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
|
|---|---|---|---|---|---|---|
A7HGZ6
|
TSAD_ANADF
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
unclassified Anaeromyxobacter
|
MRILAIETSCDETAAAIVEDGRRALADVISTQIDIHRRWGGVVPELASRNHVVQVMPVVDEALSRAGVGPDGLDAIAVTSGPGLVGALLVGVQAAKALALAWQKPLVRVNHLEGHLVAAFLSETAPAFPYLGLVVSGGHTSLYAAHGFGDYRLLGQTRDDAAGEAFDKGAKLLGLPYPGGVAIDRLAKEGDARAIRFPKAIVKGADLDFSFSGLKTALLHHVKKHGLPEGKGLADLCASYQEAIVRALVEKAFRAARRLQYDRLVLSGGVAANSRLRGAVAERAREYEGMEVFLPAPRLCTDNAAMIAVAGTHAFLRGERAGADLNADPAWRL
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
A7HGZ6
|
P0CI53
|
SNAAL_LYCMC
|
Neurotoxin LmNaTx21.1
|
Lychas
|
LILVACLMMSCVHCKKDGYPVDWNNCMYDCGYDNAYCEKICKEKGGESGYCYFWKISCYCEGLPDNVEIKGYGRCRG
|
Binds voltage-independently at site-3 of voltage-gated sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission.
|
P0CI53
|
P25929
|
NPY1R_HUMAN
|
Neuropeptide Y receptor type 1
|
Homo
|
MNSTLFSQVENHSVHSNFSEKNAQLLAFENDDCHLPLAMIFTLALAYGAVIILGVSGNLALIIIILKQKEMRNVTNILIVNLSFSDLLVAIMCLPFTFVYTLMDHWVFGEAMCKLNPFVQCVSITVSIFSLVLIAVERHQLIINPRGWRPNNRHAYVGIAVIWVLAVASSLPFLIYQVMTDEPFQNVTLDAYKDKYVCFDQFPSDSHRLSYTTLLLVLQYFGPLCFIFICYFKIYIRLKRRNNMMDKMRDNKYRSSETKRINIMLLSIVVAFAVCWLPLTIFNTVFDWNHQIIATCNHNLLFLLCHLTAMISTCVNPIFYGFLNKNFQRDLQFFFNFCDFRSRDDDYETIAMSTMHTDVSKTSLKQASPVAFKKINNNDDNEKI
|
Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is NPY > [Pro-34] PYY, PYY and [Leu-31, Pro-34] NPY > NPY (2-36) > [Ile-31, Gln-34] PP and PYY (3-36) > PP > NPY free acid.
|
P25929
|
P53218
|
POP6_YEAST
|
RNases P/MRP 18.2 kDa subunit
|
Saccharomyces
|
MINGVYYNEISRDLDISSSTQCLRFLKETVIPSLANNGNNSTSIQYHGISKNDNIKKSVNKLDKQINMADRSLGLQQVVCIFSYGPHIQKMLSILEIFKKGYIKNNKKIYQWNKLTSFDIKREGRNELQEERLKVPILVTLVSDSEIIDLNLHSFTKQ
|
Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.
|
P53218
|
Q7UN13
|
RL16_RHOBA
|
50S ribosomal protein L16
|
Rhodopirellula
|
MALMPKRVKHRKSQRGRIKGNATRGNTVVFGDYGIQSLDAGWIKATTIEAGRIAAQQYVRGQGKLYIRIFPDKSVTSTPLETRMGKGKGEPDFWAAVVKPGTILYELSGVTEQQAKVCFARLASKMPVKVRFVERRSA
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q7UN13
|
P02488
|
CRYAA_MACMU
|
Alpha-crystallin A chain
|
Macaca
|
MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKIQTGLDATHERAIPVAREEKPSSAPSS
|
Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
|
P02488
|
B9KZW3
|
RS13_THERP
|
30S ribosomal protein S13
|
Thermomicrobium
|
MARIAGVDLPRDKRIEYALTLIYGIGWTTARKILERTGIDPWTKVRDLTDDEVQRLRDIIEKEMVVEGDLRRQVAMNIKRLIDIGCYRGLRHRMGLPVRGQRTRTNARTRKGPRPRIGVKKKGKQAGS
|
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.
|
B9KZW3
|
A0RM16
|
RL22_CAMFF
|
50S ribosomal protein L22
|
Campylobacter
|
MSRAIIKFIRLSPTKARLIADEVQGMNAELALASLSFMPNRGAKYIASAISSAVANGGFEPEEVVVKSCRVDAGPVLKRFRPRARGSASRIRKPTSHILVEVSKPESKEA
|
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
|
A0RM16
|
A1B323
|
ISPG_PARDP
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Paracoccus
|
MSHNPIRPWRNIDRRNSRRIMVGNVPVGGDAPISVQTMTNTDTSDVRATLDQIIRAADVGADIVRVSTPDQDSTRALREICRESPVPIVADIHFHYKRAIEAAEAGAACLRINPGNIGDATRVREVIKAARDHGCSIRIGVNAGSLEKHLLEKYGEPCPDAMVESGLDHIRILQDNDFHEFKISVKASDVFLAAAAYQQLADATDAPIHLGITEAGGLTAGTVKSAIGLGNLLWMGIGDTIRVSLSADPVEEVKVGFEILKSLGLRTRGVQIISCPSCARQGFDVIKTVEILEKRLEHIKTPMSLSIIGCVVNGPGEALMTDIGFTGGGAGSGMVYLAGKQNHKMTNAQMVDHIVELVEKRAAEIEAAQSAAAE
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
A1B323
|
A0QX88
|
HIS3_MYCS2
|
Phosphoribosyl-AMP cyclohydrolase
|
Mycolicibacterium
|
MSLDPAIAARLKRNADGLFAAVTQERGTGKVLMVAWMDDDALARTLQTREATYFSRSRGEQWVKGATSGHTQKVHSVRLDCDGDTVLLEVDQVGGACHTGDHTCFDADLLLGPDE
|
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
|
A0QX88
|
A2XED8
|
G1L7_ORYSI
|
Protein G1-like7
|
Oryza sativa
|
MDPSGPGPSSAAAGGAPAVAAAPQPPAQLSRYESQKRRDWNTFLQYLRNHRPPLTLARCSGAHVIEFLRYLDQFGKTKVHASGCAFYGQPSPPGPCPCPLRQAWGSLDALIGRLRAAYEESGGTPESNPFAARAVRIYLREVRDSQAKARGIPYEKKKRKRSQAAQPAGVEPSGSSSAAAAAAGGGDTGSGGGAAATTTAQPGGSGTAPSAS
|
Probable transcription regulator that acts as a developmental regulator by promoting cell growth in response to light.
|
A2XED8
|
B9L8G5
|
CMOB_NAUPA
|
tRNA U34 carboxymethyltransferase
|
Nautilia
|
MDINKVLKERQKWFEWKNIKPIYEKIVQWQIENKQLNVKNVKLNDIIEITLDENKEKLKEIEQIAKMLKPWRKGPFKINDLFIDTEWRSFIKWNIIKPHINLENKDVLDVGCNNGYYMFRMLEMNPKSITGFDPSALFNLQFEFINNFIKSDIEYKLLGVEHIPFYDKKFDTIFCLGVLYHRPDPITMLKELKAGLNPGGEVILDTLIIEGDEEIALCPVRYQKMKNVYFIPTLKALYNWIEKAKFKDVKFIGKRYTDLEEQRKTDWIEGESLNNFLNEDLTKTVEGYPPPLRVYLKLKN
|
Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
|
B9L8G5
|
P11139
|
TBA1_ARATH
|
Tubulin alpha-1 chain
|
Arabidopsis
|
MREIISIHIGQAGIQVGNSCWELYCLEHGIQPDGTMPSDSTVGACHDAFNTFFSETSSGQHVPRAVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTVGREIVDTCLERLRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDFGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVVVLLDNEAIYDICRRSLDIERPTYSNLNRLISQTISSLTTSLRFDGAINVDITEFQTNLVPYPRIHFMLSSYAPVISSAKAYHEQFSVPEITTSVFEPSNMMAKCDPRHGKYMACCLMYRGDVVPKDVNTAVAAIKAKRTIQFVDWCPTGFKCGINYQPPSVVPGGDLAKVQRAVCMISNNTAVAEVFSRIDHKFDLMYSKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGGEGAEDDDEEGDEY
|
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
P11139
|
B2IW30
|
COFH_NOSP7
|
FO synthase subunit 2
|
Nostoc
|
MLTKIAVEKILERALMGYDLSPQEGVVLLQQTEPEAIAAIRATSDTLRHTQAGDMVTYIINRNINFTNICEQHCSFCAFRRDDGDVGAYWLDSAQILEKATDAVRRGATEICMQGGLNPQAQINGKSLPYYLKVVETIKQEFPQIHLHAFSPQEVEFIARLDGLEYADVIIALRDAGVGSMPGTAAEVLDDEVRRILCPEKINTATWLGIVSTAHKLGLHTTSTMLSGHIETHEQQIGHLEKLRSLQQTAINQGYPAKITEFILLPFVGQEAPKPLRRRVGRDQPILSDALLLGAVARIYLGNWIPNHQQSWVKLGLAGATEALVWGCNDIGGTLMEEHITTMAGALGGTCMEVETLKTAIASLGRPYQQRNTLYQKVNS
|
Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.
|
B2IW30
|
Q2NDC1
|
CLPX_ERYLH
|
ATP-dependent Clp protease ATP-binding subunit ClpX
|
Erythrobacter
|
MTKLSGTDSKSTLYCSFCGKSQHEVRKLIAGPTVFICDECVELCNDIIREETKAGLTGRKEGDVPAPSEICATLNDYVIGQDRAKRVLSVAVHNHYKRLKHSGKADGVELAKSNILLVGPTGSGKTLLAQTLARTFDVPFTMADATTLTEAGYVGEDVENIILKLLQASDYNVDKAQHGIVYIDEIDKITRKAENPSITRDVSGEGVQQALLKLMEGTTASVPPQGGRKHPQQEFLQVDTTNILFICGGAFAGLDKIIADRLQKRSIGFGAHVADPDKRKVGELLEKSEPEDLLKFGLIPEFVGRLPVIATLHDLDVDALVTILQEPKNAIVKQYSKLFELEDVELTFTDEALQAIAERAILRKTGARGLRSIVEGILLDTMFDLPDLDDISEVVIDADVVEGKKEPIRVVSNDDDGKKEEAA
|
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
|
Q2NDC1
|
A7H0Z1
|
RS11_CAMC5
|
30S ribosomal protein S11
|
Campylobacter
|
MAKRKIVKKKVVRKSIAKGIVYISATFNNTMVTVTDEMGNAIAWSSAGGLGFKGSKKSTPYAAQQAVEDALNKAKEHGIKEVGIKVQGPGSGRETAVKSVGAVEGIKVTFLKDITPLAHNGCRPPKRRRV
|
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
|
A7H0Z1
|
B4F7E8
|
NIBA2_RAT
|
Protein FAM129B
|
Rattus
|
MGDVLSTHLDDARRQNIAEKTEKILREFLRFYEDQYGVSLFNSMRHEIEGTGPPQAQLLWRKVPLDERIIFSGNLFQYQEDNKKWRNRFSLVPHNYGLVLYENKVAYERQIPPRAVINSAGYKVLTSLDQYLELVGNSLPGTTSKSGSTPILKCPTQFPLILWHPYARHYYFCMMTEAEQDKWQAVLQDCVRHCNNGIPENSKVEGPAFTDAIRMYRQSKEQYGTWEMLCGNEVQILSNLVMEELGPALKTELGPRLKGKPQERQRQWIQISDAVYRLVFEQAKVHFEEVLCKLQLARPAMEAVIRTDMDQIITSKEHLASKIRAFILPKAEVCVRNHVQPYIPSILEALMVPTSQGFTEVRDVFFKEVTDMNLNVINEGGIDKLGEYMEKLSQLAYHPLKMQSCYEKMEPLRLDGLQQRFDVSSTSVFKQRAQIHMREQMDNAVYTFETLLHQELGKGPTKEELCKSIQRILERVLKKYDYDSSSVRKRFFREALLQITIPFLLKKLAPTCKSELPRFQELIFEDFARFILVENTYEEVVLQTVMKDILQAVKEAAVQRKHNLYRDSVVLHNSDPNLHLLAEGAPIDWGEQYGDGGDGSDSGGSPCPSEAATLTEKRRRAKQVVSVVQDEESGLPFEAGSEPPSPASPDNVTELRGLLAQDLQAESSPPASPLLNGAPVQESPQPMTVLEASPPASPLRHLPPGKAVDLEPPKPSDQETGEKVSSPGSRPPIHTTTEDSAGVQTEF
|
May play a role in apoptosis suppression.
|
B4F7E8
|
C0MF07
|
RF1_STRS7
|
Peptide chain release factor 1
|
Streptococcus
|
MNIYDQLQAVEDRYEELGELLSDPEVVSDTKRFMALSKEEASTRETVAAYRQYKAIIQSIDDAEEMIKEAGGDPDIEEMAKEELKEAKAAKETYEDKLKLLLLPKDPNDDKNIILEIRGAAGGDEAALFAGDLLAMYQKFAESQGWRFEVMEASYNGVGGIKEVVAMVSGQSVYSKLKYESGAHRVQRVPVTESQGRVHTSTATVLVMPEVEEVEYDIDPKDLRIDIYHASGAGGQNVNKVATAVRIVHLPTNIKVEMQEERTQQKNRDKAMKIIRARVADHFAQIAQDEQDAERKSTIGTGDRSERIRTYNFPQNRVTDHRIGLTLQKLDTILSGKLDEIVDALVLYDQTQKLESLNNQ
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
C0MF07
|
B1JSU1
|
GPMA_YERPY
|
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
|
Yersinia
|
MAVTKLVLVRHGESQWNNENRFTGWYDVDLSEKGRSEAKAAGKLLKDEGFTFDFAYTSVLKRAIHTLWNILDELDQAWLPTEKTWKLNERHYGALQGLNKSETAEKYGDEQVKQWRRGFAITPPALEKSDERFPGHDPRYAKLTDAELPTTESLALTIERVIPYWNDVIKPRIASGERVIIAAHGNSLRALVKYLDDLGEDEILELNIPTGVPLVYEFDENFKPIKHYYLGNADEIAAKAAAVANQGKAK
|
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
|
B1JSU1
|
A8F791
|
SYE2_PSELT
|
Glutamyl-tRNA synthetase 2
|
Pseudothermotoga
|
MTVRLRFAPSPTGYLHVGGARTALFNWLYARKMNGKFVLRIEDTDLQRSTKESEKAIIESLKWCGIDWDEGPDIGGDFGPYRQSERVSEGIYKRYAQILVEKQCAYYTVYDKVDRKKVLFNTFEYPEEYEKKGHDITISFRVPEGITKFHDLLKGNMEFQNSVIGDFVIVKSDGFPTYNFAVVIDDYLMRITHVFRGEDHLSNTPKQIMIYKALGWEIPQFMHIPLILGFDRTPLSKRHGATSVEHFRKIGILNMGLMNYLALLGWSVGEEEVFDVKEKLVNFEPESISNKGVIFDPEKLEWVNGKHMRMINIEQLWNEFVEWIKFTNRKIPHCEESYALKVLNVCREKVNTLSQLYDFSYSFFFDDYTLEERFVSEYLSTSYAKEILRKAVVLFSELKDWSIEGTEKVCRALADMKIASKNKVFQLLRGAVTGKLVTPGLFETLSILGKKRVIERFEKLLNSVDC
|
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
|
A8F791
|
Q5FMB2
|
ALR_LACAC
|
Alanine racemase
|
Lactobacillus
|
MVPGYHRPAAVKVNLGAIRRNLENEMKHLDPGQKMLAVVKANAYGHGAVEVAKVAEEVGAAGFCVAVLDEGLQLRHADIVKPILVLGVVSPKYAPIAAVNNISLTVPNFEWLKEAEKYLAKENLQLKIHLGIDSGMGRIGFNEDDEFIEANKFLENNDQFFVEGMFAHFASADSADESYFEHQLEKFNHMKSLLTVKPKWIHVSNTAASIFHKNIKSDLVRFGIGIYGLNPSSNPASADLNPDIKLEPALSFESELTHVKTIHKGDGVSYGSTFVADKDTIIGTVPVGYADGWIRKFQGFKVKVGDKYCPIVGRICMDQFMVELPEKMPVGTKVVIISNNPDDPNNIKAAADYVNTIHYEVACLLNDRLPRIYYEK
|
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
|
Q5FMB2
|
A0A3G9HRC2
|
ALT2_ALTAL
|
NADPH--cytochrome P450 reductase
|
Alternaria alternata complex
|
MAISSPSQARSVGNPSPRCVKSSTYPFLGNILDIDPDNFTKSLGDVYMINYGSYRDVIVTSRKVAQELCDESRFCKLPGGAIDRMKRVIGNGLFTAETRDPRWQSAHRVIAPLFNPMRIRGMMDDMRDVCEQMCLRWARFGPGVPIKICDEMTKLTLDTIALCTVDHRFNSFYRPDGIEEPFAEAVVNVMTDSLIQSNLPDWINNWVRFRSMNKFNRQADELRHAIEELIESRRKNPVDRNDLLNAMLSHEDPETGQRLSDELVVDNLLTFFIAGHETTSSLLSFCMYYLLECPDVLQKARAEVHATVGTSTIMPEHLSKLPYLESVLRETLRLRDPGPGFFVKPLRDDVIAGKYFVKKDQSIFIVFDSVHRDPDVYGDDADEFRPERMSQEKFDQLPPCAYKPFGNGVRACIGRPFAMQQAILAVAMILQHFDLIKDESYKLKIHVTMTVRPIGLTMKVRPREGLRATDVNLRMHQASGTATPKPLASGTDGSMLTVTKNGPMHLAIVHASNSGTSEALAGLLASNAVDRGLGVKSISVANDIVEKLPRDVPVVIITASYNGEPSRNAADFVSWLKSTKQHELEGVRYAVFGCGHRDWASSLFAVPKLIDSLLSTNGAEQIAQMGTSDTGGSTDIYSDFEDWTTKFLFPYLNSKQEMKDTKLNSGADTRDVDLHVSLGKPPRVAMRKGFAAATVTKNRSLSAPGVPEKCELELCLPDGFTYKAGDHLQILPRNSSNDVQSVLRHFHLEAETLVSIQSAHRNKRLGLPLDVPIMASELFAAYVELGRTASSRNIHVLAGLVRSDKPKIKRILLSLANGESYKTEVLDKRISVLDLLKQFPDIEISLAGFLSLLMPIRPRSYSFSSGPNWKPGFATLTYTVVGAGKLVSKAKMTEHVAMSMRGGLASTFLSTLSARDDLYVSLDPASPSFYDDQSVSCPIIMIAAGTGIAPFIGFLQERKLSLAHTALLQGSKKAGPYARTLLFFGCRGPALDSLYTEELAAFEADGLVEVRRAFSRDHTAAGSNGCKYVDQRLAASAEELVELWRLGARVFVCGGKKMANNVFDVLGPLFHEADKLDQKTAEDDVGKWRTTLGKGRYAEEIFI
|
Bifunctional cytochrome P450/NADPH--P450 reductase; part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AAL-toxins, sphinganine-analog mycotoxins responsible for Alternaria stem canker on tomato by the tomato pathotype . The biosynthesis starts with the polyketide synthase ALT1-catalyzed C-16 carbon chain assembly from one starter acetyl-CoA unit with malonyl-CoA extender units . ALT1 also selectively transfers methyl groups at the first and the third cycle of chain elongation for AAL toxin . The C-16 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of glycin by decarboxylation, on the carbonyl carbon of polyketide acyl chain (Probable). This step is probably catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase ALT4 (Probable). The respective functions of the other enzymes encoded by the cluster have still to be elucidated (Probable). The sphingosine N-acyltransferase-like protein ALT7 seems not to act as a resistance/self-tolerance factor against the toxin in the toxin biosynthetic gene cluster, contrary to what is expected (Ref.5).
|
A0A3G9HRC2
|
Q15345
|
LRC41_HUMAN
|
Protein Muf1
|
Homo
|
MAAPEAWRARSCWFCEVAAATTMEATSREAAPAKSSASGPNAPPALFELCGRAVSAHMGVLESGVWALPGPILQSILPLLNIYYLERIEETALKKGLSTQAIWRRLWDELMKTRPSSLESVTCWRAKFMEAFFSHVLRGTIDVSSDRRLCDQRFSPLLHSSRHVRQLTICNMLQGATELVAEPNRRVLETLASSLHTLKFRHLLFSDVAAQQSLRQLLHQLIHHGAVSQVSLYSWPVPESALFILILTMSAGFWQPGPGGPPCRLCGEASRGRAPSRDEGSLLLGSRRPRRDAAERCAAALMASRRKSEAKQMPRAAPATRVTRRSTQESLTAGGTDLKRELHPPATSHEAPGTKRSPSAPAATSSASSSTSSYKRAPASSAPQPKPLKRFKRAAGKKGARTRQGPGAESEDLYDFVFIVAGEKEDGEEMEIGEVACGALDGSDPSCLGLPALEASQRFRSISTLELFTVPLSTEAALTLCHLLSSWVSLESLTLSYNGLGSNIFRLLDSLRALSGQAGCRLRALHLSDLFSPLPILELTRAIVRALPLLRVLSIRVDHPSQRDNPGVPGNAGPPSHIIGDEEIPENCLEQLEMGFPRGAQPAPLLCSVLKASGSLQQLSLDSATFASPQDFGLVLQTLKEYNLALKRLSFHDMNLADCQSEVLFLLQNLTLQEITFSFCRLFEKRPAQFLPEMVAAMKGNSTLKGLRLPGNRLGNAGLLALADVFSEDSSSSLCQLDISSNCIKPDGLLEFAKRLERWGRGAFGHLRLFQNWLDQDAVTAREAIRRLRATCHVVSDSWDSSQAFADYVSTM
|
Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
|
Q15345
|
Q11PK1
|
KUP_CYTH3
|
Probable potassium transport system protein kup
|
Cytophaga
|
MSTIADSKNHGHQKLTAAGLLISLGIIYGDIGTSPLYVMKAIAGGNVISENLILGGLSCVFWTITLQTTIKYVIITLRADNKGEGGIFSLFALIRRRNPNLVWPAMIGGAAMLADGIITPPISVSSAVEGLLIFNKDIPTIPIVLAIIVMLFMIQRFGTNIVGKFFGPIMFIWFAMLATLGLSQLMGNFYVLKAINPMYAFNLLTQYTTVDDKSGFWLLGAVFLCTTGAEALYSDLGHCGRPNIRISWIFVKLALLINYFGQGAWILQNKGYVIKGNPFFGIMPEWFIVYGIIIATMAAIIASQAMISGSYTLISEALRLNLWPKVRVKYPSVKKGQLFIPSINLLLLAGCIFVVLWFGESSAMEGAYGLAINITFLMTTILLAYYLLIIKRISFIWVGLLILMYLIIEVSFLVANLEKFFHGGYFTLISSGILAFIMIIWYTAHRIKRRLTEYVKIQDYFPLIKELSEDTSIPKYSTHLIYLTGADNYTQIESKVIYSIFQKQPKRADIYWFLHIDVVDEPYTMEYKVRTMLADDVIRIDFKLGFRVEHRINLFFRKVVEDMVNNKEVDFTSRYTSLNKRNVIGDFRFVVLEKHLSNDNDLSVMEQFAMDWYFFLKHISISESSAFGLDTSSVTVEKVPMVISPMEAFQLKRVY
|
Transport of potassium into the cell.
|
Q11PK1
|
B8HXS4
|
DEOC_CYAP4
|
Phosphodeoxyriboaldolase
|
unclassified Cyanothece
|
MVAPSAEIDLAPYIDHTLLDPLATPAAIAQLCEEADRYHFATVCLAPIYVRQAVELLYRRTPRVCTVIGFPTGAHTSAVKLYEAQEAADHGATELDVVVNLGWLKAGQTEAVHQEMAEIVAATGVTVKAILETTVLSETEKRLAAEICLDAGVSFLKTSTGWRGGATVADVKLLAQVARDRIGVKASGGIRTAAQALELIHAGATRLGTSRGVDLIRNRDTLEGETNY
|
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
|
B8HXS4
|
Q8DBD5
|
RNH_VIBVU
|
Ribonuclease HI
|
Vibrio
|
MTKQVEIFTDGSCLGNPGPGGYGVVLRYKQVEKTLAQGYRLTTNNRMEMMATIVALQALKEPCNVILTTDSQYVRQGITQWIHNWKKRGWKTADKKPVKNADLWQALDKETTRHTIDWRWVKGHAGHRENEMCDELARAAAENPTLDDTGYQPAE
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
Q8DBD5
|
Q31GZ0
|
HIS1_HYDCU
|
ATP phosphoribosyltransferase
|
Hydrogenovibrio
|
MADQLTIALSKGRIYKDTLPLLEAANIIPQEDPSKSRKLIIPTNHEHVRLLIVRATDAPTYVAHGAADIGVAGKDVLMEAPSDNLNELLDLQIAKCKLMVAGPKEAKPHGHRLKIATKYIQSAKAYYAQKGQQVDLIKLYGSMEIAPLIDLADKIVDLVDTGNTLKANGLVPEEHIADISSRLIVNEHAYKTKFKQINDIVEKFRSAI
|
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
|
Q31GZ0
|
Q2G9P6
|
MIAB_NOVAD
|
tRNA-i(6)A37 methylthiotransferase
|
Novosphingobium
|
MSSSAPSSASPKTFRVKSFGCQMNVYDGERMAELLAAQGMSAAGDGDDADLVVLNTCHIREKATEKVYSDIGRLRRADGSAPLIAVAGCVAQAEGEEIMARAPSVKVVVGPQSYHRLPEMVADAAAGKRSTETDMPAEAKFAALPKRRKSAPTAFLTVQEGCDKFCTYCVVPYTRGAEISRPFSDLVEEAKLLVAGGAREITLLGQNVNAWAGEDDKGRPIGLDGLARALAAEPDLKRIRYTTSHPNDMTDGLIAAHGELEKLMPFLHLPVQAGNDRVLKAMNRSHTADSYMALLERIRAARPDIALSGDFIVGFPGETDAEFEDTLRLVDAVGYAQAFSFKYSARPGTPAATMENHVPVAVMDERLQRLQAALNRDQLAFNKASVGKTCEVLVERRGKHPGQWLGKSPWLQSVHFSGEAEIGDMVTVELIEAGPNSISGRLA
|
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.
|
Q2G9P6
|
Q2GI13
|
SYY_EHRCR
|
Tyrosyl-tRNA synthetase
|
Ehrlichia
|
MKLESQFLSFLYSRGYCSQCTNISMLDQLMSQQCVHAYIGFDCTAKSLHVGSLIQVMILRHLQKFGHKPIILLGDGTTKIGDPSGKDKSRAMLSASEIEENALGIYEVLKKFIVFGDGPHDALLVRNAEWLNGLNYIEFLRDIGKHFSVNNMLTFDSVRLRLEREQNLSFLEFNYMLLQSYDFVELNRRYNCLLQIGGSDQWGNIVSGVELGRKLRLPELFGLTTNLLLTSSGEKMGKTAQGAVWLDGNMYSPVDYWQYFRNVKDEDVGRFLRLFTELSLNEIRNLELLQGHEINESKKILATEATRICHGEEIAQSVANDALKVFECNDDSGLSVFYVKKYDVELGLPIIKLLQMCEMEKSSSSARRLINDKGCKINDVVVLDMNYKLSLKDFYNTSYVKLSCGKKRHLKVMLESDF
|
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).
|
Q2GI13
|
Q91V45
|
KISSR_MOUSE
|
Metastin receptor
|
Mus
|
MATEATLAPNVTWWAPSNASGCPGCGVNASDDPGSAPRPLDAWLVPLFFATLMLLGLVGNSLVIYVICRHKHMQTVTNFYIANLAATDVTFLLCCVPFTALLYPLPAWVLGDFMCKFVNYIQQVSVQATCATLTAMSVDRWYVTVFPLRALHRRTPRLALAVSLSIWVGSAAVSAPVLALHRLSPGPRTYCSEAFPSRALERAFALYNLLALYLLPLLATCACYGAMLRHLGRAAVRPAPTDGALQGQLLAQRAGAVRTKVSRLVAAVVLLFAACWGPIQLFLVLQALGPSGAWHPRSYAAYAVKIWAHCMSYSNSALNPLLYAFLGSHFRQAFCRVCPCCRQRQRRPHTSAHSDRAATHTVPHSRAAHPVRIRSPEPGNPVVRSPCAQSERTASL
|
Receptor for metastin (kisspeptin-52 or kp-52), a C-terminally amidated peptide of KiSS1. KiSS1 is a metastasis suppressor protein. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis. The receptor is essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/KISS1R system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood. Analysis of the transduction pathways activated by the receptor identifies coupling to phospholipase C and intracellular calcium release through pertussis toxin-insensitive G(q) proteins.
|
Q91V45
|
Q70KF0
|
DOIAD_MICEC
|
2-deoxy-scyllo-inosamine dehydrogenase
|
Micromonospora
|
MGGRMRALQFHGGHKAQIIDTPRPEAPPGWAVVKVHYCCLCGSDLWLYRGKWHGNRYPIVPGHEWAGVVDSAPEGYESWVGRPVTGDLIVGCQGCGPCRDGLPVMCENLIEIGFTVDGGCAGYVAVPITNLYLLPEGMDLAAASQTEPLAVALHAVDRINLRPAERVAVLGAGGIGQLILQSARATGATVTLATDLVAERRKIAEESGAAAAVHPSELPELTSYADKVDVVFEASGDPESVVRALDLVRPGGRVCLVGYQVGAEHALETARLPLSYASLVGVMGPGGKYREAVDLLANGAIDTQPILTDIVTLDDYAPAIDRAINRTDGTVRVVFDLRNE
|
Catalyzes the oxidation of 2-deoxy-scyllo-inosamine (DOIA) with NAD(+) or NADP(+), forming 3-amino-2,3-dideoxy-scyllo-inosose (amino-DOI).
|
Q70KF0
|
P59265
|
PA2BB_PROFL
|
Phosphatidylcholine 2-acylhydrolase
|
Protobothrops
|
HLLQFRKMIKKMTGKEPIVSYAFYGCYCGKGGRGKPKDATDRCCFVHDCCYEKVTGCDPKWSYYTYSLENGDIVCEGDPYCTKVKCECDKKAAICFRDNLKTYKNRYMTFPDIFCTDPTEGC
|
Snake venom phospholipase A2 (PLA2) that displays edema-inducing activities. PLA-B is three times more active than PLA-A in edema-inducing activities. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
P59265
|
A4G2T6
|
RIMM_HERAR
|
Ribosome maturation factor RimM
|
Herminiimonas
|
MKVPEDLVLVGYISGAYGLNGWVRVRPYSADADALLNAKTWWLDKPEFRDVAMMQSKIHSGDVVAQLMGVAGRDAAEALKGATVQIPRSHFPALSDNEFYWVDLIGLEVENLQGVRLGQVSDMMDNGAHPILRVAVPQTSEADPKAAQELLIPFVEQFVITIDQTAKKITVDWGLDY
|
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.
|
A4G2T6
|
Q3AH76
|
EX7L_SYNSC
|
Exodeoxyribonuclease VII large subunit
|
unclassified Synechococcus
|
MSADRLPSYSVAELNTAIGSLLERGFAPRFLLEATVSRPQLKKGHLWLTLTDGSASISGVVWASKLAQLSYQPKDGDGVTVVGKLNFWAARASLTVQALDIRPSLSTVLRDFERVRQVLEQEGVIDPSRLRPLPSQPASIAVLTSVPSSALADMLRTAAERWPLTQLIVVPIPVQGSVAPTIINTLEAIAERTAELGLQALVLARGGGSREDLAVFDNEALCRLLANYPIPVVTGLGHEDDLTVADLVADHRAATPTAAIVALLPDREAERQGLTQRQSRLKDTLLGRILRERQRLQDRAVALQQQSPREKIMRKRQELIQKHQLLKALSPERWLKRGLALISNKAGDPIPGLESVKIGDQLNIRMSDGSLEARVDQIQPSAPNTTS
|
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
|
Q3AH76
|
Q41065
|
IBBA_PEA
|
Seed trypsin/chymotrypsin inhibitor I
|
Pisum
|
LSFAANVVNARFDSTSFITQVLSNGDDVKSACCDTCLCTKSNPPTCRCVDVRETCHSACDSCICAYSNPPKCQCFDTHKFCYKACHNSEVEEVIKN
|
Inhibitor of trypsin and of chymotrypsin. May function as a natural phytochemical defense against predators.
|
Q41065
|
A6Q200
|
NDK_NITSB
|
Nucleoside-2-P kinase
|
unclassified Nitratiruptor
|
MERTLSIIKPDAVAKNVIGKIIDRFETNGLRIAAMKKIQLSKNDAAKFYEVHKERPFFNDLVDYMTSGPVVVMVLEGENAVAKNRELMGATDPKEAKPGTIRADFAESIEANAVHGSDSLENAQKEIAFFFAQREIL
|
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
|
A6Q200
|
A2Q898
|
MCR1_ASPNC
|
Mitochondrial cytochrome b reductase
|
Aspergillus subgen. Circumdati
|
MFARQAFRCAQPLKQGFRKYSTEAPKGKSSLAPIYAAVGITGVGVGLYRYNSATAEAPAAVDRPKVFKGGDQGWFDLKLSEIEVLNHNTKRLRFEFEDKEALSGLQVASALLTKFKPADAKAVIRPYTPTSDEETPGYIDLVVKVYPNGPMSEHLHSMNVGQRLDFKGPIVKYPWETNKHNHICLIAGGTGITPMYQLAREIFKNPEDQTKVTLVFGNVKEEDILLKKEFEELENTYPRRFRAFYVLDNPPKEWTGGKGYISKELLKTVLPEPKEENIKIFVCGPPGMYKAISGTKNSPTDQGELSGILKELGYSKEQVFKF
|
May mediate the reduction of outer membrane cytochrome b5.
|
A2Q898
|
A6RSH5
|
DBP7_BOTFB
|
ATP-dependent RNA helicase dbp7
|
Botrytis
|
MADDGMLMNFEIGDVPIVAKQAFKGGRWKDRLAAKKTAQHRVTKSTNKPSAREIFSEPQHDTSAEEYIGREASSRAPKRQRVDDNYNSYGGRNENTAAYASGKLPSGSINVGGGRKTTFQEEPRTAFVAGKLPPGSINIGGKKATQIEDEGRAAYASGKLPPGSINSGAKKAISFQDETRPAYVSGKLPHGSIDGMRNREMAAVHREIAEGGRKPGQVVSSLFTFNPTSKKTFDEPEEQAEPAKPSNAPLTEEMATFTNLGLSRRLAAHLSTKLDMKAPTAIQKASVQQLVSDDSDAFIQAETGSGKTLAYLLPIVERILALSENGVQIHRDSGLFAIILSPTRELCKQIAAVLEKVLRCAPWIVGTTVNGGESKQSEKARLRKGVNILVATPGRLADHLDNTEVLNVATVRWLVLDEGDRLMELGFEEEIKGIVEKIGRRSVAKANSDMGSLPKRRVTILCSATMKMNVQRLGEISLKDAVHIQADPSEQEKQDKENGVEAQDKAFSAPTQLKQSYAIVPAKLRLVTLTALLKRAFARKGSVMKAIVFISCADSVDFHFSLFSRTPEASAEVVDEEKVDLPALPKSELVKETIAHGTTISNNSNPVILHKLHGSLAQNIRTATLKAFSESADPCVMICTDVASRGLDLPNVDFVIEYDPPFSAEDHLHRVGRTARAGREGRALIFLMPGVEEEYVSILASGYREGKKALTRHTAEDLIQKGFGGIGREWEERATNFQLEVERWSLDSPKYLEMARRGYQSHIRAYATHVANERHIFNMQELHLGHLAKAFALRDKPGSIKVPGLRPAKMTKADRSVAARKAKRGEKAEDKAPEGERVRKQKKMELDLPTVDGNEAAARMKRKMKEHMAAASEFNIG
|
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
|
A6RSH5
|
Q5SQN1
|
SNP47_HUMAN
|
Synaptosomal-associated 47 kDa protein
|
Homo
|
MRAARRGLHCAGAERPRRRGRLWDSSGVPQRQKRPGPWRTQTQEQMSRDVCIHTWPCTYYLEPKRRWVTGQLSLTSLSLRFMTDSTGEILVSFPLSSIVEIKKEASHFIFSSITILEKGHAKHWFSSLRPSRNVVFSIIEHFWRELLLSQPGAVADASVPRTRGEELTGLMAGSQKRLEDTARVLHHQGQQLDSVMRGLDKMESDLEVADRLLTELESPAWWPFSSKLWKTPPETKPREDVSMTSCEPFGKEGILIKIPAVISHRTESHVKPGRLTVLVSGLEIHDSSSLLMHRFEREDVDDIKVHSPYEISIRQRFIGKPDMAYRLISAKMPEVIPILEVQFSKKMELLEDALVLRSARTSSPAEKSCSVWHAASGLMGRTLHREPPAGDQEGTALHLQTSLPALSEADTQELTQILRRMKGLALEAESELERQDEALDGVAAAVDRATLTIDKHNRRMKRLT
|
Plays a role in intracellular membrane fusion.
|
Q5SQN1
|
Q2KHY1
|
CPNE6_BOVIN
|
Copine VI
|
Bos
|
MSDPEMAWVPEPPAMTLGASRVELRVSCHGLLDRDTLTKPHPCVLLKLHSDEQWVEVERTEVLRSCSSPVFSRVLALEYFFEEKQPLQFHVFDAEDGSTSPRNDTFLGSTECTLGQIVSQTKVTKPLLLKNGKNAGKSTITIVAEEVSGTNDYVQLTFRAHKLDNKDLFSKSDPFMEIYKTNGDQSDQLVWRTEVVKNNLNPSWEPFRLSLHSLCSCDVHRPLKFLVYDYDSSGKHDFIGEFTSTFQEMQEGTANPGQEMQWDCINPKYRDKKKHYKSSGTVVLAQCTVEKVHTFLDYIMGGCQISFTVAIDFTASNGDPRSSQSLHCLSPRQPNHYLQALRAVGGICQDYDSDKRFPAFGFGARIPPNFEVSHDFAINFDPENPECEEISGVIASYRRCLPQIQLYGPTNVAPIINRVAGPAQREQSTGQATKYSVLLVLTDGVVSDMAETRTAIVRASRLPMSIIIVGVGNADFSDMRLLDGDDGTLRCPRGVPAARDIVQFVPFRDFKDASPSALAKCVLAEVPRQVVEYYASQGISPGAPRPCTPAMTPSPSP
|
Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Binds phospholipid membranes in a calcium-dependent manner. Plays a role in dendrite formation by melanocytes.
|
Q2KHY1
|
Q12IL8
|
KGUA_SHEDO
|
GMP kinase
|
Shewanella
|
MSARGNLFIVSAPSGAGKSSLITALLKDKPQDMQVSVSHTTRAPRPGEVDGQHYHFVSVEQFKALIAENAFFESAEVFGNFYGTSRQVIENTLSLGIDVFLDIDWQGAQQVKKIMPEAIGVFILPPSKAELERRLTGRGQDSSDVIAARMAQAVSEMSHYNEYDFVIINDDFEQALADLKSIIFSQRLTCASQFHTHNDMLVDLLAD
|
Essential for recycling GMP and indirectly, cGMP.
|
Q12IL8
|
Q3ZM03
|
RSSA_XENLA
|
Laminin-binding protein precursor p40
|
Xenopus
|
MSGGLDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVCVISSRNTGQRAVLKFASASGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPITEASYVNIPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKATTKEEFQGEWTAPVAEFPQAEVADWSEGVQVPSVPIQQFTAERTDVPPAPKPTEDWSTQPASTDDWSAAPTAQASEWTGTTTEWS
|
Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis.
|
Q3ZM03
|
P0AA29
|
THIO_SALTI
|
Thioredoxin 1
|
Salmonella
|
MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLA
|
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
|
P0AA29
|
B3H1B5
|
PYRD_ACTP7
|
Dihydroorotate oxidase
|
Actinobacillus
|
MYSLIRKCLFSMDAETAHNFSIQALKLAGKLPINVLPMPLNPVEVMGLQFKNPIGLAAGADKNGEAIDGFGKLGFGFIEVGTVTPVAQDGNPKPRQFRILEAEGIINRNGFNNLGVDVLVENVKKAKYDGIIGINIGKNAVTPIERALDDYQICLRKVYEHADYITVNISSPNTKNLRTLQYGEALDDLLRSLKSEQESLSQKFNRYKPLVLKIAPDLTDEEIASVADGLIRHKIDGVIAGNTTLSRDPVVGLKNAEQQGGLSGKPLNTLSTRLISTLAEELNGTLPIIGSGGIHSVASGQEKIDAGASLLQVYSAMIYQGLALIQNLAKHIQVR
|
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
B3H1B5
|
A8LC60
|
RS7_FRASN
|
30S ribosomal protein S7
|
unclassified Frankia
|
MPRKGPAPKHPVVVDPVYGSPLVTALVNKVLLSGKKSVAERIVYGALEGAKNKTGNDPVVTLKRALDNVKPTLEVRSRRVGGATYQVPVEVRAGRSTTLALRWIVGYSRGRREKTMTERLMNELIDASNGLGASVKRREDTHKMAESNKAFAHYRW
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
|
A8LC60
|
D9S0S1
|
CBIM_THEOJ
|
Energy-coupling factor transporter probable substrate-capture protein CbiM
|
Thermosediminibacter
|
MRKITFIAALLSLLPRYALAMHVMEGFLPFKWCLLWYSIYIPFLMAGLIYIKKNIAEEPSKKILLGFAGAFVFALSALKLPSVAGSSSHPTGIGLGAILLGPLPMAVIGGIVLLFQALLLAHGGITTLGANAFSMAVAGSFAAYGLYKVAGRVGLSKSASVFLGAASGDLMTYIITSLQLALAFPASRGGVAASFAGFSGIFAVTQLPLAIGEGILTVIVLNLLEIHAGVVVGRLVKGASNDEG
|
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
|
D9S0S1
|
Q2KID7
|
OSTC_BOVIN
|
Oligosaccharyltransferase complex subunit OSTC
|
Bos
|
MESLYRVPFLVLECPNLKLKKPPWVHMPSAMTVYALVVVSYFLITGGIIYDVIVEPPSVGSVTDEHGHQRPVAFLAYRVNGQYIMEGLASSFLFTMGGLGFIILDRSNAPNIPKLNRFLLLFIGFVCVLLSFFMARVFMRMKLPGYLMG
|
Specific component of the STT3A-containing form of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1.
|
Q2KID7
|
B2U8X6
|
PXPA_RALPJ
|
5-oxoprolinase (ATP-hydrolyzing) subunit A
|
Ralstonia
|
MTAIDLNADLGEGCDTDEALLALVSSANIACGWHAGDVNTMRQTVGWALRQGVSIGAHPSFPDRENFGRTEMHLQPDEIYAGVLFQIGGLSAIVRAQGGKLAHVKAHGALYNQASRDRPLAMAIVHAIRDFDPSLVVFGLAGGELVKAARELGLQAKEEVFADRGYNADGSLVKRGTPGALIDSEDAALDQTLTMVREQRVKAIDGTWVPIRAETVCLHGDGAHALAFARRIRERLGSEGIAVRAGA
|
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
|
B2U8X6
|
Q96EX3
|
DC2I2_HUMAN
|
WD repeat-containing protein 34
|
Homo
|
MATRAQPGPLSQAGSAGVAALATVGVASGPGPGRPGPLQDETLGVASVPSQWRAVQGIRWETKSCQTASIATASASAQARNHVDAQVQTEAPVPVSVQPPSQYDIPRLAAFLRRVEAMVIRELNKNWQSHAFDGFEVNWTEQQQMVSCLYTLGYPPAQAQGLHVTSISWNSTGSVVACAYGRLDHGDWSTLKSFVCAWNLDRRDLRPQQPSAVVEVPSAVLCLAFHPTQPSHVAGGLYSGEVLVWDLSRLEDPLLWRTGLTDDTHTDPVSQVVWLPEPGHSHRFQVLSVATDGKVLLWQGIGVGQLQLTEGFALVMQQLPRSTKLKKHPRGETEVGATAVAFSSFDPRLFILGTEGGFPLKCSLAAGEAALTRMPSSVPLRAPAQFTFSPHGGPIYSVSCSPFHRNLFLSAGTDGHVHLYSMLQAPPLTSLQLSLKYLFAVRWSPVRPLVFAAASGKGDVQLFDLQKSSQKPTVLIKQTQDESPVYCLEFNSQQTQLLAAGDAQGTVKVWQLSTEFTEQGPREAEDLDCLAAEVAA
|
Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Inhibits the MAP3K7-induced NF-kappa-B activation pathway. Inhibits MAP3K7 phosphorylation at 'Thr-184' and 'Thr-187' upon Il-1 beta stimulation.
|
Q96EX3
|
Q7M3B6
|
HBA_SAGMY
|
Hemopressin
|
Saguinus
|
VLSPADKSNVKAAWGKVGGHAGDYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVALVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHHPADFTPAVHASLDKFLASVSTVLTSKYR
|
Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling.
|
Q7M3B6
|
O23116
|
EIL3_ARATH
|
ETHYLENE INSENSITIVE 3-like 3 protein
|
Arabidopsis
|
MGDLAMSVADIRMENEPDDLASDNVAEIDVSDEEIDADDLERRMWKDRVRLKRIKERQKAGSQGAQTKETPKKISDQAQRKKMSRAQDGILKYMLKLMEVCKVRGFVYGIIPEKGKPVSGSSDNIRAWWKEKVKFDKNGPAAIAKYEEECLAFGKSDGNRNSQFVLQDLQDATLGSLLSSLMQHCDPPQRKYPLEKGTPPPWWPTGNEEWWVKLGLPKSQSPPYRKPHDLKKMWKVGVLTAVINHMLPDIAKIKRHVRQSKCLQDKMTAKESAIWLAVLNQEESLIQQPSSDNGNSNVTETHRRGNNADRRKPVVNSDSDYDVDGTEEASGSVSSKDSRRNQIQKEQPTAISHSVRDQDKAEKHRRRKRPRIRSGTVNRQEEEQPEAQQRNILPDMNHVDAPLLEYNINGTHQEDDVVDPNIALGPEDNGLELVVPEFNNNYTYLPLVNEQTMMPVDERPMLYGPNPNQELQFGSGYNFYNPSAVFVHNQEDDILHTQIEMNTQAPPHNSGFEEAPGGVLQPLGLLGNEDGVTGSELPQYQSGILSPLTDLDFDYGGFGDDFSWFGA
|
Probable transcription factor that may be involved in the ethylene response pathway.
|
O23116
|
Q8W4H8
|
GDL19_ARATH
|
Probable myrosinase-associated protein GLL23
|
Arabidopsis
|
MMAKNCNLVSVLCVFLVLTLFNKPITVAGQNIPAVGLFTFGDSNFDAGNKQTLTKTLLPQTFWPYGKSRDDPNGKFSDGLIAPDFLAKFMRIPIVIPPALQPNVNVSRGASFAVADATLLGAPVESLTLNQQVRKFNQMKAANWNDDFVKKSVFMIYIGANDYLNFTKNNPNADASTQQAFVTSVTNKLKNDISLLYSSGASKFVIQTLAPLGCLPIVRQEFNTGMDQCYEKLNDLAKQHNEKIGPMLNELARTAPASAPFQFTVFDFYNAILTRTQRNQNFRFFVTNASCCGVGTHDAYGCGFPNVHSRLCEYQRSYLFFDGRHNTEKAQEMFGHLLFGADTNVIQPMNIRELVVYPADEPMRESWVPPTSATVQLRESRGYEYY
|
Involved in the control of the PYK10 complex size and possibly substrate specificity. May be exported from the endoplasmic reticulum upon interaction with MVP1.
|
Q8W4H8
|
Q2U6N1
|
NACB_ASPOR
|
Beta-NAC
|
Aspergillus subgen. Circumdati
|
MLNRSPSGTAFDHENGKLTHTYPQCIISPSSSHTRSTPNSYKPDHESTRLTNSLKNRGKGTPRRKVKKVHKSSGADDKKLQATLKKMNVQPIQAIEEVNMFKEDGNVIHFGAPKVHASVPSNTFALYGNGEEKELTELVPGILNQLGPDSLASLRKLAESYQNMQKNQAGAEGKKDDDEDDIPDLVEGENFESNVE
|
Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. EGD1 may act as a transcription factor that exert a negative effect on the expression of several genes that are transcribed by RNA polymerase II.
|
Q2U6N1
|
B2A0B9
|
RLMN3_OPITP
|
tRNA m2A37 methyltransferase 3
|
Opitutus
|
MKFTPAKPPLTGETLESLTARLRERGEPAFRASQILDWVYKKRARSWDGMTNLPKPLRTWLDDTFDLMPATLVLNKQSADVTDKLLLELRDGSLIETVIIRAPQEGVGQDHSRKTICISTQVGCAMGCVFCASGLAGLKRDLSAGEIVAQLLQVCYREDALTPRAHMELASFDNIVVMGMGEPLANYDALIRALTILNADWGLGFGARRITVSTSGLVPKILQLADEPLGFRLAISLHGATDEVREKIMPVNKAFPLAKLLPAVKAFSEKHGRMITLEFILIDGVNDSLEQAEKLRDIALDLHAHVNLIPYNTVEGLAWKRPSITRQERFADVLRARRVSVTLRREKGHDIDAACGQLRLKTEKERQVLAAAKT
|
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
|
B2A0B9
|
Q3J818
|
AROE_NITOC
|
Shikimate dehydrogenase (NADP(+))
|
Nitrosococcus
|
MPDRYAVMGNPIAHSKSPQIHTAFAQQTGQALTYTGLQVEAGKLAEAITAFQQQEGKGLNITIPLKAEAWRLVDQCSPQAQRAKAVNTILLEKNGALLGDNTDGVGLVRDLINNHGGRITGQQVLLLGAGGAASGVIEALLKEHPSHLIIVNRTPAKAIELAARFSPFGAITGGGYELLENNSFHLIINATASSLQGELPPLPRGILRSGGWVYDMMYGNEPTIFMKWGQTHGAARSLDGLGMLVEQAAEAFFIWRKVRPKSAPIIAQLRREMDIKNPAMPL
|
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).
|
Q3J818
|
A6UP86
|
GLMM_METVS
|
Phosphoglucosamine mutase
|
Methanococcus
|
MKLFGTSGIRMKNLDPLIAYKVGFAISKNFKKAVIGRDTRTTGNLIESAITAGLLNGGCDVTILGIVPTPVLGFSAKSHDIGIMITASHNPPEYNGIKLFNNNGTSFTPNQEESLEEIIEKSDFLDPSWDIVGNVSEDKTAVKKYLDYILSNINIKKKFNVVVDCANAAACGISPNLFTNAGCKVISVNSHCDGRFVGRMPEPNEKNLVETVDIVKGLNLSGRDFIGIAHDGDADRMIAIDEMGRVTDFDKLLAAFCKYVVQKTNAKKIVTTVDASMAIEEYLKEFGAEVIRTKIGDVSVAYEIEKTGAIFGGEPSGTWIHKSIHLTPDGILSGLRVLEMMEFYDKRLCEIMDEVPSYINLREKLPCPDELKNKVMKYVSKEGKLLFKKEPETLDGVRFSFENGWILIRPSGTESYIRVRVEAKDETFANELLNNGISLVNNGILK
|
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
|
A6UP86
|
B2S670
|
RS17_BRUA1
|
30S ribosomal protein S17
|
Brucella
|
MPKRVLQGVVVSDKNDKTVVVKVERRYSHPLLQKTVRQSKKYKAHDENNQFKVGDFVSIQESAPISKDKRWVVLTSEAAG
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
B2S670
|
Q6BUX9
|
HSV2_DEBHA
|
SVP1-like protein 2
|
Debaryomyces
|
MNTLSAISNNKQSKELQILNINFNQDQGCFAVGHEYGFLVYNTNPIDIRVKRNFNINGHGSGIAHITMLHRTNYLALVGGGKNPKFANNKLVIWDDLKRKNSLNLEFMSPVLNVLLSRIRIIVVLKNQVLVYGFSSPPKKFATYETIENEFGLADLSVNFTNSIGNNLSTSNSSISSLVSNQVSYDSNKYQTLAFPGRSIGQIQIVDVSPSGQEKNLVSIIKAHKSKIRCLALNRSGTLVASASETGTIIRVHSTHNTALLYEFRRGLDRAIVTSMKFSHDDSKLAVLSDKNTLHVYNVSPLNTSSGATSDLVTHNETYPVNRSHLLGSIAFPIPIPKYFKSTWSFCSVNTNKYHPSGSDNDTINDVGIIGWSGNDSIIIIWQNKKIWEKYVIVEKRNKYLGDINDGLNTSHQGSSNWELVRFNWKNLDNLD
|
Involved in mitochondrial or peroxisomal functions and amino acid signaling pathways.
|
Q6BUX9
|
A0LIZ1
|
MTNA_SYNFM
|
S-methyl-5-thioribose-1-phosphate isomerase
|
Syntrophobacter
|
MPQQWLPPIYWDGDAVAILDQRLLPQREAVIRCTSPKQVVAAIKNMAIRGAPAVGVAGAMALALGAVLIQAADARTFKSKFARLCRQVRTARPTGRNLGWAVDRIHALVEGNRDADVPRLHELIRREADLILAEDVAGNVAIGSWGKTVIPRGAGIMTYCNAGALATADYGTAVGVIRAAFDADPGIRVFSCETRPFLQGARLTVYELMKAGIPVTLITDNSIGSLMSRGMIDVVVVGADRIAANGDTANKIGTYMAAVLACTHGIPFYVAAPRSTIDASLPDGDGIPIEQRAPKEVTHFNGRRVAPQGAAALNAAFDVTPNKYITGIITEVGILSKPFGRAIRQALKA
|
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
|
A0LIZ1
|
Q8NL02
|
RL14_XANAC
|
50S ribosomal protein L14
|
Xanthomonas
|
MIQMQSYLDVADNSGAKEVMCIKVLGGSKRRYAHIGDIIKVTVKDAIPRGKVKKGEVYDAVVVRTRKGVRRPDGSLIRFDGNAAVLLNNKQEPIGTRIFGPVTRELRSEKFMKIVSLAPEVL
|
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
|
Q8NL02
|
Q98DD1
|
DNAK_RHILO
|
Heat shock protein 70
|
Mesorhizobium
|
MAKVIGIDLGTTNSCIAIMDGKEPKVIENAEGARTTPSIVAISGDGERLVGQPAKRQAVTNPENTIFAVKRLIGRRYDDPVTEKDKKLVPYKIVKGDNGDAWVEAGGKKQSPSQISAMILQKMKETAEAYLGEKVEKAVITVPAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKKDGKTIAVYDLGGGTFDISVLEIGDGVFEVKSTNGDTFLGGEDFDMRLVEYLAAEFKKEQGIDLKNDKLALQRLKEAAEKAKIELSSTTQTEINLPFITADATGPKHLTLKLTRAKFESLVEDLVQRTIDPCKAALKDAGLKAGEIDEVVLVGGMTRMPKIQEIVKQFFGKEPHKGVNPDEVVALGAAIQAGVLQGDVKDVLLLDVTPLSLGIETLGGVFTRLIERNTTIPTKKSQVFSTAEDSQSAVTIRVFQGEREMAADNKALGQFDLVGIPPAPRGVPQIEVTFDIDANGIVNVSAKDKGTGKEHQIRIQASGGLSDADIEKMVKDAEANAETDKKRRAVVEARNQAEALVHSSEKSLKEYGDKVSEAERTAISDAIAALKTAAEGDDAADIEAKSQALAEASMKLGQAMYEASQKEAAEADAKADAAKDSDVVDADFEEIDEDDDKKKSA
|
Acts as a chaperone.
|
Q98DD1
|
Q94AT3
|
PUKI_ARATH
|
Pseudouridine kinase
|
Arabidopsis
|
MEPVIIGALILDVHAKPSTTPISGTTVPGQVLFAPGGVARNVADCIFKLGITPFMIGTLGLDGPANVLLKEWKLSMKGILRREDISTPIVSLVYDTNGEVAAGVAGVDAVENFLTPEWIQRFEYNISSARLLMVDANLSSLALEASCKLAAESSVPVWFEPVSVTKSQRIASIAKYVTIVSPNQDELIAMANALCAKNLFHPFRSDENKLSIEDMFRALKPAILVLLKNGVKVVIVTLGSNGALLCSKGNPKKALNIDRKFLRSGEVFKRVQSVCSPNRFSELGSNRSPSLFAMHFPTIPAKVKKLTGAGDCLVGGTVASLSDGLDLIQSLAVGIASAKAAVESDDNVPPEFKLDLISGDAELVYNGAKMLMVHQSML
|
Catalyzes the phosphorylation of pseudouridine to pseudouridine 5'-phosphate (PsiMP) . Catalyzes the first step in a pseudouridine degradation pathway . Acts together with the pseudouridine 5'-phosphate glycosidase PUMY in the peroxisome to prevent toxic pseudouridine monophosphate accumulation .
|
Q94AT3
|
A2C6Z4
|
ATPB_PROM3
|
F-ATPase subunit beta
|
Prochlorococcus
|
MAAAATATAGTKGVVRQVIGPVLDVEFPAGKLPKILNALRIDGKNPSGQHIAITAEVQQLLGDHRVRAVAMSSTDGLVRGMEALDTGSAISVPVGEATLGRIFNVLGEPVDEQGPVTTDATAPIHRPAPKLTELETKPTVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINNIAKEHGGVSVFGGVGERTREGNDLYEEFKESGVINSDDLSKSKVALCFGQMNEPPGARMRVGLSALTMAEHFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTDVGALQERITSTLEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLARALAAKGIYPAVDPLDSTSTMLQPSVVGDEHYRTARSVQATLQRYKELQDIIAILGLDELSEDDRRTVDRARKIEKFLSQPFFVAEIFTGMSGKYVKLEETIAGFNMILAGELDHLPEQAFYLVGNIDEVKAKAEKIASEAKG
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
A2C6Z4
|
Q5NL34
|
PANB1_ZYMMO
|
Ketopantoate hydroxymethyltransferase 1
|
Zymomonas
|
MNQHGRSAEPGVASEGIAPYGDAHRGIAAKRKKTTTARISQMRVDGEKIAVLTAYDATFAAAADAAGVDCIMVGDSLGMVCQGRTTTVGVSLEDMLYHTRCVSQGIARADGSALIIADLPFGSYQQSNEQAIASAVQLMQAGAHMVKLEGGDWWTVDIVEFLVQRGIPVCAHLRLTPQTVSALGGYRVQGRSEEAAEKLRVDAGALDNAGASMMVLEMIPTELATSITSEMKSCATIGIGAGSGTAGQVLVMHDMLGINLGRMAKFVRNFMRDAEDVPTAFAAYVAAVKDGSFPDDKLHGFL
|
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
|
Q5NL34
|
G8XHD7
|
BESB_STREN
|
L-propargylglycine synthase
|
Streptomyces
|
MSAGSPAEPRPVPGSVHSVSVSIPDVRSVIGFESGDPATLRRIAWGYPRFRTHPYVARVAALVAGAVGGRAQDLVLTRSVRAAEAAAAYAGLAPGAVFEASGVRGVRVAEDDPALAAVRGHVQHTGAHLTSREAEDVLLEAGLIEARQAEEAVSEEPAEAVRSALATAYGAGDPADVSLHNSGMNAVAAAVAAVTDLQRPAGRRRWIQLGWIFFDTMSLLDKRLFGTDHVTVPDPFDLAALSRVVAAHPGQLAGIIAELPSNPSLRCPDVPALREIADRAGCALVLDATIATPHNVDVLGYADVVCESLTKYATGSADVLMGAAVVGSASPWAAQLREGLRRFGDVPYHRDAARVAARIRDYGDRMKRVNAGAVALAGFLERQSAVRAVSWPYDAASQANYRKVERLSDAPGGLLMVDLRVPLERVYDRLAVAKGPSFGAEFTMASPQIFIAHFDLLSTPEGRAELRSRGLHRDMLRISVGVEDPELIAEVFRDAFDGAG
|
Involved in the biosynthesis of terminal alkyne-containing amino acids such as L-propargylglycine (Pra) and L-beta-ethynylserine, that are produced as antibiotics by S.cattleya. Catalyzes gamma-elimination of chloride from 4-chloro-allyl-L-glycine (also named L-2-amino-4-chloropent-4-enoate), followed by an isomerization, to form the terminal-alkyne product L-propargylglycine.
|
G8XHD7
|
Q47IP4
|
TSAD_DECAR
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Dechloromonas
|
MLILGVESSCDETGIALYDSEAGLLSHALYSQVAMHAEYGGVVPELASRDHIRRVVPLLREALGQAGKMLDEVDAVAYTRGPGLAGALLVGCAFAEALALAIDKPTIPVHHLEGHLLSPLLSSDPPTFPFVALLVSGGHTQLMKVTGVGEYELLGETLDDAAGEAFDKSAKLLGLPYPGGALLSKLAEQGTPGVHELPRPMLHSGDLSFSFSGLKTAVLTLVREHADAMSDEFKANAARAFQEAIVEVLVKKSLKAMKQTGLKQLVVAGGVGANKQLRTTLNDEAKRKRFRVYYPELEFCTDNGAMIALAGCLRLQSGSPSKAAGSFAVQPRWPLMEMSVSPTK
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
Q47IP4
|
Q5JIR6
|
RRP41_THEKO
|
Exosome complex component Rrp41
|
Thermococcus
|
MMGRPEGLKLIDENGKRIDGRKKYELRPIKMEVGVLKNADGSAYVEWGKNKVLAAVYGPREIHPKHLQRPDRAILRVRYNMAPFSVEERKKPGPDRRSVEISKVIRGALEPALLLHMFPRTAIDVFIEILQADAGTRVAGITAASLALADAGIPMKDLVAACAAGKIDGEIVLDLNKEEDNYGEADVPVAIMPLKNDITLLQMDGYLTKDEFLEAVRLAIKGAKAVYQKQREALKEKYLKIAQEVEGNE
|
Catalytic component of the exosome, which is a complex involved in RNA degradation. Has 3'->5' exoribonuclease activity. Can also synthesize heteromeric RNA-tails.
|
Q5JIR6
|
A2PYH4
|
HFM1_HUMAN
|
SEC63 domain-containing protein 1
|
Homo
|
MLKSNDCLFSLENLFFEKPDEVENHPDNEKSLDWFLPPAPLISEIPDTQELEEELESHKLLGQEKRPKMLTSNLKITNEDTNYISLTQKFQFAFPSDKYEQDDLNLEGVGNNDLSHIAGKLTYASQKYKNHIGTEIAPEKSVPDDTKLVNFAEDKGESTSVFRKRLFKISDNIHGSAYSNDNELDSHIGSVKIVQTEMNKGKSRNYSNSKQKFQYSANVFTANNAFSASEIGEGMFKAPSFSVAFQPHDIQEVTENGLGSLKAVTEIPAKFRSIFKEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVQSVSQTLKNTSTAIPMRFVAVSATIPNAEDIAEWLSDGERPAVCLKMDESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVIMTRLSTRDKYIQMLACRDTVESSLHRHLIEHLNAEIVLHTITDVNIAVEWIRSTLLYIRALKNPSHYGFASGLNKDGIEAKLQELCLKNLNDLSSLDLIKMDEGVNFKPTEAGRLMAWYYITFETVKKFYTISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKDPNRITIRFPMEGRIKTREMKVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDFVAAQEKKFAVLLNSLILAKCFRCKLWENSLHVSKQLEKIGITLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEQITRYSDTTAEILVTVILRNFEQLQTKRTASDSHYVTLIIGDADNQVVYLHKITDSVLLKAGSWAKKIAVKRALKSEDLSINLISSEFVGLDIQQKLTVFYLEPKRFGNQITMQRKSETQISHSKHSDISTIAGPNKGTTASKKPGNRECNHLCKSKHTCGHDCCKIGVAQKSEIKESTISSYLSDLRNRNAVSSVPPVKRLKIQMNKSQSVDLKEFGFTPKPSLPSISRSEYLNISELPIMEQWDQPEIYGKVRQEPSEYQDKEVLNVNFELGNEVWDDFDDENLEVTSFSTDTEKTKISGFGNTLSSSTRGSKLPLQESKSKFQREMSNSFVSSHEMSDISLSNSAMPKFSASSMTKLPQQAGNAVIVHFQERKPQNLSPEIEKQCFTFSEKNPNSSNYKKVDFFIRNSECKKEVDFSMYHPDDEADEMKSLLGIFDGIF
|
Required for crossover formation and complete synapsis of homologous chromosomes during meiosis.
|
A2PYH4
|
Q0K635
|
RL18_CUPNH
|
50S ribosomal protein L18
|
Cupriavidus
|
MMNKKDARLRRARQTRAKIAEMKVNRLTVFRTNSHIYAQVFSECGTKVLASASTAEVEVRKELDGKGATAAAATVVGKRIAEKAKAAGVETVAFDRAGFRFHGRVKALADAAREAGLKF
|
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.
|
Q0K635
|
Q9JM93
|
AR6P4_MOUSE
|
Splicing factor SRrp37
|
Mus
|
MAHVGSRKRSRSRSRSRSGRRGSEKRSKRSSKDASRNCSASRSQGHKAGSASGVEERSKHKAQRTSRSSSTSSSSSSSSSASSSSSSDGRKKRAKHKEKKRKKKKKKRKKKLKKRVKEKAVAVHQAEALPGPSLDQWHRSAGEDNDGPVLTDEQKSRIQAMKPMTKEEWDARQSVIRKVVDPETGRTRLIKGDGEVLEEIVTKERHREINKQATRGDGLAFQMRTGLLP
|
Involved in modulating alternative pre-mRNA splicing with either 5' distal site activation or preferential use of 3' proximal site.
|
Q9JM93
|
A6UFK4
|
NUOD2_SINMW
|
NDH-1 subunit D 2
|
Sinorhizobium
|
MTEVTELMRPEGEALNTKEVLLNLGPQHPSTHGVLRLVLQLDGEYVERIDPHIGYLHRGTEKLAESFTYTQIFPLTDRLDYLCPPSNNLAFALAVEKLLGIEAPIRAQYIRVMMAELARISGHLLITGALPMDLGAMTALLYAMREREMIMDLLEMITGARMHTSYCRVGGVREDLPDGFLPKIREFCEIFPNRIRDYERLIENNRVFLSRTQGIGVISAADAVDLGLSGPNLRASGVDWDIRRDEPYEIYDRLDFDVITREEGDCYARWLCRVDEMRESIRLIEQCMEQMPEGPFQVDIPTIAFPVDKERVHCSMEALIQHFDLSAYGFDVPAGEVYSVIEAPKGELGFYIISDGSPKPFRMKVRAPSFVNLQALFGVTNARYLADMIAVLGSLDPVMAEVDK
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
|
A6UFK4
|
Q8Y4B8
|
ATPF_LISMO
|
F-type ATPase subunit b
|
Listeria
|
MLQPHLVIGSAFTFGDAFFTLFAFAILLVLIRIYAWKPLMGIMKEREEHIGSEIDAAEENRAQSEKLLAEQKSVLQQARVESQTMIENAKQLGEKEREEIVKTARRESERIKEEAKSDIAREKEDAISALREQVGSLSVLIASKVIEKNLDEKEQSNLIQDYIERLGDDK
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
Q8Y4B8
|
Q9LZJ7
|
PRP3_ARATH
|
Proline-rich protein 3
|
Arabidopsis
|
MAITRSSLAICLILSLVTITTADYYSPSSPPVYKSPEHKPTLPSPVYTPPVYKPTLSPPVYTKPTIPPPVYTPPVYKHTPSPPVYTKPTIPPPVYTPPVYKPTLSPPVYTKPTIPPPVYTPPVYKPTPVYTKPTIPPPVYTPPVYKPTPSPPVYKKSPSYSSPPPPYVPKPTYTPTTKPYVPEILKAVDGIILCKNGYETYPILGAKIQIVCSDPASYGKSNTEVVIYSNPTDSKGYFHLSLTSIKDLAYCRVKLYLSPVETCKNPTNVNKGLTGVPLALYGYRFYPDKNLELFSVGPFYYTGPKAAPATPKY
|
May contribute to cell wall structure in root hairs.
|
Q9LZJ7
|
P24181
|
ACRF_ECOLI
|
Protein EnvD
|
Escherichia
|
MANFFIRRPIFAWVLAIILMMAGALAILQLPVAQYPTIAPPAVSVSANYPGADAQTVQDTVTQVIEQNMNGIDNLMYMSSTSDSAGSVTITLTFQSGTDPDIAQVQVQNKLQLATPLLPQEVQQQGISVEKSSSSYLMVAGFVSDNPGTTQDDISDYVASNVKDTLSRLNGVGDVQLFGAQYAMRIWLDADLLNKYKLTPVDVINQLKVQNDQIAAGQLGGTPALPGQQLNASIIAQTRFKNPEEFGKVTLRVNSDGSVVRLKDVARVELGGENYNVIARINGKPAAGLGIKLATGANALDTAKAIKAKLAELQPFFPQGMKVLYPYDTTPFVQLSIHEVVKTLFEAIMLVFLVMYLFLQNMRATLIPTIAVPVVLLGTFAILAAFGYSINTLTMFGMVLAIGLLVDDAIVVVENVERVMMEDKLPPKEATEKSMSQIQGALVGIAMVLSAVFIPMAFFGGSTGAIYRQFSITIVSAMALSVLVALILTPALCATLLKPVSAEHHENKGGFFGWFNTTFDHSVNHYTNSVGKILGSTGRYLLIYALIVAGMVVLFLRLPSSFLPEEDQGVFLTMIQLPAGATQERTQKVLDQVTDYYLKNEKANVESVFTVNGFSFSGQAQNAGMAFVSLKPWEERNGDENSAEAVIHRAKMELGKIRDGFVIPFNMPAIVELGTATGFDFELIDQAGLGHDALTQARNQLLGMAAQHPASLVSVRPNGLEDTAQFKLEVDQEKAQALGVSLSDINQTISTALGGTYVNDFIDRGRVKKLYVQADAKFRMLPEDVDKLYVRSANGEMVPFSAFTTSHWVYGSPRLERYNGLPSMEIQGEAAPGTSSGDAMALMENLASKLPAGIGYDWTGMSYQERLSGNQAPALVAISFVVVFLCLAALYESWSIPVSVMLVVPLGIVGVLLAATLFNQKNDVYFMVGLLTTIGLSAKNAILIVEFAKDLMEKEGKGVVEATLMAVRMRLRPILMTSLAFILGVLPLAISNGAGSGAQNAVGIGVMGGMVSATLLAIFFVPVFFVVIRRCFKG
|
Part of the tripartite efflux system AcrEF-TolC. Involved in the efflux of indole and organic solvents.
|
P24181
|
Q2N9C1
|
RL14_ERYLH
|
50S ribosomal protein L14
|
Erythrobacter
|
MIQMQSNLDVADNSGAKRVQCIKVLGGSKRRTASVGDVIVVSVKEAQPRAKVKKGDVHRAVIVRTKKDVRRPDGSVIRFDSNAAVLVSKNEEPIGTRIFGPVVRELRGRGFMKIISLAPEVL
|
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
|
Q2N9C1
|
Q31YT6
|
MSBA_SHIBS
|
Lipid A export ATP-binding/permease protein MsbA
|
Shigella
|
MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQFGQ
|
Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
|
Q31YT6
|
Q8EK70
|
EFTU2_SHEON
|
Elongation factor Tu 2
|
Shewanella
|
MAKAKFERSKPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLELVEMEVRELLSEYDFPGDDLPVIQGSALKALEGEPEWEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEIVGIRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGSINPHTTFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLICPIAMDEGLRFAIREGGRTVGAGVVAKIIA
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
Q8EK70
|
A7GN77
|
PANC_BACCN
|
Pantoate-activating enzyme
|
Bacillus cereus group
|
MKVITTVKDMQQIAGELRASGKEIGFVPTMGYLHEGHATLLRQAKKENDIVILSVFVNPLQFGPDEDFDRYPRDIKRDERVAKEAGVDYLFYPSVDEMYPAEQTTKIEVVKRTNVLCGKRRPVHFAGVATVLMKLFHITMPTRAYFGMKDAQQVAVVEGIVSDFHIPVTIVPVEIVREADGLAKSSRNVYLSEQERKEAPHLYRSLCIAKQKIEEGERHPRNITTVVKEYIEANTNGIVDYVDIYAYPALTPLEIIKGRIILAIAVQFKNARLIDNITLTVQ
|
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
|
A7GN77
|
A3D5N8
|
PEPE_SHEB5
|
Dipeptidase E
|
Shewanella
|
MTINALLLSSSRVGDTPYLAHAIPFIKPLTTNAQKWIFIPYAGVSMSYDTYLASVVTGLSELELDISGIHQHPDPQQAIKDADGILIGGGNTFHLLHQLYRYDLVTLIGEQVALGKPYIGWSAGSNVSGLSIRTTNDMPIIEPPSFNALNLVPFQLNPHYSNYQAPGHNGETRAQRLLEFTKVDPLTPVVGIVEGSALWRQGDKLSLLGDQPAYLFCGEQQEIPIPVGSDLSHLLKA
|
Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.
|
A3D5N8
|
A7IJG7
|
OIAT_XANP2
|
3-oxo-isoapionate-4-phosphate transcarboxylase/hydrolase
|
Xanthobacter
|
MSERVYATYWMETGGDPARTAEVIAGEQSSGTFVALATETAELKERSGARVERLDILDTADIPSLPGGMASDRYTRAILELSWPVENFGPSLPNLMSTIAGNLFELHQVSGLRLIDLKLPPSFTNAFAGPAFGIAGTRKLAGVAQGPIIGTIIKPSIGLTPEETAQQVRELIAGDIDFIKDDELQADGARCPFEARVKAVMRVVNDAADRRGRKVMVAFNITGDLDEMRRRHDLVLAEGGTCVMVCLNSIGLVGVREIRRHTQLPIHGHRAGWGYLYRCPSLGWDYAPWQQLWRLAGVDHLHVNGLDNKFSEANASVIAAARAVLSPLNHAAPMGAMPVFSSGQTGRQAAETYAAIGCADLIHTAGGGIFGHPAGVPAGVEALRAAWRAAMAGASLEDEATRSPALRSALGFWR
|
Involved in catabolism of D-apiose. Catalyzes the conversion of 3-oxo-isoapionate 4-phosphate to 3-phosphoglycerate and glycolate.
|
A7IJG7
|
P07128
|
KHSE_CORGL
|
Homoserine kinase
|
Corynebacterium
|
MAIELNVGRKVTVTVPGSSANLGPGFDTLGLALSVYDTVEVEIIPSGLEVEVFGEGQGEVPLDGSHLVVKAIRAGLKAADAEVPGLRVVCHNNIPQSRGLGSSAAAAVAGVAAANGLADFPLTQEQIVQLSSAFEGHPDNAAASVLGGAVVSWTNLSIDGKSQPQYAAVPLEVQDNIRATALVPNFHASTEAVRRVLPTEVTHIDARFNVSRVAVMIVALQQRPDLLWEGTRDRLHQPYRAEVLPITSEWVNRLRNRGYAAYLSGAGPTAMVLSTEPIPDKVLEDARESGIKVLELEVAGPVKVEVNQP
|
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
|
P07128
|
P27477
|
THTR_SYNE7
|
Rhodanese-like protein
|
Synechococcus
|
MSVRSLRWPRQKAFLAVISLVVAVLLAVPGWLTPATAASQATVQFVAPTWAAERLNNKQLKILDVRTNPLAYIEGHLPGAVNIADAAYRGPNGFLPVQIWDPEKLASLFGRAGVSNNDTVLVYSDGNDVLGATLVAYLLERSGVQNIAVLDGGYKGYKDAGLPVTKEYPRYQAARFAPKDNRAFRVDIKQVEQLTGKSTFVDPRPPALFSGEQQVFIRNGHIPGARNIPWPTFTEANNANESLKNPHKLKPLSELKAILEAKGVTPDKDVIVTCSTGREASLQYLVLKHLLKYPKVRIYEGSWTEYSASNLPVETGPDRV
|
May be a sulfotransferase involved in the transport of sulfate. Displays very low rhodanese activity.
|
P27477
|
B9DX62
|
ATPG_CLOK1
|
F-ATPase gamma subunit
|
Clostridium
|
MAGAGLVTIKRRIKSITSTQKITKAMGLIATSKLRKVRKKLEANNKYCELFSSIVNELAMEAEQNNIYIKGNKSNKKLYIALNSDTGLCGGFNANVVNELNSIRSKEKEDFLLITMGQKGKMYFRRLNYNIESEYIDIPDVPTIKETEDVVYKALELYRNGEIGEINIVFTKFISTIKQNVIVEKLLPLEVKKVEKRNFIVKFEPSADEMIEDIVELHLRQKLLNCIINSKVSEQSSRMTAMDGATKNANDLLDELNLQYNRERQTAITQEITEIVGGAEALK
|
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.
|
B9DX62
|
B1KFT2
|
RPIA_SHEWM
|
Phosphoriboisomerase A
|
Shewanella
|
MTQDEMKKAAGWAALEYVEKDSIVGVGTGSTVNHFIDALATMKAEIEGAVSSSEASTQKMKDLGIPVFDLNSVDELSVYVDGADEINAHMDMIKGGGAALTREKIVAAVADKFICIVDNTKQVDVLGEFPLPVEVIPMARSYVARQLVKLGGDPVYREGVITDNGNIILDVYNMKIVNPKELEQQINKIVGVVTNGLFANRGADVLLVGSPDGVKTLK
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
B1KFT2
|
O57762
|
THS_PYRHO
|
Chaperonin subunit
|
Pyrococcus
|
MAQLAGQPILILPEGTQRYVGRDAQRMNILAARIIAETVRTTLGPKGMDKMLVDSLGDIVITNDGATILDEMDIQHPAAKMMVEVAKTQDKEAGDGTTTAVVIAGELLKKAEELLDQNIHPSIIIKGYTLASQKAQEILDSIAKEVKPDDEEVLLKAAMTAITGKAAEEEREYLAKLAVEAVKLVAEEKDGKLKVDIDNIKLEKKEGGAVRDTRLIRGVVIDKEVVHPGMPKRIENAKIALINDALEVKETETDAEIRITSPEQLQAFLEQEEKMLKEMVDKIKEVGANVVFVQKGIDDLAQHYLAKYGILAVRRVKKSDMEKLAKATGAKIVTNIRDLTPEDLGEAELVEERKVAGENMIFVEGCKNPKAVTILIRGGTEHVVDEVERALEDAIKVVKDILEDGKIIAGGGASEIELSIKLDEYAKEVGGKEQLAIEAFAEALKVIPRTLAENAGLDPIETLVKVIAAHKEKGQTIGIDVYEGEPADMMERGVIEPVRVKKQAIKSASEAAIMILRIDDVIAASKLEKEKEGEKGGGSEEFSGSSDLD
|
Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
|
O57762
|
C5BPQ5
|
CCA_TERTT
|
Phosphatase
|
Teredinibacter
|
MKIYLVGGAVRDQLLGYPHHEQDWVVVGATPQQMLDAGFKPVGKDFPVFLHPETQEEYALARQERKTAPGYTGFAFHADETVTLEQDLLRRDLTINAIAMDEEGTIIDPYNGKRDIETRTLRHVSQAFCEDPVRILRIARFAARYHHLGFRIAPETLALMRDMVQAGEVDHLVAERVWKELSRALEEQHPAIFIQTLRECGALHRLMPELNALFGIPQPEAHHPEVDTGVHALLALERACELSSTPEVRFAALIHDLGKGVTPKHLWPSHHGHEQDGVALVEQLCNRLSTPNQFRELAVAVCAYHTHCHRAFELNAKTLLKTLLALDGLRRPERFQQFCLCCQADAQGRTGLENRPYPQAAYFLQALEEIQKVDAKMFVAQGKKGAEIGEAMYSARLQKIKLLKTAQTPHE
|
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.
|
C5BPQ5
|
B2S928
|
G6PI_BRUA1
|
Phosphohexose isomerase
|
Brucella
|
MARDATKLEATVAKLKKHWAESAPRDMRAAFSTDPGRFGRYSLCLDDLLFDWSKCRVNDETMALLKELAVAADVEGRRAAMFAGEHINNTEDRAVLHVALRDTSSKEVLVDGHNVLPDVKHVLDRMAAFADGIRSGALKGATGRKITDIVNIGIGGSDLGPVMATLALAPYHDEPRAHFVSNIDGAHIADTLSPLDPASTLIIVASKTFTTIETMTNAQTARKWVADTLGEAAVGAHFAAVSTALDKVAAFGIPEDRVFGFWDWVGGRYSVWSAIGLPVMIAVGPDNFRKFLAGAHAMDVHFRDAPLEKNLPVMLGLIGYWHRAICGYGSRAIIPYDQRLSRLPAYLQQLDMESNGKSVTLDGKPVSGPTGPVVWGEPGTNGQHAFFQLLHQGTDTIPLEFIVAAKGHEPTLDHQHEMLMANCLAQSEALMKGRTLDEARAQLQAKNLPASQVERIAPHRVFSGNRPSLTLIHDMLDPYALGRLIALYEHRVFVEAQIFGINAFDQWGVELGKELATELLPVVSGKEGASGRDASTQGLVAHLHARRKA
|
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
|
B2S928
|
A5CEN6
|
IF2_ORITB
|
Translation initiation factor IF-2
|
Orientia
|
MTDKHNEEGKEKKLKLPSKMIIGKHVDSKKFKTSYFTSHNNSVTVEIKGGRKFSSSSSLPHKINTQISTIDEFNEKISLLKKAASFAKSEEYRSNVTNFSSTVEVTEQQTEAENSTNINLSEQTIKNNSHQSSSNTIETTQEKKQNDDLSSNITPVEAITQLEPNQKILQNQQNSSSISLNSIISKPQNKSSIENNVEFETEATSTKSSAIWTKKNNSAKPKKSDIYQMLDSDSKSKTRSFAAIKRARDKEKRKLQNNALTKKIYREVIIPDTITVNELALRMSEKLSDVMQALLKLGIKANINQSIDVDTAELIAISLGHSVKRTQDSDVENILHSDKDTQDSLLPRAPIITVMGHVDHGKTCLLDALRSTDVISTEAGGITQHIGAYKVNLPNNKSITFIDTPGHEAFSEIRTRGAKVTDIVVLVIAANDGIKPQTIEAINHAKAAKVPILVAINKIDAPDANPDKVKNALLAHNIVPEDLGGETLVVPISALKKINLDKLEEAILLLADMLELKANPNALASGTVIESQVDHKSGVIATILVQRGTLKIGDILIAGNGFGKVKRMINDKNQQVNYAYPSDPVKILGLSQIPNAGDAVAVVQNEKQARSIVDYRIRKAKEEQDLKVHNISLEELLKQASANQFKELSLILKTDVHGSLEAIVASINKIVNDEVKIKILHAAVGVINESDIILANASNATILGFNVKIDSTASIKAERNKTNIKYYSIIYDLIDYVKSAVSGMLSPIIHEEYTGRAEVRAVFNITKVGKIAGCYVTKGYIQRNSKVKLLRNNEVIFSGPLQTLKRFKEHTKEVKEGFECGIELANYYDINVGDIIEAFIVTEEKAKL
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
A5CEN6
|
Q7U571
|
PSAJ_PARMW
|
Photosystem I reaction center subunit IX
|
Parasynechococcus marenigrum
|
MQKFLTTAPVVAAIWFTLTAGILIEWNRFFPDLLFHPM
|
May help in the organization of the PsaE and PsaF subunits.
|
Q7U571
|
B5Z6T1
|
ACP_HELPG
|
Acyl carrier protein
|
Helicobacter
|
MALFEDIQAVIAEQLNVDAAQVTPEAEFVKDLGADSLDVVELIMALEEKFGVEIPDEQAEKIVNVGDVVKYIEDNKLA
|
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
|
B5Z6T1
|
A1RDZ0
|
AROE_SHESW
|
Shikimate dehydrogenase (NADP(+))
|
Shewanella
|
MTDKYAVFGNPISHSKSPFIHGQFAAPTQELLTYEAILAPVDGFEASLTAFFNAGGKGANVTVPFKEQAFALCDSLSPEAKLAGAVNTLSLLADGTIRGDNTDGLGLVADLIANLGSLQGKRVLLIGAGGAARGCILPLLNAGIAQLTISNRTHTKAQLLVDIFTSVDNGAFANRVTAVEMNELVGEFDIIINSTSASLAGELPPVPAHIITPQTVCYDMMYGASVTAFNQWALSQGAAKVIDGLGMLVGQAAKSFTLWRGVEPDTQVVLTLLRDKLKAEPK
|
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).
|
A1RDZ0
|
A7ZP75
|
ARNT_ECO24
|
Undecaprenyl phosphate-alpha-L-Ara4N transferase
|
Escherichia
|
MKSVRYLIGLFAFIACYYLLPISTRLLWQPDETRYAEISREMLASGDWIVPHLLGLRYFEKPIAGYWINSIGQWLFGANNFGVRAGVIFATLLTTALVTWFTLRLWRDKRLALLATVIYLSLFIVYAIGTYAVLDPFIAFWLVAGMCSFWLAMQAQTWKGKSAGFLLLGITCGMGVMTKGFLALAVPVLSVLPWVATQKRWKDLFIYGWLAVISCVLTVLPWGLAIAQREPDFWHYFFWVEHIQRFALDDAQHRAPFWYYVPVIIAGSLPWLGLLPGALYTGWKNRKHSATVYLLSWTIMPLLFFSVAKGKLPTYILSCFASLAMLMAHYALLAAKNNPLALRINGWINIAFGVTGIIATFVVSPWGPMNTPVWQTFESYKVFCAWSIFSLWAFFGWYTLTNVEKTWPFAALCPLGLALLVGFSIPDRVMEGKHPQFFVEMTQESLQPSRYILTDSVGVAAGLAWSLQRDDIIMYRQTGELKYGLNYPDAKGRFVSGDEFANWLNQHRQEGIITLVLSVDRDEDINSLAIPPADAIDRQERLVLIQYRPK
|
Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
|
A7ZP75
|
A1WY18
|
QUEC_HALHL
|
Queuosine biosynthesis protein QueC
|
Halorhodospira
|
MAERPQRVPASTEQESALVLFSGGQDSTACLAWALEYFSRVETVGFAYGQRHDVELSAREEVLDGLRALRPDWAARLGSDRVLDAGVLGEISDTALTQDAEIAYDARGLPTTFVPGRNLLFFTLAAAVAHRRGIRHLVAGVCETDFSGYPDCRDDTVKSLQVTLNLGMAERLVLHTPLMWLDKAQTWMLAEQLGGSALVDLTVEASHTCYYGMREQRHEWGYGCGECPACRLRAEGWHRFRHGSGAQ
|
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
|
A1WY18
|
Q14FE6
|
YCF4_POPAL
|
Photosystem I assembly protein Ycf4
|
Populus
|
MSWRSEHIWIELIAGSRKISNFCWAIILFLGSLGFLLIGISSYLDRNLISLFPSQQIIFFPQGLVMSFYGLAGLFISSYLWCTISWNVGSGYDRFDRKEGIVCIFRWGFPGKNRRILLRLFMKDIQSIRIEVKEGFYARRVLYMEIRGQGAIPLTRTDENLTPREIEQKAAELAYFLRVPIEVF
|
Seems to be required for the assembly of the photosystem I complex.
|
Q14FE6
|
Q32BA8
|
RL13_SHIDS
|
50S ribosomal protein L13
|
Shigella
|
MKTFTAKPETVKRDWYVVDATGKTLGRLATELARRLRGKHKAEYTPHVDTGDYIIVLNADKVAVTGNKRTDKVYYHHTGHIGGIKQATFEEMIARRPERVIEIAVKGMLPKGPLGRAMSRKLKVYAGNEHNHAAQQPQVLDI
|
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.
|
Q32BA8
|
P56689
|
DPOL_THEGO
|
TO POL
|
Thermococcus
|
MILDTDYITEDGKPVIRIFKKENGEFKIDYDRNFEPYIYALLKDDSAIEDVKKITAERHGTTVRVVRAEKVKKKFLGRPIEVWKLYFTHPQDVPAIRDKIKEHPAVVDIYEYDIPFAKRYLIDKGLIPMEGDEELKMLAFDIETLYHEGEEFAEGPILMISYADEEGARVITWKNIDLPYVDVVSTEKEMIKRFLKVVKEKDPDVLITYNGDNFDFAYLKKRSEKLGVKFILGREGSEPKIQRMGDRFAVEVKGRIHFDLYPVIRRTINLPTYTLEAVYEAIFGQPKEKVYAEEIAQAWETGEGLERVARYSMEDAKVTYELGKEFFPMEAQLSRLVGQSLWDVSRSSTGNLVEWFLLRKAYERNELAPNKPDERELARRRESYAGGYVKEPERGLWENIVYLDFRSLYPSIIITHNVSPDTLNREGCEEYDVAPQVGHKFCKDFPGFIPSLLGDLLEERQKVKKKMKATIDPIEKKLLDYRQRAIKILANSFYGYYGYAKARWYCKECAESVTAWGRQYIETTIREIEEKFGFKVLYADTDGFFATIPGADAETVKKKAKEFLDYINAKLPGLLELEYEGFYKRGFFVTKKKYAVIDEEDKITTRGLEIVRRDWSEIAKETQARVLEAILKHGDVEEAVRIVKEVTEKLSKYEVPPEKLVIYEQITRDLKDYKATGPHVAVAKRLAARGIKIRPGTVISYIVLKGSGRIGDRAIPFDEFDPAKHKYDAEYYIENQVLPAVERILRAFGYRKEDLRYQKTRQVGLGAWLKPKT
|
In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.
|
P56689
|
D2Y234
|
H4B01_CYRHA
|
Hainantoxin-IV-2
|
Haplopelma
|
MKASMFLALAGLALLFVVCYASESEEKEFSNELLSSVLAVDDNSKGEERECLGFGKGCNPSNDQCCKSSNLVCSRKHRRCKYEIGK
|
Neurotoxin. Selectively blocks neuronal tetrodotoxin-sensitive voltage-gated sodium channels (Nav). Does not affect tetrodotoxin-resistant voltage-gated sodium channels or calcium channels.
|
D2Y234
|
P32961
|
NRL1_ARATH
|
Nitrilase 1
|
Arabidopsis
|
MSSTKDMSTVQNATPFNGVAPSTTVRVTIVQSSTVYNDTPATIDKAEKYIVEAASKGAELVLFPEGFIGGYPRGFRFGLAVGVHNEEGRDEFRKYHASAIHVPGPEVARLADVARKNHVYLVMGAIEKEGYTLYCTVLFFSPQGQFLGKHRKLMPTSLERCIWGQGDGSTIPVYDTPIGKLGAAICWENRMPLYRTALYAKGIELYCAPTADGSKEWQSSMLHIAIEGGCFVLSACQFCQRKHFPDHPDYLFTDWYDDKEHDSIVSQGGSVIISPLGQVLAGPNFESEGLVTADIDLGDIARAKLYFDSVGHYSRPDVLHLTVNEHPRKSVTFVTKVEKAEDDSNK
|
Can convert indole-3-acetonitrile to the plant hormone indole-3-acetic acid.
|
P32961
|
Q92A81
|
AROB_LISIN
|
3-dehydroquinate synthase
|
Listeria
|
MPEITVRAKSKTYPVYINEFALTDVKEQWTKSLAKYSHVFVLTDEHVANLHKAKLDAVLADLPVVTYYVAPNGEEAKTFRVYEDVMTKMIETGLDRKAVLIAFGGGVIGDLGGFVAATYMRGIPFYQVPTTVLAHDSAVGGKVAINHPLGKNMIGNFYQPEAVIYDTQFFATLPEREMRSGFAEMIKHALISDHALLTALMDTFTEPKDFYTKDLTPFLQRGIEIKANIVAQDETEQGVRAYLNFGHTFGHALEAYGNFGKWLHGEAITYGMIYALTMSETVYGLDFDLAKFTTWLERLGYNTTFDVTVPFSNILDNMRHDKKTTFNEISMVLLEDIGKPVIFKAEDELIFDTYKSVMRNGGDLF
|
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
|
Q92A81
|
Q7L5N1
|
CSN6_HUMAN
|
Vpr-interacting protein
|
Homo
|
MAAAAAAAAATNGTGGSSGMEVDAAVVPSVMACGVTGSVSVALHPLVILNISDHWIRMRSQEGRPVQVIGALIGKQEGRNIEVMNSFELLSHTVEEKIIIDKEYYYTKEEQFKQVFKELEFLGWYTTGGPPDPSDIHVHKQVCEIIESPLFLKLNPMTKHTDLPVSVFESVIDIINGEATMLFAELTYTLATEEAERIGVDHVARMTATGSGENSTVAEHLIAQHSAIKMLHSRVKLILEYVKASEAGEVPFNHEILREAYALCHCLPVLSTDKFKTDFYDQCNDVGLMAYLGTITKTCNTMNQFVNKFNVLYDRQGIGRRMRGLFF
|
Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Has some glucocorticoid receptor-responsive activity. Stabilizes COP1 through reducing COP1 auto-ubiquitination and decelerating COP1 turnover rate, hence regulates the ubiquitination of COP1 targets.
|
Q7L5N1
|
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