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AlphaFoldDB
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B2RLY1
RL24_PORG3
50S ribosomal protein L24
Porphyromonas
MSKLHIKKGDTVMVISGEDKGHSGRVLEVLVKEQRAIVEGLNMIKKHAKPSAKNPQGGIISKEAPIHISNLNVVDPKTGKATRIGRRLNENGKLVRYAKKSGEEIK
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
B2RLY1
P77774
BAMB_ECOLI
Outer membrane protein assembly factor BamB
Escherichia
MQLRKLLLPGLLSVTLLSGCSLFNSEEDVVKMSPLPTVENQFTPTTAWSTSVGSGIGNFYSNLHPALADNVVYAADRAGLVKALNADDGKEIWSVSLAEKDGWFSKEPALLSGGVTVSGGHVYIGSEKAQVYALNTSDGTVAWQTKVAGEALSRPVVSDGLVLIHTSNGQLQALNEADGAVKWTVNLDMPSLSLRGESAPTTAFGAAVVGGDNGRVSAVLMEQGQMIWQQRISQATGSTEIDRLSDVDTTPVVVNGVVFALAYNGNLTALDLRSGQIMWKRELGSVNDFIVDGNRIYLVDQNDRVMALTIDGGVTLWTQSDLLHRLLTSPVLYNGNLVVGDSEGYLHWINVEDGRFVAQQKVDSSGFQTEPVAADGKLLIQAKDGTVYSITR
Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits . A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins .
P77774
O14618
CCS_HUMAN
Superoxide dismutase copper chaperone
Homo
MASDSGNQGTLCTLEFAVQMTCQSCVDAVRKSLQGVAGVQDVEVHLEDQMVLVHTTLPSQEVQALLEGTGRQAVLKGMGSGQLQNLGAAVAILGGPGTVQGVVRFLQLTPERCLIEGTIDGLEPGLHGLHVHQYGDLTNNCNSCGNHFNPDGASHGGPQDSDRHRGDLGNVRADADGRAIFRMEDEQLKVWDVIGRSLIIDEGEDDLGRGGHPLSKITGNSGERLACGIIARSAGLFQNPKQICSCDGLTIWEERGRPIAGKGRKESAQPPAHL
Delivers copper to copper zinc superoxide dismutase (SOD1).
O14618
B8CI18
HSLU_SHEPW
Unfoldase HslU
Shewanella
MSEMTPREIVHELDSHIIGQQKAKRSVAIALRNRWRRMQLAADLRQEVTPKNILMIGPTGVGKTEIARRLARLAKAPFIKVEATKFTEVGYVGKEVEQIIRDLTDSAIKLTREEQMAKCKFRAEEAAEERILDALLPKPKEDWDNEKPSDNATRQVFRKKLREGQLDDKEIEIDIAAPQAGIEIMSPPGMEEMTNQLQSMFQNMGPGASKRRKMPIKEAHKLLIEEEAAKLVNADDLKEQAIELVEQHGIVFLDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVNTKHGMVKTDHILFIASGAFQMSKPSDLIPELQGRLPIRVELEALSADDFKRILTEPHASLTEQYVALMGTEGVEVEFKDSGIDAIAEAAWQVNERTENIGARRLHTVMERLMEELSYEASDKSGSVTVVDADYVKAHLDNLVQDEDLSRFIL
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
B8CI18
Q8ZW59
AROD_PYRAE
Type I dehydroquinase
Pyrobaculum
MLQYGVLICGVVPVRKPRDIEKALEAPVTCLELRLDYLEADLAEVRPLLEHAVARRVVIFTVRRREEGGQWRGDEEGREALYRKLLELNPHYIDVEAESPIIGEVAKIKGKAQLIASRHDFEKTPPLDVLSQWAKKAAAVGDLVKIVTYAKEPGDGLRVLSLIGAVEKPTVAFAMGPAGAYTRVAAAALGSPIMYVSLGEATAPGQLTADAYYAALLALGITPSGGGLPALREALDWVDGGLMYLLKKRLEVCRDMGRLKKDAGLPIYDDVREAQVLRRAGDFKQIFELVVQMCKAVQLVA
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Q8ZW59
P67586
SYW_BRUME
Tryptophanyl-tRNA synthetase
Brucella
MSTFKPLVFSGVQPTGNLHLGNYLGAIKRWVEVQKTEECIYCVVDMHALTVSPDPVELMQSTREVTAAFLAAGIDPKKSIVFNQSRVMQHAELAWVFNCVARIGWMSRMTQFKDKAGKDRENASLGLFAYPSLMAADILLYRATAVPVGEDQKQHLELTRDIAQKFNNDYSDRIASLGVGVDMKVGDEQVSGFFPLTEPMISGPAMRIMSLRDGTKKMSKSDPSDLSRINLIDDEDTITKKIRKAKTDSDGLPSEVDGLEGRPEADNLVGIYAALSSTTKEDVLKEFGGRQFSDLKASLADLAVARLSPITHEMRRLVADPAHIDSVLRDGGEQAGAIAEQTMRHVRDIVGWLQN
Catalyzes the attachment of tryptophan to tRNA(Trp).
P67586
B9JK76
APIBP_AGRRK
D-apiose binding SBP
Agrobacterium tumefaciens complex
MKLTRRLTLAAFASVLALGTAAPAFSADLIAIITPAHDNPFFKAEAVGAEAKAKELGYDTLVMSHDDDANKQSEVIDTAIGRGAKAIILDNAGADATVAAIKKAKDAGIPSFLIDREINVTGIAVAQIVSNNYQGAQLGAQEFVKLMGEKGNYAELVGREADTNAGIRSQGYHDVIDDYPDLKLVAKQSANWSQTEAYAKMETILQANPDIKGVISGNDTMAMGAIAALQAAGRKDVIVVGFDGSNDVRDSIKAGGIKATVMQPAYAQAQIAVQQADAYIKNKTVPKDEKQLMDCVLINADNADKLETFALKN
Part of an ABC transporter complex involved in D-apiose import.
B9JK76
Q9URQ3
TAD3_YEAST
tRNA-specific adenosine-34 deaminase subunit TAD3
Saccharomyces
MVKKVNNPLKIDYQNGIIENRLLQIRNFKDVNTPKLINVWSIRIDPRDSKKVIELIRNDFQKNDPVSLRHLKRIRKDIETSTLEVVLCSKEYICDEGEINNKLKSIWVGTKKYELSDDIEVPEFAPSTKELNNAWSVKYWPLIWNGNPNDQILNDYKIDMQEVRNELSRASTLSVKMATAGKQFPMVSVFVDPSRKKDKVVAEDGRNCENSLPIDHSVMVGIRAVGERLREGVDEDANSYLCLDYDVYLTHEPCSMCSMALIHSRVRRVVFLTEMQRTGSLKLTSGDGYCMNDNKQLNSTYEAFQWIGEEYPVGQVDRDVCC
Deaminates adenosine-34 to inosine in many tRNAs.
Q9URQ3
Q1WS94
RS19_LIGS1
30S ribosomal protein S19
Ligilactobacillus
MSRSLKKGPFVDEHLMKKVEAQADQEKKSVIKTWSRRSTIFPSFIGYTIAVYDGRKHVPVYIQEDMVGHKLGEFVPTRTFHGHGNDDKKTGVR
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Q1WS94
Q7V8W6
SEPF_PROMM
Cell division protein SepF
Prochlorococcus
MSLISRLRAVVAGDDYLDSDYDDLDYDTDDHMDADHRSDHASGGALATPSDSSPFDLGGGFSGSNVIGMPGVGSTSAEVNLMEPRSFDEMPRAIQALRERKTVILNLTMMEPDQAQRAVDFVAGGTFAIDGHQERVGESIFLFAPSCVTVSNTSYDEASAPSMVSQDHDSVPSSSQQTGAAPVPAWEATSAGGL
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
Q7V8W6
Q6ZNB7
ALKMO_HUMAN
Transmembrane protein 195
Homo
MKNPEAQQDVSVSQGFRMLFYTMKPSETSFQTLEEVPDYVKKATPFFISLMLLELVVSWILKGKPPGRLDDALTSISAGVLSRLPSLFFRSIELTSYIYIWENYRLFNLPWDSPWTWYSAFLGVDFGYYWFHRMAHEVNIMWAGHQTHHSSEDYNLSTALRQSVLQIYTSWIFYSPLALFIPPSVYAVHLQFNLLYQFWIHTEVINNLGPLELILNTPSHHRVHHGRNRYCIDKNYAGVLIIWDKIFGTFEAENEKVVYGLTHPINTFEPIKVQFHHLFSIWTTFWATPGFFNKFSVIFKGPGWGPGKPRLGLSEEIPEVTGKEVPFSSSSSQLLKIYTVVQFALMLAFYEETFADTAALSQVTLLLRVCFIILTLTSIGFLLDQRPKAAIMETLRCLMFLMLYRFGHLKPLVPSLSSAFEIVFSICIAFWGVRSMKQLTSHPWK
Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of ether lipids. Ether lipids are essential components of brain membranes.
Q6ZNB7
Q8VE98
CD276_MOUSE
Costimulatory molecule
Mus
MLRGWGGPSVGVCVRTALGVLCLCLTGAVEVQVSEDPVVALVDTDATLRCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFTEGRDQGSAYSNRTALFPDLLVQGNASLRLQRVRVTDEGSYTCFVSIQDFDSAAVSLQVAAPYSKPSMTLEPNKDLRPGNMVTITCSSYQGYPEAEVFWKDGQGVPLTGNVTTSQMANERGLFDVHSVLRVVLGANGTYSCLVRNPVLQQDAHGSVTITGQPLTFPPEALWVTVGLSVCLVVLLVALAFVCWRKIKQSCEEENAGAEDQDGDGEGSKTALRPLKPSENKEDDGQEIA
Modulates T-cell-mediated immune responses and the development of acute and chronic transplant rejection. Plays a positive regulatory role in bone formation and has a dual role in the bone-immune interface. Induces antitumor immunity as it activates both acquired and innate immunity leading to natural killer cell and CD8 T-cell dependent killing of tumor cells.
Q8VE98
Q4A172
SYS_STAS1
Seryl-tRNA(Ser/Sec) synthetase
Staphylococcus
MLDIKLFRNDPEFLKEKVAKRGMDSKVVDEVLELDEQRRQLISQAEEMKAERNKVSGEIAQKKRNKEDADDAIAAMRNLGDEIKVLDDTLNQVDVDLNDKLSRIPNIIHDDVPEGATDEDNIEVKRWGTPRTFEFEDKAHWDLVEELEMVDFERAAKVSGARFVFLTGDGAQLERALMNYMITKHTTQHGYTEMMVPQLVNADSMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNYYRNEIIAPDVLPAKFTAQSACYRSEAGSAGRDTRGLIRLHQFDKVEMVRIEKPEDSWQALEDMTHHAEAILEELGLPYRRVILCTGDIGFGSSKTYDLEVWLPSYNDYKEISSCSNITDFQARRSNIRFKRDKNAKPELAHTLNGSGLAVGRTFAAIVENYQNEDGSVTIPEVLVPFMGGKTVIRPTK
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Q4A172
P13762
DRB4_HUMAN
MHC class II antigen DRB4
Homo
MVCLKLPGGSCMAALTVTLTVLSSPLALAGDTQPRFLEQAKCECHFLNGTERVWNLIRYIYNQEEYARYNSDLGEYQAVTELGRPDAEYWNSQKDLLERRRAEVDTYCRYNYGVVESFTVQRRVQPKVTVYPSKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSMMSPLTVQWSARSESAQSKMLSGVGGFVLGLLFLGTGLFIYFRNQKGHSGLQPTGLLS
Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.
P13762
Q0I3F9
FABA_HAES1
Trans-2-decenoyl-[acyl-carrier-protein] isomerase
Histophilus
MNKKNSYSYEDLLASGRGELFGEKGPQLPAPSMLMMDRVVEMNEEGGLFNKGYVEAELDINPSLSFFGCHFIGDPVMPGCLGLDAMWQLVGFYLGWIGGQGKGRALGVGEVKFTGQILPTAKKVIYRINMKRVINRKLVMGMADGEVEVDGKVIYTATDLKVGLFQDTSTF
Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length.
Q0I3F9
D4H9Y2
BIOWF_CUTAS
8-amino-7-ketopelargonate synthase
Cutibacterium
MVFNCYPVANAEESPMSSQNPTTVAWWSVRMRATGTLDDEPYHVSGAESLVAPGMIEQTVAGLTQRALAPGHTVKARQVRVSLDQLDVEPTIIPALPTELKECPDPVAARQYFVDVLSRFVPHPAEALRVLTEGPTMRGAAMVEAGTDRRLEADPLRGVRVTKFGDLTESAPGASLAHKKHHHEAVLLASKVAAAPGVLAEFCISDDPHYTRGYVCVDGVYTTVTNVKADGDPNGGRVILVDTARADPTTITTWLENHPVLIGPATASSQKATSWHGHLCGRLNAWRAAGLERRPRTFCSAQDPDAVTTDGPALLFSSSDYLGLSTEPKVQQAMNNTVRRLGSSSGGSRLTTGTSVAHHQAEHEIAAWLGYPQAVFMASGYQANIATIQLLADPHVTVISDAENHASLIDGCRLARARTVVVPHADLDVIDTALDCVTTDRALVLTEGVYSMGGDVAPVGELVEIAHRHGALVVVDDAHGIGTVGPTGRGATEELPASQRPDVLLGTASKALGVEGGFACLDETLATLMRNCARGYVFSSAPSPVVAAGVAAAVEYLRTDTRRVCSLQANVAQARLLLAEADLIPPSAAHDRGPIIRIPVGPESRAVAAQEELARRGLMVGAIRYPAVARGDAILRICLTARHTDEHIRILVTSLREVLDGALSDAPR
Catalyzes both the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide, and the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.
D4H9Y2
B0VYX9
COX5A_CEBPY
Cytochrome c oxidase polypeptide Va
Cebuella
MLGAALRRCAVAATARAGPRGLLHSAPTPGPAAAIQSVRCYSHGSSETDEEFDARWVTYFNKPDIDAWELRKGINTLVTYDLVPEPKIIDAALRACRRLNDFASTVRILEAVKDKAGPHKEIYPYVIQELRPTLNELGISTPEELGLDKV
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
B0VYX9
P58554
G3P2_NOSS1
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
Nostoc
MIRVAINGFGRIGRNFARCWLGRENTNIELVAVNDTSDPRTNAHLLKYDSMLGKLKNVDITADDNSITVNGKTIKCVSDRNPENLPWKEWEIDLIIEATGVFVSKEGATKHINAGAKKVLITAPGKNEDGTFVMGVNHHDYDHNLHNIISNASCTTNCLAPIAKVLNDKFGIIKGSMTTTHSYTGDQRLLDASHRDLRRARAAAINIVPTSTGAAKAVALVIPELKGKLNGVALRVPTPNVSMVDFVVQVEKRTITEEVNQALKDASEGPLKGILDYSELQLVSSDYQGTDASSIVDANLTLVMGNDLVKVMAWYDNEWGYSQRVLDLAELVAEKWV
Gap2 has a major role in carbon fixation as a component of the Calvin cycle. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NADP. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NADP to NADPH. The reduced NADPH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
P58554
B8DU54
ARGC_BIFA0
N-acetyl-glutamate semialdehyde dehydrogenase
Bifidobacterium
MTKYTVAVAGATGYAGGEALRILAAHPAFEVTAVAGHSSIGHRLGEYQPHIPQLADLIVEDTTPAVLDGHDVIVLALPHGASGALAAQLDDDAVVVDLGADHRLERQQAWDDYYGGDFYQHWTYGMPELILGIGSDGKYVRQRDELTGAKRIAGPGCNVTATTLALQPAIAQGLVDTKSIVADLAVGYSGAGKNLKRTNLLASEAMGSASPYSVGGTHRHIPEIRQNFAHAAGLGASQADMFSLAFTPILVPMSRGILASVSAKLTDEALALTDEQIHDIWVQAYEGQEFIFVLDPGVMPATQNVLGSNAAHVQVAVDRRSGTLHAFTAIDNLNRGTAGQAIESLNIAFGLNDATGLSKIGVAP
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
B8DU54
P0A3S2
NIFH_TRIAZ
Nitrogenase reductase
Trichormus
MTDENIRQIAFYGKGGIGKSTTSQNTLAAMAEMGQRIMIVGCDPKADSTRLMLHAKAQTTVLHLAAERGAVEDLELHEVMLTGFRGVRCVESGGPEPGVGCAGRGIITAINFLEENGAYQDLDFVSYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMAMYAANNIARGILKYAHSGGVRLGGLICNSRKTDREAELIENLAERLNTQMIHFVPRDNIVQHAELRRMTVNEYAPDSNQGQEYRALAKKIINNDKLTIPTPIEMDELEALLIEYGILDDDSKHAEIIGKPAEATK
The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
P0A3S2
A1DMV3
FAEB2_NEOFI
Ferulic acid esterase B-2
Aspergillus subgen. Fumigati
MTKLSLLPLLALASAVLAKQDAFQAKCASFGHRIKLPNVHVNFVEYVPGGTNLTLPDNHVTCGASSQIVSADMCRVAMAVDTSKSSQITLEAWFPRNYTGRFLSTGNGGLSGCIQYYDLAYTAGLGFATVGANNGHNGTSGKPFYQHPEVIEDFAYRSIHTGVVVGKQLIKMFYSEGFDKSYYLGCSTGGRQGFKSIQKYPNDFDGVVAGAPAFNFVNLISWSIHFYSITGSNTSDTYLSPASWKVVHDEIVRQCDGIDGAKDGIIEDTDLCHPILETIICKPGASSTTNCITGTQAKTVRNVLSPFYGVNGTLLYPRMQPGSELFASSIMYNGQPFSYSTDWYRYVVYNNPNWDATKWTVEDAAVALAQNPYNIQTWDADISSFQKAGGKVLTYHGIQDQLISSDNSKLYYARVAETMGLGPEELDDFYRFFPVSGMAHCSGGDGAYGIGNGLRTYNGAEPENNVLMAMVQWVEKGVAPEFIRGAKFSNGVGSPVEYTRKHCKYPRRNVYKGPGNYSDENAWECV
Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin.
A1DMV3
Q9UJZ1
STML2_HUMAN
Paraprotein target 7
Homo
MLARAARGTGALLLRGSLLASGRAPRRASSGLPRNTVVLFVPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEASAVLAKAKAKAEAIRILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTILLPSNPGDVTSMVAQAMGVYGALTKAPVPGTPDSLSSGSSRDVQGTDASLDEELDRVKMS
Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation.
Q9UJZ1
A6GZ85
RS8_FLAPJ
30S ribosomal protein S8
Flavobacterium
MYTDPIADYLTRVRNAAKANHKVVEIPASNMKKEITKILFDQGYILSYKFEDNAVQGSIKIALKYDKVTKESVIRDIQRISKPGLRKYSGSSTIPRILNGLGIAIVSTSKGLMTGKLAKQLNVGGEVICYVY
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.
A6GZ85
Q6NG19
PDXY_CORDI
Pyridoxal kinase PdxY
Corynebacterium
MNILSIQSHVSYGHVGNSAAVFPLQRIGHEVWPVHTVNFSNHTGYGQWGGELIPAAQVRNVIDGMEQRGAFERIDAILSGYQGGSDIADVIVDAVARIKEANPQAVYACDPVMGNAKSGCFVSDLIPPLLRDKVVPVADIITPNQFELEYLTGVPAHDTTSTLEAIAAAQEMGPNTVLVTSVRRPETPADAIEMIAANEQGAWLVRTPFIDFKRNGSGDVTAALFTGHYIRERDAADALARTASSVFDLIETTFTADSRELLIIESQEAIAHPRLQFEVEQIA
Pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP.
Q6NG19
O64964
TIP11_MAIZE
ZmTIP1;1
Zea
MPINRIALGSHQEVYHPGALKAAFAEFISTLIFVFAGQGSGMAFSKLTGGGPTTPAGLIAAAVAHAFALFVAVSVGANISGGHVNPAVTFGAFVGGNITLFRGLLYWVAQLLGSTVACFLLRFSTGGQATGTFGLTGVSVWEALVLEIVMTFGLVYTVYATAVDPKKGSLGTIAPIAIGFIVGANILVGGAFDGASMNPAVSFGPALVSWEWGYQWVYWVGPLIGGGLAGVIYELLFISHTHEQLPSTDY
Water channel required to facilitate the transport of water across cell membrane. May support the rapid influx of water into vacuoles during cell expansion, permit osmotic equilibration between the cytosol and the vacuolar content and rapid transcellular water flow through living cells. Its function is impaired by Hg(2+).
O64964
Q04KY2
TRMFO_STRP2
Folate-dependent tRNA(M-5-U54)-methyltransferase
Streptococcus
MSQSYINVIGAGLAGSEAAYQIAERGIPVKLYEMRGVKSTPQHKTDNFAELVCSNSLRGDALTNAVGLLKEEMRRLGSVILESAEATRVPAGGALAVDRDGFSQMVTEKVANHPLIEVVRDEITELPTDVITVIATGPLTSDALAEKIHALNDGDGFYFYDAAAPIIDVNTIDMSKVYLKSRYDKGEAAYLNAPMTKQEFMDFHEALVNAEEAPLNSFEKEKYFEGCMPIEVMAKRGIKTMLYGPMKPVGLEYPDDYTGPRDGEFKTPYAVVQLRQDNAAGSLYNIVGFQTHLKWGEQKRVFQMIPGLENAEFVRYGVMHRNSYMDSPNLLEQTYRSKKQPNLFFAGQMTGVEGYVESAASGLVAGINAARLFKEESEVIFPETTAIGSLAHYITHADSKHFQPMNVNFGIIKELEGERIRDKKARYEKIAERALADLEEFLTV
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Q04KY2
B2AHB8
RECA_CUPTR
Recombinase A
Cupriavidus
MDDKKAGAGVSAEKQKALAAALSQIEKQFGKGSIMRLGDGEVEKDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTCAFIDAEHALDVNYASKLGVNVGDLLISQPDTGEQALEITDALVRSGSIDLIIIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGSIKKGDDVIGNETKVKVVKNKVSPPFREAFFDILYGQGISRQGEIIDLGVDAKIVEKSGAWYSYNGEKIGQGKDNAREYLRENPDIAAEIENKVRAALGVVAMNPTAAAVAATVED
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
B2AHB8
B2A5V3
CH60_NATTJ
Chaperonin-60
Natranaerobius
MAKDIKFREDARARLEQGVNKLADTLKVTLGPKGRNVVLDKKFGSPQITNDGVTIARDIDLEDNYENMGAQLVKEVATQTNDVAGDGTTTATILAQAMVNEGIKNVTAGANPMIIRKGIQKAVDRAVEELQKNAVSVEDKESISQVASISANDEEVGKLIAEAMEKVGKDGVITVEESKSFKTDLNVVEGMQFDRGYVSPYMVTDNEKMEAHLEEPYILITDKKIGNIQEILPVLEKIVEQGKEVLLIAEDIEGEALATLVVNKLRGTFTCVGVKAPGFGDRRKAMLEDIAVLTGGQVISEDVGLELKNADISMLGRARQVTITKDDTTIVDGYGNEEDIQKRITQLRTQIEETTSDFDREKLEERLAKLAGGVAVVEVGAATETEMKEKKLRIEDALNSTRAAVEEGIVAGGGTALIDVLPSLEEVQADGDESTGVSIVRRALEEPVRQLAHNSGAEGSIVAEQVKQKGTNIGFNALENDYTNMLDAGVVDPKKVTRSALENAGSIAAMFLTTEAVVADLPDEDDNDDGDMGGGAPGMGGMGGMPGM
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.
B2A5V3
P47404
RL16_MYCGE
50S ribosomal protein L16
Mycoplasma
MLQPKRTKYRKPHNVSYEGHTKGNGYVAFGEYGIVATKGNWIDARAIESARVAISKCLGKTGKMWIRIFPHMSKTKKPLEVRMGSGKGNPEFWVAVVKKGTVMFEVANIPEQQMIKALTRAGHKLPVTWKLMKREENS
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
P47404
Q61UA0
UFSP_CAEBR
Odorant response abnormal protein 8
Caenorhabditis
MSGSQTVSVIGYTKMAPQSPPATVNELWFIDTQAMFQNYANLRSFSKSNSTETQTTIGGVVFGRKARKQVIHVFFAYAEDLTESNLQFLESSLSSDIELVGNVNIDGQSTLIGNGTFTLQLSSKMLENKNTSEFLDQNVIFNNDHISMEGASCVSKVGFEWSLRAGREQEDVKSAAERLSMASFRFSYLNAEHELVIREHKPETAKQKYMDKFTKGALPYKDVIEFTAMQSLTRDTSNDTEDQKLVPTVKVTKDNKHFTRLVTIGEVVFPAYFGDSSFDLYKRAREALNRRANNTMMVTVNGIRSGRGVTTTTSATYLPPGWVSLLHLQLPSKWTENEKRNYRIRLHKLFNLPSSKPCLRLSQSLPLHSESVRLTNKKLIREPHLSISNYQPAGVVTAVKGPYNYHHYMQDGIDDSGWGCAYRSFQTIWSWFILNGYTDKPVPSHRDIQQALVNIGDKEQKFVGSRQWIGSTEISYVLNELLKLECRFIATNSGAEVVERARELARHFETSGTPVMIGGNMLAHTILGVDFNEMTGETKFLILDPHYTGSEDIKTITSKGWCAWKPASFWSADHFYNMVLAQPPTDSI
Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ufm-1, a ubiquitin-like modifier protein bound to a number of target proteins. Required, with oct-4, for the localization of a subset of 7 transmembrane domain odorant receptors, including odr-10, to the cilia of olfactory neurons AWA and AWC. Operates in aggregation behavior, and responses to oxygen levels.
Q61UA0
P55034
PSMD4_ARATH
Multiubiquitin chain-binding protein 1
Arabidopsis
MVLEATMICIDNSEWMRNGDYSPSRLQAQTEAVNLLCGAKTQSNPENTVGILTMAGKGVRVLTTPTSDLGKILACMHGLDVGGEINLTAAIQIAQLALKHRQNKNQRQRIIVFAGSPIKYEKKALEIVGKRLKKNSVSLDIVNFGEDDDEEKPQKLEALLTAVNNNDGSHIVHVPSGANALSDVLLSTPVFTGDEGASGYVSAAAAAAAAGGDFDFGVDPNIDPELALALRVSMEEERARQEAAAKKAADEAGQKDKDGDTASASQETVARTTDKNAEPMDEDSALLDQAIAMSVGDVNMSEAADEDQDLALALQMSMSGEESSEATGAGNNLLGNQAFISSVLSSLPGVDPNDPAVKELLASLPDESKRTEEEESSSKKGEDEKK
Plays a role in maintaining the structural integrity of the 19S regulatory particle (RP), subcomplex of the 26S proteasome. Plays a major role in both the direct and indirect recognition of ubiquitinated substrates of ubiquitin/26S proteasome-mediated proteolysis (UPP). Binds and presumably selects ubiquitin-conjugates for destruction. Prefers multiubiquitin chains rather than single ubiquitins, with a binding affinity for 'Lys-48'-linked ubiquitin chains. Acts as a potential docking subunit for both ubiquitin receptors RAD23s and DSK2s. Plays a role in the growth and development via the proteasome-dependent degradation of the ABA-signaling protein ABI5/DPBF1. Plays an important role for balancing cell expansion with cell proliferation rates during shoot development.
P55034
Q6CYJ1
ATPF_PECAS
F-type ATPase subunit b
Pectobacterium
MNINATILGQAIAFVLFVWFCMKYVWPPMMAAIEKRQKEIADGLASAERAKKDLNLAQANATDQLKKAKADAQVIIEQANKRRAQILDEAKAEAEAERNKIVAQAQAEIEAERKRAREELRKQVAVLAIAGAEKIIERSVDEAANSDIVDKLVAEL
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Q6CYJ1
Q9VRB3
CP6V1_DROME
CYPVIV1
Sophophora
MVYSTNILLAIVTILTGVFIWSRRTYVYWQRRRVKFVQPTHLLGNLSRVLRLEESFALQLRRFYFDERFRNEPVVGIYLFHQPALLIRDLQLVRTVLVEDFVSFSNRFAKCDGRSDKMGALSLFLAKQPEWREIRTRLAPAFAGAKLKQMFSLMEEIGCDLEWYLKRLTRDLRRGDAERGAIVSIKDVCDLYNTDMIASIAFGLRSYSLRNTQSEIGSHCQDLFRPNVRRIIDLFVIFYLPKLVPLLRPKLFTEPHAEFLRRVIQLVIEERERGGDLRNDLIEMLLTLKKEADLQQDKSHFTHHRDFLAAQAASFEVAGIETCSASMSFALYELAKQPLMQSRLRREIREAFASNPNGRLTYEAVARMEFLDMVVEETLRKYPIVPLLERECTPINKKRFYSLRPHAECYTRRGMPVFISNLAIHHDPKYWPDPDRFDPERFSAANKALQAPMSYMPFGAGPRNCIGMQIGLLQIKLGLVYFLHQHRVEICDRTVERIQFDAKFALLASEQRIYLKVDCL
May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Q9VRB3
A5VYG5
RF1_PSEP1
Peptide chain release factor 1
Pseudomonas
MKASLLNKLEILQDRFEELTALLGDAEVISDQTRFRAYSREYAEVEPVYAAYKEWRKVQDDLEGAQALLKDSDPDLREMALEEVREAKEQLLTLEAQLQRMLLPKDPNDGRNVFLEIRAGTGGDEAAIFSGDLFRMYSRYAEKRGWRLEILSENEGEHGGYKEIIARVEGENVYGKLKFESGAHRVQRVPETESQGRVHTSACTVAVLPEPDEQAAIEINPADLRVDTYRASGAGGQHVNKTDSAIRITHLPTGIVVECQEERSQHKNRARAMSWLSAKLNDMQTSAAQNAIASERKLLVGSGDRSERIRTYNYPQGRVTDHRINLTLYSLDDILSGGVDAVIEPLLAEYQADQLAALGD
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
A5VYG5
B4UGV2
LPXA_ANASK
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
unclassified Anaeromyxobacter
MAIHPTAIVEAGAQVDPSCEIGPFAVIGPLVRMGPGNSVGPHAVVTGRTTLGASNRIFPHAVIGGIPQDLKYRGEDTALVIGDRNTFREFATVNLGTAGGGGVTRIGSGGLFMASSHIGHDCQVGDGAIIANSVAIAGHVLIEDHVHFGGLSASHQFCRVGRLAFVGGMTGVAMDVAPYCTVAGARGELAGLNAIGMQRAGLTEEQIGRVKQAYKIVFRSSLGLAEAIAQLEAELAGHPETDHFIAFLKGSQRGITR
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
B4UGV2
Q7TPD3
ROBO2_MOUSE
Roundabout homolog 2
Mus
MNPLMFTLLLLFGFLCIQIDGSRLRQEDFPPRIVEHPSDVIVSKGEPTTLNCKAEGRPTPTIEWYKDGERVETDKDDPRSHRMLLPSGSLFFLRIVHGRRSKPDEGSYVCVARNYLGEAVSRNASLEVALLRDDFRQNPTDVVVAAGEPAILECQPPRGHPEPTIYWKKDKVRIDDKEERISIRGGKLMISNTRKSDAGMYTCVGTNMVGERDSDPAELTVFERPTFLRRPINQVVLEEEAVEFRCQVQGDPQPTVRWKKDDADLPRGRYDIKDDYTLRIKKAMSTDEGTYVCIAENRVGKVEASATLTVRVRPVAPPQFVVRPRDQIVAQGRTVTFPCETKGNPQPAVFWQKEGSQNLLFPNQPQQPNSRCSVSPTGDLTITNIQRSDAGYYICQALTVAGSILAKAQLEVTDVLTDRPPPIILQGPINQTLAVDGTALLKCKATGEPLPVISWLKEGFTFLGRDPRATIQDQGTLQIKNLRISDTGTYTCVATSSSGETSWSAVLDVTESGATISKNYDMNDLPGPPSKPQVTDVSKNSVTLSWQPGTPGVLPASAYIIEAFSQSVSNSWQTVANHVKTTLYTVRGLRPNTIYLFMVRAINPQGLSDPSPMSDPVRTQDISPPAQGVDHRQVQKELGDVVVRLHNPVVLTPTTVQVTWTVDRQPQFIQGYRVMYRQTSGLQASTVWQNLDAKVPTERSAVLVNLKKGVTYEIKVRPYFNEFQGMDSESKTVRTTEEAPSAPPQSVTVLTVGSHNSTSISVSWDPPPADHQNGIIQEYKIWCLGNETRFHINKTVDAAIRSVVIGGLFPGIQYRVEVAASTSAGVGVKSEPQPIIIGGRNEVVITENNNSITEQITDVVKQPAFIAGIGGACWVILMGFSIWLYWRRKKRKGLSNYAVTFQRGDGGLMSNGSRPGLLNAGDPNYPWLADSWPATSLPVNNSNSGPNEIGNFGRGDVLPPVPGQGDKTATMLSDGAIYSSIDFTTKTTYNSSSQITQATPYATTQILHSNSIHELAVDLPDPQWKSSVQQKTDLMGFGYSLPDQNKGNNGGKGGKKKKTKNSSKAQKNNGSTWANVPLPPPPVQPLPGTELGHYAAEQENGYDSDSWCPPLPVQTYLHQGMEDELEEDEDRVPTPPVRGVASSPAISFGQQSTATLTPSPREEMQPMLQAHLDELTRAYQFDIAKQTWHIQSNTPPPQPPAPPLGYVSGALISDLETDVPDEDADDEEEPLEIPRPLRALDQTPGSSMDNLDSSVTGKAFSSSQRQRPTSPFSTDSNTSAAQNQSQRPRPTKKHKGGRMDPQPVLPHRREGMPDDLPPPPDPPPGQGLRQQIGLSQHSGNVENSTERKGSSLERQQAANLEDTKSSLDCPAKTVLEWQRQTQDWINSTERQEETRKAPHKQGVGSEESLVPYSKPSFPSPGGHSSSGTSSSKGSTGPRKADVLRGSHQRNANDLLDIGYVGSNSQGQFTE
Receptor for SLIT2, and probably SLIT1, which are thought to act as molecular guidance cue in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development.
Q7TPD3
P52742
ZN135_HUMAN
Zinc finger protein 78-like 1
Homo
MTPGVRVSTDPEQVTFEDVVVGFSQEEWGQLKPAQRTLYRDVMLDTFRLLVSVGHWLPKPNVISLLEQEAELWAVESRLPQGVYPDLETRPKVKLSVLKQGISEEISNSVILVERFLWDGLWYCRGEDTEGHWEWSCESLESLAVPVAFTPVKTPVLEQWQRNGFGENISLNPDLPHQPMTPERQSPHTWGTRGKREKPDLNVLQKTCVKEKPYKCQECGKAFSHSSALIEHHRTHTGERPYECHECLKGFRNSSALTKHQRIHTGEKPYKCTQCGRTFNQIAPLIQHQRTHTGEKPYECSECGKSFSFRSSFSQHERTHTGEKPYECSECGKAFRQSIHLTQHLRIHTGEKPYQCGECGKAFSHSSSLTKHQRIHTGEKPYECHECGKAFTQITPLIQHQRTHTGEKPYECGECGKAFSQSTLLTEHRRIHTGEKPYGCNECGKTFSHSSSLSQHERTHTGEKPYECSQCGKAFRQSTHLTQHQRIHTGEKPYECNDCGKAFSHSSSLTKHQRIHTGEKPYECNQCGRAFSQLAPLIQHQRIHTGEKPYECNQCGRAFSQSSLLIEHQRIHTKEKPYGCNECGKSFSHSSSLSQHERTHTGEKPYECHDCGKSFRQSTHLTQHRRIHTGEKPYACRDCGKAFTHSSSLTKHQRTHTG
Plays a role in the regulation of cell morphology and cytoskeletal organization. May be involved in transcriptional regulation.
P52742
A4WDA9
ISCA_ENT38
Iron-sulfur cluster assembly protein
Enterobacter
MSITLSDSAAARVSSFLENRGKGYGLRLGVRTSGCSGMAYVLEFVDEPATDDTVFEDKGVKVVIDGKSLQFLDGTQLDFVKEGLNEGFKFTNPNVKDECGCGESFHV
Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system TrxA/TrxB.
A4WDA9
Q18A79
GLGA_CLOD6
Starch [bacterial glycogen] synthase
Clostridioides
MKVFYVTAECWPFAKTGGLGDVSYALPKELKKEGVDVRVIMPKYSTIPSYLKDQLKEIAVFSVRVGWRNQYCGLLEMELDGVKFYFIDNEFYFRREDERKSIYGYGDDAERYTFFTDAVLEAISRIDFYPDVIHINDWHTGMLPLILKERYATLEGYKNIKTMYTIHNLQYQGVFDKHVLYDILDLPQKYFDNGDIEYYGSINFMKAGINFADKIITVSPTYANEIQTSFYGEQLDGLLRKESGKLKGILNGIDYDLNDPAKDKDIFVHYDVDSINKKVENKLRLQDILGLKKDSSIPLIGIVSRLVSQKGFDLIAYMMPELMREDLQIVVLGTGEHQYQSMFNYYDSNFSDKVSARITFNASLAQQIYAASDMFLMPSLFEPCGIGQMLAMRYGSLPIVRETGGLRDTVTPYNKFTGEGNGFSFKNYNAHEMFFCLKNAIKVFKDKEKWIKLVENAMKTDNSWKKSAKEYIETYRDICD
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Q18A79
Q6DUW7
IDL3_ARATH
Protein IDA-LIKE 3
Arabidopsis
MSSRSHRSRKYQLTRTIPILVLLLVLLSCCNGARTTNVFNTSSPPKQKDVVSPPHDHVHHQVQDHKSVQFLGSLPRQFPVPTSGPSRKHNEIGLSSTKT
May be involved in floral abscission.
Q6DUW7
Q0VA61
HYOU1_XENTR
Hypoxia up-regulated protein 1
Silurana
MRPLVCVFTMFLLALLSSNTESVAVMSVDMGSEWMKIAIVKPGVPMEIVLNKESRRKTPVAIALKENERLFGDSALGMAVKNPKVTFRYFQDLLGKRADNPHVKAFEARFPEYQLVKDEHRETVLFKLSEELTYSPEELLGMMLNYSRSLAEEFAEQPVKDVVITVPAFFNQAERRAVLQAAQLSDLKVLQLINDNTAVALNYGVFRRKDINATAQNIMFYEMGSRSTICTIVTYQSVKTKDSGMQPQLQIRGVGFDRTLGGIEMDLRLRDHLAKLFNEQKKSKKDVRENQRAMSKLLKEANRVKTILSANNDHMAQIEGLMDDIDFKAKVTRQELEDLCADLFNRVSAPVQHALSSAEMKMEEIDQVILVGGATRVPKVQELLLKVVGKEELGKNINADEAAAMGAVYQAAALSKAFKVKPFIVRDAAIFPIQVEFTREVEEEDHSKSLKHNKRILFQRLAPYPQRKVITFNRYTDNFAFSINYGDLSYLGPDDLKVFGSLNLTTVKLNGVGESFQKRSDYESKGIKAHFNMDESGLLTLDRVEAVFETVVDEKPEQESTLTKLGNTISSLFGGGSSVPETKENATDSVQEEDEVPTEPTKEEEQESADAADKQKDKEKGTTATNEEEEGKKEEEKSEPQEE
Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding.
Q0VA61
A2BVN3
NDHL_PROM5
NDH-L
Prochlorococcus
MESILNNSVITFVAYVGIISIYLFVIPLILFYWMNNRWNVMGKLERLGVYGLVFLFFPGLILFSPFLNLRLRGNNEG
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
A2BVN3
Q3J7Z6
BPT_NITOC
Aspartate/glutamate leucyltransferase
Nitrosococcus
MTSYWNFDFYLSPPQPCSYLPDQTATNLFADPEAAMDIARYSTLVRLGFRRSGRLVYRPRCLHCSACQPARIPVAQFRPNRSQRRAWKFNQDLSACYRPVEFRAEHFDLFRRYLGTRHPQGGMDDSTPEDYLNFIASGWNETSLIEFRDGKEQLLAVAAVDALTDGLSAVYSFFDPNAKKRSLGTYIILWEIGEAKALNLPYVYLGYWIKNSHKMSYKSAFHPLEVYQDKKWSILKET
Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Q3J7Z6
A1T696
NUOK_MYCVP
NDH-1 subunit K
Mycolicibacterium
MSPDNYLYLSALLFTIGAAGVLLRRNAIVMFMCIELMLNAANLAFVTFSRIHGHLDGQVVAFFTMVVAACEVVIGLAIITMIFRTRRSASVDAANLLKH
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 are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
A1T696
Q18KN9
DCD_HALWD
Deoxycytidine triphosphate deaminase
Haloquadratum
MILSDDDILARLETQELVVEPIDDLDMQIQPASIDLRLGEEFLEFQRTNISCIHPNRKEEVSEYVSETIVSEGDEFILHPGDFVLGTTKERVEIPSDLLATVEGRSSLGRLAVVIHATAGVVDPGYCGQITLELSNLGTAPVALTPGMRVSQLVFTELTQPSARPYGAARDSKYQNQTGPQASRIGEDPEFDQTDDTAQHNKENTT
Catalyzes the deamination of dCTP to dUTP.
Q18KN9
A2C4Y2
RL15_PROM1
50S ribosomal protein L15
Prochlorococcus
MTIKLESLQSNKGSRRKKMRKGRGIAAGQGASCGFGMRGQKSRSGRPTRPGFEGGQMPLYRRVPKLKHFPIVNQKNFTVLNVSRLNALKDGTIVNLDLLVKEGILTKPKNPLKILGNGNLEVKLTVQAAAFTASAKKKIEEVGGSCELYN
Binds to the 23S rRNA.
A2C4Y2
Q8XQE8
FUMC_RALSO
Iron-independent fumarase
Ralstonia
MTTRTERDTFGPIEVPADRLWGAQTQRSLQNFDIAGDRMPRELIDALARIKRASAAVNQRLGLLPADKANAVIAAADEVIAGKHPGEFPLVVWQTGSGTQSNMNMNEVLANRASELLGGERGEARLVHPNDDVNRSQSSNDVFPTAMHVAAVTAITRHLLPSLRALRETLARKAIDFDDIIKIGRTHLQDATPLTLGQEFSGYAAQLQHSETHLNAALPHLCELALGGTAVGTGLNAPAGYAEQVAAELAALTGLPFVTSPNKFETMASADGLVHAHGALKTLAASLTKIANDIRWLASGPRSGLGELSIPENEPGSSIMPGKVNPTQSEAMTMLCAQVFGNDVAVNIGGASGNFELNVFRPMIAYNFLHSARLLADGMRSFNDHCAVGIEPNRERIAELVQRSLMLVTALNPHIGYDKSAQIAKKAHKEGTSLREAALALGYVTAEQFDAWVRPEQMVGR
Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Q8XQE8
B5QWI7
ASTB_SALEP
N-succinylarginine dihydrolase
Salmonella
MTAHEVNFDGLVGLTHHYAGLSFGNEASTRHRFQVSNPRLAVKQGLLKMKALADAGFLQAVIPPHERPFIPALRQLGFTGSDEQILDKVARQAPRWLSSVSSASPMWVANAATVCPSADALDGKVHLTVANLNNKFHRALEAPVTEALLRAIFRDENQFSVHSALPQVALLGDEGAANHNRLGGEYGSAGVQLFVYGREEENEIRPARYPARQSREASEAVARLNQVNPQQVIFAQQNPEVIDQGVFHNDVIAVSNRQVLFCHEAAFARQKVLINQLRTRVDGFMAIEVPAEEVSVSDAVATYLFNSQLLSRDDGSMLLVLPRECQDHAGVWRYLNKLVAEDNPISAIQVFDLRESMANGGGPACLRLRVVLTEEERRAVNPAVMMNDALFTALNAWADRYYRDRLTAADLADPLLLREGREALDVLTRLLDLGSVYPFQQTGAADG
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
B5QWI7
P57849
THII_PASMU
tRNA 4-thiouridine synthase
Pasteurella
MKFVIKLFPEIMIKSESVRKRFVKILTGNIRNILTKHDETIAVVRHWDYIEVRSKKEENRPHLIELLGRIPGIHHFLEVDEKPFTTIHDIFEQTLQDIGTSLENKTFCVRVRRKGKHTFNSLDVERYVGGGLNQHIPSAKVQLSKPDVTVRIDIENDNMMLIKARHVGIGGYPIGTQEDVLSLISGGFDSGVSSYMLIRRGSRVHYCFFNLGGAAHEIGVKQMAYHIWQRYSASHKVRFVAINFEGVVGEILEKVDNGQMGVVLKRMMVRAASRIAERFGIQAIVTGEALGQVSSQTLTNLRLIDEASESLVLRPLITHDKEQIIAMAKEIGTDDIAKSMPEFCGVISKNPTVKAIKAKIEQEERHFDFAVLESAVQNAQYLDIRQIAEQTEKEVVAVDTVAVLSAQDVILDIRSPEETDEKPLNMENVQLMPFYKLSSQFANLDQSKNYLLYCERGVMSKLQALYLKEQGFSNVKVFRQ
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
P57849
Q9HGZ2
G6PI_ASPOR
Phosphohexose isomerase
Aspergillus subgen. Circumdati
MPAFSQATDLSAWKELQEHHTAVGRNIVLKEAFEKDPQRFEKFSRTFKNTVDNSDILFDFSKNFLTEETLSLLVKLAKEANVEELRDAMFKGEHINFTEDRAVYHAALRNVSNEPMQVDGKSVVEDVNSVLEHMKEFSEQVRSGEWKGYTDKKIDTIINIGIGGSDLGPVMVTEALKPYGAPGMKLHFVSNIDGTHIAEALKDSNPETTLFLIASKTFTTAETTTNANSAKKWFLETAKDESHIAKHFVALSTNEAEVTKFGIDKKNMFGFESWVGGRYSVWSAIGLSVALYIGYDNFHQFLAGAQAMDKHFREAPLEQNIPAIGGLLSVWYSDFFGAQTHLVAPFDQYLHRFPAYLQQLSMESNGKAITRSGEYVKYTTGPILFGEPATNAQHSFFQLLHQGTKLIPSDFIMAAESHNPVEGGKHQRMLASNFLAQSEALMVGKTPEQVKTEGAPDNLVPHKTFLGNRPTTSILAQKITPSTLGALIAYYEHLTFTEGAVWNINSFDQWGVELGKVLAKKIQQELETSGAGAGHDASTSGLLAAFKQKANLA
In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis.
Q9HGZ2
B1VSR0
NUON1_STRGG
NDH-1 subunit N 1
Streptomyces
MGMSVNSDPAALVPEITLLVSAVTGLLAGAWTPRERQGTIHVLAALATVVGLVATALAARQPDETVFGTYVLDTATHTTRAIVLVAVLALIALSRDTVAGHKRETEFVVLLQLGALGSIALAGAGDLIMLFAAFLLASVPFYALAGWAKQGRATEAALKYYLAGALAGVTTAAGVTILFGVAGATDYEKVADGISRGPAAAAAVGLIAVLAGLAFKAGAVPAHFWVPDIAEGTPPPVAAALTTVPKIGALVAFYRLLDTAIPAAAIDWRLITAVLATAGMTLGNLAAFAQTSALRMLGYSTVSQVGYLLMAVAVAGRTPLAQPALLLYLAAYALTNIAGFAVVATTHEHRIDRYRGLFHRDPLLALALTVALLGLVGTPPTAVFVGKLEIFTAAMDGGLAWLVVIAALNTLASLFYYLRWITPAFRPAEDDSAAVTPPSRWARAVALTTAALTLLLGIGSGIVLNALGASG
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 are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
B1VSR0
Q8R6K8
MNME_CALS4
tRNA modification GTPase MnmE
Caldanaerobacter
MEFDTIAAISTFPGEAGIGIVRISGDEALEIISKIFRPFRKKDIKSVKSHTIHYGHIVDPETGEVYDEVLVTVMRKPNTYTREDVVEINCHGGIVVSSKILELVLKHGARLAEPGEFTKRAFLNGRIDLSQAEAVIDIITSKTMLANRYAQKQLAGVLGQKMKDLKNKIMELLSHLLALIDFPEEDVEELEREEIKRRAKDILNDIEYLIASSESGRIIREGLKTAIIGKPNVGKSSLLNALLKQNRAIVTDIPGTTRDVIEEYMNIKGIPIKLIDTAGIRHTDELVEKIGVEKSKEVLAEADLILFVLDASRDLTKEDYEIFDILSGKNIIFVLNKVDLPKKIDEEELKKLVGNGIIVEVSTVERTGLDKLESEIYNLVFKGKVSATEEEIITNARHREVLINAKKHMESVIEAIEKGYSEDLITIDVNGALNEIGKITGETATEDVINQIFERFCVGK
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Q8R6K8
A1KB30
EFG_AZOSB
Elongation factor G
Azoarcus
MARKTPIERYRNIGISAHIDAGKTTTTERILYYTGVNHKIGEVHDGAATMDWMAQEQERGITITSAATTCFWKGMDLNFPEHRFNIIDTPGHVDFTIEVERSMRVLDGACMVYCAVGGVQPQSETVWRQATKYKVPRLAFVNKMDRSGANFYKVVDQMKMRLKANPVPIVLPIGAEEGFKGVVDLIKMKAIIWDEASQGMKFEYQDIPAELQGDAETWREQMVEAAAEANEDLMNEYLENGDLSEEKIKLGLRTRTIACEIQPMLCGTAFKNKGVQRMLDAVIEFLPSPVDIPPVAGVDDNEKEVTRKADDKEKFAALAFKLMTDPFVGQLTFVRVYSGVLNSGETVLNSVKNKKERIGRILQMHANEREEIKEVLAGDIAACVGLKEVTTGETLCDPSAPIILERMVFPDPVIHVAVEPKTKGDQEKMGIALGRLAAEDPSFRVRTDEESGQTIISGMGELHLEIIVDRMKREFNVEANVGAPQVAYREAIRKAVEQEGKFVKQSGGRGQYGHVWIKLEPNETGKGYEFVDAIKGGVVPREYIPAVDKGLQETLPNGVLAGFPVVDVKVTLFDGSYHDVDSNENAFKMAASMAFKDAMRKANPILLEPMMAVVVETPEDYMGNVMGDLSGRRGIVQGMDDLPGGMKEIKAEVPLAEMFGYATQLRSLTQGRATYSMEFKHYSEAPKSVAEAVISNRK
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
A1KB30
A7ZPL4
CYSZ_ECO24
Sulfate transporter CysZ
Escherichia
MVSSFTSAPRSGFYYFAQGWKLVSQPGIRRFVILPLLVNILLMGGAFWWLFTQLDVWIPTLMSYVPDWLQWLSYLLWPLAVISVLLVFGYFFSTIANWIAAPFNGLLAEQLEARLTGATPPDTGIFGIMKDVPRIMKREWQKFAWYLPRAIVLLIIYFIPGIGQTVAPVLWFLFSAWMLAIQYCDYPFDNHKVPFKEMRTALRTRKITNMQFGALTSLFTMIPLLNLFIMPVAVCGATAMWVDCYRDKHAMWR
High affinity, high specificity proton-dependent sulfate transporter, which mediates sulfate uptake. Provides the sulfur source for the cysteine synthesis pathway.
A7ZPL4
P80368
OMP1_ACTPL
40 kDa major outer membrane protein
Actinobacillus
VTVYDAEGTKVQIDGSLRVEL
Structural rigidity of the outer membrane of elementary bodies and porin forming, permitting diffusion of solutes through the intracellular reticulate body membrane.
P80368
Q6A6T3
RL13_CUTAK
50S ribosomal protein L13
Cutibacterium
MTTYSPKVGEVQRNWYVIDAEDIVLGRLATTAANLLRGKHKPQYAPHIDTGDFVVVVNASKIALTGKKATDSLRYDHSGRPGGLRVTSIGEMLAKNPRRAVERAVWGMMPKNKLSRQQLKKLKVYGGPEHPHAAQNPQPYEITQIAQ
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
Q6A6T3
Q8VEE1
LMCD1_MOUSE
LIM and cysteine-rich domains protein 1
Mus
MAKVAKDLNPGVQKMSLGQQQSARGVACLRCKGMCSGFEPHSWRKICKSCKCSQEEHCLSSDLDDDRKIGRLLMDSKYATLTARVKGGDGIRIYKRNRMIMTNPIATGKDPTFDTITYEWAPPGVTQKLGLQYMELIPKERQPVTGTEGALYRRRQLMHQLPIYDQDPSRCRGLVENELKAMEEFVKHYKSEALGVGEVALPGQGGLPKEENKTQEKPEGTETTAPTTNGSLGDPSKEVEYVCELCKGAAPVDSPVVYADRAGYSKQWHPTCFQCIKCSEPLVDLIYFWKDGAPWCGRHYCESVRPRCSGCDEIIFSEDYQRVEDLAWHRKHFICEGCEQLLSGRAYIVTKGQLLCPTCSKSKRS
Transcriptional cofactor that restricts GATA6 function by inhibiting DNA-binding, resulting in repression of GATA6 transcriptional activation of downstream target genes. Represses GATA6-mediated trans activation of lung- and cardiac tissue-specific promoters. Inhibits DNA-binding by GATA4 and GATA1 to the cTNC promoter. Plays a critical role in the development of cardiac hypertrophy via activation of calcineurin/nuclear factor of activated T-cells signaling pathway.
Q8VEE1
B1JV92
ZAPD_BURCC
Z ring-associated protein D
Burkholderia cepacia complex
MILYEYPFNERIRTLLRLEDLFERFAFFLAQEDPREHHVALTTLFEIAEVTGRADLKSDLMKELERQRQTLAPFRGNPGIEQNALEAVLGEIEQTLANLAQMQGKTGQHLVDNEWLASIRSRAVIPGGTCKFDLPSYYAWQQWPAEQRRQDIAKWILPMLPLRDAAAIVLRLARESGQASKVMAMQGSYQQMLSGRSYQLMQVRVPPELRVIPEASANKYMLWVRFTMQDGDVRPRAVDIDVPFHLTLCNL
Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity.
B1JV92
B9MB93
LIPA_ACIET
Sulfur insertion protein LipA
Diaphorobacter
MSTPDVVREAQSTEAYNPLAKQKAAAKLSRIPIKVEQGEVLKKPEWIRVKAGSPTTRFYEIKNILREHKLHTVCEEASCPNIGECFGRGTATFMIMGDKCTRRCPFCDVGHGRPDPLDKDEPLNLAKTIAALRLKYVVITSVDRDDLRDGGSGHFVECIQRTRELSPSTQIEILTPDFRGRDDRALEILKAAPPDVMNHNLETVPRLYKEARPGSDYQFSLNLLKKFKQLHPGVPTKSGLMVGLGETDEEILEVMRDMRAHGIEMLTIGQYLAPSNSHLPVRRYVHPDTFKMFEEEAYKMGFSHAAVGAMVRSSYHADQQAHAAGV
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
B9MB93
B7NDX8
CYSG_ECOLU
Sirohydrochlorin ferrochelatase
Escherichia
MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAATDDDALNQRVSEAAEAHRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPLHLGQVAKYAGQLRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAITETTEQLINEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHLKTGGELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQLGELAQQMNSPSLIIIGRVVGLRDKLNWFSNH
Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
B7NDX8
Q6CRM2
DSE2_KLULA
Daughter-specific expression protein 2
Kluyveromyces
MQFKKSSIVSFLSLLGSLTKAAAEVRLVTMDGVVYSYQVVTSTIKPATTYVETIYYTTTYVEAVTLTNHAVTSTTRESVVTSTLSSTSLLPETTEESTQEDEQTTDFTSTTDVESTTDVTSTTAETATLEPTTSDETYTTELTPTTSVKTTLENDDSTSVITTKSTSKANTQSISRKTSTLTPTVTSETTESTSAETLSSTDKSTSTSSSSVLEPMVTNTDCQVVYEYTDDDEYYSTVEISGTESVDAATTYTKTRTVYATISS
Involved in pseudohyphal growth, cell wall metabolism and required for the separation of the mother and daughter cells.
Q6CRM2
Q18JG3
SYP_HALWD
Prolyl-tRNA synthetase
Haloquadratum
MSEDQDLGITQSKIHNTGEWYAEVVQKAELANYGPEGMSGFIVTRPRAYGLWERVQSYLDTRFKQTGVQNAYFPLFIPEGYLEREKEIVEGFDPEVAWVEQAGRNELEERLAVRPTSESIIAPYLSQWIRSYRDLPLRVNQWTSVVRWEATETKPFFRTKEFLWQEGHTAHATRADAWAETMLRLNQYESTYEDLLAIPVLQGAKPEHDKFPGADTTTTVEALMPDGKSVQGATSHYLGTEFADAFDITYTDTDETSRVAHTTSWGLSWRALGALIMTHSDNQGLVLPPTVAPEQVVIVPIWQTETKERVLEYAEDVANNLDDAGIRVELDDRDDQNPGFKFNEWELKGVPLRAEIGPDEATEGTVTLIHRPDGESITAERSEIVETVQEQFDAVYAKLYAAAEETLNSNIRIAETRSELLGTIGQHGGYVKTPWCGDEGCETAIKDEIAAEIVMVPISSDEDDEQDTTDENMGVNNDTTVESNEKSLDLTDSTCVVCDNPAFKTAYFAKSY
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
Q18JG3
Q566G2
RNKB_XENLA
Ribonuclease kappa-B
Xenopus
MVSLLCCGPKLAACGIVLSVWGVIMLVLLGVFFNVHSAVLIEDVPFTEADMFEDPNPPAKMYRLYEQVSYNCFIAAAIYIVLGGFSFCQVRLNKRKEYMVR
Endoribonuclease which preferentially cleaves ApU and ApG phosphodiester bonds.
Q566G2
A8F8Y4
DNAA_BACP2
Chromosomal replication initiator protein DnaA
Bacillus
MENILDLWNKALQKIETKLSKPSFETWMKSTKAHSLQGDTLTITAPNEFARDWLESRYLHLIADTIYELTGEELSIKFIIPQNQDEVEAMPKSPIKKMSKEDPVDIPQNMLNPKYTFDTFVIGSGNRFAHAASLAVAEAPAKAYNPLFIYGGVGLGKTHLMHAIGHYVIDHNPSAKVVYLSSEKFTNEFINSIRDNKAVDFRNRYRNVDVLLIDDIQFLAGKEQTQEEFFHTFNTLHEESKQIVISSDRPPKEIPTLEDRLRSRFEWGLITDITPPDLETRIAILRKKAKAEGLDIPNEVMLYIANQIDSNIRELEGALIRVVAYSSLINKDINADLAAEALKDIIPSSKPRVITIKDIQRIVGQQFNIRLEDFKAKKRTKSVAYPRQIAMYLSREMTDSSLPKIGEEFGGRDHTTVIHAHEKISKLMVEDEQLQQHVKEIKEQLK
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
A8F8Y4
A4G4S3
PYRH_HERAR
Uridine monophosphate kinase
Herminiimonas
MTTPAYKRVLLKLSGEALMGDDPYGINRATIERMVADVSEVSRLGVELAIVIGGGNIFRGVAPGAEGMDRATADYMGMLATVMNSLALADAMRQVGITARVMSAIAIEQVVEPYVRPKALQYLEEGKIVVFAAGTGNPFFTTDTAAALRGAEIGAEIVLKATKVDGVYSADPNKDPDATRYSTITFDEAISKHLQVMDATAFALCRDQKLPIKVFSIVKPGALKRVVMGEDEGTLVHV
Catalyzes the reversible phosphorylation of UMP to UDP.
A4G4S3
Q2RWM9
IF1_RHORT
Translation initiation factor IF-1
Rhodospirillum
MAKEELIEMDGVVTDVLPDSRFKVQLDNGHEVMAYSAGKMKKHRIRIMVGDRVDMEMTPYDLTKARITYRHKVGGPPGPVTGGGNRPPPRQPRRR
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-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Q2RWM9
B3DP38
RSMA_BIFLD
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
Bifidobacterium
MNDTIPATGHLLGAADIRRIAADAGISPTKKFGQNFVIDPGTVRRIVREAGVTAANHVMEVGPGLGSLTLAILETGATMTAVEIDPPLAERLPGTVAEFMPEATSRLTVVNRDALTVTPENVPDFSDDASFTLVANLPYNVATPILLTLLERFDNLGSFLVMVQKEVADRLAAKPGSKIYGTPSVKLAWYGTAERVGTIGRNVFWPAPNVDSALVKFTRYQADDPAAPGTANSTDDGTQRELVFRLIDAAFGQRRKTLHAALKTIAPSEAFSIAGIDPTRRGETLTIAEFTALAKAIESCGDGDEAQ
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
B3DP38
Q0IC13
SURE_SYNS3
Nucleoside 5'-monophosphate phosphohydrolase
unclassified Synechococcus
MTPLRILISNDDGVFADGIRTLAAAAAAAGHQVTVVCPDQERSATGHGLTLQTPIRAERADELFEPGIKAWACSGTPADCMKLALFELLPEKPDLVLSGINHGPNLGTDVFCSGTVAAAMEGTLEGLPAMAVSSACFQWREFQAAAHLAIQVAEAALADQWPENLLLNLNVPPCKQEAMGKLSWTRLSIRRYDEQFSPRVDPRGRTYYWLAGEAVEDFESGGDGPRDWPTDVAQIQADAPSLTPIQPELFWRGGLSSLPQLNIDQ
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Q0IC13
Q8CI15
SPHK1_MOUSE
Acetyltransferase SPHK1
Mus
MEPVECPRGLLPRPCRVLVLLNPQGGKGKALQLFQSRVQPFLEEAEITFKLILTERKNHARELVCAEELGHWDALAVMSGDGLMHEVVNGLMERPDWETAIQKPLCSLPGGSGNALAASVNHYAGYEQVTNEDLLINCTLLLCRRRLSPMNLLSLHTASGLRLYSVLSLSWGFVADVDLESEKYRRLGEIRFTVGTFFRLASLRIYQGQLAYLPVGTVASKRPASTLVQKGPVDTHLVPLEEPVPSHWTVVPEQDFVLVLVLLHTHLSSELFAAPMGRCEAGVMHLFYVRAGVSRAALLRLFLAMQKGKHMELDCPYLVHVPVVAFRLEPRSQRGVFSVDGELMVCEAVQGQVHPNYLWMVCGSRDAPSGRDSRRGPPPEEP
Has serine acetyltransferase activity on PTGS2/COX2 in an acetyl-CoA dependent manner. The acetyltransferase activity increases in presence of the kinase substrate, sphingosine. During neuroinflammation, through PTGS2 acetylation, promotes neuronal secretion of specialized preresolving mediators (SPMs), especially 15-R-lipoxin A4, which results in an increase of phagocytic microglia.
Q8CI15
F4KHG8
PR39B_ARATH
Pre-mRNA-processing factor 39b
Arabidopsis
MVTTEVRTAVSDKEPLQRSPELDSSTDFLDNDRLKETFSSGALDFDEWTLLISEIETTSFPDDIEKLCLVYDAFLLEFPLCHGYWRKYAYHKIKLCTLEDAVEVFERAVQAATYSVAVWLDYCAFAVAAYEDPHDVSRLFERGLSFIGKDYSCCTLWDKYIEYLLGQQQWSSLANVYLRTLKYPSKKLDLYYKNFRKIAASLKEKIKCRIDVNGDLSSDPMEEDLVHTRHTDEEISIVVRELMGPSSSSAVSKALHTYLSIGEQFYQDSRQLMEKISCFETQIRRPYFHVKPLDTNQLDNWHAYLSFGETYGDFDWAINLYERCLIPCANYTEFWFRYVDFVESKGGRELANFALARASQTFVKSASVIHLFNARFKEHVGDASAASVALSRCGEELGFGFVENVTKKANMEKRLGNFEAAVTTYREALNKTLIGKENLETTARLYVQFSRLKYVITNSADDAAQILLEGNENVPHCKLLLEELMRLLMMHGGSRQVDLLDPIIDKELSHQADSSDGLSAEDKEEISNLYMEFIDLSGTIHDVRKALGRHIKLFPHSARAKLRGSRPSGNLFRELIQRREKTRERLNQDLLTNKGISSIVDSPPKEKKESSLDSYGTQSKDAVRADYVNTEPNQGCLTSGHLVEGNDNVIERETLCESQSDLSMGLKANEGGKRSHEVSLPIQASPEHGFVTKQAHFSSNSVDTVKSDAIVIQPSGSQSPQSYQSQESLRQTGRNRYHRRDLNQMHRDSKPRSQERPPQMPYSPVGTGREILGQHMAFTHQDNRVALQSSTSQNPQNQFQNSALQMHPVVQTSNAYPQSQIHGQHMIVSPPESQNPQNQCQNSTSQVQTSFAYPQTQIPQNPVQSNYQQEGQMQSHEAYNQMWQQYYYSYYYYQQQQQLMSEQPQPNQNPQPQLDQNLVQLLSKQYQSQAKTQYLQPQQVEQVNTQQQSQEPQNQQQIQFQQQQQQQEWFQQQQQWQQQQYLLYIQQQQLQGEAKGDEQRLSMPQGSTTNSDIQKSQESGAVNEANLSSDTSISSI
Involved in pre-mRNA splicing.
F4KHG8
A4WNM7
MDH_CERS5
Malate dehydrogenase
Cereibacter
MARPKIALIGAGQIGGTLAHLAAIKELGDVVLFDIAEGTPQGKALDIAQSGPSEGFDAVMKGANSYEDIAGADVCIVTAGVPRKPGMSRDDLIGINLKVMKSVGEGIKAHAPNAFVICITNPLDAMVWALQQFSGLPPEKVVGMAGVLDSARFRHFLSVEFNVSMRDVTAFVLGGHGDTMVPLVRYSTVAGIPLPDLVQMGWTSQEKLDQIVQRTRDGGAEIVGLLKTGSAYYAPATSAIEMAEAYLKDQKRLLPCAAWVDGAFGLDGMYVGVPTIIGAGGIEKVVDIKLNADEQAMFDKSVDAVKGLVAACKGIEPSLA
Catalyzes the reversible oxidation of malate to oxaloacetate.
A4WNM7
Q9SHI3
RLP2_ARATH
Receptor-like protein 2
Arabidopsis
MRSKAKGLVRPLITKPVQPLSSHMHLFLLCILFLSALFLTLSEAVCNLQDRESLIWFSGNVSSSVSPLNWNLSIDCCSWEGITCDDSSDSHVTVISLPSRGLSGTLASSVQNIHRLSRLDLSYNRLSGPLPPGFFSTLDQLMILNLSYNSFNGELPLEQAFGNESNRFFSIQTLDLSSNLLEGEILRSSVYLQGTINLISFNVSNNSFTGPIPSFMCRSSPQLSKLDFSYNDFSGHISQELGRCLRLTVLQAGFNNLSGVIPSEIYNLSELEQLFLPANQLTGKIDNNITRLRKLTSLALYSNHLEGEIPMDIGNLSSLRSLQLHINNINGTVPLSLANCTKLVKLNLRVNQLGGGLTELEFSQLQSLKVLDLGNNSFTGALPDKIFSCKSLTAIRFAGNKLTGEISPQVLELESLSFMGLSDNKLTNITGALSILQGCRKLSTLILAKNFYDETVPSKEDFLSPDGFPKLRIFGVGACRLRGEIPAWLINLNKVEVMDLSMNRFVGSIPGWLGTLPDLFYLDLSDNLLTGELPKELFQLRALMSQKITENNYLELPIFLNPNNVTTNQQYNKLYSFPPTIYIRRNNLTGSIPVEVGQLKVLHILELLGNNLSGSIPDELSNLTNLERLDLSNNNLSGSIPWSLTNLNFLSYFNVANNSLEGPIPSEGQFDTFPKANFEGNPLLCGGVLLTSCKPTRAKENDELNRTFLMGIAIGYFLSFVSILVVRAW
Involved in the perception of CLV3 and CLV3-like peptides, that act as extracellular signals regulating meristems maintenance.
Q9SHI3
P00273
DESR_MEGGA
Desulforedoxin
Megalodesulfovibrio
MANEGDVYKCELCGQVVKVLEEGGGTLVCCGEDMVKQ
Nonheme iron protein possibly involved in electron transport.
P00273
Q8UDS3
TYSY_AGRFC
Thymidylate synthase
Agrobacterium tumefaciens complex
MKQYLDLLRHVMETGSDRGDRTGTGTRSVFGYQMRFDLSEGFPVLTTKKLHLRSIIHELLWFLNGDTNIAYLKENGVSIWDEWADENGDLGPVYGAQWRSWPAPDGRHIDQIALLIEALKTNPNSRRHIVSAWNPALVDEMALPPCHCLFQFYVSDGKLSCQLYQRSADIFLGVPFNIASYALLTLMVAQVVGLKPGDFVHTLGDAHIYANHFEQAQLQMTRTPKALPTMRLNPDVKNLFGFKFEDFTLENYEADSSIKAPIAV
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Q8UDS3
Q9Z5J1
NUSA_MYCLE
Transcription termination/antitermination protein NusA
Mycobacterium
MNIDMAALHAIEMDRGISVNELLDTIRSALLTAYRHTQGHQIDARIDIDRKTGVVKVIAREVDDDGNVISEWDDTPEGFGRIAATTARQVMLQRFRDAENERTYGEFSTREGEIVAGVIQRDSRANARGLVVVRMGSETKASEGVIPAAEQVLGESYEHGNRLRCYVVGVTRGAREPLITLSRTHPNLVRKLFSLEVPEIADGSVEIVSVAREAGHRSKIAVASRVPGLNAKGACIGPMGQRVRNVMSELSGEKIDIIDYDEDPARFVANALSPAKVVSVSVIDQTARAARVVVPDFQLSLAIGKEGQNARLAARLTGWRIDIRGDSPPCSAGQSEQNASHGMAHER
Participates in both transcription termination and antitermination.
Q9Z5J1
Q8U0S7
CETZ_PYRFU
Tubulin-like protein CetZ
Pyrococcus
MRAIIIGIGQCGTKIADIFSLVDFEALAINTSRGDLEYLKHIPPDRRILIGESIVGGKGVNANPVLGREAMKRDLPMVMKKISSLVGFEDVDIFFLTFGFGGGTGAGGTPVLAEALKEEYPDSLVVAIGALPLKEEGIRPTINAAITIDKLSKIVDSIIAIDNNKLKESNEDISQAYERINYAIVERIASLLALIDVPGEQTLDASDLKFVLRAMGSFATVGYAKADATKIKSLSRLIIRSFENEGLYLDVNIESALYGLVAIHGPPEALKANEIFEALNELTQRIRGKQIFRGFYPDPREREVEVVTLLSGIYESKSIEEIVITAKKYAQEFLKAKEEGESKKKKLLSGLPDFDDIYPGEADDQS
Involved in cell shape control.
Q8U0S7
Q987X5
UXUA_RHILO
D-mannonate hydro-lyase
Mesorhizobium
MEQCWRWYGPDDPVTLDHVRQAGATGVVSALHHIYDGRAWPEADVLERKRIIEAAGLTWSVVESIPVHNSFKIGAPERERYAGYYRDSIRTLATAGIKTICYNFMPVVDWTRTDLMYRLPTTGYALRFDAVDFAAYDLFVLQRKDGAASYTPARIAEAEKRLKALTSEQVDQIERNLIAGLPATERKYDRDSFREALAEYDGIGPKELRDNLAWFLREIIPVAEEEGVRMCIHPDDPPFSLYGLPRVVSTAQDARFILNAVDSPANGLTFCTGSYGTRADNDIVAMVKEFADRIHFVHLRNITIEEDGSFYEAEHLEGGTDMAHVILALMQEEARRRKEGRADWRIPMRPDHGHLLADDIGKKKINPGYSLIGRLKGLAELRGIMRAVEKFGLA
Catalyzes the dehydration of D-mannonate.
Q987X5
O64479
PME10_ARATH
Pectin methylesterase 10
Arabidopsis
MKGVTIHNFCYSYFKVCLLVMSLAYGSAEWDGSSSQIAKTIIVNPNDARYFKTVQSAIDSIPLQNQDWIRILISNGIYSEKVTIPRGKGYIYMQGGGIEKTIIAYGDHQLTNTSATFTSYPSNIIITGITFKNKYNIASSSSPTKPAVAAMMLGDKYAIIDSSFDGFQDTLYDDYGRHYYKRCVISGGIDFIFGGAQSIFEGCTLKLRVGIYPPNEVYGTITAQGRDSPTDKGGFVFKDCTVMGSGKALLGRAWKSYSRVIFYRSMFSDNILPIGWDAWKAKGQEGHITFVEFGCTGVGADTSKRVPWLTKASEKDVLQFTNLTFIDEEGWLSRLPIKF
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
O64479
B7KDN8
THIC_GLOC7
Thiamine biosynthesis protein ThiC
Gloeothece citriformis
MRAEWIAKRRGQSNVSQMHYARQGVITEEMHYVANRENLPVDLIRDEVARGRMIIPANINHVNLEPMCIGIASQCKVNANIGASPNSSDINEELEKLRLAVKYGADTVMDLSTGGGDLDTIRTAIINDSPVPIGTVPIYQALESVHGRIENLTPDDFLHIIEKHAQQGVDYMTIHAGILMEYLPLVRNRLTGIVSRGGGIIAKWMLHHHKQNPLYTHFDDIIEIFKKYDVSFSLGDSLRPGCLHDASDEAQLSELKTLGQLTRRAWEHDVQVMVEGPGHVPMDQIEFNVKKQMEECSEAPFYVLGPLVTDIAPGYDHITSAIGAAMAGWYGTAMLCYVTPKEHLGLPNAEDVRNGLIAYKIAAHAADVARHRQGARDRDDQLSNARYNFDWNRQFELSLDPDRAKEYHDETLPADIYKTAEFCSMCGPKFCPMQTKVDADALTELEKFLAKDKETVSQS
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
B7KDN8
Q1XDH0
PSBK_NEOYE
Photosystem II reaction center protein K
Neopyropia
MNSALFLAKLPEAYAIFKPIIDILPVIPVFFLLLAFVWQAAIGFR
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Q1XDH0
A4FME7
RL19_SACEN
50S ribosomal protein L19
Saccharopolyspora
MNTLDALDAQSLRSDIPAFRPGDTLKVHVRVIEGSRERNQVFQGVVIRRQGGGVRETFTVRKVSFGVGVERTFPVHSPNIAKVEVATRGDVRRAKLYYLRELRGKAAKIKEKRETAPAS
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
A4FME7
B1XLH8
DER_SYNP2
GTP-binding protein EngA
unclassified Synechococcus
MKLPIIAVIGRPNVGKSTLVNRIAGDQQAIVHDQPGITRDRTYRPGFWQDRNFQIVDTGGIVFDDHEEFLPLIREQAAIALAEAAVALFVVDGQAGLNAADQEIADWLRQQNVPVVLAVNKCESLEQGYTQAAEFWELGMEEPFPISAIHGSGTGDLLDKVIEYLPTITDVEEDTTINVAIIGRPNVGKSSLLNALTGEQRAIVSPISGTTRDAIDTIIERNGQQYRLIDTAGIRRKKNVDYGAEFFSINRAFKAIRRADVVLFVIDVLDGVTEQDLKLAGRIIDEGRAVIIVANKWDAVEKDTYTINQYRKELQARLFFMEWAEMLFISAQTGQRVNKILDLVDQAAESHRRRVSTAVINEVIQEAVSWHSPPTSRQGKQGRIYYGTQVRSQPPTISLFVNDPKRFNDSYRRYIEKQFRQDLGFAGTPIRLVWRGKRVRDAERGTPNRATKV
GTPase that plays an essential role in the late steps of ribosome biogenesis.
B1XLH8
Q6LY39
HDRC1_METMP
CoB--CoM heterodisulfide reductase iron-sulfur subunit C1
Methanococcus
MVLKSSEFNPDFPKQIIESGEWIFGDHASSFQKCYQCGTCTGACPSGRITALRTRKLIRSALAGIDSILSGDDLWMCTTCYECYEKCPREVKITDIIKIIRNIAAEKGYIAEPHRKTSLLVFKTGHAVPVNDEIKKARLAIGLTEIPPTTHKYPEALEIVRDIMEDLNFCKKVGICRETMDLEPLNVQKSEE
Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B).
Q6LY39
P18985
HBB_MICAD
Hemoglobin beta chain
Mico
VHLTGEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMNNPKVKAHGKKVLGAFSDGLTHLDNLKGTFAHLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPVVQAAYQKVVAGVANALAHKYH
Involved in oxygen transport from the lung to the various peripheral tissues.
P18985
Q9NPH9
IL26_HUMAN
Protein AK155
Homo
MLVNFILRCGLLLVTLSLAIAKHKQSSFTKSCYPRGTLSQAVDALYIKAAWLKATIPEDRIKNIRLLKKKTKKQFMKNCQFQEQLLSFFMEDVFGQLQLQGCKKIRFVEDFHSLRQKLSHCISCASSAREMKSITRMKRIFYRIGNKGIYKAISELDILLSWIKKLLESSQ
May play a role in local mechanisms of mucosal immunity and seems to have a pro-inflammatory function. May play a role in inflammatory bowel disease. Activates STAT1 and STAT3, MAPK1/3 (ERK1/2), JUN and AKT. Induces expression of SOCS3, TNF-alpha and IL-8, secretion of IL-8 and IL-10 and surface expression of ICAM1. Decreases proliferation of intestinal epithelial cells. Is inhibited by heparin.
Q9NPH9
Q8EK73
RPOC_SHEON
Transcriptase subunit beta'
Shewanella
MKDLLKFLKQQSKTEEFNGIKIGLASPDLIRSWSFGEVKKPETINYRTFKPEREGLFCARIFGPVKDYECLCGKYKRLKHRGVICEKCGVEVTQTKVRRERMGHIELASPVAHIWFLKSLPSRIGLMLDMTLRDIERVLYFESFVVIEPGMTSLERGQMLTEETYLDALEEYGDEFEAKMGAEAVLELLRAIDLEKEIEQMREELPSINSETRRKKVTKRLKLMEAFHTSGNKPEWMILKVLPVLPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLDLAAPDIIVRNEKRMLQESVDALLDNGRRGRAITGSNKRPLKSLADMIKGKQGRFRQNLLGKRVDYSGRSVITVGPTLRLHQCGLPKKMALELFKPFIYGKLEGRGLATTIKAAKKMVEREVAEVWDVLDEVIREHPVMLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCAAYNADFDGDQMAVHVPLTLEAQLEARALMMSTNNILSPANGEPVITPSQDVVLGLYYTSRERINGRGEGMYFMSVAEVEKAYATGAAELHARVKVRITETIIDENGERSEQRRIVDTTVGRALLSQILPAGLSFDLVNQNMGKKQISKLLNTCYRQLGLKDTVIFADQLMYTGFRYATISGASVGIDDMVIPAEKYTLVADAEAEVLEIQEQFQSGLVTAGERYNKVIDIWASANEKVSKAMMENLSTETVINRDGVEEKQASFNSIYMMADSGARGSAAQIRQLAGMRGLMAKPDGSIIETPIVANFREGLNVLQYFISTHGARKGLADTALKTANSGYLTRRLVDVAQDLVVIEDDCGTHEGLTMKPLIEGGDVVEPLRERVLGRVVAVDVFYPGTEDVLAPRNTLLDEAWCDKLEEHSIDEVIVRSVITCDTDFGVCAACYGRDLARGHIINHGEAIGVVAAQSIGEPGTQLTMRTFHIGGAASRASAENNVQVKNSGSLKLHNAKYVTNTDGKLVIVSRSSELAIIDELGREKERYKVPYGTVLEKLEEASVEAGDIIANWDPHTHPIITEVAGSIKFVDMIDGVTMTRQTDELTGLSSIVILDVGQRGSAGKEMRPMIRLVGADGSDLMIPGTEVPAQYFLPGSAIVNLDDNAQIAVGDALARIPQESSKTRDITGGLPRVADLFEARKPKEPAILAEISGTISFGKETKGKRRLVITPADGGEQYEEMIPKWRNLNVFEGEKVERGEVIADGPEAAHDILRLRGIHNVANYIVNEVQDVYRLQGVKINDKHIEVIIRQMLRKCVITAAGDSEFLEGEQVEVSRVKIANRELVEQGKVPATFERELLGITKASLATESFISAASFQETTRVLTEAAVGGKSDNLRGLKENVIVGRLIPAGTGYAYHKTRNDARAKKDEPVVVNKITASEAEQNLADLLNLAGSQD
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q8EK73
Q9F488
ISIA_FISMU
CP43'
Fischerella
MQTYDNPKVKYDWWAGNARFANLSGLFIGAHVAQAALTTLWAGAFTWFELSRYQSGVPMGEQGLILLPHLATLGFGVGAGGQIVDTYPYFVIGALHIISSAVLGAGALLHTFKGPENLKDATGPAREFHFEWDDANKLGLILGHHLLFLGAGALLLVAKAMFWGGLYDTTIHDVRVVTEPTLNPFIIFGYQTHFASVDNLEDVVGGHIYVGLLLIFGGVWHILVKPLAWAKKLLIFSGEAILSYSLGGIALAGFVAAYFCAVNTLAYPVEFYGPPLEVKFWYLRPYFADTIQLPYGNYTSRAWLANTHFFLAFFFLQGHLWHALRAIGFDFKRVEKALSAVETSS
Functions as an antenna for photosystem I (PSI) under iron-limiting conditions, when phycobilisomes disappear. In the (PSI)3(Isi3)18 complex most of the harvested energy is probably used by PSI; in other PSI-containing supercomplexes a large part of the energy will probably not be used for light harvesting, but rather is dissipated to protect the organism from light damage.
Q9F488
Q9FT25
PDX1_PHAVU
pvPDX1
Phaseolus
MEGEGSRVVALYDGNGAITETKKSPFSVKVGLAQMLRGGVIMDVVNADQARIAEEAGACAVMALERVPADIRAQGGVARMSDPQLIKEIKRAVTIPVMAKARIGHFVEAQILEAIGIDYVDESEVLTLADDANHINKHNFRIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNIIEAVRHVRSVMSDIRVLRNMDDDEVFTFAKSIAAPYDLVMQTKQLGRLPVVHFAAGGVATPADAALMMQLGCDGVFVGSGVFKSGDPAKRARAIVQAVTHYSDPEILAEVSCGLGEAMVGINLSDTNVERFANRSE
Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by PDX2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Also plays an indirect role in resistance to singlet oxygen-generating photosensitizers.
Q9FT25
Q9HWC4
NUSG_PSEAE
Transcription termination/antitermination protein NusG
Pseudomonas
MAKRWYVVHAYSGYEKHVMRSLIERVKLAGMEEEFGEILVPTEEVVEMRNGQKRKSERKFFPGYVLVQMEMNEGTWHLVKDTPRVMGFIGGTADKPAPITDREADAILRRVADSGDKPKPKTLFEPGETVRVIDGPFADFNGVVEEVNYEKSRIQVAVLIFGRSTPVELEFSQVEKV
Participates in transcription elongation, termination and antitermination.
Q9HWC4
A1Z3X3
GET4_ORYLA
Conserved edge expressed protein
Oryzias
MSDPESLRCSSVRNRGGVQRVEGKLRASVERGDYYEAHQMYRTLFFRYMSQAKHAEARELMYRGALLFFSHNQQNSAADLSMLVLEVLEKSDAKVEDEILEHLAKLFSLMDQNSPERAAFVSRALKWSTGGSSKLGHPKLHQLLALTLWKEQNYSESRYHFLHSSDGEGCAQMLVEYWASRGYRNEVDLFVAQAVLQFLCLKNKSSASVVFSTYTEKHPSIQKGPPFVQPLLNFIWFLLLAVDGGKLTVFTVLCEQYQPSLKRDPMYNEYLDRIGQLFFGVPPKQSPSYGGLLGNLLNSLMGSGEDDDGVEEAQEDSSPIELD
As part of a cytosolic protein quality control complex, the bag6/bat3 complex, maintains misfolded and hydrophobic patches-containing proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The bag6/bat3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Similarly, the bag6/bat3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The bag6/bat3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome.
A1Z3X3
B3EJ26
RL19_CHLPB
50S ribosomal protein L19
Chlorobium
MDQFIQLVEASQVRNDLPDIHPGDTVKLQLKVIEGEKERLQAFEGVIISDKGMGTSKTITVRKISNGVGVERIIPLCSPNIESITVLRKGKTRRAKLSYLRKRTGKAALKVKERKVFTPSK
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
B3EJ26
Q5KXX4
PAND_GEOKA
Aspartate 1-decarboxylase alpha chain
Geobacillus thermoleovorans group
MFRTLMNAKIHRARVTEANLDYVGSITIDEDILDAVGIVANEKVQVVNNHNGARFETYVIPGERGSGVFCLNGAAARLVQKGDVIIVISYVLVPEEKIAAHRPKIAIMDENNRIVQLIAEEPAHTVL
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Q5KXX4
O28548
KU_ARCFU
Non-homologous end joining protein Ku
Archaeoglobus
MRATWKGSISFGLVNIPVKVYKATTQKEIQFHLLHSADGGRIRYRKVCEKCGKEVSDGEIVKGYEISKNEYVILTDEDFEKIPLKSTKSIEIRQFFDPAELGLIYYSSFYYISPDKGGEKAYYLLKKAMEETNSMGIGKMTMRGKENLVALRPYDGGIVLAQLHYIDEVRSPLELPGWGAVAEITEEELELAKKLILAMKKPLKLEEFRDEYKEALMQLIEAKLSGREIVVSEGVEEVKSLIDALKASLEAVK
With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD.
O28548
C3PKQ1
RS10_CORA7
30S ribosomal protein S10
Corynebacterium
MAGQKIRIRLKAYDHEAIDASAKKIVETVTRTGARVVGPVPLPTEKNVYAVIRSPHKYKDSREHFEMRTHKRLIDILDPTPKTVDALMRIDLPASVDVNIQ
Involved in the binding of tRNA to the ribosomes.
C3PKQ1
A6QBH4
PNP_SULNB
Polynucleotide phosphorylase
unclassified Sulfurovum
MNEQIIEINLNNLDEKYEFNKIAKQASGAVMYRQGKAVLIAAVAVDEKAVEEDFLPLTVQYMERSYAAAKIPGGFIKRETKPGDFETLTSRIVDRSLRPLFPKGFYYPVTISVMVVSSDSEVDMQVAALHAANAALYVSDISVQRSIAAVRVGKIEDELVLNPTLSQQDESVLDLLVVGSEQDIIMIEMRAIASEKIDDIEMDMIDPMMGGVPLILEHQECNEVDNEALVDAIAFAAKAIEEASAIYEKEFTPVMRTPLGLSLAEEKVDEELYAYIKENYSEAVAKAISHMAKSERSTELKKVRAQIMEALESEGKEADKELVSKVLDRYKTTVVRDMILDKGIRADGRGLDEVRPITIETNILPSVHGSCLFTRGQTQALVTATLGDKKDAQMFELITDKNTQSENFMVHYNFPGYSVGEAKFIGAPGRRELGHGNLAKRALEPVIPINYDGTIRLVSEVLESNGSSSMATICGGALALRAAEVDMVELVAGIAMGLVTDGERVAVLTDIMGLEDHDGDMDFKIAGTRNGITALQMDIKLGGIDLITLKVALEKAAQGKDHILDLMEEAEKKMESSQALPSTEHFSINPQKIADIIGKAGATIRDIIEKFEVSIDLDRDKGGVKLSGHDKEKVAAAKEHIEKIANAPVRKQMQYEVGKTYVGKVKKIVDFGIFVEMPDGFDALLHISKVAKERVNNLNERYHEGDDITVVVMEQKGKKVELATPEYLA
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
A6QBH4
Q07824
TPO1_YEAST
Polyamine transporter 1
Saccharomyces
MSDHSPISNKENHLLPSDSSRSSSSDMHSTGTTGTTGVEPVDFTGEGAKYTTATEGNGGADLAIQRTTTMNSAAESEVNITRRLTKILTGSVNEPDRVEVDYTNCAPMGGDRPYPPSLPSRDLYEVTFDGPNDPLHPFNWPMKKKVLLCLVLCLDSIAIAMCSSIFASAVPQICEIYHVIEVVAILGITLFVLGFAASPVIYAPLSELYGRKGVLVLSAFGFALFQFAVATAENLQTIFICRFFGGFIGAAPMAVVPAAFADMFDTNVRGKAIALFSLGVFVGPILSPVMGSYIAQRTTWRWLEYVVGCFASAVFVAIVLFFEETHHPTILVNKAKQMRKQSNNWGIHAAHEDVELSIKDIVQKTVTRPIIMLFVEPLLLFVTIYNSFVYGILYLLLEAYPLVFVEGYGFTENGELPYIALIIGMMVCAAFIWYMDNDYLKRCRAKGKLVPEARLYAMVIAGTVFPIGILWFCWTGYYPHKIHWMVPTVGGAFIGFGLMGIFLPCLNYIIESYLLLAASAVAANTFMRSAFGACFPLFAGYMFRGMGIGWAGLLLGLFAAAMIPVPLLFLKYGESIRKKSKYAYAA
Cell membrane polyamine/proton antiporter, involved in the detoxification of excess polyamines in the cytoplasm. Catalyzes polyamine uptake at alkaline pH and excretion at acidic pH. Recognizes spermidine, spermine and putrescine, the polyamine analogs methylglyoxal bis(guanylhydrazone) (MGBG) and paraquat, the antimalarial drug quinidine, and cycloheximide. Confers resistance to the non-steroidal anti-inflammatory drug indomethacin.
Q07824
B7M6X7
GLPK_ECO8A
Glycerokinase
Escherichia
MTEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSSTLVEVLAKADISSDQIAAIGITNQRETTILWEKETGKPIYNAIVWQCRRTAEICEHLKRDGLEDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPISGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNYALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERNYRYAGWKKAVKRAMAWEEHDE
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
B7M6X7
Q505H4
VWC2L_MOUSE
Brorin-like
Mus
MALHIHEACILLLVIPGLVTSAAISHEDYPADEGDQASSNDNLIFDDYRGKGCVDDSGFVYKLGERFFPGHSNCPCVCALDGPVCDQPECPKIHPKCTKVEHNGCCPECKEVKNFCEYHGKNYKILEEFKPSPCEWCRCEPSNEVHCVVADCAVPECVNPIYEPEQCCPVCKNGPNCFAGTTIIPAGIEVKVDDCNICHCHNGDWWKPAQCSKRECQGKQTV
May play a role in neurogenesis. May promote matrix mineralization , but has been shown to weakly, but significantly inhibit BMP2 and BMP6 activity in a preosteoblastic cell line .
Q505H4
Q5WFM6
RNC_ALKCK
Ribonuclease III
Alkalihalobacillus
MAQSSKYQRKPRSGERKRSQRRLELTEEQKKQFDDLLVRTGLTFENRKLLIQAFTHSSYVNEQRIFSSSDNERLEFLGDAVLELAVSQYLFKTYKNMSEGDMTKLRASIVCEPSLARFAEELQFGKLVLLGKGEEVTGGRTRPALLADVFEAFIGALYMDQGLEPVFMFLARFMYPKIKEGAFTYKMDFKSQLQEFVQRDNRGQIRYLIVQERGPAHDREFVSDVQLNEETIGTGTGRSKKEAEQLAAKQALLALNQKES
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). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Q5WFM6
A8FHQ0
WHIA_BACP2
Probable cell division protein WhiA
Bacillus
MSFASETKKELTNLDVKDCCTKAELSALIRMNGSLSFSNRKLILDIQTENAAIARRIYTLLKKKYDVTVELLVRKKMRLKKNNVYIVRLVERAKTILEDLKILGEQFVFERNISEELVKKRCCKRSYMRGAFLAGGSVNNPETSSYHLEIFSLYKEHNDALCELMNQFHLNSKTLERKKGYITYMKEAEKITEFLSVVGAHNSLLRFEDVRIVRDMRNSVNRLVNCETANLNKTIGASLRQVENIQFIDEKIGLDALPDKLREIAKLRVDYQEVTLKELGEMVESGKISKSGINHRLRKLDQIAEQLRNGQAVTLK
Involved in cell division and chromosome segregation.
A8FHQ0