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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Q9X8U2 | RS6_STRCO | Small ribosomal subunit protein bS6 (30S ribosomal protein S6) | MRHYEVMVILDPDLEERSVSPLIENFLSVVRDGGGKVEKVDTWGRRRLSYEIKKKPEGIYSVIDLQAEPAVVKELDRQMNLNESVLRTKVLRPEMH | Binds together with bS18 to 16S ribosomal RNA. |
Q9X8U5 | RL9_STRCO | Large ribosomal subunit protein bL9 (50S ribosomal protein L9) | MKIILTHEVSGLGAAGDVVDVKDGYARNYLIPRKFAIRWTKGGEKDVEQIRRARKIHEIQTIEQANQVKAQLEGVKVRLAVRSGDAGRLFGSVTPADVASAIKAAGGPEVDKRRIELGSPIKTLGAHETSVRLHPEVDAKVSIEVVAA | Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00503}. |
Q9X8Z8 | KDPC_STRCO | Potassium-transporting ATPase KdpC subunit (ATP phosphohydrolase [potassium-transporting] C chain) (Potassium-binding and translocating subunit C) (Potassium-translocating ATPase C chain) | MNTSLTNAARLFTAGLRALLVLTVVTGIVYPLVVTGVAQGLFPGKANGSEIKADGKVVGSSLIGQSYNLPLKEGRETPEPDLRWFQGRPANGLGTNTVNTRYELILSGATNRSADDPELLQWVQDAKAAVVRDNSVPGHPVRPEDVPADAVTSSGSGLDPDISPRYADLQVHRVAAKNGLPAERVQELVDEHTTPRTLGFIGEPRVNVLELNIALVELVAPGAGH | Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation... |
Q9X900 | KDPA_STRCO | Potassium-transporting ATPase potassium-binding subunit (ATP phosphohydrolase [potassium-transporting] A chain) (Potassium-binding and translocating subunit A) (Potassium-translocating ATPase A chain) | MSPVLAGVLQLLALTAALALAHVPLGNYLARVYSSPKHLRIEKWIYKSIGADPDTEMRWPAYLRGVLAFSLAGVLFLYLLQRLQGVLPGSLGFASIDPDQAFNTAASFVANTNWQSYYGEQAMGHVVQTAGLAVQNFVSAAVGIAVAVALVRGFARSRTGELGNFWADLVRGVVRVLVPIAAVGAVILVACGVIQNFSGIHEVGQFMGGTQEWNGGAVASQEVIKELGTNGGGYFNANSAHPFENPTPFTNLFEIFLILLIPVALTRTFGIMTGSVRQGYAILGTMAAIWAGFVALMMWTEFAHHGPALQAAGGAMEGKE... | Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunne... |
Q9X929 | NHAA3_STRCO | Na(+)/H(+) antiporter NhaA 3 (Sodium/proton antiporter NhaA 3) | MTAPRTPRKAFGRLSLPERTYLADALRTETVGGVLLLVAAIAALVWANIPALHDSYESVSHFHFGPAALGLNLSVAHWAADGLLAIFFFVAGIELKRELVAGDLKDPKAAALPVVAALCGMVVPAVVYTVTSTAGGGSLSGWAVPTATDIAFALAVLAVIGTSLPSALRAFLLTLAVVDDLFAILIIAVFFTETLNFAALGGAVVGLAVFWLLLRKGVRGWYVYVPLGLVIWALMYNSGVHATIAGVAMGLMLRCHRREGEDHSPGEHIEHLVRPLSAGLAVPLFALFSAGVAITGGALADVFTKPETLGVVLGLVVGKT... | Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. {ECO:0000255|HAMAP-Rule:MF_01844}. |
Q9X9F2 | FLHD_XENNE | Flagellar transcriptional regulator FlhD | MSTVELLKHIYDINLSYLLLAQRLINHEKASAMFRLGISESMADTLAELTLPQLVKLAETNQLICHFRFEDHETVQQLTKESRVDDLQQIHTGILLSTHLFQQLSAQDDTSIKKRA | Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 gene... |
Q9X9F3 | FLHC_XENNE | Flagellar transcriptional regulator FlhC | MVEKSIVQEAKDIQLAMELITLGARLQMLESETQLSRGRLIRLYKELRGSPPPKGMLPFSTDWFMTWEQNIHSSMFYNAYRFLLKSGHCEGVEVVVKAYRLYLEQCPPGNNGDAPILALTRAWTLVRFVDSGMLQPTECRCCGGTFITHAHQPVNSFVCSLCQPPSRAVKKRKLSPQPADTNSQLLDGFAQKAM | Functions in complex with FlhD as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 gene... |
Q9X9J4 | FLGI2_VIBPA | Flagellar P-ring protein 2 (Basal body P-ring protein 2) | MKRIVLLLMSVALFSTAAQAARIKDVAQVAGVRSNQLVGYGLVSGLPGTGEANPFTEQSFAAMLQNFGIQLPPGTKPKIKNVAAVMVTAELPPFSKPGQQVDVTVSSIGSAKSLRGGTLLQTFLKGLDGQVYAVAQGNLVVSGFSAEGADGSKIVGNNPTVGLISSGATVEREIPNPFGRGDYITFNLLESDFTTAQRMADAVNNFLGPQMASAVDATSVRVRAPRDVSQRVAFLSAIENLEFDPADGAAKIIVNSRTGTIVVGKHVRLKPAAVTHGGMTVAIKENLNVSQPNSFSGGQTVVVPDSDIEVTEEKGKMFKF... | Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. |
Q9X9K2 | CHER_VIBPA | Chemotaxis protein methyltransferase (EC 2.1.1.80) | MTAITISDQEYRDFSRFLESQCGIVLGDSKQYLVRSRLSPLVTKFKLASLSDLLRDVVAGRNRELRIAAVDAMTTNETLWFRDTYPFTVLADKLLPEVAANKRPIKIWSAASSSGQEPYSIAMTILETQQRKPGLLPSVSITATDISASMLEMCRAGVYDNLALGRGLSPERRRTFFEDAGDGRMKVKDNVKRLVNFRPQNLMDSYALMGKFDIIFCRNVLIYFSPEMKSKVLNQMASSLNPGGYLLLGASESLTGLTDKFEMVRCNPGIIYKLK | Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. |
Q9XA06 | ISPT2_STRCO | Isoprenyl transferase 2 (EC 2.5.1.-) | MRAKVRAALDALYMKRLVRELEGRPRPQHIGIMLDGNRRWAKMSGIDDPREGYRAGGAKVLDFLRWCDSAQIEHVTLFMLSDDNLARPEEQLNPLIDIIAEVVEQLAAPGNPWPVEAVGALDLLPAESASRLKTATAATQGRKGGTKVDVAVGYGGRREIVDAVRSALTEHSSQGGDIDEFIETFTMEHISKHLYSKTRSESDLIIRTSGEQRLSGFLLWQSAYAEVHFCETYWPDFREIDFLRALRSYSLRERRYGR | Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. {ECO:0000255|HAMAP-Rule:MF_01139}. |
Q9XAC0 | TAL2_STRCO | Transaldolase 2 (EC 2.2.1.2) | MTDALKRLSDEGVAIWLDDLSRKRITSGNLAELIDQQHVVGVTTNPSIFQKAISQGDGYDQQLADLAVRGVTVEEAIRMITTADVRDAADILRPVYDNTGGKDGRVSIEVDPRLAHNTHATVAEAKQLAWLVDRPNTFIKIPATEAGLPAIAETIGLGISVNVTLIFSLERYRKVMDAFLTGLEKAKERGLDLSQIHSVASFFVSRVDTEIDKRIDALGTDEAKAQRGKAAVANARLAYQAYEEVFGTDRWAALEKAGANKQRPLWASTGVKDKAYSDTMYVTDLVAPNTVNTMPEATLLATEDHGEITGDAVAGSYERA... | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00493}. |
Q9XAD5 | CSD_STRCO | Probable cysteine desulfurase (EC 2.8.1.7) | MTQLPGLLDTEAIRKDFPILDRQVHDGHKLVYLDNAATSQKPRQVLDALSEYYERYNANVHRGVHVLAEEATALYEGARDKVAEFINAPSRDEVIFTKNASESLNLVANMLGWADDPYRVDHETEIVITEMEHHSNIVPWQLLAQRTGAKLRWFGLTDDGRLDLSNIDEVITEKTKVVSFVLVSNILGTQNPVEAIVRRAQEVGALVCIDASQAAPHMPLDVQALQADFVAFTGHKMCGPTGIGVLWGRQELLEDLPPFLGGGEMIETVSMHSSTYAPAPHKFEAGTPPVAQAVGLGAAIDYLNSIGMDKILAHEHALTE... | Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. |
Q9XAI3 | Y3619_STRCO | Nucleoid-associated protein SCO3619 | MIPGGGQPNMQQLLQQAQKMQQDLAKAQEELARTEVDGQAGGGLVKATVTGSGELRGLVIDPKAVDPEDTETLADLVVAAVQAANENAQNLQQQKLGPLAQGMGGGGSGIPGLPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. {ECO:0000255|HAMAP-Rule:MF_00274}. |
Q9XAI4 | RECR_STRCO | Recombination protein RecR | MYEGVVQDLIDELGRLPGVGPKSAQRIAFHILQAEPVDVRRLAQALMEVKAKVRFCATCGNVAQEEQCNICRDTRRDPSVICVVEEPKDVVAIERTREFRGRYHVLGGAISPIDGVGPDDLRIRELLARLADGSVTELILATDPNLEGEATATYLARMIKPMGLKVTRLASGLPVGGDLEYADEVTLGRAFEGRRLLDV | May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. {ECO:0000255|HAMAP-Rule:MF_00017}. |
Q9XAQ6 | NUOC_STRCO | NADH-quinone oxidoreductase subunit C (EC 7.1.1.-) (NADH dehydrogenase I subunit C) (NDH-1 subunit C) | MSDANNTAGDANEVNPEKDLSAENLPGQRGQGGEEIRVQRGMFGANNGGDTSGYGGLVRSVRLPGPASRPYGGWFDEVADELEGALEEQGLLPDNAIEKTVVDRGELTFHIEREHLVRVARTLRDDPALRFELCTGVSGVHYPHDKGRELHAVYHLRSITHNRLIRLEVSAPDGDPHIPSLVSVYPTNDWHERETYDFFGIVFDDHPALTRIMMPDDWQGFPQRKDYPLGGIPVEYKGAQIPAPDQRRSYS | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions ar... |
Q9XAQ7 | NUOD2_STRCO | NADH-quinone oxidoreductase subunit D 2 (EC 7.1.1.-) (NADH dehydrogenase I subunit D 2) (NDH-1 subunit D 2) | MSTSHASPRETTEGTVYTVTGGDWDEVVQSAARADDERIVVNMGPQHPSTHGVLRLILEIDGETVTEARCGIGYLHTGIEKNLEYRTWTQGTTFVTRMDYLTPFFNEAAYCLGVEKLLGIDDQIPDRATIIRVLLMELNRLSSHLVAIATGGMELGATTIMIYGFRDRELILDIYELITGLRMNHAYIRPGGLAQDLPPGAVDQIREFVKKMNKNLPEYDKLATGNPIFKARMQDVGYLDLAGCMALGATGPVLRSTGLPHDLRKTQPYCGYETYDFDVPTADTCDSYGRFLIRLEEMRQSLRIVEQCLDRLQPGPVMVA... | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions ar... |
Q9XB14 | DHAA_MYCBO | Haloalkane dehalogenase (EC 3.8.1.5) | MTAFGVEPYGQPKYLEIAGKRMAYIDEGKGDAIVFQHGNPTSSYLWRNIMPHLEGLGRLVACDLIGMGASDKLSPSGPDRYSYGEQRDFLFALWDTLDLGDHVVLVLHDWGSALGFDWANQHRDRVQGIAFMEAIVTPMTWADWPPAVRGVFQGFRSPQGEPMALEHNIFVERVLPGAILRQLSDEEMNHYRRPFVNGGEDRRPTLSWPRNLPIDGEPAEVVALVNEYRSWLEETDMPKLFINAEPGAIITGRIRDYVRSWPNQTEITVPGVHFVQEDSPEEIGAAIAQFVRQLRSAAGV | Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. {ECO:0000255|HAMAP-Rule:MF_01231}. |
Q9XB20 | DBH_STRGN | DNA-binding protein HU | MANKQDLIAKVAAATELTKKDSAAAVDAVFAAVTEYLSKGEKVQLIGFGNFEVRERAARKGRNPQTGKETKIAASKVPAFKAGKALKDAVK | Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. Seems also to act as a fortuitous virulence factor in delayed sequelae by binding to heparan sulfate-proteoglycans in the extracellular matrix of target organs ... |
Q9XB21 | DBH_STRMU | DNA-binding protein HU | MANKQDLIAKVAEATELTKKDSAAAVDAVFSAVSSYLAKGEKVQLIGFGNFEVRERAARKGRNPQTGEEIKIKASKVPAFKAGKALKDAVK | Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. Seems also to act as a fortuitous virulence factor in delayed sequelae by binding to heparan sulfate-proteoglycans in the extracellular matrix of target organs ... |
Q9XB22 | DBH_STRDO | DNA-binding protein HU | MANKQDLIAKVAEATELTKKDSAAAVDTVFSSIEGFLSKGEKVQLIGFGNFEVRERAARKGRNPQTGAEIKIAASKVPAFKAGKALKDAVK | Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. Seems also to act as a fortuitous virulence factor in delayed sequelae by binding to heparan sulfate-proteoglycans in the extracellular matrix of target organs ... |
Q9XB52 | KDGT_PECCC | 2-keto-3-deoxygluconate permease (KDG permease) | MKIKQAIDKIPGGLMLVPLFLGALCNTFTPGAGKYLGSFSNGLITGTIPILAVWFFCMGASIEFKATGTMLRKSGVLVVTKIATAWVVALIAGTFLPGDGIQNGMLAGISVLALVAAMDMTNGGLYAALMNQYGSKEEAGAFVLMSLESGPLMTMVILGASGIATFEPQLFVGAVLPFLIGFALGNLDPDLRKLFGNSVQTLIPFFAFALGNTINLSVILQTGFAGIFLGLLVIVVTGIPLILADKFIGGGNGTAGVAASSSAGAAVATPLLIANMAPEFAPVAQQATALVATSVIVTSVLVPIITALWAKRFSPKHA | Catalyzes the proton-dependent uptake of 2-keto-3-deoxygluconate (KDG) into the cell. {ECO:0000255|HAMAP-Rule:MF_00070}. |
Q9XB53 | KDUI_PECCC | 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase (EC 5.3.1.17) (5-keto-4-deoxyuronate isomerase) (DKI isomerase) | MDVRQSVHSEHAKTLDTTELRKKFLIEQIFTPNQYTMTYSHIDRIVVGGIMPVDGEITFDDGIGKQFGVNYFLERRELGLINIGGPAKIVIDGTSYEVGNEEALYVGKGAKALAFSSLDSAKPAKLYYNSAPAHAVFPTRIITQDDAIKAPLGDVKTCNKRTICKYLVPEVVETCQLSMGLTRLAEGSNWNSMPTHTHERRMEVYFYFDMAEDTIIFHMMGEPHETRHLVMHNEQAVISPSWSIHTGVGTKNYAFIWGMIGENLTFDDMDHIAMLDLR | Catalyzes the isomerization of 5-dehydro-4-deoxy-D-glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate. {ECO:0000255|HAMAP-Rule:MF_00687}. |
Q9XBG0 | PHOU_BURSP | Phosphate-specific transport system accessory protein PhoU homolog (Pst system accessory protein PhoU homolog) | MIDKHLSSQFDADLESVCAQMLEMGRLVKMQVTDAMDALNHLDAQAAQRVMRNEQRINTLEIDIDQECSNIIVRRQPAARDLRLLMAISKIITDLERVGDEAEKIAVCTQRLTQAGAQPHLMDGSALKQAGAMAISMLHRALESFMHLDTAATAQIVRDDCVINEAFHAFVRTLITYMKEDTQMISTGLDYLSAAKAIERIGDHATNLAEFTIYIVKGTDVRHISPEQLAQEALC | Plays a role in the regulation of phosphate uptake. |
Q9XBG6 | TILS_BRADU | tRNA(Ile)-lysidine synthase (EC 6.3.4.19) (tRNA(Ile)-2-lysyl-cytidine synthase) (tRNA(Ile)-lysidine synthetase) | MSDDDNSPISAREAKQLFAELKSAPALVLAVSGGPDSIALMWLAARWQRSLARGPRLTVVTVDHGLRAEAAREAREVKRLATELGLPHRTLRWRGAKPKTGLPAAAREARYRLLMQAARSAGASHVLTAHTRDDQAETLLMRLVRGSGLAGLSAMARLTERDGIVLARPLLDVPKAQLIATLKRAKIGFADDPTNRDTAFTRPRLRALLPQLAAEGGDARSLARLAARLARANAAVEVLTDGAERFLRLRDRDDAPHGPDMRSFEAGAFATLPEEVRLRMLLRAINALGHEGPAELGKVETLLAALDQAIAAGMAAAPRA... | Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. {ECO:0000255|HAMAP-Rule:MF_01161}. |
Q9XBH4 | YDJC_BACC1 | Carbohydrate deacetylase (EC 3.5.1.-) | MIKLIVNADDFGLTEGTNYGIIDGHINGLVNSTTMMMNMPGTEHAVRLAKEHNTLGVGVHLVLTAGKPLLGDVPSLVSSDGLFHKQSVVWEGKINPEEVEREWTAQIEKFLSYGLTPTHLDSHHHVHGLPILHDVLEKLAATYNVPIRRCEEERAVRPFSDVFYSDFYADGVTEDYFVKLKERVQGEQTVEIMVHPAYIDPELVKRSSYVMDRVKELRILTESELPEGIELVKF | Probably catalyzes the deacetylation of acetylated carbohydrates an important step in the degradation of oligosaccharides. {ECO:0000255|HAMAP-Rule:MF_01246}. |
Q9XBL8 | RUBR_TRIV2 | Rubredoxin (Rd) | MSEQAVENTVLDRFECRSCGYVYEPEKGDSKHDIAPETPFAELPINWRCPVCTAKKAAFSNIGPAGTASGFRENLGYGLGVNKLTPAQKNILIFGALALGFLFFISLYGLQ | Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Could be involved in hydrogenase-linked redox processes (By similarity). |
Q9XBR7 | Y1337_ZYMMO | Putative quercetin 2,3-dioxygenase ZMO1337 (Putative quercetinase) (EC 1.13.11.24) (Pirin-like protein ZMO1337) | MIVKRPYKNLGFADHGWLQARHHFSFARYFDPDRINWGAVRVWNDDRIAPDTGFGMHPHKDMEIVTYIREGALTHEDSLGNKGRIEAGDVQVMSAGTGIVHSEYNREASDTRLFQIWIMPNQSGHKPSWGSRSFPKKDHAGRFVVLASGYPEDKEALPIHADAAVLGATLNKGDVINYPLEEQRYGYLVVSKGIIAIENCTLQEGDAAGLAEVETISIEAKEDSEIVMVVTGAKI | Putative quercetin 2,3-dioxygenase. |
Q9XBV2 | DSBA_YERPE | Thiol:disulfide interchange protein DsbA | MKNVWLALVGIVMAFSVTAAQFTDGKQYLTLDKPVTGEPQVLEFFSFYCPHCYQFEEVYQVPKAVKKALPEGTKMTRYHVEFLGPLGKQLTQAWAVAMALGVEEKITPLMFEGVQKTQTVQTPGDIRNVFIKAGISGEDYDAALNSFVVKSLVAQQQKAAEDLQLRGVPAMFVNGKYMIKNDGMDTSSMDNYVKQYADVVTFLLTQK | Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis (By similarity). |
Q9XC11 | FGD_MYCFO | F420-dependent glucose-6-phosphate dehydrogenase (FGD) (G6PD) (EC 1.1.98.2) | MAELKLGYKASAEQFAPRELVELAVLAEAAGMDSATVSDHFQPWRHEGGHAPFSLAWMTAVGERTQRLVLGTSVLTPTFRYNPAVIAQAFATMGCLYPGRVFLGVGTGEALNEIATGYIGQWPEFKERFARLRESVKLMRELWLGDRVDFDGEYYKLRGASIYDVPEGGIPVYIAAGGPVVAKYAGRAGDGFICTSGKGEELYKDKLIPAVREGAEAAGRNAEDIDRMIEIKISYDPDPELALENTRFWAPLSLTPEQKHSIDDPIEMEKAADALPIEQVAKRWIVASDPDEAVEKVGQYVTWGLNHLVFHAPGHDQRRF... | Catalyzes the coenzyme F420-dependent oxidation of glucose 6-phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. {ECO:0000255|HAMAP-Rule:MF_02123}. |
Q9XCB0 | CH10_RHOMR | Co-chaperonin GroES (10 kDa chaperonin) (Chaperonin-10) (Cpn10) | MAKVKIKPLSDRVVIKPEPPEEKTESGLYIPDTAKEKPQRGTVIAVGPGRVENGTKIEMSVKEGDKVLYGKYAGTEITIDGEEYLIMRETDILGIIEEEK | Together with the chaperonin GroEL, 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. GroES binds to the apical surface of ... |
Q9XCB1 | DNAK_RHOMR | Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70) | MGKIIGIDLGTTNSVVAVMEGGEPKVIINPEGSRVTPSVVAFTADGEPLVGAPAKRQAITNPKNTIFSIKRFMGRFYDEVTEEISMVPYKVVRGENNTVRVEVEVGGEKRLYTPQEISAMILQKLKQTAEEYLGVPVTEAVITVPAYFNDAQRKATKEAGEIAGLKVRRILNEPTAAALAYGLDKKDKELKIAVYDLGGGTYDISILELGDGVFEVKATNGDTHLGGDNFDQRLIDYIADEFQKQEGIDLRKDPMALQRLKEAAEKAKIELSSAMKTTVNLPFITATAEGPKHLVMEITRAKFEQLIEDLVARTIPPMEQ... | Acts as a chaperone. |
Q9XCM5 | EFTS_BARQU | Elongation factor Ts (EF-Ts) | MSITAAQVKELRELSGAGMMDCKAALADTNGDMEAAVDWLRKKGIAKADKKAGRTAAEGLIGIVSKDTSAVLVEINSETDFVARNDLFQDIVRNVATAALDTQGNVESVSASFYPGSEKTVEATIKDAISTIGENMTFRRSAKLSVKDGVVATYIHSKVAEGLGKLGVLVAVETTGNKEAAAVFGRQVAMHIAATNPLALTAEDVDSGAVEREKAIFSDQARQSGKPENIIEKMVEGRLRKFFEEVVLLSQAFVMNPDITVEAALKDAEKSIGAPARITGFIRFALGEGVEKKESNFAAEVAAAAKG | Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity). |
Q9XCV1 | MGSA_THETR | Methylglyoxal synthase (MGS) (EC 4.2.3.3) | MVNLNIALIAHDMKKSLMIDFAIAYKDILEKCNIYATGATGQLVEEATGIKVNKFLPGPMGGDQQIGAMIAEDKMDLVIFLRDPLTAQPHEPDILALLRVCDVHSIPLATNLATAEVLIKGLDAGLLEWRNAVK | Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. {ECO:0000255|HAMAP-Rule:MF_00549}. |
Q9XCW3 | VIOB_ECOLX | dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase (EC 2.3.1.209) | MAYLDEIQLKEMGFKSVGENVKISDKASFYGCDNISIGNNVRIDDFCVFSAGEGGIDIHDYIHIAVYSSIIGKGKVTISDYANISSRVSIYSSNEYYSGNYMSNPVVPSEYTNIHSGTVFIGKHVIIGCGSIVLPDVILHEGAAIGALSVVKEDCEAFTVNVGIPAKPISERSKKLLELESVFKPSAIGDNL | Catalyzes the conversion of dTDP-4-amino-4,6-dideoxy-D-glucose (dTDP-D-Qui4N) to dTDP-4-acetamido-4,6-dideoxy-D-glucose (dTDP-D-Qui4NAc). |
Q9XCX7 | RECO_PSEAE | DNA repair protein RecO (Recombination protein O) | MSFAAAQATYVLHSRPYKETSALVDFFTPLGRLRAVLRGARGKAGALARPFVPLEAEWRGRGELKTVARLESAGVPNLLNGQALFSGLYLNELLIRLLPAEDPQPEIFAHYAATLPLLAAGRPIEPLLRAFEWRLLEQLGYGFALDVDIDGRPIEPQALYQLLPEAGLEPVAQLQPGLFQGSELLSMADADWSAPGALAAAKRLMRQALAPHLGGRPLVSRELFMNRKESPRD | Involved in DNA repair and RecF pathway recombination. |
Q9XD10 | RS4_LEPIN | Small ribosomal subunit protein uS4 (30S ribosomal protein S4) | MARYRGPVVKIMRREGVDLFLKSSYTFNKDKFHRKGPPGMPTKRKGKVSEYGAQLREKQKLKRAYGLLEKQFRRYYEEASHAHGVTGEILLQLLERRLDNVVYRLGFAITRRQARNFIAHRHILVNGERVDIPSYRLNVGDKVEIREKFKTSSFIADNIKLSQSLQGIPSWLSADYTNFGGDVTALPERHHIDLPVKEQVIVELYSK | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01306}. With S5 and S12 plays an important role in translational accuracy. {ECO:0000255|HAMAP-Rule:MF_01306}. |
Q9XD11 | RS11_LEPIN | Small ribosomal subunit protein uS11 (30S ribosomal protein S11) | MADDKKSVKKEKKVKKKEKKIVPRGKVYITASFNNTIVTITDMAGNTISWSTSGAMGFRGSKKSTPYAAQIAAGNAAEKAMDSAGLQEVDVMVSGPGIGRESAIRSLVARGLNIKMIKDVTPLPHNGCRPRKRRRV | Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01310}. |
Q9XD12 | RS13_LEPIN | Small ribosomal subunit protein uS13 (30S ribosomal protein S13) | MARIAGIDLPREKRIVVGLTYIFGIGNSLSKLILKKAGIDESIRVKDLNESQEAAIRKTLEETAKVEGDLRSEIQLNIKRLMDIGCYRGLRHRRGLPVNGQRTRTNARTRKGGKKTVANKKKVTK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. {... |
Q9XD14 | IF1_LEPIN | Translation initiation factor IF-1 | MAKEEAITVDGTVLEPLPNAMFRVELENGHKVLAHISGKMRMHYIRILPGDKVTVELSPYDLSKGRITYRKK | One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-... |
Q9XD17 | RL15_LEPIN | Large ribosomal subunit protein uL15 (50S ribosomal protein L15) | MKKERLEQASAFGKDRVKKKKNTDTSSNLIPVPKGATKEKKRVGRGPGSKVGKTAGRGSKGQYARNTVRRGFEGGQMPIHRRLPKRGFTSKFHKEFYPVNLRDIEKSGLTGNIDAKIMVQSKILDKETTLFKILGTGEIKKAIHVIADGFSQSAKEKIEKAGGSIKLRAELKLATSETKK | Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01341}. |
Q9XD19 | RS5_LEPIN | Small ribosomal subunit protein uS5 (30S ribosomal protein S5) | MAYQDEESKEYSEKVVKIDRVAKVVKGGRRFSFNALSVVGDQRGKVGIGFGKANEVPDAIRKSIESAKKHLVKINFKGHTIPHEVIGKFKSARVILKPSTAGTGIIAGASVRSIVEKAGIQDVLTKSWGSSNPVNIVKATLDALEQLETPILAAKKRGISLNKLFGKD | With S4 and S12 plays an important role in translational accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}. Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. {ECO:0000255|HAMAP-Rule:MF_01307}. |
Q9XD20 | RL18_LEPIN | Large ribosomal subunit protein uL18 (50S ribosomal protein L18) | MIDRLKKSISKTKRAERSRFKLKKLGSRPRLVFIKSNQYLSCQIIDDIQGVTLAYATTSEKTFTGEGKSKKDKGAAKVLGKLIAERGSQKGVKQVMLDRSGMIFHGRIAAFAEGAREAGLEF | This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. {ECO:0000255|HAMAP-Rule:MF_01337}. |
Q9XD21 | RL6_LEPIN | Large ribosomal subunit protein uL6 (50S ribosomal protein L6) | MSRIGKAEIKLPDKVEVKQENANIKVKGPLGELFTPIFEGISVKTENGIVKLERSNEDQKVVALHGLTRALLMNCVKGVSQGWEKNLEITGVGYRAQKRGEDLVMSLGFSHEVVYKAPKGIKIDVQEQLKIKVSGIDKQLVGQVAADIRSKRPPEPYKGKGIKYAEEFIKKKAGKTGKK | This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}. |
Q9XD22 | RS8_LEPIN | Small ribosomal subunit protein uS8 (30S ribosomal protein S8) | MSMSDPIGDMLTRIRNAGRAKHETCLVPGSKIKKSILDLMKEEGFIKDYESVKVNETFEDYKVFLKYDHTKRPIIRELVRVSTPGRRVYIKSAEIRPYKNNIGTLIVSTSKGIMTGKNARKLKLGGEVILKMS | One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01302}. |
Q9XD23 | RS14Z_LEPIN | Small ribosomal subunit protein uS14 (30S ribosomal protein S14 type Z) | MAKTSITVRHQRKKKFEVREYNRCPICGRSRGYLRRFDMCRICFRKLASGAQIPGVVKSSW | Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. {ECO:0000255|HAMAP-Rule:MF_01364}. |
Q9XD24 | RL5_LEPIN | Large ribosomal subunit protein uL5 (50S ribosomal protein L5) | MAARLRTKYKKEIVPELNKKFKFSSIMQVPRLEKIVLNVGMGEAHTNPKALEAAVEELALITGQRPVKTKAKKSIAGFKIREGMSLGCMVTLRGDYMYEFLDRLVNVALPRVRDFKGVSEKGFDGRGNYNMSIKEQIIFPEIKVDKINTLYGINMTFVTNSKSNEEAYSLLAAFGMPYRNQK | This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits this bridge is implicated in subunit movement.... |
Q9XD25 | RL24_LEPIN | Large ribosomal subunit protein uL24 (50S ribosomal protein L24) | MAKLTYRGSEYTKFKKFRIKKNDEVICITGKHKGKRGKVLSIDKKRDRVIVEGLNKRKRFMRPTQENPQGGVIEVEAPIHISNVMFYDPKKKKKAGVRVGFETVKGKKVRVSRPDKKEL | One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. |
Q9XD26 | RL14_LEPIN | Large ribosomal subunit protein uL14 (50S ribosomal protein L14) | MIQQETLLQVADNSGIKKVMCIKVLGGSKKRYASVGDEIIVAVKDAQPAFGLKDSTGKKVHNKAVQRAVVVRTTKEIRRPDGSYIRFDDNACAIIDDKGNPKGTRIFGPVARELRDKKYAKIISLAPEVL | Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}. |
Q9XD27 | RS17_LEPIN | Small ribosomal subunit protein uS17 (30S ribosomal protein S17) | MTAGKQHINKSLLYEGRVVSNSMNKTVVILVETRKTHPKFKKIVRRSVRLKVHDEKNECVVGDKILAIETRPLSKEKRHRLYKIVEKAK | One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. {ECO:0000255|HAMAP-Rule:MF_01345}. |
Q9XD29 | RL16_LEPIN | Large ribosomal subunit protein uL16 (50S ribosomal protein L16) | MLSPKRVKFRKRQRGRLKGTDERGSSVSFGEFGLKAVTSGRLTARQIEAARITINRQVKRGGKLWIRIFPHTPITKKPAETRMGKGKGNPEFWIAEIRPGRILFEMSGIDEETAKKALSLASYKLPIHTEFVKRSAL | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. {ECO:0000255|HAMAP-Rule:MF_01342}. |
Q9XD30 | RS3_LEPIN | Small ribosomal subunit protein uS3 (30S ribosomal protein S3) | MGQKVNPIGLRIGITRGWDSIWFSQSDYKKNLHEDIKIRKFVQNRFNNAGVVKVVIERFPEKINVNLHTAKPGIVIGQKGANIEAVKKILKTMTDKPVNLNIIEVKKPETVAQCIAESIALQIEQRQPFRRVMKQELRRAMRGGVEGIKILISGRLNGADMARRENYKEGRIPLHTLRAKIDLGFKEAKTTFGQIGVKVWTYSGDFIQSKEESEEDKYAVKRRTS | Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. {ECO:0000255|HAMAP-Rule:MF_01309}. |
Q9XD31 | RL22_LEPIN | Large ribosomal subunit protein uL22 (50S ribosomal protein L22) | MEAKAVSRFVRMSPRKVRLVADEIRGYAVNEALDILKFTNKRAIEPLTKVILSASANASVLNNKVDFNQLFIKKIYVDEGPIMKRFRPRARGRAARIRKRLSHITVVLSD | This protein binds specifically to 23S rRNA its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). {ECO:0000255|HAM... |
Q9XD32 | RS19_LEPIN | Small ribosomal subunit protein uS19 (30S ribosomal protein S19) | MARSVKKGPFIDDHLMKKITKLNSENQKKPFKTWSRRSTIFPDMVGHTVMVHNGKQFTPVYINENMIGHKLGEFSPTRTFRGHVAGDKKAAKK | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. |
Q9XD33 | RL2_LEPIN | Large ribosomal subunit protein uL2 (50S ribosomal protein L2) | MGIKKFKPVTSASRYKSVLDFAEITETEPYKPLTLTLNYKAGRGDGGKIAVRHKGGRVKRKYRIIDFKRRKANIPAVVKSLEYDPNRSAFISLICYKDGEYSYILAPDGIKVGDTVQSGAGSEIKIGNAMPIGKIPPGTNVHNVELQIGKGGQIARTAGSFGTIAGRDGEYILLKLPSSEVRKVHENCYATIGICSNKDHNLVSIGKAGRSRWLGKRPSVRGVVMNPVDHPHGGGEGRTSGGRHPVSPWGQPTKGYKTRRSTRPSDKFIIQKRKRNRNR | One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. {... |
Q9XD34 | RL23_LEPIN | Large ribosomal subunit protein uL23 (50S ribosomal protein L23) | MNLQDVILTPIVTEKSQDLETIGANSKKGTRMVKYTVKVHIDANKTLIKEAFKKIFKVTPSSVNVQVYRGKIKRFRNMPAARPHWKKAIVTFRDGASIDFAKEA | One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}. |
Q9XD35 | RL4_LEPIN | Large ribosomal subunit protein uL4 (50S ribosomal protein L4) | MKAQKYSKEGKLISEIELPSALFESKLSVASIYEAIKAENANLRSGNHATKTRSMVSGGGKKPWSQKGTGRARQGSTRAPHWVGGGTVHGPQKRDYSYKVSSKLKHRAVLSILGKKAQASAVKVVEDLDPKEYNTKAFDSIFKNMNLKNTGVIGLLVQGENDFLKKSVRNIPTVKYINSKRISCRDILYNRNLVITEAALKEMLVQYGAQK | One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}. Forms part of t... |
Q9XD36 | RL3_LEPIN | Large ribosomal subunit protein uL3 (50S ribosomal protein L3) | MAKGLIGKKVGMSQIFDEQGNIIPVTVLEVGPCAVSQVKSVENDGYEAIQLAFQDIKEIQTSKAEKNHLAKAGLGPKKVLKEFRSFGDSPTAGSVLKIQDVFAVSDVVKVTGVSKGRGYQGVVKRHGHAGGPGAHGSRFHRHPGSMGANSTPSRVFKGVKLPGRTGSQKTTVRNLKVVRINEEKNLLFVSGAVPGTANTVITIEKI | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01325}. |
Q9XD37 | RS10_LEPIN | Small ribosomal subunit protein uS10 (30S ribosomal protein S10) | MAGQKIRVKLKAFDHRLIDQSTYEIVATAKRTGATVSGPIPLPTKKEIYTVLRSPHVNKKSREQFELKTHKRLIDILDTNEDTVEALMKLQLPAGVSVDIKS | Involved in the binding of tRNA to the ribosomes. {ECO:0000255|HAMAP-Rule:MF_00508}. |
Q9XD38 | EFTU_LEPIN | Elongation factor Tu (EF-Tu) | MAKEKFDRSKPHLNVGTIGHVDHGKTTLTAAITTTLAKAIGGKNKAVAYDQIDNAPEEKARGITIATSHQEYETANRHYAHVDCPGHADYVKNMITGAAQMDAAILVVSATDGPMPQTKEHILLARQVGVPYVIVFINKADMLAADERAEMIEMVEMDVRELLNKYSFPGDTTPIVHGSAVKALEGDESEIGMPAILKLMEALDTFVPNPKRVIDKPFLMPVEDVFSITGRGTVATGRVEQGVLKVNDEVEIIGIRPTTKTVVTGIEMFRKLLDQAEAGDNIGALLRGTKKEEIERGQVLAKPGSITPHKKFAAEVYVLT... | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00118}. |
Q9XD50 | YCIB_VITS1 | Inner membrane-spanning protein YciB | MNAKTLDAIKPFLDWIPLIVFFYIYKTTEGEGSEHIIAATTGLLIATLIVYGLMFVLQKFTLEKRQWLVVVLTVVFGGLTMAFQDDFYIRLKAPIINAVFAFGLAMSPLFLGGTPGIQKMLGPIFEMTPKQWMKLNWVWVGFFTLMAVLQALFAFVWVEYWAMFTAFGDMIVMVVFMVAQFWFLRGFMRKDIK | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. {ECO:0000255|HAMAP-Rule:MF_00189}. |
Q9XD64 | NRDI_CORGL | Protein NrdI | MLIVYFSSATDNTHRFVQKLDLPNVRIPLTRVEEPLKINEPYVLITPTYGGGVSMTGENSRPVPPQVIRFLNDEHNRSFIRAVVAGGNSNFGSDFGLAGEIISKKCKVPYVYRFELMGNEEDVSILRGGLTQNAQALGLEPQEPVTSR | Probably involved in ribonucleotide reductase function. |
Q9XD73 | NRDJ_STRCT | Vitamin B12-dependent ribonucleotide reductase (EC 1.17.4.1) (Ribonucleoside-diphosphate reductase NrdJ) | MHLDNSSCNLASLNLMKFLRDDTASDGASGAGGNMSLDAERFAKVVELVITAMDISICFADFPTEKIGETTRAFRQLGIGYANLGALLMATGHAYDSDGGRALAGAITSLMTGTSYRRSAELAAVVGPYEGYARNADAHKRVMRQHADANTAAQRMDDLDTPVWAAATEAWQDVLRLGEQNRFRNAQASVLAPTGTIGLMMDCDTTGVEPDLALVKFKKLVGGGSMQIVNNTVPKALKRLGYQPEQVEAVVAHIAEHGNVIDAPGLKPEHYEVFDCAMGERAISPMGHVRMMAAAQPFLSGAISKTVNMPESATVEEIEE... | Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen (By similarity). |
Q9XDA6 | ZURA_LISMO | Zinc uptake system ATP-binding protein ZurA | MKKIIEVNNVSYHYDKEHALENIHFQVAKGSFTGLIGPNGSGKSTMLKLILGVLKKQQGSISLFGEKQADFKDWVKIGFVSQKSNAFNSAFPATVKEVVASGLTKKKGLFKTLNNKDKEDIDYALKRVEMTDYLHRNIGELSGGQQQRVFIARALVSRPELLILDEPTVGVDVENVKAFYELLAELNRTEEMTLLLVTHDLMAVNTYVNHVISINKRIIFDGSAHEYQHYLADRELEILAEQRRREDACLDCDASPV | Involved in a zinc uptake transport system. |
Q9XDE8 | CHER_LISMO | Chemotaxis protein methyltransferase (EC 2.1.1.80) | MIPDLEKDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKKYITFGEFFKHLKKDAVLLDEFISLITINVSSFFRNRNRWDALEKQVLPRLLEDSRGKLRVWSAACSSGEEPYSLAMMMERSVGTRHYDILATDLEPAILKRAVIGEYQSRQMEELSEQERHTAFVEKGDTYQILPKYRKSIRFRRHDLLTDYYEKGFDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGGVLFIGGSEQILNPADYGLATLNNFFYIKT | Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. |
Q9XDH5 | DPO3A_THEAQ | DNA polymerase III subunit alpha (EC 2.7.7.7) | MGSKLKFAHLHQHTQFSLLDGAAKLQDLLKWVKETTPEDPALAMTDHGNLFGAVEFYKKATAMGVKPIIGYEAYVAAESRFDRKRGKGLDGGYFHLTLLAKDFTGYQNLVRLASRAYLEGFYEKPRIDREILREHAQGLIALSGCLGAEIPQFILQDRLDLAEARLNEDLSIFGDRFFIEIQNHGLPEQKKVNQVLKEFARKYGLGMVATNDGHYVRKEDARAHEVLLAIQSKTTLDDPERWRFPCDEFYVKTPEEMRAMLPEAEWGDEPFDNTVEIARMCDVDLPIGDKMVYRIPRFPLPEGRTEAQYLRELTFLGLLR... | DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity). |
Q9XDH6 | DPO3A_PSEFL | DNA polymerase III subunit alpha (EC 2.7.7.7) | MPASFVHLRLHTEYSLVDGLVRIKPLVKALTGMGMPAVAVTDQNNMCSLVKFYKNAMGAGIKPICGADLWLSNKDPDGPLSRISLLVMNAQGYRNLTELISRGFIDGQRNGMVIIEREWVAEANEGLIMLSAAKEGEIGMAMIGGNPAEAEALAREWMAVFPDRFYLEIQRTNRPNDEEQLHGAVALADKLGAPLVATNDVRFIKQEDFAAHETRVCIGEGRALDDPRRSKNYSDQQYLKSAEEMAELFSDLPDAIENTVEIAKRCNIDVKLGKHFLPDYPIPDGMTIDEYFRKVSFDGLEERLSVLLPKDTTEDYEAKR... | DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity). |
Q9XDM0 | RL10_AQUPY | Large ribosomal subunit protein uL10 (50S ribosomal protein L10) | MAEFNREAYSERERSAASMKTLLRKQELVNSYKERLQRSNGFVVFFNFQGIDAYPLTLLRLDIKDLKGEIVVGKNTLFYRAFSDTALSDHRDIFIGPTAALFAYEDPVAVTKKLVEFLKETFDKEWEGRIKGGLLDYKYISPEQVKELAELPSKEELIAKLLGVMMAPVTQLAMTLKAVPQKLVLVLKAIEEEKSKGGQ | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. |
Q9XDM1 | RL1_AQUPY | Large ribosomal subunit protein uL1 (50S ribosomal protein L1) | ILGPRGLMPSPKTGTVTKNVEQAIKDAKRGRVEFKVDKAGNIHMPVGKVSFDKAKLLDNIYAAIDAVVRAKPPGAKGQYVKNIALSLTMSPSVKIDINETLRKLQERAA | Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. |
Q9XDP0 | DSBI_LELAM | Protein-disulfide oxidoreductase DsbI | MVDIKGMWKDLRATPVETLVRWQEQRFLWLLMAVAMGGLIILAHSFFQIYLYMAPCEQCVYIRFAMFVMVFGGLIAAINPKNIILKLIGCLAAFYGSIMGIKFSVKLNGIHYAVHNPDPDALFGVQGCSTDPTFPFGLPLAEWAPEWFRPTGDCGYDAPVVLTRNAQFCPAVVCGNVSALRRLVSDPALAFYEYGAGVPAGVWAMFCTVADYERRLGNQAD | Required for disulfide bond formation in some proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT. {ECO:0000255|HAMAP-Rule:MF_01311}. |
Q9XDP1 | DSBL_LELAM | Thiol:disulfide interchange protein DsbL | MSAKWINSIFKSVVLTAALALPFTASAFTEGTDYMVLEKPIPDADKTLIKVFSYACPFCYKYDKAVTGPVADKVADLVTFVPFHLETKGEYGKQASELFAVTMAKDKAAGVSLFDEKSQFKKAKFAWYAAYHDKKERWSDGKDPAAFLKTGLDAAGMSQAEFEAALKEPAVQQTLQKWKAAYEVAKIQGVPAYVVNGKYLIYTKNIKSIDSMAQLVRELATK | Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT. {ECO:0000255|HAMAP-Rule:MF_00932}. |
Q9XE11 | KDPA_ALIAD | Potassium-transporting ATPase potassium-binding subunit (ATP phosphohydrolase [potassium-transporting] A chain) (Potassium-binding and translocating subunit A) (Potassium-translocating ATPase A chain) | MTLSGILAIFLVVLALVACAWPLGGYIYRTFVGERVRPDAVMVPVERAIYRLIGVNPEVEMDWKAYLRAMMVSNLVMALFAYAVFRLQGVLPLNPAHIPAMPPYLAFNTAASFITNTNWQNYAGEQSLSYLSQMIGITFLQFTSAATGLAAAMAFLRGLSRQKTDALGNFWVDLVKAHTRLLLPIAAILAVLLLALGVPETLSGPAVVHTLAGSMQTIARGPVATLEAIKQLGTNGGGFFNANSAHPFENPNAWTCILEIMGMGLIPTALVFTAGHFLRSRRLAIVLCTLLGAILLAGAYIVYAYEAAGNPILAHALGIH... | Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunne... |
Q9XEK9 | IF2C_EUGGR | Translation initiation factor IF-2, chloroplastic | FQSSGSPIKPRINLDRPSTSTPTPPEAPTSPSARQPVTQVPQANSVPAGAVASQAEVKKPADPQPPATPSAPVLRRPVRTAMPASPPRMVINLDDIPDRSKPVWPAPPPRAKGQGGGKGGKGGKGGKGGKGGKGDREQPAVVRRAKPRRTASTAEGPAAESKESGGREAQIWVTPKGGKGRDKWKKGKEEVDKSEALLLKARKKTRLERKERREEVREANAAKKEEIIEVGPQGMTVSEIAGKLAITPANVVTVLFKKGIMSAPSQTIAYDLVKIVCDEYKVEVLEVEEEDGIASMEDRFVLDEEAEALVSRPPVVTIMG... | One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity). |
Q9XER8 | RAB7_GOSHI | Ras-related protein Rab7 | MASRRRMLLKVIILGDSGVGKTSLMNQYVNRKFSNQYKATIGADFLTKEVQFDDRLFTLQIWDTAGQERFQSLGVAFYRGADCCVLVHDVNVMKSFDNLNNWREEFLIQASPSDPENFPFVVLGNKVDVDGGNSRVVSEKKAKAWCASKGNIPYFETSAKEGFNVDAAFECIARNALKNEPEEEIYLPETIDVASGGRPQRSTGCEC | Protein transport. Probably involved in vesicular traffic (By similarity). |
Q9XF37 | PROF_APIGR | Profilin (Minor pollen allergen Api g 4) (allergen Api g 4) | MSWQAYVDDHLMCEVEGNPGQTLTAAAIIGHDGSVWAQSSTFPQIKPEEIAGIMKDFDEPGHLAPTGLYLGGAKYMVIQGEPNAVIRGKKGSGGVTIKKTGQALVFGVYDEPVTPGQCNVIVERLGDYLIDQGL | Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity). |
Q9XF38 | PROF_PYRCO | Profilin (Allergen Pyr c 3) (allergen Pyr c 4) | MSWQAYVDDHLMCDIDGHHLTAAAILGHDGSVWAQSSTFPKFKPEEITAIMKDFDEPGSLAPTGLHLGGTKYMVIQGEGGAVIRGKKGSGGVTVKKTSQALVFGIYEEPLTPGQCNMIVERLGDYLIDQGL | Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity). |
Q9XF39 | PROF_PRUAV | Profilin (Allergen Pru a 3) (allergen Pru av 4) | MSWQAYVDDHLMCDIDGNRLTAAAILGQDGSVWSQSATFPAFKPEEIAAILKDLDQPGTLAPTGLFLGGTKYMVIQGEAGAVIRGKKGSGGITVKKTNQALIIGIYDEPLTPGQCNMIVERLGDYLIEQGL | Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity). |
Q9XFH3 | MAD2_MAIZE | Mitotic spindle checkpoint protein MAD2 | MASRSASKDIITLRGSAAIVSEFFGYAANSILYNRAVYPEESFSKVKKYGLTMLLTQDEGVKNFIASLTSQLSEWLEAGKLQRIVLVIMSKATSEVLERWNFNIVTDAEVVEKGAIKEKSDKEIMREIQAIMRQIASCITYLPCLDEPCVFDVLAYTDTDVDAPGTWVESDAKLIDNPQMVKLHSFDTKIHKVDTLVSYKKDEWDEEE | Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and delays the onset of anaphase when this process is not complete. It inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate ... |
Q9XG77 | PSA6_TOBAC | Proteasome subunit alpha type-6 (20S proteasome alpha subunit A) (20S proteasome subunit alpha-1) | MSRGSGGGYDRHITIFSPEGRLFQVEYAFKAVKAAGITSIGVRGKDSVCVVTQKKVPDKLLDQTSVSHLFPITKYLGLLATGMTADARTLVQQARNEAAEFRFKYGYEMPVDVLSKWIADKSQVYTQHAYMRPLGVVAMILGIDEEKGPQLFKCDPAGHFFGHKATSAGSKEQEAINFLEKKMKNDPAFSYEETVQTAISALQSVLQEDFKASEIEVGVVKKEDPIFRVLTTEEIDEHLTAISERD | The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity). |
Q9XGC9 | MSH2_MAIZE | DNA mismatch repair protein MSH2 (MUS1) | MEGDDFTPEGGKLPEFKLDARQAQGFISFFKKLPQDPRAVRLFDRRDYYTAHGENATFIARTYYHTMSALRQLGSSSDGILSASVSKAMFETIARNILLERTDCTLELYEGSGSNWRLTKSGTPGNIGSFEDILFANNDMEDSPVIVALFPACRESQLYVGLSFLDMTNRKLGLAEFPEDSRFTNVESALVALGCKECLLPADCEKSIDLNPLQDVISNCNVLLTEKKKADFKSRDLAQDLGRIIRGSVEPVRDLLSQFDYALGPLGALLSYAELLADDTNYGNYTIEKYNLNCYMRLDSAAVRALNIAEGKTDVNKNFS... | Involved in postreplication mismatch repair. Binds specifically to DNA containing mismatched nucleotides thus providing a target for the excision repair processes characteristic of postreplication mismatch repair (By similarity). |
Q9XGJ4 | GGM13_GNEGN | MADS-box protein GGM13 | MGRGKIEIKRIENTTNRQVTFSKRRGGLLKKAHELSVLCDAELGLIIFSSSGKLFEYSSASSSMKKIIERYQKVSGARITEYDNQHLYCEMTRMKNENEKLQTNIRRMMGEDLTSLTMTELHHLGQQLESASSRVRSRKNQLMLQQLENLRRKERILEDQNSHLCRLLAEQQAAVEGVQEPLLEFGVFCPPPDNKTAAAANAGPLHLGHHLPAFRLQPTQPNLQESSIVPNRPVLQL | Probable transcription factor. |
Q9XGX4 | RBS3_AMAHP | Ribulose bisphosphate carboxylase small subunit, chloroplastic 3 (RuBisCO small subunit 3) | MASSLMSNAITAVVGASGAQANMVAPFNGLKSIASFPVTRKSNDITSIASNGGRVQCMQVWPPVGKKKFETLSYLPPLSDAQLLAQVQYLLNNGWIPCIEFELEHPFVYRENHRSPGYQDGRYWTMWKLPMYGCTDPAQVLNEVEEAKKAYPSAFIRIIGFDNKRQVQCVSFIAFKPPGY | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it... |
Q9XGX5 | RBS2_AMAHP | Ribulose bisphosphate carboxylase small subunit, chloroplastic 2 (RuBisCO small subunit 2) | MASSMMSNAATAVAVAATSGGAQANMVAPFNGLKSIASFPVTRKSNDITSIASNGGRVQCMQVWPPVGKKKFETLSYLPPLSDAQLLAQVQYLLNKGWIPCIEFELEHPFVYRENHRSPGYQDGRYWTMWKLPMYGCTDPAQVLNEVEEAKKAYPTAFIRIIGFDNKRQVQCVSFIAYKPADSY | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it... |
Q9XGX7 | TIM9_ORYSJ | Mitochondrial import inner membrane translocase subunit Tim9 | MDKSMLGDLDGLPEEDKMRMAAMVDQLQIRDSLRMYNSLVERCFTDCVDTFRRKTLDKQEESCVRRCAEKFLKHSMRVGMRFAELNQGVATPD | Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. ... |
Q9XGX8 | TIM9_MESCR | Mitochondrial import inner membrane translocase subunit Tim9 | MDKNMLGDLDNLPEEDKLKMASMIEQLQIRDSLRMYNNLVERCFTDCVDSFRRKTLDKQEETCVKRCAEKFLKHSMRVGLRFAELNQGAATTD | Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. ... |
Q9XGY5 | TIM13_ORYSJ | Mitochondrial import inner membrane translocase subunit Tim13 | MDSFSSSSGSPPNTEALMDQIKAQLAQAYAQEFLETVGNKCFAKCVTKPGSSLSGSESSCISRCVDRYIEATGIVSRALFSSTR | Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Ac... |
Q9XGY7 | FAR_SIMCH | Alcohol-forming fatty acyl-CoA reductase (EC 1.2.1.84) | MEEMGSILEFLDNKAILVTGATGSLAKIFVEKVLRSQPNVKKLYLLLRATDDETAALRLQNEVFGKELFKVLKQNLGANFYSFVSEKVTVVPGDITGEDLCLKDVNLKEEMWREIDVVVNLAATINFIERYDVSLLINTYGAKYVLDFAKKCNKLKIFVHVSTAYVSGEKNGLILEKPYYMGESLNGRLGLDINVEKKLVEAKINELQAAGATEKSIKSTMKDMGIERARHWGWPNVYVFTKALGEMLLMQYKGDIPLTIIRPTIITSTFKEPFPGWVEGVRTIDNVPVYYGKGRLRCMLCGPSTIIDLIPADMVVNATI... | NADPH-dependent alcohol-forming fatty acyl-coenzyme A reductase that catalyzes the reduction of fatty acyl-CoA to fatty alcohols. The recombinant enzyme accepts saturated and mono-unsaturated fatty acyl-CoAs of 16 to 22 carbons. |
Q9XH06 | LOG9_ARATH | Putative cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG9 (EC 3.2.2.n1) (Protein LONELY GUY 9) | MHIEHISGETVGEVRIVSDMHERKATMAQEAGAFIALLGERYETMEELLEMITWAQLGIHKKTVGLLNVDGYYNNLLAFFDTGVEEGFIKQGACNIVVSAPSARELMEKMELYTPSHKYIASHQSWKVEPLGDYPLLNENKPQ | Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms (By similarity). |
Q9XH42 | CET4_TOBAC | CEN-like protein 4 | MGSKMSDPLVIGRVIGEVVDYFTPSVKMSVTYNSSKHVYNGHELFPSSVTSKPRVEVHGGDLRSFFTLIMIDPDVPGPSDPYLREHLHWIVTDIPGTTDCSFGREIVGYEMPRPNIGIHRFVFLLFKQKKRQTLLSAPLSRDRFNTRKFSEENELGSPVAAAFFNCQRETAARRR | May form complexes with phosphorylated ligands by interfering with kinases and their effectors. |
Q9XH43 | CET2_TOBAC | CEN-like protein 2 | MGSKMSDPLVIGRVIGEVVDYFTPSVKMSVTYNSSKHVYNGHELFPSSVTSKPRVEVHGGDLRSFFTMIMIDPDVPGPSDPYLREHLHWIVTDIPGTTDCSFGKEIVGYEMPRPNIGIHRFVFLLFKQKKRQTVLTAPLSRDRFNTRKFAEENELGSPVAAVFFNCQRETAARRR | May form complexes with phosphorylated ligands by interfering with kinases and their effectors. |
Q9XH44 | CET1_TOBAC | CEN-like protein 1 | MASRVVEPLVVARVIGEVVDSFNPSVKLNVIYNGSKQVFNGHELMPAVIAAKPRVEIGGEDMRSAYTLIMTDPDVPGPSDPYLREHLHWIVTDIPGSTDSSFGREIVSYESPKPVIGIHRYVLLLYKQSGRQTVKPAATRDHFNTRRYTAENGLGSPVAAVYFNAQRETAARRR | May form complexes with phosphorylated ligands by interfering with kinases and their effectors. |
Q9XHL7 | TCTP_TOBAC | Translationally-controlled tumor protein homolog (TCTP) | MLVYQDLLSGDELPSDSFSYTELGNGVLWEVQGKWVVQGAVDVNIGANPSAEGADEDEGVDDQAIKVVDIVDTFRLQEQPSFDKKQFVAYMKKYIKNLTPKLGAEQEEVFKNNIQGATKYLLSKLSDLQFFVGESMADDTGMVFAYYKDGATDPTFLYLAHGLKEVKC | Involved in calcium binding and microtubule stabilization. |
Q9XI17 | PUM20_ARATH | Putative pumilio homolog 20 (APUM-20) (AtPUM20) | MAHQLRFAAAREPISEEYPAVALPHPRCISVAFPPPRFTPSPSPLTNYSFLAALTPQELEMRLQIAMDVQMISKLDQRKLQTMASLLTSDPDYFLMIARNMNGSKRIQKLLGKTDDVDALFAAAILRRFLHIITDKYASYVVRRGMTVFDKKKKKAMYEHILHYASHIARDKHGNLALNDIITDAYRNKLFDVIAHKALVLSNDAYGNFVIQRVLKLNDLRSKNNIVVSLRGHFVDLSFQKYGSYVVDVLLETKESMVVVVEELMECEGDMLMRLARNEYGNFLVCKALRVTQKEMVRTDLFWGLVHKLKPFHNLLRWSR... | Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs. |
Q9XI74 | PUMP3_ARATH | Mitochondrial uncoupling protein 3 (AtPUMP3) | MERSRVTREAPTGTRILLASLSAMVAESVTFPIDLTKTRMQLHGSGSASGAHRIGAFGVVSEIARKEGVIGLYKGLSPAIIRHLFYTPIRIIGYENLKGLIVRSETNNSESLPLATKALVGGFSGVIAQVVASPADLVKVRMQADGRLVSQGLKPRYSGPIEAFTKILQSEGVKGLWKGVLPNIQRAFLVNMGELACYDHAKHFVIDKKIAEDNIFAHTLASIMSGLASTSLSCPADVVKTRMMNQGENAVYRNSYDCLVKTVKFEGIRALWKGFFPTWARLGPWQFVFWVSYEKFRLLAGISSF | PUMPS are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. This leads to a decrease in the efficiency of oxidative phosphorylation and an increase in heat production. May be involved in protecting plant cells against oxidativ... |
Q9XIA4 | CCS1_ARATH | Cytochrome c biogenesis protein CCS1, chloroplastic (C-type cytochrome synthesis protein 1) | MIVTLNPKILHFSKIHPFSRPSSYLCRTRNVSLITNCKLQKPQDGNQRSSSNRNLTKTISLSDSAPPVTEETGDGIVKGGGNGGGGGGDGRGGLGFLKILPRKVLSVLSNLPLAITEMFTIAALMALGTVIEQGETPDFYFQKYPEDNPVLGFFTWRWISTLGLDHMYSAPIFLGMLVLLAASLMACTYTTQIPLVKVARRWSFMKSDEAIKKQEFADTLPRASIQDLGMILMGDGFEVFMKGPSLYAFKGLAGRFAPIGVHIAMLLIMVGGTLSATGSFRGSVTVPQGLNFVMGDVLAPIGFFSIPTDAFNTEVHVNRF... | Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. |
Q9XIE0 | FH7_ARATH | Formin-like protein 7 (AtFH7) (AtFORMIN-7) | MSFLFRKNGSSSRRKIKEKLRGRHSDRGGKREEDERYGGSGSDLPPPPSPWGFLFPEDFVRIDGNLKAVIVDDEGLDVIYWKKLLELENSGKIRKNPKPRRRGDKSGDGFRRTGADQDDNDDGDDEVGDESIEEAFSFHVKKSQSASSSGGEIRDQSNNGGGGGGGGGGGGRYYTSSSASPSRPSSSSASAASPSRTSYATSAGSDYGGGGGGKQSQSKFQAPGGGSFPSSPSQIHSGGGRSPPLPLPPGQFTAGNASFPSSTQPPPGQYMAGNASFPSSTPPPPGQYMAGNAPFSSSTPLPPGQYPAVNAQLSTSAPSV... | Might be involved in the organization and polarity of the actin cytoskeleton. |
Q9XIH6 | PLT2_ARATH | Putative polyol transporter 2 | MSSSGEERGVVVAESEPPRGNRSRFAFACAILASMTSIILGYDIGVMSGAAIFIKDDLKLSDVQLEILMGILNIYSLIGSGAAGRTSDWIGRRYTIVLAGFFFFCGALLMGFATNYPFIMVGRFVAGIGVGYAMMIAPVYTTEVAPASSRGFLSSFPEIFINIGILLGYVSNYFFAKLPEHIGWRFMLGIGAVPSVFLAIGVLAMPESPRWLVMQGRLGDAFKVLDKTSNTKEEAISRLNDIKRAVGIPDDMTDDVIVVPNKKSAGKGVWKDLLVRPTPSVRHILIACLGIHFSQQASGIDAVVLYSPTIFSRAGLKSKN... | Plasma membrane sugar-proton symporter. |
Q9XIH7 | PLT1_ARATH | Putative polyol transporter 1 | MNSSGVEQGVVIAESEPPRGNRSRYAFACAILASMTSIILGYDIGVMSGASIFIKDDLKLSDVQLEILMGILNIYSLVGSGAAGRTSDWLGRRYTIVLAGAFFFCGALLMGFATNYPFIMVGRFVAGIGVGYAMMIAPVYTAEVAPASSRGFLTSFPEIFINIGILLGYVSNYFFSKLPEHLGWRFMLGVGAVPSVFLAIGVLAMPESPRWLVLQGRLGDAFKVLDKTSNTKEEAISRLDDIKRAVGIPDDMTDDVIVVPNKKSAGKGVWKDLLVRPTPSVRHILIACLGIHFAQQASGIDAVVLYSPTIFSKAGLKSKN... | Plasma membrane sugar-proton symporter. |
Q9XIK6 | SNL6_ARATH | Paired amphipathic helix protein Sin3-like 6 | MRDLLLGTTIPSYFSWLGLFPRFLVWFGFLKASFFCSSRNQSAGESGRRLKMKRAREDVHTDTQKRKPEVSSRGETNKLPRTIDALTYLKAVKDIFHDNKEKYESFLELMKEFKAQTIDTNGVIERIKVLFKGYRDLLLGFNTFLPKGYKITLLPEEEKPKIRVDFKDAIGFVTKIKTRFGDDEHAYKRFLDILNLYRKEKKSISEVYEEVTMLFKGHEDLLMEFVNFLPNCPESAPSTKNAVPRHKGTATTAMHSDKKRKQRCKLEDYSGHSDQREDGDENLVTCSADSPVGEGQPGYFRDYENREDTETDTADRTEKS... | Acts as a transcriptional repressor. Plays roles in regulating gene expression and genome stability (By similarity). |
Q9XIN1 | ALMT7_ARATH | Aluminum-activated malate transporter 7 (AtALMT7) | MEKVREIVREGRRVAKEDPRRVVHSFKVGLVLALVSSFYYYQPLYDSFGVNAMWAVMTVVVVFEFSVGATLGKGLNRVAATLFAGGLGIGAHHLASMSGPTGEPILLAVFVFVQAALSTFVRFFPRVKARYDYSLLIFILTFALISVSGFREEQVVKLTHKRISTVIIGGLSCVIISIFVCPVWAGQDLHSLIASNFEKLSFFLLGNSFHYVSSDLNSITLLRKIKSWRLADFGDKYCEVVENDGAKEVDKRKKDFDNYKSVLNSKSNEESLANFAKWEPGHGQFRFRHPWKQYLAVGELIRQCAYRIHALNSYLNADNQ... | Malate transporter. |
Q9XIQ7 | FBT7_ARATH | Probable folate-biopterin transporter 7 | MSSSSDTHAGESRHRRNPIRWLLGFGFFVQGFRGFPWLGANFFLTEQLRVNPSVLQLLQNSANLPMVAKPIYGVVSDSVYFFGQHRIPYIAVGALLQAISWLAIAFLSRSNVSILALSIYLLLSNLGASLVEVANDAIVAESGKQKTSETQSGELPSFVWMVSSLGGILGNLLGGIAIKTFSAQSTFLVFGILALLQFLVTINIREKSLNLPENPSPAGGIRKHLSDLSHVLRKPEISYSIAWIAVSTAVVPVLTGTMFFYQTKFLKIDASLLGISKVFGQIAMLLWGFAYNRWLKAMRPRKLLTAIQVTIAFFVISDLL... | Could mediate folate transport. |
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