNLMAKHIMSMDPGEEETEQLKKEYVTFMKGVVSAPLNLPGTAYHKALQSRATILKFIERKMEERKLDIKEEDQEEEEVKTEDEAEMSKSDHVRKQRTDDDLLGWVLKHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQACPKAVEELREEHLEIARAKKELGESELNWDDYKKMDFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVISAVHLDNSRYDQPNLFNPWRWQQQNNGASSSGSGSFSTWGNNYMPFGGGPRLCAGSELAKLEMAVFIHHLVLKFNWELAEDDKPFAFPFVDFPNGLPIRVSRIL
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Catalyzes the C22-alpha-hydroxylation step in brassinosteroids biosynthesis. 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). Can also use cholesterol and cholestanol as substrates.
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O65020
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ETO1_ARATH
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Ethylene-overproduction protein 1 (Protein ETHYLENE OVERPRODUCER 1) (Protein ETO1)
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MRSLKLAEGCKGTQVYALNPSAPTPPPPPGNSSTGGGGGGGSGGGTGGVGDKLLQHLSDHLRVNSVRSKSSRTYPPPTQPNAVVSPEFLLPCGLPVTDLLEPQIDPCLKFVDLVEKMAQVYRRIENCSQFEKSGAYLEQCAIFRGISDPKLFRRSLRSSRQHAVDVHAKVVLASWLRFERREDELIGTTSMDCCGRNLECPKATLVSGYDPESVYDPCVCSGASRSEMMNEDECSTSQEVDYDMSFCIGDEEVRCVRYKIASLSRPFKAMLYGGFREMKRATINFTQNGISVEGMRAAEIFSRTNRLDNFPPNVVLELLKLANRFCCDELKSACDSHLAHLVNSLDEAMLLIEYGLEEAAYLLVAACLQVFLRELPSSMHNPNVIKIFCSAEGRERLASLGHASFTLYFFLSQIAMEDDMKSNTTVMLLERLVECAVDSWEKQLAYHQLGVVMLERKEYKDAQRWFNAAVEAGHLYSLVGVARTKFKRDHRYSAYKIINSLISDHKATGWMHQERSLYCSGKEKLLDLDTATEFDPTLTFPYKFRAVALVEENQFGAAIAELNKILGFKASPDCLEMRAWISIGMEDYEGALKDIRALLTLEPNFMMFNWKIHGDHMVELLRPLAQQWSQADCWMQLYDRWSSVDDIGSLAVVHHMLANDPGKSLLRFRQSLLLLRLNCQKAAMRSLRLARNHSKSEHERLVYEGWILYDTGHREEALAKAEESISIQRSFEAFFLKAYALADSTLDPDSSNYVIQLLQEALKCPSDGLRKGQALNNLGSVYVDCEKLDLAADCYTNALTIKHTRAHQGLARVYHLKNQRKAAYDEMTKLIEKAQNNASAYEKRSEYCDREMAQSDLCLATQLDPLRTYPYRYRAAVLMDDHKESEAIDELSRAISFKPDLQLLHLRAAFYDSMGEGASAIKDCEAALCIDPGHADTLELYHKAREPNDQK
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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.
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O65041
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UBA3_ARATH
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NEDD8-activating enzyme E1 catalytic subunit (EC 6.2.1.64) (RUB-activating enzyme) (Ubiquitin-activating enzyme E1-like protein)
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MADLDVPPQVPQSKTRDLDKLLLRHGNLVDPGFVPGPGLRDDIRDYVRILVIGAGGLGCELLKDLALSGFRNLEVIDMDRIEVTNLNRQFLFRIEDVGKPKAEVAAKRVMERVSGVEIVPHFSRIEDKEIEFYNDFNIIALGLDSIEARKYINGVACGFLEYNEDDTPKRETIKPMVDGGTEGFKGHARVILPGVTPCFECTIYLFPPQVKFPLCTLAETPRNAAHCIEYAHLIQWETVHRGKTFDPDEPEHMKWVYDEAIRRAELFGIPGVTYSLTQGVVKNIIPAIASTNAIISAACALETLKIVSACSKTLVNYLTYNGGEGLYTEVTKFERDTECLVCGPGILIELDTSVTLSKFIEMLEDHPKLLLSKASVKQGENTLYMQAPPVLEEFHRPKLSKPLYDLMGRVQKDTIHVFGQRALKNNEKESCTTKVRVVFKGADGVADMDTAIGA
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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 cysteine of RCE1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:10611386, ECO:0000269|PubMed:9624055}.
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O65201
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ACOX2_ARATH
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Acyl-coenzyme A oxidase 2, peroxisomal (AOX 2) (EC 1.3.3.6) (Long-chain acyl-CoA oxidase) (AtCX2)
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MESRREKNPMTEEESDGLIAARRIQRLSLHLSPSLTPSPSLPLVQTETCSARSKKLDVNGEALSLYMRGKHIDIQEKIFDFFNSRPDLQTPIEISKDDHRELCMNQLIGLVREAGVRPFRYVADDPEKYFAIMEAVGSVDMSLGIKMGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYTGCFAMTELHHGSNVQGLQTTATFDPLKDEFVIDTPNDGAIKWWIGNAAVHGKFATVFARLILPTHDSKGVSDMGVHAFIVPIRDMKTHQTLPGVEIQDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDVSRDGTYTSSLPTINKRFGATLGELVGGRVGLAYASVGVLKISATIAIRYSLLRQQFGPPKQPEVSILDYQSQQHKLMPMLASTYAYHFATVYLVEKYSEMKKTHDEQLVADVHALSAGLKSYVTSYTAKALSVCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKRYKEKFQGGTLTVTWSYLRESMNTYLSQPNPVTARWEGEDHLRDPKFQLDAFRYRTSRLLQNVAARLQKHSKTLGGFGAWNRCLNHLLTLAESHIETVILAKFIEAVKNCPDPSAKAALKLACDLYALDRIWKDIGTYRNVDYVAPNKAKAIHKLTEYLSFQVRNVAKELVDAFELPDHVTRAPIAMQSDAYSQYTQVVGF
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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.
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O65202
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ACOX1_ARATH
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Peroxisomal acyl-coenzyme A oxidase 1 (AOX 1) (EC 1.3.3.6) (Long-chain acyl-CoA oxidase) (AtCX1)
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MEGIDHLADERNKAEFDVEDMKIVWAGSRHAFEVSDRIARLVASDPVFEKSNRARLSRKELFKSTLRKCAHAFKRIIELRLNEEEAGRLRHFIDQPAYVDLHWGMFVPAIKGQGTEEQQKKWLSLANKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHTPTQTASKWWPGGLGKVSTHAVVYARLITNGKDYGIHGFIVQLRSLEDHSPLPNITVGDIGTKMGNGAYNSMDNGFLMFDHVRIPRDQMLMRLSKVTREGEYVPSDVPKQLVYGTMVYVRQTIVADASNALSRAVCIATRYSAVRRQFGAHNGGIETQVIDYKTQQNRLFPLLASAYAFRFVGEWLKWLYTDVTERLAASDFATLPEAHACTAGLKSLTTTATADGIEECRKLCGGHGYLWCSGLPELFAVYVPACTYEGDNVVLQLQVARFLMKTVAQLGSGKVPVGTTAYMGRAAHLLQCRSGVQKAEDWLNPDVVLEAFEARALRMAVTCAKNLSKFENQEQGFQELLADLVEAAIAHCQLIVVSKFIAKLEQDIGGKGVKKQLNNLCYIYALYLLHKHLGDFLSTNCITPKQASLANDQLRSLYTQVRPNAVALVDAFNYTDHYLNSVLGRYDGNVYPKLFEEALKDPLNDSVVPDGYQEYLRPVLQQQLRTARL
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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 involved in the biosynthesis of jasmonic acid.
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O65258
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BAM2_ARATH
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Beta-amylase 2, chloroplastic (EC 3.2.1.2) (1,4-alpha-D-glucan maltohydrolase) (Beta-amylase 9)
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MAIRLNHSVIPVSVKLGAPTRVSARSSLPFSVGDWRGVSTFSGARPLVLAKVKLRAESTEEDRVPIDDDDDSTDQLVDEEIVHFEERDFAGTACVPVYVMLPLGVIDMNSEVVEPEELLDQLRTLKSVNVDGVMVDCWWGIVESHTPQVYNWSGYKKLFQMIRELGLKIQVVMSFHECGGNVGDDVHIQIPEWVREIGQSNPDIYFTDSAGRRNTECLTWGIDKQRVLRGRTALEVYFDYMRSFRVEFDEFFEEKIIPEIEVGLGPCGELRYPSYPAQFGWKYPGIGEFQCYDKYLMNSLKEAAEVRGHSFWGRGPDNTETYNSTPHGTGFFRDGGDYDSYYGRFFLNWYSRVLIDHGDRVLAMANLAFEGTCIAAKLSGIHWWYKTASHAAELTAGFYNSSNRDGYGPIAAMFKKHDAALNFTCVELRTLDQHEDFPEALADPEGLVWQVLNAAWDASIPVASENALPCYDREGYNKILENAKPLTDPDGRHLSCFTYLRLNPTLMESQNFKEFERFLKRMHGEAVPDLGLAPGTQETNPE
|
Low beta-amylase activity. Interacts poorly with starch or other alpha-1,4-glucan.
|
O65272
|
KEA2_ARATH
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K(+) efflux antiporter 2, chloroplastic (AtKEA2)
|
MDFASSVQRQSMFHGGADFASYCLPNRMISAKLCPKGLGGTRFWDPMIDSKVRSAIRSKRNVSYRSSLTLNADFNGRFYGHLLPAKPQNVPLGFRLLCQSSDSVGDLVGNDRNLEFAEGSDDREVTFSKEEKDTREQDSAPSLEELRDLLNKATKELEVASLNSTMFEEKAQRISEVAIALKDEAASAWNDVNQTLNVVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAEGYNTSEESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAVAFELEATQRVNDAEIALQRAEKTLFGSQTQETTQGKVLDGKNTIVGEDEVLSEIVDVSHQAERDLVVVGVSSDVGTQSYESDNENGKPTADFAKEAEGEAEKSKNVVLTKKQEVQKDLPRESSSHNGTKTSLKKSSRFFPASFFSSNGDGTATVFESLVESAKQQWPKLILGFTLLGAGVAIYSNGVGRNNQLPQQPNIVSTSAEDVSSSTKPLIRQMQKLPKRIKKLLEMFPQQEVNEEEASLLDVLWLLLASVIFVPLFQKIPGGSPVLGYLAAGILIGPYGLSIIRNVHGTKAIAEFGVVFLLFNIGLELSVERLSSMKKYVFGLGSAQVLVTAAVIGLITHYVAGQAGPAAIVIGNGLALSSTAVVLQVLQERGESTSRHGRATFSVLLFQDLAVVVLLILIPLISPNSSKGGIGFQAIAEALGLAAIKAAVAITGIIAGGRLLLRPIYKQIAENRNAEIFSANTLLVILGTSLLTARAGLSMALGAFLAGLLLAETEFSLQVESDIAPYRGLLLGLFFMTVGMSIDPKLLLANFPLIMGTLGLLLVGKTILVVIIGKLFGISIISAVRVGLLLAPGGEFAFVAFGEAVNQGIMTPQLSSLLFLVVGISMALTPWLAAGGQLIASRFELQDVRSLLPVESETDDLQGHIIICGFGRIGQIIAQLLSERLIPFVALDVSSDRVAIGRSLDLPVYFGDAGSREVLHKIGADRACAAAIALDTPGANYRCVWALSKYFPNVKTFVRAHDVDHGLNLEKAGATAVVPETLEPSLQLAAAVLAQAKLPTSEIATTINEFRSRHLSELAELCEASGSSLGYGFSRSTSKPKPPSPSETSDDNQIIEGTLAI
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Electroneutral K(+)/H(+) efflux antiporter modulating monovalent cation and pH homeostasis in plastids, especially during plastid division and thylakoid membrane formation. Transports K(+) and Cs(+) preferentially relative to Na(+) or Li(+). May function in osmotic adjustment. Collaboratively with KEA1, adjusts alkaline stromal pH upon light to dark transitions in plastids. Together with KEA1, critical for chloroplast development, including chloroplast RNA-metabolism (e.g. rRNA maturation, polysome loading and RNA-protein interactions) and plastid gene expression (PGE), ion homeostasis, and photosynthesis. Contributes, during early seedling development, to the regulation of photosynthesis and abscisic acid- (ABA-) mediated primary root growth in a sucrose-dependent manner. Involved in the regulation of reactive oxygen and nitrogen species (ROS and RNS) metabolism. Required in roots for rapid hyperosmotic-induced Ca(2+) responses and for osmo-sensory potentiation in hyperosmotic conditions. May counteract resilience to drought and salt stress, involving photorespiratory pathway and stomata closure.
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O65282
|
CH20_ARATH
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20 kDa chaperonin, chloroplastic (Chaperonin 10) (Ch-CPN10) (Cpn10) (Chaperonin 20) (Protein Cpn21)
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MAATQLTASPVTMSARSLASLDGLRASSVKFSSLKPGTLRQSQFRRLVVKAASVVAPKYTSIKPLGDRVLVKIKEAEEKTLGGILLPSTAQSKPQGGEVVAVGEGRTIGKNKIDITVPTGAQIIYSKYAGTEVEFNDVKHLILKEDDIVGILETEDIKDLKPLNDRVFIKVAEAEEKTAGGLLLTETTKEKPSIGTVIAVGPGSLDEEGKITPLPVSTGSTVLYSKYAGNDFKGKDGSNYIALRASDVMAILS
|
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. Required to activate the iron superoxide dismutases (FeSOD). Involved in abscisic acid (ABA) signaling, independently of its co-chaperone role. Acts as negative regulator of the CHLH-WRKY40 coupled ABA signaling pathway, downstream of CHLH and upstream of WRKY40.
|
O65312
|
MEDEA_ARATH
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Histone-lysine N-methyltransferase MEDEA (EC 2.1.1.356) (Maternal embryogenesis control protein) (Protein EMBRYO DEFECTIVE 173) (Protein FERTILIZATION-INDEPENDENT SEED 1) (Protein SET DOMAIN GROUP 5)
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MEKENHEDDGEGLPPELNQIKEQIEKERFLHIKRKFELRYIPSVATHASHHQSFDLNQPAAEDDNGGDNKSLLSRMQNPLRHFSASSDYNSYEDQGYVLDEDQDYALEEDVPLFLDEDVPLLPSVKLPIVEKLPRSITWVFTKSSQLMAESDSVIGKRQIYYLNGEALELSSEEDEEDEEEDEEEIKKEKCEFSEDVDRFIWTVGQDYGLDDLVVRRALAKYLEVDVSDILERYNELKLKNDGTAGEASDLTSKTITTAFQDFADRRHCRRCMIFDCHMHEKYEPESRSSEDKSSLFEDEDRQPCSEHCYLKVRSVTEADHVMDNDNSISNKIVVSDPNNTMWTPVEKDLYLKGIEIFGRNSCDVALNILRGLKTCLEIYNYMREQDQCTMSLDLNKTTQRHNQVTKKVSRKSSRSVRKKSRLRKYARYPPALKKTTSGEAKFYKHYTPCTCKSKCGQQCPCLTHENCCEKYCGCSKDCNNRFGGCNCAIGQCTNRQCPCFAANRECDPDLCRSCPLSCGDGTLGETPVQIQCKNMQFLLQTNKKILIGKSDVHGWGAFTWDSLKKNEYLGEYTGELITHDEANERGRIEDRIGSSYLFTLNDQLEIDARRKGNEFKFLNHSARPNCYAKLMIVRGDQRIGLFAERAIEEGEELFFDYCYGPEHADWSRGREPRKTGASKRSKEARPAR
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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 fertilization. After fertilization, it probably also regulates the embryo and endosperm proliferation and anteroposterior organization during seed development. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Interacts with the promoter and repress the transcription of genes such as PHE1 and PHE2, that are paternally active and maternally silenced genes.
|
O65351
|
SBT17_ARATH
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Subtilisin-like protease SBT1.7 (EC 3.4.21.-) (Cucumisin-like serine protease) (Subtilase subfamily 1 member 7) (AtSBT1.7) (Subtilisin-like serine protease 1) (At-SLP1)
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MSSSFLSSTAFFLLLCLGFCHVSSSSSDQGTYIVHMAKSQMPSSFDLHSNWYDSSLRSISDSAELLYTYENAIHGFSTRLTQEEADSLMTQPGVISVLPEHRYELHTTRTPLFLGLDEHTADLFPEAGSYSDVVVGVLDTGVWPESKSYSDEGFGPIPSSWKGGCEAGTNFTASLCNRKLIGARFFARGYESTMGPIDESKESRSPRDDDGHGTHTSSTAAGSVVEGASLLGYASGTARGMAPRARVAVYKVCWLGGCFSSDILAAIDKAIADNVNVLSMSLGGGMSDYYRDGVAIGAFAAMERGILVSCSAGNAGPSSSSLSNVAPWITTVGAGTLDRDFPALAILGNGKNFTGVSLFKGEALPDKLLPFIYAGNASNATNGNLCMTGTLIPEKVKGKIVMCDRGINARVQKGDVVKAAGGVGMILANTAANGEELVADAHLLPATTVGEKAGDIIRHYVTTDPNPTASISILGTVVGVKPSPVVAAFSSRGPNSITPNILKPDLIAPGVNILAAWTGAAGPTGLASDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAYKTYKDGKPLLDIATGKPSTPFDHGAGHVSPTTATNPGLIYDLTTEDYLGFLCALNYTSPQIRSVSRRNYTCDPSKSYSVADLNYPSFAVNVDGVGAYKYTRTVTSVGGAGTYSVKVTSETTGVKISVEPAVLNFKEANEKKSYTVTFTVDSSKPSGSNSFGSIEWSDGKHVVGSPVAISWT
|
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. Essential for mucilage release from seed coats. Triggers the accumulation and/or activation of cell wall modifying enzymes necessary either for the loosening of the outer primary cell wall, or to facilitate swelling of the mucilage.
|
O65355
|
GGH2_ARATH
|
Gamma-glutamyl hydrolase 2 (AtGGH2) (EC 3.4.19.9) (Conjugase) (GH) (Gamma-Glu-X carboxypeptidase)
|
MWSYVWLPLVALSLFKDSIIMAKAATILLPSQTGFDISRSPVCSAPDPNLNYRPVIGILSHPGDGASGRLSNATDASSIAASYVKLAESGGARVIPLIFNEPEEILFQKLELVNGVILTGGWAKEGLYFEIVKKIFNKVLERNDAGEHFPIYAICLGFELLTMIISQNRDIFEKMDARNSASSLQFVENVNIQGTIFQRFPPELLKKLGTDCLVMQNHRFGISPQSFEGNIALSNFFKIVTTCVDDNGKVYVSTVQSTKYPVTGFQWHPEKNAFEWGSSKIPHSEDAIQVTQHAANHLVSEARKSLNRPESKKVLSNLIYNYKPTYCGYAGIGYDEVYIFTQQRSLL
|
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-gamma-L-glutamate substrates and is responsible for the production of folic acid, also called pteroylglutamic acid (PteGlu) from teroylpolyglutamates.
|
O65359
|
SYP41_ARATH
|
Tlg2p-like protein a (AtTLG2a) (Syntaxin-41) (AtSYP41)
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MATRNRTLLFRKYRNSLRSVRAPLSSSSLTGTRSGGVGPVIEMASTSLLNPNRSYAPISTEDPGTSSKGAITVGLPPAWVDVSEEISVNIQRARTKMAELGKAHAKALMPSFGDGKEDQHNIESLTQEITFLLKKSEKQLQRLSASGPSEDSNVRKNVQRSLATDLQLLSMELRKKQSTYLKRLRQQKEDGMDLEMNLSRNRYRPEEDDFGDMLNEHQMSKIKKSEEVSVEREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKAERTQRHGGMVKCASVLVILCFIMLLLLILKEIFL
|
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. Together with VTI12, required for membrane fusion. Vesicle trafficking protein that functions in the secretory pathway and mediates liposome fusion the fusion of phospholipid vesicles containing SYP41 and VTI12 is triggered by YKT61 and YKT62. Required for extracellular resistance responses to a fungal pathogen. Also involved in the protection of chloroplasts from salicylic acid-dependent biotic stress.
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O65375
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LRX1_ARATH
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Leucine-rich repeat extensin-like protein 1 (AtLRX1) (LRR/EXTENSIN1) (Cell wall hydroxyproline-rich glycoprotein)
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MLFPPLRSLFLFTLLLSSVCFLQIKADHDDESDLGSDIKVDKRLKFENPKLRQAYIALQSWKKAIFSDPFNFTANWNGSDVCSYNGIYCAPSPSYPKTRVVAGIDLNHADMAGYLASELGLLSDLALFHINSNRFCGEVPLTFNRMKLLYELDLSNNRFVGKFPKVVLSLPSLKFLDLRYNEFEGKIPSKLFDRELDAIFLNHNRFRFGIPKNMGNSPVSALVLADNNLGGCIPGSIGQMGKTLNELILSNDNLTGCLPPQIGNLKKVTVFDITSNRLQGPLPSSVGNMKSLEELHVANNAFTGVIPPSICQLSNLENFTYSSNYFSGRPPICAASLLADIVVNGTMNCITGLARQRSDKQCSSLLARPVDCSKFGCYNIFSPPPPTFKMSPEVRTLPPPIYVYSSPPPPPSSKMSPTVRAYSPPPPPSSKMSPSVRAYSPPPPPYSKMSPSVRAYPPPPPPSPSPPPPYVYSSPPPPYVYSSPPPPPYVYSSPPPPPYVYSSPPPPYVYSSPPPPYVYSSPPPPPPSPPPPCPESSPPPPVVYYAPVTQSPPPPSPVYYPPVTQSPPPPSPVYYPPVTNSPPPPSPVYYPPVTYSPPPPSPVYYPQVTPSPPPPSPLYYPPVTPSPPPPSPVYYPPVTPSPPPPSPVYYPPVTPSPPPPSPVYYPSETQSPPPPTEYYYSPSQSPPPTKACKEGHPPQATPSYEPPPEYSYSSSPPPPSPTSYFPPMPSVSYDASPPPPPSYY
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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.
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O65390
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APA1_ARATH
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Aspartic proteinase A1 (EC 3.4.23.-)
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MKIYSRTVAVSLIVSFLLCFSAFAERNDGTFRVGLKKLKLDSKNRLAARVESKQEKPLRAYRLGDSGDADVVVLKNYLDAQYYGEIAIGTPPQKFTVVFDTGSSNLWVPSSKCYFSLACLLHPKYKSSRSSTYEKNGKAAAIHYGTGAIAGFFSNDAVTVGDLVVKDQEFIEATKEPGITFVVAKFDGILGLGFQEISVGKAAPVWYNMLKQGLIKEPVFSFWLNRNADEEEGGELVFGGVDPNHFKGKHTYVPVTQKGYWQFDMGDVLIGGAPTGFCESGCSAIADSGTSLLAGPTTIITMINHAIGAAGVVSQQCKTVVDQYGQTILDLLLSETQPKKICSQIGLCTFDGTRGVSMGIESVVDKENAKLSNGVGDAACSACEMAVVWIQSQLRQNMTQERILNYVNELCERLPSPMGESAVDCAQLSTMPTVSLTIGGKVFDLAPEEYVLKVGEGPVAQCISGFIALDVAPPRGPLWILGDVFMGKYHTVFDFGNEQVGFAEAA
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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}.
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O65396
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GCST_ARATH
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Aminomethyltransferase, mitochondrial (EC 2.1.2.10) (Glycine cleavage system T protein) (GCVT)
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MRGGSLWQLGQSITRRLAQSDKKVVSRRYFASEADLKKTALYDFHVAHGGKMVPFAGWSMPIQYKDSIMDSTVNCRENGSLFDVAHMCGLSLKGKDCVPFLETLVVADVAGLAPGTGSLTVFTNEKGGAIDDSVITKVTDEHIYLVVNAGCRDKDLAHIEEHMKAFKSKGGDVSWHIHDERSLLALQGPLAAPVLQHLTKEDLSKLYFGNFQILDINGSTCFLTRTGYTGEDGFEISVPDEHAVDLAKAILEKSEGKVRLTGLGARDSLRLEAGLCLYGNDMEQHISPVEAGLTWAIGKRRRAEGGFLGADVILQQLKDGPTIRRVGFFSSGPPARSHSEVHDESGNKIGEITSGGFSPNLKKNIAMGYVKSGQHKTGTKVKILVRGKPYEGSITKMPFVATKYYKPT
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The glycine decarboxylase (GDC) or glycine cleavage system catalyzes the degradation of glycine.
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O65398
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GLX1_ARATH
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Lactoylglutathione lyase GLX1 (EC 4.4.1.5) (Glyoxalase I) (AtGLX1) (GlyI)
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MAEASDLLEWPKKDNRRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETSNFVVELTYNYGVSSYDIGTGFGHFAISTQDVSKLVENVRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFELIQRGPTPEPFCQVMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEEYESIVLELTYNYDVTEYTKGNAYAQIAIGTDDVYKSGEVIKIVNQELGGKITREAGPLPGLGTKIVSFLDPDGWKTVLVDNKDFLKELE
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Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
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O65440
|
BAME3_ARATH
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Leucine-rich repeat receptor-like serine/threonine-protein kinase BAM3 (EC 2.7.11.1) (Protein BARELY ANY MERISTEM 3)
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MADKIFTFFLILSSISPLLCSSLISPLNLSLIRQANVLISLKQSFDSYDPSLDSWNIPNFNSLCSWTGVSCDNLNQSITRLDLSNLNISGTISPEISRLSPSLVFLDISSNSFSGELPKEIYELSGLEVLNISSNVFEGELETRGFSQMTQLVTLDAYDNSFNGSLPLSLTTLTRLEHLDLGGNYFDGEIPRSYGSFLSLKFLSLSGNDLRGRIPNELANITTLVQLYLGYYNDYRGGIPADFGRLINLVHLDLANCSLKGSIPAELGNLKNLEVLFLQTNELTGSVPRELGNMTSLKTLDLSNNFLEGEIPLELSGLQKLQLFNLFFNRLHGEIPEFVSELPDLQILKLWHNNFTGKIPSKLGSNGNLIEIDLSTNKLTGLIPESLCFGRRLKILILFNNFLFGPLPEDLGQCEPLWRFRLGQNFLTSKLPKGLIYLPNLSLLELQNNFLTGEIPEEEAGNAQFSSLTQINLSNNRLSGPIPGSIRNLRSLQILLLGANRLSGQIPGEIGSLKSLLKIDMSRNNFSGKFPPEFGDCMSLTYLDLSHNQISGQIPVQISQIRILNYLNVSWNSFNQSLPNELGYMKSLTSADFSHNNFSGSVPTSGQFSYFNNTSFLGNPFLCGFSSNPCNGSQNQSQSQLLNQNNARSRGEISAKFKLFFGLGLLGFFLVFVVLAVVKNRRMRKNNPNLWKLIGFQKLGFRSEHILECVKENHVIGKGGRGIVYKGVMPNGEEVAVKKLLTITKGSSHDNGLAAEIQTLGRIRHRNIVRLLAFCSNKDVNLLVYEYMPNGSLGEVLHGKAGVFLKWETRLQIALEAAKGLCYLHHDCSPLIIHRDVKSNNILLGPEFEAHVADFGLAKFMMQDNGASECMSSIAGSYGYIAPEYAYTLRIDEKSDVYSFGVVLLELITGRKPVDNFGEEGIDIVQWSKIQTNCNRQGVVKIIDQRLSNIPLAEAMELFFVAMLCVQEHSVERPTMREVVQMISQAKQPNTF
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Necessary for male gametophyte development, as well as ovule specification and function. Required for the development of high-ordered vascular strands within the leaf and a correlated control of leaf shape, size and symmetry. LRR-rich receptor-like kinase (LRR-RLK) involved in the perception of CLE45 peptide ligand which mediates root growth inhibition by repressing protophloem differentiation this mechanism requires CRN. BRX, BAM3, and CLE45 act together to regulate the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem. Necessary for CLE45 peptide-triggered accumulation of MAKR5 in developing sieve elements.
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O65493
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XCP1_ARATH
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Cysteine protease XCP1 (EC 3.4.22.-) (Xylem cysteine peptidase 1) (AtXCP1)
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MAFSAPSLSKFSLLVAISASALLCCAFARDFSIVGYTPEHLTNTDKLLELFESWMSEHSKAYKSVEEKVHRFEVFRENLMHIDQRNNEINSYWLGLNEFADLTHEEFKGRYLGLAKPQFSRKRQPSANFRYRDITDLPKSVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDTTFNSGCNGGLMDYAFQYIISTGGLHKEDDYPYLMEEGICQEQKEDVERVTISGYEDVPENDDESLVKALAHQPVSVAIEASGRDFQFYKGGVFNGKCGTDLDHGVAAVGYGSSKGSDYVIVKNSWGPRWGEKGFIRMKRNTGKPEGLCGINKMASYPTKTK
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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.
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O65502
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HC244_ARATH
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Protein HIGH CHLOROPHYLL FLUORESCENCE PHENOTYPE 244, chloroplastic
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MASLRLPAQLVTRGNLIHHNSSSSSSGRLSWRRSLTPENTIPLFPSSSSSSLNRERSIVVPVTCSAAAVNLAPGTPVRPTSILVVGATGTLGRQIVRRALDEGYDVRCLVRPRPAPADFLRDWGATVVNADLSKPETIPATLVGIHTVIDCATGRPEEPIKTVDWEGKVALIQCAKAMGIQKYVFYSIHNCDKHPEVPLMEIKYCTEKFLQESGLNHITIRLCGFMQGLIGQYAVPILEEKSVWGTDAPTRVAYMDTQDIARLTLIALRNEKINGKLLTFAGPRAWTTQEVITLCERLAGQDANVTTVPVSVLRVTRQLTRFFQWTNDVADRLAFSEVLSSDTVFSAPMTETNSLLGVDQKDMVTLEKYLQDYFSNILKKLKDLKAQSKQSDIYF
|
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. Forms a trimeric complex with OHP1 and OHP2 that is required to promote PSII core subunit assembly. The trimeric complex forms a transient PSII reaction center-like complex with PsbA, PsbD, PsbE, PsbF and PsbI subunits in thylakoids for early assembly of PSII as well as PSII repair. The trimeric complex is required for the recruitment of ribosomes to the psbA mRNA during PSII biogenesis and repair.
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O65508
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NAC76_ARATH
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NAC domain-containing protein 76 (ANAC076) (Protein VASCULAR RELATED NAC-DOMAIN 2)
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MESVDQSCSVPPGFRFHPTDEELVGYYLRKKVASQKIDLDVIRDIDLYRIEPWDLQESCRIGYEERNEWYFFSHKDKKYPTGTRTNRATMAGFWKATGRDKAVYDKSKLIGMRKTLVFYKGRAPNGQKTDWIMHEYRLESDENAPPQEEGWVVCRAFKKKPMTGQAKNTETWSSSYFYDELPSGVRSVTEPLNYVSKQKQNVFAQDLMFKQELEGSDIGLNFIHCDQFIQLPQLESPSLPLTKRPVSLTSITSLEKNKNIYKRHLIEEDVSFNALISSGNKDKKKKKTSVMTTDWRALDKFVASQLMSQEDGVSGFGGHHEEDNNKIGHYNNEESNNKGSVETASSTLLSDREEENRFISGLLCSNLDYDLYRDLHV
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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 involved in secondary wall biosynthesis and programmed cell death, genes driven by the secondary wall NAC binding element (SNBE). Triggers thickening of secondary walls.
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O65517
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SRS2_ARATH
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Protein SHI RELATED SEQUENCE 2 (Protein STYLISH 2)
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MAGIFSLGGNNNNNGDEEEENQQQQKTNWVWYRSNANTNNINPSSSQQVWQIPPEQMLMHHHSHPQQQSLDLYPGHQIDVSDLATSSRSITISCRDCGNQAKKDCTHMRCRTCCKSRGFDCSTHVRSTWIPVARRRERQQQLHMSTSGGGGGSGSGGAGGGGSSIPKRHRDPTLPGTSSSSRLPSHSAGLEMGEASFPGEVSSDALFRCVKMSGVDDGGDGQYAYQTTVNIGGHLFKGILYDQGPESSYMSGGSGGSDHQSSSAGGGGGGHPFNPPVVTDGGGGVSSAMFVDPNSGGYYSSNMTTSVFMPPGTQFYQNPPRS
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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 development in a dose-dependent manner, controlling apical-basal patterning. Promotes style and stigma formation, and influence vascular development during gynoecium development. May also have a role in the formation and/or maintenance of the shoot apical meristem (SAM).
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O65554
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CIPK6_ARATH
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CBL-interacting serine/threonine-protein kinase 6 (EC 2.7.11.1) (SNF1-related kinase 3.14) (SOS2-like protein kinase PKS4) (SOS3-interacting protein 3)
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MVGAKPVENGSDGGSSTGLLHGRYELGRLLGHGTFAKVYHARNIQTGKSVAMKVVGKEKVVKVGMVDQIKREISVMRMVKHPNIVELHEVMASKSKIYFAMELVRGGELFAKVAKGRLREDVARVYFQQLISAVDFCHSRGVYHRDLKPENLLLDEEGNLKVTDFGLSAFTEHLKQDGLLHTTCGTPAYVAPEVILKKGYDGAKADLWSCGVILFVLLAGYLPFQDDNLVNMYRKIYRGDFKCPGWLSSDARRLVTKLLDPNPNTRITIEKVMDSPWFKKQATRSRNEPVAATITTTEEDVDFLVHKSKEETETLNAFHIIALSEGFDLSPLFEEKKKEEKREMRFATSRPASSVISSLEEAARVGNKFDVRKSESRVRIEGKQNGRKGKLAVEAEIFAVAPSFVVVEVKKDHGDTLEYNNFCSTALRPALKDIFWTSTPA
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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 AKT1. Binds to CBL4 to modulate AKT2 activity by promoting a kinase interaction-dependent but phosphorylation-independent translocation of the channel to the plasma membrane.
|
O65570
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VILI4_ARATH
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Villin-4
|
MSVSMRDLDPAFQGAGQKAGIEIWRIENFIPTPIPKSSIGKFFTGDSYIVLKTTALKTGALRHDIHYWLGKDTSQDEAGTAAVKTVELDAALGGRAVQYREVQGHETEKFLSYFKPCIIPQEGGVASGFKHVVAEEHITRLFVCRGKHVVHVKEVPFARSSLNHDDIYILDTKSKIFQFNGSNSSIQERAKALEVVQYIKDTYHDGTCEVATVEDGKLMADADSGEFWGFFGGFAPLPRKTANDEDKTYNSDITRLFCVEKGQANPVEGDTLKREMLDTNKCYILDCGIEVFVWMGRTTSLDDRKIASKAAEEMIRSSERPKSQMIRIIEGFETVPFRSKFESWTQETNTTVSEDGRGRVAALLQRQGVNVRGLMKAAPPKEEPQVFIDCTGNLQVWRVNGQAKTLLQAADHSKFYSGDCYVFQYSYPGEEKEEVLIGTWFGKQSVEEERGSAVSMASKMVESMKFVPAQARIYEGKEPIQFFVIMQSFIVFKGGISSGYKKYIAEKEVDDDTYNENGVALFRIQGSGPENMQAIQVDPVAASLNSSYYYILHNDSSVFTWAGNLSTATDQELAERQLDLIKPNQQSRAQKEGSESEQFWELLGGKAEYSSQKLTKEPERDPHLFSCTFTKEVLKVTEIYNFTQDDLMTEDIFIIDCHSEIFVWVGQEVVPKNKLLALTIGEKFIEKDSLLEKLSPEAPIYVIMEGGEPSFFTRFFTSWDSSKSAMHGNSFQRKLKIVKNGGTPVADKPKRRTPASYGGRASVPDKSQQRSRSMSFSPDRVRVRGRSPAFNALAATFESQNARNLSTPPPVVRKLYPRSVTPDSSKFAPAPKSSAIASRSALFEKIPPQEPSIPKPVKASPKTPESPAPESNSKEQEEKKENDKEEGSMSSRIESLTIQEDAKEGVEDEEDLPAHPYDRLKTTSTDPVSDIDVTRREAYLSSEEFKEKFGMTKEAFYKLPKWKQNKFKMAVQLF
|
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.
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O65572
|
CCD1_ARATH
|
Carotenoid 9,10(9',10')-cleavage dioxygenase 1 (EC 1.14.99.n4) (AtCCD1) (Neoxanthin cleavage enzyme NC1) (AtNCED1)
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MAEKLSDGSSIISVHPRPSKGFSSKLLDLLERLVVKLMHDASLPLHYLSGNFAPIRDETPPVKDLPVHGFLPECLNGEFVRVGPNPKFDAVAGYHWFDGDGMIHGVRIKDGKATYVSRYVKTSRLKQEEFFGAAKFMKIGDLKGFFGLLMVNVQQLRTKLKILDNTYGNGTANTALVYHHGKLLALQEADKPYVIKVLEDGDLQTLGIIDYDKRLTHSFTAHPKVDPVTGEMFTFGYSHTPPYLTYRVISKDGIMHDPVPITISEPIMMHDFAITETYAIFMDLPMHFRPKEMVKEKKMIYSFDPTKKARFGVLPRYAKDELMIRWFELPNCFIFHNANAWEEEDEVVLITCRLENPDLDMVSGKVKEKLENFGNELYEMRFNMKTGSASQKKLSASAVDFPRINECYTGKKQRYVYGTILDSIAKVTGIIKFDLHAEAETGKRMLEVGGNIKGIYDLGEGRYGSEAIYVPRETAEEDDGYLIFFVHDENTGKSCVTVIDAKTMSAEPVAVVELPHRVPYGFHALFVTEEQLQEQTLI
|
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 biosynthesis.
|
O65583
|
UKL4_ARATH
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Uridine kinase-like protein 4 [Includes: Uridine kinase (UK) (EC 2.7.1.48); Putative uracil phosphoribosyltransferase (UPRTase) (EC 2.4.2.9) (UMP pyrophosphorylase)]
|
MGSKSVVDMIEAASRAHFSGLHVNGHMNGLEPSALKETTSASEDIQRQPFVIGVAGGAASGKTTVCDMIIQQLHDQRVVLINLDSFYHNLTEEELARVHEYNFDHPDAFDTEHLLSCMEKLRQGQAVDIPKYDFKTYRSSVFRRVNPTDVIILEGILLFHDPRVRKLMNMKIFVCTDADVRLARRIKRDTVENGRDIGTVLDQYSKFVKPAFDDFILPTKKYADIIIPRGGDNHVAIDLIVQHICTKLGQHDLCKIYPNLYVIHSTFQIRGMHTLIRDSQTTKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVITPTGCVYSGVDFCKRLCGVSVIRSGESMENALRACCKGIKIGKILIHREGDNGQQLVYEKLPNDISERHVLLLDPILGTGNSAVEAINLLISKGVPEGNIIFLNLISAPQGVHVVCKKFPRIKIVTSEIDNGLNEEFRVIPGMGEFGDRYFGTDDD
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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.
|
O65639
|
CSP1_ARATH
|
Cold shock protein 1 (AtCSP1) (Cold shock domain-containing protein 1)
|
MASEDQSAARSTGKVNWFNASKGYGFITPDDGSVELFVHQSSIVSEGYRSLTVGDAVEFAITQGSDGKTKAVNVTAPGGGSLKKENNSRGNGARRGGGGSGCYNCGELGHISKDCGIGGGGGGGERRSRGGEGCYNCGDTGHFARDCTSAGNGDQRGATKGGNDGCYTCGDVGHVARDCTQKSVGNGDQRGAVKGGNDGCYTCGDVGHFARDCTQKVAAGNVRSGGGGSGTCYSCGGVGHIARDCATKRQPSRGCYQCGGSGHLARDCDQRGSGGGGNDNACYKCGKEGHFARECSSVA
|
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.
|
O65660
|
PLAT1_ARATH
|
PLAT domain-containing protein 1 (AtPLAT1) (PLAT domain protein 1)
|
MARRDVLLPFLLLLATVSAVAFAEDDPDCVYTFYLRTGSIWKAGTDSIISARIYDKDGDYIGIKNLQAWAGLMGPDYNYFERGNLDIFSGRAPCLPSPICALNLTSDGSGDHHGWYVNYVEITTAGVHAQCSTQDFEIEQWLATDTSPYELTAVRNNCPVKLRDSVSRVGSEIRKKLSWVV
|
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.
|
O65683
|
BZP11_ARATH
|
bZIP transcription factor 11 (AtbZIP11) (G-box-binding factor 6) (bZIP transcription factor ATB2)
|
MESSSSGTTSSTIQTSSGSEESLMEQRKRKRMLSNRESARRSRMKKQKLLDDLTAQVNHLKKENTEIVTSVSITTQHYLTVEAENSVLRAQLDELNHRLQSLNDIIEFLDSSNNNNNNNMGMCSNPLVGLECDDFFVNQMNMSYIMNQPLMASSDALMY
|
Transcription factor that binds to the DNA sequence 5'-ACTCAT-3' in target gene promoters. Promotes POX1/PRODH1 expression in response to hypoosmolarity stress. Positively regulates the expression of ASN1 and POX2/PRODH2 genes, which are involved in amino acid metabolism. Regulates several metabolic pathways such as myo-inositol, raffinose and trehalose. Regulates several trehalose metabolism genes, including TRE1, TPP5 and TPP6. Mediates recruitment of the histone acetylation machinery to activate auxin-induced transcription. Interacts with ADA2B adapter protein to promote ADA2B-mediated recruitment of SAGA-like histone acetyltransferase complexes to specific auxin-responsive genes.
|
O65717
|
CNGC1_ARATH
|
Cyclic nucleotide-gated ion channel 1 (AtCNGC1) (Cyclic nucleotide- and calmodulin-regulated ion channel 1)
|
MNFRQEKFVRFQDWKSDKTSSDVEYSGKNEIQTGIFQRTISSISDKFYRSFESSSARIKLFKRSYKSYSFKEAVSKGIGSTHKILDPQGPFLQRWNKIFVLACIIAVSLDPLFFYVPIIDDAKKCLGIDKKMEITASVLRSFTDVFYVLHIIFQFRTGFIAPSSRVFGRGVLVEDKREIAKRYLSSHFIIDILAVLPLPQMVILIIIPHMRGSSSLNTKNMLKFIVFFQYIPRFIRIYPLYKEVTRTSGILTETAWAGAAFNLFLYMLASHVFGAFWYLFSIERETVCWKQACERNNPPCISKLLYCDPETAGGNAFLNESCPIQTPNTTLFDFGIFLDALQSGVVESQDFPQKFFYCFWWGLQNLSSLGQNLKTSTYIWEICFAVFISIAGLVLFSFLIGNMQTYLQSTTTRLEEMRVKRRDAEQWMSHRLLPENLRKRIRRYEQYKWQETRGVDEENLLSNLPKDLRRDIKRHLCLALLMRVPMFEKMDEQLLDALCDRLQPVLYTEESYIVREGDPVDEMLFIMRGKLLTITTNGGRTGFLNSEYLGAGDFCGEELLTWALDPHSSSNLPISTRTVRALMEVEAFALKADDLKFVASQFRRLHSKQLRHTFRYYSQQWKTWAACFIQAAWRRYIKKKLEESLKEEENRLQDALAKEACGSSPSLGATIYASRFAANILRTIRRSGSVRKPRMPERMPPMLLQKPAEPDFNSDD
|
Acts as 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+).
|
O65718
|
CNGC2_ARATH
|
Cyclic nucleotide-gated ion channel 2 (AtCNGC2) (Cyclic nucleotide- and calmodulin-regulated ion channel 2) (Protein DEFENSE NO DEATH 1)
|
MPSHPNFIFRWIGLFSDKFRRQTTGIDENSNLQINGGDSSSSGSDETPVLSSVECYACTQVGVPAFHSTSCDQAHAPEWRASAGSSLVPIQEGSVPNPARTRFRRLKGPFGEVLDPRSKRVQRWNRALLLARGMALAVDPLFFYALSIGRTTGPACLYMDGAFAAVVTVLRTCLDAVHLWHVWLQFRLAYVSRESLVVGCGKLVWDPRAIASHYARSLTGFWFDVIVILPVPQAVFWLVVPKLIREEKVKLIMTILLLIFLFQFLPKIYHCICLMRRMQKVTGYIFGTIWWGFALNLIAYFIASHVAGGCWYVLAIQRVASCIRQQCMRTGNCNLSLACKEEVCYQFVSPTSTVGYPCLSGNLTSVVNKPMCLDSNGPFRYGIYRWALPVISSNSLAVKILYPIFWGLMTLSTFANDLEPTSNWLEVIFSIVMVLSGLLLFTLLIGNIQVFLHAVMAKKRKMQIRCRDMEWWMKRRQLPSRLRQRVRRFERQRWNALGGEDELELIHDLPPGLRRDIKRYLCFDLINKVPLFRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKGVLATSTLEPGGYLGDELLSWCLRRPFLDRLPPSSATFVCLENIEAFSLGSEDLRYITDHFRYKFANERLKRTARYYSSNWRTWAAVNIQMAWRRRRKRTRGENIGGSMSPVSENSIEGNSERRLLQYAAMFMSIRPHDHLE
|
Acts as 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 function in homeostasis, re-establishing ionic balance after defense action and/or other stimuli. Could mediate the initiation of the developmentally regulated cell death programs.
|
O65719
|
HSP7C_ARATH
|
Heat shock 70 kDa protein 3 (AtHsp70-3) (Heat shock protein 70-3) (Heat shock cognate 70 kDa protein 3) (AtHsc70-3) (Heat shock cognate protein 70-3)
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MAGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPINTVFDAKRLIGRRFTDSSVQSDIKLWPFTLKSGPAEKPMIVVNYKGEDKEFSAEEISSMILIKMREIAEAYLGTTIKNAVVTVPAYFNDSQRQATKDAGVIAGLNVMRIINEPTAAAIAYGLDKKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKNKKDISGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGIDFYAPITRARFEELNIDLFRKCMEPVEKCLRDAKMDKNSIDDVVLVGGSTRIPKVQQLLVDFFNGKELCKSINPDEAVAYGAAVQAAILSGEGNEKVQDLLLLDVTPLSLGLETAGGVMTVLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVYEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDIDANGILNVSAEDKTTGQKNKITITNDKGRLSKDEIEKMVQEAEKYKSEDEEHKKKVDAKNALENYAYNMRNTIRDEKIGEKLAGDDKKKIEDSIEAAIEWLEANQLAECDEFEDKMKELESICNPIIAKMYQGGEAGGPAAGGMDEDVPPSAGGAGPKIEEVD
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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.
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O65782
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C83B1_ARATH
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Cytochrome P450 83B1 (EC 1.14.14.45) (Protein ALTERED TRYPTOPHAN REGULATION 4) (Protein RED ELONGATED 1) (Protein SUPERROOT 2)
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MDLLLIIAGLVAAAAFFFLRSTTKKSLRLPPGPKGLPIIGNLHQMEKFNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMKRFIDILYETQALLGTLFFSDLFPYFGFLDNLTGLSARLKKAFKELDTYLQELLDETLDPNRPKQETESFIDLLMQIYKDQPFSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRSVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDNPNEFIPERFMNEHKGVDFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPKGIKPEDIKMDVMTGLAMHKKEHLVLAPTKHI
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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 indole-3-acetaldoxime also serves as a precursor for auxin biosynthesis. Specifically metabolizes (E)-p-hydroxyphenylacetaldoxime into an S-alkyl-thiohydroximate.
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O65797
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ADS1_ARATH
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Delta-9 acyl-lipid desaturase 1 (EC 1.14.19.-)
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MSLSASEKEENNKKMAADKAEMGRKKRAMWERKWKRLDIVKAFASLFVHFLCLLAPFNFTWPALRVALIVYTVGGLGITVSYHRNLAHRSFKVPKWLEYFFAYCGLLAIQGDPIDWVSTHRYHHQFTDSDRDPHSPNEGFWFSHLLWLFDTGYLVEKCGRRTNVEDLKRQWYYKFLQRTVLYHILTFGFLLYYFGGLSFLTWGMGIGVAMEHHVTCLINSLCHVWGSRTWKTNDTSRNVWWLSVFSFGESWHNNHHAFESSARQGLEWWQIDISWYIVRFLEIIGLATDVKLPSESQRRRMAMVR
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Involved in delta-9 desaturation of fatty acids (Probable). Involved in the production of very-long-chain fatty acids (VLCFAs). May desaturate chloroplastic monogalactosyl diacylglycerol (MGDG) and alter chloroplast membrane fluidity, which is required to prime a cold acclimation response.
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O65896
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CDA1_ARATH
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Cytidine deaminase 1 (At-CDA1) (EC 3.5.4.5)
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MDKPSFVIQSKEAESAAKQLGVSVIQLLPSLVKPAQSYARTPISKFNVAVVGLGSSGRIFLGVNVEFPNLPLHHSIHAEQFLVTNLTLNGERHLNFFAVSAAPCGHCRQFLQEIRDAPEIKILITDPNNSADSDSAADSDGFLRLGSFLPHRFGPDDLLGKDHPLLLESHDNHLKISDLDSICNGNTDSSADLKQTALAAANRSYAPYSLCPSGVSLVDCDGKVYRGWYMESAAYNPSMGPVQAALVDYVANGGGGGYERIVGAVLVEKEDAVVRQEHTARLLLETISPKCEFKVFHCYEA
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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.
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O65934
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ABC1_MYCTU
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ABC transporter ATP-binding/permease protein Rv1747 (EC 7.-.-.-)
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MPMSQPAAPPVLTVRYEGSERTFAAGHDVVVGRDLRADVRVAHPLISRAHLLLRFDQGRWVAIDNGSLNGLYLNNRRVPVVDIYDAQRVHIGNPDGPALDFEVGRHRGSAGRPPQTTSIRLPNLSAGAWPTDGPPQTGTLGSGQLQQLPPATTRIPAAPPSGPQPRYPTGGQQLWPPSGPQRAPQIYRPPTAAPPPAGARGGTEAGNLATSMMKILRPGRLTGELPPGAVRIGRANDNDIVIPEVLASRHHATLVPTPGGTEIRDNRSINGTFVNGARVDAALLHDGDVVTIGNIDLVFADGTLARREENLLETRVGGLDVRGVTWTIDGDKTLLDGISLTARPGMLTAVIGPSGAGKSTLARLVAGYTHPTDGTVTFEGHNVHAEYASLRSRIGMVPQDDVVHGQLTVKHALMYAAELRLPPDTTKDDRTQVVARVLEELEMSKHIDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDRQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLLAPGGKTAFCGPPTQIGPVMGTTNWADIFSTVADDPDAAKARYLARTGPTPPPPPVEQPAELGDPAHTSLFRQFSTIARRQLRLIVSDRGYFVFLALLPFIMGALSMSVPGDVGFGFPNPMGDAPNEPGQILVLLNVGAVFMGTALTIRDLIGERAIFRREQAVGLSTTAYLIAKVCVYTVLAVVQSAIVTVIVLVGKGGPTQGAVALSKPDLELFVDVAVTCVASAMLGLALSAIAKSNEQIMPLLVVAVMSQLVFSGGMIPVTGRVPLDQMSWVTPARWGFAASAATVDLIKLVPGPLTPKDSHWHHTASAWWFDMAMLVALSVIYVGFVRWKIRLKAC
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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.
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O66200
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CH60_ENTAG
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Chaperonin GroEL (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin-60) (Cpn60)
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MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGIDKAVASAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLVIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVGQIRKQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVDDALHATRAAVEEGVVAGGGVALVRVAAKLAGLTAQNEDQNVGIKVALRAMEAPLRQIVSNAGEEPSVVANNVKAGEGNYGYNAATEEYGNMIDFGILDPTKVTRSALQYAASVAGLMITTECMVTDMPKGDAPDLXAAGMGG
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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:MF_00600}.
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O66465
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MRAY_AQUAE
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Phospho-N-acetylmuramoyl-pentapeptide-transferase (EC 2.7.8.13) (UDP-MurNAc-pentapeptide phosphotransferase)
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MLYQLALLLKDYWFAFNVLKYITFRSFTAVLIAFFLTLVLSPSFINRLRKIQRLFGGYVREYTPESHEVKKYTPTMGGIVILIVVTLSTLLLMRWDIKYTWVVLLSFLSFGTIGFWDDYVKLKNKKGISIKTKFLLQVLSASLISVLIYYWADIDTILYFPFFKELYVDLGVLYLPFAVFVIVGSANAVNLTDGLDGLAIGPAMTTATALGVVAYAVGHSKIAQYLNIPYVPYAGELTVFCFALVGAGLGFLWFNSFPAQMFMGDVGSLSIGASLATVALLTKSEFIFAVAAGVFVFETISVILQIIYFRWTGGKRLFKRAPFHHHLELNGLPEPKIVVRMWIISILLAIIAISMLKLR
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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 as lipid I. {ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000269|PubMed:23990562, ECO:0000269|PubMed:27088606, ECO:0000269|PubMed:29459785}.
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O66663
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KDTA_AQUAE
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3-deoxy-D-manno-octulosonic acid transferase (Kdo transferase) (EC 2.4.99.12) (Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase) (Monofunctional Kdo transferase)
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MQFEVLKRFFPKESLKNCKGALWVHTASIGEFNTFLPILKELKREHRILLTYFSPRAREYLKTKSDFYDCLHPLPLDNPFSVKRFEELSKPKALIVVEREFWPSLIIFTKVPKILVNAYAKGSLIEKILSKKFDLIIMRTQEDVEKFKTFGAKRVFSCGNLKFICQKGKGIKLKGEFIVAGSIHTGEVEIILKAFKEIKKTYSSLKLILVPRHIENAKIFEKKARDFGFKTSFFENLEGDVILVDRFGILKELYPVGKIAIVGGTFVNIGGHNLLEPTCWGIPVIYGPYTHKVNDLKEFLEKEGAGFEVKNETELVTKLTELLSVKKEIKVEEKSREIKGCYLEKLREFLRGL
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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 acceptor lipid.
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O66990
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PYRC_AQUAE
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Dihydroorotase (DHOase) (EC 3.5.2.3)
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MLKLIVKNGYVIDPSQNLEGEFDILVENGKIKKIDKNILVPEAEIIDAKGLIVCPGFIDIHVHLRDPGQTYKEDIESGSRCAVAGGFTTIVCMPNTNPPIDNTTVVNYILQKSKSVGLCRVLPTGTITKGRKGKEIADFYSLKEAGCVAFTDDGSPVMDSSVMRKALELASQLGVPIMDHCEDDKLAYGVINEGEVSALLGLSSRAPEAEEIQIARDGILAQRTGGHVHIQHVSTKLSLEIIEFFKEKGVKITCEVNPNHLLFTEREVLNSGANARVNPPLRKKEDRLALIEGVKRGIIDCFATDHAPHQTFEKELVEFAMPGIIGLQTALPSALELYRKGIISLKKLIEMFTINPARIIGVDLGTLKLGSPADITIFDPNKEWILNEETNLSKSRNTPLWGKVLKGKVIYTIKDGKMVYKD
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Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000269|PubMed:15381710, ECO:0000269|PubMed:24314009}.
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O67049
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AROE_AQUAE
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Shikimate dehydrogenase (NADP(+)) (SD) (SDH) (EC 1.1.1.25)
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MINAQTQLYGVIGFPVKHSLSPVFQNALIRYAGLNAVYLAFEINPEELKKAFEGFKALKVKGINVTVPFKEEIIPLLDYVEDTAKEIGAVNTVKFENGKAYGYNTDWIGFLKSLKSLIPEVKEKSILVLGAGGASRAVIYALVKEGAKVFLWNRTKEKAIKLAQKFPLEVVNSPEEVIDKVQVIVNTTSVGLKDKDPEIFNYDLIKKDHVVVDIIYKETKLLKKAKEKGAKLFDGLPMLLWQGIEAFKIWNGCEVPYSVAERSVRDLRG
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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}.
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O67082
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RNC_AQUAE
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Ribonuclease 3 (EC 3.1.26.3) (Ribonuclease III) (RNase III)
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MKMLEQLEKKLGYTFKDKSLLEKALTHVSYSKKEHYETLEFLGDALVNFFIVDLLVQYSPNKREGFLSPLKAYLISEEFFNLLAQKLELHKFIRIKRGKINETIIGDVFEALWAAVYIDSGRDANFTRELFYKLFKEDILSAIKEGRVKKDYKTILQEITQKRWKERPEYRLISVEGPHHKKKFIVEAKIKEYRTLGEGKSKKEAEQRAAEELIKLLEESE
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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 present in the organism.
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O67226
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RGYR2_AQUAE
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Reverse gyrase 2 [Includes: Helicase (EC 3.6.4.12); Topoisomerase (EC 5.6.2.2)]
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MALELIERGCPNCGGVISSDRLEKGLPCSKCLPKPTEEKVCDALEELKTLKYLKPFCDTDKSLERFINFFEKAVGAKPWSLQRVWAKRVFMNQSFAIVAPTGVGKTTFGLVMSLFLKGRVLAIFPTRLLAQQAGDRLSELAQKVGVNKKILIYQSKKNIREQFLNGDWDILLGTNMFLHKNFENLINFKFKLIFIDDIDSFLKRGKNVDYLFKLLGFSGEEIKLALKENKTQRDYDRLARIRKRKRDTVLIVSSATLKPRGKRAYLFRNLLGFDVQKAITTLRNIVDVAEPVKDLEEALEKSVELIKKLGKGGLVYLSVFYGKDKVQEVKEFYRKHGINAVSYLDYKPEELYQILEKGEFDVAVGISHITNPLVRGIDLPHIIRYAVFLDPPKHVFPTELTLSPPLLHGLLLTLLNLFEGDDRLKAIQYVMYLKRYLTLREEQLDNYPRIKERVEEIKNFLENYLKDENFLKKIKESEDISLVPKEGKLYIVVGDANSYIQASGRTSRFIAGGMTKGLSVVYYSDPKAFYSLKKRLALYYMTQEIEFKRLSEVDLNKLIKEIDEDRKRAREILQGKGVAQIKDLFKTTLVIVESPNKARTIAGFFGKPQMRLVEDSVAYEVPLGDRLLVITASLGHVLDLVTDKGFFGVLDDTYPYLPVYDTIKICRETHEQHTEYEYLKKRCKGKIEDKLEIIKGVREVSYEVDEVFIATDPDAEGEKIGYDLYLLSKPFNFNIKRAEFHEVTPKAFREAIQNPREVDLNLVKAQLVRRILDRWVGFTLSHILWDAFGKKWLSAGRVQTPVLGWVIKRYEESKEKKGEILLHVNDFPLKIEIEDLMFAKEIFKDLELADISLSNPQEEEKRPLPPYTTDTVLEDANEKLHLSAHKTMKILQELFEAGYITYHRTDSTRVSDAGKYLVAKPYITKMFGEEYFYPRSWGEGGAHECIRPTRPLEPKDLEFMITAGIAEFEDPENALKVYELIFKRFMASQMRPAKVITEEIILKLPYFEWKERVVTEVKEHGFDLMYPTFKVFPKKEKLEITHKEFREVPKVYPYTQGTLIQEMKRRGLGRPSTYAQIVQTLLERHYVVEEKGFLIPTDLGREVYEYLTKHFPEWTSEELTRKLEEAMDKIERGELDYMEVLKEVHRIKVLLKEEKAFKK
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Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication. {ECO:0000255|HAMAP-Rule:MF_01125}.
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O67496
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ISPG_AQUAE
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4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (EC 1.17.7.3) (1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase)
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MIQKRKTRQIRVGNVKIGGDAPIVVQSMTSTKTHDVEATLNQIKRLYEAGCEIVRVAVPHKEDVEALEEIVKKSPMPVIADIHFAPSYAFLSMEKGVHGIRINPGNIGKEEIVREIVEEAKRRGVAVRIGVNSGSLEKDLLEKYGYPSAEALAESALRWSEKFEKWGFTNYKVSIKGSDVLQNVRANLIFAERTDVPLHIGITEAGMGTKGIIKSSVGIGILLYMGIGDTVRVSLTDDPVVEVETAYEILKSLGLRRRGVEIVACPTCGRIEVDLPKVVKEVQEKLSGVKTPLKVAVMGCVVNAIGEAREADIGLACGRGFAWLFKHGKPIKKVDESEMVDELLKEIQNMEKDGGTN
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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}.
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O67648
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LPXC_AQUAE
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UDP-3-O-acyl-N-acetylglucosamine deacetylase (UDP-3-O-acyl-GlcNAc deacetylase) (EC 3.5.1.108) (UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase)
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MGLEKTVKEKLSFEGVGIHTGEYSKLIIHPEKEGTGIRFFKNGVYIPARHEFVVHTNHSTDLGFKGQRIKTVEHILSVLHLLEITNVTIEVIGNEIPILDGSGWEFYEAIRKNILNQNREIDYFVVEEPIIVEDEGRLIKAEPSDTLEVTYEGEFKNFLGRQKFTFVEGNEEEIVLARTFCFDWEIEHIKKVGLGKGGSLKNTLVLGKDKVYNPEGLRYENEPVRHKVFDLIGDLYLLGSPVKGKFYSFRGGHSLNVKLVKELAKKQKLTRDLPHLPSVQAL
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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}.
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O67911
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CATNT_AQUAE
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CC-adding tRNA nucleotidyltransferase (C-adding TNT) (EC 2.7.7.-) (CC-adding enzyme)
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MENIEIVSSGKHTLHGLNFYLSYFDDVAKVLPREHYCFIVGGWVRDRILGEPVGYNIDVDFLTTADPVELAKNFAKRIGGHFFVFEKRGFLIKRPTIASVVLHLPPYRYRFDFSPLKGKDLEKALIEDLKERDFTANAIAVNLDDVLSIGAKQTIVYDPTGGIKDLEQGLLRPVSIENLKRDPVRVLRGFRIAIEKNLQLTEDFYEFVKEDPRIVLKSAVERITHELFKIMKEKTAHKVIRELYEYGVLEAIIPEIGRLREVKDQGEHHIYPLDEHTLKTLEYLEQVIEDRAKYLSAELLENFGKKRVLGEFTDVELLKWGALFHDIGKPQTFAVREGKVTFYEHDKVGAQIVREIGERLRWGDEATEFVAKLVRHHLRPFFLREAFKKGELKRRGMANFWRECGDIAPHLFLLSIADAMASGDEEEDIKALMETIAELESFNRNEMKEEIQKPLLNGDEIMEILGIKPGKIVGILKKALLEAQIDGKVETKEEAIEFIKRSTKNLKPLDEG
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tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the two cytidine residues to tRNA.
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O67931
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SQRD_AQUAE
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Sulfide-quinone reductase (SQR) (EC 1.8.5.4) (Sulfide:quinone oxidoreductase)
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MAKHVVVIGGGVGGIATAYNLRNLMPDLKITLISDRPYFGFTPAFPHLAMGWRKFEDISVPLAPLLPKFNIEFINEKAESIDPDANTVTTQSGKKIEYDYLVIATGPKLVFGAEGQEENSTSICTAEHALETQKKLQELYANPGPVVIGAIPGVSCFGPAYEFALMLHYELKKRGIRYKVPMTFITSEPYLGHFGVGGIGASKRLVEDLFAERNIDWIANVAVKAIEPDKVIYEDLNGNTHEVPAKFTMFMPSFQGPEVVASAGDKVANPANKMVIVNRCFQNPTYKNIFGVGVVTAIPPIEKTPIPTGVPKTGMMIEQMAMAVAHNIVNDIRNNPDKYAPRLSAICIADFGEDAGFFFADPVIPPRERVITKMGKWAHYFKTAFEKYFLWKVRNGNIAPSFEEKVLEIFLKVHPIELCKDCEGAPGSRC
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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.
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O68008
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BACC_BACLI
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Bacitracin synthase 3 (BA3) [Includes: ATP-dependent isoleucine adenylase (IleA) (Isoleucine activase); ATP-dependent D-phenylalanine adenylase (D-PheA) (D-phenylalanine activase); ATP-dependent histidine adenylase (HisA) (Histidine activase); ATP-dependent D-aspartate adenylase (D-AspA) (D-aspartate activase); ATP-dependent asparagine adenylase (AsnA) (Asparagine activase); Aspartate racemase (EC 5.1.1.13); Phenylalanine racemase [ATP hydrolyzing] (EC 5.1.1.11)]
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MKTKVEKIYPLSNMQKGMLFHAMKDEASHAYFEQFIIELKGDVDERMFEESLNEVMKRHEILRASFHHRLDEPLHVIIKDRHMKFDYLDIRGRHDQDGVLERYLAEDRQKGFDLAKDTLMRACLIRMSDDSYQFVWTYHHILLDGWCLGIILDELLTIYEMKRKGQNHQLEDPRPYSDYIKWLEDQDKEEAQSYWESYLSGYDQKNSLPKLRTPSETGFKRREKTIECSKELTNRLIKLANRNHVTINTVLQSIWGVILAKYNNSEDVVFGTVVSGRDAEVEGIETMVGVFINTIPTRIRLDKDKLFKDVLRQTQADALESSRYNYMNLAEVQALSELKNDLIDHVMVFENYAVDQKAFEEKNDVGFEMVNVSGEEQTNYHFSISAALDDQLKLLFIYDENVYDTTIIETLEKHIITVAEQVAEDETQTLRDINLVSKEEQHRILDTFNDTKTGYPKDKPLHELFEEQAMKTPDHTALVFGAQRMTYRELNEKANQTARLLREKGIGRGSIAAIIADRSFEMIIGIIGILKAGGAYLPIDPETPKHRIAFMLSDTKAGVLLAQGKAADGIDCEADIIHLDKGVADGFSKKRLSSVNDSGDTAYIIYTSGSTGMPKGVVTPHYSAARVVKNTNYIDITEDDAILQLSNYSFDGSVFDIFGALLNGASLVLIEKETVLNTHELAEVIKKEQVSVMFITTALFNTLADINIGCLAKLRKIFLGGERASIPHVRKVLNHVGRDKLIHVYGPTESTVYATYYFINEIDDEAETIPIGSPLANTSVLIMDEAGKLLPIGVPGELCIAGDGLSKGYLNREELTAEKFIPHPFIPGERLYKTGDLAKWLPDGNIEFIGRIDHQVKIRGFRIELGEIESRLEMHEDINETIVTVREDEESRPYICAYITANREISLDELKGFLGEKLPEYMIPAYFVKMDKLPLTKNGKVDRKALPEPDRTAGAENEYEAPRNETEEKLAAIWRDILKVEKSGINDHFFEMGGHSLKAAAMAARIRKELKAEIPLGQIFKTPTIKGLGEYIRSTKDSVYSSIQKVEEKEYYRLSSAQKRLYILDQIEGSGLSYNIPFTMKVKGRFDIRRFENALKTIIQRHEALRTSFLMADGEPVQKIEKEVDFSIKCSKIQSLSIQEIIKQFVRPFDLKKAPLFRTEVVKVDDEEHIILFDMHHIISDGASMGVLTKEICDLYGGKELKPLSLQYKDYSEWQRDFYQKDEMKRQKEYWLNIFKGEIPVLNMPTDYPRPQMHSVEGDRIGFAIDGELTKKLKRIAKDNGATMYMLLLAAYTVLLRTYSGQEDVIIGTPIQGRKHHELKHVIGMFVNTLAMRNHPKGDKTFAEYLQDVKETALKAYENQDYQFDDLVEQLDLERDMSRNPLFDTMFVLQNLEKADAEIEGLTFEPFESDIHISKFDLTLSAIEKDSKIEFDLEYCTKLFKRETVERMAAHFVRVLEDISKRTDKRLDQIEAMSEDEKNTLLYRFNDTKTDAPTDKTICQLFAERAETSPDKTAVVFEDQTLTYRQLHERSNQLARFLREKGVQPDTAVGIMVDRSPEMIIGLLGILKAGGAYLPLDPAYPEDRIKYILGDSQTKFLLSEEALIKKRAFIKEADMINIDIHDKQIAAQDAAQLEPVSRSGDLAYIIYTSGSTGKPKGVLIEQKGLSNLVSAVVKLMHLNTGSRVIQFASLSFDASAFEIFPALAAGSALVLGRQEEMMPGQPLTSFLRQYNITHATLPPTVLDVLNESGLENLKVIVSAGSACSEELAKRWSGNRLFINAYGPTETTVCATAGIYEGSGRPHIGSPIANTNVYVLDQNQKPVPTGVVGELCVGGMSLARGYLNRPELTAEKFISHPFASGERLYRTGDLARWLPDGHLEFLGRIDHQVKIRGYRIELGEIENQLLKLDKIDEAAVIARKDDDHSDYLCAYIVSKEDWTSTEISEWLEKELPHYMIPAYFVRLDKLPLTSNDKVDRKALPAPDRHVATGAVYEAPRNDTEAKLVDIWRDVLGAGDIGISHHFFAAGGDSIKALQIVSRLSRLGLKLEMKDLFANPRIKDLAKYVKKQSQRKNANTIVTGHAELTPIQKWYFANNKEELDHFNQSFVLFRKGGFDESCVKKAFNKIMEQHDALRMIYEEKGGDFIQYNRSFREDLFDLDVYDVRGLDRQAEKVYELATSIQKLSSIRKGKLVHLGIFRADEGDHLLIVIHHLVVDGVSWRILFEDFETLYSQALKGQTLEIGYKTDSYQEFARRLKAYAHSRTLSKEAEYWRNIAKARVRFIPPKNVLKEDVYENSTTLSIKLGKEATADLLRNTNRAYNTEINDILLTALLTGARDITGENKLKVMMEGHGREDILEGVDITRTIGWFTTMYPVLLDAGEEKALSQQIKMVKETLRKIPNKGIGYGLLKYMAEDPDFTNEEKARISFNYLGDIDADMNRGEFSGSSFSEGESIGGKIARSHSIEINAIVMNHELVIHTTFNQMEYEKDTISRLNHQLKERLEQIIKHCTQQTESERTPSDYGDTNISLAELEEIKGKYRSAIEKIYPLANMQKGMLFHAIEDHTSDAYFQQTVMDIEGYVDPAILEASFNDIMKRHEILRASYEYEIVEEPRQIIIENRSIDFTYFNIAKSSAQQQEMFIERLLNEDRKKGFDLSKDVLMRAYLLKTAERSYRLVWSHHHILLDGWCLGIIMRELFVIYENRMNGKASPLKETKPYSDYIKWLERQDQEEARQYWREYLKGYEEQAQLPTLTKRKKSSRYDRREKVIHLSKQLTKQLKELAAKNSVTLHTVIQTIWGLMLTRYTKIDDVVFGTVVSGREANVDGIEDMIGLFINTIPTRIRFNEQARFNDCLQKVQEDAIQSNRYNYMNLAEVQALSSLKKDLIDHILVFENYEADEQDFEESQMKTGFKVNEISAAEQSITAFSMSVTPGEELTLVLTYDGNVYDRDIINNIEGHIKRVAEQVTANENRKIAEIDMLAEEERKTLLYEFNRTNADYPRNKTIHQLFEEQAERTPGHTAVVFEKEELSYKALNERSNQLAGLLREKGVKPDMIVGVMAERSVEMIVGMLAVLKAGGAYLPIDPEYPEDRIRYMIEDSGISILLKKADKQIDVDFTCIDMNEKGLAKDMAAENLGHTSGSSDMAYVIYTSGSTGKPKGVMVNHQSIVNTLYWRKQSYGYSTADATLQVPSFSFDSSVEDIFTTLISGAKLVLIRDLRMNPREIIGVLRTHKATNLLAVPSFYLNLLDTIEQPLDDLRFVTVAGEGFNESLIRQHFEKLPNVKLFNEYGPTENSVCSTRGELRKDDEKVVIGRPISNHKVYILNHNQQLLPLGTPGELCLSGEGLARGYLNRPDLTLEKFVPNPFAPGESMYRTGDLARFLPDGQIEYLGRIDHQVKIRGFRIELGEIENQLLKIEGIDAAAVMAREDQAGGKYLCAYIVADKAAGVADVRKCLLKELPDYMVPSYFVKLDQLPLTANGKIDRKALPEPSSTISEATYEAPRNRTEEKLVSIWEDVLGIENIGISHNFFELGGHSLKAAALTAKLHKEMKIEVPLRQLFETPTIKDIGDFIESMKESPYASITQAEEKEYYALSSAQRRLYILNQIEPGGLSYNMPFAMKIAGDFDVDRFEDAFRQLIERHEALRTAFVMVDGEPVQKIEKEVDFKVKYGRLGQDPLEEKIKAFIKPFALEKAPLLRAEVLKASGDEHVLMLDMHHIISDGVSMAIFTRELAELYEGKTLPPLTIQYKDFSEWQKLFYQKDEVKRQEDYWLNVFQGEVPVLNLPADEKRPQKRSIEGDIVQFEIDGETSAMLNKLAKENGATMYMLLLAGYTTLLAKYTGQEDIVVGSPIAGRHHSDLKHVIGLFINTLAMRNHPKGDMPFADYLKEVKETALKAYENQDYPFDELVEKLDVKRDMSRHPLFDTMLVLQNFDGDEADIDGLTFQPLQTEVNISKFDLTLTAAETNEGIQCVFNYSTKLFKRSTIERMAGHLINILKEAANDPHMPLSDVNMLSDEEMNALLDQNQGKQADYPQDQTVHQLFEQQADKTPEQTAVVYADEKLTYRELNERANQLARLLRDKGADADQPVAIMIEPSLEMIISMLAVLKAGAAYVPIEPEQLAKRTNEILSDSRAAILLVKGSVKENVAFAGEIVNVADGLIDAKVASNLSASGSADQNAYIIYTSGSTGKPKGVFVRHGNVVNYTTWFMKEAGLTENDKAMLVSSYAFDLGYTSIFSALLSGSELHIARKECYTNAHRALKYIKENGITYIKLTPSLFNIFVNDPGFSAEKPCATLRLVVLGGEMINTRDVETFYNQYPDHVVMNHYGPTETTIGSVFKVIDPEHLDSFKECPVIGTPIHNTNAYVLDENMKLLPEGVYGELCIAGAGVTGGYVNRPDETKEKFIENPFAPHTKMYRTGDLARRLSDGNIELAGRIDTQVKVRGYRIEPEEIKNRLLAHDDIKEAFIAAREDHKGAKQLCAYFTADAELPFEDIRTYLMHELPEYMIPSSFVQIEKMPLSANGKIDTAALPEPQPGKETEYEPPRNETEEKLVQIWEEVLGIDKIGITHHFFAAGGDSIKALQMISRLSREGLSLEMKDLFANPQIKSLSRYVKAESDKSASYETVEGEVLLTPIQQEYFSLNKTDRNHYNHAVMLYRKNGFDESIVKRVFKEIIKHHDALRTVFTEEDGKIIQYNRGPDKQLFDLFVYDVSSENDQPQKVYQLATELQQSIDIETGPLVKLAVFKTNNGDHLLIIIHHLVVDGISWRILFEDLAIGYSQLANGEKVEFYPKTASYQAYARHIAEYAKSVKLLSEKQYWLKAIAEGVEFLDMNENAGAFKVEDSRTFSTELEKEETKRLLRETNRAYHTEINDILITALLVAARDMNGQNQLRITLEGHGREQVADGIDISRTVGWFTSKYPVFIDLGQETDMSRTIKMVKEHLRNVPNKGIGYGILKYLTRDSEIAKGAASPILFNYLGQLDEDINSGEFSSSHLSPGEAAGKGITREHPLEINAVVFRGKLAIQTTYNTRAYSEDVVRAFAQNYKEALKAVIRHCAEREETEKTPSDYGDKGISLDQLEEIKLKYKGMEIEKIYPLANMQRGMLFHALEDKESQAYFEQMAINMKGLIDERLFAETFNDIMERHEILRASIEYEITDEPRNVIIKDRKINLDYHDLRKQSPAEREQVIQAYRKADREKGFRLNSEPLIRAALMRTEDDSYTFIWTNHHILLDGWSRGIIMGELFHMYHMKEARQKHRLEEARPYSDYIGWLQQQDKEAAKAYWRNYLSGFTEKSPISVLAGSSGHAKYKRKEAVIEFPEQLTGRITELASRNNVTFHTVLQCIWGMLLARYNQTDDVVFGTVISGRDAQVTGIEKMVGLFINTVPTRIRLDKSQSFKELIKSVQEQALEGRTYHDMNLSEVQSLSELKRELLDHILIFENYAVDQSAFETSGKRGAGFVFEEIHAEEQTNYGFNIVAVPGERLVIKLTYDGNIYHDHIIAGIKGHLQQVMEQVVQHEDQSLNDITVLSEAERNRLLYEWNDTKAEYPNQTIHRLFEEQAEKTPELAAVVSGNDKLTYRELNEKSNQLARYLRDKGVKADTIVAIMAERSPEMVVGIMGILKAGGAYLPIDPDYPEERIKYMLEDSGAAIILADHKQDLGTLHQEAVELTGDFSSYPADNLEPAGNADSLAYIIYTSGSTGKPKGVMIRQRGLVNYITWADRVYVQGEQLDFALYSSIAFDLTVTSIFTPLISGNRVIVYRHSEDGEPLIRKVFRDQKAGIVKLTPSHLSLVKDMDASGSSIKRLIVGGEDLKTELAKEITERFHHNIEIYNEYGPTETVVGCMIYQYDAGWDRQVSVPIGKPASNVQLYILDERQEVQPVGIAGELYISGDGVAKGYLNKPELTSEKFLPNPFLPGERMYRTGDLAKMRPDGHIEYLGRIDHQVKIRGYRIELGEIEHQLLRHSDIKEAAVAAKTDQNNDQVLCAYVVSERDITQKDIKTFLAKELPEYMVPSYLLKLDELPLTPNGKVDLKALPEPDRSAGALLEYEPPRHELEEKMAAIWEDILNIEQIGINANIFDIGANSLNVMSFVSRLYAELGFRVPFKDIFSKPTIKELSDFLKHAQDLLKDYTDDCMQLTRAEEGGKNLFCFPPAASMGIAYMGLAKHLKQHSVYSFNFIPSANRIRKYADIIKNIQGEGPYTLIGYSSGGILAFDVAKELNRQGYEVEDLIIIDSKYRTKAEKHQFTEEEYREEISKTFELEKYRDVEKLLSDYLVDLVMKSYVYIQNTVTTGAIDGHISYIKSSDNQRGENMMMWEKATSKTFTVVQGAGTHMQMISKSHPDILERNARLIHDIINKTVKI
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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.
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O68252
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PCEA_SULMU
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Tetrachloroethene reductive dehalogenase (EC 1.21.99.5) (PCE dehalogenase)
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MEKKKKPELSRRDFGKLIIGGGAAATIAPFGVPGANAAEKEKNAAEIRQQFAMTAGSPIIVNDKLERYAEVRTAFTHPTSFFKPNYKGEVKPWFLSAYDEKVRQIENGENGPKMKAKNVGEARAGRALEAAGWTLDINYGNIYPNRFFMLWSGETMTNTQLWAPVGLDRRPPDTTDPVELTNYVKFAARMAGADLVGVARLNRNWVYSEAVTIPADVPYEQSLHKEIEKPIVFKDVPLPIETDDELIIPNTCENVIVAGIAMNREMMQTAPNSMACATTAFCYSRMCMFDMWLCQFIRYMGYYAIPSCNGVGQSVAFAVEAGLGQASRMGACITPEFGPNVRLTKVFTNMPLVPDKPIDFGVTEFCETCKKCARECPSKAITEGPRTFEGRSIHNQSGKLQWQNDYNKCLGYWPESGGYCGVCVAVCPFTKGNIWIHDGVEWLIDNTRFLDPLMLGMDDALGYGAKRNITEVWDGKINTYGLDADHFRDTVSFRKDRVKKS
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Catalyzes the reductive dechlorination of tetrachloroethene (PCE) to trichloroethene (TCE) and of trichloroethene to cis-1,2-dichloroethene (DCE). In addition, trans-1,3-dichloropropene, 1,1,3-trichloropropene and 2,3-dichloropropene are reduced to a mixture of mono-chloropropenes, 1,1-dichloropropene, and 2-chloropropene, respectively. Is also able to convert brominated phenols such as 4-bromophenol (4-BP), 2,4-dibromophenol (2,4-DBP) and 2,4,6-tribromophenol (2,4,6-TBP). Utilizes formate or pyruvate as electron donors. Titanium(III) citrate could also serve as electron donor. Reduced methyl viologen can act as the artificial electron donor.
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O68691
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SCTF_YERPE
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Type 3 secretion system needle filament protein (T3SS needle filament protein) (Yop proteins translocation protein F) (Yop secretion protein F)
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MSNFSGFTKGTDIADLDAVAQTLKKPADDANKAVNDSIAALKDKPDNPALLADLQHSINKWSVIYNINSTIVRSMKDLMQGILQKFP
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Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. YscF/SctF forms the external needle filament that protrudes from the bacterial surface. Essential for the calcium-dependent regulation of T3SS and Yop secretion. Required to block Yop secretion in the presence of extracellular calcium. May be the extracellular T3SS component that senses extracellular calcium and/or participates in transmitting the calcium signal to the cytoplasmic compartment where the block in secretion is initiated. During infection, can induce innate immune responses. The needle proteins interact with host TLR2 or TLR4, and induce signaling by NF-kappa-B and/or AP-1. This activation is MyD88 dependent and results in increased expression of cytokines, including TNF-alpha, IL-6 and IL-8. Innate immune responses are modulated by the N-terminal region of YscF/SctF.
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O68900
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PET_ECO44
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Serine protease pet autotransporter (EC 3.4.21.-) [Cleaved into: Serine protease pet (Plasmid-encoded toxin pet); Serine protease pet translocator]
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MNKIYSIKYSAATGGLIAVSELAKKVICKTNRKISAALLSLAVISYTNIIYAANMDISKAWARDYLDLAQNKGVFQPGSTHVKIKLKDGTDFSFPALPVPDFSSATANGAATSIGGAYAVTVAHNAKNKSSANYQTYGSTQYTQINRMTTGNDFSIQRLNKYVVETRGADTSFNYNENNQNIIDRYGVDVGNGKKEIIGFRVGSGNTTFSGIKTSQTYQADLLSASLFHITNLRANTVGGNKVEYENDSYFTNLTTNGDSGSGVYVFDNKEDKWVLLGTTHGIIGNGKTQKTYVTPFDSKTTNELKQLFIQNVNIDNNTATIGGGKITIGNTTQDIEKNKNNQNKDLVFSGGGKISLKENLDLGYGGFIFDENKKYTVSAEGNNNVTFKGAGIDIGKGSTVDWNIKYASNDALHKIGEGSLNVIQAQNTNLKTGNGTVILGAQKTFNNIYVAGGPGTVQLNAENALGEGDYAGIFFTENGGKLDLNGHNQTFKKIAATDSGTTITNSNTTKESVLSVNNQNNYIYHGNVDGNVRLEHHLDTKQDNARLILDGDIQANSISIKNAPLVMQGHATDHAIFRTTKTNNCPEFLCGVDWVTRIKNAENSVNQKNKTTYKSNNQVSDLSQPDWETRKFRFDNLNIEDSSLSIARNADVEGNIQAKNSVINIGDKTAYIDLYSGKNITGAGFTFRQDIKSGDSIGESKFTGGIMATDGSISIGDKAIVTLNTVSSLDRTALTIHKGANVTASSSLFTTSNIKSGGDLTLTGATESTGEITPSMFYAAGGYELTEDGANFTAKNQASVTGDIKSEKAAKLSFGSADKDNSATRYSQFALAMLDGFDTSYQGSIKAAQSSLAMNNALWKVTGNSELKKLNSTGSMVLFNGGKNIFNTLTVDELTTSNSAFVMRTNTQQADQLIVKNKLEGANNLLLVDFIEKKGNDKNGLNIDLVKAPENTSKDVFKTETQTIGFSDVTPEIKQQEKDGKSVWTLTGYKTVANADAAKKATSLMSGGYKAFLAEVNNLNKRMGDLRDINGEAGAWARIMSGTGSAGGGFSDNYTHVQVGADNKHELDGLDLFTGVTMTYTDSHAGSDAFSGETKSVGAGLYASAMFESGAYIDLIGKYVHHDNEYTATFAGLGTRDYSSHSWYAGAEVGYRYHVTDSAWIEPQAELVYGAVSGKQFSWKDQGMNLTMKDKDFNPLIGRTGVDVGKSFSGKDWKVTARAGLGYQFDLFANGETVLRDASGEKRIKGEKDGRMLMNVGLNAEIRDNVRFGLEFEKSAFGKYNVDNAINANFRYSF
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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.
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O69078
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CSRA_PSEAE
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Translational regulator CsrA (Carbon storage regulator) (Global translational regulatory protein RsmA)
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MLILTRRVGETLMVGDDVTVTVLGVKGNQVRIGVNAPKEVAVHREEIYQRIQKEKDQEPNH
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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'-UTR binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s). {ECO:0000255|HAMAP-Rule:MF_00167}. Binds to mRNA to regulate gene activity at a post-transcriptional level (Probable). Represses expression of many toxic extracellular enzymes and compounds decreases translation of lasI and rhlI. Positively controls swarming motility and rhanolipid and lipase, possibly via expression of rhlA activates transcription of the CsrA/RsmA antagonistic sRNA RsmZ. Overexpression dramatically reduces extracellular protease, elastase (lasB) and staphyolytic (lasA) activities, decreases HCN production, decreases levels of autoinducers 3-oxo-C12-HSL (3-oxo-N-(tetrahydro-2-oxo-3-furanyl)-dodecanamide) and C4-HSL (N-butanoylhomoserine lactone), and abolishes production of cytotoxic internal lectin PA-IL (lecA). Control of hcn expression is post-transcriptional. Replaces endogenous gene(s) in E.coli and P.fluorescens. Probably binds to and is sequestered by non-coding small RNA (sRNA) RsmZ overexpression of rsmZ produces very similar phenotypes to deletion of rsmA, while rsmZ deletion has no phenotype.
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O69199
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CYAB_AERHY
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Adenylate cyclase CyaB (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase)
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MSSQHFQGRFEVEFKYRLSDVDAFTCALAALNPEVMLEDNQEQDSYFDTPEHSLAAEGKSLVIRTMQPSGIQLWIVKGPEADRCEAVNITDADKAASMLRTLGYRQVLAISKRRSIYFVGPFHVTRDHLEGIGDFAELAIMTDDEALLPDYRQQLQDLATRLGLSSAQLETRSYRTLCEQSLTLNSEKVPS
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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 slight preference for ThTP over ATP and PPPi in the presence of manganese ions. This PPPase activity is probably not of physiological importance.
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O69652
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CDS1_MYCTU
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L-cysteine desulfhydrase Cds1 (EC 4.4.1.1)
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MSGGACIAVRSLSRSWTDNAIRLIEADARRSADTHLLRYPLPAAWCTDVDVELYLKDETTHITGSLKHRLARSLFLYALCNGWINENTTVVEASSGSTAVSEAYFAALLGLPFIAVMPAATSASKIALIESQGGRCHFVQNSSQVYAEAERVAKETGGHYLDQFTNAERATDWRGNNNIAESIYVQMREEKHPTPEWIVVGAGTGGTSATIGRYIRYRRHATRLCVVDPENSAFFPAYSEGRYDIVMPTSSRIEGIGRPRVEPSFLPGVVDRMVAVPDAASIAAARHVSAVLGRRVGPSTGTNLWGAFGLLAEMVKQGRSGSVVTLLADSGDRYADTYFSDEWVSAQGLDPAGPAAALVEFERSCRWT
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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 contributes to redox homeostasis. Probably eliminates toxic levels of Cys (which can induce oxidative stress).
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O69711
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NMTR_MYCTU
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HTH-type transcriptional regulator NmtR
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MGHGVEGRNRPSAPLDSQAAAQVASTLQALATPSRLMILTQLRNGPLPVTDLAEAIGMEQSAVSHQLRVLRNLGLVVGDRAGRSIVYSLYDTHVAQLLDEAIYHSEHLHLGLSDRHPSAG
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Represses transcription of ctpJ/nmtA, by binding to its promoter region.
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O69729
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TCRY_MYCTU
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Probable sensor histidine kinase TcrY (EC 2.7.13.3)
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MGITAATEMALRRHLVAQLDNQLGGTSYRSVLMYPEKMPRPPWRHETHNYIRSGPGPRFLDAPGQPAGMVAAVVSDGTTVAAGYLTGSGSRAALTSTGRSQLERIAGSRTPLTLDLDGLGRYRVLAAPSRNGHDVIVTGLSMGNVDATMLQMLIIFGIVTVIALVAATTAGIVIIKRALAPLRRVAQTASEVVDLPLDRGEVKLPVRVPEPDANPSTEVGQLGSALNRMLDHIAAALSARQASETCVRQFVADASHELRTPLAAIRGYTELTQRIGDDPEAVAHAMSRVASETERITRLVEDLLLLARLDSGRPLERGPVDMSRLAVDAVSDAHVAGPDHQWALDLPPEPVVIPGDAARLHQVVTNLLANARVHTGPGTIVTTRLSTGPTHVVLQVIDNGPGIPAALQSEVFERFARGDTSRSRQAGSTGLGLAIVSAVVKAHNGTITVSSSPGYTEFAVRLPLDGWQPLESSPR
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Member of the two-component regulatory system TcrY/TcrX. Activates TcrX by phosphorylation.
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O69762
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HCHL_PSEFL
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Hydroxycinnamoyl-CoA hydratase-lyase (HCHL) (EC 4.1.2.61) (P-hydroxycinnamoyl CoA hydratase/lyase) (Trans-feruloyl-CoA hydratase/vanillin synthase)
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MSTYEGRWKTVKVEIEDGIAFVILNRPEKRNAMSPTLNREMIDVLETLEQDPAAGVLVLTGAGEAWTAGMDLKEYFREVDAGPEILQEKIRREASQWQWKLLRMYAKPTIAMVNGWCFGGGFSPLVACDLAICADEATFGLSEINWGIPPGNLVSKAMADTVGHRQSLYYIMTGKTFGGQKAAEMGLVNESVPLAQLREVTIELARNLLEKNPVVLRAAKHGFKRCRELTWEQNEDYLYAKLDQSRLLDTEGGREQGMKQFLDDKSIKPGLQAYKR
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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). The enzyme is also active with caffeoyl-CoA and 4-coumaroyl-CoA producing 3,4-dihydroxybenzaldehyde and 4-hydroxybenzaldehyde, respectively.
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O70126
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AURKB_MOUSE
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Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B)
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MAQKENAYPWPYGSKTSQSGLNTLSQRVLRKEPATTSALALVNRFNSQSTAAPGQKLAENKSQGSTASQGSQNKQPFTIDNFEIGRPLGKGKFGNVYLAREKKSRFIVALKILFKSQIEKEGVEHQLRREIEIQAHLKHPNILQLYNYFYDQQRIYLILEYAPRGELYKELQKSRTFDEQRTATIMEELSDALTYCHKKKVIHRDIKPENLLLGLQGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEMVDLWCIGVLCYELMVGNPPFESPSHSETYRRIVKVDLKFPSSVPSGAQDLISKLLKHNPWQRLPLAEVAAHPWVRANSRRVLPPSAL
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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 microtubule stabilization and spindle assembly (By similarity). Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis (By similarity). Required for central/midzone spindle assembly and cleavage furrow formation (By similarity). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (By similarity). AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP (By similarity). Phosphorylation of INCENP leads to increased AURKB activity (By similarity). Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPTIN1, VIM/vimentin, HASPIN, and histone H3 (By similarity). A positive feedback loop involving HASPIN and AURKB contributes to localization of CPC to centromeres (By similarity). Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). AURKB is also required for kinetochore localization of BUB1 and SGO1 (By similarity). Phosphorylation of p53/TP53 negatively regulates its transcriptional activity (By similarity). Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes. Acts as an inhibitor of CGAS during mitosis: catalyzes phosphorylation of the N-terminus of CGAS during the G2-M transition, blocking CGAS liquid phase separation and activation, and thereby preventing CGAS-induced autoimmunity (By similarity). Phosphorylates KRT5 during anaphase and telophase.
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O70127
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ABCBB_RAT
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Bile salt export pump (EC 7.6.2.-) (ATP-binding cassette sub-family B member 11) (Sister of P-glycoprotein)
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MSDSVILRSVKKFGEENHAFESDGSHNNDKKSRLQDKMKEGDIRVGFFELFRFSSSKDIWLMLMGGVCALLHGMAQPGILIIFGIMTDIFIKYDIERQELEIPGKACVNNTIVWINSSFHQNMTNGTVCGLVDIESEMIKFSGIYAGVGMTVLILGYFQIRLWVITGARQIRRMRKIYFRRIMRMEIGWFDCTSVGELNSRFADDIEKINDAIADQLAHFLQRMSTAMCGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSIAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYEKNLVFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSTLVLDEEEYTPGTLVQIFLCVILAAMNIGHASSCLEIFSTGCSAATNIFQTIDRQPVIDCMSGDGYKLDRIKGEIEFHNVTFHYPSRPDVKILDNLSMVIKPGETTALVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRFGREDATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEARVQEALNKIQHGHTIISVAHRLSTVRAADVIIGFEHGVAVERGTHEELLERKGVYFMLVTLQSQGDNAHKETSIMGKDATEGGTLERTFSRGSYRDSLRASIRQRSKSQLSLLTHDPPLAVADHKSSYKDSKDNDVLVEEVEPAPVRRILKYNIPEWHYILVGSLSAAINGAVTPIYSLLFSQLLGTFSLLDKEQQRSEIHSMCLFFVILGCVSIFTQFLQGYTFAKSGELLTKRLRKFGFKAMLGQDIGWFDDLRNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIIAALLIAFFFSWKLSLIITIFFPFLALSGAVQTKMLTGFASQDKQALEKAGQITSEALSNIRTVAGIGVEGRFIKAFEVELQTSYKTAVRKANIYGLCFAFSQGIAFLANSAAYRYGGYLIAYEGLGFSHVFRVVSSVALSATAVGRTFSYTPSYAKAKISAARFFQLLDRKPPINVYSEAGEKWDNFQGKIDFIDCKFTYPSRPDIQVLNGLSVSVNPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNIQFLRSNIGIVSQEPVLFDCSIMDNIKYGDNTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQTALDKAREGRTCIVIAHRLSTIQNSDIIAVVSQGVVIEKGTHEKLMAQKGAYYKLVITGAPIS
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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 lipid secretion in a bile salts dependent manner. Transports taurine-conjugated bile salts more rapidly than glycine-conjugated bile salts. Also transports non-bile acid compounds, such as pravastatin and fexofenadine in an ATP-dependent manner and may be involved in their biliary excretion.
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O70131
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NINJ1_MOUSE
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Ninjurin-1 (Nerve injury-induced protein 1) [Cleaved into: Secreted ninjurin-1 (Soluble ninjurin-1) (sNinJ1)]
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MESGTEEYELNGDLRPGSPGSPDALPPRWGLRNRPINVNHYANKKSAAESMLDIALLMANASQLKAVVEQGNDFAFFVPLVVLISISLVLQIGVGVLLIFLVKYDLNNPAKHAKLDFLNNLATGLVFIIVVVNIFITAFGVQKPVMDVAPRQ
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[Ninjurin-1]: Homophilic transmembrane adhesion molecule involved in various processes such as inflammation, cell death, axonal growth, cell chemotaxis and angiogenesis. Promotes cell adhesion by mediating homophilic interactions via its extracellular N-terminal adhesion motif (N-NAM). Involved in the progression of the inflammatory stress by promoting cell-to-cell interactions between immune cells and endothelial cells. Involved in leukocyte migration during inflammation by promoting transendothelial migration of macrophages via homotypic binding. Promotes the migration of monocytes across the brain endothelium to central nervous system inflammatory lesions (By similarity). Acts as a regulator of Toll-like receptor 4 (TLR4) signaling triggered by lipopolysaccharide (LPS) during systemic inflammation directly binds LPS. Acts as a mediator of both programmed and necrotic cell death. Plays a key role in the induction of plasma membrane rupture during programmed and necrotic cell death: oligomerizes in response to death stimuli to mediate plasma membrane rupture (cytolysis), leading to release intracellular molecules named damage-associated molecular patterns (DAMPs) that propagate the inflammatory response. Plays a role in nerve regeneration by promoting maturation of Schwann cells. Acts as a regulator of angiogenesis. Promotes the formation of new vessels by mediating the interaction between capillary pericyte cells and endothelial cells. Also mediates vascular functions in penile tissue as well as vascular formation. Promotes osteoclasts development by enhancing the survival of prefusion osteoclasts. Also involved in striated muscle growth and differentiation. Also involved in cell senescence in a p53/TP53 manner, possibly by acting as an indirect regulator of p53/TP53 mRNA translation. [Secreted ninjurin-1]: Secreted form generated by cleavage, which has chemotactic activity. Acts as an anti-inflammatory mediator by promoting monocyte recruitment, thereby ameliorating atherosclerosis.
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O70132
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FEV_RAT
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Protein FEV (PC12 ETS domain-containing transcription factor 1) (PC12 ETS factor 1) (Pet-1)
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MRQSGTSQPLLINMYLPDPVGDGLFKEGKSPSWGPLSPAVQKGSGQIQLWQFLLELLADRANAGCIAWEGGHGEFKLTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMSKVHGKRYAYRFDFQGLAQACQPPPAHAHAAAAAAAAAAAAQDGALYKLPAGLAPLPFPGLSKLNLMAASAGVAPAGFSYWPGPNATAAAAATAALYPTPGLQPPPGPFGAVAAASHLGGHYH
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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.
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O70133
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DHX9_MOUSE
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ATP-dependent RNA helicase A (EC 3.6.4.13) (DEAH box protein 9) (mHEL-5) (Nuclear DNA helicase II) (NDH II) (RNA helicase A) (RHA)
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MGDIKNFLYAWCGKRKMTPAYEIRAVGNKNRQKFMCEVRVEGFNYAGMGNSTNKKDAQSNAARDFVNYLVRINEVKSEEVPAVGIVPPPPILSDTSDSTASAAEGLPAPMGGPLPPHLALKAEENNSGVESSGYGSPGPTWDRGANLKDYYSRKEEQEVQATLESEEVDLNAGLHGNWTLENAKARLNQYFQKEKIQGEYKYTQVGPDHNRSFIAEMTIYIKQLGRRIFAREHGSNKKLAAQSCALSLVRQLYHLGVIEAYSGLTKKKEGERVEPYKVFLSPDLELQLQNVVQELDLEIVPPPVDPSMPVILNIGKLAHFEPSQRQNAVGVVPWSPPQSNWNPWTSSNIDEGPLAYASTEQISMDLKNELTYQMEQDHNLQSVLQERELLPVKKFEAEILEAISSNSVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVAVAERVAYERGEEPGKSCGYSVRFESILPRPHASIMFCTVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVLAYPEVRIVLMSATIDTTMFCEYFFNCPIIEVYGRTFPVQEYFLEDCIQMTQFIPPPKDKKKKDKEDDGGEDDDANCNLICGDEYGPETKLSMSQLNEKETPFELIEALLKYIETLNVPGAVLVFLPGWNLIYTMQKHLENNSHFGSHRYQILPLHSQIPREEQRKVFDPVPDGVTKVILSTNIAETSITINDVVYVIDSCKQKVKLFTAHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSRARFDRLETHMTPEMFRTPLHEIALSIKLLRLGGIGQFLAKAIEPPPLDAIIEAEHTLRELDALDANDELTPLGRILAKLPIEPRFGKMMIMGCIFYVGDAVCTISAATCFPEPFISEGKRLGYIHRNFAGNRFSDHVALLSVFQAWDDARMSGEEAEIRFCEQKRLNMATLRMTWEAKVQLKEILINSGFPEDCLLTQVFTNTGPDNNLDVVISLLAFGVYPNVCYHKEKRKILTTEGRNALIHKSSVNCPFSSQDMKYPSPFFVFGEKIRTRAISAKGMTLVTPLQLLLFASKKVQSDGQIVFIDDWIRLQISHEAAACITIRAAMEALVVEVSKQPNIISQLDPVNEHMLNTIRQISRPSAAGINLMIGSVRYGDGPRPPKMARYDNGSGYRRGYGGGGYGGGGYGGGYGSGGFGGGFGSGGGFGGGFNSGGGGFGSGGGGFGSGGGGFGGGGGGFSGGGGGGFGGGRGGGGGGFGGSGGFGNGGGGYGVGGGGYGGGGGGGYGGGSGGYGGGGYGGGEGYSISPNSYRGNYGGGGGGYRGGSQGGYRNNFGGDYRGSSGDYRGSGGGYRGSGGFQRRGYGGGYFGQGRGGGGGGGY
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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'-single-stranded tail as entry site for acid nuclei unwinding activities as well as the binding and hydrolyzing of any of the four ribo- or deoxyribo-nucleotide triphosphates (NTPs). Unwinds numerous nucleic acid substrates such as double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA forks composed of either partially complementary DNA duplexes or DNA:RNA hybrids, respectively, and also DNA and RNA displacement loops (D- and R-loops), triplex-helical DNA (H-DNA) structure and DNA- and RNA-based G-quadruplexes. Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA. Binds also to circular dsDNA or dsRNA of either linear and/or circular forms and stimulates the relaxation of supercoiled DNAs catalyzed by topoisomerase TOP2A. Plays a role in DNA replication at origins of replication and cell cycle progression. Plays a role as a transcriptional coactivator acting as a bridging factor between polymerase II holoenzyme and transcription factors or cofactors, such as BRCA1, CREBBP, RELA and SMN1. Binds to the CDKN2A promoter. Plays several roles in post-transcriptional regulation of gene expression. In cooperation with NUP98, promotes pre-mRNA alternative splicing activities of a subset of genes (By similarity). As component of a large PER complex, is involved in the negative regulation of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. Acts also as a nuclear resolvase that is able to bind and neutralize harmful massive secondary double-stranded RNA structures formed by inverted-repeat Alu retrotransposon elements that are inserted and transcribed as parts of genes during the process of gene transposition. Involved in the positive regulation of nuclear export of constitutive transport element (CTE)-containing unspliced mRNA. Component of the coding region determinant (CRD)-mediated complex that promotes cytoplasmic MYC mRNA stability. Plays a role in mRNA translation. Positively regulates translation of selected mRNAs through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR). Involved with LARP6 in the translation stimulation of type I collagen mRNAs for CO1A1 and CO1A2 through binding of a specific stem-loop structure in their 5'-UTRs. Stimulates LIN28A-dependent mRNA translation probably by facilitating ribonucleoprotein remodeling during the process of translation. Also plays a role as a small interfering (siRNA)-loading factor involved in the RNA-induced silencing complex (RISC) loading complex (RLC) assembly, and hence functions in the RISC-mediated gene silencing process. Binds preferentially to short double-stranded RNA, such as those produced during rotavirus intestinal infection. This interaction may mediate NLRP9 inflammasome activation and trigger inflammatory response, including IL18 release and pyroptosis. Finally, mediates the attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin filaments in the nucleus (By similarity).
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O70137
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ALX3_MOUSE
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Homeobox protein aristaless-like 3 (Proline-rich transcription factor ALX3)
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MDPERCAPFSVGPAAGPYAAAGDEAPGPQGTPDAAPHLHPAPPRGPRLSRFPACGPLEPYLPEPAKPPAKYLQDLGPGPVLNGGHFYEGSAEAEEKASKAASFPQLPVDCRGGPRDGPSNVQASPGPCLASLSVPLSPGLPDSMELAKTKSKKRRNRTTFSTFQLEELEKVFQKTHYPDVYAREQLALRTDLTEARVQVWFQNRRAKWRKRERYGKMQEGRNPFTTAYDISVLPRTDSHPQLQNSLWPSPGSGSPGGPCLMSPEGIPSPCMSPYSHSHGNVAGFMGVPASPAAHPGIYSIHGFPPALGGHSFEPSPDGDYKSPSLVSLRMKPKEPPGLLNWTT
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Transcriptional regulator with a possible role in patterning of mesoderm during development.
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O70138
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MMP8_MOUSE
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Neutrophil collagenase (EC 3.4.24.34) (Collagenase 2) (Matrix metalloproteinase-8) (MMP-8)
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MFRLKTLPLLIFLHTQLANAFPVPEHLEEKNIKTAENYLRKFYNLPSNQFRSSRNATMVAEKLKEMQRFFSLAETGKLDAATMGIMEMPRCGVPDSGDFLLTPGSPKWTHTNLTYRIINHTPQLSRAEVKTAIEKAFHVWSVASPLTFTEILQGEADINIAFVSRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDSEETWTQDSKNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYGPSDNPIQPTGPSTPKACDPHLRFDATTTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSGYDLQQGYPRDISNYGFPRSVQAIDAAVSYNGKTYFFINNQCWRYDNQRRSMDPGYPKSIPSMFPGVNCRVDAVFLQDSFFLFFSGPQYFAFNFVSHRVTRVARSNLWLNCS
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Can degrade fibrillar type I, II, and III collagens. May play a role in the degradation of collagen fibers during uterine involution.
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O70143
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SHC3_RAT
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SHC-transforming protein 3 (Neuronal Shc) (N-Shc) (SHC-transforming protein C) (Src homology 2 domain-containing-transforming protein C3) (SH2 domain protein C3)
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MLPRTKYNRFRNDSVTSVDDLLHSLSVSGSGGKVSAEPAASPYLVSGEALRKAPDDGPGSLGHLLHKVSHLKLSSSGLRGLSSAARERAGARLSGSCSAPSLAAPDGGSATPGSRAPAASMSATRKSRASDEPLPRPPRGAPHASDQVLGSGVTYVVKYLGCIEVLRSMRSLDFSTRTQVTREAISRVCEAVPGAKGAFKKRKPPSKMLSSILGKSNLQFAGMSISLTISTASLNLRTPDSKQIISNHHMRSISFASGGDPDTTDYVAYVAKDPVNRRACHILECCDGLAQDVIGSIGQAFELRFKQYLQCPSKIPALQDRMQSLDEPWTEEEGDGPDHPYYNSVPNKMPPPGGFLDARLKARPHAPDAAQFSGKEQTYYQGRHLGDAFGEDWQRAPTRQGSLDIYSTPEGKAHMVPVGETPTYVNTQPVPPQVWPAATSSTESSPRKDLFDMKPFEDALRNQPLGPVLSKAASVECISPVTPRAPDAKMLEELNAEPWYQGEMSRKEAEALLQEDGDFLVRKSTTNPGSFVLTGMHNGQAKHLLLVDPEGTVRTKDRVFDSISHLITYHLESSLPIVSAGSELCLRQPVERKP
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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).
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O70145
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NCF2_MOUSE
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Neutrophil cytosol factor 2 (NCF-2) (67 kDa neutrophil oxidase factor) (NADPH oxidase activator 2) (Neutrophil NADPH oxidase factor 2) (p67-phox)
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MSLAEAIRLWNEGVLAADKKDWKGALEAFSEVQDPHSRICFNIGCVNTILENLQAAEQAFTKSINRDKHSAVAYFQRGMLYYRMEKYDLAIKDLKEALTQLRGNQLIDYKILGLQFKLFACEVLYNIALMHAKKEEWKKAEEQLALATNMKSEPRHSKIDKAMESIWKQKLFEPVVIPVGRLFRPNERQVAQLAKKDYLGKATVVASVVHQDNFSGFAPLQPQSAEPPPRPKTPEIFRALEGEAHRVLFGFVPETPEELQVMPGNIVFVLKKGSDNWATVMFNGQKGLVPCNYLEPVELRIHPQSQPQEDTSPESDIPPPPNSSPPGRLQLSPGHKQKEPKELKLSVPMPYMLKVHYKYTVVMETRLGLPYSQLRNMVSKKLALSPEHTKLSYRRRDSHELLLLSEESMKDAWGQVKNYCLTLWCEHTVGDQGLIDEPIQRENSDASKQTTEPQPKEGTQVVAIFSYEAAQPEDLEFVEGDVILVLSHVNEEWLEGECKGKVGIFPKAFVEGCAAKNLEGIPREV
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NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).
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O70146
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TESK1_MOUSE
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Dual specificity testis-specific protein kinase 1 (EC 2.7.12.1) (Testicular protein kinase 1)
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MAGERPPLRGPGPGEAPGEGPGGAGGGPGRGRPSSYRALRSAVSSLARVDDFDCAEKIGAGFFSEVYKVRHRQSGQVMVLKMNKLPSNRSNTLREVQLMNRLRHPNILRFMGVCVHQGQLHALTEYMNGGTLEQLLSSPEPLSWPVRLHLALDIAQGLRYLHAKGVFHRDLTSKNCLVRREDRGFTAVVGDFGLAEKIPVYREGTRKEPLAVVGSPYWMAPEVLRGELYDEKADVFAFGIVLCELIARVPADPDYLPRTEDFGLDVPAFRTLVGNDCPLPFLLLAIHCCSMEPSTRAPFTEITQHLEQILEQQPEATPLAKPPLTKAPLTYNQGSVPRGGPSATLPRPDPRLSRSRSDLFLPPSPESPPSWGDNLTRVNPFSLREDLRGGKIKLLDTPCKPATPLPLVPPSPLTSTQLPLVTTPDILVQPETPVRRCRSLPSSPELPRRMETALPGPGPSPMGPTEERMDCEGSSPEPEPPGLAPQLPLAVATDNFISTCSSASQPWSPRSGPPLNNNPPAVVVNSPQGWAREPWNRAQHSLPRAAALERTEPSPPPSAPREPEEGLPCPGCCLGPFSFGFLSMCPRPTPAVARYRNLNCEAGSLLCHRGHHAKPPTPSLQLPGARS
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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 microtubule breakdown via inhibition of TAOK1/MARKK kinase activity (By similarity). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1. Positively regulates integrin-mediated cell spreading, via phosphorylation of cofilin (By similarity). Suppresses ciliogenesis via multiple pathways phosphorylation of CFL1, suppression of ciliary vesicle directional trafficking to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (By similarity). Probably plays a central role at and after the meiotic phase of spermatogenesis (By similarity).
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O70150
|
KCC1B_RAT
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Calcium/calmodulin-dependent protein kinase type 1B (EC 2.7.11.17) (CaM kinase I beta) (CaM kinase IB) (CaM-KI beta) (CaMKI-beta) (Pregnancy up-regulated non-ubiquitously-expressed CaM kinase homolog)
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MLLLKKQTEDISSVYEIREKLGSGAFSEVMLAQERGSAHLVALKCIPKKALRGKEALVENEIAVLRRISHPNIVALEDVHESPSHLYLAMELVTGGELFDRIMERGSYTEKDASHLVGQVLGAVSYLHSLGIVHRDLKPENLLYATPFEDSKIMVSDFGLSKIQAGNMLGTACGTPGYVAPELLEQKPYGKAVDVWALGVISYILLCGYPPFYDESDPELFSQILRASYEFDSPFWDDISESAKDFIRHLLERDPQKRFTCQQALQHLWISGDAALDRDILGSVSEQIQKNFARTHWKRAFNATSFLRHIRKLGQSPEGEEASRQGMTRHSHPGLGTSQSPKW
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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.
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O70152
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DPM1_MOUSE
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Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83) (Dolichol-phosphate mannose synthase subunit 1) (DPM synthase subunit 1) (Dolichyl-phosphate beta-D-mannosyltransferase subunit 1) (Mannose-P-dolichol synthase subunit 1) (MPD synthase)
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MASTGASRSLAASPRPPQGRSSRQDKYSVLLPTYNERENLPLIVWLLVKSFSESAINYEIIIIDDGSPDGTREVAEQLAEIYGPDRILLRPREKKLGLGTAYIHGIKHATGNYVIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFITQILLRPGASDLTGSFRLYRKEVLQKLIEKCVSKGYVFQMEMIVRARQMNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT
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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 (DPM) synthase complex.
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O70156
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OLR1_RAT
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Oxidized low-density lipoprotein receptor 1 (Ox-LDL receptor 1) (Lectin-like oxidized LDL receptor 1) (LOX-1) (Lectin-like oxLDL receptor 1) (Lectin-type oxidized LDL receptor 1) [Cleaved into: Oxidized low-density lipoprotein receptor 1, soluble form]
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MAFDDKMKPVNGQPDQKSCGKKPKGLHLLSSTWWCPAAVTLAILCLVLSVTLIVQQTQLLQVSDLLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAANSSGPCPQDWIWHKENCYLFHGPFNWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHSTSPFWMGLHRKNPNHPWLWENGSPLSFQFFRTRGVSLQMYSSGTCAYIQGGVVFAENCILTAFSICQKKANLLLTQ
|
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-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria.
|
O70157
|
TOP3A_MOUSE
|
DNA topoisomerase 3-alpha (EC 5.6.2.1) (DNA topoisomerase III alpha)
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MIFPVTLLAFQWHRRPGGRALSRAAMEVAFRGVRKVLCVAEKNDAAKGIADLLSNGRMRRKEGLSKFNKIYEFDYHLYGQNVTMIMTSVSGHLLAHDFQMQFRKWQSCNPLVLFEAEIEKYCPENFIDIKKTLERETHHCQALVIWTDCDREGENIGFEIIHVCKAVKPNLRVLRARFSEITPHAVRTACENLTEPDQRVSDAVDVRQELDLRIGAAFTRFQTLRLQRIFPEVLAEQLISYGSCQFPTLGFVVERFKAIQAFVPEVFHKIKVTHDHKDGTVEFNWKRYRLFNHTACLVLYQLCMEDPMATVVEVRSKPKSKWRPQALDTVELEKLASRKLRINAKETMRIAEKLYTQGYISYPRTETNIFPKDLNLVALVEQQTVDPHWGAFAQTILERGGPTPRNGSKSDQAHPPIHPTKYTSGLQGDDRRLYEFIVRHFLACCSQDAQGQETTVEIDIAQERFVAHGLIILARNYLDVYPYDHWSDKLLPVYEQGSHFQPSTVEMVDGETSPPQLLTEADLIALMEKHGIGTDATHAEHIETIKARMYVGLTSDKRFLPGHLGMGLVEGYDSMGYEMSKPDLRAELEADLKLICEGKKDKFQVLRQQVQKYKQVFIEAVAKAKKLDEALSQYLGERTEMAQQEEIYPAMPEPVRKCPQCNKDMVLKTKKSGGFYLSCMGFPECRSAVWFPDSVLEASRDNSVCSVCQPPPVYRLKLKFKRGSLPPAMPLEFVGCIGGCDETLKEIFGLRFPRALPRASQPSGHLQASQALNRMDSSQHNLSQPLVNRHTRPSKTVAQALLPPTTAGESNSVTCNCGREAVLLTVRKQGPNQGRHFYKCSNGDCNFFLWADSSHSTGGGTPTSASGPPGSSVGCPSSVGSHMDGFGSLGSDSDGGTPCLCGQPAVTRTVQKDGPNKGRQFHTCAKPREQQCGFFQWVDENVAPGSFAAPAWPGGRGKAQRPEAASKRPRAGSSDAGSTVKKPRKCSLCHQPGHTRTFCPQNR
|
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. As an essential component of the RMI complex it is involved in chromosome separation and the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity. It is required for mtDNA decatenation and segregation after completion of replication, in a process that does not require BLM, RMI1 and RMI2.
|
O70161
|
PI51C_MOUSE
|
Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (PIP5K1-gamma) (PtdIns(4)P-5-kinase 1 gamma) (EC 2.7.1.68) (Phosphatidylinositol 4-phosphate 5-kinase type I gamma) (PIP5KIgamma)
|
MELEVPDEAESAEAGAVTAEAAWSAESGAAAGMTQKKAGLAEAPLVTGQPGPGHGKKLGHRGVDASGETTYKKTTSSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQQERERQAEGAQSKADEKRPVAQKALYSTAMESIQGGAARGEAIETDDTMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSSTVFRKSSSLKSSPSKKGRGALLAVKPLGPTAAFSASQIPSEREDVQYDLRGARSYPTLEDEGRPDLLPCTPPSFEEATTASIATTLSSTSLSIPERSPSDTSEQPRYRRRTQSSGQDGRPQEEPHAEDLQKITVQVEPVCGVGVVPKEEGAGVEVPPCGASAAASVEIDAASQASEPASQASDEEDAPSTDIYFPTDERSWVYSPLHYSARPASDGESDT
|
Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility. PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By similarity). PIP5K1A-mediated phosphorylation of PtdIns(4)P is the predominant pathway for PtdIns(4,5)P2 synthesis (By similarity). Together with PIP5K1A, is required for phagocytosis, both enzymes regulating different types of actin remodeling at sequential steps. Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport. Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis (By similarity). Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2). Required for clathrin-coated pits assembly at the synapse (By similarity). Participates in cell junction assembly (By similarity). Modulates adherens junctions formation by facilitating CDH1/cadherin trafficking (By similarity). Required for focal adhesion dynamics. Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions (By similarity). Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins (By similarity). Required for uropodium formation and retraction of the cell rear during directed migration. Has a role in growth factor-stimulated directional cell migration and adhesion. Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor. Negative regulator of T-cell activation and adhesion. Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor. Together with PIP5K1A has a role during embryogenesis and together with PIP5K1B may have a role immediately after birth.
|
O70165
|
FCN1_MOUSE
|
Ficolin-1 (Collagen/fibrinogen domain-containing protein 1) (Ficolin-A) (Ficolin-alpha) (M-ficolin)
|
MQWPTLWAFSGLLCLCPSQALGQERGACPDVKVVGLGAQDKVVVIQSCPGFPGPPGPKGEPGSPAGRGERGFQGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGEKELGDTLCQRGPRSCKDLLTRGIFLTGWYTIHLPDCRPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYLHLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFLEGTAGDSLTKHNNMSFTTHDQDNDANSMNCAALFHGAWWYHNCHQSNLNGRYLSGSHESYADGINWGTGQGHHYSYKVAEMKIRAS
|
Extracellular lectin functioning as a pattern-recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8. Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage (By similarity).
|
O70166
|
STMN3_MOUSE
|
Stathmin-3 (Hippocampus abundant transcript 3) (SCG10-like protein) (SCG10-related protein HiAT3)
|
MASTVSAYKEKMKELSVLSLICSCFYSQPHPNTIYQYGDMEVKQLDKRASGQSFEVILKSPSDLSPESPVLSSPPKRKDASLEELQKRLEAAEERRKTQEAQVLKQLAERREHEREVLHKALEENNNFSRLAEEKLNYKMELSKEIREAHLAALRERLREKELHAAEVRRNKEQREEMSG
|
Exhibits microtubule-destabilizing activity, which is antagonized by STAT3.
|
O70167
|
P3C2G_MOUSE
|
Phosphatidylinositol 3-kinase C2 domain-containing subunit gamma (PI3K-C2-gamma) (PtdIns-3-kinase C2 subunit gamma) (EC 2.7.1.137) (EC 2.7.1.154) (Phosphoinositide 3-kinase-C2-gamma)
|
MAYSWQTEPNRTEPQEDGSDTQQFHHTNQHLSSRQVRLGFDQLVEEINNKTPLSESEKEEDTYFVPDAPNLGSKWPSIYETHPRYFSEFTSQSPDSSQLRFGKLSAIGFNPAVLPTHQLIHEGASWRNPSGKYHGIEYPRFDALPPSSTGQGECNPQGQSGTKHHNYCGEHEGNLPHHHSSYSIDSIPNREKRRSGDVNLVEPSLEFSKDSFLPRTSENVSVESTEPIGCPIEIVEVPQGSNKNLASFCNKVKKIRESYHASDINSNSGKIWAITTAYPSRLFADTKFRVKISIDNSAQLLLLMPHANYLVKDLIAEILLLCANEPLSPKEYLLSVCGSEEFLQMDHSLGSHKIFQKNKSVIQLHLQKNRDTPGKLSRKSEDDHSPFHLNQLLEFTHIWKISRQCLSTVMKKYNLHVEHLLKPQKDMEEKHLSSMVSGNQHTSQPHVNNVLEEVKNICSVLGCIETKQVSDAVKELNLILQRPSQNFHQNSETSKKGFIERVTAELSRSIYQLIDVYCSSFCTDFQPVHTPGGVSHVHAGLQSHLSFTVCSLHNVPETWAHSYKAFSFSCWLTYAGKKLCQVKSCRPLPVTKSFSLLVNWNEIINFPLEIKSLPRESMLVIKLFGIDSATHSTNLLAWTCLPLFPRQESVLGSRLFSVTLQSEPPIEMIAPGVWDGSQPSPLTLQIDFPDAGWEYLKPESEENRTDHEEPPRECLKHIAKLSQKKSPLLLSEEKRRYLWFYRLYCNNENSSLPLVLGSAPGWDEETVSEMHAILRRWTFSHPWEALGLLTSRFPDQDIREVAVQQLDTLLTDELLDCLPQLVQAVKFEWNLESPLVELLPRRPLQSIRVAHCLYWLLRDAQGEAYFKSWYQELLAALQFCAGEALNEELSKEQKLVKLLGDIGEKVKSASDPQRKDVLKKEIGSLEEFFKDIKTCHLPLNPALCIKGIDRDACSYFTSNASPLKITFINANPMGKNISVIFKAGDDLRQDMLALQIIQVMDNAWLQEGLDMQMITYGCLSTGRAQGFIEMVPDAVTLAKIHLHSGLIGPLKENTIKKWFSQHNHLKEDYEKALRNFFYSCAGWCVVTFILGVCDRHNDNIMLTKSGHMFHIDFGKFLGHAQTFGGIKRDRAPFIFTSEMEYFITEGGKNIQHFQDFVELCCRAYNIVRKHSQLILSLLEMMLHAGLPELRGIEDLKYVHNNLRPQDTDLEATSHFTKKIKESLECFPVKLNNLIHTLAQMPALSLAKPAPQTLLQESCILNKTRTIQRVTILGFSKTHSNLYLMEVTCSDNRRSLTKKSFEQFYRLHSQMQKQFSSLALPEFPHWWHLPFTDSDHKRIRDLSHYVEQVLRGSYEVANSDCVLSFFLSEHIQPTLEDSPFVDPGENSLDKSPKVQLLMTYEDSRLTILVKHLKNIHLPDGSVPSAHVEIYLLPHPSEVRRKKTKCVPKCTDPTYNEIVVYDEVLGLQGHVLMLIVKSKTVFVGAVNIQLCSVPLNEEKWYPLGNSII
|
Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. May play a role in SDF1A-stimulated chemotaxis.
|
O70172
|
PI42A_MOUSE
|
Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (EC 2.7.1.149) (1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha) (Diphosphoinositide kinase 2-alpha) (Phosphatidylinositol 5-Phosphate 4-Kinase) (PI5P4Kalpha) (Phosphatidylinositol 5-phosphate 4-kinase type II alpha) (PI(5)P 4-kinase type II alpha) (PIP4KII-alpha) (PtdIns(5)P-4-kinase isoform 2-alpha)
|
MATPGNLGSSVLASKTKTKKKHFVAQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVECHGVTLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECEENDGEEEGESDSTHPIGTPPDSPGNTLNSSPPLAPGEFDPNIDVYAIKCHENAPRKEVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGHIL
|
Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Has both ATP- and GTP-dependent kinase activities. May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2 (By similarity). May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation (By similarity). Required for lysosome-peroxisome membrane contacts and intracellular cholesterol transport through modulating peroxisomal PtdIns(4,5)P2 level (By similarity). In collaboration with PIP4K2B, has a role in mediating autophagy in times of nutrient stress. Required for autophagosome-lysosome fusion and the regulation of cellular lipid metabolism. Negatively regulates insulin signaling through a catalytic-independent mechanism. PIP4Ks interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (By similarity). May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size.
|
O70173
|
P3C2G_RAT
|
Phosphatidylinositol 3-kinase C2 domain-containing subunit gamma (PI3K-C2-gamma) (PtdIns-3-kinase C2 subunit gamma) (EC 2.7.1.137) (EC 2.7.1.154) (Phosphoinositide 3-kinase-C2-gamma)
|
MAYNWQTEPNRAEPQEGGHDHQQCHHADQHLSSRQVRLGFDQLVEELSNKTPLPEDEKEGTCFVPDTPNLDSKWQSIYGPHPRHFNEFTSQSPHFSQLPFGKASAIGFNPAVLPAHQFIHEGASWRNPTRKYHGGEDPRFSALTPSSTGLDKCHQQGQSGTEHCNYYVEPENNVPHHYSPYSMDSIPDSEEKGSGDADLVEPSLVFSKDSFLPRASENMSVESTEPIGCPLEIVEAPQGSNKSLASFCNNVTKIRGLYHASDTNSNSGKIWAITTAYPSRLFADTQFRVKISTDNSAQLLLLKPPANYLVKDLIAEILLLCANEQLSPKEYLLSICGSEEFLQTDHCLGSHKIFQKSKSVIQLHLQRSRDTPGKLSRKRDDDRSRVHLNQLLEFTHIWKISRQCLSTVMKSYNLHVEHLLKTQEDVEEKPLSSMFSCGRHPPQPHGNDIIEDVRNICSVLGCIETKQVSDAVKELTLILQRPSQNFHQNSETSKKGFIENVTSELSRSLHQLVDVYCSSFCTDFRPARAPGGVSRDHAGLHSHLSFTVCSLHNVPETWAHSYKAFSFSCWLTYAGKKLCQVKSCRSLPVTKSFSFSVNWNEIINFPLEIKSLPRESMLVIKLFGIDSATHSANLLAWTCLPLFPKEKSPLGSRLLSMTLQSEPPIEMMAPGVWDGSQPTPLTLQIDFPAATWEYVKPETEENRTDHQEPPRECLKHIARLSQKQPPLLLSVEKRRYLWFYRFYCNNENSSLPLVLGSAPGWDEGTVSEMHAVLRRWTFSHPLEALGLLTSRFPDQDIREVAVQQLDNFLTDELLDCLPQLVQAVKFEWSLESPLVELLLHRSLQSIRVAHRLFWLLRDAQGEDYFKSWYQELLAALQFCAGEALIEELSKEQKLVKLLGDIGEKVKSAGDAQRKDVLKKEIGSLEEFFKDIKTCHLPLNPALCVKGIDRDACSYFTSNALPLKITFINANPMGKNISVIFKAGDDLRQDMLVLQIIQVMDNVWLQEGLDMQMIIYGCLATGKAQGFIEMVPDAVTLAKIHLHSGLIGPLKENTIKKWFSQHNHLKEDYEKALRNFFYSCAGWCVVTFILGVCDRHNDNIMLTKSGHMFHIDFGKFLGHAQTFGGIKRDRAPFIFTSEMEYFITEGGKNTQHFQDFVELCCRAYNIVRKHSQLLLSLLEMMLHAGLPELRGIEDLKYVHDNLRPQDTDLEATSHFTTKIKQSLECFPVKLNNLIHTLAQMPAFSLARPAPQTPPQECCVLNKTRTIQRVTILGFSKTHSNLYLIEVTRSDNRKNLAKKSFEQFYRLHSQIQKQFPLLTLPEFPHWWHLPFTDSHHERIRDLSHYVEQVLHGSYEVANSDCVLSFFLSEHIQQTLEDSPFVDPGDHSPDKSPQVQLLMTYEDTKLTILVKHLKNIHLPDGSAPSAHVEIYLLPHPSEVRRKKTKCVPKCTDPTYNEIVVYDDVSGLQGHVLMLIVKSKTVFVGAVNIQLCSVPLNEEKWYPLGNSII
|
Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. May play a role in SDF1A-stimulated chemotaxis (By similarity).
|
O70174
|
ACHA4_MOUSE
|
Neuronal acetylcholine receptor subunit alpha-4
|
MEIGGSGAPPPLLLLPLLLLLGTGLLPASSHIETRAHAEERLLKRLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPGDYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFYDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVSMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFIIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKVTLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPRTHTMPAWVRRVFLDIVPRLLFMKRPSVVKDNCRRLIESMHKMANAPRFWPEPESEPGILGDICNQGLSPAPTFCNRMDTAVETQPTCRSPSHKVPDLKTSEVEKASPCPSPGSCHPPNSSGAPVLIKARSLSVQHVPSSQEAAEGSIRCRSRSIQYCVSQDGAASLTESKPTGSPASLKTRPSQLPVSDQTSPCKCTCKEPSPVSPITVLKAGGTKAPPQHLPLSPALTRAVEGVQYIADHLKAEDTDFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPWLAGMI
|
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodium ions.
|
O70176
|
PACA_MOUSE
|
Pituitary adenylate cyclase-activating polypeptide (PACAP) [Cleaved into: PACAP-related peptide (PRP-48); Pituitary adenylate cyclase-activating polypeptide 27 (PACAP-27) (PACAP27); Pituitary adenylate cyclase-activating polypeptide 38 (PACAP-38) (PACAP38)]
|
MTMCSGARLALLVYGIIMHSSVSCSPAAGLSFPGIRPEDEAYDQDGNPLQDFYDWDPPGVGSPASALRDAYALYYPADRRDVAHEILNEAYRKVLDQLSARKYLQSVVARGAGENLGGSAVDDPAPLTKRHSDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVKNKGRRIAYL
|
Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells (By similarity). Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway (By similarity). In chromaffin cells, induces long-lasting increase of intracellular calcium concentrations and neuroendocrine secretion (By similarity). Involved in the control of glucose homeostasis, induces insulin secretion by pancreatic beta cells.
|
O70191
|
ATF5_MOUSE
|
Cyclic AMP-dependent transcription factor ATF-5 (cAMP-dependent transcription factor ATF-5) (Activating transcription factor 5-alpha/beta) (BZIP protein ATF7) (NAP1) (NRIF3-associated protein) (Transcription factor ATFx) (Transcription factor-like protein ODA-10)
|
MSLLATLGLELDRALLPASGLGWLVDYGKLPLAPAPLGPYEVLGGALEGGLPGGGEPLAGDGFSDWMTERVDFTALLPLEAPLPPGTLPPPSPAPPDLEAMASLLKKELEQMEDFFLDAPLLPPPSPPPPPPPAAAPSLPLPLPLPTFDLPQPPTLDTLDLLAVYCRSEAGPGDSGLSTLPVPQQPPPLAPLPSPARPAPYPSPASTRGDRKQKKRDQNKSAALRYRQRKRAEGEALEGECQGLEARNRELRERAESVEREIQYVKDLLIEVYKARSQRTRST
|
Transcription factor that either stimulates or represses gene transcription through binding of different DNA regulatory elements such as cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), ATF5-specific response element (ARE) (consensus: 5'-C[CT]TCT[CT]CCTT[AT]-3') but also the amino acid response element (AARE), present in many viral and cellular promoters. Critically involved, often in a cell type-dependent manner, in cell survival, proliferation, and differentiation. Its transcriptional activity is enhanced by CCND3 and slightly inhibited by CDK4 (By similarity). Important regulator of the cerebral cortex formation, functions in cerebral cortical neuroprogenitor cells to maintain proliferation and to block differentiation into neurons. Must be down-regulated in order for such cells to exit the cycle and differentiate. Participates in the pathways by which SHH promotes cerebellar granule neuron progenitor cells proliferation. Critical for survival of mature olfactory sensory neurons (OSN), directs expression of OSN-specific genes. May be involved in osteogenic differentiation. Promotes cell proliferation and survival by inducing the expression of EGR1 sinergistically with ELK1. Once acetylated by EP300, binds to ARE sequences on target genes promoters, such as BCL2 and EGR1 (By similarity). Plays an anti-apoptotic role through the transcriptional regulation of BCL2, this function seems to be cell type-dependent (By similarity). Cooperates with NR1I3/CAR in the transcriptional activation of CYP2B6 in liver. In hepatic cells, represses CRE-dependent transcription and inhibits proliferation by blocking at G2/M phase. May act as a negative regulator of IL1B transduction pathway in liver. Upon IL1B stimulus, cooperates with NLK to activate the transactivation activity of C/EBP subfamily members. Besides its function of transcription factor, acts as a cofactor of CEBPB to activate CEBPA and promote adipocyte differentiation. Regulates centrosome dynamics in a cell-cycle- and centriole-age-dependent manner. Forms 9-foci symmetrical ring scaffold around the mother centriole to control centrosome function and the interaction between centrioles and pericentriolar material (By similarity).
|
O70194
|
EIF3D_MOUSE
|
Eukaryotic translation initiation factor 3 subunit D (eIF3d) (Eukaryotic translation initiation factor 3 subunit 7) (eIF-3-zeta) (eIF3 p66)
|
MAKFMTPVIQDNPSGWGPCAVPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDETSFQLVDTARTQKTAYQRNRMRFAQRNLRRDKDRRNMVQFNLQTLPKSAKQKERERIRLQKKFQKQFGVRQKWDQKSQKPRDSSVEVRSDWEVKEEMDFPQLMKMRYLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAMEATYINHNFSQQCLRMGRERYNFPNPNPFVEDDMDKNEIASVAYRYRRWKLGDDIDLIVRCEHDGVMTGANGEVSFINIKTLNEWDSRHCNGVDWRQKLDSQRGAVIATELKNNSYKLARWTCCALLAGSEYLKLGYVSRYHVKDSSRHVILGTQQFKPNEFASQINLSVENAWGILRCVIDICMKLEEGKYLILKDPNKQVIRVYSLPDGTFSSEEDEEDEEEEEEEEEEEET
|
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs. {ECO:0000255|HAMAP-Rule:MF_03003}.
|
O70196
|
PPCE_RAT
|
Prolyl endopeptidase (PE) (EC 3.4.21.26) (Post-proline cleaving enzyme) (rPop)
|
MLSFQYPDVYRDETSVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNTLSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFTCMAWTHDGKGMFYNSYPQQDGKSDGTETSTNLHQKLCYHVLGTDQSEDVLCAEFPDEPKWMGGAELSDDGRYVLLSIWEGCDPVNRLWYCDLQQGSNGINGILKWVKLIDNFEGEYDYITNEGTVFTFKTNRNSPNYRLINIDFTDPDESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLRNVKNILQLHDLTTGALLKTFPLDVGSVVGYSGRKKDSEIFYQFTSFLSPGVIYHCDLTREELEPRVFREVTVKGIDASDYQTIQVFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTTSKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKFTIGHAWTTDYGCSDSKQHFEWLLKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIVGRSRKQSNPLLIHVDTKAGHGPGKPTAKVIEEVSDMFAFIARCLNIEWIQ
|
Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has high activity on the succinyl- (suc-) peptide-4-methylcoumaryl-7-amide (MCA) substrates suc-Gly-Pro-Leu-Gly-Pro-MCA, suc-Gly-Pro-MCA and suc-Ala-Ala-Ala-MCA.
|
O70200
|
AIF1_MOUSE
|
Allograft inflammatory factor 1 (AIF-1) (Ionized calcium-binding adapter molecule 1)
|
MSQSRDLQGGKAFGLLKAQQEERLEGINKQFLDDPKYSNDEDLPSKLEAFKVKYMEFDLNGNGDIDIMSLKRMLEKLGVPKTHLELKRLIREVSSGSEETFSYSDFLRMMLGKRSAILRMILMYEEKNKEHKRPTGPPAKKAISELP
|
Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation.
|
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