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Full Name
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147
⌀
taxon
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46
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
stringlengths
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10
P08092
RAN1_SCHPO
Negative regulator of sexual conjugation and meiosis
Schizosaccharomyces
MMRENPELLLGQVLGDSLRFVSIIGAGAYGVVYKAEDIYDGTLYAVKALCKDGLNEKQKKLQARELALHARVSSHPYIITLHRVLETEDAIYVVLQYCPNGDLFTYITEKKVYQGNSHLIKTVFLQLISAVEHCHSVGIYHRDLKPENIMVGNDVNTVYLADFGLATTEPYSSDFGCGSLFYMSPECQREVKKLSSLSDMLPVTPEPIESQSSSFATAPNDVWALGIILINLCCKRNPWKRACSQTDGTYRSYVHNPSTLLSILPISRELNSLLNRIFDRNPKTRITLPELSTLVSNCKNLTRRLRPAPLVSSRYLAYQQQQQQQQMNLQQGIQGYPHQGYMPTQNIGFPWPPTPQFVSNWNHCATPTIPVSLQVLTPNSSLKVDPTTPLTAPIHATESFWPSAAAAAAAVHNNANSYMPITPTPYPNNAKIFGYPNQPPLTPIPFTGFVLHPAPVGRAADAVDPSRKSL
This protein is a negative regulator of both sexual conjugation and meiosis. It phosphorylates mei2. It blocks the onset of meiosis until conjugation takes place.
P08092
O15126
SCAM1_HUMAN
Secretory carrier-associated membrane protein 1
Homo
MSDFDSNPFADPDLNNPFKDPSVTQVTRNVPPGLDEYNPFSDSRTPPPGGVKMPNVPNTQPAIMKPTEEHPAYTQIAKEHALAQAELLKRQEELERKAAELDRREREMQNLSQHGRKNNWPPLPSNFPVGPCFYQDFSVDIPVEFQKTVKLMYYLWMFHAVTLFLNIFGCLAWFCVDSARAVDFGLSILWFLLFTPCSFVCWYRPLYGAFRSDSSFRFFVFFFVYICQFAVHVLQAAGFHNWGNCGWISSLTGLNQNIPVGIMMIIIAALFTASAVISLVMFKKVHGLYRTTGASFEKAQQEFATGVMSNKTVQTAAANAASTAASSAAQNAFKGNQI
Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.
O15126
Q20EV4
MIND_OLTVI
Putative septum site-determining protein MinD
Oltmannsiellopsis
MAYSVSRLVCSDGSIFSSNTNFETPFQPRVFHPSTSSEINERPDLNLLEGTPRTIVVTSGKGGVGKTTATANLGMSIARLGYRVVLVDADIGLRNLDLLLGLENRVLYTAMDILDGQCRLDQALIRDKRWKNLSLLAISKNRQRYNVTRKRMNMLIESLQKQGYDYILIDCPAGIDVGFINAVSPAKEAIIVTTPEITSIRDADRVAGLLESNGIYNVKLLVNRVRSEMIQQNDMMSVRDVQEMLGIPLLGAIPEDNHVIISTNRGEPLVLKKKLTLSGIAFENAARRLIGKQDYFIDLQTPYRNVFQRFQQFLGF
ATPase required for the correct placement of the division site.
Q20EV4
B1LD60
NUDL_ECOSM
Uncharacterized Nudix hydrolase NudL
Escherichia
MEYRSLTLDDFLSRFQLLRPQINRETLNHRQAAVLIPIVRRPQPGLLLTQRSIHLRKHAGQVAFPGGAVDDTDASVIAAALREAEEEVAIPPSTVEVIGVLPPVDSVTGYQVTPVVGIIPPDLPYRASEDEVSAVFEMPLAQALHLGRYHPLDIYRRGDSHRVWLSWYEQYFVWGMTAGIIRELALQIGVKP
Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.
B1LD60
Q1MH45
FABZ_RHIL3
Beta-hydroxyacyl-ACP dehydratase
Rhizobium
MTEEATTTLSSADIIEIMKLLPHRYPFLMVDKIIEIDGDNTAIGIKNVTVNEPHFTGHFPESPIMPGVLLIEGMAQTAGAICAKKDGQPGNLVYFMTIENARFRKPVVPGDRVEFHVRKHKQRGNIWKFHCDAKVDGALVAEADIGAMIVRKDQA
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Q1MH45
B1Y822
RS15_LEPCP
30S ribosomal protein S15
Leptothrix
MSEINKAEIVASNARAPSDTGSPEVQVALLTARINHLMPHFKTHMKDHHGRRGLLRMVSRRRKLLDYLKSRDADRYTSLIQKLGLRK
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
B1Y822
Q5X0P4
ATPE_LEGPA
F-ATPase epsilon subunit
Legionella
MSITTHLDIVSAEHEIFSGVVEMVVATGELGEIGITPGHAPLLTVLRPGEVRITLQGGTQDIYYVQGGMLEVQPHCVTILADVAERAEHLDEAAALAAKAKAEAAIASKGGDIDYSVAAAELARAVAQIRAIQKTRKKMK
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Q5X0P4
Q3MCT0
PSBA1_TRIV2
Photosystem II Q(B) protein 1
Trichormus
MTTLLEQRSSANLWHRFGNWITSTENRMYVGWFGVLLIPTALTAAIVFILAFIAAPPVDVDGIREPVSGSLLYGNNIITATVVPTSAAIGLHLYPIWEAASLDEWLYNGGPYQMIVLHFLIAIYAYMGRQWELSYRLGMRPWIPVAFSAPVAAATAVLLIYPIGQGSFSDGMMLGISGTFNFMIVFSPEHNILMHPFHMIGVAGVFGGALFSAMHGSLVTSTLVRETSEVESANTGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVIGIWFAALGISTMSFNLNGFNFNNSILDHQGRTIDTWADLLNRANLGIEVMHERNAHNFPLDLASGEVQPIALAAPAIAS
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.
Q3MCT0
P78567
H2B_AGABI
Histone H2B
Agaricus
MAPKPASTAGKAPASTASKAPVKSDAAKTASKSKVSSGADGEKKKRKKTRKETYSSYIYKVLKQVHPDTGISNKAMAILNSFVNDIFERIATEASKLASYSKKSTISSREIQTSVRLILPGELAKHAISEGTKSVTKFSSGGK
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
P78567
Q54TT4
COG3_DICDI
Component of oligomeric Golgi complex 3
Dictyostelium
MNNQTNQQSQTQSQSQQRINFDITGWEKKSKLSTQQYLLINNLNKSTQEKPLPQKYLEDKINNDIKKEENQQLQQQQQQQQQQQQQQQSPIIENFMDNFNPKTDIDNLSDFYQWYSIIDKNNPHLHQYEWFLETIVNYSKGSNQLLSMVENCDKLVESIQTDYSNLTKKTNQLNEDCEKFFNEELKLRYIAQSIHDKLKFYNQLEIQTKKFNTTNFNVTDSTFLTSLENLENSINFMKSNSTFMESNKYLTQYGFIFSRALGLIKDYISSNLKILSRDIINAQKQLKTSVSTPTSPQLQSSSGGSPLINDFSNSTDFNDLFQHSNIRFRAFAPKLRPLCLELEKRAIGPYLSYLYDTQNIYFNNRRSILSLIMFEKLQSLSKMTDISSMIRSSSLFMIQFYENEYQIYSNFFSPPDLNNNNNNNNNNNNNDNINNSTNINNSNNTNNNNQDIINNCPAFSNILDEYSQQLYDTIRPIYIHIHSFETLCNLAHLIRNELIDDLVQKSMKYSNGFKMTIERMLQDIQERLIFIIQTYIRDEIRSYHPNSDDLDYPNKLKIYVTAESTAVDGDGNGSGNSSPTLSYKSIYSTWYPTLEKSLTCLSKLYLVLETRIFEGLAQEVVEACTFTLIQASRLLLIQQKNDPYIILDSQLFLIKNLLTLREQIAPFDINFVIIEKIVDFPNLKHSLSTLYNVGSFLTLSTNNPILSLLSPRVTNTSIDSKKDLEKELKQSIESFILSNANTIIDPLLSLLTKISVFLNQSNKNQTDPMLLSQQSFADPQRIKEIIEQVKEKASNYLPQVIDRMKLYLSISTQILLMKPIRTNIIDSFDQINQYTKKYYTEDQIKIIDLQSLKLILDKILTPSKQSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKNENNENENENNSNVNSPSPQQL
Required for normal Golgi function.
Q54TT4
Q1CAK9
SYP_YERPA
Prolyl-tRNA synthetase
Yersinia
MRTSQYLLSTQKETPADAEVISHQLMLRAGMIRKLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYGPELLRFVDRGERPFVLGPTHEEVITDLIRGEINSYKQLPLNFFQIQTKFRDEVRPRFGVMRAREFLMKDAYSFHTTQESLQETYDAMYTAYSKIFSRMDLNFRAVLADTGSIGGSASHEFQVLAESGEDDIVFSTGSDYAANIEFAEALAPTEPRAPATEELRIVDTPNAKTIAELVEQFKLPIEKTVKTLLVHAHEESGHKLVALLVRGDHDLNEIKAEKLPQVAKPLTFASEEEIRAAIGAGPGSLGPVNLSLPVIADHSVAVMSDFGAGANIDGKHYFGINWERDLALPLVADLRNVVEGDISPDGKGTLQIKRGIEVGHIFQLGTKYSEVMKATVQGEDGRNQVMTMGCYGIGVSRVVAAAIEQNHDDRGIIWPDAIAPFQVAILPMNMHKSFRVKELAEELYTTLRSHGIDVILDDRKERPGVMFADMELIGVPHNIVIGDRNLDSEEVEYKNRRVGEKQMIKTSEIVEFLLSQIKR
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.
Q1CAK9
Q94125
AGE1_CAEEL
Aging alteration protein 1
Caenorhabditis
MSMGRSPSTTFRSRTGSHGARDLIAGHGRNSRRISQMHVNILHPQLQTMVEQWQMRERPSLETENGKGSLLLENEGVADIITMCPFGEVISVVFPWFLANVRTSLEIKLSDFKHQLFELIAPMKWGTYSVKPQDYVFRQLNNFGEIEVIFNDDQPLSKLELHGTFPMLFLYQPDGINRDKELMSDISHCLGYSLDKLEESLDEELRQFRASLWARTKKTCLTRGLEGTSHYAFPEEQYLCVGESCPKDLESKVKAAKLSYQMFWRKRKAEINGVCEKMMKIQIEFNPNETPKSLLHTFLYEMRKLDVYDTDDPADEGWFLQLAGRTTFVTNPDVKLTSYDGVRSELESYRCPGFVVRRQSLVLKDYCRPKPLYEPHYVRAHERKLALDVLSVSIDSTPKQSKNSDMVMTDFRPTASLKQVSLWDLDANLMIRPVNISGFDFPADVDMYVRIEFSVYVGTLTLASKSTTKVNAQFAKWNKEMYTFDLYMKDMPPSAVLSIRVLYGKVKLKSEEFEVGWVNMSLTDWRDELRQGQFLFHLWAPEPTANRSRIGENGARIGTNAAVTIEISSYGGRVRMPSQGQYTYLVKHRSTWTETLNIMGDDYESCIRDPGYKKLQMLVKKHESGIVLEEDEQRHVWMWRRYIQKQEPDLLIVLSELAFVWTDRENFSELYVMLEKWKPPSVAAALTLLGKRCTDRVIRKFAVEKLNEQLSPVTFHLFILPLIQALKYEPRAQSEVGMMLLTRALCDYRIGHRLFWLLRAEIARLRDCDLKSEEYRRISLLMEAYLRGNEEHIKIITRQVDMVDELTRISTLVKGMPKDVATMKLRDELRSISHKMENMDSPLDPVYKLGEMIIDKAIVLGSAKRPLMLHWKNKNPKSDLHLPFCAMIFKNGDDLRQDMLVLQVLEVMDNIWKAANIDCCLNPYAVLPMGEMIGIIEVVPNCKTIFEIQVGTGFMNTAVRSIDPSFMNKWIRKQCGIEDEKKKSKKDSTKNPIEKKIDNTQAMKKYFESVDRFLYSCVGYSVATYIMGIKDRHSDNLMLTEDGKYFHIDFGHILGHGKTKLGIQRDRQPFILTEHFMTVIRSGKSVDGNSHELQKFKTLCVEAYEVMWNNRDLFVSLFTLMLGMELPELSTKADLDHLKKTLFCNGESKEEARKFFAGIYEEAFNGSWSTKTNWLFHAVKHY
Phosphatidylinositol 3-kinase homolog that regulates longevity and diapause . Promotes cell survival during embryonic development by recruiting akt-1/2 to the plasma membrane through the production of PtdIns(3,4,5)P3 . Could function in the development or neuroendocrine signaling of the dauer pathway . Mediates susceptibility to enteropathogenic E.coli infection . May negatively regulate AYI interneuron neurite outgrowth . Plays a role in aversive olfactory learning when an odor is associated with food deprivation . Regulates this process by promoting the nuclear relocalization of egl-4 in AWC olfactory neurons after odor conditioning .
Q94125
Q5RHU7
MDM1_DANRE
Nuclear protein MDM1
Danio
MPVRFKGISEYRSKYKGRTSRSRSDSPHRRMRLAGLRSDQSGITQEPQFISKRRVPFYPSQVSSSFRWEGRDHSQQQLEKSRSPAVSPVLRATSAERQVTPLAPRDPPEGTTAPSQPPQAEAAQTSTFAVQKQKQALNGINHALRMKAGLRSEHQRNGLNSEYQRQFMWKTPVAESPLLAAHQMLYSNNRAIPPFKTNPVIMESEYKRSFKGSPLPRPPRLRRDVEQYEVPEFLTESKTPEKSKRKKKKKERPHSRKSSPEQEVAYLQQQEVKSPHNLKDPSPKVMRKGKTEYRSNFHSPLQYSYKDGAWLKIKSAKEEVKELRERAEAYKKRAWGTHFSRQHLNQILSDQNWMWEPSSGTSSSSIESEACRSTSHIIEALDLARAGSVRESSSPGHSASVVVSRRSSSGEVGLPEEPTLPVQRKLAWDEEEQLGEREEIVQDRLTDKEGKTRNENGMERNERLNSLESESLSSAEEGSEASVNGGRLPTPKLKTMQTVQRTHHDRTTPSIDFNLHYIAKAANGSLPRSSPVAGLTTVDVLPMREDVWSDEEVTDYRSLKPPKPSRKQQSSQRHKANAAPPANRIQGTMRNAEFQHNGNLGIFRPELFVLPQSDSALSDNDDKMSQISSRSAASCSMASEVLGRAQRRKQEFWGKS
Microtubule-binding protein that negatively regulates centriole duplication. Binds to and stabilizes microtubules.
Q5RHU7
Q9YDV3
TYW3_AERPE
tRNA wyosine derivatives biosynthesis protein Taw3
Aeropyrum
MGSIEEVLLEERLIGYLDPGAEKVLARINRPSKIVSTSSCTGRITLIEGEAHWLRNGARVAYKTHHPISRSEVERVLRRGFTNLWLKVTGPILHLRVEGWQCAKSLLEAARRNGFKHSGVISIAEDSRLVIEIMSSQSMSVPLVMEGARIVGDDALDMLIEKANTILVESRIGLDTFSREVEELVECF
S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wyosine derivatives biosynthesis pathway. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72.
Q9YDV3
A8ZV67
RL14_DESOH
50S ribosomal protein L14
Desulfosudis
MIQTETRLKVADNSGAKIVYCIKVLGGSRRRYATVGDVIVVSVKEAIPNSKVKKGDVLKAVIVRTKKEIKRPDGSYIRFDENSAVLISGNNEPLGTRIFGPVARELRAKRFMKIVSLAPEVL
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
A8ZV67
Q5PD50
CLCA_SALPA
H(+)/Cl(-) exchange transporter ClcA
Salmonella
MKTDTSTFLAQQIVRLRRRDQIRRLMQRDKTPLAILFMAAVVGTLTGLVGVAFEKTVSWVQNMRIGALVQVADHAFLLWPLAFILSALLAMVGYFLVRKFAPEAGGSGIPEIEGALEELRPVRWWRVLPVKFIGGMGTLGAGMVLGREGPTVQIGGNLGRMVLDVFRMRSAEARHTLLATGAAAGLSAAFNAPLAGILFIIEEMRPQFRYNLISIKAVFTGVIMSSIVFRIFNGEAPIIEVGKLSDAPVNTLWLYLILGIIFGCVGPVFNSLVLRTQDMFQRFHGGEIKKWVLMGGAIGGLCGILGLIEPAAAGGGFNLIPIAAAGNFSVGLLLFIFITRVVTTLLCFSSGAPGGIFAPMLALGTLLGTAFGMAAAVLFPQYHPEAGTFAIAGMGALMAASVRAPLTGIVLVLEMTDNYQLILPMIITCLGATLLAQFLGGKPLYSTILARTLAKQDAEQAAKNQNAPAGENT
Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.
Q5PD50
P28246
BCR_ECOLI
Sulfonamide resistance protein
Escherichia
MTTRQHSSFAIVFILGLLAMLMPLSIDMYLPALPVISAQFGVPAGSTQMTLSTYILGFALGQLIYGPMADSFGRKPVVLGGTLVFAAAAVACALANTIDQLIVMRFFHGLAAAAASVVINALMRDIYPKEEFSRMMSFVMLVTTIAPLMAPIVGGWVLVWLSWHYIFWILALAAILASAMIFFLIKETLPPERRQPFHIRTTIGNFAALFRHKRVLSYMLASGFSFAGMFSFLSAGPFVYIEINHVAPENFGYYFALNIVFLFVMTIFNSRFVRRIGALNMFRSGLWIQFIMAAWMVISALLGLGFWSLVVGVAAFVGCVSMVSSNAMAVILDEFPHMAGTASSLAGTFRFGIGAIVGALLSLATFNSAWPMIWSIAFCATSSILFCLYASRPKKR
Involved in sulfonamide (sulfathiazole) and bicyclomycin resistance . Probable membrane translocase. A transporter able to export peptides. When overexpressed, allows cells deleted for multiple peptidases (pepA, pepB, pepD and pepN) to grow in the presence of dipeptides Ala-Gln or Gly-Tyr which otherwise inhibit growth . Cells overexpressing this protein have decreased intracellular levels of Ala-Gln dipeptide, and in a system that produces the Ala-Gln dipeptide overproduction of this protein increases export of the dipeptide .
P28246
Q6EM90
RR7_HOUCO
30S ribosomal protein S7, chloroplastic
Houttuynia
MSRRGTTEEKTAKSDPIYRNRLVNMLVNRILKHGKKSLAYQIIYRAVKKIQQKTETNPLSVLRQAIRGVTPDIAVKARRVGGSTHQVPIEIGSTQGKALAIRWLLWASRKRPGRNMAFKLSSELLDAAKGSGDAIRKKEETHRMAEANRAFAHFR
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit.
Q6EM90
Q7VGE3
RL4_HELHP
50S ribosomal protein L4
Helicobacter
MSKAILLDKKLQQSNELALPERYAQIKEHNLYLYVKSYLSSLRANSASAKKRGEVSGGGKKPWKQKGGGRARAGSITSPVFVGGGVSHGPSNDKNYTLKINKKQKRLALECALFQKAQEGKLFVVDSLAMPSGKTKDAYAMFKALKQRSTLFVAQMSDEPTFLAFRNLQQCYLADANELNAYLVAAFRSVVIEKAVFDEIIAEKKGE
Forms part of the polypeptide exit tunnel.
Q7VGE3
P81726
ICI2_CANLI
Subtilisin inhibitor CLSI-III
Canavalia
NDVDVVMDASSKPIFPGGEYYIMPAIWGPPGGGVRLAKTRNSDCPVTVLQDYGEVIFGQPVKFTLPGRGSGLIITNTPVEEFIKKPECASSSKWSVFVDDEIEKACVGIGGHEDHPGEQVFSGTFTIQKSRTPYNSYKLVFCESDSSTCSDIGRYDNNEGGRRLILTHHNPFQVVFMDASTFDGTIRSDG
Inhibits subtilisin-type microbial serine proteases incuding proteinase K, subtilisin BPN', subtilisin Carlsberg and subtilisin E in a non-stoichiometric manner. Weakly inhibits A.oryzae protease and some metalloproteases including pronase E. Does not inhibit trypsin, chymotrypsin, S.griseus alkaline protease or A.lyticus lysyl endopeptidase. CLSI-II has a wider inhibitory specificity than CLSI-III.
P81726
Q8D9J9
NPD_VIBVU
Regulatory protein SIR2 homolog
Vibrio
MNFPYRNIVVLTGAGISAESGIQTFRAQDGLWENHRIEDVATPEGFARDPDLVQDFYNQRRKKLQDPNIEPNAAHLALGRLEAELDGQVTIVTQNIDNLHERGGNKNIIHMHGELLKSRCSVSNQVIEETGDILTGDLCHCCQMPSQMRPHVVWFGEMPLRMGEIYSALETADLFISIGTSGVVYPAAGFVHDAKMHGAHTIEINLEPSAIESEFVEKRYGKASVEVPKLVEELLAHLESNVESA
NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.
Q8D9J9
Q9VDW3
DMDB_DROME
Protein detached
Sophophora
MTAKPPPPIPPTLGGDDSGTHGPKLAPEIPRINSELAAQAALRGQQLLRKQGSQEQHATNTLPAHKTGAPPPLPPTQSRPVPAIPARGASDRAAPPEIPPKRHSLKSMPDGQPMMVPGLPPTMRQPPPLPRKPASTQSSAQNSAQSSPLAGMKFKDKPPPPPEKHSTLSAEGMAARRCSNPFEMPPPPPPLVLQSAVAALSEQSSKNGLNPVPSPAPTRASEAKKINQRSIASPTEEFGSEDALRGIESGLRNMERAMQEQMNLRNMEAAVQNNFDLSFKASLAAGARHLGGGSVNLRTANYERNLSLDEGRAGDSRQSLEELKQLRAQAQQQSLLNNSSSSSSNSQVEQSMRSTIEHHMRSLDRNLPLELQYSRHRFQNNLNAVAAAGGGGGNSSTGNAVANSGTSGSQQPPMPLSSEFREQIRQQLLGNIPPQVVHNMGQSPGSAAAAALLQHQAQSRAAAAAAAAAAAAAAAQVAAGSGALSREELRMRRRSSHDETQLTQNSSGGIQVTRLREHWDETSQCVLQRAAQLKNMLSDSQRFEAKRLELEKWLARMEQRAERMGTIATTADILEAQQKEQKSFHAELHQNKQHFDIFNELTQKLIAVYPNDDTTRIKKMTEVINQRYANLNSGVINRGKQLHAAVHSLQSFDRAMDQFLAFLSETETLCENAESDIERNPLMFKDLQSEIETHRVVYDRLDGTGRKLLGSLTSQEDAVMLQRRLDEMNQRWNNLKSKSIAIRNRLESNSEHWNALLLSLRELTEWVIRKDTELSTLGLGPVRGDAVSLQKQLDDHKAFRRQLEDKRPIVESNLTSGRQYIANEAAVSDTSDTEANHDSDSRYMSAEEQSRELTRSIRREVGKLSEQWNNLIDRSDNWKHRLDEYMTKMRQFQKILEDLSSRVALAEQTKTSWLPPSSVGEANEQMQQLQRLRDKMTTASALLDDCNEQQSFFTANQVLVPTPCLSKLEDLNTRMKLLQIAMDERQKVLCQAGAQQTHENGDDGRTTSNSGTIGPLPNLGQSVKPPWERATTAANVPYYIDHERETTHWDHPEMIELMKGLADLNEIRFSAYRTAMKLRSVQKRLALDRISMSTACESFDRHGLRAQNDKLIDIPDMTTVLHSLYVTIDKIDLTLMLDLAINWILNVYDSQRTGQIRVLSFKVGLVLLCKGHLEEKYRYLFRLVADTDRRADQRRLGLLLHDCIQVPRQLGEVAAFGGSNIEPSVRSCLEQAGISQEAIDGNQDISIELQHFLGWLQHEPQSLVWLPVLHRLAAAEAAKHQAKCNICKEYPIVGFRYRCLKCFNFDMCQKCFFFGRNAKNHKLTHPMHEYCTTTTSTEDVRDFTRALKNKFKSRKYFKKHPRVGYLPVQSVLEGDALESPAPSPQHTTHQLQNDMHSRLEMYASRLAQVEYGGTGSNSTPDSDDEHQLIAQYCQALPGTSNGSAPKSPVQVMAAMDAEQREELEAIIRDLEEENANLQAEYQQLCSKEQSGMPEDSNGMQHSSSSMTGLSGQGEQGQDMMAEAKLLRQHKGRLEARMQILEDHNRQLEAQLQRLRQLLDEPNGGGSSATSSGLPSAPGSALNSKPNTLQTRSVTASQLNTDSPAKMNQQNGHYEHNSKNSSGLVTVITEQELESINDDLEDSSSSNTTNTTTTTTTTATTEKTCVELQK
Required for the maintenance of appropriate synaptic retrograde communication and the stabilization of muscle cell architecture or physiology. May play a role in anchoring the cytoskeleton to the plasma membrane.
Q9VDW3
Q74IG8
RF3_LACJO
Peptide chain release factor 3
Lactobacillus
MTKLTDEVKKRRTFAIISHPDAGKTTITEQMLLFGGVIRSAGTVKARKSGHYATSDWMAIEKKRGISVTSSVMQFEYQGKRINILDTPGHQDFSEDTYRTLMAVDAAVMVIDSAKGIEPQTKKLFKVVKKRGIPIFTFMNKLDRDGREPLDLIAELEDLLGIEGVAMNWPIGMGKQLKGLYDIANNRVELYRKDEDDRYLPLDENGKLSEDEALAQDSLYQSTLDDIDLLKEAGNTFDKDKILRGDQTPVFFGSALTNFGVETFLDSFVNLAPAPQEHVVNEDEKLAADDPEFSGFVFKIQANMNPNHRDRIAFVRIGSGEFKKGIDVTLARTGKPVRLNNATEFMSSERVQVSDAVAGDIVGLYDTGNFQIGDSIYAGKKKIVYPELPQFTPEIFMRVTAKNVMKQKSFHKGMNQLVQEGAIQLYRGYSTDDYILGAVGQLQFEVFSFRMKNEYNSEVELHTLGNRVARWINPDQLDPKMSSSRNLLVKDRDGEPLFLFENAFAERWFKDKYPDVELTSRL
Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.
Q74IG8
Q8FUD1
BIOB_COREF
Biotin synthase
Corynebacterium
MPNTTSILDTARHQVLGDGIGLDQSQLIEILNLPDEDIPALMELAHQVRLKWCGEEIEVEGIISLKTGGCPEDCHFCSQSGLFESPVRSVWLDIEQLVEAAKQTAKSGATEFCIVAAVKGPDDKLMNQLEEAVAAIQREVDIEVAASVGSLTPEQVTRLARAGVHRYNHNLETARSFFPQVVTTHTWEERRETLRLVAEAGMEVCSGGILGMGETLEQRAEFAVQLAELNPTEVPINFLDPRPGTPFADRPLMESEDALRAIGAFRLAMPHTMIRFAGGRELTLGAEGSEQGLLGGINAIIVGNYLTTLGRPMEDDLEMMDRLQLPLKVLNKVI
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Q8FUD1
Q8P1W7
CAPP_STRP8
Phosphoenolpyruvate carboxylase
Streptococcus
MPLKKLESSNNQAIIAEEVALLKEMLENITRRMIGDDAFTVIESIMVLSEKQDYIELEKVVANISNQEMEVISRYFSILPLLINISEDVDLAYEINYQNNTDTDYLGKLALTIKDLAGKDNGKDILEQVNVVPVLTAHPTQVQRKTILELTTHIHKLLRKYRDAKAGVISLEKWRQELYRYVEMIMQTDIIREKKLQVKNEIKNVMQYYDGSLIQAVTKLTTEYKNLAQKHGLELDNPKPITMGMWIGGDRDGNPFVTAETLCLSATVQSEVILNYYIDKLAALYRTFSLSSTLVQPNSEVERLASLSQDQSIYRGNEPYRRAFHYIQSCLKQTQIQLTNQPAARMSSSVGLNTSACPSPASLENPILAYDSPVDFKADLKAIEQSLLDNGNSALIEGDLREVMQAVDIFGFFLASIDMRQDSSVQEACVAELLKGANIVDDYSSLSETEKCDVLVQQLMEEPRTLSSAAVAKSDLLEKELAIYTTARELKDKLGEEVIKQHIISHTESVSDMFELAIMLKEVGLVDQQRARVQIVPLFETIEDLDNACDIMAAYLSHDIVKSWIATNRNYQEIMLGYSDSNKDGGYLASGWTLYKAQNELTAIGEEHGVKITFFHGRGGTVGRGGGPSYDAITSQPFGSIKDRIRLTEQGEIIENKYGNKDVAYYHLEMLISASINRMVTQMITDSNEIDSFREIMDSIVADSNMIYRKLVFDNPHFYDYFFEASPIKEVSSLNIGSRPAARKTITEITGLRAIPWVFSWSQNRIMFPGWYGVGSAFKRYIDRAQGNLERLQHMYQTWPFFHSLLSNVDMVLSKSNMNIAFQYAQLAESQDVRDVFYEILDEWQLTKNVILAIQDHDDLLEDNPSLKHSLKSRLPYFNVLNYIQIELIKRWRNNQLDENDEKLIHTTINGIATGLRNSG
Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Q8P1W7
Q54WR1
MTR1_DICDI
Cap1 2'O-ribose methyltransferase 1
Dictyostelium
MFQSNQYDEYNKTNKSDEENESNENENENENENENRSEDGDQDSEDSFIYEEDDEEEEDTPKLSFGAKFLAKHGHIEGQGLGKEKDGRIDLIEVDRFQSTKGLGFAENDLPEFYRVTKHILEDEDVDFPSKQRFEWISCNSEGYNFWEGFPVDHTLVKFVANDSITDKPRRGHCSVELLMELDQHKNALDTLDPNRFYVARKKSNPYESIKGSIFINRAAVKMANIDKLADLLTPIIPVPGKPRDFIYFGDVCAGPGGFTEYVYWKKTRGGKIKGEEGLDLDDVVKGFGFTIKGQCDWNVEKFSKQIPIHNFVKEYGLDDTGNILKSENIRDFSSKVFYNTNGFGLQLFLADGGINTDGKESLQELMLQQLILCQILTMFETIGRGGNFVCKIFDTFTPFTIGLLYLVYQHFQSFSIVKPFTSRPLNSERYIICKNFLSYRPMNIIDFLHYINSLLNNNQTILELIEINSMDPNFLRYILESNELICLRQIKAFSLFKKYVEDIELPPIDQKEIRAKCLEEWGLPKETKYDIENYQKHKNRQKHHHNNHSNNNNNNNNSNNNNNNNNQHQHQHHQHQHHQNQHQNQYQHQNQHKKYNNNINNNSNNSSPNSSPNLTSSPNLNSPPNINNGNNHQNNNNNNSNNNNNNNNNNNNNNNNNNNNNNNNNNNKNRRFISTKLVKNNSQFQQKPPPPHRHMSPLQIQQQFLLQQQKEQQLLQQPQKDQLHQLHQQQSQSALPDFSAANFMEALLKRKNDSQQ
S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1). Cap1 modification is linked to higher levels of translation.
Q54WR1
A5UCP4
MTNN_HAEIE
S-adenosylhomocysteine nucleosidase
Haemophilus
MKIGIVGAMAQEVEILKNLMADRTETRVASAVIFEGKINGKDVVLLQSGIGKVAAAIGTTALLQLAKPDLVINTGSAGGVAKGLKVGDIVISDETRYHDADVTAFGYEKGQLPANPAAFLSDKKLADLAQEIAEKQGQSVKRGLICSGDSFINSEDKITQIKADFPNVTGVEMEATAIAQVCYAFNVPFVVVRAISDGGDGKASISFEEFLPLAAKQSSALVLEMIDRL
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine.
A5UCP4
Q5HM15
RL18_STAEQ
50S ribosomal protein L18
Staphylococcus
MISKIDKNKVRLKRHARVRTKLSGTAEKPRLNVYRSNKHIYAQIIDDVKGVTLAQASSQDKDIANTSASKVDLATTVGQEIAKKANDKGIKEIVFDRGGYLYHGRVKALADAARENGLEF
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
Q5HM15
Q8U242
PSTB_PYRFU
Phosphate-transporting ATPase
Pyrococcus
MKFAIETINLHVYYGRNHVLRGINLQIPQRGIFAIMGPSGCGKSTLLRTFNRLIELNQDARVEGEVRIFGKNIYSEDVDPIEVRKKVGMVFQYPNPFPHLTIYENVAIGVKLNKLVKSQKELDERVRWALKKAALWEEVKDRLNDYPGNLSGGQRQRLVIARVLAMKPDILLMDEPTANIDPVGTAKIEELLLELKTDYTIVLVTHSPAQAARIADYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGALG
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Q8U242
B2GDU5
RS13_LIMF3
30S ribosomal protein S13
Limosilactobacillus
MARIAGVDLPRDKRIVIGLTYIFGIGNTTAQKILANAGVSEDIRVRDLTPDQEEKIRAEVDQIKVEGDLRREVSLNIKRLQEIGSYRGMRHRHGLPVRGQHTKNNARTRKGKAVAIAGKKK
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
B2GDU5
Q2SY12
METN_BURTA
Methionine import ATP-binding protein MetN
pseudomallei group
MIEIRNLSQRFEGPRGWIEALHNVNLTIPQGEVFGIIGRSGAGKSTLVRTINLLTRPSEGNVFVDGRDLTQLSAGELRGARRDIGMIFQHFNLLSSRTVFGNVALPLELAGVKRAEIEATVLPLLDLVGLAAQKDRYPAQISGGQKQRVGIARALASKPKVLLSDEATSALDPETTRAILDLLRRINRELGLTIVLITHQMEVIKDVCDRVAVLDAGRVVEEGNVIDVFMRPHHEVTRALIGDVIAQELPPAMKARVAERLKTGSGHLLRLAFTGSGVDQPILSETIRRYELDFNILHGQIDEIQGRAFGSLAVLATGEPGKVGQAFAYLREQGVVVEELSYVE
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Q2SY12
O68905
TRPB_MYCIT
Tryptophan synthase beta chain
Mycobacterium avium complex (MAC)
MDISPRTRPDLPLPSAAIAEPTRHEPDAGGHFGVYGGRYVAEALMAVIEEVTTAYEKERVNQDFLDTLDYLQANYAGRPSPLYEAPRLSEQAGARIFLKREDLNHTGSHKINNVLGQALLAQRMGKKRVIAETGAGQHGVATATACALLGLECVIYMGAVDTERQALNVARMRLLGATVVSVQSGSKTLKDAINEAFRDWVTNADNTFYCFGTAAGPHPFPAMVRDFQRIIGLEARAQIQAQAGRLPDAVLACIGGGSNAIGIFHPFIDDPGVRLIGFEAAGDGVETGRHAATFSGGSPGAFQGSFSYLLQDEDGQTIESHSISAGLDYPGVGPEHAWLRERVSTTRGWVRNTRGCARFRTLCRTEGIIPAIESAHAVAGALKVAPELGKAAIIVVNLSGRGDKDVETAAQWFGLLGSSDR
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
O68905
Q9F0C9
NODA_METNO
Nodulation protein A
Methylobacterium
MRFPSDLCPSSGTGELSARSQVRWRLCWENELELADHAELAEFLRKAYNPSGTFNARPFEGGRSWAGARPEVRAIGYDSRGVAAHIAALRRFIKVGAVDLLVAELGLYAVRPDLEGLRISHSMLVMYPALKELGVPFGFGTVRHALQKHLTRLLGKAGLATIVSGVRVRSTLRDMRLDMPPTRVEDLLILVFPIGRPMSDWPAGTIIDRNGPEL
N-acyltransferase required for nodulation. Acts in the production of a small, heat-stable compound (Nod) that stimulates mitosis in various plant protoplasts.
Q9F0C9
Q46XM6
LSPA_CUPPJ
Signal peptidase II
Cupriavidus
MASTTSRSARPARRNNKASGNTTPLLWMAFALLVVVLDQFFKIVIVRTFTYGESRPVTRFFNLVLVYNKGAAFSFLADAGGWQRWFFTGLGLVVGAFIVWLLYRHTGQKLFCFAVSLILGGAVGNVVDRVVYGHVIDFLDFYVRNYHWPAFNVADCAITVGAVLLIVDELRRVRKH
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Q46XM6
Q6FPK6
RGI1_CANGA
Respiratory growth induced protein 1
Nakaseomyces/Candida clade
MAKKDKKPKVNTIVTKDGESLKVFEDLNDFEMFIKNETEDEEFDHIHCKLTYYPPFVLHESHDDPEKIKDTNNSHNKKFVRHLHQHVEKHLLKDIKEALHKPELKFHDKSKDETFEHIVWHYGEETEYHDRKFRIQVTVTCNHDDAMVDVDYKTIPL
Involved in the control of energetic metabolism and significantly contribute to cell fitness, especially under respiratory growth conditions.
Q6FPK6
B7GIH1
SELO_ANOFW
Protein adenylyltransferase SelO
Anoxybacillus
MNANWNFDNSYARLPERFFTRIYPTPVSDPKLVVLNHSLAKELGLNAEVLASEEGVAVFAGNRVPEGAEPLAQAYAGHQFGYFNMLGDGRAILLGEHVTPSGERVDIQLKGSGRTPYSRGGDGRAALGPMLREYIISEAMHALGIPTTRSLAVVTTGEVVMRETELPGAILTRVAASHLRVGTFQYAGRFLSKEELQALADYAIKRHYPNGEHASNRYVFLLEEVMKKQAALVAKWQLVGFIHGVMNTDNMTISGETIDYGPCAFMDVYDPETVFSSIDTQGRYAYGNQPYIAGWNIARFAESLLPLLHDEEEKAIEIAQKVIEQFPALYETYWLQGMRAKLGLWTEEAEDKKLIGELLHLMYTHRLDYTNTFRSLTLEEWHFCEQELRDWYTRWQQRIARQDMTKEEVYECMRQNNPAIIPRNYRVEEALAAAVEHGDDTVMERLLHVLSDPYAYMEEQEEYAKTPEPSDRPYRTFCGT
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
B7GIH1
Q8UBZ5
RL19_AGRFC
50S ribosomal protein L19
Agrobacterium tumefaciens complex
MTNIIQQLEAEQAAKIEAKRTLPEFSPGDTLRVNVRVTEGNRTRVQAYEGVCIARSGGGLSESFTVRKISYGEGVERVFPIYSPLVEGVEIVRRGKVRRAKLYYLRDRRGKAARIVENTGTRARKLNESERQAAAEEKARLEAEKVAAAQALAAEKAAAEAAEAKAAEEAAKAAEATAE
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.
Q8UBZ5
Q9LPK7
AEE10_ARATH
AMP-binding protein 10
Arabidopsis
MELLLPHPSNSTPLTVLGFLDRAASVYGDCPSILHTANTVHTWSETHNRCLRIASALTSSSIGIKQGQVVSVVGPNVPSVYELQFAVPMSGAILNNINPRLDAHALSVLLRHSESRLVFVDHRSISLVLEAVSLFTQHEKPHLVLLDDDQENDSSSASDFLDTYEEIMERGNSRFKWIRPQTEWQPMVLNYTSGTTSSPKGVVLSHRAIFMLTVSSLLDWSVPNRPVYLWTLPMFHANGWGYTWGTAAVGATNICTRRVDAPTIYNLIDKHNVTHMCAAPMVLNMLINYPLSTPLKNPVQVMTSGAPPPATIISRAESLGFNVSHSYGLTETSGPVVSCAWKPKWDHLDPLERARLKSRQGVRTLGFTEVDVRDRKTGKSVKHDGVSVGEIVFRGSSVMLGYYKDPQGTAACMREDGWFYSGDIGVIHKDGYLEIKDRSKDVIICGGENISSAEIETVLYTNPVVKEAAVVAKPDKMWGETPCAFVSLKCDNNGDGSVPVTEREIREFCKTKLPKYMVPRKVIFQEELPKTSTGKIQKFLLRQMAKTLS
May act as an acid--thiol ligase that activates carboxylic acids by forming acyl-CoAs.
Q9LPK7
B4TWD6
RBFA_SALSV
Ribosome-binding factor A
Salmonella
MAKEFGRPQRVAQEMQKEIAIILQREIKDPRLGMMTTVSGVEMSRDLAYAKVFVTFLNDKDEDAVKAGIKALQEASGFIRSLLGKAMRLRIVPELTFFYDNSLVEGMRMSNLVTNVVKHDEERRVNPDDNKED
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
B4TWD6
Q8SZZ8
ICE2_DROME
Interactor of little elongator complex ELL subunit 2
Sophophora
MFSMDSFAMDKDAKLYEGNALFRNQPSYKVFNKSFEHVDDALYTLLNEVEPDVLRMELQETGDLFKSFNRNSALRDPRNNEVPPKPTRDLTTASSLYSFPNPLEQYSELNLKQQAACMRVLLAWQCSQPVDEQDIVVWQATEKKRYNEQQRVQKYIHDHEQGRKEVIYAPMKSLVAVYRKWYELGVKKLQQTYPNDSYMTFSGLPQLPQCRSLNAQTASIEQVELERIVGRVRLLPEVEVRHEALRTLRLRLDRYATRETRAPVQLLREEDKELELEAGNVFVLPLDSLLMLLTTGSYIDLPTEMFLSLRESPNSKHKCMEFQSPFPPRNCGWHTNSLILKLAYGAYISQPGQAKWLDFNINGAVKEVPDEPACDKSSIDLQMVYKPRAIDQQPSDIEDGNCNSALVSWTLRCKGEGDDCNDFQIFSTLSIPAVKDSSGKEPLGCHFIKLENKPDCGCEIMSKYELISAWVQLKLMRAEMGHCTRISLRDFEPMLEEKLTLISLEQQLHDYYNTSMPQLLSNLCEFLKLLDTVPAGDYLLRYSPKYKDKFLLCIVTKEATPQSFQLHQLLTESIPSDQAFLTQSSYLPISPTLCGRLHEELHLLPCAFPAKANGRSVQRRKVVVPIPEPSRQAPVRRQRLKKWSEAQTREFRRRCKVDQKKRARARKTAAANKEKIELEKIMTL
Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III.
Q8SZZ8
O06465
AHPF_XANCH
Alkyl hydroperoxide reductase subunit F
Xanthomonas
MLDANLKTQLTAYLERVTRPIQINASIDDSAGSREMLDLLEELVLLSDKISLDIHRDDNQRKPSFALTTPGQDISLRFAGLPMGHEFTSLVLALLQVGGHPSKAAAELIEQVQHLEGDYQFETYFSLSCQNCPDVVQALNLAAVLNPRIKHVAIDGAWFQDEVQARQIMSVPTVYLNGELFDQGRMTLEQIVAKLDTNAAKRDAAKIAAKEAFDVLVVGGGPAGSAAAVYAARKGIRTGVAAERFGGQVLDTMSIENFISVPETEGPKMAAALEQHVRQYDVDIMNLQRAEQLIPAGADGLIEIKLANGASLKSKTVILSTGARWRQMNVPGEDQYKNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVAHVTLVEFDDKLRADEVLQRKLRSLHNVRIITSAQTTEVLGDGQKVTGLVYKDRTGGDIQHIELEGVFVQIGLLPNTEFLRGTVALSPRGEIIVDDRGQTDVPGVFAAGDATTVPYKQIVIAMGEGSKAALSAFDHLIRTSAPATADSVAQAA
Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein.
O06465
P9WFH0
Y3399_MYCTO
Putative S-adenosyl-L-methionine-dependent methyltransferase MT3507
Mycobacterium tuberculosis complex
MARPMGKLPSNTRKCAQCAMAEALLEIAGQTINQKDLGRSGRMTRTDNDTWDLASSVGATATMIATARALASRAENPLINDPFAEPLVRAVGIDLFTRLASGELRLEDIGDHATGGRWMIDNIAIRTKFYDDFFGDATTAGIRQVVILAAGLDTRAYRLPWPPGTVVYEIDQPAVIKFKTRALANLNAEPNAERHAVAVDLRNDWPTALKNAGFDPARPTAFSAEGLLSYLPPQGQDRLLDAITALSAPDSRLATQSPLVLDLAEEDEKKMRMKSAAEAWRERGFDLDLTELIYFDQRNDVADYLAGSGWQVTTSTGKELFAAQGLPPFEDDHITRFADRRYISAVLK
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
P9WFH0
A5VR16
RL7_BRUO2
50S ribosomal protein L7/L12
Brucella
MADLAKIVEDLSALTVLEAAELSKLLEEKWGVSAAAPVAVAAAGGAAPAAAAEEKTEFDVVLADGGANKINVIKEVRALTGLGLKEAKDLVEGAPKAVKEGVSKDEAEKIKAQLEAAGAKVELK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
A5VR16
Q3AGZ9
NU4C_SYNSC
NDH-1, chain 4
unclassified Synechococcus
MQATVPWLSLSILVPIVGALLVPLVPDKGEGKQVRWYALIVTLITFLITVAAYLTGYDPSLSGLQLSERVSWLPDLGLTWAVGADGLSMPLILLTSFITSLACLAAWPVSFKPRLFYFLLLAMDGGQIAVFAVQDMLLFFLAWELELIPVYLLLAIWGGKKRQYAATKFILYTAGSSLFILLAALAMGFFGGGTPSFEYTALAAKDFGTGFQLLCYAGLLIAFGVKLPIVPLHTWLPDAHGEATAPVHMLLAGILLKMGGYALLRFNCELLPAAHSQFAPLLIVLGVVNIIYAALTSFAQRNLKRKIAYSSISHMGFVLIGVGSFSALGTSGAMLQMISHGLIGASLFFLVGATYDRTHTLQLDEMGGIGQKMRIMFALWTVCALASLALPGMSGFVSELMVFAGFATDEAYTLPFRVVICGLAAVGVILTPIYLLSMLREIFFGKEKEELVSHTNLVDAEPREVYIIGCLLVPIIGIGLYPKLMTDSYRSSIEALVSRNLGAMEQVISPTAPLIRGQAPVPAIIQAPAVGAS
NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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.
Q3AGZ9
Q9B6F0
CYB_THRSW
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Thryonomys
MKITRKAHPLLKMINHSFIDLPTPPNISSWWNFGSLLGACLALQILTGLFLAMHYTADTTTAFSSVTHICRDVNYGWLIRYLHANGASMFFICLYLHVARGMYYGSYMFLETWNLGVILLLFVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGPTLVEWVWGGFSVDKATLTRFFALHFILPFIITALTMVHLLFLHETGSNNPTGLNSDCDKIPFHPYYSMKDLIGLLLLFFFLLLLVLFFPDILGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILILMIIPFIHLSKQRSMSFRPLSQCLFWTLAANLIILTWIGGQPVEHPYITIGQVASILYFTIILILMPLASLIENKILKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Q9B6F0
Q0UUH1
TPC1_PHANO
Mitochondrial thiamine pyrophosphate carrier 1
Parastagonospora
MSEGVAQLKHEGSRQQVVVAGAAAGLVSRFVIAPLDVIKIRLQLQIHSLSEPTSYRGLNGPVYKGTLGTLKQILRDEGVTGLWKGNIPAELLYLTYGSVQFSAYTNISQMLDTIPAPYTLPSSANSFISGAGAGAAATTVTYPLDLLRTRFAAQGKDRVYTSIVASLKSIAQHEGPTGFFRGLGAGVSQIVPYMGLFFASYESLKPVMADSPLPLPLGSSDAVAGVVASVVSKTAVYPLDTTRKRLQVQGPNRARYVHRNIPTYSGVLMTLQHIWKHEGRRGMYRGLTVSLLKAAPASAVTMWTYERAMGIMVAFEKDGME
Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria.
Q0UUH1
Q2QNK7
S40A2_ORYSJ
Solute carrier family 40 member 2, chloroplastic
Oryza sativa
MGMVTATAAAALLASPPQGHLGRRCHLVVPGLRLRPPASSSPPHAAPPLRLSNFVPRCYITNVEVDVSHTSEQEALDDHPPLLPACAIPVVHLRDVPDASPFPLHESASHSTDFEELPVLSEGELHTIAATPAHPAGLYALYASYLFGNLVEQLWNFAWPAALAILHPSLLPVAIVGFFTKLSVFIGAPIVGKLMDHFPRIPMYTGLNAVQVATQLISAAMVIYAMKNVTHASTSAVVLKPWFIALVAAGAIERLAGLALGVAMERDWVVLLAGTNRPVALAQANAVLNRLDLVCETVGASVFGLLLSKYHPVTCLKIACGLMICSFPVLVVLGQLINRFSCHALDSSRTPSEESICANLLDVRKIVQNGLSAIRNGWNEYKQQTVLPASVATVFLNFNVALAPGAIMTALLMHRGISPSIVGAFSGLCSIMGLVATFISSSLVERVGILKAGAAGLIVQASLLSVALVVYWTGSISQRTPLLIFLAAIALSRLGHMSYDVVGTQILQTGVPASKANLIGGMEVSISSLAELVMLGMAIIANDVSHFGFLAILSVSSVAGAAWMFCQWLGNPTDEQRELFMFDPHFQVEPI
May be involved in iron transport and iron homeostasis.
Q2QNK7
A8F972
RL10_BACP2
50S ribosomal protein L10
Bacillus
MSNAIDTKKVVVDEITSKFKDSMSTVIVDYRGLSVSEVTELRKQLRDAGVEFKVYKNTLTRRAVEQVELTGLNDFLTGPNAIAFSNEDVIAPAKIINEFAKSHEALEIKAGVIEGNVATVEEVKALAELPSREGLLSMLLSVLQAPVRNLALATKAVADQKEEQGA
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
A8F972
Q99MB2
MTFR1_MOUSE
Chondrocyte protein with a poly-proline region
Mus
MLGWIKCLMRMWFQRVGVSMQSVLWSGKPYGSSRSIVRKIGTNLSLIQCPRVQFQLTSHATEWSPAHSGEDAVASFADVGLVATEEGECSIRLRAEVSSKPPHEDDPPCFEKPPSRHTSFPSLSQDKPSPERTLASEEALQKISALENELAALRAQIAKIVTLQEQQSPSAGCLDSSTSVTVAPPPPPPPPPPPLPLVLHQSTSALDLIKERREQRLSAGKTLATGHPKKPDMPNMLEILKDMNSVKLRSVKRSEKDVKPRPADTDHAAFIAEALKKKFAYRHNSQGETERGIPKPESEATSEPALFGPHILKSTGKMKALIENVPDS
May play a role in mitochondrial aerobic respiration. May also regulate mitochondrial organization and fission.
Q99MB2
A2BYS6
RL14_PROM5
50S ribosomal protein L14
Prochlorococcus
MIQQETYLTVADNSGAKRLQCIRVLGSNRRYAHVGDVVVASVKDALPNMGVKKSDVVKAVIVRTRHTLRRNTGNSIRFDDNAAVLINEDKNPKGTRVFGPVARELRDKNFTKIVSLAPEVI
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
A2BYS6
Q0V9A8
VOPP1_XENTR
EGFR-coamplified and overexpressed protein homolog
Silurana
MKSLHCVGLYLLSLLCEFTEAKKHCWYFEGLYPTYYICRAYEDCCGSRCCVRALSIQRLWYFWFLLMMGVLFCCGAGFFIRRRMYPPLLVDEPTFNVSYTRQPAGPPPGPQHPGMPYYSDPGGAMGNPVTPSFHVQPSPQGNPPFPPPPSYCNTPPPPYEQVVKSCK
May be involved in the transcriptional activity of NFKB1.
Q0V9A8
A0T0T6
CYB6_THAPS
Cytochrome b6
Thalassiosira
MGKVYDWFEERLEVQAIADDISSKYVPPHVNIFYCFGGIVFTCFLVQVATGFAMTFYYRPSVVDAFASVEYIMTSVNFGWLIRSIHRWSASMMVMMLVLHVFRVYLTGGFKKPRELTWVTGVILAVVTVSFGVTGYSLPWDQVGFWACKIVTGVPAAVPIVGPPLVLVLRGGESVGQSTLTRFYSAHTFVLPLAAAVLMLTHFLMIRKQGISGPL
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
A0T0T6
P33198
IDHP_PIG
Oxalosuccinate decarboxylase
Sus
ARAAARHYADQRIKVAKPVVEMDGDEMTRIIWQFIKEKLILPHVDVQLKYFDLGLPNRDQTNDQVTIDSALATQKYSVAVKCATITPDEARVEEFKLKKMWKSPNGTIRNILGGTVFREPIICKNIPRLVPGWTKPITIGRHAHGDQYKATDFVVDRAGTFKIVFTPKDGSSAKQWEVYNFPAGGVGMGMYNTDESISGFAHSCFQYAIQKKWPLYMSTKNTILKAYDGRFKDIFQEIFEKHYKTDFDKYKIWYEHRLIDDMVAQVLKSSGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYREHQKGRPTSTNPIASIFAWTRGLEHRGKLDGNQDLIRFAQTLEKVCVETVESGAMTKDLAGCIHGLSNVKLNEHFLNTSDFLDTIKSNLDRALGRQ
Plays a role in intermediary metabolism and energy production . It may tightly associate or interact with the pyruvate dehydrogenase complex .
P33198
C7GIN5
ARO1_YEAS2
Shikimate dehydrogenase
Saccharomyces
MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMIAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKMSIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVIPPGSKSISNRALIIAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVEGHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTPSQKYIVLTGNARMQQRPIAPLVDSLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSATYPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKPLKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKFGVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERDEVANPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAGKTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYGDDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIREVWNRREEWYKECSNFSFFAPHCSAEAEFQALRRSFSKYIATITGVREIEIPSGRSAFVCLTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRTKKQGGNFPDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDFQGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTSKGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSRSPILHNTGYEILGLPHKFDKFETESAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDELTDAAKVIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRAALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVPADKPLDDELLSKLERFLVKGAHAAFAPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQMLVHQGVAQFEKWTGFKAPFKAIFDAVTKE
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.
C7GIN5
A1AJH6
NANM_ECOK1
Sialic acid epimerase
Escherichia
MNKTITALTIIMASFATNASVLPETPVPFKSGTGAIDNDTVYIGLGSAGTAWYKLDTQAKDKKWTALAAFPGGPRDQATSAFIDGNLYVFGGIGKNSEGLTQVFNDVHKYNPKTNSWVKLMSHAPMGMAGHVTFVHNGKAYVTGGVNQNIFNGYFEDLNEAGKDSTTIDKINAHYFDKKAEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEAKPGLRTDAVFELDFTGNNLKWNKLAPVASPDGVAGGFAGMSNDSLIFAGGAGFKGSRENYQNGKNYAHEGLKKSYSADIHLWHNGKWDKSGELSQGRAYGVSLPWNNSLLIIGGETAGGKAVTDSVLISVKDNKVTVQN
Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers. Probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses.
A1AJH6
B5FA13
GRPE_ALIFM
HSP-70 cofactor
Aliivibrio
MSNEENKVNEEAVVEEQVEAVGTEADVEWNESAEDSQEAKIAELEAALLASQAQIKEQQDTVLRAKAEEQNVRRRAEEDVDKARKYALKKFAGELLPVLDNLERALENGDKENEAAKALLEGVELTLQTFVSTVEKFGLTVINPMGEAFNPELHQAIGMQASPDHESNTVMIVMQKGYTLNDQVLRPAMVMVAQ
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
B5FA13
Q92NU9
MACB_RHIME
Macrolide export ATP-binding/permease protein MacB
Sinorhizobium
MAPLISLQDVSKTYFNGDIAVEVLHHISLDIEAGEFVAIIGQSGSGKSTLMNILGCLDQPTSGSYFIEGENVSGFDSDELAALRRRTFGFIFQSYNLIPTASARENVEVPAVYAGVSARDRHDRAEALLQSLKLGERIDHRPNQLSGGQQQRVSIARALMNGGRVILADEPTGALDSQSGDEVMRLLRDMNENGHTVIVITHSREVAAQADRLIEISDGHIVADRSKKRRSNRDAAVGLAQRTREGFAAIADVSEAVKMALRALRANLFRTILTLLGIVIGVGSVVAMLAIGTGAQNSVLDRISSMGSDLLVVRPSMANFRGSAGGTNVTLVPADADAITELANVAFAVPEMTSTVTLRRGNIDYQTTANGTVPQFTEAKSWKIGRGEFINRNDMETYAPVAVLGETVVKTLFPEGSDPIGQYVLVNKIPFQVIGVMSGMGASAGGNDQDDVVLVPLTTGSMRLFGQRNIRTITVKVQDASAIDLTQERIQALLNERHRKDDTQITNMSSVREAFTETSNTMKFFLGSVAAISLLVGGIGVMNIMLVSVSERTREIGVRMATGARERDILVQFIVEALVVSAIGGAIGVVAGLSTGYAAKAFGMPVSFTPGPVALAFACAFLTGLLFGYLPARNASRLQPAVALSAD
Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Q92NU9
Q74AA5
KUP2_GEOSL
Probable potassium transport system protein kup 2
Geobacter
MKTEAQSYWGGIIKSMGLVFGDIGTSPIYTLTVIMTLTKPDAEHVLGILSLIVWTLIILVTVEYAWLAMSLGRKGEGGTIVLKEILIRLLKSGRQMAFAGFLAFLGVSLLLGDGVITPAISILSAVEGMRLIPGLEDLAQGGLILVAAVIAVFLFIFQFKGTDKVASAFGPIMVVWFSALTVSGLVSIIGTPTVVQAISPHHAVLFLKHNGLAGFFVLSEVILCATGGEALYADMGHLGRKPIIRAWYFVFCALVINYLGQGAFILRNPEAKNILFSMVKSQVPMLYIPFLLLTISATIIASQALISGVFSIVYQGITTRILPLMKVDYTSTHLKSQIYIGSVNWSLLVAVIFIMILFQRSENLAAAYGLAVTGTMFITGIMMTMIFSRTTKKWKVPIALAVTVIDFAYLTANLHKLPHGGYWSLVLASIPLAIMVIWTRGQRALYRSLKPLDLDTFLLSYEQIYAKGHNIPGTGLFFVRETPVVPPYVIHCIIRSNIIYERNVFVSLTRTDEPFDVRTKLTRGIGTGLDAFEVNAGYMERLDIEKLLKKHGVEEKVIFYGIEDIDTSNPVWRIFATIKRQSANFVQFNKLPVSKLQGVVTRVEM
Transport of potassium into the cell.
Q74AA5
A4WGH1
MNME_ENT38
tRNA modification GTPase MnmE
Enterobacter
MSHNDTIVAQATPPGRGGVGILRISGLKAREVAEAVLGKLPKPRYADYLPFNDADGTALDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTLPGLRIAKPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSTRVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNTVMADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLRDASDEVERIGIERAWQEIEQADRVLFMVDGTTTSAVDPADIWPDFIARLPAKLPITVVRNKADMTGETLGLSDVNGHSLIRLSARTGEGVEDLRNHLKQSMGFETNMEGGFLARRRHLQALEAAANHLDQGKAQLLGAWAGELLAEELRLAQQSLSEITGEFTSDDLLGRIFSSFCIGK
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.
A4WGH1
Q8EHP1
LNT_SHEON
Apolipoprotein N-acyltransferase
Shewanella
MLTNIRAFAQQKSRLSALRLVLAFILGASTALSFAPYSLWIIYPIAMSLALWQSESLNPKASFFHWLSFGFGCFAVGISWVHVSMDTFGGLPLPASVALMALLALYLALYPALTGLGLAWFTRTNSHSLWRNLLLFPALWTLTEWARGWVLTGFPWIWAGYSQTEGPLKALASIIGALGLSFIIAMIAGALALCFSKRYKSLLILLPITAVAAWVAPKLSQIQPTGESVKVALVQGNIPQSMKWEPEALWPTLLKYMDLSREHFDADIIVWPEAAIPAPESMVQDFLDNANKVANLNHTSIITGIISRQQEDFYNSLIVLGNHNQKQQDNPDYESDGSNQFKKHHLLPIGEFVPFQALLRPIAPFFNLPMSSFARGDYLQPNLSALGHKVAPAICYEIAFPEQLRDSVNLGTDLLLTVSNDAWFGTSNGPLQHMEIAQMRAIELGRPLVRATNNGVTAVVDENGNITAALPQFETGVLSATIPLVTGQTWFAKIGQTPLLILCGALLLVGFIRRQKQQ
Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Q8EHP1
Q3AMP6
RS5_SYNSC
30S ribosomal protein S5
unclassified Synechococcus
MTDSSPQSNPNAVPGAADVPAAAEGQQQQEQRRGRGDRDGRRGDRRGGRRGQERDSEWQERVVQIRRVSKTVKGGKKMSFRAIVVVGNEKGQVGVGVGKAGDVIGAVRKGVADGKKHLVKVPLTRHNSIPTLSNGRDGAASVLIRPAAPGTGVIAGGSIRTVLELAGIKNVLAKRLGSKTPLNNARAAMVALSLLRTHKETAKERGISLEQIYS
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
Q3AMP6
Q80WT2
DMRT3_MOUSE
Doublesex- and mab-3-related transcription factor 3
Mus
MNGYGSPYLYMGGPVSQPPRAPLQRTPKCARCRNHGVLSWLKGHKRYCRFKDCTCEKCILIIERQRVMAAQVALRRQQANESLESLIPDSLRALPGPPPPGDAAATAATASQSSPASQASQPPAPPRPTAELAAAAALRWVAEPQPGTLPAQLAKPDLTEERVGDSSSTDNTAEAFSDKDTDQRSSPDVVKSKNCFTPESPEIVSVDEGGYAVQKNGGNPESCPDSPKYHAEQSHLLIEGPSGTVSLPFSLKANRPPLEVLKKIFPNQKPTVLELILKGCGGDLVSAVEVLLSSRSSAAGAERTAEESLVLPSSGHIFEHTLGSYPISSSKWSVGSAFRVPDTLRFSADSSNVVPNPLAVPLQHPFPQPPRYPLMLRNTLARNQSSPFLPNDVTLWNTMTLQQQYQLRSQYVSPFPSNSTSVFRSSPVLSSRTTEDPRISIPDDGCPIVTKQSIYTEDDYDERSDSSDSRILNTSS
Probable transcription factor that plays a role in configuring the spinal circuits controlling stride in vertebrates. Involved in neuronal specification within specific subdivision of spinal cord neurons and in the development of a coordinated locomotor network controlling limb movements. May regulate transcription during sexual development.
Q80WT2
C3MAX1
RL7_SINFN
50S ribosomal protein L7/L12
Sinorhizobium
MADLAKIVEDLSSLTVLEAAELSKLLEEKWGVSAAAPVAVAAAGGAAGGAAAAAEEEKTEFDVILTDAGANKINVIKEVRAITGLGLKEAKDLVEGAPKAVKEAVSKAEAADLKKKLEDAGAKVDVK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
C3MAX1
B1J1P0
COBS_PSEPW
Cobalamin-5'-phosphate synthase
Pseudomonas
MLPFWIALQFLSSLPVRLSGMPEPREMGRSLLCYPLVGLLFGLLLWLASHLLQGAPAPLHAALLLTLWVLLSGALHLDGLADSADAWLGGFGDRERTLKIMKDPRSGPIAVVTLVLVLLLKFCALWVLVERGAGALLVLAPVVGRAAMLGLFLGTPYVRPGGLGQALAEHLPRQTAGWVLLGSLLLCLLLGGWSAIWPMALALGVFLWLRRLMCQRLGGTTGDTAGAMLELLELTVVLGLALAT
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
B1J1P0
Q7VJR7
LUXS_HELHP
Autoinducer-2 production protein LuxS
Helicobacter
MPLLDSFKVDHTKMPAPAVRLAKTMQTPKGDTISVFDLRFTRPNCELLSEKGIHTMEHLIAGFMREHLNNTRVEIIDISPMGCRTGFYMSVVGAPNEYNVKEAWESSMRDVLRICDEKDIPELNIYQCGTAKMHSLKEAQDIAQVVLDKGVSVMNTQELLLKDFA
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).
Q7VJR7
B4M375
NFU1_DROVI
NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
Drosophila
MSKLISYAAKNTLRNTRLGANPICQHATRDYMHLAAASAARNTYSTPAVGFAKQPVLRQAVNTVAVMGQISRRSMFIQTQDTPNPESLKFLPGVDVLGKGNTYDFPSGSAAHCSPLAKLLFRVEGVRAVFFGGDFITISKEESGEWGLIKPEVFAVIMDFFASGLPVIHEARPNADTEILEDDDETVMMIKELLDTRIRPTVQEDGGDIVFMGYENGIVKLKMQGSCSSCPSSIVTLKNGVQNMLQFYIPEVESVEQVFDDADKMANKEFERFEKSLMQKESVNQPNAPVNIGGGTPN
Molecular scaffold for [Fe-S] cluster assembly of mitochondrial iron-sulfur proteins.
B4M375
D4D891
AMPP1_TRIVH
Prolidase
Trichophyton
MTIFRPHLRFLFKPHFLYFQSPAGQSSRPFSTSQILRTALDMPPPPVDTTQRLAKLRELMAQNKVDVYSMQFRYTIKAPLIITVVYSFFFFLLLALKLCLRKTAISQSTLLHVMGVETLIRITAAFISSFTGSAGCAIVSMSKAALSTDGRYFSQAAKQLDSNWTLLKRGVEGVPTWEEWTAEQAENGKVVGVDPSLITAGENLHYTPLTSVVVTNCSYVIADARKLSQTLKTTGGSLVGIDQNLIDAVWGNERPARPANQITVQPVERAGKPFEEKVEDLRKELAAKKRSAMVISTLDEIAWLFNLRGSDIPYNPVFFSYAIVTPSVAELYVDESKLSPEARKHLEGKVVLKPYDSIFQASKVLAESKASASSGSSGKFLLSNKASWSLSLALGGEQNVVEVRSPITDAKAIKNEVELEGFRKCHIRDGAALIEYFAWLENALIKEGAQLDEVDGADKLFEIRKKYDLFVGNSFDTISSTGANGATIHYKPEKSTCAVIDPKAMYLCDSGGQYLDGTTDTTRTLHFGEPTEFQKKAYALVLKGHISIDNAIFPKGTTGYAIDSFARQHLWKEGLDYLHGTGHGVGSFLYAEVPLSASNVLSNEPGYYEDGNFGIRLENLVICKEVQTAHKFGDKPFLGFESITLVPFCQKLLDASLLTEAERKWVNDYHARVWEKTSPFFEKDELTTAWLKRETQPI
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
D4D891
Q2YQ73
NDVA_BRUA2
Beta-(1-->2)glucan export ATP-binding/permease protein NdvA
Brucella
MSLLKIYWRAMQYLAVERTATITMCVASVLVALVTLAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIMAAVFVARGADRLAHRRRLGVMIDSYERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFAQLMIGRLDQISAFINQTVTARAKLEEFFQMEDATADRQEPENVADLNDVKGDIVFDNVTYEFPNSGQGVYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVTQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLLRAGGLKLEDKQPKQPVVEGSNVMPFPVKGAVA
Involved in beta-(1-->2)glucan export. Its export to the periplasmic space is required to exert its action as a virulence factor. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).
Q2YQ73
P02839
LCP1_DROME
Larval cuticle protein I
Sophophora
MFKFVMICAVLGLAVANPPVPHSLGRSEDVHADVLSQSDDVRADGFDSSLHTSNGIEQAASGDAHGNIHGNFGWISPEGEHVEVKYVANENGYQPSGAWIPTPPPIPEAIARAVAWLESHPPAPEHPRHH
Component of the larval cuticle.
P02839
A4VQN0
RS6_PSEU5
30S ribosomal protein S6
Pseudomonas
MRHYEIIFLVHPDQSEQVGGMVERYTKLIEEDGGKIHRLEDWGRRQLAYAINNVHKAHYVMLNVECSGKALAELEDNFRYNDAVIRNLIIRRDEAVTEQSEMLKAEENRSERRERRDRPDNTDGSNENDSDSDNNADE
Binds together with S18 to 16S ribosomal RNA.
A4VQN0
Q75A60
MKAR_ASHGO
Microsomal beta-keto-reductase
Eremothecium
MGSLSDISFFDHLQELARRDCCVNALLWCAFTVGAVKLTTFMLSLISIALETTVLPSASYKKYGARKGAYALVTGASDGIGKEFALQLASKGFNVLLVSRTEAKLLELKQEIMAKYKVDARVLSVDFGVDNRLTYTAISELCGELPVTVLVNNVGVSHSIPVSFLETTEEELRGIITVNNTATLMVTQTVAPLVIANARRLQCRGLVLTMGSFGGLLPTPLLATYSGSKAFLQAWSAALAGELAPHNVDVQIVLSYLVTSAMSKVRRASALIPTPRAFVRSTLASLGRRVGAQERYATCTPYWSHALYHFLIENTVGVHSRLANAINYRFHADIRKRALRKAARKAAEKQE
Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
Q75A60
E8Y6Y6
PAGP_ECOKO
Lipid A acylation protein
Escherichia
MNVSKYVAIFSFVFIQLISVGKVFANADEWMTTFRENIAQTRQQPEHYDLYIPAITWHARFAYDKEKTDRYNERPWGGGFGLSRWDEKGNWHGLYAMAFKDSWNKWEPIAGYGWESTWRPLADENFHLGLGFTAGVTARDNWNYIPLPVLLPLASVGYGPVTFQMTYIPGTYNNGNVYFAWMRFQF
Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors.
E8Y6Y6
A5EJU4
TRMFO_BRASB
Folate-dependent tRNA(M-5-U54)-methyltransferase
unclassified Bradyrhizobium
MIGAGLAGSEAAWQLAEAGVDVVLHEMRPDRMTEAHRTATPAELVCSNSFRSDDAANNAVGLLHAEMRRLGSLIMRAADANQVPAGGALAVDREGFSAAVATALNGHPRIELRRGEITGLPPSDWDNVIIATGPLTSQPLAEAIRDLTDETALAFFDAIAPIVHRDTIDMSKAWFQSRYDKVGPGGTGADYINCPMTKDQYDTFVAALLAGEKTDFKDWETNTPYFDGCLPIEVMAERGHETLRHGPMKPVGLTNPHNPTVKPHAIVQLRQDNKLGTLYNMVGFQTKLKYGPQQQIFRTIPGLENAEFARLGGLHRNTFLNSPKLLDAQLRLRAQPRLRFAGQMTGCEGYVESASIGLIAGLYAAAEARGTGLSPPPATTALGALLGHITGGHIETIDGATRSFQPMNINFGLFPPLAVAPTRKPDGSRLKGNEKTVAKKQALSARALADLDGWIAEHLRVAAAA
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
A5EJU4
Q0T4E8
RSXC_SHIF8
Rsx electron transport complex subunit C
Shigella
MLKLFSAFRKNKIWDFNGGIHPPEMKTQTNGTPLRQVLLAQHFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKMLPVHAPTSGTVTAIAPHSTAHPSALAELSVIIDADGEDCWIPRDGWVDYRSRSREELIERIHQFGVAGLGGAGFPTGVKLQGGGDKIETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSNDISLRVIPTKYPSGGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRHLLNDAGFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSANELGEPQEEQSCIRCSACADACPVDLLPQQLYWFSKGQQHDKATTHNIADCIECGACAWVCPSNIPLVQYFRQEKAEIAAIRQEEKRAAEAKARFEARQARLEREKATRLERHKSAAVQPAAKDKDAIAAALARVKEKQAQATQPIVIKAGERPDNSAIIAEREARKAQARAKQAELEQTNDAATVAEPRKTAVEAAIARSKARKLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQANAEPEEQVDPRKAAVEAAIARAKARKLEQQQANAEPEEQVDPRKAAVAAAIARVQAKKAAQQKVVNED
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR.
Q0T4E8
Q2YBK2
RL13_NITMU
50S ribosomal protein L13
Nitrosospira
MKTFSAKPHEVNREWFVIDAAGKVLGRLAAEIAHRLRGKHKPIYTPHVDTGDFIVVINVDKMRVTGNKAESKMYYRHSGYPGGIYETSFAKMHARFPGRPLEKAVKGMLPKGPLGYAMLKKLKIYAGAAHPHAAQQPRQLEVRA
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.
Q2YBK2
O82833
GELLY_BACSP
C-terminal gellan lyase
Bacillus
MRFSWKKLVSAALVMALLVGIVYPAASGRGAVASAASGTTVELVPTDDAFTSAVAKDANANGTWMQLKGSIGGQRYIYMKFDLTALAGVEADRIENAKVWLKKMGTNGTAMTVGLRAVDDTSWSESTLTWNNAPVYGSQVLSQQSVLSTPDVYYPFDLDEYLKTQLAAGKSKLAIAFVPISTLNENMEFYARESTANTPKLVVELKDEPPAPTGLMQLVQSFGGHNKGHLRVVEFDATPASTTGNGTVGITADGAAPAAAADFPIALRFGTDGTIKAANAAGFESKTPVNYTAGQKYHVKAMINLSLGTYDLWLTPPNAGQPVLLAADYAFAASAPALNDIGGVHATADAQSTDVPAVANARLIADHFVSKAPFKDEQGQSLAIRLESDNSLANRSYAIKFDMNLTGNPLETDALISYADRSVTLNGFPDLAYIVRSNFGNFDVRNDNVYASSHPSTAQSNRTYQVEVRINPASGTGQPTRTYDVWIAPEGEQPVQLADQFKARNYANTGYALNNIGQAFVYSQADGLLSIDNHVVQDGQRLDEALARVNAASGEAAMTAALESNALGLPMERYRLMDAAKRAQVAQDVLAGRPAEGYAHALSVQAVFVSAVANRLDTENPTAPANVQVAISNTMQAHVSWTASSDDTGILYYKVFRDGALVGTVTNATSFVDNGLAPATEYTYVVKAYDLVLKEAVSQPATATSPGEQAQVRIPFSAEAIATAFGQPLLDYNLETHSGTLKWVMEWREEYEKSANALKLLTLLSASAPDYIGPDGVTTASAKALQHLRSVTAGGNEPGFAGNGLSGQGYMPLLSAIVMAKKKAPAIWNALTAAEKEKLDLMILAGLYGAKFAYDDENDNKTGIDATGNFDKEWNPNHRSGIAGAIMAMYYFEDAQWLNDQMRSFNYDDWLARLTAAGLTNVRTIYQNSGKTLTEREIRKDAAGDGFVYKGHPLSQPGKIMAEFVNYTFSHPVSPVGGFDSGIGKYRGYIVDGQDDLPNLGADSMGFEFDTLDANGKRSSLVYVFMGWKPNVDAITPVLLLDNIDSGLTSAETRDVVSRLSIGTTDMLYKNEHGYMTYAKGVNEGVKSLNGPILTINEEIWNRILNNPAAPMEAVNQASSAGQMRTALEASALGMILYGYGALSETGKNAVAQHVLDARPAAGYANKAAAQNELYEGVRLQALLALSQAQTAEQMRSALESRALGLYKPKYETASQDKKQFVAQYLLDNKPADGFLTKTEVREQVESALEPQGNQLRNLPPLASGEKRINLADYDHWPQQHGDAEVALWADDKTGAFSLTIDDNFENEHDTWRSLAQQYGFKFSWFVITSLIKDPNKWRTLAAEGHEIGSHTVTHEDKGSTLDPAHLHSEYADSQALLNTIEGVRATTLAYPFGSGREDIAAEYYIAARGTVGLPNPADSINYMNTQSLSVRPGSLELTNQAANGNSVEAMVKTLVDPNHKVWSASYYRGWSNMLVHSLNESGKTPSDGVTRTSRDLTQYLLTLLDTYRDQIWVGRYGDIVRYSQQRDTAHIVVTRKDDRKITFNLTDRMDDTLFDYPLTVKVRVDDAWSDIGATQAGEPIPFVETIRDGKRYLLVKAVPDKGSVSIVPDAASPLNVVNGAVTSEQMLSAIAAPGLGLDLGEFNALGAGKKRMVGSRLLEVRPADGYADAAALQDALDAAVEEANNAPSLSENASLSDLKVNGVTIAGFAPETYAYDIMLPEGTTALPVVSFKVADTGKATAVLQNAPALPGTAKVTVTAEDNWTVATYTLRFQVRISALQRVNTAPDASAMRTAIENAALGLVLAAYNGLTSEQKNSVAASVLTHRPATGYADVQAVQAELNAALPKINAPLLAHAIVDQLNPDTVSTANWTNLYGGTSGRKGGVYMKFNIASLAGLEADAIGDAKVQFFTTREGTVIGYAAPSSWEAPLTWNTQPLADLKNSNMAALAEIGRTAVQATGANYEMNITQYVKDAAAADKTELSLVLLGSNNTNITMQKIPTAFALSVTLATYGEPNPEPSPLAAVNEAGDAAAMQGAIAAVELDLNLTAYNGLTAAQRIDVAQALLDNRPAAGYAHALAVQVALDAAVAAAQPANQAPGGTLAASAEQLQPGQQLELTVGVSDASRFTGADILVHYDPQALTFATELYEGVRMLKAEAIASLQANYQVAAAMAEQPGTIKILLFTAGAGQPLSGTLPLFKLRASVKDDAQTGVSTAVSLSDFELTFEGEDSVWPDTTRAAVSLQIAAHPVEADKTALIAKIAHAQALLTGATVGANPGQYPQAAYDALADAIGLAEEKRDLTGVSQAAVDEAVASLGTAEQQFLNAVIPGVPADLTALNAAIAKAQRLHDNGPYGEKIGQYPQSAKVPLKSALDAAKAVGGSGASSQESVNAAAASLNGAIQTFERSLVTLVGGGATKVGIRDLSIVAKYYGVTSSDPNWGKVSAAAIDGGNEITIEVLAAVARMILADWAAGQ
Cleaves the glycosidic bonds of gellan backbone and releases tetrasaccharide units of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the non-reducing terminal. The enzyme is highly specific to the heteropolysaccharide gellan, especially deacetylated gellan.
O82833
A7TQC5
GEP3_VANPO
Found in mitochondrial proteome protein 38
Vanderwaltozyma
MFVVRRSIVFQQSRRQFSGSIAWLQACSSCGIKLQSKNPALIGYYTKPKPLEVGKVETLEDVKYMLFSQDIQKIKEIEDGTTLEDEKNRIPHSLICKRCSDAVHQNKYDVMDFKNCSLKEVIRSVPNDKPIVSIASLPEFPFHVNKNILENEKESVLVFTKADQVLKTSSATSTRLPIFFKDYFKYHLGLQVNKVLAVSSLKKWNLSGLLSNLRNNSYFLGNPNVGKSTLMNSLIQRYNGTKLDFNSNISDDMVNDAQHKHLRKAQLAGVSHIPNLTRECQGYQVDKKRIYDLPGYSENVDELPLERIVKSNWLEWVRKTNLFDTKKVKKKPYITIKGTENGRCYTIGGLFFLQPPPYSINQIIKFIPGEPYIFKNVTRALETFKSVYGNDTPHPLEKYCGINDEYCDITKYQRHVIPPFQGSIEIVFKDIGYILLRSTGRYSFNGLYEIWVPKGISVCIREPLEKLIEEGYVQYTESKNKISSCPKGRPLVSSTYIMDPNEEDTFAKIREMYLDRTENEISVRRLVKEDPLEVVSNKHDTPPNLYWHYKW
May be involved in the mitochondrial lipid metabolism.
A7TQC5
B5F4R7
XNI_SALA4
Flap endonuclease Xni
Salmonella
MAAHLLIVDALNLIRRIHAVQGSPCVETCQHALDQLIIHSQPTHAVAVFDDDARSSGWRHQRLPDYKAGRPPMPDDLHNEMPALRAAFEQRGVRCWASDGNEADDLAATLALKVTEAGHQATIVSTDKGYCQLLSPGLRIRDYFQKRWLDAPFIEKEFGVLPRQLPDYWGLAGISSSKVPGVAGIGPKSATQLLIQFQNLEGIYAHLDEVPEKWRKKLETHKEMAFLCRDIARLQTDLHIDGNLQQLRLAR
Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment.
B5F4R7
A7N0Y5
ATPF1_VIBC1
F-type ATPase subunit b 1
Vibrio
MNINATLLGQAISFALFVWFCMKYVWPPLMQAIEERQKKIADGLQAAERAAKDLDLAQANASDQMKEAKRTATEIIDQANKRKSQIIDEAREEAQAERQKILAQAEAELEAERNRARDELRKQVATLAVAGAEKILERTIDKDAQKDILDNITAKL
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
A7N0Y5
B9DFZ0
NTH2_ARATH
Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 2
Arabidopsis
MILTGAASTFPIVARVLNAMNRRMYAATTLSSAKSISAESLNLRSDSNSEAAHGASESETRVSLRKKRIKQDDLEPVKKCSARETKARKDMCGLPDIEDSPYKKTNGTASSRTRKLNSYIKSTEASPSASSIKTAGLGIPPENWEKVLEGIRKMKPSEEAPVNAVECDRTGSFLPPKERRFYVLIGTLLSSQTKEHITGAAVERLHQNGLLTPEAIDKADESTIKELIYPVGFYTRKATNVKKVAKICLMEYDGDIPRTLEELLSLPGVGPKIAHLVLHVAWNDVQGICVDTHVHRICNRLGWVSKPGTKQKTSSPEETRVALQQWLPKGEWVAINFLLVGFGQTICTPLRPHCGTCSITEICPSAFKETPSTSSKLKKSIKSKKL
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
B9DFZ0
Q87Z79
HGD_PSESM
Homogentisicase
Pseudomonas
MAIHSSFEALAYQSGFANQFSSEALPGALPMGQNSPQKHPLGLYAEQFSGTAFTVARNEARRTWLYRIKPSAAHPRYQRMDRQITGREQGPINPNRLRWNAFDIPAEPVDFIDGLIALASTSAADQAEGVSVYVYAANTSMQRAFFSADGEWLIVPQQGRLRIITEMGVLDIGPLEIAVLPRGLKFSVQLLDGSARGYLCENHGGVLRLPELGPIGSNGLANPRDFLTPVAWFEERDEPVQLVQKFLGELWTTQLQHSPFDVVGWHGNNVPYTYDLRRFNTIGTVSYDHPDPSIFTVLTSPGAVHGQANIDFVIFPPRWMVAENTFRPPWFHRNLMNEFMGLIDGAYDAKAEGFMPGGSSLHNCMSAHGPDNITAEKAIAADLKPHKIENTMAFMFETGKVLRPSLHALACPQLQADYDACWNGMARTFNKESS
Involved in the catabolism of homogentisate (2,5-dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate.
Q87Z79
Q5X4K3
ASTB_LEGPA
N-succinylarginine dihydrolase
Legionella
MNAYELNMDGLVGQTHHYAGLSSGNIASTNNALSISNPQAAARQGLEKMRQLYNMGLKQGLLPPHQRPNLNLLYQLGFKGSPSEQINKAYKTAPELLSACYSASSMWTANAATVSASVDTEDNKVHFTAANLISNLHRHQEADFSKKLLEFIFSNSDYFNHHPLLPKSMGTSDEGAANHNRLCQSHAHSGINLFVYGKKVLGNHQFEQSPIKYPARQTKEASEAIARNHLLNPERVIFACQNPLAIDQGVFHNDVISVANEHVFLVHEEAFYNQAYVLDQLKEKADFPLVIIQISKEQISVSEAVDTYLFNSQLITLPDQKNMILIAPAECQANLKVKTCIDGLVADSQNPINSVYYLDLKQSMRNGGGPACLRLRVPLNDYELKAMHQGILIDNDLLDILDKWVLKYYRTELKISDLADPQLLYECLDALDELTQILKLGSIYPFQS
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
Q5X4K3
Q6AZR3
DHSDA_XENLA
Succinate-ubiquinone reductase membrane anchor subunit A
Xenopus
MVTVLRLSSLCRANRASAFKSLLIRPVPCLSQDLHTVQTSQIHTSQNHHAASKAASLHWTSERALSVALLGLLPAAYLYPGAAVDYSLAAALTLHGHWGLGQVVTDYVHGDAKIKLANTSLFALSALTFAGLCYFNYHDVGICKAVAMLWSL
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Q6AZR3
Q2JD90
APT_FRACC
Adenine phosphoribosyltransferase
Frankia
MTSIDDAPQRSAAHDAVAEVLRGHIRDIPDWPQPGVVFKDITPLLATPTAFGVVIGALADAARALGATTIAGIEARGFLLAAPVADRLGTGLVPIRKQGKLPGPTRSASYDLEYGAATIEIHADAVHDGDRVLLVDDVLATGGTAAAAHSLLAAGGGEVVGLAVLMELSFLPGRDRVAPLDVVSLLTI
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Q2JD90
B3NVC6
T23O_DROER
Tryptophanase
Sophophora
MSCPYAGNGNDHDDSAVPLTTEVGKIYGEYLMLDKLLDAQCMLSEEDKRPVHDEHLFIITHQAYELWFKQIIFEFDSIRDMLDAEVIDETKTLEIVKRLNRVVLILKLLVDQVPILETMTPLDFMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFSDEEARNSIRNSEKDPSLLELVQRWLERTPGLEESGFNFWAKFQESVDRFLEAQVQSAMMEPVEKAKNYRLMDIEKRREVYRSIFDPAVHDALVRRGDRRFSHRALQGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRMIGSQQLGTGGSSGYQYLRSTLSDRYKVFLDLFNLSTFLIPREAIPPLDETIRRKLVHKSV
Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
B3NVC6
B0S0I2
RS12_FINM2
30S ribosomal protein S12
Finegoldia
MPTINQLVRQGRKSKTYKSDSPALSRNFNSIKKSYTEANSPQKRGVCTSVRTMTPKKPNSALRKVARVRLTNGMEVLSYIPGIGHNLQEHSVVLIRGGRVKDLPGVRYHIVRGALDTAAVQNRMQGRSKYGAKKPKK
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
B0S0I2
Q1I7T4
RNH_PSEE4
Ribonuclease H
Pseudomonas
MSDSVEIYTDGACKGNPGPGGWGVLMVFKGVEKELWGGERETTNNRMELMAAIEGLKALKRECEVVLTTDSQYVMKGINEWMVNWKKRGWKTAAKEPVKNADLWMALDEQVNRHKVTWKWVRGHIGHPGNERADQLANRGVDEVRAQR
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Q1I7T4
Q10252
COQ2_SCHPO
p-hydroxybenzoate polyprenyl diphosphate transferase
Schizosaccharomyces
MEMALLPQPSPARYFLRTPSWSAVAIFQAVKIKPLQLRTNSSNSVTPNLISPSKKSWKDLFSKRWQYYAEISRAGSPTGTYLLYSPCTWSILMAAYAYDSSLVNVTKMLALFGVGSFLMRSAGCVINDLWDRELDAKVERSKSRPLASGKLSVRQAISLLSVQLTASLGILLQLNPYTIKLGVASLVPVCIYPAMKRITYYPQVVLGLTFGYGAVMGWPALAGEACMNWSVVAPLYLSTISWIVLYDTIYAHQDKRDDVKANIYSTALRFGDNTKPVLCGLAALQIATLATAGIMNGQGPVFYTLGVAGAAYRLSSMIYKVDLDDPKDCFRWFKRNSNTGYLVAAAIALDWLAKSFIYDS
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Q10252
Q9Z959
SYM_CHLPN
Methionyl-tRNA synthetase
Chlamydia
MPQKVLITSALPYANGPLHFGHIAGVYLPADVYARFRRLLGDDVLYICGSDEFGIAITLNADREGLGYQEYVDMYHKLHKDTFEKLGFALDFFSRTTNPFHAELVQDFYSQLKASGLIENRISEQLYSEQEQRFLADRYVEGTCPRCGFDHARGDECQSCGADYEAIDLIDPKSKISGVELVKKETEHSYFLLDRMKDALLSFIQGCYLPDHVRKFVVDYIEHVRSRAITRDLSWGIPVPDFPGKVFYVWFDAPIGYISGTMEWAASQGNPDEWKRFWLEDGVEYVQFIGKDNLPFHSVVFPAMELGQKLDYKKVDALVVSEFYLLEGRQFSKSEGNYVDMDKFLSSYSLDKLRYVLAATAPETSDSEFTFLDFKTRCNSELVGKFGNFINRVLAFAEKNHYDKLSYHSVVLEDSDRAFLEEVRQLVRDAEKCYREYSLRKATSVIMSLAALGNVYFNQQAPWKLLKEGTRERVEAILFCACYCQKLLALISYPIIPESAVAIWEMISPKSLENCNLDTMYARDLWKEEILDVINEEFHLKSPRLLFTTVE
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Q9Z959
Q9KLG8
PXPA_VIBCH
5-oxoprolinase (ATP-hydrolyzing) subunit A
Vibrio
MSKRTIQLNCDMGESFGVWTMGADEEVMPWIDMANIACGFHASDPHVMSRTIDLALEHEVMIGAHPSYPDLQGFGRRSLAMNEQEVSEIILYQVGALKALCESKNGQLSYVKPHGALYNDMMSDPSIFRAVVDAVSCFNLPLMVLASANNQDYLDIADRFDVPLLFEAFADRTYLANGKLTPRSQPNAVLSSEEAILNQVRQIARYGKVTSSDGFVIPIEADTLCVHGDNPNAVSLIARIRAALDE
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Q9KLG8
B4F114
MRAY_PROMH
UDP-MurNAc-pentapeptide phosphotransferase
Proteus
MLVWLAEYLVKYHTFFNVFSYLTFRAIVGLLTALIIALWMGPHLIAWLQKMQIGQVVRNEGPESHFSKRGTPTMGGIMILFSIAVSTLLWARLDNPYVWCVLLVLIGYGIIGFIDDYRKVVRKDTRGLIARWKYFWQSVLALAVAFSMYAIGKDTPATQLVVPFFKDVMPQLGMLYILLAYFVIVGTSNAVNLTDGLDGLAIMPTVFVAAGFALVAWATGNVNFASYLKIPYLMHAGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGTIAVLLRQEFLLVIMGGVFVVETLSVILQVGSFKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISLMLVLIGLATLKVR
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
B4F114
A8AYH0
GLGA_STRGC
Starch [bacterial glycogen] synthase
Streptococcus
MKILFVAAEGAPFSKTGGLGDVIGALPKSLVKHGHQVGVILPYYDMTDAKFGDQVEDLFYFEVSVGWRRQYVGVKRLVLNGVSFYFIDNQHYFFRGHVYGDFDDGERFAYFQLAAVELMERIDFIPDVLHVHDYHTAMIPFLVKEKYHWIQAYRNIKTVLTIHNLEFQGQFPDSMLWELFGVGYERYADGTLRWNDCLNWMKAGILYADRVTTVSPSYAGEIRTPEFGCNLDQILRMESGKLVGIVNGIDTEIYNPETDPLLAHHFDKSDLSGKLENKRALQERVGLPVRDDVPLVGIVSRLTRQKGFDLVVEELHNFLQQDVQIILLGTGDPAFEQAFAWFGQAYPDKLSANILFDVGLAQEIYAASDIFLMPSRFEPCGLSQMMAMRYGTLPLVHEVGGLRDTVEPYNVYTGQGTGFSFNNFSGYWLSWTFKEALNLYTHDKEAWKSMQEQAMERDFSWDTASLAYSDLYQSLL
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
A8AYH0
C5CGI1
KAD_KOSOT
Adenylate monophosphate kinase
Kosmotoga
MNIILLGPPGAGKGTQAKKIAMRYGIPHISTGDMLREAVAAGTELGKKVKEIIEKGLLVPDDLMVAIVEDRLKKPDSAKGFILDGFPRTVQQAESLSGILGNLGKELDAVILIDAPEEVVVERISSRRVCPSCGKVYNLLTIKPKNDMLCDDCNIGLIQREDDKPATVRERYRVYMEKTAPVINYYSEHGSLITIDGSLDIEAVTEEIFKNLENL
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
C5CGI1
A8FSD6
RNC_SHESH
Ribonuclease III
Shewanella
MEPIKNMPRLCRTLGYEFNDQSLLEHALTHRSASSKHNERLEFLGDSILSIIISDALFHQFPKATEGDLSRMRATLVCGKMLAEIGFEFKLGDYLNLGPGELKSGGFRRESIIADAVEAIIGAVYIDSGVEKCRCLVLSWYESRLAIIQPVNQKDPKTLLQELLQGFKKPLPVYKVIDIKGEAHAQTFTVECYVEELSKPVIGIASSRRKAEQLAAADALELMKR
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.
A8FSD6
Q6HKA1
ILVC2_BACHK
Ketol-acid reductoisomerase type I
Bacillus cereus group
MKTYYEQDANVGLLQGKTVAVIGYGSQGHAQAQNLRDSGVEVVVGVRPGKSFEVAKADGFKVMSVSEAVRTAQVVQMLLPDEQQAHVYKAEVEENLREGQMLLFSHGFNIHFGQINPPSYVDVAMVAPKSPGHLVRRVFQEGNGVPALVAVHQDATGTALHVALAYAKGVGCTRAGVIETTFQEETETDLFGEQAVLCGGVTALVKAGFETLTEGGYRPEIAYFECLHELKLIVDLMYEGGLTNMRHSISDTAEFGDYVTGSRIVTDETKKEMKRVLTEIQQGEFAKKWILENQAGRPTYNAMKKAEQNHQLEKVGEELREMMSWIHAPKELVKK
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Q6HKA1
Q9WUP1
RAMP3_MOUSE
Receptor activity-modifying protein 3
Mus
MKTPAQRLHLLPLLLLLCGECAQVCGCNETGMLERLPRCGKAFADMMQKVAVWKWCNLSEFIVYYESFTNCTEMETNIMGCYWPNPLAQSFITGIHRQFFSNCTVDRTHWEDPPDEVLIPLIAVPVVLTVAMAGLVVWRSKHTDRLL
Plays a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a GPER1-dependent manner. Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL.
Q9WUP1
Q9XX11
ACKMT_CAEEL
ATP synthase subunit C lysine N-methyltransferase
Caenorhabditis
MGMNTGLVIAGVAGATALAISAAAIPFVAPALRRVCIPYVPATTEQLANVSRALSLATSSNSNKKGTLIDLGSGDGRVVLQCAREGFNSTGVELNSILVAYSKYRSIREGLGKETRFMRKNIFKTDLNPYQTAVIFGAESLMGDLVPKLSEMRSNTNLLACRFPLPENDAWKLEHQIGEGIDAVWVYKRN
Mitochondrial protein-lysine N-methyltransferase that trimethylates ATP synthase subunit C. Trimethylation is required for proper incorporation of the C subunit into the ATP synthase complex and mitochondrial respiration.
Q9XX11
A6QB58
ATPE_SULNB
F-ATPase epsilon subunit
unclassified Sulfurovum
MELMKLEIVTPNGVIFDDDVKQVTLPGSEGEFGVLPKHATLVSLLDTGVIVIEKADGSEVAVAINSGYVKVDEEKTTCIVDGAVALSGEDSDLAKALEEAKELIKKAESSSVAIASAVSKVEQIGKSF
Produces ATP from ADP in the presence of a proton gradient across the membrane.
A6QB58
P41829
NHR6_CAEEL
Steroid hormone receptor family member cnr8
Caenorhabditis
MEQLSIQTDELQDQFSNCSPASVDSSYSSCSSVEDEIEIYTRLVRNEEPLRRDFFREMSKNSSCSSSFDYGEFGPSSSSRKGSKTTDADLDSLFHSLVETSDQVNTVPKPTKTEVESIPEEFEQKPSSSSHRLPSEMNASITHIKSELDPTMQAFQMPHNDLFLATAAPHYNPFALSNDFMPNPLMPSFTSPFYPQHFPVSDSRRGSQGTTSSSNNTGGTPSPHSSSLPTSPPQLQGFLRSFLNPDNLSTPTSFGVPSETALDADKMCAVCNDRAVCLHYGARTCEGCKGFFKRTVQKNSKYTCAGNKTCPIDKRYRSRCQYCRYQKCLEVGMVKEIVRHGSLSGRRGRLSSKTKLARSEDQPSPPLPLLALMGKAIEDHTNMTVVRQFMQPFDETIALRILHGELHATKKLLMAMPQISEIQPADFQILLSRSFFAIMAIRVANRCGNSTDTIMFESGELFSLNAFPACFQQIIRFMVDKARTFSSLVDWEPQAFAAFIALQFLAGNTEHNVLGLTNKPLVDQVQSTIINALKDHCSGSQNKLAKIVRLTQEFDVFHALGLQALDILYPSHQLPEEFMFLINLTRAPLRSTDAPPACGSPVAPSGSSLFNFQMGPAAF
Transcriptional activator that induces gene expression by binding to the NGFI-B response element (NBRE) 5'-AAAGGTCA-3' . Required for proper morphogenesis of the spermatheca and the spermatheca-uterine valve formation . Promotes cell proliferation and differentiation of the spermatheca precursor cells during spermatheca development in larval stage L4 . Might play a role in promoting G1/S phase progression in the spermatheca precursor cell lineage . Also required for the differentiation of the spermatheca-uterine junction core (sujc) cells which are generating the spermatheca-uterine valve .
P41829
B8CJF9
CCA_SHEPW
Phosphatase
Shewanella
MKIYLVGGAVRDSLLELPIKDRDYMVVGATPEQMLAQGYKQVGKDFPVFLHPKTQQEYALARTERKTAAGYGGFSVDAAPNVTLEQDLLRRDLTINAIAQDDQGNRYDPFNGIADLNARLLRHVSDAFIEDPLRVLRVARFAARFHSLGFNIAAETMALMTKISQSGELEALTAERVYIELDKSLTSDAPQVFFSVLKECGALAVLFPEIDALFGIPQPEQWHPEIDSGVHTLMVLEQAAKLSNDNAVRFASLVHDLGKALSPKASLPKHHGHGQKGLPLIKALCERFRVPNEYRDLALLVSDQHQNIHNAHELRADTIVKLFDKADFWRKPHRLEQLLLSCEADAKGRTGFELSPYPQASYIQQCFKAASNVSVKDIIDAGYKGAEIRQQLTSSRVEAVQEIKLNLE
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.
B8CJF9