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2.75k
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5.51k
AlphaFoldDB
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O09345
P3H2_STRSQ
Proline 3-hydroxylase type II
Streptomyces
MRSHILGKIELDQTRLAPDLAYLAAVPTVEEEYDEFSNGFWKHVPLWNASGDSEDRLYRDLKDAAAQPTAHVEHVPYLKEIVTTVFDGTHLQMARSRNLKNAIVIPHRDFVELDREVDRYFRTFMVLEDSPLAFHSNEDTVIHMRPGEIWFLDAATVHSAVNFSEISRQSLCVDFAFDGPFDEKEIFADATLYAPGSTPDLPERRPFTAEHRRRILSLGQVIERENFRDILFLLSKVHYKYDVHPSETYDWLIEISKQAGDEKMVVKAEQIRDFAVEARALSERFSLTSW
Dioxygenase that catalyzes the 2-oxoglutarate-dependent selective hydroxylation of free L-proline to cis-3-hydroxy-L-proline (cis-3-Hyp).
O09345
Q8CVR2
NANM1_ECOL6
Sialic acid epimerase 1
Escherichia
MITMKVKNFIYLPFCLFIGTSVAGALPEIPEPFKYGVGGIENGKIYIGLGSLGNNWYMIDTNQSEKKWTKIAQWPTVPREQATATIIDGKIYVFGGIGKDTSGVITLQKDVYSYDIAKDKWEKLMTRPPVSLAGHVSFIHNGHAVSTGGVNENIFNGYFSDVELSKGNSALTEKVNRDYFSKPADDYFLNNHIISYDPSKNQWKNLGTTPFPGTAGSSVIFAEQQIYILGGERKPGLRSVRSWTGELSHDRIKWSELPPVASPEGVSGAYASVIDGNIFLAGGAYFPGAAEKYSNGEYWSHKGLDKAYSKEIYQLIKNDWKKVGSLPEGLAYGVSLPWQGGMLILGGEKKDGKAVSDVIYLKKNDKQIKIVK
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.
Q8CVR2
P80041
DDC_PIG
DOPA decarboxylase
Sus
MNASDFRRRGKEMVDYMADYLEGIEGRQVYPDVQPGYLRPLIPATAPQEPDTFEDILQDVEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLQLPEAFLAGEAGEGGGVIQGSASEATLVALLAARTKVVRRLQAASPGLTQGAVLEKLVAYASDQAHSSVERAGLIGGVKLKAIPSDGKFAMRASALQEALERDKAAGLIPFFVVATLGTTSCCSFDNLLEVGPICHEEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKRRTDLTGAFKLDPVYLKHSHQGSGLITDYRHWQLPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVQLSHEFEAFVLQDPRFEVCAEVTLGLVCFRLKGSDGLNEALLERINSARKIHLVPCRLRGQFVLRFAICSRKVESGHVRLAWEHIRGLAAELLAAEEGKAEIKS
Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin.
P80041
Q5L3V8
RSMA_GEOKA
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
Geobacillus thermoleovorans group
MYKDIATPGRTKEILERYGFSFKKSLGQNFLIDANILRKIVDVADISPDTGAIEIGPGIGALTEQLARRAKKVVAFEIDGRLLPILADTLSPYDNVRIFHQDVLKADLHAVIAEELADVSDRMVVANLPYYVTTPIIMKLLTERLPIRGMVVMLQKEVADRLAAKPGTKDYGSLTIAVQYYTEAEVIMTVPRTVFMPQPNVDSAVIRLVKRQHPPVVVDDEGVFFQVVRASFAQRRKTLFNNLTNNLPGGKENKEQIERVLVALGIDPRRRGETLDIAEFASLSNALAPLFGK
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.
Q5L3V8
Q803K4
SETD6_DANRE
SET domain-containing protein 6
Danio
MATEAKRPKTGDEKSVLEPLNNFLLWCESVQLTLSDKVYLSKEGTAAEYGMLAKEDIEEGHVLFTIPREALLHQGTTKVKKVLEEGKKCLESASGWVPLLLSLMYEYTSSTSHWKPYLSLWPDFRTLDQPMFWSEEECDKLLKGTGIPESVITDLRKLQDEYNSVVLPFMKSHPDLWDPEKHNLELYKSLVAFVMAYSFQEPVEDDDEDEEDDEKKPNLPMMVPMADMLNHISKHNANLEYTPECLKMVSIRRIGKGEEVFNTYGQMANWQLLHMYGFAEPFPNNINETADIKMASVYKAAAQVARSEANQQLLEDKWKMLCEMEVVGEKGVFIFGQSGSLTYHELYTTLKVLCMSSQIFEDFRENEGWEEDDEDDDDKMEQDLSFEGLASLSVEWKRLLCVAATETLDSYNEDVETDRRLMEDQRALAELSSRERRALYVRLGQKNILQRIQQLTKPAS
Protein-lysine N-methyltransferase.
Q803K4
Q2NFZ3
RS13_METST
30S ribosomal protein S13
Methanosphaera
MAEQEFRHMVRITRKDVDGNSTIATALTEIRGIGKAFAIAICKVLDLDQDAQIGYIDDESVKQIEAVLENPQEFGIPEWFLNRRNDYETGETKHLIESDLNMTLRDDLNRMKMIRSYKGKRHEVGLPVRGQRTKSTFRHGSSVGVSRTRPTGN
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.
Q2NFZ3
A0A0B5A051
PT1L_HUMLU
Humulus lupulus prenyltransferase-1-like
Humulus
MELSSVSSFSLGTNPFISIPHNNNNNLKVSSYCCKSKSRVINSTNSKHCSPNNNNNNNTSNKTTHLLGLYGQSRCLLKPLSIFSCKDQRGNSIRASAQIEDRPPESGNLSALTNVKDFVSVCWEYVRPYTAKGVIICSSCLFGRELLENPNLFSWPLIFRALLGMLAILGSCFYTAGINQIFDMDIDRINKPDLPLVSGRISVESAWLLTLSPAIIGFILILKLNSGPLLTSLYCLAILSGTIYSVPPFRWKKNPITAFLCILMIHAGLNFSVYYASRAALGLAFVWSPSFSFITAFITFMTLTLASSKDLSDINGDRKFGVETFATKLGAKNITLLGTGLLLLNYVAAISTAIIWPKAFKSNIMLLSHAILAFSLFFQARELDRTNYTPEACKSFYEFIWILFSAEYVVYLFI
Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the first prenylation step in the beta-bitter acid pathway . Uses dimethylallyl diphosphate (DMAPP) as the prenyl donor .
A0A0B5A051
P31304
MTSA_STRSA
Saliva-binding protein
Streptococcus
MKKLGFLSLLLLAVCTLFACSNQKNASSDSSKLKVVATNSIIADITKNIAGDKIDLHSIVPVGKDPHEYEPLPEDVKKTSQADLIFYNGINLETGGNAWFTKLVKNANKEENKDYYAVSDGVDVIYLEGQSEKGKEDPHAWLNLENGIIYAQNIAKRLIEKDPDNKATYEKNLKAYVEKLTALDKEAKEKFNNIPEEKKMIVTSEGCFKYFSKAYNVPSAYIWEINTEEEGTPDQIKSLVEKLRKTKVPSLFVESSVDDRPMKTVSKDTNIPIHAKIFTDSIADQGEEGDTYYSMMKYNLDKISEGLAK
Part of an ATP-driven transport system for manganese. Also acts as an adhesin which is involved on adherence to extracellular matrix. It is an important factor in the pathogenesis and infection. It may contribute to the formation and accumulation of dental plaque.
P31304
B0XZT4
IELA_ASPFC
Elastase inhibitor AFLEI
Aspergillus subgen. Fumigati
MKFSLACLLALAGLQAALADPATCEKEAQFVKQELIGQPYTDAVANALQSNPIRVLHPGDMITMEYIASRLNIQVNENNEIISAHCA
Elastase inhibitor.
B0XZT4
Q56017
APAG_SALTY
Protein CorD
Salmonella
MINSPRVCIQVQSVYIEAQSSPDDERYVFAYTVTIRNLGRAPVQLLGRYWLITNGHGRETEVQGEGVVGVQPRIAPGEEYQYTSGAVIETPLGTMQGHYEMIDENGDAFTIDIPVFRLAVPTLIH
Not known; mutations in apaG/corD give a phenotype of low-level Co(2+) resistance. They also decrease Mg(2+) efflux but not influx via the CorA Mg(2+) transport system.
Q56017
Q0T8K2
RLMC_SHIF8
23S rRNA(m5U747)-methyltransferase
Shigella
MQCALYDAGRCRSCQWITQPIPEQLSAKTADLKNLLADFPVEEWCAPVSGPEQGFRNKAKMVVSGSVEKTLLGMLHRDGTPEDLCDCPLYPASFAPVFAALKPFIARAGLTPYNVARKRGELKYILLTESQSDGGMMLRFVLRSDTKLAQLRKALPWLHEQLPQLKVITVNIQPVHMAIMEGETEIYLTEQQALAERFNDVPLWIRPQSFFQTNPAVASQLYATARDWVRQLPVKHMWDLFCGVGGFGLHCATPDMQLTGIEIAPEAIACAKQSAAELGLTRLQFQALDSTQFATAQGEVPELVLVNPPRRGIGKPLCDYLSTMAPRFIIYSSCNAQTMAKDIRELPGYRIERVQLFDMFPHTAHYEVLTLLVKQ
Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA.
Q0T8K2
Q48LZ4
ISPG_PSE14
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
Pseudomonas
MHGESPIKRRESRKIWVGSVPVGGDAPIAVQSMTNSDTNDVAATVAQINRLEAAGVDIVRVSVPDMDAAEAFGRIKQLVKVPLVADIHFDYRIALRVAELGVDCLRINPGNIGREDRVRAVVDAARDRGIPIRIGVNAGSLEKDLQKKYGEPTPEALVESALRHVEHLERLNFQDFKVSVKASDVFMAVAAYRLLAKQIVQPLHLGITEAGGLRSGTVKSAVGLGMLLAEGIGDTIRISLAADPVEEVKVGYDILKSLRLRSRGINFIACPSCSRQNFDVVKTMNELEGRLEDLLVPLDVAVIGCVVNGPGEAKEAHIGLTGGTPNLIYIDGKPAQKLTNDNLVDELERLIREKAAEKAEADASVIVRG
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Q48LZ4
Q4A5Q7
THII_MYCS5
tRNA 4-thiouridine synthase
Mycoplasmopsis
MYKKILIRYGELVLKGKNRTTFIKQLGSNIKEILNTEYEMEFDRMYIPYSEENLKNLKYVFGISSFSPVIETNKNLEDIQSAITKLINKNASTFKIAARRNDKSFELNSDQLNNLLGGFVLKNSHLKVNVKNPDQIFNIEIRKNSVYVFDKSINGIGGIPVGISGKVLHLISGGFDSPVAAYLLMKRGFKVDFLTFVTPPQTDETTIDKIKNLTKVLSRYQKESNLYVCDFSLISSYIEFTEFKSFKIILMRRSFYRIASELAKQNEILMISNGENLAQVASQTNESMAVIGSSIKNEILRPLLTYDKNEIINLSKVIETHDISILKSKEACELFAPKNPVTKPTEAKTLRIESKLDELKTYEEIVLNQKMKKFAI
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
Q4A5Q7
A9VY49
SYS_METEP
Seryl-tRNA(Ser/Sec) synthetase
Methylorubrum
MHDIRAIRENPEAFDRDLERRGLAPLSAELIALDDARKGAVSAAQAAQERRNALSKEIGAAKKAKDEARATELMAEVARLKEEAPGLEAAQGEAAKALDERLAAIPNRPKDDVPPGADEHGNVEYRRFDSSRERLAQGRQHFELGEATGLMDFEAAAKLSGSRFVVLKGQLARLERALGQFMLDLHTGEHGYTEVVPPVLVREEAMFGTAQLPKFRDDQFAAGENFWLIPTAEVPLTNLVRESILAEDELPLRFTALTPCFRAEAGAAGRDTRGMLRQHQFNKVELVSITAPEKSAEEHERMLACAEAVLQKLDLTYRVMTLCTGDMGFASQKTYDIEVWVPGQQTYREISSCSVCGEFQARRMNARYRAKEGRGVGFVHTLNGSGVAVGRALIAVMENYQNPDGSVTIPSALQPYMGGLTRIEGPKN
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
A9VY49
A5CYD0
TAL_PELTS
Probable transaldolase
Pelotomaculum
MKLFIDTANIEEIREAYALGIICGVTTNPSLIAREGRNFAQVVREIAAIVDGPISAEAVSPDAAGMIAEAEELSSIHPNIVVKIPMTAEGLKAVKILAQKGIRTNVTLIFSANQALLAARAGASYVSPFVGRLDDVSQDGAALIYDIMEIFERHCIRTEVIAASIRHPVHVTMAAKAGAHIATVPYKVLMQMIGHPLTEAGIKKFLEDWEKVKDK
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
A5CYD0
Q86I79
PSCA_DICDI
Penicillin-sensitive carboxypeptidase A
Dictyostelium
MKNYKIITLLLIISILFNIIRSNKISLKDSDSGSNGNQDIQILINDILNNCSSSESSSCFGTQWGVVADIYTPSNGEFTNIFSLNELQAFTPASNTKLFTTISIFYTFGEDFKVFTPFFTDKPFNSVSGGSSNSELDFICVKGMGDPSMSIDNLIEAAKFFSSNPTMKKVNKLLLDTSFYNIGNGVDGNIPSAWEWEDLTSTYGSIPTPLIINENTMDIYITPSNVIGGKPTASFKYSGEDKYLPVIILATTTTTSNSSTSTLNYSFKMSSQSIYITGNCDINGGIQIITVPILDPEQYFLTVFSALLEDGGVEISQTAIGSCNYTGMDYKSFEVISPELSEMLNYTLLTSNNLYAETFLRQMGTFNSAASESTPTYQAGLEYIQQTLSIPTSLYTQVDGSGLSRNNFITPKSLITVIENVYTNVGDPQHDYISYLPVASLSGTLSKRFINTPASGIVHAKTGSMTGVNSLTGVILPNGLSDDQQNSIFFSIIANNSPAQNTDIIDIIDQIVILLTKFILSS
Carboxypeptidase.
Q86I79
A0T0Z4
RPOA_THAPS
Plastid-encoded RNA polymerase subunit alpha
Thalassiosira
MNSSNLLMECIKSEKIESGPMYGQFLIDSLSSGQGITIGNLLRRVLLGDLQGTAITGVRIAGVKDEFSLIPGVREDILEILLNLKGIVLKSKTPNRQFGRLRLQGPAVITASSIQLPPEIEIINPNHYIATISSSHILEIEFKIESGSKYRLANELFSDKFEDFIETDAIFMPVQKVDFKVENVYDNSNNIKERLLIDIWTNGSISPEQAIFSGSNLIINLFKSIGEQKINKEKENIKEKNHIKPIDPYTHIAIEELQLSVRPYNCLKRAQINTIGDLLDYSPEKLLELKNFGRKSADEVFATLKNKLGIVLK
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
A0T0Z4
Q2SJE4
AROC_HAHCH
5-enolpyruvylshikimate-3-phosphate phospholyase
Hahella
MSGNTFGKLFTVTTFGESHGLALGCIVDGCPPGLPLTEEDLQVDLDRRKPGTSRHTTQRREPDQVRILSGVFEGKTTGTPIGLLIENTDQKSKDYSNIKDQFRPAHADYAYWHKYGVRDYRGGGRSSARETAMRVAAGAIAKKFLQTVYGVRIRGYLSQLGPIKVEKVDWSIVNDNPFFCPDADKIPEMEKYMDALRKEGDSIGAKITVVAEGVPPGLGEPIFDRLDADLAHALMSINAVKGVEIGAGFDVVEQKGTEHRDEMTPEGFLSNNAGGVLGGISSGQDVIAHMALKPTSSLRLPGKSIDVNGDPVEVITTGRHDPCVGIRATPIAEAMMAMVLMDHLLRHRGQNADVKVDTPDIAAIARVKAQD
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Q2SJE4
Q82VR4
PSTB_NITEU
Phosphate-transporting ATPase
Nitrosomonas
MQIFKPASGHTHSTVQKSVVNKLNFYYGGYQALKNIDMMVYEKQVTALIGPSGCGKSTFLRCFNRMHDLYPRNHYEGEIILHPDNANILSPEVDPIEVRMRISMVFQKPNPFPKSIFENVAYGLRIRGVKRRSILEERVENALRNAALWEEVKDRLGDLAFNLSGGQQQRLCIARALATDPEILLFDEPTSALDPIATASIEELISDLRNKVTILIVTHNMQQAARVSDYTAYMYMGELIEFGATDTIFIKPKNKQTEDYITGRFG
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Q82VR4
Q6YRW7
ARSI2_SYNY3
Arsenate reductase ArsI2
unclassified Synechocystis
MIVIYHNPDCGTSRNVLQLIEAAGYLPQVIEYVKEGWTKPQLLGLFAAADLTPRSALRTTKSPAAELNLLEETVTDAQILDAMVEYPILVNRPIVCTPKGVRLCRPSEVVLDLLDHWPSGPFAKEDGELIIDERGNRVYT
Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. Does not constitute the major arsenate reductase in cells: essential only in the absence of ArsC (AC P74313).
Q6YRW7
A6MM44
RBL_BUXMI
Ribulose bisphosphate carboxylase large chain
Buxus
MSPQTETKASVGFKAGVKDYKLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEENQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREASKWSPELAAACEVWKEIKFEFPAMDTL
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
A6MM44
Q7L2K0
TEDC2_HUMAN
Tubulin epsilon and delta complex protein 2
Homo
MLPAGCSRRLVAELQGALDACAQRQLQLEQSLRVCRRLLHAWEPTGTRALKPPPGPETNGEDPLPACTPSPQDLKELEFLTQALEKAVRVRRGITKAGERDKAPSLKSRSIVTSSGTTASAPPHSPGQAGGHASDTRPTKGLRQTTVPAKGHPERRLLSVGDGTRVGMGARTPRPGAGLRDQQMAPSAAPQAPEAFTLKEKGHLLRLPAAFRKAASQNSSLWAQLSSTQTSDSTDAAAAKTQFLQNMQTASGGPQPRLSAVEVEAEAGRLRKACSLLRLRMREELSAAPMDWMQEYRCLLTLEGLQAMVGQCLHRLQELRAAVAEQPPRPCPVGRPPGASPSCGGRAEPAWSPQLLVYSSTQELQTLAALKLRVAVLDQQIHLEKVLMAELLPLVSAAQPQGPPWLALCRAVHSLLCEGGARVLTILRDEPAV
Acts as a positive regulator of ciliary hedgehog signaling. Required for centriole stability.
Q7L2K0
P18101
RL40_DROME
60S ribosomal protein L40
Sophophora
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLRILAQKYNCDKMICRKCYARLHPRATNCRKKKCGHTNNLRPKKKLK
Component of the 60S subunit of the ribosome.
P18101
Q2NVV3
MURD_SODGM
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
Sodalis
MTDYRGEQVVIIGLGLTGLSCVDFLRRRGVTPRVMDTRFTPPGLEKLPADVPRHLGSLHEQWLLDATLIVTSPGVPLSHPALAEAAAAGVAIIGDIELFAREASAPVVAITGSNGKSTVTCMVGEMAAAAGWQVGVGGNIGLPALTLLDSPCQLYVLELSSFQLETTHSLKAAAATVLNISEDHMNRYPLGLQQYRAAKLKIYHDAAVCVVNAEDALTLPVRGHDARCISFGAERGDYCLRRHAGQTWLMARGEPLLEGAELRVGGRHNYTNALAALALSDALGIPSAASLAALRQFRGLTHRFELVHERRGVRWINDSKATNVGSTEAALNGLEVVGTLHLLLGGDGKSADFTPLTPWLQGDRVQLYCFGQDGAQLASLCPEAATLTETLEQAMRIIGSRVRAGDLVLLSPASASLDQFSNFEVRGDVFTRLAREVG
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Q2NVV3
P59151
RR4_WOORA
30S ribosomal protein S4, chloroplastic
Woodwardia
MGRGKTPNLGEFRVATDQSASRKISQFCVRLEAKQRLRFNYGLTERQLLKYVRIARKTRGSTGQVPPQLLEMRLDNVIFRLGMASTIPAARQLVNHRHILVNNRIVDVPSYRCKPKDIITVRNRPTSCNALKGESPGGGETPDHLTASLSEGSRPTGLVNRIANRESVSLNINELLVVEYYSRKA
With S5 and S12 plays an important role in translational accuracy.
P59151
A8AE11
NAPA_CITK8
Periplasmic nitrate reductase
Citrobacter
MKLSRRSFMKANAVAAAAAAAGLSVPGVARAVVGQQEAIKWDKAPCRFCGTGCGVLVGTQQGRIVACQGDPDAPVNRGLNCIKGYFLPKIMYGKDRLTQPMLRMKDGQYNKEGEFTPISWDQAFDVMEEKFKASLKEKGPEAIGMFGSGQWTVWEGYAAAKLFKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGSNMAEMHPILWSRITNRRLSDPNVNVAVLSTFQHRSFELADNGIVFTPQSDLVILNYIANYIIQNNAINQDFFSKYVNLRKGTTDIGYGLRPTHPLEKAAKNPGSDASEPMSFDEYKAFVAEYTLEKTAEMTGVPKDQLEQLAQLYADPKKKVISYWTMGFNQHTRGVWANNLVYNLHLLTGKISQPGCGPFSLTGQPSACGTAREVGTFSHRLPADMVVTNEKHRDICEKHWQIPTGTIPAKIGLHAVAQDRALKDGKLNVYWVMCNNNMQAGPNINEERMPGWRDPRNFVIVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQIKAPGEAKSDLWQLVQFARRFKTEEVWPEDLLAQKPELRGKTLYDVLFATPAVSKFPLTDLAEDQLNDESRELGFYLQKGLFEEYAWFGRGHGHDLAPFDDYHKARGLRWPVVDGKETQWRYSEGHDPYVKAGEGYKFYGKPDGKAVIFALPFEPAAEAPDKEYDLWLSTGRVLEHWHTGSMTRRVPELHRAFPEAVLFIHPLDAKTRDLRRGDKVKVISRRGEVISVVETRGRNRPPQGLVYMPFFDAAQLVNNLTLDATDPLSKETDFKKCAVKLAKV
Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.
A8AE11
Q9ZJC4
RL25_HELPJ
General stress protein CTC
Helicobacter
MLEGVIRESITKANAKALKKDGYLIANIYGKGVENVNCAFKLNPFIKYLKEKKHLIFPVKLGDKTFEVVVQEYQKNPVTNELIHVDLLAVTKGVKSKFKVPVKHQGTPVGLKNKGILMLSKKRISVECAPEHLPDHYLVDVAPLDVNESILVRDLEKHENVKILDHDSIAVIGVIKAK
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
Q9ZJC4
A6X0D5
RS5_BRUA4
30S ribosomal protein S5
Brucella
MAQRERNREDRGREERDSEFVDKLVHINRVAKVVKGGRRFGFAALVVVGDQKGRVGFGHGKAREVPEAIRKATEAAKRDMIFVPLRSGRTLHHDVEGRHGAGKVLLRAAPAGKGIIAGGPMRAVFETLGVQDVVAKSLGSSNPYNMVRATFDALKHQMHPKDIAAQRGIKYSTLQARRHDVVGSEE
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
A6X0D5
Q12046
CWC2_YEAST
Synthetic lethal with CLF1 protein 3
Saccharomyces
MTSWRDKSAKVQVKESELPSSIPAQTGLTFNIWYNKWSQGFAGNTRFVSPFALQPQLHSGKTRGDNDGQLFFCLFFAKGMCCLGPKCEYLHHIPDEEDIGKLALRTEVLDCFGREKFADYREDMGGIGSFRKKNKTLYVGGIDGALNSKHLKPAQIESRIRFVFSRLGDIDRIRYVESKNCGFVKFKYQANAEFAKEAMSNQTLLLPSDKEWDDRREGTGLLVKWANEDPDPAAQKRLQEELKLESLNMMVHLINNNTNSAGTEVNNKNNERLDRTFPEASVDNVKKRLLPLDNGMESDDFIEKLKKVKKNISRENISSKPSVGKLGGPLLDYLSSDED
Involved in the first step of pre-mRNA splicing. Required for cell growth and cell cycle control. Plays a role in the levels of the U1, U4, U5 and U6 snRNAs and the maintenance of the U4/U6 snRNA complex. May provide the link between the 'nineteen complex' NTC spliceosome protein complex and the spliceosome through the U6 snRNA. Associates predominantly with U6 snRNAs in assembled active spliceosomes. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Binds also to U1, U4, U5 and U6 snRNAs and to pre-mRNAs, in vitro. Is not required for the Prp2-mediated remodeling of the activated spliceosome.
Q12046
Q8UEH0
GLMU_AGRFC
Glucosamine-1-phosphate N-acetyltransferase
Agrobacterium tumefaciens complex
MERSSLAVILAAGDSTRMKSSKSKVLHPVAGRPMIGHVVEAVAGAGVGAVALVVGRDADNVAAAASLKGLQVEAFLQKERKGTGHAVLAAREAIKRGFDDVIVAYGDVPLITSATLDRAREAIAAGADVAVIGFHTDRPTGYGRLLVENGELVAIREEKDATDEERKVTWCNSGLMAINGRNALDLLDRIGNSNVKGEYYLTDVVEIARSLGRRAIAIDAPEKELTGCNNRAELAFIERLWQERRRHELMVDGVSMIAPETVFLSFDTKIGQDVLIEPNVVFGPGVTIEPGAIVHAFSHLEGAHLAEGAVVGPFARLRPGANLHANAKVGNFCEVKKAEIGEGAKVNHLTYIGDAFVGAGSNIGAGAITCNYDGYNKSETRIGANSFIGSNSSLVAPVTIGERAYIASGSVITDDVPADALAFGRARQEVKPGRAVALRERAKAQKEAKKKSS
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Q8UEH0
B0Y6V2
PRM1_ASPFC
Plasma membrane fusion protein prm1
Aspergillus subgen. Fumigati
MLFSRSGRSIFPLLPPYAAHAPNPNQGHIIALPPDGLTPYLGLRARLSQVWINRWTILLLLVLVRVLLAASGLQADMSTAKREALSACTSVESMGSSMASMPHYLSQGVNELTATGVEKAVSGLKSMLMLTITGVEELVLFIIKVLYQTYLCLFTLAVRGSVHVAVGVIKEAADFLNSTVKEVGDDIGKAVSTFESAFNKFLDGVNTVASAFGASVPTLDLNSSISTLENLQLPSSIDQGLDKLNSSLPTFDEVNNFTQTVLRTPFEEVKKLVNESLGTYTFDRSLLPVPAKEQLTFCEGSNGIDSFFDSVTDLVMKARKIFIAILIVAATLACVPMAWQEIRRWRSMKERSQLVRKEAHDPMDVVYIVSRPYTAAAGIKAASRFSNSRRQILVRWAIAYATTPAALFVLCLGVAGLLSCLCQYLLLQAVEKTVPELSTQVGAFADKVVDSLQNASAEWANDANGVIGHMSQDLNENVFGWVNTSTTALNDTLNTFVDKTTGVLNDTFGGTLLYEPLMDVFGCLIGLKVQGIQKGLTWVHDHAHIDFPLLPNDTFSRGAAASISSNSSNPSDSFLADAGDQTSNKITEVVIRVVNKVEDGIRTETIISGVIILIWVFIALIGIVRALTLFWVRDRNRGEGGGARVNHHLSDAGGFIDVPLMAVSNTNTDARSMPPPAPAPRYEASTSTVVASRAVPVSSTHHEDEKLGFAGERQYGSALKVDGAADLRGSSYVEYDMEKR
Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
B0Y6V2
Q6C1L3
PXR1_YARLI
PinX1-related protein 1
Yarrowia
MGLAGVSKKIKYGKDPRNLGWSNNTERFGHKHMSKLGWKDGEGLGHEDRKAQSITQNIKIVLKDDNVGLGAGLAKADKDEAFGLMDFQKLLGKLNGRAQEIEAEVERQQKDVLRGKFGMVFVSGGLLQGTIEEFNKKRGSEAVEESDSDSEESESESDDDKKSRKSSKKEKKDKKSKKRKADDDSDEEEKKSKKSKKDKKEKKEKKEKKEKKEKKEKKEKKEKKDKKEKKDKKEKKDKKSESPTPHDGMEKPSASSTSALRGRMAGRAKFIRSKRMAVMDEKSLNEIFMVKN
Involved in rRNA-processing at A0, A1 and A2 sites and regulates negatively telomerase.
Q6C1L3
P08855
ICAL_RABIT
Erythrocyte calpastatin
Oryctolagus
MNPAEAKAVPISKEMEGPHPHSKKRHRRQDAKTEPEKSQSTKPPVDHEKKAQEGKPKEHTKPKSTHKHASDGEGKHGRNEKTASRSKEPVTPAKRTEPETKPQDTKPAGGKSVAAGTTAAPGKAGDPKKEKKSLPAAALAEPKPDEPSGKSGMDAALDDLIDTLGEPSETQEDSTAYTGPEISDPMSSTYIEELGKREVTIPPKYRELLEKKTGVAGPPPDSVTPLGPDDAIDALSSDFTCSSPVASGKEAGKEAAKSAGEVLEAESAKVMRAAAPPQEKKRKVEEDAMSDQALEALSASLGTRMAEPELDLSSIKEVAEAKRKEEKVEKCGEDDETVPAEYRLKPATDKDGKPLLPEPAEKPKPRSESELIDELSKDFSQAKSNEKQPKPTGKTEESKAAVPAPVAEAVPRTSMCSIQPVPPKPASLQKSTVPDDAVEALAGSLGRKEADPEEGKPVADKIKEKSKEEEREKLGEKEETIPPDYRLEEAKDKDGKPLLPSEPTAQLPALSEDLLLDALSEDFSGPSSASSLKFDDAMLSAAVSEVVSQSPASITRATAPPPDTRPSNKELDDALDKLSDSLGQRQPDPDENKPMEDKVKERAKKEHKDKLGERDDTIPPEYRHLLDQGEQDKPEKPPTKKSKEIKKPAGDQDPIDALSGDLDSCPPAAETSQATEKDKSKTTTASSSKAAKHGDKAKDSAQTTEETSKPKANEKNAS
Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.
P08855
A1WVW8
AROE_HALHL
Shikimate dehydrogenase (NADP(+))
Halorhodospira
MSDHYAVVGNPIAHSKSPQIHTRFAAEVGADLHYHRLWAPEDHFAPVAEAFFAGGGHGLNVTVPFKGAAYTFADTLSDRARAAGAVNTLRAEPDGRHFGDNTDGIGLLRDLQTNHGIDLAGRRLLLLGAGGAARGVLHDLLGEDPRTVVIANRTVDRAEALAGNDHRIRACGFDVLAGERFEVVINTTAAGLQGEMPPLPDDLLAPGATAYDLVYADEDTPFMAWARARGAVTVCDGLGMLVEQAAESFYQWRGTYPQTAPVIEALRIGA
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
A1WVW8
P36589
CDC14_SCHPO
Cell division control protein 14
Schizosaccharomyces
MEDLLNNAKQHLCMRNPKLIRIGLRQVESIVYHVAKPSHDDKIPREIFLKLQDSPLYNSTTPCIYALDSLLEYQQNEEAYEKNFQFIQKLIDDLLHVIEGLVLIHPKSQTLFEDKATLRLFIHLLQPSQPSMLQVAAMKTLVCIMADRPLAIRLFEQINGLQQICVVFKHKQTSQDTRFQILEFFYFYLSPEPYSIDVIAYRKTRTEKQAYLSKYLSNVQGLRDDLDKFQPFGKLDETFD
Has a role in the septation initiation network (SIN) required for cytokinesis.
P36589
A8MKQ1
RECR_ALKOO
Recombination protein RecR
Alkaliphilus
MNYYSASISQLIEEFTKLPGIGRKTAQRLAFHVINMPIQDAHNLADAIVKAKENIKYCKVCTNLTDQEVCNICSDERRDPLLICVVEDPRDVVAMERTKEFKGYYHVLHGAISPLEGIGPEDIKIKELLVRLSAQSADEVIIATNPNIEGEATAMYLSKLLKPMGIKVSRIAHGIPVGGDLEYADEVTLTKALEGRREI
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
A8MKQ1
Q6AVZ9
RPAP2_ORYSJ
RNA polymerase II-associated protein 2 homolog
Oryza sativa
MGPTTATDTGARMKPTTVASAVHRVQMALYDGAAASREPLLRAAASLLSGPDYADVVTERSIADACGYPACPNPLPSEDARGKAAPRFRISLREHRVYDLEEARKFCSERCLVASAAFGASLPPDRPFGVSPDRLDALVALFEGGGGGGDDGGLALGFGASGDGKEVEEGRKVEIMEKEAAGTGEVTLQEWIGPSDAIEGYVPRRDRVVGGPKKEAKQNDACSAEQSSNINVDSRNASSGESGMVLTENTKAKKKEATKTPLKMFKQDEDNDMLSSCISDSIVKQLEDVVLEEKKDKKKNKAAKGTSRVGKSKPAKRPVGRDGHEVDFTSTIIMGDRGSEMMDHGALGQYNFSSSILANEQPSSSQYAAIDSVQAYTEELDELFSNAVNIAKDETSDDSGRCTLRSSLKAVGSKNAGHSVKWADENGSVLETSRAFVSHSSKSQESMDSSVRRESAEACAAALIEAAEAISSGTSEVEDAVSKAGIIILPDMVNQQQYNNDYDNDKDAGENEIFEIDRGVVKWPKKTVLLDTDMFDVDDSWHDTPPEGFSLTLSSFATMWAALFGWVSRSSLAYVYGLDESSMEDLLIAGGRECPQKRVLNDGHSSEIRRALDTCVCNALPVLVSNLRMQIPVSKLEITLGYLLDTMSFVDALPSLRSRQWQLMVLVLLDALSLHRLPALAPIMSDSKLLQKLLNSAQVSREEYDSMIDLLLPFGRSTQSQASLPS
Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Q6AVZ9
Q9JIY2
HAKAI_MOUSE
RING-type E3 ubiquitin transferase Hakai
Mus
MDHTDNELQGTNSSGSLGGLDVRRRIPIKLISKQASKVKPAPRTQRTVSRMPAKAPQGDEEGFDYNEEQRYDCKGGELFGNQRRFPGHLFWDFKINILGEKDDTPVHFCDKCGLPIKVYGRMIPCKHVFCYDCAILHEKKGDKMCPGCSDPVQRIEQCTRGSLFMCSIVQGCKRTYLSQRDLQAHINHRHMRAGKPVTRASLENVHPPIAPPPTDIPDRFIMPPDKHHMSHIPPKQHIMMPPPPLQHVPHEHYNQPHEDIRAPPAELSMAPPPPRSVSQETFRISTRKHSNLITVPIQDDSSSGAREPPPPAPAPAHHHPEYQGQPVVSHPHHIMPPQQHYAPPPPPPPPISHPMPHPPQAAGTPHLVYSQAPPPPMTSAPPPITPPPGHIIAQMPPYMNHPPPGPPPPQHGGPPVTAPPPHHYNPNSLPQFTEDQGTLSPPFTQPGGMSPGIWPAPRGPPPPPRMQGPPSQTPLPGPHHPDQTRYRPYYQ
E3 ubiquitin-protein ligase that mediates ubiquitination of several tyrosine-phosphorylated Src substrates, including CDH1, CTTN and DOK1 . Targets CDH1 for endocytosis and degradation . Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing . Its function in the WMM complex is unknown .
Q9JIY2
Q5F9U4
SYT_NEIG1
Threonyl-tRNA synthetase
Neisseria
MLNITLPDCSVRQYESPVTVAQIAASIGAGLAKAAVAGKVNGKLVDACDPIVEDSAVQIITPKDQEGIEIIRHSCAHLVGHAVKQLYPNAKMVIGPVIEEGFYYDIATEKPFTPEDVAAIEARMKELIAQDYDVVKIMTPRAEAIKIFQERGEEYKLRLIDDMPEVEAMGIYHHQEYVDMCRGPHVPNTRFLKNFKLTKLAGAYWRGDSNNEMLQRIYGTAWATKDELKDYIQRIEEAEKRDHRKLGKQLDLFHLQDEAPGMVFWHPKGWALWQTIEQHMRKELNAAGYKEVKTPQIMDKTFWEKSGHWDNYKDNMFVTSSEKREYAVKPMNCPGHVQIFNNGLRSYRDLPMRLAEFGSCHRNEPSGALHGLMRVRGFVQDDAHIFCTEDQIVSEARAFNELLVRIYKQFGFHDVSVRLSLRPEKRAGSDDVWDKAEQGLREALTACGVEWGELPGEGAFYGPKIEYHVKDALGRSWQCGTLQLDFVLPERLDAEYVTENNDRARPVMLHRAILGSLERFIGILIENHAGSFPLWLAPVQMVIMNITENQADYCREVAAKLQAAGFRAELDLRNEKIGYKIRDNSQYRFPYQIVIGDKEKQENKVAVRRKAEDLGSLDLDDFIAQLQQEITDALVNH
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Q5F9U4
P07634
ANFB_PIG
Brain natriuretic peptide 26
Sus
MGPRMALPRVLLLLFLHLLLLGCRSHPLGGAGLASELPGIQELLDRLRDRVSELQAERTDLEPLRQDRGLTEAWEAREAAPTGVLGPRSSIFQVLRGIRSPKTMRDSGCFGRRLDRIGSLSGLGCNVLRRY
May affect cardio-renal homeostasis. Able to promote the production of cGMP although its potency is very low compared to brain natriuretic peptide 32.
P07634
P17552
CHRB1_CUPMC
Protein ChrB
Cupriavidus
MNALPSSPETAWLLLVVSLPTSASTARMRFWRGIKALGATALRDGAYLLPNLPGLRAPLQTLATDAASEDGKVWMLSVQAADDQQEAEYRALFDRSTEYAEWMVELSSARSTLSDSDEAELLRVARRHGRGIDAIRKVDFFPNEASARAELQWRDFNAAIDILLSPGEPHGVAGNIPRRDPTQYQGRQWATRQHLWVDRVACAWLIRRFIDPHATFLWLEDVRQCPDDALGFDFDGATFTHIGDRVSFEVLLASFGLDEDKGLARLGQMIHVLDVGGTPVAEASGFEAVLAGARERLPNDDALLDEVGYVLDSLYTHFSSPRKR
Together with ChrA1, this protein reduces chromate accumulation and is essential for chromate resistance, possibly as a regulatory protein.
P17552
A7GKG0
CH60_BACCN
Chaperonin-60
Bacillus cereus group
MAKDIKFSEEARRSMLRGVDTLANAVKVTLGPKGRNVVLEKKFGSPLITNDGVTIAKEIELEDAFENMGAKLVAEVASKTNDVAGDGTTTATVLAQAMIREGLKNVTAGANPMGLRKGIEKAVATAVEELKTISKPIEGKSSIAQVAAISAADEEVGQLIAEAMERVGNDGVITLEESKGFTTELDVVEGMQFDRGYASPYMITDSDKMEAVLDNPYILITDKKISNIQEILPVLEQVVQQGKPLLIIAEDVEGEALATLVVNKLRGTFNVVAVKAPGFGDRRKAMLEDIAILTDGEVITEELGRDLKSATIESLGRAGKVVVTKENTTIVEGVGSTEQIEARIGQIRAQLEETTSEFDREKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALNSTRAAVEEGIVAGGGTSLMNVYAKVASIAAEGDEATGINIVLRALEEPVRQIAINAGLEGSVVVERLKGEKVGVGFNAATGEWVNMLESGIVDPAKVTRSALQNAASVAAMFLTTEAVVADKPEENKPAMPDMGAMGGMPGMM
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
A7GKG0
Q9K968
EX7S_HALH5
Exodeoxyribonuclease VII small subunit
Halalkalibacterium (ex Joshi et al. 2022)
MIKNEQPPLSFEEAMEQLEEVVEQLEQGDVPLEEAISMFQKGMNLSKVCHEKLATVEKQMDQILKEDGNFEETVLQEEQE
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Q9K968
P24098
LEU3_THEAQ
Beta-IPM dehydrogenase
Thermus
MRVAVLPGDGIGPEVTEAALRVLKALDEREGLGLTYETFPFGGAAIDGYGEPFPEVTRKGVEAAEAVLLGSVGGPKWDALPRKIRPESGLLALRKSQDLFANLRPAKVFPGLERLSPLKEEIARGVDVLIVRELTGGIYFGEPRGMSEAEAWNTERYSKPEVERVAKVAFEAARKRRRHLTSVDKANVLEVGEFWRKTVEEVHKGYPDVALDHQYVDAMAMHLVKNPARFDVVVTGNIFGDILSDLASVLPGSLGLLPSASLGRGTPVFEPVHGSAPDIAGKGIANPTAAILSAAMMLEHAFGLVELARRVEAAVAKALRETPPPDLGGSAGTQAFTEEVLRHL
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
P24098
Q12HQ0
ATPG_SHEDO
F-ATPase gamma subunit
Shewanella
MAGAKEIKTKIASVKNTQKITSAMEMVAASKMRRAQERMAASRPYAESMRKVIGHVAQGSLEFKHPYLEVREAKRVGYIVVATDRGLCGGLNVNLFKKVTLDVKNWKAQGAEVEFCPIGARSVQFFKSFGGQVSAHASGLGDAPKLADLIGTVRVMLQAYNEGKLDRLYVVFNKFVNTMAQTPVIEQLLPLPKSADDVKTNRWDYIYEPDPKEILETLLVRYVESQVYQGVIENLASEQAARMVAMKAATDNAGDMIDGLQLVYNKARQAAITQELSEIVSGASAV
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Q12HQ0
B2V097
MINE_CLOBA
Cell division topological specificity factor
Clostridium
MGFFKGLSSRPTPKQVAKDRLKLILIHDRGEIPTDTLEKIRKEILGVISKYIEIQVDDVEISVNKSEDMEGENTSALIASIPIKSIRR
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
B2V097
Q91W78
USB1_MOUSE
3'-5' RNA exonuclease USB1
Mus
MSSAPLVGYSSSGSEDEAEAVAAGRSKPGTGFHRCGQNPVPSEKLPVPDSVLSMFPSTEEGPEDDSAKHGGRIRTFPHERGNWATHIYIPYEAKEDFRDLLDALLPRAQMFVPRLVLMEEFHVSLSQSVVLRHHWILPFVQVLKDRMASFQRFFFTANRVKIYTNQEKTRTFIGLEVSSGHAQFLDLVSEVDRAMKEFDLTTFYQDPSFHISLAWCVGDASLQLEGQCLQELQEIVDEFEDSEMLLRVLANQVRCKSGNKFFSMPLK
3'-5' RNA exonuclease that trims the 3' end of oligo(U) and oligo(A) tracts of the pre-U6 small nuclear RNA (snRNA) molecule, leading to the formation of a mature U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate. Participates in the U6 snRNA 3' end processing that prevents U6 snRNA degradation. In addition also removes uridines from the 3' end of U6atac snRNA and possibly the vault RNA VTRNA1-1.
Q91W78
B9KGM2
BIOB_ANAMF
Biotin synthase
Anaplasma
MIRNNWTLEEALELFRMPFSDLILKAHSVHVQNFRNNEVQVAALMNIKTGSCPENCRYCAQSAHYNTGLEKKSLSTVEEVKTAAKRAKEIGADRFCFAAAWRNLHDRDLEKICQFVEAIKSEGLESCASLGMLKLDQAQKLKESGLDFYNHNVDTSREFYHNVVTTRTYEERLETVRNVQQAGIKVCCGGILGMGESTEDRASMLVTLANLEQHPLSVPINRLVPIEGTPMEGNPKIDNIDFVRTIAVARIMMPASYVRLAAGRGEMSEEMQALCMLAGANSIFCGEKLLTTPNARPEDDQRLFSQLGITPSRAACTTSDAQLA
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
B9KGM2
Q83HI6
ILVD_TROW8
Dihydroxy-acid dehydratase
Tropheryma
MFMSSDANACEIDIKPRSRVVTHGIEATTSRGMLRAVGMGDADWEKPQIGIASSWNNITPCNLSLDRLAQGAREGVHAAGGYPLQFCTISVSDGISMGHEGMHFSLVSREVITDSVETVLMAEALDGVVLLAGCDKSLPGMLMAAARLDVSAVFLYAGSIAPGYVTLKCGESKEVTIIDSFEAVGAYKAGLIDQDDLGRIERAICPGEGACGGMYTANTMASVAEALGMSLLGSASPPSADRRRDVYAHKSGEAVVELLKRGITARDILTKEAFENAIAVVMALGGSTNAVLHLLAIAHEAHVPLTIDDFNKIGNRVPHIADLKPFGRYVMNDVDRVGGIPVVINALMREGFIHGDVITVSGRTMAEEISDINPGLPDGKVIHSFSSPLHPTGGIKVLKGTLAPDGAVAKTAGFDTVVFQGPAMVFDRERAAMDALSAGNIKKGSVIVIRYEGPKGGPGMREMLAITAAIKGSGLGKDVLLLTDGRFSGGTTGLCIGHIAPEAVDLGPIAFVQDGDIIRVDIEKSSIDVLVDEKQLRARHLTPPPPRYTSGVLSKYSKLVKSASLGAIT
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Q83HI6
S0F1M6
TOK1G_ATRRO
Omega/kappa-hexatoxin-Ar1g
Atrax
MNTATGFIVLLVLATVLGGIEAGESHMRKDAMGRVRRQYCVPVDQPCSLNTQPCCDDATCTQELNENDNTVYYCRA
Toxin that may inhibit ion channels.
S0F1M6
Q99247
DUF1_YEAST
DUB-associated factor 1
Saccharomyces
MNQLTVSYGLISPDYCTSQDAHILPITKILYPDIPGKNYFLTSGRDGSIILHKNTQLSNEPETAATTIKNDAIRMQVHSDWASDLIHVNMKNSDPSAGDTFISVSHDFSIVLISVNAQLTTWDKKIIGDHDDYIKCIVPIHYEMSNDYELEEQEGGPDNVHDGINNGIVVDEQNNFLFVTGGLDRKIKLWCLSSGPEKMATLLHTFDNAQSNDTGSIYSMSPIIPKYSFDDNQTSRPFDFVAGDCNGDLIFYSCKYRKEVIRIQNAHRTNIKVVRTLDDSTRLISTSSDGVINVWDLNCRHDQTTGALQLPKKIGSWSWDSSIWCVQGTSLDKLYFGDSQGNVMRANLSSYEDAKLTRIFKPDHHHHHHHHHEHEEQNISTTDAKVKKYGGILDIALLPNEKLLFSFCTDSNLNVLDLTNNHFSVNEGGFALTRSSLLTNRRHVITENTKGQMQRWDIVSCELLNTFDSSEGSFDDIVMKYTSKEILSHWCTVSVKVGMLFVKINPKFLKTEVYGSALKDYQVVNNIEINSDERYNLGKIVINSLFNEFISYEVQKDKLLRKKIFSLKKKDLTNSLTLDTGYNSESKKNNKDKKRKSTFKISSTLSIGNTNSSGTPPNSAPATPVMAETIVLEEQPLLQSASDKAIDDSLELVQPLPASKKPYFRTQSSGSLLSRKFKSFRSTSGRATTGLNTPEEPKGILPDTPHVINDDSAFPQAINTTQQSKDATPESMLWNHPFKLEQKLSAISSQDLPSNNTHNKLRSSENSRANSTSTLEGNEKKKPEFMPDLLEQIQESYKQQYMNTSSLKYLTKRLPVTKIIKASSCPIIRVKSATLVLVHLWKEGSCGGRVLFSTLLPPSHVDNETVSGGKENSKPPDDEEVDLQAVDDDKLGKYDLIDGELGSRLNRRQIFEQLEENLPYWFAKALFRDIKTVEEQPKLNFLIMPWSSVGGSEAAGNENKKKFISASDTTESSGNDSSDSSLGNGNEAVSPSTQQQFHNMLKFGRPKTSEQELNPTDLPRISEANVKLVAPGMIRVKKIKLYVADRFETKTPEMKAKMEPSLWLDLLCRGQVLDNDMTLNTVRTLYWKSQGDIVLEYRRKVHNSPLVHEVNGNEGK
Ubiquitin-binding protein involved in the resistance to phenanthroline, sanguinarine, nordihydroguaiaretic acid (NDGA), isopropyl (N-3-chloro-phenyl)-carbamate (IPCPC) and guanosine 5'-O-(2-thiodiphosphate).
Q99247
Q5N4S8
PHCB2_SYNP6
C-phycocyanin-2 beta subunit
Synechococcus
MTFDAFTKVVAQADARGEFLSDAQLDALSRLVAEGNKRIDTVNRITGNASSIVANAARALFAEQPSLIAPGGNVYTNRRMAACLRDMEIILRYVTYAVFTGDASILDDRCLNGLRETYLALGVPGASVAEGVRKMKDAAVAIVSDRNGITQGDCSAIISELGSYFDKAAAAVA
Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod.
Q5N4S8
B3Q855
RIMM_RHOPT
Ribosome maturation factor RimM
Rhodopseudomonas
MPSGLICVARIGAPHGVRGAVRLWSFTADPFAVSDYGPLVTKDGARQFEIASAREAKSHLVVTLKGVATRDEAERLNGVELYVARDKLPPTEADEYYHADLIGLAAVTTAGDALGKVVAIHNFGAGDIIEIAPPSGPTLLLPFTNAVVPTVDLAAGQVVIELPNEIEGDTPNHPEA
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
B3Q855
Q6ENE3
PETD_ORYNI
17 kDa polypeptide
Oryza
MGVSKKPDLNDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPSMIGEPADPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMVSVPTGLLTVPFLENVNKFQNPFRRPVATTVFLIGTAVALWLGIGATLPIEKSLTLGLF
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.
Q6ENE3
Q7M9J0
SSRP_WOLSU
Small protein B
Wolinella
MARKVIANNKKALFDFHILERLEAGIALSGSEVKAIRAGRVNLKDSFVKIIKGEAFLLNAHISYLETTNPHYKPDERRPRKLLLHRKQIDKLTGSVSTEGMTLVTLSIYFNERNRAKAEIALAKGKNLHDKRETLKKRILDREVKAALKEH
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Q7M9J0
Q3K331
FABZ_STRA1
Beta-hydroxyacyl-ACP dehydratase
Streptococcus
MIDIKEIREALPHRYPMLLVDRVLEVSEDEIVAIKNVSINEPFFNGHFPEYPVMPGVLIMEALAQTAGVLELSKEENKGKLVFYAGMDKVKFKKQVVPGDQLVMTAKFVKRRGTIAVVEAIAEVDGKLAASGTLTFAIGN
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Q3K331
Q9XUK7
NHR85_CAEEL
Nuclear hormone receptor family member nhr-85
Caenorhabditis
MDLSTSGSLPCHLPLSLLTNLQTPPIDTSFSSPPATSSSSLLSPSPSSAFRPVVPKSLMNPQPAMDTFYMSAIQSLVVSTTNDDQYSEHGALEGSKSLAKDENASTSAGTILCQVCSDKASGFHYGVFACEGCKGFFRRSIQQKITYRACTRAEDCLILRNNRNRCQCCRLKKCLAVGMSRDAVRFGRVPKREKARMFEEMQKTNVQSQRDQIAIQYENLTEVMHKINQAFGTLQATLEKCTGPIYTDRCPITSNFIVIPLKAAIDFANSIPAFLSITQTQRVHLLQNSVFDVMLLASASASTSQHFPPGGLTYDQSSANPIIPQAIQSISARIRQLPPQTVPILTAIAVCQADLLPESQQPMLLAERLWCVLGKLGGIQSLATAPSLLADVRTLRQWHSDRLRQMSQISQHFSQNLLIAPVAAAAPVLLPPAFLSPPASATSTSSSSVKSEFIERHPSIASLLERPRRISSSGAQEPLNLSLPHVRHQVKRDVDSDEQLEEMKVSPVPTTLSE
Orphan nuclear receptor.
Q9XUK7
B1IMQ2
AROK_CLOBK
Shikimate kinase
Clostridium
MENIVLIGMPLSGKSTLGRELSKILKYDLIDTDTLIEEMEDKSIKEIFKIYGEDYFREKELEIINKLKKESNKVISTGGGLPIYNKNIYELKNIGFTVYLKVPLEELIKRMVKKEYDTRPLLKNNDTKFLEEMYKNRIEIYEKAHTIICNTNYEESLIKIVRAYKKWKGI
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
B1IMQ2
B8E9T4
GUAA_SHEB2
Glutamine amidotransferase
Shewanella
MSDIHEHKILILDFGSQYTQLIARRIREIGVYCELWAWDVTEAQIREFAPNGIILAGGPESVTAENSPRAPEYVFTAGVPVLGICYGMQTMSEQLGGKVIQGVGEGEFGYAQIEMLTDSLLFKGIEDAVNSEGKPLLDVWMSHGDKVSAIPEGFVAVAKTDTCPFAAMANEEKQFFGVQFHPEVTHTRQGMRMLSHFALDICGCAANWKPSSIIEDAIERLKKQIGDDEVILGLSGGVDSSVVAMLLHRAIGKKLTCVFVDNGLLRLNEAEQVMEMFGDHFGLNIIHVDAENRFLDAMKGEADPEAKRKIIGRVFVEIFDEESKKCANAKWLAQGTIYPDVIESAGSATGKAHVIKSHHNVGGLPDHMELGLVEPLRELFKDEVRKIGLELGLPYNMLYRHPFPGPGLGVRVLGEVKKEYCDLLRRADAIFIEELHKADLYNKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETVDFMTAHWAHLPYDFLGRVSNRIINEVDGISRVVYDISGKPPATIEWE
Catalyzes the synthesis of GMP from XMP.
B8E9T4
Q9ZCV4
PTH_RICPR
Peptidyl-tRNA hydrolase
typhus group
MILVIGLGNPGTEYQYTRHNIGFIAIERIASKYHLSFSIKKKFNCEIAEAVIDRQKIIFIKPTTYMNLSGKSVILVKTYYNIKYEKVFVIHDDIDLEIGRIKFKTGGGNGGHNGLKSIDVVIGNHYNRIRIGIGRPKNNHDVADYVLNNFSESEYKIAMQSIDNIANNFGLILEHKLAEFTNKIV
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Q9ZCV4
P05013
IFNA6_HUMAN
Interferon alpha-K
Homo
MALPFALLMALVVLSCKSSCSLDCDLPQTHSLGHRRTMMLLAQMRRISLFSCLKDRHDFRFPQEEFDGNQFQKAEAISVLHEVIQQTFNLFSTKDSSVAWDERLLDKLYTELYQQLNDLEACVMQEVWVGGTPLMNEDSILAVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSSSRNLQERLRRKE
Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
P05013
A5WCK6
RL18_PSYWF
50S ribosomal protein L18
Psychrobacter
MFDKKAARLRRAKKTRAHIRHLGVHRLVVNRTPRHIYAQIISPTGGEVLAQASTLDASLRSGATGNVDAAAAVGKLIAERGTSAGITKVAFDRSGFKYHGRVKALADAARENGLEF
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.
A5WCK6
A7FWJ9
ISCS_CLOB1
Cysteine desulfurase IscS
Clostridium
MNKQVYMDYSATTYTKPEVLEEMLPFFTENFGNPSSLYSFSDKTKKAVNLARERVSKALNAEKNEIFFTSGGSEADNWAIKGIAYANKKKGNHIITTKIEHHAILHTAQFLEKEGFKVTYLPVDEEGFVSVEDIKNAITDETILVSVMFANNEIGTIEPIKEIGELCKEKNIYFHTDAVQAIGHVDIDVKDMNIDLLSMSAHKFYGPKGVGALYIKNGVKIQNLIHGGGQERGKRASTENTAGIVGLGKAIELAMENMPEENEKLSNLRGRLIRGIEARIPEVKLNGPKDMSRRLPNNVNFSFIGIEGETLLLDLDMNGIFGSTGSACASASLDPSHVLLSIGLPHETAHGSLRLSLGAKNTEEDIDYVLEVLPKIIKQRREMSPLWEDYMKNKEEK
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
A7FWJ9
P06184
PGTA_SALTY
Phosphoglycerate transport system transcriptional regulatory protein PgtA
Salmonella
MLNDECSILLIDDDVDVLDAYTQMLEQAGYRVRGFTHPFEAKEWVKADWEGIVLSDVCMPGCSGIDLMTLFHQDDDQLPILLITGHGDVPMAVDAVKKGAWDFLQKPVDPGKLLILIEDALRQRRSVIARRQYCQQTLQVELIGRSEWMNQFRQRLQQLAETDIAVWFYGEHGTGRMTGARYLHQLGRNAKGPFVRYELTPENAGQLETFIDQAQGGTLVLSHPEYLTREQQHHLARLQSLEHRPFRLVGVGSASLVEQAAANQIAAELYYCFAMTQIACQSLSQRPDDIEPLFRHYLRKACLRLNHPVPEIAGELLKGIMRRAWPSNVRELANAAELFAVGVLPLAETVNPQLLLQEPTPLDRRVEEYERQIITEALNIHQGRINEVAEYLQIPRKKLYLRMKKYGLSKEHYKF
Member of the two-component regulatory system PgtB/PgtA that regulates the inducible phosphoglycerate transport system. When activated by PgtB it acts in conjunction with sigma-54 as a transcriptional activator.
P06184
A4FMT5
MNMA_SACEN
tRNA-specific 2-thiouridylase MnmA
Saccharopolyspora
MRVLAAMSGGVDSAVAAARAVEAGHEVVGVHLALSAKPGTLRTGARGCCTIEDSHDARRAADILGIPFYVWDFAERFTEEVIETFVGEYAAGRTPNPCLTCNEKIKFEALLEKAMALGFDAVCTGHYARLTVEDGVPVLRRSRDEGKDQSYVLASLTAEQLGHSMFPLGDSLKSQVRQEAAERGLAVAKKPDSHDICFIPDGDTKKFLESKLGQKPGQLVDAETGAVLGEHTGVHGFTVGQRKGLGIDAPAPDGRPRYVLSLEPVSGTVKVGSADHLGVTEIDAKRPIWPSQRELDGPTECVVQVRAHGGTADAVAEVADGGMSIRLRRPLRGVAPGQAVVLYRPEEEGDLVLGSALIAATR
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
A4FMT5
A1RX88
IF5A_THEPD
eIF-5A
Thermofilum
MSTRPEEAGNIKVGSFIVIDGEPCKVVEVEKSKTGKHGSAKARIVGIGFFDGGKRSIVVPTDARVEVPIIKKFTAQVVAFVGDNVQLMNLEDYSTFEIPMPQEEEIKSKLSEGVEVEVWEVMGRHKIMRVRA
Functions by promoting the formation of the first peptide bond.
A1RX88
Q54MI9
GACK_DICDI
GTPase activating factor for raC protein K
Dictyostelium
MTLVYEKSSFVLIMAQIAEAQNIMTRSTSSNDLLSTSAGSPPSPTSAAILLSSSPSPTITIASLPSGLNIVSNPNGNPAINVVLLNVNLNKEEEKMTLGQLLACFPEVPSNIPIQLNPNQHKLRRDTIVSQPVITSKQSSLFETSKQSNIPLSASVTNLQTLNKEKENYNLLNSSTNSLHSLIITPPTSNNTSSNNFVGGNIINSSSEDSILPPPHIITTTTTTTTSLPPRSPMPLPSSNCINIPNNINIPDNISESSTCSLSSNASNNYPQSPPKYNNFEINQNNNNSISLSKSQSLDNILTNSNNNNNNEITISSNIPIPLPPQSSSPPPTRNNQSSPSPSSPQQQNIMPTPPSTSLTPPQSPTLSPSSSTHSTPTQTTTTIKLPPSSPPSTISQNNARKTQIPTTTTTTTTTTTTTSTTSTTSPNPVVNNKNLNTPSSSFSPTKRLTIAFGSLTRSSNTPPPESSIVPIRWEINLNQIKIASTSTSNTNTVSSQNLINSSNTNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSGNNNNNNNNNNNNNNQLYEQYYKLCKGEFQQNTSLYNKTFNQLLDVDINTSLSLLDKCYDSILKSNGIGLLSSKDQYLSTQSKEKDPNRVKSLLSVVKNAVSEDILNVKPSKTMLYFSNFGKTIPINLEVIDECILNNFSSKKVKFKVLMGPPSKTHTINVSEKEGFIGKKSSITLNFSLILKSSIKLRRVVIIEIEGGVRYFILVQVESNKTAFGQPIEDSELVEDNTSFGPMLVPRALVILKQAFFGCNAHLTESIFRLPPANDSEYNIVKDRVNREAIGTTEPHCIATLIKVFFRELPNLLLNDIDPEIFLNFKPTAQSADTASSAATANSSSSGSGNGNSSPNNDDPTMDPVFIVNLIEEKRRSTFLWLVDLLAEVTKFESSNKMNSKSLSIIFSPNLYFAPSICSAENSFAISGKVVSFILELIQFNKSL
Rho GTPase-activating protein involved in the signal transduction pathway.
Q54MI9
O74477
MCA1_SCHPO
Metacaspase-1
Schizosaccharomyces
MSYNSNPYNGGQYPPYNTYTRPNYSPNNGSQSNNTVHQYQPPRMPPPSTRPQTDGNSNQIPMENVGHISLSSANSHAYAPPSGPPPNTGANSYGNPNYSGPQLPNTQTQSYNLAGGGNFQYQYSTCQGKRKALLIGINYLNTQNELQGCINDVMSMSQLLIQRYGYKQEDMVIMTDTASNQRAIPTRQNMLDAMRWLVSDAQPNDALFFHYSGHGGQTKDLDGDEVDGYDETIYPLDHQYAGQIIDDEMHEIMVKPLPAGCRLTALFDSCHSGGALDLPFTYSTKGVLKEPNMLKESGMDVLHAGLSYASGDIMGAINNVKNIFTSATNGFNNNALQYSRQVKFSPADVISLSGCKDNQTSADTSVNGFATGALSYAFREVVTQNPQLSYLQLLRGIRQVLSNKYSQLPQLSCSHPLDMNLAMVL
Involved in cell death (apoptosis).
O74477
Q9S7E4
FDH_ARATH
NAD-dependent formate dehydrogenase
Arabidopsis
MAMRQAAKATIRACSSSSSSGYFARRQFNASSGDSKKIVGVFYKANEYATKNPNFLGCVENALGIRDWLESQGHQYIVTDDKEGPDCELEKHIPDLHVLISTPFHPAYVTAERIKKAKNLKLLLTAGIGSDHIDLQAAAAAGLTVAEVTGSNVVSVAEDELMRILILMRNFVPGYNQVVKGEWNVAGIAYRAYDLEGKTIGTVGAGRIGKLLLQRLKPFGCNLLYHDRLQMAPELEKETGAKFVEDLNEMLPKCDVIVINMPLTEKTRGMFNKELIGKLKKGVLIVNNARGAIMERQAVVDAVESGHIGGYSGDVWDPQPAPKDHPWRYMPNQAMTPHTSGTTIDAQLRYAAGTKDMLERYFKGEDFPTENYIVKDGELAPQYR
Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Involved in the cell stress response.
Q9S7E4
Q9K3C5
FLID2_PSEAE
Flagellar cap protein
Pseudomonas
MAGISIGVGSTDYTDLVNKMVNLEGAAKTNQLATLEKTTTTRLTALGQFKSAISAFQTALTALNSNAVFMARTAKSSNEDILKASATQSAVAGTYQIQVNSLATSSKIALQAIADPANAKFNSGTLNISVGDTKLPAITVDSSNNTLAGMRDAINQAGKEAGVSATIITDNSGSRLVLSSTKTGDGKDIKVEVSDDGSGGNTSLSQLAFDPATAPKLSDGAAAGYVTKAANGEITVDGLKRSIASNSVSDVIDGVSFDVKAVTEAGKPITLTVSRDDAGVKDNVKKFVEAYNTLTKFINEQTVVTKVGEDKNPVTGALLGDASVRALVNTMRSELIASNENGSVRNLAALGITTTKDGTLEIDEKKLDKAISADFEGVASYFTGDTGLAKRLGDKMKPYTDAQGILDQRTTTLQKTLSNVDTQKADLAKRLAALQEKLTTQFNLLSAMQDEMTKRQKSITDNLASLPYGSGKKT
Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. Essential for motility. Responsible for adhesion to mucin, which is the initial event in colonization by this organism of the airways of cystic fibrosis patients.
Q9K3C5
Q8PM12
RL9_XANAC
50S ribosomal protein L9
Xanthomonas
MDLILLQKVTNLGNLGDKVSVKPGYGRNFLVPQGKAVPATAANVEAFETKRAEYEAKANSILAEAQSRATKFEGASVTIGAHASTEGKLYGSVGPRDIAEAFTAAGLPLEKSEVILGEGAFRNVGEYDVVLHLHADVETTVKVIVESDA
Binds to the 23S rRNA.
Q8PM12
P70774
ASAI_AERSA
Autoinducer synthesis protein AsaI
Aeromonas
MLVFKGKLKEHPRWEVENELYRFRNRVFSDRLGWDVESHRGLEQDSFDTPDTHWVLIEDEEGLCGCIRLLSCAQDYMLPSIFPTALAGEAPPRSSDVWELTRLAIDANRAPRMGNGVSELTCVIFREVYAFARAKGIRELVAVVSLPVERIFRRLGLPIERLGHRQAVDLGAVRGVGIRFHLDERFARAVGHPMQGEYADARELVTE
Required for the synthesis of N-butanoyl-L-homoserine lactone (BHL), an autoinducer molecule which binds to AsaR.
P70774
Q09FY8
TI214_PLAOC
Translocon at the inner envelope membrane of chloroplasts 214
Platanus
MILKSFLLGNLLSLCMKIINSVVVVGLYYGFLTTFSIGPSYLFLLRARVMEEGTEKEVSATTGFITGQLMMFISIYYAPLHLALGRPHTITVLVLPYLLFHFFWHNHKYFLNINYGSTIRNSIRNLNIQCVFLNNLIFPLFNHFILPSSTLARLINIYMFQCNNKMLFVTSSFVGWLIGHILFMKWVELVLIWIRQNHFFRSNALFIRSNVLIVPKKNLVPELRNSMARIFSILLFITCIYYLGRMPSTLVTKKMKETSKMKQMGQSEEETDVEIETTSETKETKEEQEGSTEEDPSPSLYSEEKEDPDKIDETEEIRVNGNEKSKDEFHFRFKKTCYKYKNSPVFQNFYLDGNQENSKLEILKYEKKNLFWFQKPLVTLLFDYKRWNRPLRYIKNNQLENAVRNEMSQYFFYTCQSDGKQRISFTYPPSLSTFWEMIQRKMSLYTTEKLSPEELYNHWVYTNEQKRNNVSKEFINRIEALDKGSLTLDVLEKRTRLCNDKTEQQCLPKVYDPFLNGPYRGTIKKVSSSSIMNDYLITSIENSIEKLWINKIHGILPTDYREFEQKEKIDTFDGKSLSTDIFHFLTPISKFAGESTTSLNWKGLPLLAEQERNYSKDQAKYLKFLFAAVTTDPNNQIIRNKSIVINEICKKVPRWSYKLIDDLEQQEGEYEEESAEDHQIRSRKAKRVVIFTDNEPDTNTHTNTNNTSDRDEVEEVALIRYSQQPDFRRDIIKGSMRAQRRKIVIWELFQANVHSPLFLDKIDKTFFFSFDISEMTKFIFRNCMGKNTKLKTSDPEEKEKKEKKEENERIAVAETWDSILFAQPIRGSMLVTQSILRKYIVLPLLIIAKNTARILLFQFPEWFEDWEEWNREIHVKCTYNGVPLSETEFPRNWLKDGIQIKILFPLCLKPWHRFKLRSHHRGPMKKKGKKYNFCFLTVWGMETELPFGSPRNQPSFFEPILKELEKKIRKVKNQFFRILRVVKERTKWFLTVLKEKKRWVIEIILFIKRIMKELAKINPILLFGLKEVYESSENKNRKNSQNSITIISNQIIHESPIRIRSTDWTNYYYSLTEKKMKNLADRTSTIRNQIERITKDKKKIFLTPEINISPKKMSCGDKRSESLKSFWEIVKKRSIRLIRKWHFFLKFVIEKIYLLCIINIPRINAQLFLESTKKILDKYIYNYNDETNQEEIDEINQKKIHFISTIKKSLFHISNNNSQIFCDLSSLSQAYVFYKLSQTKVINKYHLRSVLEYHERSLFLKDRIKDYFRTQGIFHFESRHKKLRNSGMNDWKNWLKGHYQYQYDLSQTRWARLVPQKWQNRVNQRRTTQNKDSKKLGSYEKDQLIHYQKQNDYAVELLSNKKEKLKKHYGYDLLSHKYINYENKKDLYIYRSPLQVNEGREITYNYTTHKLESFCVLGGIPIRDYLGEDYIIETDKNPDRKYFDWGILHFCLRKEVDIDTWTNMDTEASINKKTKTGTNYSQIVEKINKKDLFMIHEEINPSNQKKKPFDWMGMNEEILNRTISNLELWFVPEFLLLYDTYKMKPWGIPIKLLLVNLNGNENVSENKNINRKQKKNLPLSSNKNKKKSLELENRNQEEKESSSQGDLGSNAQNQGNLGPNAQNQGNLGSVLPNQQKNLEEDYAGSDIKKVRKKKQFKSKAEVELDLLLKKYLLFQLRWNGSLNQRILNNIKIYCFLLRLINPKEITISSIQKGEMSLGIMLIKRDLTFTELIKRGIFIIEPVRLSIKWDGQFIMYQTIGISLVHKSKHQTNQRYREKRCIDKNHFEGFIARHENMLGNGDENHYDLLVPENISSPRRRRELRILTCFHFLNGNVLDRNPVFCNGNNVKNCGQFLNEDKHLDRDTNKLINMKLKFFLWPNYRLEDLACMNRYWFDTNNGSRFSMSRIHMYPRLKIS
Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope.
Q09FY8
Q28LR4
LEPA_JANSC
Ribosomal back-translocase LepA
unclassified Jannaschia
MTDLNRIRNFSIVAHIDHGKSTLADRLIQLTGTVAARDMQAQLLDQMDIERERGITIKANTVRIEYPAKDGHTYILNLIDTPGHVDFAYEVSRSMQAVEGSLLVVDASQGVEAQTLANVYQAIDADHEIVPVLNKVDLPAAEPDRVREQIEDVIGIDASEAVEISAKTGIGIPDVLEAIVTRLPAPKGDRDAPLKAMLVDSYYDSYLGVVVLIRVIDGVIKKGDKIKMMRTGGQYPVDRLGVFTPKMKDIGELGPGEMGFLTASIKQVRDTRVGDTITHDKHGAEQPLAGFKPSQPVVFCGLFPVDTNQFEDLRDAIEKLALNDASFSHEMETSAALGFGFRCGFLGLLHLEVIRDRLEREYDIDLITTAPSVIYHVHMRDETMVDLHNPADMPDPAAIDRIEEPRIKATILVPDDYLGDVLKLCQDRRGIQIDLTYAGTRAMVVYDLPLNEVVFDFYDRLKSVTKGYASFDYQMIGYREDALVKMQVLVNDEPVDALSIMVHRDRAETRGRAMVEKLKDLIPRHMFKIPIQAAIGGRVIARETLSAMRKDVTAKCYGGDASRKRKLLDKQKAGKKKMRQFGKVEIPQSAFISALKMDG
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Q28LR4
A2BYR0
RL13_PROM5
50S ribosomal protein L13
Prochlorococcus
MNKTITPSIETIERNWFLVDAKDKTLGRLATEIASVLRGKNKPTFTPHLDTGDFVIVVNAEKVEVTGKKTSQKLYRRHSGRPGGMKVEKFESLQERIPERIIEQAVKGMLPHNSLGRQQFKKLKVYKGSEHPHAAQNPVSLNS
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.
A2BYR0
B0T1T2
RECR_CAUSK
Recombination protein RecR
unclassified Caulobacter
MAASAGPEIERLIALLSKLPGLGPRSGRRAALALLKKRDTLLAPLTAALVDAQAKVRTCSVCGSLDTSDPCAICSDAARDNRLLCVVEEVGSLWAMERGGSFKGRYHVLGGLLSALDGVGPEALRVGELLGRAKGGEVSEVILALPATVDGQTTAHYLADRLAPTGVSVTMLARGVPVGGDLDWLDDGTIAQALRARRPA
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
B0T1T2
B2LMJ8
NU3C_GUIAB
NADH-plastoquinone oxidoreductase subunit 3
Guizotia
MFLLYEYDIFWAFLIISSLIPILVFFISGFLAPSSKGPEKLSSYESGIEPIGDAWLQFRIRYYMFALVFVVFDVETVFLYPWAMSFDVLGVSVFVEALIFVLILIVGLVYAWRKGALEWS
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory 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.
B2LMJ8
B2IGL1
ATP6_BEII9
F-ATPase subunit 6
Beijerinckia
MAEPHEIDPIHQFHIDRIIPLHFLGTDVSFTNAAFFMLVIVALASLVLLAGTRNHSLVPGRLQSIAEVSYEFIASTLQLSSGRDGMRFFPFVFSIFMFVFLANLIGLVPYTFTVTSQIAVTFGLAMIVIGTVVIYGLIKHGTHFLGIFAPSGVSPLLLPFMIMIEVISFISRPISLSIRLFANMLAGHITLKVMGGFVAGLLGAGSVYALVAPLPLAMVVIFTAFELLVAFLQAYVFTILTCVYLNDAVHPGH
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
B2IGL1
Q89Q06
RUTF_BRADU
NADH:flavin oxidoreductase
Bradyrhizobium
MRMRMQDVAPQDYRDAMACLGAAVNIVTTDGSAGRAGFTASAICSVTDDPPTLLVCINRGSSAYSSVTRNEVVCVNVLSARHEPLSRLFGGKVPADERFAAAAWSTLATGAPVLADCSAAFDCRIADTVNVGTHDVLFCRVVALQRFGCTDNLIYFGRAYHTVGVTDPAEAGPESALDAS
Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway.
Q89Q06
Q6NVD9
BFSP2_MOUSE
Lens intermediate filament-like light
Mus
MSKRRVAADLPSGTNSSMPVQRHRVSSLRGTHSPSSLDSPPASRTSAVGSLVRAPGVYVGVAPSGGIGGLGARVTRRALGISSVFLQGLRSSGLANVPAPGPERDHTTVEDLGGCLVEYMTKVHALEQVSQELETQLRAHLESKAKSSGGWDALRASWASSYQQVGEAVLENARLLLQMETIQAGADDFKERYENEQPFRKAAEEEVSSLYKVIDEANLTKTDLEHQIESLKEELGFLSRSYEEDVKVLYKQLAGSELEQADVPMGTGLDDVLETIRVQWERDVEKNRAEAGALLQAKQQTEVVHVSQTQEEKLAAALSVELHDTSRQVQSLQAETESLRALKRGLENSLHDAQHWHDMELQNLGAVVGRLEAELAEIRSETEQQQQERAHLLACKSQLQKDVASYHALLDREENN
Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA . Plays a role in maintenance of retinal lens optical clarity .
Q6NVD9
Q9HZM7
MURB_PSEAE
UDP-N-acetylmuramate dehydrogenase
Pseudomonas
MSLELQEHCSLKPYNTFGIDVRARLLAHARDEADVREALALARERGLPLLVIGGGSNLLLTRDVEALVLRMASQGRRIVSDAADSVLVEAEAGEAWDPFVQWSLERGLAGLENLSLIPGTVGAAPMQNIGAYGVELKDVFDSLTALDRQDGTLREFDRQACRFGYRDSLFKQEPDRWLILRVRLRLTRRERLHLDYGPVRQRLEEEGIASPTARDVSRVICAIRREKLPDPAVLGNAGSFFKNPLVDATQAERLRQAFPDLVGYPQADGRLKLAAGWLIDKGGWKGFRDGPVGVHAQQALVLVNHGGATGAQVRALAERIQEDVRRRFGVELEPEPNLY
Cell wall formation.
Q9HZM7
Q8GWU0
PGP2_ARATH
Phosphoglycolate phosphatase 2
Arabidopsis
MAPQLLSSSNFKSLFDSVDTFLFDCDGVIWKGETLIDGVSQTLDLIRSKGKNVVFVTNNSVKSRRQYAEKFRSLGVTSITQDEIFSSSFAAAMYLKVNNFPKDKKVYVIGGEGVLEELQIAGFTGLGGPEDGEKKAQWKSNSLFEHDKSVGAVVVGLDPNINYYKLQYGTLCVRENPGCLFIATNRDAVGHMTDLQEWPGAGCMVAAMCGSTEREPIVVGKPSTFMMDFLLQKFGTETSRMCMVGDRLDTDILFGQNAGCKTLLVLTGVTSESNLLDKGNKIEPDYYTSTVSDIIKLMESP
Dephosphorylates 2-phosphoglycolate, but does not contribute to photorespiratory metabolism.
Q8GWU0
L0E172
PHQN_PENFE
Paraherquamide biosynthesis cluster protein N
Penicillium
MTMSQMNQDAEGYFRVWKPEEASPGHQESPEELDSGRMCGHLCRLSPNEPMAQSLVRHEHYLAHRVNIQEGQRIIDLGCGIGNPARSIARFTGANITGLNINAQQLRQARQLTQEAGLSYQVNFVEQNFLKIEFADDTFDGAYAIESTCYAPDLVEVYSEIFRVLKPGARFGVYEAVLTDKYDDNNPMHREVKTNIERGGGLARIHTSAEAIAAMKAVGFEVLAIDDLGARPDQIPWETQLSDPFLEKQGLLSFALLSVFFAARAMPLINRGLQAVVGKLEQMTVFPAGSQKVVDLVVTILDGMYRGGELGIFSPMFLIVARKPEA
Methyltransferase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first steps in the biosynthesis of paraherquamide is the production of the beta-methyl-proline precursor from L-isoleucine (Probable). They require oxidation of a terminally hydroxylated L-isoleucine to the corresponding aldehyde by enzymes which have still to be identified (Probable). Spontaneous cyclization and dehydration would yield the 4-methyl pyrolline-5-carboxylic acid, which is then reduced by the pyrroline-5-carboxylate reductase phqD leading to the beta-methyl-proline precursor (Probable). The next step of paraherquamide biosynthesis involves coupling of beta-methyl-proline and L-tryptophan by the bimodular NRPS phqB, to produce a monooxopiperazine intermediate (Probable). The reductase (R) domain of phqB utilizes NADPH for hydride transfer to reduce the thioester bond of the T domain-tethered linear dipeptide to a hemithioaminal intermediate, which spontaneously cleaves the C-S bond to release the aldehyde product . This compound undergoes spontaneous cyclization and dehydration to give a dienamine which is reverse prenylated at C-2 by the reverse prenyltransferase phqJ (Probable). The other prenyltransferase present in the cluster, phqI may be a redundant gene in the pathway (Probable). During biosynthetic assembly, the key step to produce the polycyclic core is catalyzed by the bifunctional reductase and intramolecular [4+2] Diels-Alderase, phqE, resulting in formation of the [2.2.2] diazaoctane intermediate preparaherquamide . Following formation of preparaherquamide, an indole 2,3-epoxidation-initiated pinacol-like rearrangement is catalyzed by the phqK FAD-dependent monooxygenase (Probable). The prenyltransferase phqA, the cytochrome P450 monooxygenase phqL, and the FAD-linked oxidoreductase phqH (or the cytochrome P450 monooxygenase phqM), are proposed to be involved in the formation of the pyran ring (Probable). The FAD-dependent monooxygenase phqK is likely responsible for generation of the spiro-oxindole, and the N-methylation is likely mediated by the phqN methyltransferase leading to the isolable natural product paraherquamide F (Probable). However, the order of these biosynthetic steps has still to be determined (Probable). In late-stage paraherquamide biosynthesis, the third P450 monooxygenase, phqO, is probably responsible for the C-14 hydroxylation, transforming paraherquamide F to paraherquamide G, and paraherquamide E to the final product paraherquamide A (Probable). The expansion from the 6-membered ring pyran (in paraherquamides F and G) to the 7-membered dioxepin ring (in paraherquamides A and E) represents a poorly understood but intriguing process that probably involves the 2-oxoglutarate-dependent dioxygenase phqC (Probable). Finally, the remaining members of the paraherquamide cluster, including phqI as well as phqM (or phqH), do not have a clearly prescribed role and appear to be redundant (Probable).
L0E172
C4K1L3
RL25_RICPU
General stress protein CTC
spotted fever group
MSEILELEAESRTEFGTGAARALRRAGRVPAIIYGAGKTPVSISLEEKEITKYYRKPAFISQLINLTIDKKKYKVLPKAVELHPVTDIVRHVDFVFLEEKTQKMEVPVVYEGKERALGVKRGGYFNIVKRRVTLLCDVNNIPRNVTIDVTNMPMATSLKSSKIELPKGCSFVTKKEFVLATIIGRRGAKTEAEGEQQAAEAGK
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
C4K1L3
Q9CML8
IHFB_PASMU
Integration host factor subunit beta
Pasteurella
MTKSELIERLVQKCHAVAAKDVENAVKEILDQMSFALESGKRIEVRGFGSFSLHYRQPRLGRNPKTGEQVKLDAKSVPHFKAGKELRERVDIYA
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
Q9CML8
Q7V6P7
SASA_PROMM
Adaptive-response sensory-kinase SasA
Prochlorococcus
MDGVKANQRQQLQLLLVAARHQLSRSDLRSMIQFLENEDCGFNVTLQMADPSEQPELLELHRLVATPALIKLSPTPKQVFAGSSIFQQLQNWITRWQQDIVVTGLGLSLRPTELDGSRTQRELQLEDQLLVLRQENETLIDRLNAQERTLRMVAHELRTPLTAAVLALQSQQLGQINIEHFQDVVKRRLDEIELLSKDLLEVKSTKWEDLFNPQNLDLGNIAAEAILELEKLWLDRNIEIRTDIPSDLPKVFADQRRMRQVLLNLLENALKFTEDGGEVSLTMLHRTSHWVQVSICDNGPGIPEDEQERIFLDRVRLPQTSVSTSGFGVGLSVCRRIVEVHGGKIWVVSEPDKGACFYLTVPVWQRNGQE
May be involved in signal transduction. Participates in the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria, via its interaction with KaiC. Required for robustness of the circadian rhythm of gene expression and is involved in clock outputs.
Q7V6P7
A4XN50
MNMG_CALS8
Glucose-inhibited division protein A
Caldicellulosiruptor
MEFVAGEYDIVVVGAGHAGCEAALACARLGLKTIVFAINLDSIGNMPCNPSIGGTGKGHLVREIDALGGEMGKAADATAIQVRILNRAKGPAVYSLRAQCDRARYKLYMKRVLESQPNLDIRQGEVCDILVEDGKVTGVKLTTGAIFRAKAVVLATGTFLGGRIIIGETVYDGGPDGMHPAKYLTESLKKLGIEMMRFKTGTPARVHRRSLDFSKMQIQLGDEVITPFSFEHETLEIEQVPCYLTYTTEETHRIIRENLHRAPLFTGLIQGVGPRYCPSIEDKVVRFADKPRHQVFIEPMGRDTEEMYVQGMSSSLPEDVQIKMYRSVIGLENVQIMRPAYAIEYDCINPLQLEATLQFKKIKGLFSAGQINGTSGYEEAAAQGIIAGINAAMYVKGKEMLVLDRSQAYIGVLIDDLVTKGTNEPYRIMTSRAEYRLILRQDNADLRLTEIGYRIGLISQERYEKFLKKKKMIEDEIERLKKTVIAPSDKVNKFLIEHGSSPISTGVKLSELLKRPELSYEALREIDPQRPDLPRSVKEEVEIEIKYEGYIKKQLQQIEQFKKLENKKIPEWVDYNQISGLSTEAKQKLSQIRPASIGQASRISGVSPADISVLLIWLEQAKKGSK
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
A4XN50
Q6MX43
DODEC_MYCTU
Calcium dodecin
Mycobacterium tuberculosis complex
MSVYKVIDIIGTSPTSWEQAAAEAVQRARDSVDDIRVARVIEQDMAVDSAGKITYRIKLEVSFKMRPAQPR
Binds calcium ions. May play a role in sequestering additional small ligands.
Q6MX43
A4TEN6
CH601_MYCGI
Chaperonin-60 1
Mycolicibacterium
MSKQIEFNETARRAMEAGVDKLADAVKVTLGPRGRHVVLAKSWGGPTVTNDGVTIAREIDLEDPFENLGAQLVKSVATKTNDVAGDGTTTATVLAQALVKAGLRNVAAGANPIALGAGIAKAADAVSEALLASATPVKDAKSIGQVATVSSRDELVGELVGEAMTKVGTDGVVTVEESSTLNTELEVTEGVGFDKGFISAYFVTDFDSQEAVLEDALVLLHREKISSLPDLLPLLEKVAEAGKPLLIVAEDVEGEALSTLVVNAIRKTLKAVAVKAPFFGDRRKAFLDDLAVVTGGQVVNPDVGLVLREVGLEVLGTARRVVVDKDSTVIVDGGGTQDAIEGRKGQLRAEIEVSDSDWDREKLEERLAKLAGGVAVIKVGAATETDLKKRKEAVEDAVAAAKAAVEEGIVIGGGAALVHAGSALDSLRSELKGDELLGVEVFASALSSPLYWIATNAGLDGAVVVNKVSELPAGQGFNAATLEYGDLIGDGVIDPVKVTRSAVVNAASVARMVLTTETAVVEKPAEAEDDGHGHGHGHHHH
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
A4TEN6
B0S2F8
RL25_FINM2
General stress protein CTC
Finegoldia
MTNYKLDMQKRDKVGSNAVRKLRVKELIPGVIYGKDFEPINVTVDEKELRKVHLMAGTSSLIDVKVDGEEHTVIIKDVQKHPFKNHYVHVDFKEIKMGEVANFTIPVVLEGRDEIRLQPSVLMQLLDEVEIECLPKNLPNEAAVSVIDMQYGDTFEVKDLDVFKNPDIKVLNDETEAVCSLSEPKEEVIEEDVEEVSADVPTVSETEEEDAE
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
B0S2F8
A6VIU0
HYPA_METM7
Hydrogenase maturation factor HypA
Methanococcus
MHELSYATSVLNAILEAVEQQEALGRKVIKVNDINLEIGELTLLSVDQLQFVFEVISEDTVCKGAELKAEMVKPKIFCMDCEFEGDLDTKDELEVICPKCESRNVKLKGGKEFNIVNATIEFDDEE
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
A6VIU0
Q3IZY9
PSD_CERS4
Phosphatidylserine decarboxylase beta chain
Cereibacter
MAIDLLSTFIKPMHREGTKFVAIFAVVTLVLFLIWEPLGWIGVGLTVWCYYFFRDPVRVTPTREGLIVSPADGVVSLIEPAVPPAELGMGPAPMTRVSVFMNVFDCHVNRAPIGGTVTAVAYRPGKFLNASLDKASEDNERNALAIRLADGRQIAVVQIAGLVARRILCEVREGTPLLTGERFGMIRFGSRLDVYLPEGVQPLVCLGQVMTSGETVLADLASPEARRTGAAR
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Q3IZY9
C5D3D7
TRPD_GEOSW
Anthranilate phosphoribosyltransferase
unclassified Geobacillus
MFKQLLAKCIEGYTLTEEEAYEAMMMIMSGEASASQIASFLSILRLRGETVDELTGLVKAMRNRMMTLDYEEEAIDTCGTGGDGASTFNISTAAAIVVSSLGVKVAKHGNRAVSSKSGSADVLEALHIDIQATPEEAKRALKTKGLAFLFAPLYHSAMKYAALPRKEIGFRTVFNLIGPLSNPARCKRQVIGVYSTQYAEKLAETLHRLGSEHVLLVTGKDGLDECSISAETDVVELKHGEIRRFTIAPEQYGLARGKLEHVQVRTVQQSAELLKAVLEGRANESAINIVILNAGVALYAAGKAATIREGVEMAKEAMMTKKAYEQFERLRMKEVEKYA
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
C5D3D7
Q32C32
MLTC_SHIDS
Murein lyase C
Shigella
MKKYLALALIAPLLISCSTTQKGDTYNEAWVKDTNGFDILMGQFAHNIENIWGFKEVVIAGPKDYVKYTDQYQTRSHINFDDGTITIETIAGTEPAAHLRRAIIKTLLMGDDPSSVDLYSDVDDITISKEPFLYGQVVDNTGQPIRWEGRASNFADYLLKNRLKSRSNGLRIIYSVTINMVPNHLDKRAHKYLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVFRSQGKSGTPSRSFLFDPASNIDTGTAYLAMLNNVYLGGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAANIINTMTPGDVYQTLTTRHPSAESRRYLYKVNTAQKSYRRR
Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division.
Q32C32
Q8U3S3
PFDB_PYRFU
GimC subunit beta
Pyrococcus
MQNIPPQVQAMLGQLESYQQQLQLVIQQKQKVQADLNEAKKALEEIEKLTDDAVIYKTVGTLIVKTTKEKALQELKEKVETLEVRLNALNRQEQKINEKIKELTQKIQAALRPPTAG
Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding.
Q8U3S3
P47985
UCRI_HUMAN
Ubiquinol-cytochrome c reductase 8 kDa protein
Homo
MLSVASRSGPFAPVLSATSRGVAGALRPLVQATVPATPEQPVLDLKRPFLSRESLSGQAVRRPLVASVGLNVPASVCYSHTDIKVPDFSEYRRLEVLDSTKSSRESSEARKGFSYLVTGVTTVGVAYAAKNAVTQFVSSMSASADVLALAKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTQKEIEQEAAVELSQLRDPQHDLDRVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRLGPAPLNLEVPTYEFTSDDMVIVG
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII). UQCRFS1 undergoes proteolytic processing once it is incorporated in the complex III dimer. One of the fragments, called subunit 9, corresponds to its mitochondrial targeting sequence (MTS). The proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex III dimer, but the persistence of UQCRFS1-derived fragments may prevent newly imported UQCRFS1 to be processed and assembled into complex III and is detrimental for the complex III structure and function.
P47985
Q1D7U7
RL11_MYXXD
50S ribosomal protein L11
Myxococcus
MKKITGQVKLQIPAGKANPAPPIGPALGQQGVNIMEFCKQFNAKTQAEAKEALIIPVVITVYADRSFTFILKTPPAAVLIKKAAGLHTEKKKGSGAKKPGKEKVGQITRAQLEEIAKKKIQDTTAASLEACMSTIAGTARSMGIDVVG
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Q1D7U7
Q6CMA8
SBE2_KLULA
Protein SBE2
Kluyveromyces
MVAARPRKAGTYPTTAQVPSSANASSISSYTNSSNSKTVGSGITRRPSENMLLNMAEGKQSQNQNQQQQQQQHQTHNPRSSANGSEESDHVLSFKPPNRKAVLIKNERPISNDSINTEGDVFSINAGSSKDSSRGTSIIDDDDDENHDTEQSAVLDGKVSANVMPRGKKSFSSVKQNPVTPHSSVTDGLDDVSHLTDTSFSDADLSVTTVKVASAPKSMNTKYIFNNPGSQGKSVAPDAFQSVDSSPKLTRSMFSTVNPTAMHSSYDQHSQLHGQSQPLHNTHPLATSLHSKSVPALPSDSLNGKKPLTPSQRYRLRREQNKLHLQHSIKQKELFYDEDAKLPANDLLDESLVWSIPTASHSSTFISQRKHRASVPNVGRSAKLLDGHDMPPSPIPGVQKVSDLEYFQQVGKNLSAVYQKSEYEVTKSKLLERTQSAELLPLDFKNASVEGMEDLKLVSDDKVSIISSTRPCWLPPKDTEERRSHERDVRKTLSMASIEKLETNQRRHEQEIKNETNNQKLVLLIDRGLNRKSSLQDLKKIAWETGFSSARRSFIYNTVLNTDFNIISTKYMDDTSSLDNIIRSKMTPFPSTQMAEINKLVDDMHFPVESQIRSKLIKLLQWKSISRFGLQTGDNYLMLHFLLEGYDLELIWKLANLLQLTCFNSITRDKYDNRIMNRDGVVGRYMRKDSAFAEEFDSRYLNYMTFWNCLARVDHDLFIWIMDIIVAENARASRWTEEWQHQLRNTDWDTFKEKYIVVNYKVLCSLSLNVLLRYHFGWNNLLHLDELPPSFQLVKPVDNREPVSDQYLVFIKKWNHYYAKF
With SBE22, is involved in cell wall integrity and polarity processes like bud growth.
Q6CMA8
Q886Y6
DER_PSESM
GTP-binding protein EngA
Pseudomonas
MVPVIALVGRPNVGKSTMFNRLTRTRDAIVGDLSGLTRDRQYGEAKWQGRSYILIDTGGISGDEHGMDEKMAEQSLLAIEEADVVLFLVDARAGYTAADQMIGEHLRKRNKRSYVVANKIDNIDENLARAEFSPMGLGDAIPVAGAHGRGISQMLEIALREFPKDEDELEEGEVEEVAEGQEAKRIPGPSEKDGIKIAIIGRPNVGKSTLVNRMLGEDRVIVYDEPGTTRDSIYIPFERNEEKYTLIDTAGVRKRGKIHEEVEKFSVVKTLQAIKDANVVIFVMDAREGVVDHDLNLLGFALEAGRALVIALNKWDGMTPGERDFVKIELERRLFFVDFADIHFISALHGTGVGNLYQSVQNSFKSAVTRWPTSRLTQILEDAVSEHAPPMVGSRRIKLRYAHLGGANPPLIVIHGNQVEKVPKSYVRYLENTYRRVLKLVGTPIRIEFKGGENPYEGNKNTLTDRQVNKKRRMMSHHKKADKKRRDKR
GTPase that plays an essential role in the late steps of ribosome biogenesis.
Q886Y6
Q64695
EPCR_MOUSE
Endothelial cell protein C receptor
Mus
MLTKFLPLLLLLLPGCALCNSDGSQSLHMLQISYFQDNHHVRHQGNASLGKLLTHTLEGPSQNVTILQLQPWQDPESWERTESGLQIYLTQFESLVKLVYRERKENVFFPLTVSCSLGCELPEEEEEGSEPHVFFDVAVNGSAFVSFRPKTAVWVSGSQEPSKAANFTLKQLNAYNRTRYELQEFLQDTCVEFLENHITTQNMKGSQTGRSYTSLVLGILMGCFIIAGVAVGIFMCTSGRRC
Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation.
Q64695