accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
Q82VS4
|
FTSW_NITEU
|
Peptidoglycan polymerase
|
Nitrosomonas
|
MMSPSTSAPHNQPIQPELDVLLVSTVLLLLGLGLVMVYSASIAIAEAKFGEGSSYYFLARQASYILAGIAVGIGCFRIPLRWWQAYSHYLLGLGILLLLVVLIPGISHEINGSRRWIPLGITSFQPSELMKLIILIFTADYVVRKAAFKDHFFKGFLPILALLTIVSLLLLMEPDLGATVVIAAIVLSIMFMNGMSLKMFFGLICLVPVLLALLIIIEPYRMDRINAIFDPWNDPFDKGYQLTHALIAFGLGEWWGVGLGSSVEKLNYLPEAHTDFMFAVLAEELGFAGVVTVISLFFFLLVRIFKVGRTAARLGDQFGSLVAQGIGVWLGLQAFINMGVNMGLLPTKGLTLPFMSYGGSSIVINSIAIAILLRIDWENRLKRRGLNA
|
Peptidoglycan polymerase that is essential for cell division.
|
Q82VS4
|
Q60931
|
VDAC3_MOUSE
|
Outer mitochondrial membrane protein porin 3
|
Mus
|
MCNTPTYCDLGKAAKDVFNKGYGFGMVKIDLKTKSCSGVEFSTSGHAYTDTGKASGNLETKYKVCNYGLTFTQKWNTDNTLGTEISWENKLAEGLKLTLDTIFVPNTGKKSGKLKASYRRDCFSLGSNVDIDFSGPTIYGWAVLAFEGWLAGYQMSFDTAKSKLSQNNFALGYKAADFQLHTHVNDGTEFGGSIYQKVNERIETSINLAWTAGSNNTRFGIAAKYKLDCRTSLSAKVNNASLIGLGYTQTLRPGVKLTLSALIDGKNFNAGGHKVGLGFELEA
|
Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules.
|
Q60931
|
A9MA15
|
OMP2B_BRUC2
|
Porin Omp2b
|
Brucella
|
MNIKSLLLGSAAALVAASGAQAADAIVAPEPEAVEYVRVCDAYGAGYFYIPGTETCLRVHGYVRYDVKGGDDVYTGSDRKGWDKSARFALRVSTGSETELGTLKTFTELRFNYAANNSGVDGKYGNETSSGTVMEFAYIQLGGLRVGIDESEFHTFTGYLGDVINDDVISAGSYRTGKISYTFTGGNGFSAVIALEQGGDNDGGYTGTTNYHIDGYMPDVVGGLKYAGGWGSIAGVVAYDSVIEEWAAKVRGDVNITDQFSVWLQGAYSSAATPDQNYGQWGGDWAVWGGLKYQATQKAAFNLQAAHDDWGKTAVTANVAYELVPGFTVTPEVSYTKFGGEWKNTVAEDNAWGGIVRFQRSF
|
Forms passive diffusion pores that allow small molecular weight hydrophilic materials across the outer membrane.
|
A9MA15
|
Q7T0V2
|
LTR3A_XENLA
|
Mitogen-activated protein kinase scaffold protein 1
|
Xenopus
|
MAEELRRFLYKKLTSVEGLHAIVVSDRDGVPVIKVANENAPEQALRPAFLSTFALATDQGSKLGLSKNKSIICYYSTYQVVQFNQLPLVVSFIASSNANTGLILSLEKELGSLFKELRQAVIS
|
Regulator of the TOR pathway, a signaling cascade that promotes cell growth in response to growth factors, energy levels, and amino acids. As part of the Ragulator complex, may activate the TOR signaling cascade in response to amino acids. Adapter protein that may regulate the MAP kinase cascade.
|
Q7T0V2
|
C1CTM3
|
COAD_STRZT
|
Pantetheine-phosphate adenylyltransferase
|
Streptococcus
|
MSDKIGLFTGSFDPMTNGHLDIIERASRLFDKLYVGIFFNPHKQGFLPIENRKRGLEKALGHLENVEVVASHDELVVDVAKRLGATFLVRGLRNASDLQYEASFDYYNHQLSSDIETIYLHSRPEHLYISSSGVRELLKFGQDIACYVPESILEEIRNEKKD
|
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
|
C1CTM3
|
B3QML1
|
DUT_CHLP8
|
dUTP pyrophosphatase
|
Chlorobaculum
|
MIKVKIVRLKEKASLPAYATAHAAGMDVSACLDAPVTLEPSSSALIPTGLAIELPEGYEAQLRPRSGLALRHLISLPNSPATIDADYRGEVGVILINHGREPFTVNHGDRIAQMVVSKVDRVAFEEVDSLSDTERGEGGFGHTGVASKAE
|
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
|
B3QML1
|
B2S689
|
RL10_BRUA1
|
50S ribosomal protein L10
|
Brucella
|
MDRAEKREFVAWLNGAFKESGSVVVAHYTGLTVAQMSDLRSKMRDAGGSVKVAKNRLAKIALQGTESEGIADLFTGQTVVAYANDPITAPKVAVEFAKANDKLVILGGAMGATTLNADGVKSLASLPSLDELRAKLVGMIQTPAQRLAVLTSAPAGQIARVIGAHARKNEAA
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
B2S689
|
Q6D8D4
|
SKP_PECAS
|
Chaperone protein Skp
|
Pectobacterium
|
MKKWLCAAGLGLVLAASASVQAADKIAVVNVSSIFQQLPQRESVGKQLENEFKGRASELQSMENDLQGKMQKLQRDGSTMKASDRSKMEKDVMAQREQFSTKAQAFEQDNRRRQTEERNKILSRIQDAVKAVATKEGYDVVIDANAVAYVANAKDITADVLKQVK
|
Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm.
|
Q6D8D4
|
P53651
|
SODM_NOCAS
|
Superoxide dismutase [Mn]
|
Nocardia
|
MAEYTLPDLDYDYSALEPHISGQINELHHSKHHAAYVAGANTALEKLEAAREAGDHSAIFLHEKNLAFHLGGHVNHSIWWKNLSPNGGDKPVGELAAAIDDQFGSFDKFRAQFTAAANGLQGSGWAVLGYDTLGQKLLTFQLYDQQANVPLGIIPLLQVDMWEHAFYLQYKNVKADYVTAFWNVVNWADVQDRFGKAVNQGKGLIFG
|
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
|
P53651
|
Q06707
|
SWC7_YEAST
|
SWR1-complex protein 7
|
Saccharomyces
|
MDCPSNVVLLLLQLVLQRQQTLAHRDKSVDLQTLLKDPVIDNDVLVEFKTHKLVQLYGPQYCRDISLRGLKTMVTDIFANGIPKNAQSSGNDQPVTVVDLANYYYMQRINELQNTELPQLKEALLTRLEHMI
|
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling.
|
Q06707
|
P59799
|
FER5_AQUAE
|
2Fe-2S ferredoxin-5
|
Aquifex
|
MPKVIVANINAEFEGIENETIMQILYRNGIEIDSACGGHGQCTSCKVLIISGSENLYPAEFEEKDTLEENGMDPETERLSCQAKLNGKGDVVIYLP
|
May be involved in the assembly of iron-sulfur clusters (Isc-Fd).
|
P59799
|
A7HN78
|
SYS_FERNB
|
Seryl-tRNA(Ser/Sec) synthetase
|
Fervidobacterium
|
MIDLKLLRKDPQHFYEALKKRNYSTDIIDEIVNLDKEWRNQLNIVNNLKAKRNELSKLVARYKAEGKNQEAEEIIAESKKIGEEIAQYEGKQKELEEKMYNLALYIPNPPHESVPVGKDETENVEIRRWGEPRKFDFEPKAHWDLGPELGMLDFDRGSKLSGSRFTVMFGAIAKLERAIAQFMLDVHTKNGYIEVNVPHLVKRETITATGQLPKFSEELYTCERDDLFLIPTAEVSLAALHIDEILEENKLPKKYTAFTPCYRREAGSYGKDVRGLIRQHQFEKVELVWYTTPERSFEDLEQLTQDAERILQLLGLPYRVVTLCTGDLGFAAAKTYDIEVWLPSYNSYKEISSCSNVTDFQARRGNIRYRAKDGKLNYVHTLNGSGLAIGRTLVAIMENYQNPDGTITIPEVLRPYMGTDIIKPME
|
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).
|
A7HN78
|
Q7SYI5
|
C1GTB_DANRE
|
Core 1 beta1,3-galactosyltransferase 1-B
|
Danio
|
MKALGARSAFYVGFLVGTCSLYLLLRQAGFTRDSGSREPGTHDKTLLEMLEEENKNWKKERSALFNLNHPHHTGEDGALADSLYKRVRILCWVMTGPDNLEKKARHVKATWSRHCNIVVFISSVDNPDFPTVGLNTKEGRDQLYWKTIRAFHYVMEKHSDEADWFLKADDDTYVIVDNLRWILARHSPEDPVYFGRRFKPYVKQGYMSGGAGYVLSKEALRRFVEGFRTKVCTHTTSVEDLAMGQCMEKIGVKAGDSRDTMQRETFHPFVPESHLTGTFPKTFWYWNYCYYPIVQGPQCCSDLAVSFHYVDASHMYLLEYYTYHLRAFGYKYRYQPPEPNVKAPEKVETRVLEQKDKVEAQEEENQSPELNDKL
|
Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.
|
Q7SYI5
|
Q84W27
|
SCP43_ARATH
|
Serine carboxypeptidase-like 43
|
Arabidopsis
|
MVSSRAVVMAIMVLVTVQWLVFAEGYPEEDLVARLPGQPNVGFRQFAGYVDVDSENGRSLFYYYVEAVKEPDTKPLTLWLNGGPGCSSVGGGAFTELGPFYPTGDGRGLRLNSMSWNKASNLLFVESPAGVGWSYSNRSSDYNTGDKSTVNDMLVFLLRWFNKFPELKSRDLFLTGESYAGHYIPQLADVILSYNSRSSGFKFNVKGIAIGNPLLKLDRDFAAAYEYFWSHGMISDEVRLTIMNQCDFANPKNMSNACIYAIVESSVLTEYINSYHILLDVCYPSIVQQELRLKKMNALHANRTRLPYEWTMCSNRLNYSGIDGYIDMLPSLKRIIQNQTPVWIFSGDQDSVIPLQSSRTLVRELAEDLNFKTTIPYGAWFHKEQVGGWVTEYGNLLTFATVRGAAHMVPYAEPSRALHMFSSFMNGRRLPNKPDLKSSTDD
|
Probable carboxypeptidase.
|
Q84W27
|
A0RVY8
|
RS8_CENSY
|
30S ribosomal protein S8
|
Cenarchaeum
|
MPATNILANLFVTLYNTEARRRGDCQVYPTSKLGVEVLGTLKKAGYIGEFEHVEDSRGGKFSVHLLAKITKCGAISPRFKVKKGEYTFWEQQYLPSYDRGMLVVTTNQGVMSHHEAAERGIGGFLIGYVY
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
|
A0RVY8
|
P50207
|
HXC13_MOUSE
|
Homeobox protein Hox-C13
|
Mus
|
MTTSLLLHPRWPESLMYVYEDSAAESGSGGGGGGGGAGGAGGGCSGASPGKAPSMDGLGGSCPASHCRDLLPHPVLARPPAPLGAPQGAVYTDIPAPEAARQCAPPPAPPTSSSATLGYGYPFGGSYYGCRLSHNVNLQQKPCAYHPGDKYPEPSGALPGDDLSSRAKEFAFYPSFASSYQAMPGYLDVSVVPGISGHPEPRHDALIPVEGYQHWALSNGWDSQVYCSKEQSQSAHLWKSPFPDVVPLQPEVSSYRRGRKKRVPYTKVQLKELEKEYAASKFITKEKRRRISATTNLSERQVTIWFQNRRVKEKKVVSKSKAPHLHST
|
Transcription factor which plays a role in hair follicle differentiation. Regulates FOXQ1 expression and that of other hair-specific genes.
|
P50207
|
A4ITV2
|
GDPP_GEOTN
|
Cyclic-di-AMP phosphodiesterase GdpP
|
Geobacillus
|
MSHFYERKTYRYPSYALAALAVLMAVSLFYFQWMLGLVGLLGVGFLLYYVIWSQRSLHKELQQYISNLSYRVKKVSEEALMQMPIGILLLDEEDKIEWSNRFLAACFKEQTLIGRSLAELSEPLAAFVKKGKTDEEIIELNGKQLKVIVHRHERLLYFFDVTEHMELRRRYEIERLVLAIIFLDNYDEITQGMDDQAKSQMNSLVTSVLNRWANDYGIFLKRTSSDRFIAVLNEHILTQLEKSKFSILDEVREQTAKHQAQITLSIGIGAGVSSLPELGTLAQSSLDLALGRGGDQVAIKQGNGKVKFYGGKTNPMEKRTRVRARVISHALRELIAESDKVLIMGHKYPDMDALGAAIGILKVVQSNQKEGFLVVDAMKTDAGAQRLLEEMKKQADLWARCIKPEQALELITEDTLLIVVDTHRPSLVIEERLLYRADHIVVIDHHRRGEEFIEAPILVYMEPYASSTSELVTELLEYQPKRVKLSMLEATALLAGIVVDTKSFTLRTGSRTFDAASYLRAQGADTVLVQKLLRESVANYVKRAKLIERAAIDEHGIAIAKGDENEVHDQVLIAQTADTLLTLSGVVASFVISKRGDGTVGISARSLGDVNVQVIMERLGGGGHLTNAAAQLSDVTVGEAEQQLREAIHDYFEGGKPV
|
Has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP) and to a much lesser extent against cyclic-di-GMP (c-di-GMP) in the DHH/DHHA1 domains. Also has ATPase activity, probably via the GGDEF domain. May monitor cellular heme or NO levels.
|
A4ITV2
|
Q4KKJ8
|
ENGB_PSEF5
|
Probable GTP-binding protein EngB
|
Pseudomonas
|
MQLKNPILGLCQQATFMLSAAKVDQCPDDEGFEVAFAGRSNAGKSSALNTLTHASLARTSKTPGRTQLLNFFKLDDDRRLVDLPGYGYAKVPIPLKQHWQRHLEAYLGSRESLKGLILMMDIRHPMTDFDLLMLDWAVASGMPMHILLTKADKLTYGAAKNTLLKVQSQIRKGWGEAVTIQLFSAPKRMGLEEAYTVLAGWMELADKGAEAEA
|
Necessary for normal cell division and for the maintenance of normal septation.
|
Q4KKJ8
|
A9BFZ5
|
IF1_PETMO
|
Translation initiation factor IF-1
|
Petrotoga
|
MAKKDVVVMQGYIIEALPNANFKVKLDNGHEILAHISGRMRKNFIKILPGDRVTVEVSVYDLNKGRIVKREKVNKD
|
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
|
A9BFZ5
|
B3QAC6
|
MIAB_RHOPT
|
tRNA-i(6)A37 methylthiotransferase
|
Rhodopseudomonas
|
MSPPRKLHIKSYGCQMNVYDAQRMVDALAPEGFVETANVDDADLVILNTCHIREKASEKVYSELGRLRVARDEAANHGRRMQIAVAGCVAQAEGEEIIRRAPVVDVVVGPQSYHNLPQLLAKAEQHGRALETEFPIEDKFGVLPQPAPDAIRARGISAFVTVQEGCDKFCTFCVVPYTRGAEMSRPVVAIVEDVKRLAENGVREVTLIGQNVNAYHGDGPDGRAWSLGRLVRRLAEIPGIVRLRYSTSHPNDVDDDLLAAHRDLPALMPFVHLPVQSGSDRILAAMNRKHTADDYRRVIDRFRSASETIAFSSDFIVGFPGETERDFSATLALVAQIGYAGAYSFKYSPRPGTPAADMVEMVPAAVMDERLEQLQQLIDQQQSAFNKAAIGRTVEVLFERAGRKPGQIVGRTAYLQPAHVMAPDSIIGKVLPVRVDSLERYSLLGELASATSRPADAMAATGA
|
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
|
B3QAC6
|
Q96SZ5
|
AEDO_HUMAN
|
Cysteamine dioxygenase
|
Homo
|
MPRDNMASLIQRIARQACLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQLRAEDLNIAPRKATLQPLPPNLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGMLKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQPREREAVRPGVLRSRAEYTEASGPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSACDLPREVWLLETPQADDFWCEGEPYPGPKVFP
|
Plays a vital role in regulating thiol metabolism and preserving oxygen homeostasis by oxidizing the sulfur of cysteamine and N-terminal cysteine-containing proteins to their corresponding sulfinic acids using O2 as a cosubstrate . Catalyzes the oxidation of cysteamine (2-aminoethanethiol) to hypotaurine . Catalyzes the oxidation of regulators of G-protein signaling 4 (RGS4) and 5 (RGS5) and interleukin-32 (IL32) .
|
Q96SZ5
|
A5D2S5
|
RS15_PELTS
|
30S ribosomal protein S15
|
Pelotomaculum
|
MALTSEQKKNVISRYKLHDNDTGSPEVQVAILTERINSLTEHLKLHKGDHHSRRGLLKMVGQRRALLNYLRDRHYERYRALIDKLGLRK
|
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
|
A5D2S5
|
B2DBF0
|
PADC1_PHOAM
|
Phyllocladan-16-alpha-ol synthase
|
Diaporthe
|
MTIMDIDDHSRLRDLAVSLIRQAAEGYSPKYGYGSMSCAAYDTAWVSLVAKPFNGIKKWLFPQSFKFLLENQENDGSWGRQTSPVDRILNTAAPLLSLQRHAREPLQLHDVCEDGDLDDRIHRATLSLQRQLSDWDIASTAHVGFEIIVPALLNLLAAEGLCFSFKAQDELMKVNAAKLKRFDPEVLLYGKHKTTLLHSLEAFVGIIDFDKVVHHKVGGSFMASPSATAAYLMNASCWDDEAEDYIKNVLVNGSGRGHGAVPSAYPSSNFEYSWLLSTLLHAGFTAKDIECPELCDVAGMLENSFIEGQGTIGFARSISSDADDTAKAAFALNKLGYDVSVNEMVKEFEVKNHFQTYPSERDASLSANCNTLLALLHQKQVGAYQPQILKCVKFLTRCWWNTDGPIRDKWNQSHLYSTMLMVQALTEFQAILDQKGLPYGLNTVEMARVSICLFQGCLRTMLQQCEDGSWSHSREQTAYAVLTLGQARRLSTFKHLQSQIDSAIDQAATFIRLHSVDLAQQSLPEFIWTEKVSYTSPLVTEAYCLAALKVATSLVDNPGIVGESLDLGIPSRQRIDKYIWLFHQTPLFRSLPEWQLRASFIEGHLFLPIVNEHRLDVFPRKNMDPDDDYIRLIPFTWTATNNRNFTFASPAWLYDMIMVSVVDYQADEFMEAVAGLTFSEDLSMLVGLIQEVLTPYKTEPASPVTSLIDMSSVQCPRAKLSNIASGDIEEVRTCLRRFASFFLDHPAVRNAQRDDRATAWREVHNYLVAHVRHTQDNMRLNLQEQRRWYVSRNMPYFHWVRSNDDIACPITFGFVTCLVPYLVANPTVERAVIGNESESIVTSSDVSFDSVESKYYADDVCRHITNVTRIYNDCGSVVRDATEKNLNSVNFPEFAVTASGSEKQALRAMGEYERACCQAAFQRLEEASLQTATTEAERAKRRRRLDVWKVFLDTADPYGQIYVVRDFTARSVHVRETGIASTAKDVPLVSSSVPLVGGGPMLVT
|
Involved in the synthesis of labdane-related hydrocarbons by catalyzing the conversion of geranylgeranyl diphosphate (GGDP) to phyllocladan-16-alpha-ol in a two step via type B cyclization into a (+)-copalyl diphosphate ((+)-CDP) intermediate.
|
B2DBF0
|
Q1WSX7
|
LGT_LIGS1
|
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
|
Ligilactobacillus
|
MNFLGVINPVALQLGPFQIRWYGIIIASAVILAVYLSVLEGRKQNILDDDIYDLLLYSLPVAIICARIYYVVFEWSYYSHHLSETYRIWDGGIAIYGALIGAVIVILIFCRRRNIPTWTLLDVIAPTVILAQGIGRWGNFMNQEAHGVATTLGFLKSLHLPKFIINQMYIDGTYYQPTFLYESLWDISGFVVLIILRRQKKLLKSGEVVLSYIIWYSFGRFFIEGMRTDSLMLGSLRVSQWLSLILFISAIAAIFYRRYNDPLLKWYTE
|
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
|
Q1WSX7
|
P26270
|
PSMD7_DROME
|
Protein Mov34
|
Sophophora
|
MPSQEVSVNKVIVHPLVLLSVVDHFNRMGKIGNQKRVVGVLLGCWRSKGVLDVSNSFAVPFDEDDKDKSVWFLDHDYLENMYGMFKKVNARERVVGWYHTGPKLHQNDIAINELVRRYCPNSVLVIIDAKPKDLGLPTEAYISVEEVHDDGSPTSKTFEHVPSEIGAEEAEEVGVEHLLRDIKDTTVGSLSQKITNQLMGLKGLNAQLRDIKQYLQRVGDSKMPINHQIVYQLQDIFNLLPDITNDQFTGTMYVKTNDQMLVVYLASMVRSIIALHNLINNKLANRDAEEGKSDSKEAKEKNKDSKDKDNKETKDKDGKKAEEKADKGKDEGGKGSRK
|
Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
|
P26270
|
A9A3N5
|
MTAP_NITMS
|
5'-methylthioadenosine phosphorylase
|
Nitrosopumilus
|
MEKDVEIGIFGGTGIYDSGLLEDAKEVDIDTPYGKPSDTITVGTFKGRKIAFLPRHGKKHTIPPHMINFKANIWAFKELGVTRIIAPSAVGSLKEELAPGHFVLPTQFLDFTKSRDGSFSEDGRVIHISVADPFCPELQSSITEVTDSLDMNIHKDCTYVCIEGPRFSTKAESKFYRTTGADIIGMTLVPECQLAREAQICYASISTVTDYDVWAEKPVTAKEVLETLSKNVEGTKKILTELIEKIPKDRSCSCAKALEEAEF
|
Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
|
A9A3N5
|
P53248
|
PEX8_YEAST
|
Peroxisomal protein PAS6
|
Saccharomyces
|
MFDHDVEYLITALSSETRIQYDQRLLDEIAANVVYYVPRVKSPDTLYRLVGALFRSQFIVQLPPLRLLHIVKDVFLWKLEVSEPTLPISKFYLVWNAVFESHRATWNLSQLMVLDGVLVTYPSFKQLNNAYFIDESSNKTALYYRNWKLQLFSPIWAQLWNTAIVRANLSIQHCLLIALALLFNQSNRSALLHGVDVSWNLVTEKLLDLLEEYVHGIVQPMEIFSTDSVLSTNLNHLASCLTSSITRSNEATLVNSVRKLERICRYLSDTVASLKEQQLDFKFQNVFILIILALKELSAMNMTILPNHKDTFYSMICLSLFHVHVLTQKIGTVGFPSYDYVYDNLVTYFIVMDDLSKITTVLELMKRNNTKQDPNKLVFYINFLNKITNYYGCRIRLPFITEFIEPLLHFDVFFSGKTGNTLDIEIKESIHTLTITVLSIDSSYSSQVAQWQVSRILVYLKMSMDQFIAGKLSANQILLIFGHLSTQLPSLHNYNKHLLRDSLHETYIRIVNVKNPEKKNVLIECLIVQIAFINNPHHLIGWLNICLQLINTHNKKLLQQLWEMVSSLESSLAIDWWYTTVLSSQSSKL
|
Required for peroxisome assembly.
|
P53248
|
Q86MI0
|
DVE1_CAEEL
|
Defective proventriculus homolog protein
|
Caenorhabditis
|
MFPMRVIVETVRSQHCLTCSNEGHMITDTYAIVAGTTTLNQLVETVLAALGHSSMSTSARGLIQVNNWKPLPFDQITENLDDTVENLFKDISSHVVLKILSKPSTDSNSVQCISEVKNKLLKAAVNKNPNVLTNVDNQQVKDVINTIIAGDETLLNSEQIGAVNEWLDTLETNEDRRSPTQVQRFNTLYEIPRLDKWFKSDANPSKQKMNNYLSQLNQSPFRKNNSKISYQQICNWFTQKRSSSRTLAPVDLVQVSSAQTAAQLLPGFQLNLLQSLFGEQRQKFDFYDKLDETKIVGGSDSPSPADDEIHSNSDETIQDTLFSINIKPEPEIDSIASSPDMANSMRESLSSTSPKLLSGLDLGAFSTHSSSTNSMQNANSSVFSAARSRLMFDPLTELPVLEKWFEENPHPTWMQIDQYTQCLNNCAYRENYPHISQHNVKIWFKNRRAKCKRLLNGMQEKLEQKVFV
|
Transcription factor . Acts during mitochondrial stress by activating the mitochondrial unfolded protein response (mtUPR) . Required during mitochondrial stress for the activation of genes involved in the mtUPR, in concert with histone deacetylase hda-1 . In response to the citrate-induced mtUPR, positively regulates transcription of transcription factor nhr-80, thereby leading to modulation of lipid metabolism . May play a role in modulating the decline in protein homeostasis associated with normal aging . Required for embryonic development and maintenance of mitochondrial morphology .
|
Q86MI0
|
Q5JER9
|
NUCS_THEKO
|
Endonuclease NucS
|
Thermococcus
|
MSKDKVTVITSPSTEELVSLVNSALLEEAMLTIFARCKVHYDGRAKSELGSGDRVIIVKPDGSFLIHQSKKREPVNWQPPGSRVRLELRENPVLVSIRRKPRETLEVELEEVYMVSVFRAEDYEELALTGSEAEMAELIFENPEVIEPGFKPLFREKAIGTGIVDVLGRDSDGNIVVLELKRRRAELHAVRQLKSYVEILREEYGDKVRGILVAPSLTSGAKRLLEKEGLEFRKLEPPKRDSKKKGRQKTLF
|
Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
|
Q5JER9
|
Q39X78
|
SPEA_GEOMG
|
Biosynthetic arginine decarboxylase
|
Geobacter
|
MERWSINDSAKIYNLPNWGADLFSINKKGNVCVHPSPTSKHSIDLRALVDDLIKRKIKPPILLRFMDVLQGRIAAINRAFKYAIDENDYPSTYQTFYPIKVNQQRQVVEAIAKFGKRYNIGIEVGSKPELVIGISFATGNGIPIICNGYKDKEYIETVLYATKIGYDITIVVEKMFELEKIIALSKKTGIKPKLGIRVKLSSKGTGKWATSGGEDAKFGLRMSEIIAAIGLLEQNELLDSVKLIHFHIGSQITKIDKIKSALIEGTRVYAEMRKLGVGIEYVDIGGGLGVDYDGSKSSYFSSVNYSIEEYANDVIYQIKNICEDAGVECPNIISESGRATAAHYSVLVTNLLNTNTQNLMPDFEETLNGAEKLAPTVKKLVDIYKSIDRYSLREDYHDTVQLIQEAVSLFSLGYLTLAERAMAEWLHGKILRKINGIVEKIKPIPEELQNFQLSLRQTYFANFSLFQSIPDSWAIDQLFPIVPIQRLNQKPDVMASIADITCDSDGEITSFVGENGRTKYLPLHKIRKDEDYFVGFFLIGAYQEILGDMHNLFGDTNAVHVTFNKKTGYKIDTVINGDATWESLKYVQYKGPEILKHVRDTMEKDVALRKVSIEESSHFLELLDRTLLGYTYLGE
|
Catalyzes the biosynthesis of agmatine from arginine.
|
Q39X78
|
A4XTZ4
|
TIG_PSEMY
|
PPIase
|
Pseudomonas
|
MQVSVESTSALERRMTVGVPVERIETEVNKRLQQTARRAKVPGFRPGKVPMSVIRQRYEDAARQEALGDLIQATFYEAVVEQKLNPAGAPAVEPKSFEKGKDLEYVATFEVFPEFEVTGFDSIAIERLQADVADSDVDNMLDILRKQNTRFEAVERAAENGDQLNIDFVGKIDGEAFAGGSAKGTQLVLGSGRMIPGFEDALVGVKAGEERVINPTFPEDYQNLDLAGKTAEFAVTVNSVSAPQLPELNDEFFALFGIKEGGLEGFRAEVRKNMERELRQAIKSKVKNQVMDGLLAANPVEVPKALIGNEVNRLRVQAVQQFGGNIKPDQLPAELFEEQAKRRVVLGLIVAEVVKQFDLKPDEARVRELIEEMASAYQEPEQVVAWYYKNDQQMNEVRSVVLEEQVVDTVLQKANVTDKAVSYEDAVKPAEAPKAD
|
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
|
A4XTZ4
|
B8CIB4
|
RAPA_SHEPW
|
ATP-dependent helicase HepA
|
Shewanella
|
MPFSLGQRWISDTESELGLGTVVGMEGRMVTVLFSATGENRLFSRSEAPLTRVIFNPGDKVESHDEWSLTVTEVEEKDNLIIYHGIHSETGEQASLRETLLNHNIRFNKPQDRLFAGQIDRMDRFGVRYQCQLLRNKLATSDLLGLQGPRVGLIPHQQWIAHEVGQRFAPRVLLADEVGLGKTIEAGLIIHQQLLTGRAERILVIVPDTLRHQWLVEMLRRFNLRFSVFDEDRCVEAYADNDNPFYTEQLVICSLELLRKKKRLEQALDADWDLMVVDEAHHLEWSEDAPSRAYKVVEALSEVVPGVLLLTATPDQLGHQSHFARLRLLDPDRFYDYPSFLKEEESYKDVATAADALACGESLSSEAIASLTQLLSEKDISDSINLIQDASANADKRNQAREELLQELLDRHGTGRVLYRNSRASVKGFPTRNLHIHPQPMPEQYVTASRVSAMMNKHLDTNAKVRQVLSPEKIYQDFDSGSASWWKFDPRVDWLIDFLKTNRSKKVLIIASQAETALSLEEALRTREGIQATVFHEGMSIIERDKAGAYFAQETGGAQALICSEIGSEGRNFQFASHLVLFDLPLNPDLLEQRIGRLDRIGQKNDVEIHLPYLAGTAQERLMQWYHQGLNAFECTCPSGHILFGEFSGELLETLTTDDESSLETLLDNTKSRYQELKVAMEQGRDKLLEINSHGGERANKLVESLAARDEDTQLIGSVIRLWDIIGVEQEDSGENAIVLHPSEHMMFPTYPGLPEDGITVTFDRDMALSRDDIALITQEHPIVQTGLDLITSSETGTTSVAVLKNKALPAGTVFLELIYMADASAPKSSQLYRYLPPTPIRILLDKSGNNLSDNVTYESFDRQLSAVNRHIASKLVTASQAILHPLFAKGETFAANELKLLTETAREKMTQQLTGELERLKALKAVNPNIRDEELTHLSEQMSELNRYLDSSQLQLDAIRLVLVSHA
|
Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair.
|
B8CIB4
|
Q9XJY3
|
NU4LM_MACMR
|
NADH dehydrogenase subunit 4L
|
Macaca
|
MTPTYMNIMLAFTISLLGMLIYRSHLMASLLCLEGMMMSLFIMTTLIALNTRSPLINIMPIILLVFAACEAAVGLALLVSISNTYGLDYIHNLNLLQC
|
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
|
Q9XJY3
|
B8IN27
|
CLPX_METNO
|
ATP-dependent Clp protease ATP-binding subunit ClpX
|
Methylobacterium
|
MSKAGGNDSKSTLYCSFCGKSQHEVRKLIAGPTVFICDECVELCMDIIREESKSSLVKSRDGVPTPKEIRRVLDDYVIGQDFAKKVLSVAVHNHYKRLAHAAKHNDVELAKSNILLIGPTGSGKTLLAQTLARILDVPFTMADATTLTEAGYVGEDVENIILKLLQASDYNVERAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKIMEGTVASVPPQGGRKHPQQEFLQVDTTNILFICGGAFAGLERIISARGKGTSIGFGATVQAPDDRRTGEIFRNVEPEDLLKFGLIPEFVGRLPVLATLEDLDEIALKRILQEPKNALVKQYQRLFEMENVDLTFQEEALTLVARKAIERKTGARGLRSILESILLETMYDLPGLDSVEQVVIGPEVVDGKARPLYIHGDRSKDAPASVSA
|
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
|
B8IN27
|
Q65H34
|
AROE_BACLD
|
Shikimate dehydrogenase (NADP(+))
|
Bacillus
|
MKPIYGLIGNPVAHSMSPDIHNAALKDLSLEGHYHAFRVENEDLEDAVKGMRALGIQGFNVTVPHKVSIMKHLDRIDESAEALGAVNTVRREKEGLVGYNTDGAGFLKSLKPSLDRPLSELSILLIGAGGAARAIFTTLAAETPKRLDVANRTPEKALAFTQRFDGEARALSLQEAEADLSAYDIVIQTTSVGMHPNVEAAPLSLANAKETCLVCDIIYNPLKTALLHEAEAKGLKTLDGVGMFIGQAALAFELWTGHEPNMEKMKSIVLQQLGGKSC
|
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).
|
Q65H34
|
C0HKQ5
|
XAC1_XYLAI
|
Xylopin
|
Alloxylocopa
|
GFVALLKKLPLILKHLH
|
Antimicrobial and mast cell degranulating peptide which probably acts by forming pores in membranes . Active against both Gram-negative and Gram-positive bacterial strains as well as against yeasts . Has leishmanicidal activity (IC(50)=25uM). Has little hemolytic activity .
|
C0HKQ5
|
P0CW11
|
GRPE_METMA
|
HSP-70 cofactor
|
Methanosarcina
|
MKKSRKKENMDSKERNQKEAERSEARNSESPAEKAGETKVSPENEPSSPEAEKNPEEACREENEILKDQLFRLAADFDNFRKRTARQMEENRKSVLEQVLLDFVEVTDNFDRAIKSARTAEDMGPIVSGIEQLSKQFFSILEKYGLERVKCEKAGEFDPHRHEAIHHIETSEVPDNTIVEIYKEGYALNEKVVRPALVSVARSPEEAEK
|
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.
|
P0CW11
|
Q7NRV7
|
RL19_CHRVO
|
50S ribosomal protein L19
|
Chromobacterium
|
MDLIQKLEQEEIARLGKTLPEFAPGDTVVVQVKVKEGNRERLQAYEGVVIAKRNRGLNSAFTVRKMSAGEGVERTFQTYSPLVASVEVKRRGDVRRAKLYYLRGRTGKSARIKEKLPARKQG
|
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.
|
Q7NRV7
|
Q3A4X0
|
PPNP_SYNC1
|
Xanthosine phosphorylase
|
Syntrophotalea
|
MSEFKNVTLIKKANVYYDGKVTSRTVIFADGTKKTLGIMMPGEYTFDTAAAEVMEMLGGSMEVLLPGAETWQSFHEGQSFEVPANSQFSLKIKEVADYCCSYLK
|
Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
|
Q3A4X0
|
Q6Q5K6
|
HUG1_YEAST
| null |
Saccharomyces
|
MTMDQGLNPKQFFLDDVVLQDTLCSMSNRVNKSVKTGYLFPKDHVPSANIIAVERRGGLSDIGKNTSN
|
Involved in the MEC1-mediated checkpoint response to DNA damage and replication arrest.
|
Q6Q5K6
|
A4WR15
|
SYY_CERS5
|
Tyrosyl-tRNA synthetase
|
Cereibacter
|
MTYHPKSDFLRVMQERGYLADCTDMQALDEAMSKGVVPAYIGYDATAASLHVGHLLNIMMLRWLQKTGHKPITLMGGGTTKVGDPSFRSEERPLLTPEKIDANIAGMKQVFARYLDYSDGATGALMLNNAEWLDSLNYLDFLRDIGRHFSVNRMLSFESVKSRLDREQSLSFLEFNYMILQAYDFLELFRRYGCRLQMGGSDQWGNIVNGIDLTRRVLEGEIFGLTSPLLTTSDGRKMGKSAGGAVWLSGEMLAPYDFWQFWRNTTDADVGRFLKLYTELPVEECDRLGALQGAEINGAKIRLANEVTTLLHGREAAEAAEATARAVFEQGGVGGALEVVEIAPATLGEGLSVTHFLVAAGLVTSGKEAKRLVAENGLRFNNEPVSDANAPVTAAMIGDELKVSIGRKKHKLVRLA
|
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
|
A4WR15
|
Q5E3S1
|
CHEB_ALIF1
|
Protein-glutamate methylesterase/protein-glutamine glutaminase
|
Aliivibrio
|
MAIKVLVVDDSSFFRRRVSEIINSDPRLEVIDVAVNGKEAVEKAKSLKPDVITMDIEMPVMDGISAVREIMKACPTPTLMFSSLTHDGAKATLDALDAGALDFLPKKFEDIARNRDEAVSLLQKRIAEIARKKSFMRRPVLSSQSTSTVESRTATTRTATSALTASPVKAAPAAPIAQRFKATGKKYQLTAIGTSTGGPVALQKILTAIPANYPHPIILVQHMPATFTAAFAARLNNLCKIQVKEAEDGDVLKPGCAYLAPGGLQMMVDGRPGASRLKILDGGERMNYKPCVDVTFGSAAKVYGDKVLSMILTGMGADGREGCRMLKAGGATIWSQDEQSCVVYGMPQAVDKAGLSSESLPLDRIAERMLVEVGLK
|
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
|
Q5E3S1
|
C0ZF55
|
RIMP_BREBN
|
Ribosome maturation factor RimP
|
Brevibacillus
|
MSKVTGIVTELITPIVEEVGLELVDIEYKKEGSNWFLRVFIDNETGNIDIDDCRLVSEKLSEKLDEVDPIPTAYFLEVSSPGAERPLRKDKDFTKAVGRNVHITTKEPIEGATTFEGELVSYEDGKLTVKEAKKTYVISQEQIDTARMAIIF
|
Required for maturation of 30S ribosomal subunits.
|
C0ZF55
|
Q4WWR2
|
SLU7_ASPFU
|
Pre-mRNA-splicing factor slu7
|
Aspergillus subgen. Fumigati
|
MSRKPADVASKERNEYIPSFIAKKPFYIDDESTANDYLEHQRLQKQATDQSKWYDRGKRAGPAATKYRKGACENCGAMTHKSKECLSRPRKLGAKWTGKDIQADEVVQNVELGWDAKRDRWNGYDPSEYRQVIEEYEELEKLKRNTKPGAQDGKKIMDGELDDEEAAIEEARYAEESDMGRQQSTATRNLRIREDTAKYLLNLDLDSAKYDPKTRRMVDMGAQDDQAAALVAEENFVRASGDAAEFERAQRYAWESQERGDKKIHLQANPTSGEILRKKEQAETEAKRQAQRKALLEKYGGEEYLKPTPLRETMVIENERFVEYDESGAIKGAPKNAVKSKYPEDVLVNNHTTVFGSWWHNFQWGYACCFSTVKNSYCTGEDGKKAFEEAEMRSMGLLPGPETSDQTSPPAKGETNDIHEAEDLSDRSQRKADTETNTRKRTMMEMKSGVSEEELESYKRSRLAADDPMASFIGKE
|
Involved in pre-mRNA splicing.
|
Q4WWR2
|
A2SQG6
|
RIBB_METLZ
|
3,4-dihydroxy-2-butanone 4-phosphate synthase
|
Methanocorpusculum
|
MFTFNTIEEALKSLQNGEMIIVTDDENRENEGDLICAAEYATTENVNFMAKYGRGLICMPMGRSLVEKLCLPPMVLKNTDNHETAFTVSIDHVDTTTGISAVERGITARKCIDPNARPEDFRRPGHMFPLQAKDNGVFEREGHTEATVDLMKLAGLREAGLCCEIMADNGEMMRTPELISMAKQYNLTFVTIKDLQAYRRKQEASALAVEQKNMSPMDC
|
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
|
A2SQG6
|
Q1IYF7
|
RS20_DEIGD
|
30S ribosomal protein S20
|
Deinococcus
|
MALRHKSAQKRHRQSLKRRLINRSRKNTIKTFSKKAVVAAQNGAENAVELHRKAESLIDKAAKGSTLHKNAAARKKSRLAKALNKAKAAQAAQPA
|
Binds directly to 16S ribosomal RNA.
|
Q1IYF7
|
B7LNW4
|
FABA_ESCF3
|
Trans-2-decenoyl-[acyl-carrier-protein] isomerase
|
Escherichia
|
MVDKRESYTKEDLLASGRGELFGAKGPQLPAPNMLMMDRVVKMTETGGNYDKGYVEAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQLVGFYLGWLGGEGKGRALGVGEVKFTGQVLPTAKKVTYRIHFKRIVNRRLIMGLADGEVLVDGRLIYTASDLKVGLFQDTSSF
|
Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length.
|
B7LNW4
|
Q7Z392
|
TPC11_HUMAN
|
Trafficking protein particle complex subunit 11
|
Homo
|
MSPTQWDFPVELCCRPMAFVTLTGLDVVYNAVHRAVWDAFCANRRADRVPISFKVLPGDHEYPKCRPKRTSYEWYIPKGILKTGWMNKHLNLVPALVVVFYELDWDEPQWKEKQSECATRVEIVRQSLQGRNTKVAVVLIQKKTPLPPGEDVIASERAAALCNACELSGKSLFVLPHTDHLVGYIIRLENAFYEHAQTYYYTEIRRVKSHKEFLNKTTHQLLFVRHQFKIAFFSELKQDTQNALKNYRTAYNLVHELRAHETNILEIKTMAGFINYKICRLCFQHNTPLDAIAQFRKHIDLCKKKIGSAELSFEHDAWMSKQFQAFGDLFDEAIKLGLTAIQTQNPGFYYQQAAYYAQERKQLAKTLCNHEASVMYPNPDPLETQTGVLDFYGQRSWRQGILSFDLSDPEKEKVGILAIQLKERNVVHSEIIITLLSNAVAQFKKYKCPRMKSHLMVQMGEEYYYAKDYTKALKLLDYVMCDYRSEGWWTLLTSVLTTALKCSYLMAQLKDYITYSLELLGRASTLKDDQKSRIEKNLINVLMNESPDPEPDCDILAVKTAQKLWADRISLAGSNIFTIGVQDFVPFVQCKAKFHAPSFHVDVPVQFDIYLKADCPHPIRFSKLCVSFNNQEYNQFCVIEEASKANEVLENLTQGKMCLVPGKTRKLLFKFVAKTEDVGKKIEITSVDLALGNETGRCVVLNWQGGGGDAASSQEALQAARSFKRRPKLPDNEVHWDSIIIQASTMIISRVPNISVHLLHEPPALTNEMYCLVVTVQSHEKTQIRDVKLTAGLKPGQDANLTQKTHVTLHGTELCDESYPALLTDIPVGDLHPGEQLEKMLYVRCGTVGSRMFLVYVSYLINTTVEEKEIVCKCHKDETVTIETVFPFDVAVKFVSTKFEHLERVYADIPFLLMTDLLSASPWALTIVSSELQLAPSMTTVDQLESQVDNVILQTGESASECFCLQCPSLGNIEGGVATGHYIISWKRTSAMENIPIITTVITLPHVIVENIPLHVNADLPSFGRVRESLPVKYHLQNKTDLVQDVEISVEPSDAFMFSGLKQIRLRILPGTEQEMLYNFYPLMAGYQQLPSLNINLLRFPNFTNQLLRRFIPTSIFVKPQGRLMDDTSIAAA
|
Involved in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage.
|
Q7Z392
|
Q5R7D1
|
DDX42_PONAB
|
DEAD box protein 42
|
Pongo
|
MNWNKGGPGTKRGFGFGGFAISAGKKEEPKLPQQSHSAFGATSSSSGFGKSAPPQLPSFYKIGSKRANFDEENAYFEDEEEDSSNVDLPYIPAENSPTRQQFHSKPIDSDSDDDPLEAFMAEVEDQAARDMKRLEEKDKERKNVKGIRDDIEEEDDQETYFRYMAENPTAGVVQEEEEDNLEYDSDGNPIAPTKKIIDPLPPIDHSEIDYPPFEKNFYNEHEEITNLTPQQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAEGKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLDLAMQNAWFRKSRFKGGKGKKLNIGGGGLGYRERPGLGSENMDRGNNNVMSNYEAYKPSTGAMGDRLTAMKAAFQSQYKSHFVAASLSNQKAGSSAAGASGWTSAGSLNSVPTNSAQQGHNSPDSPITSATKGIPGFGNIGNISGAPVTYPSAGAQGVNNTASGNNSREGTGGSNGKRERYTENRGSSRHSHGETGNRHSDSPRHGDGGRHGDGYRHPESSSRHTDGHRHGENRHGGSAGRHGENRGANDGRNGESRKEACNRESKMEPKMEPKMEPKVDSNKMDKVDSKTDKTADGFAVPEPPKRKKSRWDS
|
ATP-dependent RNA helicase. Binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm.
|
Q5R7D1
|
C9J798
|
RAS4B_HUMAN
|
Ras GTPase-activating protein 4B
|
Homo
|
MAKRSSLYIRIVEGKNLPAKDITGSSDPYCIVKVDNEPIIRTATVWKTLCPFWGEEYQVHLPPTFHAVAFYVMDEDALSRDDVIGKVCLTRDTIASHPKGFSGWAHLTEVDPDEEVQGEIHLRLEVWPGARACRLRCSVLEARDLAPKDRNGTSDPFVRVRYKGRTRETSIVKKSCYPRWNETFEFELQEGAMEALCVEAWDWDLVSRNDFLGKVVIDVQRLRVVQQEEGWFRLQPDQSKSRRHDEGNLGSLQLEVRLRDETVLPSSYYQPLVHLLCHEVKLGMQGPGQLIPLIEETTSTECRQDVATNLLKLFLGQGLAKDFLDLLFQLELSRTSETNTLFRSNSLASKSVESFLKVAGMQYLHGVLGPIINKVFEEKKYVELDPSKVEVKDVGCSGLHRPQTEAEVLEQSAQTLRAHLGALLSALSRSVRACPAVVRATFRQLFRRVRERFPGAQHENVPFIAVTSFLCLRFFSPAIMSPKLFHLRERHADARTSRTLLLLAKAVQNVGNMDTPASRAKEAWMEPLQPTVHQGVAQLKDFITKLVDIEEKDELDLQRTLSLQAPPVKEGPLFIHRTKGKGPLMSSSFKKLYFSLTTEALSFAKTPSSKKSALIKLANIRAAEKVEEKSFGGSHVMQVIYTDDAGRPQTAYLQCKCVNELNQWLSALRKVSINNTGLLGSYHPGVFRGDKWSCCHQKEKTGQGCDKTRSRVTLQEWNDPLDHDLEAQLIYRHLLGVEAMLWERHRELSGGAEAGTVPTSPGKVPEDSLARLLRVLQDLREAHSSSPAGSPPSEPNCLLELQT
|
Ca(2+)-dependent Ras GTPase-activating protein, that may play a role in the Ras-MAPK pathway.
|
C9J798
|
Q8XLG5
|
ACCA_CLOPE
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
|
Clostridium
|
MSRELIRTADAWNKVKIARDPNRPNAKFYINEIFDEFIELHGDRNFGDDKAIIGGIALLNNLSFTVVGICKGENTKENIKRNFGMPHPEGYRKALRLMKQAEKFKRPVICFVDTPGAFCGIGAEERGQGQAIAQNLVELMGLKVPLISIVIGEGGSGGALALAVADKVFMLEHSIYSVLSPEGFASILWKDSSRAEEAASVMKITAQDLKSFNIIDKIIKEPRGGAHKNPIKMAQNIKKTILEALGEMKGTDLDTLLNERYNKYRNIENNL
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
|
Q8XLG5
|
Q83QL0
|
EX7L_SHIFL
|
Exodeoxyribonuclease VII large subunit
|
Shigella
|
MLPSQSPAIFTVSRLNQTVRLLLEHEMGQVWISGEISNFTQPASGHWYFTLKDDTAQVRCAMFRNSNRRVTFRPQHGQQVLVRANITLYEPRGDYQIIVESMQPAGEGLLQQKYEQLKAKLQAECLFDQQYKKPLPSPAHCVGVITSKTGAALHDILHVLKRRDPSLPVIIYPTSVQGDDAPGQIVRAIELANQRNECDVLIVGRGGGSLEDLWSFNDERVARAIFASRIPVVSAVGHETDVTIADFVADLRAPTPSAAAEVVSRNQQELLRQVQSARQRLEMAMDYYLANRTRRFTQIHHRLQQQHPQLRLARQQTMLERLQKRMSFALENQLKRAGQQQQRLTQRLNQQNPQPKIHRTQTRIQQLEYRLAEILRAQLSATRERFGNAVTHLEAVSPLSTLARGYSVTTATDGNVLKKVKQVKTGEMLTTRLEDGWIESEVKNIQPVKKSRKKVH
|
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
|
Q83QL0
|
O13353
|
CHS4_MAGO7
|
Class-IV chitin synthase 4
|
Pyricularia
|
MSLPERPGAKASYEQRNSYRKSPSRRNRPNDIEASGYYPVTGGQHQRGPSVNSFAETIRSPNSNIESAPLSPSAEQIEHGSDQPFQRKRSLIRPERNRIDRDHPNYHYRKHAAKMNTLPSSTGNDPVLEDVSGATESGPPSGSNSASGSGVREENIPRKSRKASGRETVAEKSDNTRRRVSTRNSKIVKEGKRKEKIPEQLRPPSAWNVYCAVITFWSPDFIMKCCGMPAKAQRRAWREKIGLISLILIIMGVVGFLTFGFNQAVCGGPVLRLHINSVDRSYMIFHGTAYNLDGSHHPVAEGIPKRLDGTGANVVYDLPEGYGGTDGSFMFQNVNGKCKGLITKAPNSDVPSEGDNLAWYFPCHARNQDGSSQPNMTYPYYFGYACHTTPLARSTFYTQLDKSADVYFTWADIRNNSRNLFVYSGNVLDLDLLFWFNRDQVNIPRRFEELRDKNNAANRAIRGRDATRTFMASGDRQIAECFEDIIKVGTVDTDTVGCIAAKVVLYVSLALILSVVGARFTLALIFQWFISKNYAADKTSQTSDKRKRNKQIEDWSEDIYRAPPRMPGDVGSSVAGASSSDHTSKRSSFLPTTSRFSTVYGAERSARNKSMPTTMASQASGGYMGPSSTAYRETNESRTSFLKSDPYATNTAPIEGPGPSGFIHDSVVPQPPSDWMPFGFPLAHTICLVTAYSEGELGLRTTLDSVAMTDYPNSHKVILVICDGIIKGKGESKSTPEYVLDMMKDHTIPVEDVEAFSYVAVASGSKRHNMAKIYAGFYDYGTQSNIPLDKQQRVPMMVVVKCGTPDEMVKSKPGNRGKRDSQIILMSFLQKVMFDERMTELEYEMFNGLWKVTGISPDFYEIVLMVDADTKVFPDSLTHMISAMVKDPEIMGLCGETKIANKRDSWVSAIQVFEYFISHHLAKSFESVFGGVTCLPGCFCMYRIKAPKGAQNYWVPILANPDVVEHYSENVVDTLHKKNLLLLGEDRYLTTLMLRTFPKRKQVFVPQAVCKTTVPDSFMVLLSQRRRWINSTIHNLMELVLVRDLCGTFCFSMQFVIFIELIGTLVLPAAIAFTFYVVIISIINQPPQIIPLVLLGLILGLPAILIIITAHSWSYVLWMLIYLLSLPVWNFVLPAYAFWKFDDFSWGDTRKTAGEKTKKAGIEYEGEFDSSKITMKRWAEFERDRRARQSQYWGSRENVTGGVRTASGVWASAPPHHHQQQYDEYYSDA
|
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
|
O13353
|
P42471
|
EFTU_BRELN
|
Elongation factor Tu
|
Brevibacterium
|
MAKASFERTKPHVNIGTIGHVDHGKTTLTAAITKVLADQYPDLNEARAFDQVDNAPEEKERGITINVSHVEYQTEKRHYAHVDAPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVGVPYIVVALNKSDMVDDEELLELVEFEVRDLLSSQDFDGDNAPVIPVSALKALEGDEKWVKSVQDLMAAVDDNVPEPERDVDKPFLMPVEDVFTITGRGTVVTGRVERGVLLPNDEIEIVGIKEKSSKTTVTAIEMFRKTLPDARAGENVGLLLRGTKREDVERGQVIVKPGSITPHTKFEAQVYILSKDEGGRHNPFYSNYRPQFYFRTTDVTGVITLPEGTEMVMPGDNTDMSVELIQPIAMEDRLRFAIREGGRTVGAGRVTKITA
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
P42471
|
A4QCI7
|
TYSY_CORGB
|
Thymidylate synthase
|
Corynebacterium
|
MTVPTPYEDLLRKIAEEGSHKDDRTGTGTTSLFGQQIRFDLNEGFPLLTTKKVHFHSVVGELLWFLQGDSNVKWLQDNNIRIWNEWADEDGELGPVYGVQWRSWPTPDGRHIDQISGALETLRNNPDSRRNIVSAWNVSELENMALPPCHLLFQLYVADGKLSCQLYQRSADMFLGVPFNIASYALLTHMFAQQAGLEVGEFIWTGGDCHIYDNHKEQVAEQLSREARPYPTLELNKAASMFEYSFDDITVSGYDPHPLIRGKVAV
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
|
A4QCI7
|
Q7Z614
|
SNX20_HUMAN
|
Selectin ligand-interactor cytoplasmic 1
|
Homo
|
MASPEHPGSPGCMGPITQCTARTQQEAPATGPDLPHPGPDGHLDTHSGLSSNSSMTTRELQQYWQNQKCRWKHVKLLFEIASARIEERKVSKFVVYQIIVIQTGSFDNNKAVLERRYSDFAKLQKALLKTFREEIEDVEFPRKHLTGNFAEEMICERRRALQEYLGLLYAIRCVRRSREFLDFLTRPELREAFGCLRAGQYPRALELLLRVLPLQEKLTAHCPAAAVPALCAVLLCHRDLDRPAEAFAAGERALQRLQAREGHRYYAPLLDAMVRLAYALGKDFVTLQERLEESQLRRPTPRGITLKELTVREYLH
|
May play a role in cellular vesicle trafficking. Has been proposed to function as a sorting protein that targets SELPLG into endosomes, but has no effect on SELPLG internalization from the cell surface, or on SELPLG-mediated cell-cell adhesion.
|
Q7Z614
|
Q5B0C8
|
APTC_EMENI
|
Asperthecin synthesis protein C
|
Aspergillus subgen. Nidulantes
|
MTLPVLIIGAGLSGLTTARLLTNAHIPCIVFEASPPSRTQGYAISLRDWGFNALLRALGNLPLSSLTRAVAPDRHIGGWGWLDQSWRNNQTGEIIMMPPKESKEKPTILRANRNALRQWIADAGVGEDEEIDVRYGHRLVGVQLLREGGDGNVVTAEFANGATYTGSLLIAADGVHSTVRTLILPAVKPEILPVLVYHGDFKLSREEYECVIRPHAGESTIVAGVGDGFNTPLTVCDVTSTTVHMDWTYSRPSIGDNDPLYNPNITSEEAKVIPEALIEEINAKKLGEPWSLFLNGEAMRRHRVFNWLTRCVSMERSDVNSCTGKGVVFVGDSWHAMPIFGGEGGNHAIFDGIELAKMLEVAWGRSKEDVQAAIGKYYDKSWRRCNDAVRRSKQRFYQLHRPISEWIEIAEKQKMRA
|
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment . Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules . Polyketide is subsequently hydrolyzed by the action of the hydrolase aptB into endocrocin-9-anthrone . Endocrocin-9-anthrone is then oxidized into endocrocin by the monooxygenase aptC . Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis cluster . Finally, aptC or another endogenous oxygenase catalyzes additional oxidation steps to form asperthecin .
|
Q5B0C8
|
Q8EG24
|
LPXH_SHEON
|
UDP-2,3-diacylglucosamine diphosphatase
|
Shewanella
|
MRTLFIGDLHLSADRLDITQAFNRFLDTELDDADALYILGDLFEVWVGDDLAAPFALELAHKLKQVSQTLPIFFIHGNRDFMLGKRFAEAAGMQLLPEVTCIELYGVKTVILHGDSLCTLDKAYQRFRKLRSFACARWLYSCLPKKRRQAIANKIRSNSQSSNQQKSYVIMDVEPSAVNALFVKTHTTRMIHGHTHRPAIHIVDNACQRIVVGDWYEQGSVLSVSANGVDLKSLPFETT
|
Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
Q8EG24
|
Q5A201
|
GZF3_CANAL
|
Transcriptional regulator GZF3
|
Candida
|
MSMSDIQQRPQIPTTTTAAVAAAASTNVNTGAATTSTATTGNTPTTTPTSPIENISKVPVKPSVDVPVKPKLEQQQQQQSEQSSKPPPPPPEQQQQHQLPTPPIKPPKTGTTSSSSSTTTSSATSSKISMSGPVCGNCQTQTTPLWRRDETGQVLCNACGLFLKLHGRPRPISLKTDTIKSRNRVKQNGSNSQSSKSSGANTPELKSKEGKSGKKSPKSKKKSLGNGNGNGNSSHDHNTLTPLLPATSNNTPTFKSTTSQSQHQQNQNHHHQHHNHHHHLPNHVLQTHQVPLHYPSSTPTQFAPGLQRITSPLLLSTTSSSSSIRTEPNNNNTSKLTPIQAAAGALENMSNELGPSATFKKGNNINGISLMNKTKKDVSSINGSSTSLSSSSASSSIFSSVAPSTSSSSSLSNGTTINNPAPKLPTLGSKISSPSSQPFTRSTTPLQTLPPLHKIASHESSLPPLHNISTYNNNNSGGGADGGQQSMANYSQTNRSPINGNQDNNNNNNNNNNNNNNGNNNGNNNSNNNGNNFTASAHEVTLLKTRISELELVNDLYRTRIMELEAMEQAARLRENSMKKRLDEVMNLQINYQNLLNNNGGMSSQTQPQPSQQPQQAGQYYSNNNNNNNNDQGSQSISPNVSITGSTTITSPNSRSKIISETTPTHHQQQQGGVGAGDNESIILPPLKRNRTDELTDANGNGNGNDNKKVKI
|
Probable transcription factor involved in response to fluconazole, LiCl, and copper.
|
Q5A201
|
Q5XC23
|
Y905_STRP6
|
UPF0122 protein M6_Spy0905
|
Streptococcus
|
MNTMEIEKTNRMNALFEFYAALLTDKQMNYIELYYADDYSLAEIADEFGVSRQAVYDNIKRTEKILETYEMKLHMYSDYVVRSEIFDDMIAHYPHDEYLQEKISILTSIDNRE
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein.
|
Q5XC23
|
B2GD42
|
RNC_LIMF3
|
Ribonuclease III
|
Limosilactobacillus
|
MITQLQDYLAKTYGIHFNNPALLAEAFTQASYVNEHPHENLKYYERIEFLGDAVLQLFVSEYIYRRYPELPQGKLTRLRAAMVCEDSFSKFAKECHFDQYIRLGKGEEMAGARNRASLLCDIFESFIGALYLDQGRQAVEQFIQTVIFPKLDLGWFDHAVDAKTSLQEFLQRNGDVAIEYDLLSEGGTENDPVFEVEVTVDGKKVATGQGSSKKHAEMEAAKHALEKLRMDK
|
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.
|
B2GD42
|
Q73SK9
|
Y4064_MYCPA
|
Putative S-adenosyl-L-methionine-dependent methyltransferase MAP_4064c
|
Mycobacterium avium complex (MAC)
|
MTVPNDDTWGPATSVGTTATMAAAARAIATRDGVINDPFAEPLVRAVGVNFLTRWAIGELVASDVDVEGSPWGLAQMPASIAARTRYFDEFYADAAAAGIRQAVILASGLDTRAYRLDWPAGMTVFEIDQPAVIEFKTTALARLGAEPKADLRTVAVDLRDDWSTALATAGLDSSKPTAWIAEGLFGYLAPEAQDGLLDAVTALSTPGSRLGSEAVPNTADMDPHAARERMRAATAKWRDHGFELDVDVISFAGERHDVGAYLQAHGWTTVATPMAELLADHGLPAIARADDDRQTMNGVTYYTSTLGTGRQR
|
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
|
Q73SK9
|
Q9PQE6
|
SCPA_UREPA
|
Segregation and condensation protein A
|
Ureaplasma
|
MNRMSEKQIQNSLFEYKFIDFNGPLDTLCVLIKQKRLDINNLDILELSKQYVNFVNQLIKTIDIDILGDHLAMASYLLELKTRMLMPTVDEKQIMSIEEDRQNLIDRLIEYNGYKNLSEHLKQRFEFRATMMDLPQQDYEQFYLKDAIYKPLPNHLDSMILKNIMDKIIYENELKNYKINKIKVHEYDVKQLEQLLLNYLKQSPNQQASMLSFFDIQAVIDKNKRFFAIMFLIILILINRNEILFEELDNDYLLKINIERVVDDYNSSSVEQAKNLTSNLTKDTIINFKGEDNE
|
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves.
|
Q9PQE6
|
Q03NS1
|
THIE_LEVBA
|
Thiamine-phosphate pyrophosphorylase
|
Levilactobacillus
|
MSVTFEPGLLRAYFVAGSQDVPGQDLRDVLAKMLAAGITAFQFRDKATSTLTPEQRLALGRDLRAQCRVANVPFIVDDDVELALALDADGIHVGQSDQRVQQVIQAVAGRNIFVGLSCSTMAEVTAANAIAGIDYIGSGPIFPTISKADADPVVGTAGLQKLVAQSRVPVVAIGGVTVDSLPAIAETGAAGVAVITLLTHSHDVDADTAAMRQAFSK
|
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
|
Q03NS1
|
O74935
|
ACOX2_YARLI
|
Acyl-coenzyme A oxidase 2
|
Yarrowia
|
MNPNNTGTIEINGKEYNTFTEPPVAMAQERAKTSFPVREMTYFLDGGEKNTLKNEQIMEEIERDPLFNNDNYYDLNKEQIRELTMERVAKLSLFVRDQPEDDIKKRFALIGIADMGTYTRLGVHYGLFFGAVRGTGTAEQFGHWISKGAGDLRKFYGCFSMTELGHGSNLAGLETTAIYDEETDEFIINTPHIAATKWWIGGAAHTATHTVVFARLIVKGKDYGVKTFVVQLRNINDHSLKVGISIGDIGKKMGRDGIDNGWIQFTNVRIPRQNLLMKYTKVDREGNVTQPPLAQLTYGSLITGRVSMASDSHQVGKRFITIALRYACIRRQFSTTPGQPETKIIDYPYHQRRLLPLLAYVYALKMTADEVGALFSRTMLKMDDLKPDDKAGLNEVVSDVKELFSVSAGLKAFSTWACADVIDKTRQACGGHGYSGYNGFGQAYADWVVQCTWEGDNNILTLSAGRALIQSAVALRKGEPVGNAVSYLKRYKDLANAKLNGRSLTDPKVLVEAWEVAAGNIINRATDQYEKLIGEGLNADQAFEVLSQQRFQAAKVHTRRHLIAAFFSRIDTEAGEAIKQPLLNLALLFALWSIEEDSGLFLREGFLEPKDIDTVTELVNKYCTTVREEVIGYTDAFNLSDYFINAPIGCYDGDAYRHYFQKVNEQNPARDPRPPYYASTLKPFLFREEEDDDICELDEE
|
Oxidizes strain chain acyl-CoAs with a chain length of 10 to 14 carbons. Also active toward the 2S isomers of acyl-CoA-esters containing a 2-methyl group.
|
O74935
|
P28363
|
RPA1_EUPOC
|
DNA-directed RNA polymerase I largest subunit
|
Euplotes
|
MATIFDSLISSRLDGTRFSFYNDEEIQQMSVKEIHNPMAYDELNNPTSHGICDESMGVSALDKLSKCKTCGCDSVYCPGHMGHIKLTSTCYNPFTMKLLHSLLKSKCLVCHRLRISPKRIELFEIRLKLIKLGYLVEAEKLSDFNHFSLESIDSAIRILRKKTKGKTNKKEEKEDSEEVEEDKYAAKEALENLIQKEKENREIFYSHISSILQEDTPNESIGNAITVAIRDITKEIMNSVVPSKCPHCDVCNPRIKKDGATKFFQMPLSNRDTKAMLSSHGRIDMRIDISTMGAISEYDEEDDESSGESEVREGDEEQEKKQKYLSPIEVLEHMRRLWDVEDTLLNELFDNYKIFFMNNLLVSQNRFRPESSGGKQSGDDRDYLHAHSAMLTKIINANIAFRRTIELKENLTDDRNLETESEKSKTQQIDLSKTEITSKQVIKAWAELQESVNCYLDSSLAAKLENKEKPGLRQLLERKEGIFRMKMMGKRVNFAGRSVISPDPYISTDQIGVPEFIARTITFPEPAKNIEKLKRCVINGAHKHPGANFIEYPNGERKALENMTLEEKKQSSIIRKWRKIVYRHMQTGDPLLVNRQPTLHKPSIMAHNAIILPKEQTIRMHYSNCKSYNADFDGDEMK
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. RNA polymerase I is essentially used to transcribe ribosomal DNA units.
|
P28363
|
A4YKQ8
|
ISPG_BRASO
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
unclassified Bradyrhizobium
|
MNKPETVTENSLASDVAGPAPRHQTTKVMVGNVAVGGGAPIVVQSMTNTDTADVDSTVAQVAALARAGSEMVRITVDRDEAAAAVPHIREQLDKRGITTPLIGDFHYIGHKLLTEYPACAEALAKYRINPGNVGFKDKRDTQFSTIIELANKYGKPVRIGANWGSLDQELLSKLMDENAASANPRNARAVMREAMVQSALHSAERAQELGMPKDRIILSAKVSAVQDLIAVYQDLAARSDYAIHLGLTEAGMGSKGIVASSAALGILLQQGIGDTIRISLTPEPGGDRTLEVQVAQELLQTMGFRTFVPLVAACPGCGRTTSTTFQELARSIQDFIRDEMPTWKIKYPGVEALNVAVMGCIVNGPGESKHANIGISLPGTGEAPAAPVFVDGKKFRTLRGPTIAADFKALVIDYIDQRYGSGAKAPESVTAAE
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
A4YKQ8
|
Q9C9R6
|
PUM7_ARATH
|
Putative pumilio homolog 7, chloroplastic
|
Arabidopsis
|
MDEFREASSVSSSPSTPLRTPLHSPNLFNGDFSVSNRFSFKSSSDYSLSSSFSNGLCSPEDSSSPFSSPPFNGIIPKHNHTSSSPVSFDSLFFKDHEKSHVNGTDDLGLCEDLYRMNIKEDVEEDQIRYARTETLKDPLPKSDHTDFTPDPLYNFSPKHYEPSNGGFVSGGFPYGFFRPPKESSINQSCASWSGFDQSKNDDKRNMFGNNPQQFGWPSYSSSNSGTSPYNNGQEIFENRGGMREYSAYSPPHQPEVSYKHQNYRTTTSDILPLFCQRTQVPMVSKCSEPFSSDESFFMNGKSIDHQRSNTRALMSNNGNPTEICHPSLPNMCDIQGYVYLMAKDQHGCRFLQRIFDEGTSVDAMIIFNEVIAHVVELMMDPFGNYLMQKLLDVCTEEQRTQIVLVATEEPGQLIRISLNAYGTRVVQRLVETIRSGKQISLVKLALRPGFLDLIKDLNGNHVIQRCLQCLSTEDNKFIFDAATKFCTEIATHRHGCCVLQKCIAYSMRQQREKLIAEISRNSLLLAQDPFGNYAVQFVIELRIPSAVAMMLAQLKGHYVQLSMQKFSSHMVERCLMHCPESRPQIVRELVSVPHFDQLLQDPYANFVIQAALAATKGPLHASLVEVIRPHSILRNNPYCKRIFSRNLLKK
|
Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
|
Q9C9R6
|
B7V665
|
RS13_PSEA8
|
30S ribosomal protein S13
|
Pseudomonas
|
MARIAGVNIPDNKHTVISLTYIYGVGRTTAQSICAATGVNPAAKIKDLSDEQIDQLRNEVAKITTEGDLRREINMNIKRLMDLGCYRGLRHRRGLPVRGQRTKTNARTRKGPRKPIRK
|
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.
|
B7V665
|
Q13E56
|
RNPH_RHOPS
|
tRNA nucleotidyltransferase
|
Rhodopseudomonas
|
MRPSRRAPDELRAVSLERGVVKYAEGSCLVKFGDTHVLVTATLEERLPPWLKGQGRGWVTAEYGMLPRATLERTRREAAAGKQNGRTVEIQRLIGRSLRAIVDLQALGERQITVDCDVLQADGGTRTASITGAWVALADCLGWMKTRNMIKGTVLRDNVAAISCGIYNGTPVLDLDYAEDSEAETDANFVMTGDGRIIEVQGTAEKTPFSQDEFLALMALAQKGVTRLVDLQKMAVA
|
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
|
Q13E56
|
Q2GJV4
|
RS15_ANAPZ
|
30S ribosomal protein S15
|
phagocytophilum group
|
MSITPSKKSELISEYRIKEGDTGSAYVQCAILSERIRNLTEHLRIHKKDYHCRRGLMVLVCKRRKRLQYIKNKYGSDLYLDLVKKLGIRDVFH
|
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
|
Q2GJV4
|
A5E8V7
|
PNCB_BRASB
|
Nicotinate phosphoribosyltransferase
|
unclassified Bradyrhizobium
|
MTVTDIASRTYNHGWRLDPIVRSLLDTDFYKLLMLQMIREFYPDQKVTFSVINRTKRVRLGDVIDEGELRAQLDHARTIRFTKKELIWLAGNTFYGKTHMFSPDFLAWLAHFRLPDYELHKADGQYELHFHGPWTHTTMWEIPALAIVNELRSRQAMKGQGRFALDVLFARAKAKLWAKVERLRRLEGLRLSDFGTRRRHGFLWQRWCVEAVKEGLGPSFTGTSNVLLAMDNDLEAIGTNAHELPMVAAALARDDDELRFAPYRILDQWRQTYAGNLLIALPDAFGTKAFLRDAPDWVADWTGFRPDSAPPIEAGEEIIAWWKSKGRDPKQKLLVFSDAMDVESIEQIHHRFSDRVRLSFGWGTNLTNDFVGCAPDGSVDLDPISLVCKVTSVDGQPAVKLSDNPEKATGDPAEIARYLRVFGDAGRVRTPVVV
|
Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
|
A5E8V7
|
A5VZ39
|
Y988_PSEP1
|
Nucleotide-binding protein Pput_0988
|
Pseudomonas
|
MRLIIVSGRSGSGKSTALDVLEDSGFYCIDNLPAGLLPQLAENALINTELLQPKVAVSIDARNLPSHLMRFPELLEEARARHIQCDVLYLDADEEVLLKRFSETRRRHPLTNANRSLAEAIRVESDLLGPIADLADLKIDTTNLNLYQLRDSIKLRLLNQPEPGTAFLVESFGFKRGMPVDADLVFDVRCLPNPYWKPELREHSGLDQPVIDYLAAQPDVEDMYNDISSYLLKWLPRFAASNRAYVTIAIGCTGGHHRSVYITERLGQQLQQTLKNVQVRHRDL
|
Displays ATPase and GTPase activities.
|
A5VZ39
|
P94123
|
ACP_AZOBR
|
Acyl carrier protein
|
Azospirillum
|
MSDVAERVKKIVVDHLGVEESKVTENASFIDDLGADSLDTVELVMAFEEEFGCEIPDDAAEKILTVKDAIDFIKANAAA
|
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
|
P94123
|
Q5M2R5
|
EFP_STRT2
|
Elongation factor P
|
Streptococcus
|
MIEASKLRAGMTFVTNDGKLLKVLEASHHKPGKGNTIMRMKLRDVRSGSTFDTSYRPEEKFEQAIIETVPAQYLYQMDDTAYFMNTETYDQYEIPVVNVQEELKFILENSDVKIQFYGTEVIGVQVPTTVELTVTETQPSIKGATVTGSGKPATLETGLVVNVPDFIEAGQKLVINTAEGTYVSRA
|
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
|
Q5M2R5
|
Q1ACI4
|
PETL_CHAVU
|
Cytochrome b6-f complex subunit VI
|
Chara
|
MFTVISYLSLLFISFLFALTLFIVLNKIELI
|
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. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
|
Q1ACI4
|
Q92I62
|
LSPA_RICCN
|
Signal peptidase II
|
spotted fever group
|
MLPLLKKLYLTFARSSRIIITLVIIDQLSKWWFIDNLRWKSGLMLKVTSFLNMVYTWNYGISFGLMREYYQYSNAIFLITNTIIVCYLYYLMIRSKTIGSFAGYSFVIGGAVGNLIDRFFRGAVFDFIHFHYQNYSFPVFNLADCFIIIGVIILIEDYYSTKKVIEEKAKGNYDNAQIEAMAEKIRNTDKGGNDKIASLQN
|
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
|
Q92I62
|
Q3BWY7
|
EFG_XANC5
|
Elongation factor G
|
Xanthomonas
|
MARTTPIERYRNFGIMAHIDAGKTTTSERILFYTGVSHKIGEVHDGAAVMDWMEQEQERGITITSAATTAFWSGMDKSMPQHRFNIIDTPGHVDFTIEVERSLRVLDGAVFVLCAVGGVQPQSETVWRQANKYSVPRMAFVNKMDRTGANFDKVVEQLKARLGAYAVPMQVPIGAEDGFEGVVDLLKMKAIHWDTASQGTTFEYRDIPADLVDVATEARSFMVEAAAEASEDLMDKYLNEGDLSEQEILSGLRERTLKVEIVPVFCGSAFKNKGVQAMLDGVVHLLPSPADRPPVQGIDEDEKEDTRAATDTAPFSALAFKIMTDPFVGSLTFFRVYSGTLNSGDQVYNPVKSKKERVGRILQMHSNNREEIKEVRAGDIAAAVGLKDVTTGDTLCAQDKIITLERMVFPEPVISMAVEPKTKSDQEKMGMALGRLAQEDPSFRVKTDEESGQTIISGMGELHLDIIVDRMRREFNVEANVGKPQVAYRETIRKSDVKSDYKHAKQSGGKGQYGHVVIELSPMTEEERKSENVKDDFLFINDITGGIIPKEFIPSVEKGLRETITSGPIAGFPVVGVKVKLVFGSYHDVDSSEMAFKLAASMAFKQGFAKASPVLLEPIMKVEIVSPEDYLGDVMGDVSRRRGVLQGQDDSPSGKIINAMIPLGEMFGYATSLRSMSQGRATFSMEFDHYEEAPANIADAVTKKG
|
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
|
Q3BWY7
|
E5KGE0
|
BRIZ1_ARATH
|
BRAP2 RING ZnF UBP domain-containing protein 1
|
Arabidopsis
|
MFILRVHSVDSERPISVEEEESGFTYASKRAQPPLKLIQPSLKLTDRKGLIHLYRKSSHSSLPNPSSRSTTLFIVAVPNYLSSLDFIRFCDSRISQVSDILFIRNDGMEDRYSVLITFSDQSEADGFYNNLNGKKFAPSEAEVCHILYVMSVEHTEFDEVAAEAPTGFTELPTCPICLERLDPDTSGIVSTLCDHSFQCSCTSKWTYLSCQVCRLCQQQDEILNCSICGKTENVWACLVCGFVGCGRYKEGHSIRHWKETHHCYSLDLRTQQIWDYVGDSYVHRLNHSKIDGKSVEMSTSCLSHQGDCGLCECSEDTGISGAIFNSKVDSIVIEYNDLLASQLKGQRQYYESLIVEARSKQESSIAEAVEQIVVNTMQELQNKIEKCEEEKSGITEVNTKLIKEQDTWRKKAKEIEEREAALLGSKDEMITDLQEQIRDITVFIEAKKTLKKMSSDTDGIREGTVLPVPISPEPVSSVRRQKKSNRRK
|
RING-type ubiquitin E3 ligase required for seed germination and post-germination growth.
|
E5KGE0
|
Q06RC1
|
RBL_JASNU
|
Ribulose bisphosphate carboxylase large chain
|
Jasminum
|
MSPQTETKASVGFKAGVKEYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGETDQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETGEIKGHYLNATAGTSEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVKARNEGRDLASEGNVIIREAAKWSPELSAACEVWKEIRFDFKAVDTLDPEK
|
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.
|
Q06RC1
|
Q12MI8
|
SYM_SHEDO
|
Methionyl-tRNA synthetase
|
Shewanella
|
MTQSQRKILVTSALPYANGPIHLGHMLEYIQTDIWSRFQKMRGHECHYICADDAHGTPIMLKAQQLGIAPEAMIAQVQIEHEQDFADFNVAFDNFHSTHSEENRELASDIYIKLRDAGHIKTKTISQLYDPEKSMFLPDRFVKGTCPKCKSDDQYGDNCDSCGATYSTTDLINPRSAVSGATPVMKDTEHFFFDLPAFEGMLKEWIHSGSLQSEMANKLNEWFEQGLQQWDISRDAPYFGFEIPDAPGKYFYVWLDAPIGYMGSFKNFCAKRGDINFDDFWAKDSTAEVYHFIGKDIVYFHSLFWPAMLEGAGLRKPTSVYAHGYVTVNGAKMSKSKGTFIKARTYLDHLDPEYLRYYYAAKLSSRIDDLDLNLEDFAQRVNSDLVGKLVNLASRTAGFISKRFDGKLANVTDNSLAESFIAKQEVIAEFYEAREYGKAMREIMAMADIANGFVAEQAPWQLVKDDDKQAQAHEVCSIALNLFRILTTYLKPVLPRLSQDVEAFMQLELTWDNLAKDMTAHEIAPFKAMMQRVDLDKVAAMVDASKDNLQPTEAPKADKKADKKVEKKATTGDPLTDDPISDEISFEDFAKLDLRIALIAKAEHVADADKLLKLQLDLGGVTKQVFAGIKSAYAPEDLEGKLTVMVANLAPRKMRFGMSEGMVLAAGPGGDELWILEPHQGAKPGMRVK
|
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
|
Q12MI8
|
A0KQA8
|
RL1_AERHH
|
50S ribosomal protein L1
|
Aeromonas
|
MAKLSKRMRVIREKVDGTKEYSINEAIALLKELATAKFVESVDVAVNLGIDARKSDQNVRGATVLPHGTGREVRVAVFTQGANAEAAKAAGAELVGMDDLADLVKKGEMNFDVVIASPDAMRVVGQLGQILGPRGLMPNPKVGTVTPNVAEAVKNAKAGQVRYRNDKNGIIHTTLGKVSFNEVQLKENLEALLVALKKAKPSSAKGVFIKKVSISTTMGAGVAVDQASLEAQA
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
A0KQA8
|
Q5KXJ2
|
SP2AB_GEOKA
|
Stage II sporulation protein AB
|
Geobacillus thermoleovorans group
|
MRNEMHLQFSARSENESFARVTVAAFVAQLDPTMDELTEIKTVVSEAVTNAIIHGYNNDPNGIVSISVIIEDGVVHLTVRDEGVGIPDIEEARQPLFTTKPELERSGMGFTIMENFMDEVIVESEVNKGTTVYLKKHIAKSKALCN
|
Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.
|
Q5KXJ2
|
Q110M9
|
PYRG_TRIEI
|
UTP--ammonia ligase
|
Trichodesmium
|
MTKFVFITGGVVSSIGKGIVAASLGRLLKSRGYSVSILKLDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFTDTSMSRLNSVTQGSIYQAVINKERRGDYQGGTVQVIPHITNEIKERIHRVAKNANPDVVITEIGGTVGDIESQPFLEAIRQFRKDVRRNNALYIHVTLVPWIASAGEMKTKPTQHSVKELRSIGIQPDILVCRCDRKLSEGLKEKMSEFCDVPVESVITSQDAQSIYEVPLMLETEGLAVQALELLKMEQRQPNLSHWKTLVNRLYHRDKQDIRTSQGKLSITATVEIAIVGKYIQLSDAYLSVVEALRHAAIAVGVDLNLHLVNAEDVETKGARTYLEKANGIIVPGGFGVRGIDGKIATVEYARINKIPFLGLCLGMQCAVIEWARNIAKLDAAHSFEFDPQTPNPVINLLPEQQDVVDLGGTMRLGLYPCRLQGDTLAFKTYQQEVIYERHRHRYEFNNAYRNLFKETGYIISGTSPDGRLVEIIELPAHPFFIATQFHPEFQSRPSTPHPLFHNFFQAANSQEKCDNLSVNNTEETPDNLVSKSSIPN
|
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
|
Q110M9
|
Q8S0G4
|
GPDH1_ORYSJ
|
Probable glycerol-3-phosphate dehydrogenase [NAD(+)] 1, cytosolic
|
Oryza sativa
|
MVGSVHVNGSVNGGNGTEERLDELRRLLGKSDGDLLKIVGIGAGAWGSVFAALLQDAYGRFREKVQIRIWRRAGRSVDRTTAEHLFEVINSREDVLRRLIRRCAYLKYVEARLGDRTLYADEILRDGFCLNMIDTPLCPLKVVTNLQEAVWDADIVVNGLPSTETREVFEEISKYWKERISVPVIISLAKGIEASLDPIPRIITPTQMISSATGVPTENILYLGGPNIASEIYNKEYANARICGSNKWRKPLAKFLRQPHFIVWDNSDLVTHEVMGGLKNVYAIGAGMVAALTNESATSKSVYFAHCTSEMIFITHLLTEQPEKLAGPLLADTYVTLLKGRNAWYGQMLAKGELSPDMGDSIKGKGMIQGISAVGAFFELLSQPSLSVQHPEENKQVAPAELCPILKRLYRILIKRELSTRDILQALRDETMNDPRERIEMAQSHAFYRPSLLGKP
|
May be involved in cell redox homeostasis.
|
Q8S0G4
|
Q6QT55
|
ANDR_MACMU
|
Nuclear receptor subfamily 3 group C member 4
|
Macaca
|
MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLQQQQQQQQETSPRQQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSAPECHPERGCVPEPGAAVAAGKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLEGTSTISDSAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPVLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGAGEAGAVAPYGYTRPPQGLAGQEGDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETAQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ
|
Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3.
|
Q6QT55
|
Q9SAC9
|
AP1M1_ARATH
|
Mu1-adaptin 1
|
Arabidopsis
|
MAGAASALFLLDIKGRVLVWRDYRGDVTAAQAERFFTKLIETEGDSQSNDPVAYDNGVTYMFVQHSNIYLMIASRQNCNAASLLFFLHRVVDVFKHYFEELEEESLRDNFVVVYELLDEMMDFGYPQFTEARILSEFIKTDAYRMEVTQRPPMAVTNSVSWRSEGLKFKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDRILLEAQGRAIKGKAIDLEDIKFHQCVRLARFENDRTISFIPPDGSFDLMTYRLSTQVKPLIWVEAHIERHSRSRVEMLVKARSQFKDRSYATSVEIELPVPTDAYNPDVRTSLGSAAYAPEKDALVWKIQYFYGNKEHTLKADFHLPSIAAEEATPERKAPIRVKFEIPKFIVSGIQVRYLKIIEKSGYQAHPWVRYITMAGEYELRLM
|
Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting at the trans-Golgi network and early endosomes (TGN/EE). The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. Functions redundantly with AP1M2 in multiple post-Golgi trafficking pathways leading from the TGN to the vacuole, the plasma membrane, and the cell-division plane.
|
Q9SAC9
|
Q87SA6
|
MUTH_VIBPA
|
Methyl-directed mismatch repair protein
|
Vibrio
|
MKPEPQSEAELMERAHDIAGLSFAELADEAGMTVPENLKRDKGWVGQLLEWHLGAPAGSKPQQDFSKLGIELKSIPIGYNGRPLETTFVCVAPLTGVQGLTWETSHVRNKLSRVLWVPVEGEREIPLAERRVGTPLIWSPDKEEEQILRNDWEELMEMIVFGKFDQISARHGEALHLRPKAANAKALTEAYSSNGKPMKTLPRGFYLRTQFTEQILLKHYINVQSE
|
Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair.
|
Q87SA6
|
B6EJA2
|
TRPA_ALISL
|
Tryptophan synthase alpha chain
|
Aliivibrio
|
MDRYQALFAKLAEKNQGAFVPFVTIGDPNPELSYEIMDTLVKAGADALELGIPFSDPLADGPTIQGANIRALNSKTTPIVCFDLIAKIRAKYPETPIGLLVYANLVFANGIDTFYTKCQQAGVDSVLIADVPTNESEEFRTSAIKHNVHPIFIAPPSASDETLETVAKLGGGYTYLLSRAGVTGAETKAGMPVAQLLARLNQFDAPPAILGFGISEPAQVEEAIKAGAAGAISGSATVKIIEQHQDNPAALLDALTAFTSAMKAATQK
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
B6EJA2
|
A9BEF8
|
ACCA_PROM4
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
|
Prochlorococcus
|
MARRYLLEFEKPLVELEKQIEQIRELARDSEVDVSQQLLQLETLAARRREEIFNALTPAQKIQVARHPQRPSTLDFIQMFCDDWVELHGDRNCSDDKALIGGIARIEEKSVLVIGQQKGRDTKENVARNFGMAKPGGYRKALRLMNHADRFKLPIISFIDTPGAYAGLLAEEQGQGEAIAVNLREMFRLRVPIISTVIGEGGSGGALGIGVADRLLMFEHSVYTVASPEACASILWRDAGKAPDAAAALKITGSDLMALGIVDEVLSEPSGGNNWAPLKAGEVLKESLIRNLRELDSLSIRQLRDKRYEKFRQMGRFLEPSSLDEELIT
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
|
A9BEF8
|
Q139A7
|
MIAA_RHOPS
|
Isopentenyl-diphosphate:tRNA isopentenyltransferase
|
Rhodopseudomonas
|
MFGLQMSVATSDMNGSDPGQPGQRPAAVLIAGPTASGKSALALRLAQARDGVVINTDSMQMYRDLRIITARPTAEEEALAAHRLYGSVDAAVNFSAGAYVEAAAGALAEARAAGRLPIFVGGTGLYFKALTRGLSAVPPVAAEVRDAVRLRLDRDGVLALHAELARHDPAGAARLAPADRSRIARALEVVLATGRPLADWHNQASPPLLPPEGFVAMFLAPEREALYGRIDARFAAMLQAGALEEVAALAARNLDPLLPAMKAHGVPALIRHFRGELSLEEAAAIGAADTRHYAKRQFTWFRHQLPEFRWVTPEQAESGLLGT
|
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
|
Q139A7
|
P84614
|
SCX28_HOTTS
|
Alpha-toxin Bs-Tx28
|
Mesobuthus
|
GVRDAYIADDKNCVYTCGSNSYCNTECTKNGAESGYCQWFGRWGNGCWCIKLPDKVPIRIPGKCR
|
Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin inhibits the inactivation of activated TTX-sensitive sodium channels (Nav).
|
P84614
|
C3MR85
|
RL10_SULIL
|
Acidic ribosomal protein P0 homolog
|
Sulfolobus
|
MKRLALALKQKKVASWKLEEVKELTELIKNSNTILIGSLEGFPADKLHEIRKKLRGKAIIKVTKNTLFKIAAKNAGISTEKLEQYLTGPNVFIFTKDNPFLTNMFFENYKLRRYAMPGDKAEEEVIIPAGDTGMPAGPILSVFGKLKVQTKVQDGKVHVVKDTVVAKPGDVIPTEALPILQKLGIMPVYVKLKIKVAYHEGLVIPAENLKLNLEGYRSNIAEAYRNAFTLAVEIAYPVPDVLKFTINKIFKNAITLASEIGYLTPESAQAVISKAVAKAYALATAISGKVDLGVKLPSAQQTQTQQSTAEEKKEEKKEEEKKGPSEEEIGSGLASLFG
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
C3MR85
|
A1D8A4
|
FEN1_NEOFI
|
Flap structure-specific endonuclease 1
|
Aspergillus subgen. Fumigati
|
MGIKHLFQVIQENAPDAIKAGDIKNHFGRKVAIDASMSIYSFLIAVRSEGQQLMSESGETTSHLMGMFYRTLRMVDNGIKPLYVFDGAPPKLKSGELAKRTARKAEATEAHEEAKETGTAEDVEKFSRRTVRVTREHNAECKKLLKLMGIPYIDAPTEAEAQCAVLARAGKVYAAASEDMDTLCFEAPILLRHLTFSEQRKEPIQEIHLNRTLEGLGMDRKQFIDLCILLGCDYLEPIPKVGPNTALKLIREHGSLEKVVEAIENDPKKKYVIPEDWPYQDARELFLHPDVREADHPECDFKWEAPDVEALVEFLVKDKGFNEDRVRNGAARLQKNLKTAQQSRLEGFFKPVARTDEEKASLKRKHDEKLQEQKKRKKEEAKAKKEAKAKPRGAA
|
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
|
A1D8A4
|
B4M703
|
TRMB_DROVI
|
tRNA(m7G46)-methyltransferase
|
Drosophila
|
MVTNSQEGETLPATSSVTGLPQKRFYRQRAHSNPIADHSFDYPARPEDVDWRSLYPNIGSEQQVEFADIGCGYGGFLVTLGEMFPDKLAIGMEIRVKVSDYVIDRIAALRMKNAETSAYQNIACIRTNAMKYLPNYFQKSQLEKMFFLYPDPHFKRAKHKWRIINQALLSEYAYVLRSGGLVYTMTDVEDLHKWIVSHMTQHPLYERLTDEEANADPITPKLYQSSEEGAKVVRNKGDHFLAIFRRI
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
B4M703
|
P50075
|
GYRBS_STRNV
|
DNA gyrase subunit B, novobiocin-sensitive
|
Streptomyces
|
MADSGNPNENTPSVATGENGEVTGSYNASAITVLEGLDAVRKRPGMYIGSTGERGLHHLVTEVVDNSVDEALAGHADTIDVTILADGGVRVVDNGRGIPVGIVPSEGKPAVEVVLTVLHAGGKFGGGGYSVSGGLHGVGVSVVNALSTKVAVEVKTDGYRWTQDYKLGVPTRRCAQNEATDETGTTVTFWADPDVFETTEYSFETLSRRFQEMAFLNKGLTLKLTDERESAKAVVGADVAGTDSAETPGEEPVRSVTYYYEGGIVDFVKYLNSRKGDLIHPTVIDIDAEDKERMLSVEIAMQWNSQYSEGVYSFANTIHTHEGGTHEEGFRAAMTGLVNRYAREKKFLREKDDNLAGEDIREGLTAIISVKLGEPQFEGQTKTKLGNTEAKTFVQKIVHEHLTDWFDRHPNEAADIIRKSIQAATARVAARKARDLTRRKGLLESASLPGKLSDCQSNDPSKCEIFIVEGDSAGGSAKSGRNPQYQAILPIRGKILNVEKARIDKILQNTEVQALISAFGTGVHEDFDIEKLRYHKIILMADADVDGQHINTLLLTFLFRFMRPLVEAGHVYLSRPPLYKIKWGRDDFEYAYSDRERDALVELGKQNGKRIKEDSIQRFKGLGEMNAEELRITTMDVDHRVLGQVTLDDAAQADDLFSVLMGEDVEARRSFIQRNAKDVRFLDI
|
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
|
P50075
|
Q9AGA7
|
PTUCB_KLEPN
|
PTS system alpha-glucoside-specific EIIB component
|
Klebsiella
|
MLSQIQRFGGAMFTPVLLFPFAGIVVGIAIMLRNPMFVGEALTAPDSLFAQIVHIIEEGGWTVFRNMPLIFAVGLPIGLAKQAQGRACLAVLVSFLTWNYFINAMGMTWGHFFGVDFSAEPTAGSGLTMIAGIKTLDTSIIGAIVISGLVTALHNRYFDKPLPVFLGIFQGSSFVVIVAFLAMIPCAWLTLLGWPKVQLGIESLQAFLRSAGALGVWVYIFLERILIPTGLHHFVYGPFIFGPAVVEGGLQVYWAEHLQAFSQSTEPLKTLFPEGGFALHGNSKVFGSVGIALALYFTAAPENRVKVAGLLIPATLTAMLVGITEPLEFTFLFISPLLFAVHAVLAATMATVMYICGVVGNFGGGLLDQFLPQNWIPMFHHHASMMFIQIGIGLCFTALYFVVFRTLILRLNLKTPGREESEIKLYSKADYQAARGKTTAAAAPETRLGQAAGFLQALGGADNIESINNCATRLRIALVDMAKTQSDDVFKALGAHGVVRRGNGIQVIVGLHVPQVRDQLENLMKDSLSTEHTTMTEAVS
|
Involved in the transport and simultaneous phosphorylation at O-6 of the glucosyl moiety of sucrose and its five linkage-isomeric alpha-D-glucosyl-D-fructoses. Can also transport maltose, isomaltose and maltitol, phosphorylating at O-6 of their non-reducing glucose portion.
|
Q9AGA7
|
P32198
|
CPT1A_RAT
|
Carnitine palmitoyltransferase 1A
|
Rattus
|
MAEAHQAVAFQFTVTPDGIDLRLSHEALKQICLSGLHSWKKKFIRFKNGIITGVFPANPSSWLIVVVGVISSMHAKVDPSLGMIAKISRTLDTTGRMSSQTKNIVSGVLFGTGLWVAVIMTMRYSLKVLLSYHGWMFAEHGKMSRSTKIWMAMVKVLSGRKPMLYSFQTSLPRLPVPAVKDTVSRYLESVRPLMKEEDFQRMTALAQDFAVNLGPKLQWYLKLKSWWATNYVSDWWEEYIYLRGRGPLMVNSNYYAMEMLYITPTHIQAARAGNTIHAILLYRRTLDREELKPIRLLGSTIPLCSAQWERLFNTSRIPGEETDTIQHIKDSRHIVVYHRGRYFKVWLYHDGRLLRPRELEQQMQQILDDPSEPQPGEAKLAALTAADRVPWAKCRQTYFARGKNKQSLDAVEKAAFFVTLDESEQGYREEDPEASIDSYAKSLLHGRCFDRWFDKSITFVVFKNSKIGINAEHSWADAPVVGHLWEYVMATDVFQLGYSEDGHCKGDTNPNIPKPTRLQWDIPGECQEVIDASLSSASLLANDVDLHSFPFDSFGKGLIKKCRTSPDAFIQLALQLAHYKDMGKFCLTYEASMTRLFREGRTETVRSCTMESCNFVQAMMDPKSTAEQRLKLFKIACEKHQHLYRLAMTGAGIDRHLFCLYVVSKYLAVDSPFLKEVLSEPWRLSTSQTPQQQVELFDFEKNPDYVSCGGGFGPVADDGYGVSYIIVGENFIHFHISSKFSSPETDSHRFGKHLRQAMMDIITLFGLTINSKK
|
Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion . Plays an important role in hepatic triglyceride metabolism .
|
P32198
|
Q0T2F6
|
AROC_SHIF8
|
5-enolpyruvylshikimate-3-phosphate phospholyase
|
Shigella
|
MAGNTIGQLFRVTTFGESHGLALGCIVDGVPPGIPLTEADLQHDLDRRRPGTSRYTTQRREPDQVKILSGVFEGVTTGTSIGLLIENTDQRSQDYSAIKDVFRPGHADYTYEQKYGLRDYRGGGRSSARETAMRVAAGAIAKKYLSEKFGIEIRGCLTQMGDIPLEIKDWSLVEQNPFFCPDPDKIDALDELMRALKKEGDSIGAKVTVVASGVPAGLGEPVFDRLDADIAHALMSINAVKGVEIGDGFDVVALRGSQNRDEITKDGFQSNHAGGIFGGISSGQQIIAHMALKPTSSITVPGRTINRFGEEVEMITKGRHDPCVGIRAVPIAEAMLAIVLMDHLLRQRAQNADVKTDIPRW
|
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.
|
Q0T2F6
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Q3IDE8
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RECF_PSET1
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DNA replication and repair protein RecF
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Pseudoalteromonas
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MSLSHLSLKYFRNIEALTLEPVNGVNIIYGENGSGKTSLLEAIYYLSHGKSFRTSKHKSIIAHQQEQFVIHGRKAIHDLSIPIGISKTQAGETNLKIQGKASRKISELAQLMPVQIITPESYSLFFGGPKERRKFLDLGLFHVEHEFFFLWQSFNKVLKQRNALLKSKPKNYFDQIKFWDKEFVRLAEQINKLRMAYISRFKQQFFDKMCAELTLIRDLEISFNAGWKESESLSDALELNFERDARQGFTSKGPHKADFSFSVAGSSVENIFSRGQLKLLLYALKVTQNSLIESETDKQSILLIDDLPSELSEDTKEKVGQLLAHCSSQIFISSILSESISAVVEPMQRELQMFHVKHGNLITR
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The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
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Q3IDE8
|
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