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A3MWD6

MNLKPAIFAVVIGTTDVSLIPGITVAGATPELTHYTPALDVEYLLTGRPITLDVVPVTPDGIPTPALVTRAVAFDVPKLVVNAGARVRPRVPYVDLGGEPGGDIRRGPAMSCAAAEELASRGRMLGRELGRLGVVYLGESIPGGTTTAMAILVGLGYNAWGRTSSASPNNPKELKAQVVMDALERAKPPPDPLRVVCELGDPVHPALAAIALGVAEAGGVPVLAGGTQMAAAAAIYKAMGGDLAKLHVVTTRWIVEDKSADFLGLMAEVGVKNVHVATASFGESKYEGLRAYERGAVKEGVGMGGALFYAQSMGRDVLKLVEAEYERVWRYVKRGD

Belongs to the UPF0284 family.

P0DJ33

MKSCLINVSLLILLLLPILGYASVNAESIDGENDFEEERGFGCFRSCWKAGHDDKTCKSMCG

Shows structural homology with WaTx suggesting that it acts as a cell-penetrating peptide (CPP) with defensive purpose that induces pain by specifically activating mammalian sensory neuron TRPA1 channels (By similarity). Has no effect on the voltage-gated potassium channels tested (By similarity). Expressed by the venom gland. Has the structural arrangement of two alpha-helices stabilized by disulfide bonds (CSalpha/alpha 2(S-S)). Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor kappa-KTx family. Kappa-KTx 1 subfamily.

B0Z539

MKTLYSLRRFYPVETLFNGTLALAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGLGAFLLVFKALYFGGVYDTWAPGGGDVRKITNLTLSPSILFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICILGGIWHILTKPFAWARRALVWSGEAYLSYSLAALSVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLSRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLATSHFVLGFFLFVGHLWHAGRARAAAAGFEKGIDRDFEPALSMTPLN

One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids. PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes. Belongs to the PsbB/PsbC family. PsbC subfamily.

Q1C850

MKQKVVSIGDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQQFGVKVITDVHEASQAQPVSEVVDVIQLPAFLARQTDLVEAMARTGAVINVKKPQFVSPGQMGNIVEKFKEAGNDQVILCDRGSNFGYDNLVVDMLGINVMVQATGGHPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPEPNSAKCDGPSALPLDKLEPFLVQMKAIDDLVKSFPALDTSK

D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Belongs to the KdsA family.

Q7VC23

MGEQTTISDSKGLFHKEFPYVIPPVYRKVLDEYLVELNLLSNQSNFKIDTIFSYGLIISFERFTVGYEPDSHISKILESLCNSCNIDIKAIKEYSNNIKKLINEKGIKEIINILTAEIKKSVGGIALSNQSGKDKYYSRLHAIGIYELISNINEDKKEGDDKEIISECVEALGFSKDRVEKDINQYKNSMEKIKEMMELIKLTVEETKRKAKLN

May be involved in photosynthetic membrane biogenesis. Belongs to the THF1 family.

Q67PE4

MKDVQRIALLFDFYGPLLTERQQELIRAYYLEDHSLAEIADADGVSRQAVHELIRRSEAALQEYEQRLGFVAEHQRRLRLLDELQEALDRADLSAARRALAALRAEA

Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. Belongs to the UPF0122 family.

A6W7K7

MRVLAAMSGGVDSAVAAARAVDAGHEVVGVHMALNRSPGTLRTGSRGCCTIEDALDARRAADLLGIPFYVWDLSEDFVEDVVADFVAEYAAGRTPNPCVRCNERIKFAALLDKGIALGFDAVATGHYARVVTGPDGRAELHRAADAAKDQSYVLAVLDADQVAHAMFPLGDAPTKAEVRAEAERRGLPVASKPDSHDICFIPDGDTRGFLADKLGEVPGEVVDESGEVLGTHTGTYGYTVGQRKGLGISRPAADGRPRYVLSIEPVRRTVTVGPAERLSVGALEAVEAVWNADAPVGPVEVHVQVRAHGEPVPAVAELTGPADDPVLRVRLRTPLSGVAPGQTVAVYRGTRVLGSATISGTTPLS

Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein] Belongs to the MnmA/TRMU family.

A3Q987

MEVLAKHRFARTSPQKCRLVADQIRGLPVAKALEILTFSPKKAAVLVKKVLDSAIANAEHNEGADIDELKVGKVFVDEGPTMKRIMPRAKGRADRIIKRTSHITVVVSDR

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). The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. Part of the 50S ribosomal subunit. Belongs to the universal ribosomal protein uL22 family.

Q2SUG2

MKTSMQSKLDQLTTRLAELNDLLSRENVTADLDQYRKLTREHAEIGPVVEHYAQWRQARADELAAQELLADASMRDFAEDELRGARERMSRLAAELQTMLLPKDPNDERNIFVEIRAGTGGDESALFAGDLLRMYLRYAERQRWQVEMMSESPSDLGGYKEVIVRIAGYGAYSRLKFESGGHRVQRVPATETQGRIHTSACTVAVMPEADEIGEVEINPADLRIDTFRASGAGGQHINKTDSAVRVTHIPTGIVVECQDDRSQHKNKDRALKVLAARIKDKQYHEQHAKEAATRKSLIGSGDRSERIRTYNFPQGRMTDHRINLTLYKLEQIMDGDLDELIAALVSEHQAELLASLGDAE

Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. Methylated by PrmC. Methylation increases the termination efficiency of RF1. Belongs to the prokaryotic/mitochondrial release factor family.

A5URA8

MRKTITDIQQMKVRGEPIAMLTAYDATIAALFDAAGVPMLLVGDSLGDNVLGFSSTVPVTIEDMVRHTAAVARGAQSALIVADMPFLTYATLEMAVAAARRLMQEGGAQAVKLEGGQAMVPIVRRLVECGVPVMGHLGYTPQSVHLFGKARVQGRSAAAARRMIEDALALEAAGAFALVLELVPAQLAAAITERLRIPTIGIGAGPHCDGQVQVFTDILGLRDDFKPRHTRRFAELAPLIRSAVAAYVAAVGERSFPTAEHSSRMDEAELREALEGLS

Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate Binds 1 Mg(2+) ion per subunit. Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. Homodecamer; pentamer of dimers. Belongs to the PanB family.

A7ZJ95

MPEGPEIRRAADNLEAAIKGKPLTDVWFAFPQLKTYQSQLIGQHVTHVETRGKALLTHFSNDLTLYSHNQLYGVWRVVDTGEEPQTTRVLRVKLQTADKTILLYSASDIEMLRPEQLTTHPFLQRVGPDVLDPNLTPEVVKERLLSPRFRNRQFAGLLLDQAFLAGLGNYLRVEILWQVGLTGNHKAKDLNAAQLDALAHALLEIPRFSYATRGQVDENKHHGALFRFKVFHRDGELCERCGGIIEKTTLSSRPFYWCPGCQH

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+) Binds 1 zinc ion per subunit. Belongs to the FPG family.

Q5KVY8

MPSPVESFELDHCAVKAPYVRHCGVHKVGSDGVVNKFDIRFCQPNKEAMDPAAIHTLEHLLAYTLRRHAAKYDHFDIIDISPMGCQTGFYLVVSGSPTVDEIIDLLEEAMKDALAATEVPAATERQCGQAKLHDLEAAKQLMRFWLSQEKEELKKVFG

Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5-dihydroxypentane-2,3-dione + L-homocysteine Binds 1 Fe cation per subunit. Homodimer. Belongs to the LuxS family.

Q7VU11

MSAHQARKRFGQHFLTDESVVESIVRAIGPARDDRVVEIGPGLSALTRPLLDRIDHLTAVEIDRDLAARLRRQYPAERLTVVEADALTVDFAQFGQGLRVVGNLPYNISSPLLFHLMGAAEQVRDQHFMLQREVIDRMVAEPGSGDYSRLSVMLQARYRMEKLFDVAPEAFDPPPRVVSAVVRMAPLPADRLRPASDAAFETVVARAFSQRRKMLRRVLDDWAALTPWDELGIAPTARAEEVGVAQFIGLADALLAAGAPGLARP

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. adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.

Q9LQB0

MASPTLALAQSPPPKSPAVSVSQRNPHCWSKLPLDLMQLVFERLAFLDFERAKSVCSSWQFGSKQSKPNNQIPWMILFPTDKNYCLLFNPEDKEKLYKTQHLGDDFAKSIVLATYRSWLLMQPRYEELEDQTLDQEFHLYIKDLLTCERINLPAFESDIFGLSHPILWIDDKTKDYLVIGTINRETMVSFKNGDNSWKKFPELPKSSCTDMCLNMIYKDHKLHYLDYSNLYIYDFFGEFPREAFRISVREFVGYATNPYGYDEFPEVPLKLKLNRYIYNMIVTVRGDVLIVASLHFSMAETWEFIICKMDSSKVNKWEEIVSLGDESILLGLGITVLAKDMEGITCNSIYFTADDFYEDYEENEIFIYNLDTNKVEIPHQFVSSSIPSAHARWFLPTFKRD

Extended N-terminus.

Q6FSD2

MNVYDDVIDPTVVSHSVCGHFTTTDYLELIVIRTDVLSIYKPIRSGRLYLMEEHKLSGRINDVALIPKHSNGSNGNGINLSYLLLSTGVAKLSLLMYNNMTSSIETISLHFYEDKFESATMLDLARNSQLRIEPNGNYAMLFNNDVLAILPFYTGINEDEDEDYINNDKSKINDNSKKSLFKRKKGKTQNNKVTHPSIIINCSELGPQIKNIKDIQFLCGFTKSTIGVLYQPQLAWCGNSQLVPLPTNYAIISLDMKFSIDATTFDKAIISEISQLPSDWHTIAPTLSGSLILGVNEIAFLDNTGVLQSILTLNSYSDKVLPKVRVIDKSSHEVFFNTGSKFALIPSNENERSVENILLFDENGCIFNVDLKSEGRLLTQFNITKLPLGEDVLSQKSNPSSVSIIWADGRLDTYTIFIGFQSGDATMLKLNHLHSAIEVEEPTFMKDYVNKQASAAYNNEDDDDDDDDFNLYSDEENDQVNNKNDRTFGTNESNEPFTAQELMELRNIGPINSMCVGKVSSIEDNVKGLPNPNKQEISIVCTSGYGDGSHLNAILASVQPRVEKALKFISITKIWNLHIKGKDKFLITTDSTQSQSNIYEIDNNFSQHKQGRLRRDATTIHIATIGDNKRIVQVTTNHLYLYDLTFRRFSTIKFDYEVVHVSVMDPYVLITLSRGDIKVFELENRNKKKFVKVPLPEILTEMVITSGLILKSNMCNEFLSGIGKSTIEQLLFTFVTADNQIIFFTKDHNDRIFQLNGIDQLQDSLYISTYQLPDEIIPDPSIKQIMINKLGNNSKDEYLTILTFGGEIYQYKKSRSRHSRFYRNVGRNDHPITGAPDNAYPKGVSGIERIMHYIPNFDGYSVIFVTGNTPYIIMKEDDSLPRIFPFGNIPIVSMSRWGEGSVICIDDIKNARIYSLNQDNIYYGNKLPIRKIKIGSMLQNYKTLNSIVYHERTQLYLVSYTKEISYEAKAEDGSLLIGYKPELPNAKAFKSGVLLINPKSWEVIDELDLPDNSLVNDMKSSFIQIDTRTKRKREYIIVGIGYATMEDVPPTGEFHIYDITEVVPEPGKPNTNFKLKEIFKEDIRGIVSVVNGISGRFLISQSQKIMVRDVQQDNSVIPVAFLDVPVFVTSLKTFGNLIVIGDAMQGIQFVGFDAEPYRMITLGSSITKFEVISVEFLVNNGDIYFLVTDRDSIMHVLKYAPDQPNTLSGQRLVHCSSFNLHSLNNCTMLLPKNDEFPRDQRYSRSFQTITAQVDGSISKIVPVKEETYRRLYFIQQQIIDKEPQLAGLNPRMERQDNKYYHLGHSLRPMLDFNIIKRFKDMSMNRRSHIVQKLGKNSNLEVWRDLIDLEFSLRSLKPTDQN

RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Involved in poly(A) site recognition. May be involved in coupling transcription termination and mRNA 3'-end formation (By similarity). Belongs to the CFT1 family.

Q7V1S1

MSLIDWFAARRKDQFVGKVSQDPEESDGLWVKCSECGQVAYRKDLISNFNVCSNCGHHNRINSDERINIIADKDSFKEFDESLSPTDPLKFKDRRSYSERIKESQQGTGLKDGVITGLCSVNSMPLALAVMDFRFMGGSMGSVVGEKITRIVETATIKNYPILIVCASGGARMQEGMLSLMQMAKISGALKKHRAKNLLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPDNFQTAEYLLEHGFVDVIVNRKELKSTLTKLLKIHGVKELVQTN

Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Binds 1 zinc ion per subunit. Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccD/PCCB family.

O31671

MLERCKLKILKGACGRVKLYIILVVIPAIVISFFVYEKEKDTIAAEHKQEASVLLNLHRNKINYLIGETMARMTSLSIAIDRPVDIKKMQSILEKTFDSEPRFSGLYFLNAKGDVTASTTELKTKVNLADRSFFIKAKETKKTVISDSYSSRITGQPIFTICVPVLDSKRNVTDYLVAAIQIDYLKNLINLLSPDVYIEVVNQDGKMIFASGQASHAEDQKPVSGYLDDISWNMKVYPNPVTIEELSKSLVLPLSCIIVLLNILFILVLYYLLKRQTQLERSENEAQKLELIGTLAASTAHEIRNPLTGISGFIQLLQKKYKGEEDQLYFSIIEQEIKRINQIVSEFLVLGKPTAEKWELNSLQDIIGEIMPIIYSEGNLYNVEVELQYLTEQPLLVKCTKDHIKQVILNVAKNGLESMPEGGKLTISLGALDKKAIIKVVDNGEGISQEMLDHIFLPFVTSKEKGTGLGLVVCKRIVLMYGGSIHIESEVRRGTEVTITLPVSAS

Phosphorylates the sporulation-regulatory protein spo0F and, to a minor extent, is responsible for heterogeneous expression of spo0A during logarithmical growth. Also phosphorylates spo0A under biofilm growth conditions. ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. Oligomerizes, probably forms homodimers; oligomerization is assisted by FloT. Interacts with FloT. Expressed during growth and early stationary phase. Cells lacking this gene sporulate normally in spo0F mutants.

Q97IC4

MENILDYNEAELKQWMDKNGEKTFRAKQFFDWIYNGTFDFKDMKNLPQSTRERLEKNFYIGMPSVVKRLNSKKGDTVKFLFRYNDGNIIECVVMKYDYGNSICISTQVGCRMGCSFCASTIGGRVRDLTSGEILAQILKAQKEIGERISNIVLMGSGEPLDNYDNVIKFIRIVNSEKGLNIGQRHITLSTCGIVPRIYDLMKENLQITLAISLHASDDETRKKIMPIANRYSISEIIDCCKKYSDFTGRRITFEYSLVKDVNDDKESAKKLGELLSGMLCHVNLIPVNTVNETSYEKPESSKIKKFCDTLLKYKIESTIRKEMGADINAACGQLRRNYIEESEGK

Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue. Belongs to the radical SAM superfamily. RlmN family.

B2I1Z1

MAYSYTEKKRIRKNFGKLPQVMDAPYLLSIQVDSYRTFLQDGKSPKNREDIGLQAAFRSVFPIESYSGNAALEFVEYSLGKPEFDVRECILRGSTYAAPMRVKIRLIIKDRETKSIKDVREQEVYMGEIPLMTENGTFVINGTERVIVSQLHRSPGVFFDHDKGKTHSSGKVLYSARIIPYRGSWLDFEFDAKDLVYVRIDRRRKLLATVVLRALGYNNEQILNLFYEKVPVYLDMGSYQIDLVPERLRGEMAQFDITDNEGKVIVEQGKRINARHVRQMEAAGLTKLSVPDEYLYERITAEDITLRDGEVIAANTLLSHEVMVKLAEGGVKQFNILFTNDIDRGSFVADTLRADLTRDREEALVEIYKVMRPGEPPTKEAAENLFNNLFFSSERYDLSPVGRMKFNRRLGRPYEVGTDQKSREVEGILSHEDIIDVLRTLVEIRNGKGEVDDIDHLGNRRVRSVGEMTENQFRVGLVRVERAVKERLSQAETDNLSPQDLINAKPVAAAIKEFFGSSQLSQFMDQNNPLSEITHKRRVSALGPGGLTRERAGFEVRDVHQTHYGRVCPIETPEGPNIGLINSLSVYAKANDFGFLETPYRKVVDGRVTDDVEYLSAIEEVGTVIAQADSAVDKDGNLTEEFVSVRHQGEFVRMPPEKVTHMDVSAQQVVSVAASLIPFLEHDDANRALMGSNMQRQAVPTLRADKPLVGTGMEANVARDSGVCVIANRGGVIEYVDASRIVIRVNEDEMVAGEAGVDIYNLIKYTRSNQNTCINQNVIVNLGDKVARGDILADGPSTDMGELALGQNMRVAFMTWNGYNYEDSILLSERVLQEDRLTSIHIQELSCVARDTKLGAEEITADIPNVGEAALSKLDESGIVYIGAEVTAGDILVGKVTPKGETQLTPEEKLLRAIFGEKAADVKDSSLRVPSGTKGTVIDVQVFTRDGLEKDDRALAIEKAQLDSYRKDLKEEYKIFEEAARERVIRLLKGQESNGGGSTKRGDKLSEDLLSGLELVDLLEIQPADEAIAERLTQIQVFLKEKSAEIDEKFAEKKRKLATGDELTTGVLKVVKVYLAVKRRIQPGDKMAGRHGNKGVVSNILPVEDMPHDANGVPVDIVLNPLGVPSRMNVGQILETHLGMAAKGLGDKIEKMLKEQRTVLELREFLDKIYNKVGGEQEDLDSLTDEEILALAGNLRAGVPLATPVFDGAEESQIKDLLELADISRTGQTVLFDGRTGEQFDRPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVEGRTRIYKNIVDGNHYMDPGMPESFNVLTKEIRSLGINIELKNGD

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription. Belongs to the RNA polymerase beta chain family.

Q73X44

MVTSMLPAGLVASAVVSASSANLGPGFDSIGLALSLIDEITVETTDSGLVVQVEGEGADQVPLGPEHLVVRAVECGLRAVGVRAAGLVVRCRNAIPHSRGLGSSAAAVVGGLAAANGLVAQANCQPLSDAALIQLSSEFEGHPDNAAAAVFGGAIVSWIDRGGQHPRYAAAPLRLHPDIHLYCAIPQERSLTAETRVLLPAQVSHEDARFNVSRAALLVVALTERPDLLMAATEDVLHQPQRAPAMPASAEYLRLLRRHNVAATLSGAGPSLIALTTASALPPEVMEYGAANGFTLAEMTAGEGVRWSPGVTVVG

Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5. Belongs to the GHMP kinase family. Homoserine kinase subfamily.

C0JB93

WIMGHMVNKKYQVDEFADLGANAIEFDVTFDSNYKADYTYHKVPCDCGRTCGRYEVFTEFLSYVKNETTPGHPSFREKLVLLQLDLKMSYLTESQSNEAGKDMAKKFLNYYWNRGSNGGRAYILLSIPSIDNYLFLTGFKQQLKTEGFEQYLDKVGVDFSGNEDLDSIVNVLGRLEDEHVWQSDGITNCWTRGISRLQDAIKRRDEDESRYGIKKVYTWTVDYYPSIRYYLRLGIDGVMTNFPNRVEYILNEEEFPGSLRMATIDDNPWEKYVG

Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine Binds 1 Mg(2+) ion per subunit. Expressed by the venom gland. Belongs to the arthropod phospholipase D family. Class II subfamily. The most common activity assay for dermonecrotic toxins detects enzymatic activity by monitoring choline release from substrate. Liberation of choline from sphingomyelin (SM) or lysophosphatidylcholine (LPC) is commonly assumed to result from substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or lysophosphatidic acid (LPA), respectively, as a second product. However, two studies from Lajoie and colleagues (2013 and 2015) report the observation of exclusive formation of cyclic phosphate products as second products, resulting from intramolecular transphosphatidylation. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation.

O15587

QIKPFRKIQCPIVERLVCCMMQHGKNSGKKLLAMRVVEESFEIIHLLTEKNPIQVLVDAIINASPREDSTRVGTGGNVRGQAVDVSPLRRINHALYLLIMGCRCGAFRNSKSLAECLADEIVNASKSYTGSFAIMKKEDLERVANSNR

Belongs to the universal ribosomal protein uS7 family.

Q9X8I3

MTDPVTLDGEGQIGEFDEKRAENAVRELLIAVGEDPDREGLRETPARVARAYREIFAGLWQEPEDVLTTTFDLGHDEMVLVKDIEVFSTCEHHLVPFRGVAHVGYIPSTSGKITGLSKLARLVDVYARRPQVQERLTTQIADSLMEILEPRGVIVVVECEHMCMSMRGIRKPGAKTLTSAVRGQLRDVATRNEAMSLIMAR

GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+) Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. Toroid-shaped homodecamer, composed of two pentamers of five dimers. Belongs to the GTP cyclohydrolase I family.

B7KH60

MERNTNPNRQPVELNRTSLYLGLLLVAVLGILFSSYFFN

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. This subunit is found at the monomer-monomer interface and is required for correct PSII assembly and/or dimerization. Cyanobacterial PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. Belongs to the PsbL family.

Q13U36

MSYRELIAELAREHAEEFSDALLELGALSVSVEDADADTPDEQPLFGEPGLTPDRTAWQRSRVIALLAPEHEPAVLLTAAANEIGLEAAPSFTVREVEEQDWVRLTQSQFDPIKIGERIWVVPSWHDAPDPEALVLELDPGLAFGTGSHPTTRLCMEWLEQSVQPGQSVLDYGCGSGILAILAKKCGADPVYGIDIDPQAVESARHNSERNRAEVTYGLPDACPTGEFDIVVANILSNPLKLMASMLSSKVKPGGRIALSGILARQADEVAQVYARWIDISVWREHEGWVCLSGTRRESH

Methylates ribosomal protein L11. L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine Belongs to the methyltransferase superfamily. PrmA family.

O24700

MAAQKPVRHSVHVKKGDTVQVIAGKDKGTVGEVLQVFPKTSRVLVKGVNLRTKHVKPRQEGESGQIVVEEASIHSSNVQLYSTTQKVASRVAYTFTEDGRKVRKLKKTGEIID

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. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Part of the 50S ribosomal subunit. Belongs to the universal ribosomal protein uL24 family.

P05034

MTLSINDQNKLDAFWAYCVKNQYFNIGYPESADFDYTNLERFLRFSINNCGDWGEYCNYLLNSFDFEKEVMEYFADLFKIPFEQSWGYVTNGGTEGNMFGCYLGREIFPDGTLYYSKDTHYSVAKIVKLLRIKSQVVESQPNGEIDYDDLMKKIADDKEAHPIIFANIGTTVRGAIDDIAEIQKRLKAAGIKREDYYLHADAALSGMILPFVDDAQPFTFADGIDSIGVSGHKMIGSPIPCGIVVAKKENVDRISVEIDYISAHDKTITGSRNGHTPLMLWEAIRSHSTEEWKRRITRSLDMAQYAVDRMQKAGINAWRNKNSITVVFPCPSERVWREHCLATSGDVAHLITTAHHLDTVQIDKLIDDVIADFNLHAA

H(+) + L-histidine = CO2 + histamine Homotetramer. Belongs to the group II decarboxylase family.

Q67YU7

MDHHQESNPLKEIFSLSSSPFFSTLKIKKHIFVGISLLITFLIFSVIVVDLAGFEPHLCFGFLLSPRTLTKERGNDDVCDYSYGRWVRRRRDVDETSYYGEECRFLDPGFRCLNNGRKDSGFRQWRWQPHGCDLPRFNASDFLERSRNGRIVFVGDSIGRNQWESLLCMLSQAVSNKSEIYEVNGNPISKHKGFLSMRFPEQNLTVEYHRTPFLVVVGRPPENSPVDVKMTVRVDEFNWQSKKWVGSDVLVFNTGHWWNEDKTFIAGCYFQEGGKLNKTMGVMEGFEKSLKTWKSWVLERLDSERSHVFFRSFSPVHYRNGTWNLGGLCDADTEPETDMKKMEPDPIHNNYISQAIQEMRYEHSKVKFLNITYLTEFRKDAHPSRYREPGTPEDAPQDCSHWCLPGVPDTWNEILYAQLLAMNYRTK

May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity). Contains 2 motifs that are conserved in esterases, but it is unlikely that this protein belongs to the catalytically active pectin esterases. Belongs to the PC-esterase family. TBL subfamily.

P82859

MEEFLTVGLWGGEGGDRWSFVVNNGGIIGMEIVHANGIASITFKCGDEYGVLQHSRKFGGTGEGWKTDKISLNWPEEYLTSISGTVADLWQHIIIRSISFKTNKGTEYGPYGVVTGQPFSYSTEGGVIVGFHGRSGTLLDAIGAYVKIPQKKDNTLKMALPVPRGPGPWGGHGGMEWDDGVFPAIRELHLYVGDSVIHAIRVSYQSKDGEPLLSPKHGGEGGEPIDPIKLEVSKEFLIRIAGFYGPVEGSGSFKALRSITFYTNKAKYGPYGDEIGQAFTSSVAPGRVVGFHGRSGAYLDAIGVHMEYF

D-mannose/D-glucose-binding lectin (PubMed:9779592). Binds N-linked high-mannose-type glycans. Has a preference for smaller (Man(2)-Man(6)) high-mannose-type glycans to larger (Man(7)-Man(9)) ones. Recognizes both alpha1-6 extended and alpha1-3 extended monoantennary glycans. The addition of alpha1-2Man to the Man-alpha1-3Man-beta branch results in a significant loss of affinity, but beta1-2GlcNAc has some affinity. Has less affinity for biantennary glycans, and affinity is very weak for the biantennary complex-type N-glycans with bisecting GlcNAc. No affinity is observed for tri- and tetra-antennary glycans (PubMed:18266762). Has mitogenic and hemagglutinating activities (PubMed:9779592). Belongs to the jacalin lectin family.

P59176

MSVSKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLDVEIKDRAFFANPVLAGAVHKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFQADTAVAGLQAAYARDENDEFVKATVIRAEGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVGDKNVKAVAGGKLSDIAPTMLSLMGMEIPQEMTGKPLFIVE

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Binds 2 manganese ions per subunit. Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Monomer. Belongs to the BPG-independent phosphoglycerate mutase family.

A7MLV7

MPVWVDADACPKVIKEVLFRAAERTETPVILVANQPLRVPPSKFIRARQVPAGFDVADNEIVRCCEPGDLVVTADIPLAAEVIAKGAVALNPRGERYSEATIRERLTMRDFMDTLRASGIQTGGPDALSQRDRQQFAAELDKWLSGRKRQA

Belongs to the UPF0178 family.

Q54IJ2

MWAPEEDYKQPLLTNSRVANNGNNNNSNGRGGSSSPSTRLQPEHSSRKCNDILFTILFLLVIGGMAAISGIAYTKGDPSRLVPNAPNIPSIPGFNTNTTSSENPIEQYFVSHLESLVAELKRDKDILIYSVLLAIALGAAWIQLLKSFTRFFIYFTLCVGVALVATLGGLFMALGHKEGSESTMIVGGCIIICTLVLVVVIVYLRKSIDLTCAMFTETCRGVQRSPSVFVIASLVVLFFIGFIAYWTSSFIYLFSIPGSTVNPLNDHTSSEANSTDSEQEQSAFNTKIRNLMYFMIFGFFWASSFISAVFQHCVAGVVSNWYFSRDPTGKSLVGQENAYRSLGRALSTSFGSLAFGSLLIAFIEFMAFMLRVCKNSNATNKLVVMVVSCLQCILGCIESIVRWINKFGYIYVAMHGHSFCTSTKECFDLISRNMFNAVIMDFIGGLVLLLGKILGSAASALFTTALLYGMGKSLNPITIALSAIFAFCIFNLFTHIVGIGTDTIFVCYLEDLETNKDGNLYISPDLHELLQDKCNECKEKEQKNQSKV

Belongs to the CTL (choline transporter-like) family.

Q8VPA4

MHKRTYLNACLVLALAAGASQALAAPGASEMAGDVAVLQASPASTGHARFANPNAAISAAGIHFAAPPARRVARAAPLAPKPGTPLQVGVGLKTATPEIDLTTLEWIDTPDGRHTARFPISAAGAASLRAAIRLETHSGSLPDDVLLHFAGAGKEIFEASGKDLSVNRPYWSPVIEGDTLTVELVLPANLQPGDLRLSVPQVSYFADSLYKAGYRDGFGASGSCEVDAVCATQSGTRAYDNATAAVAKMVFTSSADGGSYICTGTLLNNGNSPKRQLFWSAAHCIEDQATAATLQTIWFYNTTQCYGDASTINQSVTVLTGGANILHRDAKRDTLLLELKRTPPAGVFYQGWSATPIANGSLGHDIHHPRGDAKKYSQGNVSAVGVTYDGHTALTRVDWPSAVVEGGSSGSGLLTVAGDGSYQLRGGLYGGPSYCGAPTSQRNDYFSDFSGVYSQISRYFAP

Lysine-specific endoprotease (PubMed:12419815). Involved in corneal virulence. Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro. Experiments performed in E.coli. Experiments performed in E.coli. Processing of pro-endopeptidase to mature endopeptidase is probably autocatalytic, as mutations in the probable active site residues prevent processing, and purified inactive pro-endopeptidase disappears in the presence of active endopeptidase. Belongs to the peptidase S1 family.

Q9D2T3

MELYFGEYQHVQQEYGVHLRLASGDTPKPRNSQPSKAGSYGVSIRVQGIDGHPYIVLNNTERCLAGTPFPENAPSFPSSVINNLSLHPSNGTVLKENTPEELQLPENPYLQTSPLRGQKQFSLHEGRNGVLERKDGPTKLPHVLNFQRHPELLQPYDPEKNEVNAKKHHPPESPWLRNATEDGTNCKKSRNCFPKSYGSQPNSPTSEDLAKTNMTAIRLCSSVVIEDPQKQTSVCVNVQRCAKEGVGEETLSPRRKSPTAPSPQAYSETKKNRPDVLPFRRQDSAGPILDGARSRRSSSSSTTPTSATSLYKFLLDDQECAIHADSVNRHENRRYIPFLPGTGRDIDTCSIPGVDQLIEKFDQKPGLQRRGRSGKRNRINPDDRKRSRSVDSAFPFGLQGNTEYLTEFSRNLGKSSEHLLRPSQVFPQRSVAQEHRGKHSPSSPPAKLQGGAQGAHPKPPLQNKDGKVLNKGRQESTGACAPSLPAPNKKEEEIKIATATLMLQNRAVAATSDSGAKKISVKTFPSDSSTQATPDLLKGQQELTQQTNEETAKQILYNYLKEGGTDNEDATKRKVNLVFEKIQTLKSRAAGSAQGSNQAPNSPSEGNSLLDQKNKLILEVSELQQQLQLEMKNQQNIKEERERMREDLEELRVRHQSQVEETATLQRRLEESEGELRKSLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSTKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQAFRESVEEATKNVEVLASRSNSSEQSQAEADLREKVLKEENEKLQGRIAELERRAAQLQRQMEDVKGDEAQAKETLRKCESEVQQLEEALVHARKEEKEATCARRALEKELEQAQRELSQVSQEQKELLEKLRDEAEQKEQLRKLKNEMESERWHLDKTIQKLQKEMADIAEASRTSSLELQKQLGEYKEKNRRELAEMQTQLKEKCLEVEKARLAASKMQDELRLKEEELQDYQRAEEEALTKRQLLEQSLKDLEYELEAKSHLKDDRSRLIKQMEDKVSQLEIELEEERTNADLLSERITWSREQMEQMRSELLQEKAAKQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLENEERDRANLQLSNRRLERKVKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMGVNEQLQGQLNSLKKGLRLKTLSSKVLDDSDDDDLSSDAGSLYEAPLSYAFPKDSTIASQI

May be involved in anchoring the apical junctional complex, especially tight junctions, to actin-based cytoskeletons. Homodimer or oligomer (Probable). Interacts with CD2AP and SH3BP1; probably part of a complex at cell junctions (By similarity). Localizes to the apical junction complex composed of tight and adherens junctions. In the liver and kidney, it is also found along non-junctional actin filament bundles in addition to the apical junction. Widely expressed. Highly expressed in the kidney and lung. The head region is responsible for both junction and actin filament-based distribution. Belongs to the cingulin family.

Q8WNQ8

MGGLEPCSRLLLLPLLLAVGGLRPVQAQAQSDCSCSTVSPGVLAGIVLGDLVLTVLIALAVYFLGRLVPRGRGAAEAATRKQRITETESPYQELQGQRSDVYSDLNTQRPYYK

Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors (By similarity). TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation (By similarity). Also has an inhibitory role in some cells (By similarity). Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (By similarity). Also mediates cell activation through association with activating receptors of the CD200R family (By similarity). Required for neutrophil activation mediated by integrin (By similarity). Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (By similarity). Associates with natural killer (NK) cell receptors such as the KLRD1/KLRC2 heterodimer to mediate NK cell activation (By similarity). Associates with TREM1 to mediate activation of neutrophils and monocytes (By similarity). Associates with TREM2 on monocyte-derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (By similarity). Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) produced by TREM2 ectodomain shedding which suppresses the release of pro-inflammatory cytokines (By similarity). In microglia, required with TREM2 for phagocytosis of apoptotic neurons (By similarity). Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (By similarity). Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons (By similarity). Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allosimulatory ability (By similarity). Negatively regulates B cell proliferation (By similarity). Required for CSF1-mediated osteoclast cytoskeletal organization (By similarity). Positively regulates multinucleation during osteoclast development (By similarity). Homodimer; disulfide-linked (By similarity). Homotrimer; disulfide-linked (By similarity). Homotetramer; disulfide-linked (By similarity). Homotrimers and homotetramers form when low levels of partner receptors are available and is competitive with assembly with interacting receptors (By similarity). They may represent alternative oligomerization states or may be intermediates in the receptor assembly process (By similarity). Binding of a metal cation aids in homooligomerization through coordination of the metal ion by the subunits of the oligomer (By similarity). Interacts with TREM1 (By similarity). Interacts with TREM2 (By similarity). Interacts with CLECSF5 (By similarity). Interacts with CD300LB and CD300C2 (By similarity). Interacts with CD300E (By similarity). Interacts (via ITAM domain) with SYK (via SH2 domains); activates SYK mediating neutrophils and macrophages integrin-mediated activation (By similarity). Interacts with KLRC2 (By similarity). Interacts with CD300H (By similarity). Interacts with KLRD1 (By similarity). Following ligand binding by associated receptors, tyrosine phosphorylated in the ITAM domain which leads to activation of additional tyrosine kinases and subsequent cell activation. Belongs to the TYROBP family.

A4QEG5

MIQSTGVTHTDKSAQENPVKYRDNFTPVIITGMSGAGLSTAARVLEDLGWYVAHNIPPQIILELIDMCAREDSPVDKVAVVCDVRSREFRGSLTQVVSELRDKQLDPTVLFLEARDEVLIKRFDNVRRTHPLQGSQTLQVGIERERTVLSPVKEDASVVIDTSDLSVHDLRRAIESSFRTIATRTQHVTIESFGFKHGSPRDADFVVDVRFLPNPFWVPELRPFRGVDKPVSDYVLSQKGAEEFLNNFVDMLKDMLPGYRHEGKNFITIGVGCTGGHHRSVAVSEELAKRIADQTTLDVSVVHRDINRH

Displays ATPase and GTPase activities. Belongs to the RapZ-like family.

B0K9V4

MFKGTTIIAVRKGDKVSVAGDGQITFGENTILKHGAKKIRRLYNGEVIVGFAGSVADALTLSQKFEEKLEQYGGNLKRAAVELAQEWRKDKILRKLEALLIAVDKKDTLLISGTGEVIEPDEDVIGIGSGGNYAMAAALALRYNTDLDTEDIAKKALEIASKICVYTNNNITVETL

Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. ATP-dependent cleavage of peptide bonds with broad specificity. Allosterically activated by HslU binding. A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP. Belongs to the peptidase T1B family. HslV subfamily.

Q9CS07

MAEERDAEGTEALIAELHKKIKDAFEVFDHESNNTVDVREIGTIIRSLGCCPTEGELHDFIAEIEEEEPTGYIRFEKFIPVMTRALVERRYRPAAEDILLRAFEVLDPAKRGFLTKDELVKYMTEEGEPFSQEEMEEMLSAAIDPESNTINYRDYITMMVVDEN

Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Component of the nexin-dynein regulatory complex (N-DRC). Belongs to the DRC8 family.

A5EK88

MTIGLGHYLAVAAMLFTLGILGIFLNRKNIIVILMSVELILLAVNINLVAFSTFLGDIVGQVFALLVLTVAAAEAAIGLAVLVVYFRNRGSIAVEDVNLMKG

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 ubiquinone. 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. a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex. Belongs to the complex I subunit 4L family.

Q3IK45

MELVLGLKYIAVALLIGFGAIGTAVGFGNMGGKFLEACARQPELAPSLQVKMFILAGLIDAVAMIGVGIAMVLLFVL

F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase C chain family.

A5VI29

MKQGIHPDYHPVVFEDSSTGYKFLSGSTATSSETVKWEDGNEYPLIRVEVTSDSHPFYTGKQKFTQADGAVDKFNKKYGLK

Part of the 50S ribosomal subunit. Belongs to the bacterial ribosomal protein bL31 family. Type B subfamily.

A2S4B3

MAGHSKWANIKHKKAAADAKRGKIWTRLIKEIQVAARLGGGDVNSNPRLRLAVDKAADANMPKDNVKRAIDRGVGGADGANYEEIRYEGYGIGGAAIIVDTLTDNRTRTVAEVRHAFSKFGGNMGTDGSVAFMFDHVGQFLFAPGTSEDALMEAALEAGANDVNTNDDGSIEVLCDWQEFSKVKDALEAAGFKAELAEVTMKPQNEVDFTGEDAVKMQKLLDALENLDDVQEVYTNAVVVEE

Belongs to the TACO1 family.

Q4R826

MAAARPILGRVLPGSSILFLCDMQEKFRHNIAYFPQIVSVAARMLRVARLLEVPVLLTEQYPQGLGPTVPELGAEGLQPLTKTCFSMVPALQQELDSRPQLRSVLLCGIEAQACILNTTLDLLDRGLQVHVVVDACSSRSQVDRLVALARMRQSGAFLSTSEGLILQLVGDAAHPQFKEIQKLIKEPAPDSGLLGLFQGQNPLLH

Interacts with CDKN2A. Localizes to the nucleus in the presence of CDKN2A. Belongs to the isochorismatase family.

Q8IR45

MSRGNELVFKAKKTSEKISENIHIFANDPSLAFFRVQEHVRKVTPAIFEKRDEVFQLQNNLQGHCYDMEYGIQALRTIEKSESIFENIQEMIKASIFLKQQLKYEESRKKVKKDSTKSSVYKRFSAHLALDLPDLPDFGGVMRETSQRMENMIGPGTATGRTEAQAATSSNPGELQRSYTTLH

May participate in the coupling of lysosomes to microtubule plus-end-directed kinesin motor. Belongs to the BORCS8 family.

Q99KV6

MKSSVAHMKSSGHNRRETHSSYRRSSSPEDRYTEQERSPRDRGYSDYSRSDYERSRRGYSYDDSMESRSRDREKRRERERDADHRKRSRKSPSPDRSPARGGGQSSPQEEPTWKKKKDELDPLLTRTGGAYIPPAKLRMMQEQITDKSSLAYQRMSWEALKKSINGLINKVNISNISIIIQELLQENIVRGRGLLSRSVLQAQSASPIFTHVYAALVAIINSKFPQIGELILKRLILNFRKGYRRNDKQLCLTASKFVAHLINQNVAHEVLCLEMLTLLLERPTDDSVEVAIGFLKECGLKLTQVSPRGINAIFERLRNILHESEIDKRVQYMIEVMFAVRKDGFKDHPVILEGLDLVEEDDQFTHMLPLEDDYNPEDVLNVFKMDPNFMENEEKYKAIKKEILDEGDSDSNTDQGAGSSEDEEEEDEEEEGEDEEGGQKVTIHDKTEINLVSFRRTIYLAIQSSLDFEECAHKLLKMEFAESQTKELCNMILDCCAQQRTYEKFFGLLAGRFCMLKKEYMESFESIFKEQYDTIHRLETNKLRNVAKMFAHLLYTDSLPWSVLECIKLSEETTTSSSRIFVKIFFQELCEYMGLPKLNARLKDETLQPFFEGLLPRDNPRNTRFAINFFTSIGLGGLTDELREHLKNTPKVIVAQKPEAEQKKPALTSSSSESSSASDSSDSESDSSESSSESSSDASDSSSSSSTQSSTSGITAHSAKGTRKKRQGKARGEEVDKLARGHQALERRREGGREDQRHQEGRTERARSERRRAQNSRDADWRDPLAKHIDDRSHENSHSRVGNGREQGSHREPEDRHGEPKKRRERRDSFSENEKQRSRNQDSDNVRRKDRSKSRERSRRHSGHKGDDARCQNSAERRWEKPGRRPEQSRESKRSQDRRREKSPTTQK

Required for pre-mRNA splicing as component of the spliceosome. Promotes exon-junction complex (EJC) assembly. Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay. Component of the pre-catalytic spliceosome B and the catalytic spliceosome C complexes. Interacts with EIF4A3 and PRPF19 in an RNA-independent manner. Direct interaction with EIF4A3 is mediated by the MIF4G domain. Full interaction with EIF4A3 occurs only when EIF4A3 is not part of the EJC and prevents EIF4A3 binding to RNA. Concentrates around speckles, which are sites of pre-mRNA synthesis and processing, where it colocalizes with EJC core proteins. Belongs to the CWC22 family.

Q7LZC3

VLSASDKSNVKAAFGKIGGQAGDLGGQALERMFITYPQTKTYFPHFDLSHGSAQIKGHGKKVAEALVEAANHIDDIAGALSKLSDLHAQKLRVDPVNFKLLGHCFLVVVAAHFPSLLTPEVHASLDKFVLAVGTVLTAKYR

Involved in oxygen transport from the lung to the various peripheral tissues. Heterotetramer of two alpha chains and two beta chains. Red blood cells. Belongs to the globin family.

O53207

MTKPAADASAVLTAEDTLVLASTATPVEMELIMGWLGQQRARHPDSKFDILKLPPRNAPPAALTALVEQLEPGFASSPQSGEDRSIVPVRVIWLPPADRSRAGKVAALLPGRDPYHPSQRQQRRILRTDPRRARVVAGESAKVSELRQQWRDTTVAEHKRDFAQFVSRRALLALARAEYRILGPQYKSPRLVKPEMLASARFRAGLDRIPGATVEDAGKMLDELSTGWSQVSVDLVSVLGRLASRGFDPEFDYDEYQVAAMRAALEAHPAVLLFSHRSYIDGVVVPVAMQDNRLPPVHMFGGINLSFGLMGPLMRRSGMIFIRRNIGNDPLYKYVLKEYVGYVVEKRFNLSWSIEGTRSRTGKMLPPKLGLMSYVADAYLDGRSDDILLQGVSICFDQLHEITEYAAYARGAEKTPEGLRWLYNFIKAQGERNFGKIYVRFPEAVSMRQYLGAPHGELTQDPAAKRLALQKMSFEVAWRILQATPVTATGLVSALLLTTRGTALTLDQLHHTLQDSLDYLERKQSPVSTSALRLRSREGVRAAADALSNGHPVTRVDSGREPVWYIAPDDEHAAAFYRNSVIHAFLETSIVELALAHAKHAEGDRVAAFWAQAMRLRDLLKFDFYFADSTAFRANIAQEMAWHQDWEDHLGVGGNEIDAMLYAKRPLMSDAMLRVFFEAYEIVADVLRDAPPDIGPEELTELALGLGRQFVAQGRVRSSEPVSTLLFATARQVAVDQELIAPAADLAERRVAFRRELRNILRDFDYVEQIARNQFVACEFKARQGRDRI

an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate. Was identified as a high-confidence drug target. Belongs to the GPAT/DAPAT family.

B4TDG1

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWETLLMRMLSDLPLRLPWQNKSRDIRYIIAHLTETLGEDALPRCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLTESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEVPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYGAISSTANSS

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase] Belongs to the AceK family.

A0A0N7D483

MPKTPNGKLDRKSIAALLLRNAKRDMNGVVNDVEKMTVREGELRLLWERVLPTLGDLRLGPSSDFFMCGGNSMLLMKLQKAIKETTGIRVSTKDLYESSTLRAMTHCVFDRANRADDDAAPIDWAVETSLPASLQTQIQDLATSSPPEAGGHGTNGTEVLLTGATSFLGSHLLRSLLSSPRVKKVHCVAVPADEQATLFSHDTRIVCYSGTLLSPTLGVTPQERRTLEQSVHVIVHAGAHGHCLNRFDSLRAPNLQSLHFLATLALPRCVTILFLSSSRVVLLSGDTAPAPASMRSYPPAVDGKDGYTASKWAGEVFLENLVAHVENVASSASSPSVFWRSSLNVEVHRACTLVSESAPNSDAMNAILRHSLDMRCAPRLERAEGYLDFAPMESIVAKITVHAVEMATAVQQQQQQQQRQSQPPRDDAADGSPTERARGLRIAITLAVSSRPWATLGRIWRGRMVGDPKNWIYKSGL

Polyketide synthase-related protein; part of the gene cluster that mediates the biosynthesis of 10,11-dehydrocurvularin, a prevalent fungal phytotoxin with heat shock response and immune-modulatory activities (PubMed:26493380). The highly reducing polyketide synthase Dhc3 is responsible for biosynthesis up to the tetraketide stage (PubMed:26493380). The non-reducing polyketide synthase Dhc5 then conducts four additional chain extension cycles, producing the unreduced part of the nascent octaketide from C-1 to C-8 in 10,11-dehydrocurvularin (PubMed:26493380). The role of Dhc1 in 10,11-dehydrocurvularin biosynthesis has not been identified yet (PubMed:26493380). Mycotoxin biosynthesis.

P74352

MTKRSNLDSNHIIYRSEELLGAASNRYNITVRVAKRAKENRSEDFDSIDDPNMKPAIRAIIEMSDELTRPEIISDN

Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity). a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) In cyanobacteria the RNAP catalytic core is composed of 2 alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription (By similarity). Belongs to the RNA polymerase subunit omega family.

Q5FKT3

MIYKVLYQKDKIVNPRRETTQTLYMEADNMVEARTMVEDNTPYNIELIQELTGNSLTYEKEHADFKLTKFDKK

A non-essential component of RNA polymerase (RNAP). a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) RNAP is composed of a core of 2 alpha, a beta and a beta' subunit. The core is associated with a delta subunit, and at least one of epsilon or omega. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription. Belongs to the RNA polymerase subunit epsilon family.

Q0IDJ2

MSPNSSEKQSSADVPVAASPQPGPVSQWLNQQGFDHDALEPDHLGVEQIGVEALFLQVITAALKSNGFDYLQCQGGYDEGPGERLVCFYHFVAMAELIDGKRDNLREVRLKVFLSREGEPSLPSIYGLFRGADWQERETFDMFGIHFEGHPHPKRLLMPEDWTGWPLRKDYVQPDFYEMQDAY

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. a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+) a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n H(+)(out) + NADP(+) NDH-1 can be composed of about 15 different subunits; different subcomplexes with different compositions have been identified which probably have different functions. Belongs to the complex I 30 kDa subunit family.

A7MNR4

MRSSAKQEELVKAFKALLKEEKFSSQGEIVQALQDQGFENINQSKVSRMLTKFGAVRTRNAKMEMVYCLPVELGVPTTSSPLKNLVLDIDYNDAVVVIHTSPGAAQLIARLLDSLGKAEGILGTIAGDDTIFTTPARGFTVKDLYEAILVLFEQEL

Regulates arginine biosynthesis genes. Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Belongs to the ArgR family.

Q5U560

MVQSCSAYGCKNRYDKDKPISFHKFPLKRPLLCKKWEAAVRRAEFKPTKYSSICSDHFSADCFKRECNNKLLKDNAVPTIFAHMEIKKKSGKAVKKEQLPAEPEPVPAVPEIDPAIGLLLPPLYTPSHIAVICDHNYTVEDTVHQRRRIQQLEEQVDKLRKKLKIANQKCRRQERSLEKLEREVSEYREAKGSGYVIFPGNYYEVLNENEYKELTPEITYKEIIL

DNA-binding transcription regulator that regulates endothelial cell proliferation and G1/S cell-cycle progression. Specifically binds the 5'-[AT]NTNN[GT]GGCA[AGT]-3' core DNA sequence and acts by modulating expression of pRB-E2F cell-cycle target genes (By similarity). Belongs to the THAP1 family.

B1J5W7

MDFKDYYKILGVEPTADEKAIKAAYRKLARKYHPDVSKERDAEEKFKEANEAYEVLGDAQKRAEFDEIRKYGGQHGRPFQAPPGWENRGGAGGGFEGGDFSDFFSSIFGARGGNPFGGARQQRSAGRRGQDVELELAIFLEETLSKESKQISFQVPQTNAAGQRTGFTTKTLNVKIPAGVSDGERIRLKGQGAPGSAGGANGDLFLTIRMAPHPLFDVEGQDLIITVPLAPWEAALGTKVAVPTLDGKINLTIRPDSQSGQRLRVPGKGLANKQGERGNLYAQLKVVMPPASDASTRQLWTQLSEKAAFNPRTQWSK

DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.

Q58559

MIGDYERFKQLKKKVAEALNISEEELDRMIDKKIEENGGIILKDAALMMIAKEHGVYGEEKNDEEFLISDIEEGQIGVEITGVITDISEIKTFKRRDGSLGKYKRITIADKSGTIRMTLWDDLAELDVKVGDVIKIERARARKWRNNLELSSTSETKIKKLENYEGELPEIKDTYNIGELSPGMTATFEGEVISALPIKEFKRADGSIGKLKSFIVRDETGSIRVTLWDNLTDIDVGRGDYVRVRGYIREGYYGGLECTANYVEILKKGEKIESEEVNIEDLTKYEDGELVSVKGRVIAISNKKSVDLDGEIAKVQDIILDNGTGRVRVSFWRGKTALLENIKEGDLVRITNCRVKTFYDREGNKRTDLVATLETEVIKDENIEAPEYELKYCKIEDIYNRDVDWNDINLIAQVVEDYGVNEIEFEDKVRKVRNLLLEDGTGRIRLSLWDDLAEIEIKEGDIVEILHAYAKERGDYIDLVIGKYGRIIINPEGVEIKTNRKFIADIEDGETVEVRGAVVKILSDTLFLYLCPNCRKRVVEIDGIYNCPICGDVEPEEILRLNFVVDDGTGTLLCRAYDRRVEKMLKMNREELKNLTIEMVEDEILGEEFVLYGNVRVENDELIMVVRRVNDVDVEKEIRILEEME

Probably plays an essential for replication of the chromosome, DNA recombination and repair (By similarity). Binds approximately 20 nucleotides. Monomer. Binds to single-stranded DNA sequences.

Q8WZA6

MMKKNQTMISEFLLLGLPIQPEQQNLFYALFLAVYLTTLLGNLLVIVLIRLDSHLHMPMYLCLSNLSFSDLCFSSVTMPKLLQNMQSQNPSIPFADCLAQMYFHLFYGVLESFLLVVMAYHCYVAICFPLHYTTIMSPKCCLGLLTLSWLLTTAHATLHTLLMARLSFCAENVIPHFFCDTSTLLKLACSNTQVNGWVMFFMGGLILVIPFLLLIMSCARIVSTILRVPSTGGIQKAFSTCGPHLSVVSLFYGTIIGLYLCPLTNHNTVKDTVMAVMYTGVTHMLNPFIYSLRNRDMRGNPGQSLQHKENFFVFKIVIVGILPLLNLVGVVKLIMKYHSKSVA

Odorant receptor. A single nucleotide deletion at position Leu-17 in the gene coding for this protein is responsible for functional diversity thus producing a pseudogene. Belongs to the G-protein coupled receptor 1 family.

Q9VH39

MGQVVSMVARRANRFNVENRAHRVLEREKPTPAPKFDSNLRDMERTLELDPKFVDKLNMKDSSLDGRLKDVYVTSQDRFIKRVQERQAAEAAADNVEQRPLPLERKTPDDFEYGYLEPNRISPGHCTLRQALKFINDHQLDPESWPAKKIANEYKLKEPLVENILHYFKTFNMYIPDQKYKDTMLTQATQPLLRVKSSSEGNP

Belongs to the NDUFAF4 family.

Q748A8

MKEGIHPKYNDVMVKCACGNSFQTRSTKTEISTEICSACHPFFTGKQKLIDTAGRVERFRKKYGM

Binds the 23S rRNA. Binds 1 zinc ion per subunit. Part of the 50S ribosomal subunit. Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.

Q8Y2I3

MHKLVLIRHGESTWNLENRFTGWVDVDLTDTGIAQARQGGRLLREAGFTFDLAYTSVLKRAIRTLWHVQDEMDLMWIPTRTEWRLNERHYGGLSGLNKAETAAQYGDQQVLVWRRSYDTPPPALEAGDERDAYGNPRYAGLPREQVPLTECLKDTVARVLPLWETSIAPDIKSGKRVVIAAHGNSIRALVKYLDNISDDDIVGLNIPNGTPLVYELDANLKPIRHYYLGDQEAIAASLAAVAGQGKAK

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. Homodimer. Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. Extended N-terminus.

A6VIW5

MKHLVTTALAYTNGPLHLGHARSTYIPADIYTRYLRLKGEEVVHVGGTDNHGVPITLTAEREGVKPIDIVDRYHNAIKADLDSLNVSFDTFGRTHSDIHIETAQEFYSKLKENGYIYEKEIEQFYCEKCDMYLADRYVEGICPFCEGEARGDHCEVCGRHLEPTELVNPYCIHCNSKPEIKRTTHYFFKLSAMQDVLKEYIENSPEMPEHVKNMALRWIEELHDWDVSRNIKWGVPIPGCDDQVMYVWIEAPIGYVSFTKQLGGIWEDYWLENTGDSKISHFIGKDITVHHAVFWPGILKGIGGYKMPNAVVSGGYLTLENKKMSTSKNWVVWVKDFIENFSSDYLRYFFMINAPLNRDTDFSWDDFQKRINTELIDIIGNFTHRTLVFTERKFGSTPIVDSNQLIDEDKKLISKCESTLNRVDSLIREYNFKDALMEIILLAKEGNAYFQGMAPWAIKDDERLKEVMYTCSVALKYIIYLLSSFMPEKTALLLEYMNEELDLEVRGNPLKKPKVIFTKVSDEDISRMKENLLAATKKAETKTDEKSKKVKSGEKMDIIDIDYFGNVDLRVGQILEVEEVPRSKKLYKIIADLGDEKRQIVSGLKGAYEAEELVGKKVIIICNLKPAKLCGVESQGMLLAAEDDSIVSLLALDRDLPVGSKIH

Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met) Binds 1 zinc ion per subunit. Homodimer. Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily.

A1VYC2

MSLEMFDKEIFDLTNKELERQCEGLEMIASENFTLPEVMEVMGSILTNKYAEGYPGKRYYGGCEFVDEIETLAIQRCKKLFNCKFANVQPNSGSQANQGVYAALINPGDKILGMDLSHGGHLTHGAKVSSSGKMYESCFYGVELDGRIDYEKVREIAKKEKPKLIVCGASAYARVIDFAKFREIADEIGAYLFADIAHIAGLVVAGEHPSPFPYAHVVSSTTHKTLRGPRGGIIMTNDEEFAKKINSAIFPGIQGGPLMHVIAAKAVGFKFNLSDEWKIYAKQVRTNAQVLANVLMDRKFKLVSDGTDNHLVLMSFLDREFSGKDADLALGNAGITANKNTVPGEIRSPFITSGLRLGTPALTARGFKEKEMEIVSNYIADILDDINNEKLQENIKQELKKLASNFIIYERAMF

Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine One-carbon metabolism; tetrahydrofolate interconversion. Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. Homodimer. Belongs to the SHMT family.

P84549

AIFVDLEPTVIDEVRSLDIERPTYTNLNRFDGAINVDVTEFQTNLVPYPR

Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Belongs to the tubulin family.

Q0P585

MRAEGDGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVSERGNHCEFCFARKEGLSKCGRCKQAFYCNVECQREDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKRDLIQSDIAALHHFYSKHLEFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIHPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLNDPPKAETIRDMVRYARNVIEEFRRAKHYKSPSELLEICELSQEKMSCVFEDSNVYMLHMMYQAMGVCLYMQDWEGALRYGQKIIQPYSKHYPLYSLNVASMWLKLGRLYMGLENKAAGERALKKAIAIMEVAHGKDHPYISEIKQEIESH

Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'. L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-homocysteine L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine Interacts with RNA polymerase II and HELZ. Interacts with SIN3A and HDAC1. Interacts (via MYND-type zinc finger) with EPB41L3. Interacts (via SET domain) with p53/TP53. Interacts with RB1 and HSP90AA1 (By similarity). Belongs to the class V-like SAM-binding methyltransferase superfamily.

Q8F4P5

MSESNELIEQRIQKIEELKKQGINPYPVRFFPDSKSKDIAEKFEKNPTGPETKFKLGGRLHSKRVMGKASFAHLKDNSGIIQLYATKDDLGETQYSIFKSLDLGDIIGLEGYLFKTQKGEITLHVTSVELLAKCIRPLPVVKEKDGVVYDAFADVEQRYRMRYVDLIVNDHVRDTFITRSKIVSEIRSFLTQEGFLEVETPMMQPIAGGAAARPFVTHHNTLDMQLFLRIAPELYLKRLIVGGMDRVFELNRNFRNEGISTKHNPEFTMMEAYMAFGDMSTMLDLTERLITHLAQKICGTLKIQYGKDLIDLSPPWKRTTYVDIIKEYSGIDFSQIISLEEAKKKASELKVDVSKCQTIWKVADEVFSEKAEPNLIQPIFITDYPKELSPLAKSNPDKPGYVERFEPYVAGREIGNAFTELNDPFDQKERFEDQVKQREAGDDEAFMMDEDYIRALEYGMPPTGGLGIGIDRLVMLLTNSHSIRDTILFPLMRPE

ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys) Binds 3 Mg(2+) ions per subunit. Homodimer. Belongs to the class-II aminoacyl-tRNA synthetase family.

B8D7D6

MKKITILGSTGSIGINALSIIQKNPDLFKVIALVANKNFSIMLRQCELFSPDWVAMRDEKSAHILRKKLKHSKINTQVLTGEKDICALAALEETDHVISAIVGMAGLLPTLSAIHAGKTILLANKESLITSGYFFMKALSSSGAKIIPIDSEHNAIFQVLPLEIQKNLGKTTLEKNSIKHLVLTGSGGPFYKFSSSDLSNVTPDQACSHPNWLMGKKISVDSATMMNKGLEYAEARWLFNALESEIKILIHPESIIHSMVQYYDGSLLAQLSAPDIRTSISYAMSWPDRICTEVDYLNFYKINNLTFFEPDFTQFPCLKLAIDAFSQGQASMTVLNAANEIAVSSFLDSKISFTKIYEINMEILMSSCFSEPKCIQDILEIDRKVRILAKNKVSSLIF

Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. Homodimer. Belongs to the DXR family.

Q3B075

MVSPGLDLELSFSQAMQGFGLSPEVARLLWLPLPMLLVLVAAVVGVLVSVWLERKISAAVQQRVGPEYAGALGVLQPLADGLKLLVKEDIIPARADSILFTLGPILVVVPVIVSWLIIPFGQNLLISNVGVGIFLWIAFSSVQPIGLLMSGYASNNKYSLLGGLRAAAQSISYEIPLALAVLAIVMMSNSLSTVDIVNQQTGAGILSWNIWRQPVGFLIFWICALAECERLPFDLPEAEEELVAGYQTEYAGMKFALFYLAGYINLVLSAVLVSVLYLGGWGFPIPVEWLADWLHQPIDAPVVQVITGSVGIMMTILKAYLLVFIAILLRWTTPRVRIDQLLDLGWKFLLPLALVNLLVTAALKLAFPVAFGG

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. a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+) a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n H(+)(out) + NADP(+) NDH-1 is composed of at least 11 different subunits. Belongs to the complex I subunit 1 family.

Q83HH5

MPNAPEVNSVWDELLWRGLVCVSTDQGALKELLDGPPIRFYCGFDPTAPSLHVGNLAQILIMRRLQLAGHRPIALVGGSTGLIGDPRPGGERQLHSHEQVQEWVRALQQQLSRFLDFKGAAAAVLVNNLDWTKSLTALDFLRELGKHFRVNAMLKKDAVAARLSSTEGISYTEFSYQILQSLDFRQLYLDYKCVLQIGGSDQWGNITSGVDLIRKTEGAGVHAFGSPLLTASDGSKFGKTEGNAIWLDADLTSPWSFYQFFLNSDDADIPRLLRVFTFFTRSEIEDLNRSVRENASARLAHRHLAYSVTRLVHGADVADQVLLACSVLFGDGGALGKTQTGLPRIDSDTLNDSSGVTTIKAQDNTYTPYSPEGVRFAGTFPVDPRFLRSILFELPNATVSAHDLITHILQKVGLCRSLSEARRLISQGGIYVNNIKVTCPDALLDSFLDNSMPIRAAILRKGKKHLAAVFY

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr) Homodimer. Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.

B4TK39

MYDNLKSLGITNPEEIDRYSLRQEANNDILKIYFQKDRGEFFAKSVKFKYPRQRKTVVADGIGQGYKEVQEISPNLRYVIDELDQICQRDRSELDLKRKILDDLRHLESVVANKISEIEADLDKLTRK

Belongs to the UPF0325 family.

A5FVK3

MRLAFMGSPGFAVPALRALHAAGHDIVAVYCQPPRPVGRGHRIHKCPVHEAAEALGLTVRTPERLRRDDAERAYFRALDLDAAVVAAYGQILPADMLVAPRRGCINIHASLLPRWRGAAPIHAAILAGDAQTGVTIMQMDEGLDTGATLLAEAVPIGPEDTMVDLLDRLADLGAALVIKVLDGNFPPVPQPEGGVTYAPKLSKADAEIDWSASAAVILRRIRAFRPWPGTETRLDGEALKIIRAEPAAGQGEPGTVLDDRLAIACGDAAIRPTLVQRAGRAAMQAEAFLRGHPVAIGTRLG

Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet) Belongs to the Fmt family.

O58038

MKCKFCSREAYIKIHYPKMYLCEEHFKEYFERKVSRTIERYKLLTKDERILVAVSGGKDSAVTAYVLKKLGYNIECLHINLGISGYSEKSEEYAKKQCKLIGAPLHIVRIKEILGYGIGEVKTRRPPCSYCGLTKRYIMNKFAYDNGFDAIATGHNLDDEASFLLNNILHWNTEYLAKGGPILPQQGKFIKKVKPLYEVTEREVVAYALAVGLEYIVEECPYARGATTLDMKGVLNELEEKRPGTKFNFVRGYLKKKKLFEPEIKEKEIKECKICRMPSSGDICAFCKFWGLKKEINFKVSSTDEEPFGP

Catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T) (PubMed:28655838). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is required for cell growth at high temperatures (By similarity). Can use free sulfide as sulfur source in vitro, which may be also the sulfur source in vivo (PubMed:28655838). 5-methyluridine(54) in tRNA + ATP + hydrogen sulfide = 5-methyl-2-thiouridine(54) in tRNA + AMP + diphosphate Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe with a free coordination site may bind a small ligand, such as exogenous sulfide, thus acting as a sulfur carrier. tRNA modification. Homodimer. In TtuA from T.thermophilus, the sulfur inserted into the nucleoside comes from the C-terminal thiocarboxylate of TtuB, but there is no TtuB ortholog in P.horikoshii. Free sulfide has been shown to be present at relatively high concentrations within thermophilic archaea, and may be the sulfur source in vivo. The thiolation reaction likely consists of two steps: a first activation step by ATP to form an adenylated intermediate of the target base of tRNA, and a second nucleophilic substitution step of the sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S cluster. Belongs to the TtcA family. TtuA subfamily.

Q86648

MSFVPGQENAGGRSSSVNRAGNGILKKTTWADQTERGPNNQNRGRRNQPKQTATTQPNSGSVVPHYSWFSGITQFQKGKEFQFAEGQGVPIANGIPASEQKGYWYRHNRRSFKTPDGQQKQLLPRWYFYYLGTGPHAGASYGDSIEGVFWVANSQADTNTRSDIVERDPSSHEAIPTRFAPGTVLPQGFYVEGSGRSAPASRSGSRSQSRGPNNRARSSSNQRQPASTVKPDMAEEIAALVLAKLGKDAGQPKQVTKQSAKEVRQKILNKPRQKRTPNKQCPVQQCFGKRGPNQNFGGSEMLKLGTSDPQFPILAELAPTVGAFFFGSKLELVKKNSGGADEPTKDVYELQYSGAVRFDSTLPGFETIMKVLNENLNAYQKDGGADVVSPKPQRKGRRQAQEKKDEVDNVSVAKPKSSVQRNVSRELTPEDRSLLAQILDDGVVPDGLEDDSNV

Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Homooligomer. Both monomeric and oligomeric forms interact with RNA. Interacts with protein M. Interacts with NSP3; this interaction serves to tether the genome to the newly translated replicase-transcriptase complex at a very early stage of infection. Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection. Phosphorylated on serine and threonine residues. Belongs to the betacoronavirus nucleocapsid protein family.

F2G271

MRTSQYLLATQKETPADAEVISHQLMLRAGMIRKLASGLYTWLPSGLRVLNKVANIVREEMNKAGAIEVLMPVVQPADLWEESGRWEEYGPELLRVKDRHQRDFVLGPTHEEVITALVRNEISSYKQLPLNLYQVQTKFRDEVRPRFGIMRGREFTMKDAYSFHLEDSCLEETYQKMYDAYCAIFSRMGLDFRAVIADSGSIGGNHSHEFHVLAESGEDAIAFSSDSDYAANVEMAAAVAPEKAVPSGADVETKDAKGKDFNAILKSVDANATNAVKVVLVKGANELNDKGEDVVCDKWVALVLRADHELNDIKAEKIDGVAIPLVEASFEQAKDVLGVSPFFADATNLPVPAYVDASAAALADFTTGAGAGGKVNVNVNWPDGINTVDIRNVVAGDASPDGQGTLDIKRGIEVGHIFQLGRKYSEAMNCGVLSETGKHQTLTMGCYGIGVSRIVAAAIEQNHDKFGIKWPDPIAPFKIALIPMNMHKSHRIKEAAEALYEELVALGIEVLFDDRKERPGVMFNDMELIGIPHSIVIGERNLDNQQVEYKNRRTGEKQLLDLSAAKEFVAAL

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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS. ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro) Homodimer. Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain. Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.

D4GP28

MHYHQLAVSGERRLTASRDSTTYDLTSADADLRTFGDLARVASIARTSVDRLAAELTEDADVVDDAFVDRHATVPVDAEEIWAAGVTYQISEQAREEESSMPDMYFDVYDADRPEVFFKATPSRTVEPGDAIGVRGDSEWDVPEPELGIVLRRGEIVGYTVGNDVSSRSIEGENPLYLPQAKVYDRCCSIGPCVVTPEDVEDPHELEMSMTIERDGEVIYDDATNTSEMVRSCDELVSYFTRHNTVPELAVILTGTSLVPEQPFDLQEGDHVDITIEGIGTLSNSVTTV

Probable 2-keto-3-deoxyxylonate dehydratase involved in the degradation of D-xylose, a major component of hemicelluloses such as xylan. Catalyzes the fourth reaction in the xylose utilization pathway through dehydratation of 2-dehydro-3-deoxy-D-xylonate into alpha-ketoglutarate semialdehyde (2,5-dioxopentanoate). 2-dehydro-3-deoxy-D-arabinonate = 2,5-dioxopentanoate + H2O Carbohydrate metabolism; D-xylose degradation. Transcriptionally up-regulated by both L-arabinose and D-xylose via the pentose-specific regulator XacR. Impairs growth on D-xylose as sole energy and carbon substrate. Belongs to the FAH family.

Q3MI00

MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSSGGTNGTSFSYTFHGDPHAMFAEFFGGRNPFDNFFGQRNGEEGMDIDDPFSGFPMGMGGFTNMNFGRSRPAQEPTRKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKRGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI

Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). Interacts with DNAJC3. Interacts with HSF1 (via transactivation domain); this interaction results in the inhibition of heat shock- and HSF1-induced transcriptional activity during the attenuation and recovery phase period of the heat shock response. Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock.

A3QEG3

MSEETLSKKQITRLNKLQKRLRREVGSAIADYNMIEEGDTVMCCLSGGKDSYAMLDILVNLLQRAPVNFNLVAVNLDQKQPGFPEDILPAYLDSLKVPYHILEKDTYSIVKDKIPEGKTTCSLCSRLRRGTLYGFAQKIGATKIALGHHRDDIIETMFLNMFYAGKLKAMPPKLLSDDGANVVIRPLAYSREKDIAEYAELKAFPIIPCNLCGSQENLKRAAVKEMLKSWDKQFPGRIETIFTAMQNTSPSQGVDRDQFDFVSLKQDPDAPMKGDVAESDLPAFDFLDLANSGHIDLDAAKRSSDLLKIDVVSTYTP

Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. AH2 + ATP + cytidine(32) in tRNA + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = 2-thiocytidine(32) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[cysteine desulfurase] Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS. tRNA modification. Homodimer. The thiolation reaction likely consists of two steps: a first activation step by ATP to form an adenylated intermediate of the target base of tRNA, and a second nucleophilic substitution step of the sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S cluster. Belongs to the TtcA family.

Q58600

MVIMLKFIDLFCGCGGFSRGFVEEGFEPLVAIELNEDAAFSYALNFNGQIYEKIRPGEFKLKELKGYVGIYPFKFPFEEEDIKWLKRLGTLNEKTKKLSPVVINDDIREIHAIEIEKFIKNKKVDVIIGGPPCEGYTGANPKREKNPYDRLYKDETGRLVLEYIRIVGDLQPKIFVMENVPGIKEVRGAIIKEFREIGYEDVYFNTLRAEDYGNPSVRRRVFVSNIEINPEKTQPKTVIEAIGDLMYKGRDVPNHEFAALPARFRKRVHKLGWGDAFIYFKGANRRLGNYIRLHPLKLAETVMGKRFFIHPYEDRLLTPREQARLMSYPDYHLFAGGIRSCYNQIGESVPVALSRAIARVIKENLK

A putative methylase that probably protects DNA from cleavage by the MjaORF1200P endonuclease. a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

A4XQK6

MHQMTLAEIAKGLEAKQFSAEELSRALLARIAQLDPQLNSFITVTEDLAIEQAKAADARRAAGENGALLGAPIAHKDLFCTNGVLTSCGSKILTGFKAPYDATVVEKLKAAGTVTLGKLNMDEFAMGSANESSHYGAVKNPWDTSRVPGGSSGGSAAAVAARLLPAATGTDTGGSIRQPAALTNLTGIKPTYGRVSRWGMIAYASSLDQGGPLARDAFDCALLLGAMAGFDAKDSTSVDQPVDDYLAALAQPLAGLRIGLPKEYFGAGLDARIGEKVMAVVEELKKLGATVKDISLPNMQHAIPAYYVIAPAEASSNLSRFDGVRFGYRCENPVNLEDLYKRSRGEGFGAEVKRRIMVGTYALSAGYYDAYYIKAQQIRRLIKNDFVAAFKDVDVILGPTTPNLAWKLGEKNADPVSAYLEDIYTITANLAGIPGLSMPAGFVDGLPVGVQLLGNYFQEGRLLNVAHQYQQVSDWHKQAPTGF

Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate Heterotrimer of A, B and C subunits. Belongs to the amidase family. GatA subfamily.

Q5P324

MKASELRAKSAGELNQELLELLKAQFSLRMQLATQQLGNTSQLGKVRRDIARVRTLLQEKAVQK

Belongs to the universal ribosomal protein uL29 family.

Q4WID6

MRPFLDDAKRRVDRKLSARRQSLSASRFLPSALPDRLKDNHDAQVDFTAPPGGSGSREGHLQYMQQSIFGMIAAVGSRSDFHARFDESSDSDGETGQRPRKESSVRKGTSVSVNTSSLDPSQRSSSQTDGNSEKDLGTRGRRHRRTISDHKLLRPFMSNSKHEPDPSTGDEMPTVSPPSRPRSATPRAAPILSRMVEAQAQFDLKASSTERSQSSLNETGAKGPRDASVSPLSTRLMDMFGFDKPEKVLVEYACSLLQSMLLQGYMYVTEGHICFYAYLPKKSTVAIKSGYLHKRGRKNPKYSRYWFSLKGDVLSYYADPSNLYFPSGHVDLRYGISASLGDPKEKGREPRDFQVTTDQRTYYFRADSAMSAKEWVKALQKVIFRTHNEGESVKISFPIESIIDIEESPMVDFAETFKIRVIEDDDSYAIDEYFFTFFNSGREAFEFLKILINDQSLKISSQHLSPQPDRSPRSDRTRKSRNRWSLTSGTSRAETQRKRSASTSHMSLAHDIVKSSPATRHQDSSDSILNSFEQATESSAAWQSITDAAESASQILNRSDVFQSPTIYGLDRRPSGRERRGRRNSDETARSPSTRVNVGTGQQIDELDRRTDGNTSGREARDTTSESDQYTQDPTKSFSGAPSLNELVKAGVYPLQRAAGLAEYLRTRSKQMSNLLASESMGYIEKVSGMWTGGRKHYGEAEDVLPDDQDVDPEDKEDGCNYGDRFRAHFALPPTEKLQATYFAYLHRVLPLYGKIYVSQKKLCFRSLIPGTRTKMILPLRDIENVEKEKGFRFGYHGLVIIIRGHEELFFEFRTSDARDDCAVTLHQHLEAVKFMAESGLLAEQEQNESEAAMTEHRMLQEARYYDYGENDLRPLNESSELHPIFDDPRASIVNFKPAESLRITCLTIGSRGDVQPYIALCKGLLAEGHRPKIATHAEFEPWVRKHGIDFAPVEGDPAELMRICVENGMFTYSFLKEASQKFRGWIDDLLSSAWASCQDSDLLIESPSAMAGIHIAEALRIPYFRAFTMPWSRTRAYPHAFAVPEHRMGGAYNYITYVMFDNVFWKAIAGQVNRWRKNELGLKATTLDKMQPNKVPFLYNYSPSVVPPPLDYPDWIRITGYWFLNEGSDWTPPTALSEFIHRAREDGKKIVYIGFGSIVVSDPSALTKTVIESVLKADVRCILSKGWSDRLGDPASAKPEVPLPSEIHQIQAAPHDWLFSHIDAAVHHGGAGTTGASLRAGVPTIIKPFFGDQFFFGSRVEDLGVGICMKKLNVSVFSRALWEATHSERMIIRAQDLGARIRSEDGVATAIQAIYRDLEYAKTLARQRSIASSTPFSPTPSAKTAAEQDADDDVEDSEEWTFVGDDTDVEMSRRLRDRAISDADMLPDRLLANSVPGDSGPGRN

Probable sterol 3-beta-glucosyltransferase that mediates autophagic degradation of peroxisomes (pexophagy) (By similarity). Also required for cytoplasm to vacuole transport (Cvt) and autophagic degradation of mitochondria (mitophagy) and nuclei (nucleophagy) (By similarity). a sterol + UDP-alpha-D-glucose = a sterol 3-beta-D-glucoside + H(+) + UDP The GRAM and PH domains are required for the localization of ATG26 to the preautophagosomal structure (PAS) and are involved in autophagy (By similarity). Belongs to the glycosyltransferase 28 family.

Q9CNX9

MAQEYLDFELPIAELEAKIESLRSVASQDDEINLDDEIARLQKKSAELTKKTFANLDAWQVSKMARHPNRPYTLDYIERIFTEFEELAGDRAFADDKAIVGGLARLDGKPVMVIGHQKGRSVKDKVKRNFGMPAPEGYRKALRLMQMAERFNLPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEKASTAAEVMGLTANRLKELNLIDSIIEEPLGGAHRDFDAMAHNLKQRLLDDLKELEMLDEDNLLHRRYNRLMDYGYC

Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). Belongs to the AccA family.

B7LV66

MQPDLLSRKTAALTLQKFHTLSPLTHCMTNDVVQTFTANTLLALGASPAMVIETEEASQFAAVASALLINVGTLTQARAHAMRAAVVHAKRVKTPWTLDPVAVGSLDYRRHFCTELLSLNPDAIRGNASEIMALAGVSNSGRGVDSTDVVANALPAAVMLAQETGAVVVVTGEVDYVTDGRRTVGVGGGDPLMTKVVGTGCALSAVVAACCALPGDRLLNVASACSWMKQAGERAIVRSQGPGTFVPYFLDALWQMTQEVEA

Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+) Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1. Belongs to the Thz kinase family.

Q60HE9

MGAYAPAAGVSARGCLDAAGPWTISRALRPPLPPLCFFLLLLLAAPCARAGGYETCPTVQPNILNVHLVPHTHDDVGWLKTVDQYFYGIKNDIQHAGVQYILDSVISALLADPTRRFIYVEIAFFSRWWHQQTNAMREVVRDLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGSDGRPRVAWHIDPFGHSREQASLFAQMGFDGFFFGRLDYQDKRVRMQKLEMEQVWRASASLKPPTADLFTGVLPNGYNPPMNLCWDVLCVDQPVVEDPRSPEYNAKELVDYFLNVATAQGRHYRTNHIVMTMGSDFQYENANMWFKNLDKLIRLVNAQQAKGSSVHVLYSTPACYLWELNKANLTWSVKHDDFFPYADGPHQFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGLAANVGPYGSGDSAPLNKAMAVLQHHDAVSGTSRQHVADDYARQLAAGWVSCEVLLSNALARLRGFKDHLTFCRQLNISICPLSQTAARFQVIVYNPLGRKVNWMVRLPVSEGVFVVKDPNGRTVPSDVVIYPSSDSQAHPPELLFSASLPALGFSTYSVAQVPRWKPQARAPQPIPRRSWSPALTIENEHIRATFDPDTGLLMEIMNMNQRLLLPVRQTFFWYNASIGDNESDQASGAYIFRPNQQKPLPVSRWAQIRLVKTPLVQEVHQNFSAWCSQVVRLYPGRRHLELEWSVGPIPVGDTWGKEVISRFDTPLETKGRFYTDSNGREILERRRDYRPTWKLNQTEPVAGNYYPVNTRIYITDGKMQLTVLTDRSQGGSSLRDGSLELMVHRRLLKDDERGVSEPLMENGSGAWVRGRHLVLLDTAQAAAAGHRLLAEQEVLAPQVVLAPGGGAAYNLGAPPRTQFSGLRRELPPSVHLLTLASWGPEMLLLRLEHQFAVGEDSGRNLSAPVTLNLRDLFSTFTITRLQETTLVANQLREAASRLKWTTNTGPTPHQTPYQLDPANITLEPMEIRTFLASVQWKEVDG

Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides. Binds 1 zinc ion per subunit. Belongs to the glycosyl hydrolase 38 family.

A0A067SC43

MSSVTWAPGNYPSTRRSDHVDTYQSASKGEVPVPDPYQWLEESTDEVDKWTTAQADLAQSYLDQNADIQKLAEKFRASRNYAKFSAPTLLDDGHWYWFYNRGLQSQSVLYRSKEPALPDFSKGDDNVGDVFFDPNVLAADGSAGMVLCKFSPDGKFFAYAVSHLGGDYSTIYVRSTSSPLSQASVAQGVDGRLSDEVKWFKFSTIIWTKDSKGFLYQRYPARERHEGTRSDRNAMMCYHKVGTTQEEDIIVYQDNEHPEWIYGADTSEDGKYLYLYQFKDTSKKNLLWVAELDEDGVKSGIHWRKVVNEYAADYNIITNHGSLVYIKTNLNAPQYKVITIDLSKDEPEIRDFIPEEKDAKLAQVNCANEEYFVAIYKRNVKDEIYLYSKAGVQLTRLAPDFVGAASIANRQKQTHFFLTLSGFNTPGTIARYDFTAPETQRFSILRTTKVNELDPDDFESTQVWYESKDGTKIPMFIVRHKSTKFDGTAAAIQYGYGGFATSADPFFSPIILTFLQTYGAIFAVPSIRGGGEFGEEWHKGGRRETKVNTFDDFIAAAQFLVKNKYAAPGKVAINGASNGGLLVMGSIVRAPEGTFGAAVPEGGVADLLKFHKFTGGQAWISEYGNPSIPEEFDYIYPLSPVHNVRTDKVMPATLITVNIGDGRVVPMHSFKFIATLQHNVPQNPHPLLIKIDKSWLGHGMGKPTDKNVKDAADKWGFIARALGLELKTVE

Dual function macrocyclase-peptidase involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles (PubMed:22202811, PubMed:28866879, PubMed:29051530). Cleaves peptide bonds on the C-terminal side of prolyl residues (PubMed:29051530). The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate (PubMed:29051530). Conformational trapping of the 25 amino-acid peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (PubMed:29051530). The enzyme rebinds the 25 amino-acid peptide in a different conformation and catalyzes macrocyclization of the N-terminal eight residues (PubMed:28866879, PubMed:29051530). Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides. Monomer. Belongs to the peptidase S9A family. More to it - Issue 202 of April 2018

Q59571

MTATVLLEVPFSARGDRIPDAVAELRTREPIRKVRTITGAEAWLVSSYALCTQVLEDRRFSMKETAAAGAPRLNALTVPPEVVNNMGNIADAGLRKAVMKAITPKAPGLEQFLRDTANSLLDNLITEGAPADLRNDFADPLATALHCKVLGIPQEDGPKLFRSLSIAFMSSADPIPAAKINWDRDIEYMAGILENPNITTGLMGELSRLRKDPAYSHVSDELFATIGVTFFGAGVISTGSFLTTALISLIQRPQLRNLLHEKPELIPAGVEELLRINLSFADGLPRLATADIQVGDVLVRKGELVLVLLEGANFDPEHFPNPGSIELDRPNPTSHLAFGRGQHFCPGSALGRRHAQIGIEALLKKMPGVDLAVPIDQLVWRTRFQRRIPERLPVLW

Catalyzes C-C bond formation between the carbons ortho to the phenolic hydroxyl of cyclo(L-tyr-L-tyr) (cYY) producing mycocyclosin. Can also use cyclo(L-Tyr-L-Phe) (cYF), cyclo(L-Tyr-L-Trp) (cYW) and cyclo(L-Tyr-L-3,4-dihydroxyphenylalanine) (cY-DOPA) as substrate. cyclo(L-tyrosyl-L-tyrosyl) + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 2 H2O + mycoclysin + 2 oxidized [2Fe-2S]-[ferredoxin] Inhibited by clotrimazole, econazole, ketoconazole, and miconazole. Was identified as a high-confidence drug target. Belongs to the cytochrome P450 family.

Q2W0H2

MRTMSLNIGTIHFVGIGGIGMSGIAEILHNLGYSVQGTDIADNYNVERLRKMGIRVHIGHAAEALGDARVVVVSSAVKADNPEVQAARAKLVPVVRRAEMLAELMRLKSAIAIGGTHGKTTTTSLIAALLDTARLDPTVINGGIINAYGTNARLGASEWMVVEADESDGSFIKLPSTAVVVTNIDPEHMDHYGTVERLHEAFRTFVENIPFYGFAAMCIDHPEVQALVARVPDRKLVTYGFNHQALVRVEKLSMDITGARYDVVITDRVTGATRTIADIHLPMYGEHNVLNSLAAIAVANELGLPNDVVKTALGGFKGVKRRFTRTGEAKGVTVIDDYGHHPVEIAAVLKAARSACQGNVIAVVQPHRYSRLSSLFAEFCTCFNDADMVIVADVYAAGEKPMEGFDKAALVKGLQEHGHRRVMALADSKALAPLVNSLAGPGDMVVCLGAGNITSWAHALPADLAALPDPSPGGAE

Cell wall formation. ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the MurCDEF family.

Q4R4X4

MTTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLTEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE

Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. Homomer assembled from elementary dimers (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Interacts with BCAS3 (By similarity). Interacts with LGSN (By similarity). Interacts with SYNM (By similarity). Interacts (via rod region) with PLEC (via CH 1 domain) (By similarity). Interacts with STK33 (By similarity). Interacts with LARP6 (By similarity). Interacts with RAB8B (By similarity). Interacts with TOR1A; the interaction associates TOR1A with the cytoskeleton. Interacts with TOR1AIP1 (By similarity). Interacts with TOR1AIP1 (By similarity). Interacts with DIAPH1 (By similarity). Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament (By similarity). Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of VIM (By similarity). Interacts with NOD2 (By similarity). Interacts (via head region) with CORO1C (By similarity). Interacts with HDGF (By similarity). Interacts with PRKCE (via phorbol-ester/DAG-type 2 domain) (By similarity). Interacts with BFSP2 (By similarity). Interacts with PPL (By similarity). The central alpha-helical coiled-coil IF rod domain mediates elementary homodimerization. The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex. One of the most prominent phosphoproteins in various cells of mesenchymal origin. Phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized. Phosphorylation by PKN1 inhibits the formation of filaments. Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33. Phosphorylated on tyrosine residues by SRMS. S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex. Belongs to the intermediate filament family.

Q5WYW5

MAIISSLANQLLIAMPSLKDPNFERSVVYLCEHNEQGSVGLIINRPLQFPLSIVFEQLQIEPIRVEKNGLPLLFGGPVQPERGFVIHKQMGGWRSSLFLQDEVTVTTSNDIIRAIAYDEGPKDVLITLGYAAWTEQQLEREIMSNTWLVCPYKSEILYEVPFEERWEYAGLTLGIKMNQLSSDAGHA

Belongs to the UPF0301 (AlgH) family.

Q1JE48

MIQQETRLKVADNSGAREILTIKVLGGSGRKFANIGDVIVASVKQATPGGAVKKGDVVKAVIVRTKTGARRPDGSYIKFDDNAAVIIRDDKTPRGTRIFGPVARELREGGYMKIVSLAPEVL

Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and together make contacts with the 16S rRNA in bridges B5 and B8. Belongs to the universal ribosomal protein uL14 family.

Q07Y78

MKVSLPAFENARVLVIGDVMLDRYWVGPTGRISPEAPVPVVKINQIEDRPGGAANVALNIATLGGHVQLAGIVGQDETAQALTQGVKVFGVEPQWLTVADKPTITKLRVLSRNQQLIRLDFEEQFDKATSQALFAQSEAILDNVDVLVLSDYAKGAIDEPKDFIAKARAKGVKVLVDPKGHDFARYHGASLITPNMSEFEAVVGTVTSEDDLIEKAQKLIKLHDFEAILVTRSEKGMTLVSQNQPELHIPTVAREVHDVTGAGDTVISALATSIAAGASLAQACAIANTAAGVVVGKLGTSTVSRIELIQALALNHGESGFGVMTEDQLAYAMDQARLRGERIVMTNGCFDILHAGHVSYLQQAKALGDRLIVAVNDDSSVTRLKGPGRPVNPVDRRMAVLAGLASVDWVVPFTEDTPQRIITRLLPDSLVKGGDYKVEDIAGGAEVIAAGGKVEVLGFEDGVSTTAIIQNIMSQK

Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate. Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose. ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+) ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) = ADP-D-glycero-beta-D-manno-heptose + diphosphate Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4. Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4. Homodimer. In the N-terminal section; belongs to the carbohydrate kinase PfkB family. In the C-terminal section; belongs to the cytidylyltransferase family.

A5A8K9

MTTVLQRRESASAWERFCSFITSTNNRLYIGWFGVLMIPTLLTAVTCFVIAFIGAPPVDIDGIREPVAGSLLYGNNIITGAVVPSSNAIGLHLYPIWEAASLDEWLYNGGPYQLIIFHYMIGCICYLGRQWEYSYRLGMRPWICVAYSAPLAATYSVFLIYPLGQGSFSDGMPLGISGTFNFMFVFQAEHNILMHPFHMFGVAGVLGGSLFAAMHGSLVSSTLVRETTEGESANYGYKFGQEEETYNIVAAHGYFGRLIFQYASFSNSRSLHFFLGAWPVVCIWLTAMGISTMAFNLNGFNFNHSIVDSQGNVVNTWADVLNRANLGFEVMHERNAHNFPLDLAAGESAPVALTAPVING

Photosystem II (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. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. 2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2 The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids. Cyanobacterial PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z. C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth. Cyanobacteria usually contain more than 2 copies of the psbA gene. 2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water. Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer. Belongs to the reaction center PufL/M/PsbA/D family.

Q8EH70

MNNIIKMLNDEQMKQDVPAFGAGDTVVVQVRVKEGDKERLQAFEGVVIAKRNRGLHSAFTVRKISNGEGVERAFQTHSPLIASIEVKRRGRVRRAKLYYLRDRSGKSARIREKLATK

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. Belongs to the bacterial ribosomal protein bL19 family.

Q0AYK4

MSVVTMKQLLEAGVHFGHQTRRWNPKMATYIYMERNGIYIIDLQQTVKKFDAAYEFVKSVAAAGKGVLFVGTKKQAQETIREEASRCGMYFVNQRWLGGMLTNYKTIKRRVLRLKELEKQEAEGAFEVLSKKEVARLLNERERLERFLGGIKEMDKLPGAVFVVDPRKERIAVAEARKLNIPVVAIVDTNCDPDEIDYVIPGNDDAIRAVKLISSRIADAVLEGKQGEQITT

Belongs to the universal ribosomal protein uS2 family.

Q10ZX6

MINWLVLNAVILIVAYLLGATPSGYWIGSWFYGVDIREQGSGSTGATNVLRTLGNVPALVVLVIDIFKGALAIALVRYIYSLVFAQNLTIIAGVTDIDTAKEWMVIIAGLIAIVGHTKSIWIGFKGGKSVASSLGILLAISWVVGLGTLSVFIVVLTISRIVSLSSIIAAISVSGLMFFTGQPLPYQIFAITGGIYVIWRHISNIERLLACKEPRIGQKLSTEQKMNK

Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate Lipid metabolism; phospholipid metabolism. Probably interacts with PlsX. Belongs to the PlsY family.

Q47279

MLNSLGGGASLQITIKAGGNGGLFPSQSSQNGGSPSQSAFGGQRSNIAEQLSDIMTTMMFMGSMMGGGMSGGLGGLGSSLGGLGGGLLGGGLGGGLGSSLGSGLGSALGGGLGGALGAGMNAMNPSAMMGSLLFSALEDLLGGGMSQQQGGLFGNKQPSSPEISAYTQGVNDALSAILGNGLSQTKGQTSPLQLGNNGLQGLSGAGAFNQLGSTLGMSVGQKAGLQELNNISTHNDSPTRYFVDKEDRGMAKEIGQFMDQYPEVFGKAEYQKDNWQTAKQEDKSWAKALSKPDDDGMTKGSMDKFMKAVGMIKSAIRGDTGNTNLSARGNGGASLGIDAAMIGDRIVNMGLKKLSS

Elicits the hypersensitive response (HR) in the plant upon infection. Harpin elicits HR in non-hosts and is also required for pathogenicity in host plants. Via the HRP secretion pathway. Belongs to the harpin HrpN family.

O21587

MNMLLVIAVNTILSLILITVAFWLPQLNIYTEKANPYECGFDPMSSARLPFSMKFFLVAITFLLFDLEIALLLPIPWAIQTPHINMVLPTALILLTILALGLAYEWLQKGLEWTE

Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I. a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+) Core subunit of respiratory chain NADH dehydrogenase (Complex I) which is composed of 45 different subunits. Interacts with TMEM186. Interacts with TMEM242 (By similarity). Belongs to the complex I subunit 3 family.

P01696

IVMTQTPSSKSVPVGDTVTINCQASQSVYSNNRLAWFQQKPGQPPKLLIYKASTLASGVPSRFKGSGSGTQFTLTISDVQCADAATYYCRVASTNNIVFGGGTEVVVKGD

This chain was obtained from antibody to the polysaccharide of a streptococcal group a variant and was isolated from the serum of a single rabbit.

Q4QJS0

MTTFTHINSQGEANMVDVSAKAETVREAHAEAIVTMSKETLAMIVEGKHHKGDVFATARIAGIQAAKRTWELIPLCHPLLLSKVEVNLEPLLETNQVRIQSLCKLTGKTGVEMEALTAASVAALTIYDMCKAVQKDIVIEQVRLLEKCGGKSGHFIAEEK

Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP). (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate Cofactor biosynthesis; molybdopterin biosynthesis. Homohexamer; trimer of dimers. Belongs to the MoaC family.

O88533

MDSREFRRRGKEMVDYIADYLDGIEGRPVYPDVEPGYLRPLIPATAPQEPETYEDIIKDIEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLELPEAFLAGRAGEGGGVIQGSASEATLVALLAARTKVIRQLQAASPEFTQAAIMEKLVAYTSDQAHSSVERAGLIGGIKLKAVPSDGNFSMRASALREALERDKAAGLIPFFVVATLGTTSCCSFDNLLEVGPICNQEGVWLHIDAAYAGSAFICPEFRYLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKRRTDLTGAFNMDPVYLKHSHQDSGFITDYRHWQIPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVELSHEFESLVRQDPRFEICTEVILGLVCFRLKGSNELNETLLQRINSAKKIHLVPCRLRDKFVLRFAVCARTVESAHVQLAWEHISDLASSVLRAEKE

Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin. H(+) + L-dopa = CO2 + dopamine 5-hydroxy-L-tryptophan + H(+) = CO2 + serotonin Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 2/2. Homodimer. Belongs to the group II decarboxylase family.

Q5PI52

MTENIHKHRILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGMQTMAMQLGGHVEGSNEREFGYAQVEVLTDSALVRGIEDSLTADGKPLLDVWMSHGDKVTAIPSDFVTVASTESCPFAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFVRDICQCEALWTPAKIIDDAVARIREQVGDDKVILGLSGGVDSSVTAMLLHRAIGKNLTCVFVDNGLLRLNEAEQVMDMFGDHFGLNIVHVPAEERFLSALAGENDPEAKRKIIGRVFVEVFDEEALKLEDVKWLAQGTIYPDVIESAASATGKAHVIKSHHNVGGLPKEMKMGLVEPLKELFKDEVRKIGLELGLPYDMLYRHPFPGPGLGVRVLGEVKKEYCDLLRRADAIFIEELRKADLYDKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGRVSNRIINEVNGISRVVYDISGKPPATIEWE

Catalyzes the synthesis of GMP from XMP. ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. Homodimer.