Datasets:
habdine
/
Prot2Text-Data

Dataset card Data Studio Files
xet
Community
1
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
Q86R84
CHL18_DERFA
Allergen Der f 18
Dermatophagoides
MTRFSLTVLAVLAACFGSNIRPNVATLEPKTVCYYESWVHWRQGEGKMDPEDIDTSLCTHIVYSYFGIDAATHEIKLLDEYLMKDLHDMEHFTQHKGNAKAMIAVGGSTMSDQFSKTAAVEHYRETFVVSTVDLMTRYGFDGVMIDWSGMQAKDSDNFIKLLDKFDEKFAHTSFVMGVTLPATIASYDNYNIPAISNYVDFMNVLSLDYTGSWAHTVGHASPFPEQLKTLEAYHKRGAPRHKMVMAVPFYARTWILEKMNKQDIGDKASGPGPRGQFTQTDGFLSYNELCVQIQAETNAFTITRDHDNTAIYAVYVHSNHAEWISFEDRHTLGEKAKNITQQGYAGMSVYTLSNEDVHGVCGDKNPLLHAIQSNYYHGVVTEPTVVTLPPVTHTTEHVTDIPGVFHCHEEGFFRDKTYCATYYECKKGDFGLEKTVHHCANHLQAFDEVSRTCIDHTKIPGC
Probably a non-catalytic chitinase-like protein, which binds to insoluble chitin and enhances the activity of the catalytic chitinases. Has weak chitin-binding activity.
Q86R84
Q556Z3
TPC10_DICDI
Transport protein particle subunit TMEM1
Dictyostelium
MSNVSPNSMNLNGSTSSTASVNDSGGGGGGGNVTSPTLSSSSASSISNSNSSSSNNLKPSTQPLSSSSTLNTPTQFSLQHSSSSSSLNNTNIDIIEHITISYQDESSIWKYIEAELPNHLPLKNISWKTKTGHTKVVEKMPIEILQYNDERVKAHYDNQNLYKKPYLYLYLVHCDDPDTYKNVVRAKIKQWVTQMTERQQEWLIVYVSLGPKRFSELTSKLTRTVFDRIKNDFNVKRDRCCQLRFLDTNNTSSGNNKDKDNDNGGGSSGTGLSTSTKQQDDLWDDFLIKMKEGIISSAEQYLTTYEDEIRKMDAKRTTPGWSYQNFFFIKEGLALIYERAQLYEDALMQYFELEVLFGDPNNRSQFDQITDEVLQPNSIHCNGNILDTSFKNYRKLIYENKISLFDFKVYLFARQSKLLFLLQKPIEAATKSISFITSMSMIIKQYPNSFAPMFKESWIFSTSMELIKACQDSFDKIVNGAQQQQQQQQQQLQLQQQLQQQQQQQTINGSAQKVVKSISSTTPISKLFGAFGPFGSSSSNTPSSTSATTAANGKNTPMPSNSGIASLSAGGSTIIAGLSGSQSLNNLQSAQLSGALNTQHYIRTPSLNLTSDLSERLTEKQDRESLDFLVGDLLFSSAQRLEELAIIIGYLPVDDYNSEMFFQNVEEVIFKSVENKKIEVDSMTAFSYQPLQVSLQSSKQFTQLYFELLGQIEKLYIQSNRMRSISRLTFAIANLNFKLKEFQIAENLFKSISNLYSREHWSYIEYAVKTRLSYCQKQLGHLVDYVTTCVGLLAPGLLTNRFEKDHYLSEIIQISRKPELNIVQPMIPLFKCKVTFKETVYRYFETIKINVRIKSNLISPIRFNNGAVSFVKSGFGDKLVFQLNDFLVEPGVNNFQFTAVGTTKATFVKDSIWLKIDNLSFGYSLRNADTAIGGGGGGTNTTTTTLPGEIKVIDSESQITLESFANSPLLFYSIQYVGIKLHTHSDTIEAGVLTFTSPTGATIIPTSSVIIIQSDDKTCETSSRTINLINDKLPLSQIGYNQTLEFYLPLMAVNTDTCTHQIRIELQHQKQTKEKFSSSLVSSILFINPLTIDESVINVNNRLFLKTIIQCNSPNMIQFNSYSLEGCDSEYQSPEQQQLQQQLQQQQQLSLSSSSSSISSISSKSSQQPNLYYLVKDHNHSLAPNLNLYPGQLVSLIFEIKKYENESLSSSTSPSSATDSSNSNGNNNNNNNNNNHSKNDLKLKIKYTSKMPQQDLDRPLIRECKSLWRDQNEFSWPIKIELPTYLYQIDLSIQSRAYVGTIVLFEIEITNLKQQQQQQKESNNDNGNEKQQKQQQLQYHIVADSQIWMISGKSKHTFSFNSDTVGEKLKFSCGLIPISSGSLPIPKVTLVGINNSNISYPKTKNEKIFVYPSPQIYSCHQLQDNNNNNNNSINSQTSTNKT
May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Q556Z3
P20620
NIFD_METTL
Nitrogenase component I
Methanothermococcus
MPYILLDCDKFIPERMKHTYVYDPEENILPACNTNTVPGDMTERGCAFAGSRGVVGGPIKDAIHMVHGPIGCAYYTWGTRRALSDNEFHRRYCFCTDMQESDIVYGGEKTLEKASLEVMEEFPEASGTFIYTTCPTALIGDNVDAIARNIEKATKKPAIAINSPGFCGVSQSKGHHVFNMTFYKWLKLKRKEFPEKCMPEEEKTPYDVALIGDYNMDWDVAVIKPLLEKIGCRYVTTFTGNASLDELFQLMDVKLNIVHCQRSAEYIAQMINDGFDIPYTRATFFGLSDIAESLYDVAKALDLPKERVDQVIKEEMEAIQPKLDYYKSKLEGKTCMVYVGGPRTWHWIKAMKDLGVEYVAACCTFSHTDDYEKMNKNFKEAGIKDILVIDAPNEPELEEAVKTLDPDFMLVGLKERYLFRKYGVPTINSHSYEEGPYAGYRGFVNFARDVYKAVCHPVWNVLKEGEDKFKNFKGDLNE
This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
P20620
A3Q996
RS8_SHELP
30S ribosomal protein S8
Shewanella
MSMQDPIADMLTRIRNGQAANKVSVSMPSAKLKVAIAQTLKEEGYITDYTVAGEAKPVLEITLKYFQGQPVVETIQRVSRPGLRIYKGKNDLPKVMGGLGVAIVSTSKGLMTDRAARQQGMGGEVICYVA
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.
A3Q996
A8ER22
LUXS_ALIB4
Autoinducer-2 production protein LuxS
Aliarcobacter
MPLLDSFRVDHTIMPAPAVRVAKVMQTPKGDDITVFDLRFCVPNKSMMSEKGTHTLEHLFAGFIRNHLNSPTVEIIDVSPMGCRTGFYMSLIGTPSEQEVAVAWKKAMEDVLKVENQSDIPELNLYQCGTCAMHSLDEAKDIARDILKSQIGVMSNKELYLSEEKLKSLGN
Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
A8ER22
Q8NML5
MURA_CORGL
UDP-N-acetylglucosamine enolpyruvyl transferase
Corynebacterium
MKDKFLVTGGAQLQGAVKVYGAKNSVLKLMAAALLAEGTTTLTNCPEILDVPLMRDVLVGLGCDVTIDGSTVTITTPAELSSNADFPAVTQFRASVCVLGPLTARCGRAVVSLPGGDAIGSRPLDMHQSGLEKLGATTRISHGAVVAEAEKLVGANITLDFPSVGATENILTASVMAEGRTVLDNAAREPEIVDLCRMLRSMGANIEGEGSPTITIEGVEKLTPTQHEVIGDRIVAGTWAYAAAMTRGDITVGGIAPRYLHLPLEKLKIAGAKVETYENGFRVQMDKQPEATDYQTLPFPGFPTDLQPMAIGINAVSNGTSVITENVFESRFRFVDEMLRLGADANVDGHHVVIRGIEQLSSTSVWSSDIRAGAGLVLAALCADGVTEVHDVFHIDRGYPNFVENLQKLGATIERVSS
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Q8NML5
Q9M9A8
APCB1_ARATH
Aspartyl protease cleaving BAG 1
Arabidopsis
MEPDLHDQQQQQRVHSVVIITLPPSDDPSQGKTISAFTLTDHDYPLEIPPEDNPNPSFQPDPLHRNQQSRLLFSDLSMNSPRLVLGLLGISLLAVAFYASVFPNSVQMFRVSPDERNRDDDDNLRETASFVFPVYHKLRAREFHERILEEDLGLENENFVESMDLELVNPVKVNDVLSTSAGSIDSSTTIFPVGGNVYPDGLYYTRILVGKPEDGQYYHLDIDTGSELTWIQCDAPCTSCAKGANQLYKPRKDNLVRSSEAFCVEVQRNQLTEHCENCHQCDYEIEYADHSYSMGVLTKDKFHLKLHNGSLAESDIVFGCGYDQQGLLLNTLLKTDGILGLSRAKISLPSQLASRGIISNVVGHCLASDLNGEGYIFMGSDLVPSHGMTWVPMLHDSRLDAYQMQVTKMSYGQGMLSLDGENGRVGKVLFDTGSSYTYFPNQAYSQLVTSLQEVSGLELTRDDSDETLPICWRAKTNFPFSSLSDVKKFFRPITLQIGSKWLIISRKLLIQPEDYLIISNKGNVCLGILDGSSVHDGSTIILGDISMRGHLIVYDNVKRRIGWMKSDCVRPREIDHNVPFFQG
Involved in proteolytic processing of BAG6 and plant basal immunity.
Q9M9A8
Q9YBY6
LYSJ_AERPE
Putative [LysW]-aminoadipate semialdehyde/glutamate semialdehyde transaminase
Aeropyrum
MNVVLKFVRFYGYRGLRIVKGSMQYVWDDSGRKYLDCHAGHGAAFLGHSNPAIVEAVVRQARELVAASSSFSTPSLEEALTEFSRIAPPWAEEIVFLNTGTEAVEAALKAAWLATGKRGIVALKNSFHGRTLASLSVTWNPRYRRGVPVLDTRFLSPSTDPGEVEKLVPEDTAAIIVEPIQGEGGLTKIYAELAKALREAADRVGALLIFDEIQTGFGRTGRVWAHESLGVEPDIMTAGKSIAGGLPASAVLSREGVLATLASGRHGSTHAANPLSMAAVAAASRFLREEGVPDKARAAGALLEGLLRDRIEGLRLVRGVRGEGLMLGVELRLDPGPVLRCLQESERVLALRSGATVVRLLPPYSISREDAEMVVYGLERCICGGSGC
Involved in both the arginine and lysine biosynthetic pathways.
Q9YBY6
Q630R0
PYRG_BACCZ
UTP--ammonia ligase
Bacillus cereus group
MTKYIFVTGGVVSSLGKGITAASLGRLLKNRGLNVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDINLNKYSNVTTGKIYSSVLQKERRGEYLGGTVQVIPHITNEIKERVYRSGRETNADVVITEIGGTVGDIESLPFLEAIRQIKSDIGRDNVMYIHCTLIPYLKAAGEMKTKPTQHSVKELRSLGIQPNIIVVRTEMPVSQDMKDKLALFCDIDTKAVIEARDADTLYAVPLSLQEQNMDQIVCDHLKLDNPAADMTEWTALVEKVRNLSKKTKIALVGKYVELQDAYISVVEALRHAGYSFDTDVEVKWVNAEHVTAENVQELVGDTDGILVPGGFGDRGVEGKIVAIQYARENKVPFLGICLGMQLASIEFARNVLGLEGANSSEINPDTPYAIIDLLPEQKDVEDLGGTLRLGLYPCKLSEETNAYNAYNEPVVYERHRHRYEFNNQFRPDMEKAGFVFSGTSPDGRLVEIIELKDHPWFVAAQFHPELVSRPNRPQPLFHDFVRASITNKESK
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.
Q630R0
Q3ZJ37
RK20_TUPAK
50S ribosomal protein L20, chloroplastic
Tupiella
MTRIKRGFVARKRRKKVLNLTKGFRGSSSVLFRPANQRKMKALRFSYRDRRQRKRDLRSLWITRINSASRLYNLNYSQFVYKLKQLNIHINRKWLAQLAIRDYKVFDELIKTVF
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
Q3ZJ37
A1T056
EFTU_PSYIN
Elongation factor Tu
Psychromonas
MSKAKFERKKPHLNVGTIGHVDHGKTTLTAAISAVLTKAHGGEVKDFASIDNAPEERERGITINTSHIEYDTDTRHYAHVDCPGHADYVKNMITGAAQMDAGILVVAATDGPMPQTREHILLSRQVGVPHLIVFMNKCDMVDDEELLELVEMEVRELLSEYDFPGDDLPVIQGSALKALEGDPVWEAKVMELADALDTYIPLPERDIDKPFILPIEDVFSIAGRGTVVTGRVERGIIKVGQEVEIIGLRPTVKTTCTGVEMFRKLLDEGRAGENVGILLRGTKRDDVERGQVLAKPGSIKPHTKFEGEVYILSKDEGGRHTPFFKGYRPQFFFRTTDITGAVELPEGVEMVMPGDNLKFVVDLIGPVAMDEGLRFAIREGGRTVGAGVVSKIIE
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
A1T056
P20630
COL12_CAEEL
Cuticle collagen 12
Caenorhabditis
MTEDPKQIAQETESLRKVAFFGIAVSTIATLTAIIAVPMLYNYMQHVQSSLQSEVEFCQHRSNGLWDEYKRFQGVSGVEGRIKRDAYHRSLGVSGASRKARRQSYGNDAAVGGFGGSSGGSCCSCGSGAAGPAGSPGQDGAPGNDGAPGAPGNPGQDASEDQTAGPDSFCFDCPAGPPGPSGAPGQKGPSGAPGAPGQSGGAALPGPPGPAGPPGPAGQPGSNGNAGAPGAPGQVVDVPGTPGPAGPPGSPGPAGAPGQPGQAGSSQPGGPGPQGDAGAPGAPGAPGQAGAPGQDGESGSEGACDHCPPPRTAPGY
Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment.
P20630
A0Q5E0
RSMA_FRATN
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
Francisella
MQYKTKAKKSLGQNFLQDENIIRKIVQLANIKKHDIVIEIGPGLGALTRYLLSSSNNVSVVEFDASVIDTLIANCQKYGTPHIYNQDFLKFDISSLENSSNQKIKLIGNLPYNISSPILFKVIKDSDKIVDAHFMLQKEVVERIVSLPNSKSYGRLSVILQYHFDCSMILKIPPEVFYPQPKVDSAILRLKPKNSKELLKNYNFFEEIVKQSFAQRRKTLHNNLKSILKERKIDPSTLPVDTNLRAENLSVGDFVSLANFLS
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
A0Q5E0
Q0UK54
STHR_PHANO
Stemphyloxin II biosynthesis cluster regulator
Parastagonospora
MSTISFFATSKRTSCDRCRKQKLRCPPDKDDMGTCGRCLRAGVACATSYTKPRGRSQKHGISTDGTSHVSGLDMQEPALPTPESVLSAGLTSSVQVAEDGSQLWSPLEEYNHLPSLSNFESGALSQSQDEDFAGLWWSPLHEDLDLDVHMDPSGACQNGYSAEISSFSRTDCSRQSNDCSPETLQHVECDMRLSQLNLELCRQSKAYHHWPNTTSDGSVRRPHFAIASALRDLLQNTEAFIHILHCLRNGTELNLDGRYQEPISTHDTGVSPPSLAFPSILNLTSCFFRIVDLFNVLLSSLALELATHSPLQRRSSSSSVTSALQILPDLKLAGLAVQEVSLQTKILVLTITHHFETMERLLGLPADLRVSECKDDNGYGLLGASWTSVLSSGRREKFELGWRRTGNWVTSIESLKANMGTLTKGSC
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II.
Q0UK54
A0A0H3MDW1
CHXR_CHLT2
Transcriptional regulatory protein
Chlamydia
MAGPKHVLLVSEHWDLFFQTKELLNPEEYRCTIGQQYKQELSADLVVCEYSLLPREIRSPKSLEGSFVLVLLDFFDEETSVDLLDRGFWYLIRPITPRILKSAISLFLSQHSLHSVPESIRFGPNVFYVLKLTVETPEGSVHLTPSESGILKRLLINKGQLCLRKHLLEEIKNHAKAIVARNVDVHIASLRKKLGAYGSRIVTLRGVGYLFSDDGDKKFSQQDTKLS
May be a global positive regulator of transcription . Binds a cis-acting element of its own promoter DNA sequence and is hence probably also involved in its own transcription activation . The recognition sequence is 5'-WHGAWNH-N(3-5)-WHGAWNH-3', where W is A/T, H is C/A/T, N is G/C/A/T and the linker length in the middle is 3 to 5 nucleotides .
A0A0H3MDW1
Q8HXY0
ETFA_MACFA
Electron transfer flavoprotein subunit alpha, mitochondrial
Macaca
MFRAAAPGQLRRAASSLRFQSTLVIAEHANDSLAPITLNTITAATRLGGEVSCLVAGTKCDKVAQDLCKVAGIAKVLVAQHDAYRGLLAEDLTPLILATQKQFNYTHICAGASAFGKNLLPRVAAKLEVAPISDIIAIKSPDTFVRTIYAGNALCTVKCDEKVKVFSVRGTSFEAAATSGGTASSEKASSTSPVEISEWLDQKLTKSDRPELTGAKVVVSGGRGLKSGENFKLLYDLADQLHAAVGASRAAVDAGFVPNDMQVGQTGKIVAPELYIAVGISGAIQHLAGMKDSKTIVAINKDPEAPIFQVADYGIVADLFKVVPEMTEILKKK
Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism.
Q8HXY0
A6GYA2
KDSB_FLAPJ
CMP-2-keto-3-deoxyoctulosonic acid synthase
Flavobacterium
MKIIAVIPARYASTRFPAKLMQDLGGKTVILRTYQAAVETNLFDDVFVVTDSELIYNEIITNAGKAIMSIKEHESGSDRIAEAIQNLEVDIVVNVQGDEPFINKEPLEEVIQVFRNDTHKKVDLASLMRNITHKNDIQNPNNVKVIVDQKGFALYFSRSVIPYPREENVGVRYMQHIGIYAFRKQALLDFYHLPMLSLEASEKLEQLRYLEYGKRIKMIETTHVGIGIDTLEDLEKARSML
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
A6GYA2
Q8N668
COMD1_HUMAN
Protein Murr1
Homo
MAAGELEGGKPLSGLLNALAQDTFHGYPGITEELLRSQLYPEVPPEEFRPFLAKMRGILKSIASADMDFNQLEAFLTAQTKKQGGITSDQAAVISKFWKSHKTKIRESLMNQSRWNSGLRGLSWRVDGKSQSRHSAQIHTPVAIIELELGKYGQESEFLCLEFDEVKVNQILKTLSEVEESISTLISQPN
Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2 . Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity . Involved in the regulation of membrane expression and ubiquitination of SLC12A2 . Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits and by promoting their ubiquitination presumably involving NEDD4L. Promotes the localization of SCNN1D to recycling endosomes . Promotes CFTR cell surface expression through regulation of its ubiquitination . Down-regulates SOD1 activity by interfering with its homodimerization . Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes . Can bind one copper ion per monomer . May function to facilitate biliary copper excretion within hepatocytes. Binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) . Involved in the regulation of HIF1A-mediated transcription; competes with ARNT/Hif-1-beta for binding to HIF1A resulting in decreased DNA binding and impaired transcriptional activation by HIF-1 . Negatively regulates neuroblastoma G1/S phase cell cycle progression and cell proliferation by stimulating ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B degradation in a FAM107A- and actin-dependent manner .
Q8N668
A0LIH6
EFTU_SYNFM
Elongation factor Tu
Syntrophobacter
MGKKKFERTKPHVNVGTVGHIDHGKTTLTAAITKQLAKRGRAEFVPFDQIDKAPEERERGITIATAHVEYETDKRHYAHVDCPGHADYIKNMITGAAQMDGAILVVAADDGPMPQTREHILLSRQVGVPYIVVFLNKVDMVDDPELIELVELELRELLSKYGFPGDDVPIIKGSALRALEADDPEHPDTKCIFELMEAIDAYVPDPVRDIDKPFLMPIEDVFSISGRGTVVTGRVERGVIRVSEDVEIVGFRPTFKTVCTGVEMFRKTLDQGQAGDNVGVLLRGTKRDEVERGQVVAKPGSITPHTKFKAEVYVLKKEEGGRHTPFFPGYRPQFYFRTTDVTGIMTLPEGVEMVMPGDNISTEVHLITPVALEKELRFAIREGGRTVGAGVITEIIE
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
A0LIH6
A1UTJ1
MNMA_BARBK
tRNA-specific 2-thiouridylase MnmA
Bartonella
MFLNSLDLPGPPENSRVVVAMSGGVDSSVVAGLLKREGYDVVGITLQLYDHGAATHRAGACCAGQDIEDARRVAETLRIPYYVLDYESRFREAVIDPFAESYARGETPIPCVACNQTVKFADLLVTARELGADALATGHYIRSVSYGTHRALFRPLDSERDQSYFLFATTQEQIDYLRFPLGNLPKARVREIAKEMGLTVADKHDSQDICFVPQGKYSDVIAKLRPEASNPGDIVHINGQILGQHSGIINYTVGQRRGIGVATGEALYVIFLDVENARVIVGPREMLETHKLFLRDVNWLGDERLENFPSDCIDVAAKIRSTRPPRPARLYYKEGIFSVDLLEGESSVAPGQACVFYNESGDGARVLGGGFITHSERSTDAEERLQRVLHN
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
A1UTJ1
C5CHX9
DAPA_KOSOT
4-hydroxy-tetrahydrodipicolinate synthase
Kosmotoga
MFRGAASAVITPFKGNEIDYDSFDKFLKFQLDSGINGLIVLGTTGEAPTVTSEERREIISFAVKKVGGRVPVIIGTGSNSTAHSIELSQEAFELGADGVLVVTPYYNKPTQEGLYRHYEAIAKSVPGHVIIYNVPGRTGIDIIPETVLRCAQIENIVGIKEASGNQAQVDELLRLKAKVRPEFKIWSGNDDQAFHLVCSGGDGVISVLSNVAPSQTVEMIAAALEGDLEKAREIHLKLFPLMKALFIETNPIPVKFATHLLGFGSETLRLPLTEASKRTREVVKKAMQDCGVLR
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
C5CHX9
Q944U4
METK_DENCR
Methionine adenosyltransferase
Dendrobium
MAEVDTFLFTSESVNEGHPDKLCDQISDAILDACLEQDPDSKVACETCSKTNMVMIFGEITTKANVDYEKIVRDTCRAIGFVSDDVGLDADNCKVLVNIEQQSPDIAQGVHGHFTKRPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEVRKNGTCPWLRPDGKTQVTVEYRNDGGAMVPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPVVPEQYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVANGLARRCIVQVSYAIGVPEPLSVFVDTYGTGKIPDKEILKIVKENFDFRPGMITINLDLKRGGNRFIKTAAYGHFGRDDPDFTWEVVKPLKWDKPAA
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Q944U4
Q6ZPR5
NSMA3_MOUSE
Neutral sphingomyelinase III
Mus
MAFPHLQQPSFLLASLKADSINKPFAQRCQDLVKVIEDFPAKELHAVFPWLVESIFGSLDGVLVGWNLRCLQGRVNPVEYSTAMEFLDPSGPMMKLVYKLQAEDYNFDFPVSCLPGPVKASIQENVLPDSPLYHNKVQFPPTGGLGLNLALNPFEYYMFYFALSLISQKPMSMTLHVRTSDCAYFTLVDRYLSWFLPTEGSVPPPLCSSPGGSSPSPAPRTPAMPFASYGLHTSLLKRHISHQTSVNADPASHEIWRSETLLQVFVEMWLHHYSLEMYQKMQSPHAKLEVLHYRLTVSSALHSPAQPSLQALHAYQESFTPTEEHVLVVRLLLKHLHAFANSLKPDQASPSAHSHATSPLEEFKRAAVPRFVQQKLYVFLQHCFGHWPLDATFRAVLEMWLSYLQPWRYAPEKQAQGSDPQPRCVSEKWAPFIQENLLMYTKLFVSFLNRALRTDLVSPKNALMVFRVAKVFAQPNLAEMIQKGEQLFLEPELIIPHRQHRLFTVTTSFLSPWPPVVTDASFKVKSHVYSLEGQDCKYTPMFGPEIRTLVLRLAQLITQAKQTAKSISDQYVESPTGRSFLSWLTFGLTDTNSCYPANDLDEIGQDSIRKTDEYLEKALEYLRQIFRLSEAQLAQLTLALGSARDENGKQQLPDCIVGEEGLILTPLGRYQIINGLRRFEIEYQGDLELQPIRSYEITSLVRALFRLSSAINRRFAGQMAALCSRNDFLGSFCRYHLTEPALSNRHLLSPVGRRQVTNPARGPRLSLRFLGSYRTLLLLLMAFFVASLFCIGPLSCSLLLVLGYVLYAIAMTLLTERGKLHQL
Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide . It has a relevant role in the homeostasis of membrane sphingolipids, thereby influencing membrane integrity, and endoplasmic reticulum organization and function. May sensitize cells to DNA damage-induced apoptosis. In skeletal muscle, mediates TNF-stimulated oxidant production .
Q6ZPR5
B3EP65
RS7_CHLPB
30S ribosomal protein S7
Chlorobium
MAKKVVGGGVKPDLRFSDESVARLINAVMLDGKKDVAAKIVYGAMDIIAGKMKDEEPLEVFRRALSNVAPLVEVRSKRVGGATYQIPMEVKASRRDALAFRWIKLYATRRGGRSMSEKLAAELMDAASEQGASVKKRDEVHRMADANKAFAHFRF
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.
B3EP65
P0A922
PA1_ECO57
Phosphatidylcholine 1-acylhydrolase
Escherichia
MRTLQGWLLPVFMLPMAVYAQEATVKEVHDAPAVRGSIIANMLQEHDNPFTLYPYDTNYLIYTQTSDLNKEAIASYDWAENARKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVVGNTDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNWNTGYGGAELGLSYPITKHVRLYTQVYSGYGESLIDYNFNQTRVGVGVMLNDLF
Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities.
P0A922
B7M5B2
HDFR_ECO8A
H-NS-dependent flhDC regulator
Escherichia
MDTELLKTFLEVSRTRHFGRAAESLYLTQSAVSFRIRQLENQLGVNLFTRHRNNIRLTAAGEKLLPYAETLMSTWQAARKEVAHTSRHNEFSIGASASLWECMLNQWLGRLYQNQDAHTGLQFEARIAQRQSLVKQLHERQLDLLITTEAPKMDEFSSQLLGYFTLALYTSAPSKLKGDLNYLRLEWGPDFQQHEAGLIGADEVPILTTSSAELAQQQIAMLNGCTWLPVSWARKKGGLHTVVDSTTLSRPLYAIWLQNSDKNTLIRDLLKINVLDEVY
Negatively regulates the transcription of the flagellar master operon flhDC by binding to the upstream region of the operon.
B7M5B2
A6L2G2
FOLD_PHOV8
Methenyltetrahydrofolate cyclohydrolase
Phocaeicola
MQLIDGKAISELVKQEIAAEVAGIVAKGGKRPHLAAILVGHDGGSETYVAAKVKACEVCGFKSSLIRYEADVTEEELLAKVRELNEDADVDGFIVQLPLPKHISEQKVIETIDYRKDVDGFHPINVGRMSIGLPCYVSATPNGILELLKRYHIETQGKKCVVLGRSNIVGKPMASLMMQKAYPGDATVTVCHSRSKDLVKECQEADIIIAALGQPNFVKAEMVKEGAVVIDVGTTRVPDATKKSGFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAIYK
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
A6L2G2
A7X5F4
RL16_STAA1
50S ribosomal protein L16
Staphylococcus
MLLPKRVKYRRQHRPKTTGRSKGGNYVTFGEFGLQATTTSWITSRQIESARIAMTRYMKRGGKVWIKIFPHTPYTKKPLEVRMGAGKGAVEGWIAVVKPGRILFEVAGVSEEVAREALRLASHKLPVKTKFVKREELGGETNES
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
A7X5F4
B2UMU5
GPMI_AKKM8
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Akkermansia
MSSKKPVVLVIRDGWGRNPLGPDVAKEYGDATVLADTPFTDYLLANYPHSLLGASGEDVGLPDGQMGNSEVGHLNLGAGRVVFQDLCRVDNAIKDGSMGENAVLKTAFSQAASSRLHLLGLVSDGGVHSHINHLIGIVKYAYEAGVRDICIHAITDGRDCSPTSGVGFIRQLEEAVRPYGAKIATVVGRFYAMDRDKRWDRNKLAWDAIVLGRGEQCSCSPAEYVEQCYAKGETDEFLKPGIFAYGNEQRVRDNDVVFFFNFRADRARQMSDAFLYPEFDGFDREVTPKVHYVTLTEYDAKYPSPIVFEQEQLNNIFGQIVSEAGKTQLRIAETEKYAHVTFFFNGGVETQFPGEDRILVPSPREVATYDLKPQMSAAEVADKFVDAVNKYDVVIMNFANGDMVGHTGFVEAGIAACEAVDSALEKCVKKVLELGGKLLITADHGNAEHMRNEDGSPNTAHTTNLVDLIYVADDKDQVTLSDGILADVAPTLLSLMGLKQPAEMSGHSLVTPGK
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
B2UMU5
Q674X7
KAZRN_HUMAN
Kazrin
Homo
MMEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQLGAQVLLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQAVRVSPCHSRQPSVISDASAAEGDRSSTPSDINSPRHRTHSLCNGDSPGPVQKNLHNPIVQSLEDLEDQKRKKKKEKMGFGSISRVFARGKQRKSLDPGLFDDSDSQCSPTRQSLSLSEGEEQMDRLQQVELVRTTPMSHWKAGTVQAWLEVVMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIEDYRDAEAGRSLSKAAELDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLYQVNFSREALQERRARCETQNIDPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSAVFHPANSTGIREAERFGTPPGRASSVTRAGKEENSSGLKYKAGRLPLGKIGRGFSSKDPDFHDDYGSLQNEDCGDDDPQSRLEQCRLEGYNSLEVTNV
Component of the cornified envelope of keratinocytes. May be involved in the interplay between adherens junctions and desmosomes. The function in the nucleus is not known.
Q674X7
Q8TYG6
KHSE_METKA
Homoserine kinase
Methanopyrus
MTPLSTVVRAPATIANVGPGFDVFGLAVDGFHDVVEAHEADGVRIVTEDPIPTDPERNTAGRVALRMVEEFDLPGVSLEIRKGVPMGGLGSSAASAVAAAVAIDREFELGLEESELLRFAAEGERAAAGEPHYDNVAPCLLGGFVIWRFEREYVRLEVPGDLRFVTVTPTGVRVTTEEARKALRERPPSLDDVVNNLSAVALMVHALHEEDAETFARMVGWDRISEPVRKRFVPRYRELRETAYGTGALGFAISGAGPTVFAVCWREDAEDVRTALEDVLDGKCVSAVHRVSDGAEVA
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Q8TYG6
Q3A4A3
TRUB_SYNC1
tRNA-uridine isomerase
Syntrophotalea
MNGILIVDKPQGMTSHAVVGRIRRLFGLRKVGHAGTLDPLATGVLVVALGQATRILQFLMQENKVYRASLVLGKTTDTQDSEGQIVATSDPGHIDAQSVADVCHSMVGSYDQMPPMYSALKKDGVPLYKLARQGVEVSRKPRRITIFDLQLLAVEPPNITFDVHCSKGTYVRTICHDIGVKLGCGAHLTALRRLRSAPFDVKEAVTLEAIELMAPEDRPELLLSIAEALREYPSLNVCPEGIKRLGYGIPPTADMIADTIDFEEGTQVLLVGPGGALAMATYVPSRARESRGDFELLRVFNDGGSS
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Q3A4A3
Q9UHG2
PCS1N_HUMAN
SAAS CT(25-40)
Homo
MAGSPLLWGPRAGGVGLLVLLLLGLFRPPPALCARPVKEPRGLSAASPPLAETGAPRRFRRSVPRGEAAGAVQELARALAHLLEAERQERARAEAQEAEDQQARVLAQLLRVWGAPRNSDPALGLDDDPDAPAAQLARALLRARLDPAALAAQLVPAPVPAAALRPRPPVYDDGPAGPDAEEAGDETPDVDPELLRYLLGRILAGSADSEGVAAPRRLRRAADHDVGSELPPEGVLGALLRVKRLETPAPQVPARRLLPP
Endogenous ligand for GPR171. Neuropeptide involved in the regulation of feeding.
Q9UHG2
C5CBV4
TATA_MICLC
Sec-independent protein translocase protein TatA
Micrococcus
MAGLQGWQLVIIILLAILLFAAPKLPAMARNLGQSMRIFSSEVKQMRTEGKDAKDERSGTGSTAADEPVEGRVVDRDETDPRDQR
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
C5CBV4
B8E4K7
LEUD_SHEB2
Isopropylmalate isomerase
Shewanella
MQPFTTHTGLAVMIDSTNIDTDQIIPKQFLSKVTRDGFGVHLFHDWRYLDDAGDQPNPEFSLNQSRYKGASILLAQENFGCGSSREHAPWALVDFGLRAIIAPSFADIFYGNSINNGLLPVALTHAQVRQLMDEVAAEAGAQITVDLTSCKVISPSGAEFSFTLAESARHKLLNGLDAIGLTLSHAAQISQYETQIQGWRR
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
B8E4K7
Q834W6
HYEP_ENTFA
Hydrophobic dipeptide epimerase
Enterococcus
MKIKQVHVRASKIKLKETFTIALGTIESADSAIVEIETEEGLVGYGEGGPGIFITGETLAGTLETIELFGQAIIGLNPFNIEKIHEVMDKISAFAPAAKAAIDIACYDLMGQKAQLPLYQLLGGYDNQVITDITLGIDEPNVMAQKAVEKVKLGFDTLKIKVGTGIEADIARVKAIREAVGFDIKLRLDANQAWTPKDAVKAIQALADYQIELVEQPVKRRDLEGLKYVTSQVNTTIMADESCFDAQDALELVKKGTVDVINIKLMKCGGIHEALKINQICETAGIECMIGCMAEETTIGITAAAHLAAAQKNITRADLDATFGLETAPVTGGVSLEAKPLLELGEAAGLGISH
Catalyzes the epimerization of L-Ile-L-Tyr to L-Ile-D-Tyr (in vitro). Catalyzes the epimerization of dipeptides, with a preference for substrates with a hydrophobic or basic amino acid in the first position, followed by an aromatic residue in the second position. Has epimerase activity with L-Ile-L-Tyr, L-Val-L-Tyr and L-Arg-L-Tyr (in vitro).
Q834W6
Q8Y637
Y1863_LISMO
DegV domain-containing protein lmo1863
Listeria
MRKIKIITDSTAGLTLEEAAKWNIDVLYLTVEIDGKVYNPKTDITPEEFMVRMAETKELPKSSQPAIGSFVEAYEKYTAEGYEILSIHLTEKLSGTVNAARQAADMVEGNITVVDCDYTARGQAFQVLKAAEMAQSGDYSVEEIHAKINDIRDKTKLYIVVVTLDNLIKGGRVGRMQGFLGSLLNIKLIAKLTDGQLEEETKVRSNKKVLQYCLNLIKDEPKKIQHLDVVHANGLNLADDFIAESKEITGLTEIPLFFADPVISTHAGTGAFAFMYYTD
May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
Q8Y637
Q99956
DUS9_HUMAN
Mitogen-activated protein kinase phosphatase 4
Homo
MEGLGRSCLWLRRELSPPRPRLLLLDCRSRELYESARIGGALSVALPALLLRRLRRGSLSVRALLPGPPLQPPPPAPVLLYDQGGGRRRRGEAEAEAEEWEAESVLGTLLQKLREEGYLAYYLQGGFSRFQAECPHLCETSLAGRAGSSMAPVPGPVPVVGLGSLCLGSDCSDAESEADRDSMSCGLDSEGATPPPVGLRASFPVQILPNLYLGSARDSANLESLAKLGIRYILNVTPNLPNFFEKNGDFHYKQIPISDHWSQNLSRFFPEAIEFIDEALSQNCGVLVHCLAGVSRSVTVTVAYLMQKLHLSLNDAYDLVKRKKSNISPNFNFMGQLLDFERSLRLEERHSQEQGSGGQASAASNPPSFFTTPTSDGAFELAPT
Inactivates MAP kinases. Has a specificity for the ERK family.
Q99956
Q3YQU4
LGT_EHRCJ
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Ehrlichia
MIIDQVAFRIGPLQIRWYSLSYIFGMIFAYWYIKKIDKYQVFNKESYESVISWWVISVILGGRIGYILFYNLDFYIHFPIEMLKLWNGGMSFHGALVGVMIGMYIFCRKNKIDVLAAFDLGACAVPVGIFFGRIANFINGELYGKVTDIKIGMIFPASGDLLYRHPSQLYEAFGEGFLLFIITNSLFFFTKIKTSKGMLSSVFCIWYGVIRFFIEFVREPDVQIGYIIFDQITMGQLLSIFMIIMGFYFIKLAKVQDKFSI
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.
Q3YQU4
B7N8L3
BETA_ECOLU
Betaine aldehyde dehydrogenase
Escherichia
MQFDYIIIGAGSAGNVLATRLTEDPNTTVLLLEAGGPDYRFDFRTQMPAALAFPLQGKRYNWAYETEPEPFMNNRRMECGRGKGLGGSSLINGMCYIRGNALDLDNWAQEPGLENWSYLDCLPYYRKAETRDVGENDYHGGDGPVSVTTSKPGVNPLFEAMIEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPHGRRASTARGYLDQAKSRPNLTIRTHAMTDHIIFDGKRAVGVEWLEGDSTIPTRATANKEVLLCAGAIASPQILQRSGVGSAELLAEFDIPLVHDLPGVGENLQDHLEMYLQYECKEPVSLYPALQWWNQPKIGAEWLFGGTGVGASNHFEAGGFIRSREEFAWPNIQYHFLPVAINYNGSNAVKEHGFQCHVGSMRSPSRGHVRIKSRDPHQHPAILFNYMSHEQDWQEFRDAIRITREIMHQPALDQYRGREISPGVECQTDEQLDEFVRNHAETAFHPCGTCKMGYDEMAVVDGEGRVHGLEGLRVVDASIMPQIITGNLNATTIMIGEKMADMIRGKDALPRSTAGYYVANGRPVRAKK
Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate.
B7N8L3
Q9CAP8
LACS9_ARATH
Long chain acyl-CoA synthetase 9, chloroplastic
Arabidopsis
MIPYAAGVIVPLALTFLVQKSKKEKKRGVVVDVGGEPGYAIRNHRFTEPVSSHWEHISTLPELFEISCNAHSDRVFLGTRKLISREIETSEDGKTFEKLHLGDYEWLTFGKTLEAVCDFASGLVQIGHKTEERVAIFADTREEWFISLQGCFRRNVTVVTIYSSLGEEALCHSLNETEVTTVICGSKELKKLMDISQQLETVKRVICMDDEFPSDVNSNWMATSFTDVQKLGRENPVDPNFPLSADVAVIMYTSGSTGLPKGVMMTHGNVLATVSAVMTIVPDLGKRDIYMAYLPLAHILELAAESVMATIGSAIGYGSPLTLTDTSNKIKKGTKGDVTALKPTIMTAVPAILDRVRDGVRKKVDAKGGLSKKLFDFAYARRLSAINGSWFGAWGLEKLLWDVLVFRKIRAVLGGQIRYLLSGGAPLSGDTQRFINICVGAPIGQGYGLTETCAGGTFSEFEDTSVGRVGAPLPCSFVKLVDWAEGGYLTSDKPMPRGEIVIGGSNITLGYFKNEEKTKEVYKVDEKGMRWFYTGDIGRFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSISPYVENIMVHADSFYSYCVALVVASQHTVEGWASKQGIDFANFEELCTKEQAVKEVYASLVKAAKQSRLEKFEIPAKIKLLASPWTPESGLVTAALKLKRDVIRREFSEDLTKLYA
Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate and linoleate.
Q9CAP8
Q4K7D7
RUVC_PSEF5
Holliday junction resolvase RuvC
Pseudomonas
MTLILGIDPGSRITGYGVVRDTGRGCVYVASGCIRTGAGELPDRLQIVYRGVREVIQTYGPVTMGIEKVFMARNADSALKLGQARGAAIVAGAEEGLEIAEYTATQVKQAVAGTGGANKEQVQMMVMHLLKLTTKPQIDASDALAIAICHAHTRSSLLPHGLGTARSRGGRLRL
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
Q4K7D7
B7GGE9
RNC_ANOFW
Ribonuclease III
Anoxybacillus
MSKQRPYVKFKQFQEQTGIFFRNEKLLIQAFTHSSYVNEHRKRLHEDNERLEFLGDAVLELTVSQYLFEQFPQMSEGELTKMRAAIVCEPSLVTFAHALSFGDLVLLGKGEELTGGRMRPSLLADVFEAFIGALYLDQGIEAVVQFLGKTIFPKIREGAFSHVMDYKSQLQEFVQRDGSGVLEYKILQERGPAHNKEFVSRVSLNGEELGVGVGRSKKEAEQRAAQMALAKLKQLQQG
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.
B7GGE9
C1CJ39
IF2_STRZP
Translation initiation factor IF-2
Streptococcus
MSKKRLYEIAKELGKESKEVVARAKELGLDVKSHSSSVEEAVAAKIAASFKPAAAPKVEAKPAAPKVSAEKKAEKSEPAKPAVAKEEAKPAEPVAPKTEKVAAKPQSRNFKAEREARAKEQAERRKQNKGNNRDQQQNGNRQKNDGRNGGKQGQSNRDNRRFNDQAKKQQGQQKRRNERRQQEDKRSNQVAPRIDFKARAAALKAEQNAEYARSSEERFKQYQAAKEALAQANKRKEPEEIFEEAAKLAEQAQQVQAVVEVVPEKKEPAVDTRRKKQARPDKNRDDYDHEEDGPRKQQKNRSSQNQVRNQKNSNWNNNKKNKKGNNKNNRNQTPKPVTERKFHELPTEFEYTDGMTVAEIAKRIKREPAEIVKKLFMMGVMATQNQSLDGETIELLMVDYGIEAKQKVEVDNADIERFFVEDGYLNEDELVERPPVVTIMGHVDHGKTTLLDTLRNSRVATGEAGGITQHIGAYQIVENGKKITFLDTPGHAAFTSMRARGASVTDITILVVAADDGVMPQTIEAINHSKAANVPIIVAINKIDKPGANPERVIGELAEHGVMSTAWGGDSEFVEISAKFNQNIEELLETVLLVAEIQELKADPTVRAIGTVIEARLDKGKGAVATLLVQQGTLNVQDPIVVGNTFGRVRAMTNDLGRRVKVAGPSTPVSITGLNEAPMAGDHFAVYEDEKSARAAGEERAKRALMKQRQATQRVSLENLFDTLKAGELKSVNVIIKADVQGSVEALSASLQKIDVEGVKVTIVHSAVGAINESDVTLAEASNAFIVGFNVRPTPQARQQAEADDVEIRLHSIIYKVIEEMEEAMKGMLDPEFEEKVIGEAVIRETFKVSKVGTIGGFMVINGKVARDSKVRVIRDGVVIYDGELASLKHYKDDVKEVTNGREGGLMIDCYNDIKMDDVIEAYVMEEIKR
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.
C1CJ39
B3R002
RL24_PHYMT
50S ribosomal protein L24
16SrX (Apple proliferation group)
MHIKLGDKVAIIAGKNRFVTDENGKKIIKTGKILKIFHKQQKVLVEGINIVFKHKAPLKDEDKGNIIKQEAPIHISNVALIDSLKNVPTRVGYRIENNKKVRYFKKSGTIIEDLN
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
B3R002
P74516
TRML_SYNY3
tRNA (cytidine/uridine-2'-O-)-methyltransferase
unclassified Synechocystis
MVKLVLVNPQIPPNTGNIARTCAATGTELHLVGPLGFELGDRYLKRAGLDYWPYVDLHYHNSCEEFITHWRGQGGNLLGFSVTGTVNFWDYTYQSTDWLMMGSETDGLPQMMRDLSTQLLCIPMPHSEVRSLNLASSAAIALFEAGRQLRSLG
Could methylate the ribose at the nucleotide 34 wobble position in tRNA.
P74516
C2M262
DPP7_CAPGI
Dipeptidyl-peptidase 7
Capnocytophaga
MRKLIFSLVTSFFLLLPSVIRADEGMWFLMFIKRLNERDMQKKGLQLTAEEIYSINNNSLKNAIVQFNGGCTASIISPDGLVITNHHCGYGAIAGLSTPEHNYLKDGYWAKDRSQELPPKSLYVRFFVRMDNVTDRMLSVVNSSMSEKERQDALNREMEKIQKENSEGGKYVVSVRPFFQGNEYYYFVYQDFKDVRFVGTPPENVGKFGGDTDNWEWPRHTGDFSVFRVYTDKDGNPAPYSPNNIPMKAKKYLNVTLKGVQENDFAMILGYPGRTNRWVSSHWVDQQVKYGYPAWVEASKTAMDAMKAHMDKDKAVRLKYASRYASLANYWKNRQGMIDALTAHKTADLKRAAEKKFAVWANKPENKAEYGNVLSDLATYFEKTNQEAANHNYLLLFFRASRIVPQANGYVKQLNTYLNSSSDQEKQQIRERIAKELDAYYSESYLPAEIDLFADNLKLYADKATDIPQEIAQIKSQYNGDFRKFAAEVFARSIFTTKENFENFMNNPSSDALQSDPIAQIARVMIDKYYNSQSEALKDGYEKAFRKYVKGMRDSKVSLILYPDANSTLRLTYGSVKSLPKDKRNHDVKRNYYTTFKTMLEKYKPGDAEFDMPKKFVEMYEKKDFGRYLDKDGTMHVCFLTNNDITGGNSGSPVMNGKGELIGLAFDGNIEAMAGDVIFDKKLQRTIVVDIRYVLWCIDTFGGAKHIVDEMTIIQ
Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Most potently cleaves the synthetic substrate Met-Leu-methylcoumaryl-7-amide (Met-Leu-MCA), followed by Lys-Ala-, Leu-Arg- > Leu-Asp-, Leu-Glu-, >Leu-Lys, and >Val-Arg-MCA, while this enzyme does not hydrolyze Gly-Arg-, Gly-Gly-, Lys-Lys-, or Gly-Pro-MCA.
C2M262
A1RRU0
DPCKG_PYRIL
Dephospho-coenzyme A kinase
Pyrobaculum
MTCFKLCCRRDLFAFPYPVAIWKEPPRSIEVVRDLVESYGIEQIYTVGDIVTTNFLKYSLAPTSAAVDGKTRRGLKIDKPTFFRKTIEVYNPPGYITEEAWIAVEEAVRDNVMIKVNGEEDMLSLAFIKLAPPHSVVVYGHYMGALIAIPVDWYRDAICKLFEYLEKC
Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
A1RRU0
Q28221
HBG1_CEBAL
Hemoglobin gamma-1 chain
Cebus
MSNFTAEDKAAITSLWAKVNVEDAGGETLGRLLVVYPWTQRFFDSFGSLSSPSAIMGNPKVKAHGAKVLTSLGEAIKNLDDLKGTFGQLSELHCDKLHVDPENFRLLGNVLVTVLAVHHGKEFTPEVQASWQKMVAGVASALGSRYH
Gamma chains make up the fetal hemoglobin F, in combination with alpha chains.
Q28221
A0JV20
ARGC_ARTS2
N-acetyl-glutamate semialdehyde dehydrogenase
Arthrobacter
MTISVAVSGASGYAGGEVLRLLAGHPDVTIGAITAHSNAGSRLGELQPHLHGLASRILEDTTVENLSGHDVVFLALPHGASADIAAQLPEGTVVIDAGADHRLEDPAAWEKFYGSAHAGTWPYGLPELPGQREKLKGANRIAVPGCYPTSALLALTPGFAGSLLQPDDVVIVAASGTSGAGKAAKVNLIGSEVMGSMSPYGVGGGHRHTPEIEQGLGNAAGEAVTVSFTPTLAPMSRGILTTATAKVKPGVTAAELRSAWEEAYDDEPFVHLLPEGQWPSTKSVQGSNHAVMQVAFDAHTGRVIVTCAIDNLTKGTAGGAVQSMNIALGLAETAGLNLQGVAP
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
A0JV20
P0A9D1
GLPX_SHIFL
null
Shigella
MRRELAIEFSRVTESAALAGYKWLGRGDKNTADGAAVNAMRIMLNQVNIDGTIVIGEGEIDEAPMLYIGEKVGTGRGDAVDIAVDPIEGTRMTAMGQANALAVLAVGDKGCFLNAPDMYMEKLIVGPGAKGTIDLNLPLADNLRNVAAALGKPLSELTVTILAKPRHDAVIAEMQQLGVRVFAIPDGDVAASILTCMPDSEVDVLYGIGGAPEGVVSAAVIRALDGDMNGRLLARHDVKGDNEENRRIGEQELARCKAMGIEAGKVLRLGDMARSDNVIFSATGITKGDLLEGISRKGNIATTETLLIRGKSRTIRRIQSIHYLDRKDPEMQVHIL
Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate.
P0A9D1
C0MCU1
NAGB_STRS7
Glucosamine-6-phosphate isomerase
Streptococcus
MKIIRVQDQLEGGKVAFSLLKESLAEGATTLGLATGSTPITFYQELVNSDLDCSALTSINLDEYVGLPVENDQSYDYFMRDQLFNAKPFKESFLPNGLADDLEAEVKRYDQVIAEHPIDFQILGIGRNGHIGFNEPGTPFAEKTHVVDLQASTIEANSRFFASIDDVPKQAISMGIASIMASKMIVLLAFGKEKAAAIKGMVSGPVTEALPASVLQQHDHVVVIVDEAAASELD
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
C0MCU1
Q5HN32
PUTP_STAEQ
Proline permease
Staphylococcus
MFTLGTALSNQIDANWQTYVMIIVYFIILLIIGFYGYRQATGNLSEFMLGGRSIGPYITALSAGASDMSGWMIMGLPGSVYSTGLSAIWITIGLTLGAYINYFVVAPRLRVYTEIAGDAITLPDFFKNRLDDKKNIIKIISGLIIVVFFTLYTHSGFVSGGKLFESAFGLNYHAGLLIVAIIVIFYTFFGGYLAVSITDFFQGVIMLIAMVMVPIVALLKLNGWDTFHDIAQMKPTNLDLFRGTTVLGIVSLFSWGLGYFGQPHIIVRFMSIKSHKLLPKARRLGISWMAVGLLGAIGVGLTGISFISERHIKLEDPETLFIVMSQILFHPLVGGFLLAAILAAIMSTISSQLLVTSSSLTEDFYKLIRGSDKASSHQKEFVLIGRLSVLLVAIVAITIAWHPNDTILNLVGNAWAGFGAAFSPLVLYSLYWKDLTRAGAISGMVAGAVVVIVWISWIKPLATINAFFGMYEIIPGFIVSVLITYIVSKLTKKPDDYVIENLNKVKHVVKE
Catalyzes the sodium-dependent uptake of extracellular L-proline.
Q5HN32
Q7V9I5
SPEE_PROMA
Spermidine synthase
Prochlorococcus
MFENENPNGSWLDEYQNDVRYGLKGKKIIEEISNFQKITIFESNRYGKALLLDNCWMTAEYQEKQYHECIVHPALCGSKEINKVLIIGGGDGGSARECLKYQELKNLDLIEIDKRVVELSQQYLSVIGGNCWKDQRLNLKLTNGINWVKDAKDNSYDVIIIDGSDPKGPAKGLFNKDFFKDCHRILKPDGVLGAQTESPESFEDIHINTVKMIKEVFKYADPLYGYVPIYPSGIWSWTFASIKKPRHLYPIISRANTISKTCQVWSPRWQRGGFDAIPANIERKLQQ
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Q7V9I5
P50195
T2E8_ECOLX
Type-2 restriction enzyme Eco47II
Escherichia
MSLLEYISDEDLFNEVETLLTKAKKKKDAAEKTFTSNVIDPFGALFEAPGFSSHEEWRNSELARQQQKTIQNHVGTFHQKILGHVEGWRDMGIGGIVDLLNEERRIIAEVKNKYSTVTGGDLADKYKGLDELVSPKHSRFKDYCAYFVNIIPRKPTRYNSPFTPSNKGSGTLCPSNPNIRIIDGASFYELVTGRPDALQELHSALPHAIEYILSERLGQQGFSIPDKDSFIKYFGLAYG
A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GGNCC-3'; the cleavage site is unknown.
P50195
A4XQV2
RS20_PSEMY
30S ribosomal protein S20
Pseudomonas
MANSPSAKKRAKQAEKRRSHNASLRSMVRTYIKNVVKAIAAKDLELAKTAYTAAVPVIDRMADKGIIHKNKAARHKSRLNAHIKALGEAAAA
Binds directly to 16S ribosomal RNA.
A4XQV2
P26509
PGLR2_PECPM
Endo-polygalacturonase
Pectobacterium
MEYQSGKRVLSLSLGLIGLFSASAWASDSRTVSEPKTPSSCTTLKADSSTATSTIQKALNNCDQGKAVRLSAGSTSVFLSGPLSLPSGVSLLIDKGVTLRAVNNAKSFENAPSSCGVVDKNGKGCDAFITAVSTTNSGIYGPGTIDGQGGVKLQDKKVSWWELAADAKVKKLKQNTPRLIQINKSKNFTLYNVSLINSPNFHVVFSDGDGFTAWKTTIKTPSTARNTDGIDPMSSKNITIAYSNIATGDDNVAIKAYKGRAETRNISILHNDFGTGHGMSIGSETMGVYNVTVDDLKMNGTTNGLRIKSDKSAAGVVNGVRYSNVVMKNVAKPIVIDTVYEKKEGSNVPDWSDITFKDVTSETKGVVVLNGENAKKPIEVTMKNVKLTSDSTWQIKNVNVKK
Involved in maceration and soft-rotting of plant tissue.
P26509
Q54SL6
GACQ_DICDI
GTPase activating factor for raC protein Q
Dictyostelium
MKFGKKKEKENLENIEKDKDRDKEKEIKEKEKKDKKSKDKKKNQEIEKDNNINNNNNNNNVKKVFGGSLPFLFEEELPTILVQTIDYLQLFGLQTPGIFRENGSLASIQSYRSLYDNDKPVNFPPHEAHVVASLLKAYLRELKVPLCTFEHYDMFIACESIADEKVKVELLKKVIAHLPPFNRKVMKYIFSFLQKVVENSNVNKMTPDALSIVFLPTILRPQANTDLEILQFTVEDSKSTKTLMSSILLNYDEIFEDPNLFQPRTRQARAQTDFVSPPSSQNSTSSSSYLSSKNPISPRSPIGSSPNFTTASILSALPPPPISPILSSNTTNTTLPPPIITSSIDDNNEPSLSPRIITTTTTTTPSPQPTTTTTTHRLPPSNPIPPTPTSNSQSQLYPNLPPPSSDPIIKSTTTPTLNSQSQSQLYPNLPPPLPDKNKCKLLPITPITTNESNTLQPTTPTSTNIPPLSIPPQIGGNSDSNPISPTKNQSQLPILPPKPPSLTLPPKPIPKIPTILEYENNVRQRSNTTMV
Rho GTPase-activating protein involved in the signal transduction pathway.
Q54SL6
Q4UL18
RSMH_RICFE
rRNA (cytosine-N(4)-)-methyltransferase RsmH
spotted fever group
MPQSHIPVMLNEMLANLAPKDGEFYLDCTFGAGGYSKAILESCDCYITALDRDPNVIKKAEEIKQNYGERFDFIETNFADSFAKLKEKKFDGVVLDLGVSSMQLDIADRGFSFLHDGPLDMRMSGQGLSAEEFVNIAEEKELADVIYKYGDESFSRRIAKRIVEYRKTTRIDSTGKLAQIVRSSIGFRKGKIDPATKTFQAIRIYINNELGELERFLANVKNILKKDGRLVVVSFHSLEDRIVKNFFKENSEKPVARSKYAKDDIAIDPDKWLKIITNKALATSDKEVGLNIRARSAKLRAAKKIL
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Q4UL18
Q601S2
ENO_MESH2
2-phosphoglycerate dehydratase
Mesomycoplasma
MSKITKVFAREILDSRGNPTIQVDVYTLAGGFGSAIVPSGASTGSREALELRDTNTKYADNWYGQKGVMTAVDNVNNIIAPEIIGLCCKNQRLIDQKMIELDGTPNKEKLGANAILGVSLAVAKAAANELRMPLFRYLGGTNPTLMPVPMLNVINGGEHASNTLDFQEFMIMPLGFRTFKEALQAANKVFHNLAKLLKKSGFETQVGDEGGFAPNFNSHEQALDFLVDAIKESGFNPGFKGENAVAIAIDAAASEFYNGQKYVFKKLKAASLSKNQADLDEKFEFSSEELLNYYGQLLAKYPIISIEDGFAESDWQGFIAFNQKYGNNHQIVGDDLTVTNVEILKKAINLKAINSILIKLNQIGTLSETLDAIHLAQKSGMTAVISHRSGESEDTTIADLAVAVSSGQIKTGSLSRTDRIAKYNRLLVIEEYLNSYAKADYIGREVFYNLKK
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Q601S2
P40971
LYS14_YEAST
Lysine biosynthesis regulatory protein LYS14
Saccharomyces
MFESVNLDENSPEDRELAKVLSPPGSYLSPASLDSGSSFTNSGTSTSCFEPKNNLPSLSFLNARAGSLGGIFNHKQMTSPSNSNIGGENVESTTSSNDGSNENAGHPTTSEQDQNADHPTISQADDNGHSSLTPNPAVTSTVTDKKGNTVKRKYSRNGCSECKRRRMKCDETKPTCWQCARLNRQCVYVLNPKNKKRRTSNAQRVKEFRKHSTSLDNDHNNARKRQHSSCKAEKKKKVRQNLSEDTTDPKPITDNGKNVPLDEIESLEIPNLDLTTTMNGYDVNLLMQNLNDMVNMKLHDSYLLNEELKGLDLPDLDIPELLPASNVNSSVPISFLVNNVITFNTKLSSFKLGGIHDKYLKIFYYDCLDSIAPFFQNQGNPLRDILLSFAKNEAYLLSSILATGASIAYRKSNNLEDERNYCAYLSHCLSLLGEQFKNESNVLNRIEPIILTVIMLAWDCIYSMNSQWRSHLKGVTDLFKKINAGNSSKVLNVAKCWFKVMETFASISTVFGGSLIDNNDLDAIFDPYDYQYVDSLKFLNIMTPLNEFNLLRGHKEDFDLVIKEVFKSLNTIRSTEKNYFSKEEGLFTKKLDYLLLSSQTSSEKSKDQISYFNTQKILVEIDKQLDYEFIDKSGIIPSDNQSHPRISNIHDNAIDMVTLKNGEEVAISWYDISHQTQVLSFLLIVLLKLLGMPKESSTIQQVVKKIMSFFKFLDSDSPPQNSRTCYSNFAVLIAGLNAMDEETRAIVKRYYKINGGKFQKLTEHNLNRLEKVWYGKNQNYRLEEQDVLTW
Activates the transcription of lysine biosynthesis genes. This activation is dependent on the inducer alpha-aminoadipate semialdehyde and repressed by lysine.
P40971
Q7U3T7
RL1_PARMW
50S ribosomal protein L1
Parasynechococcus marenigrum
MPKLSKRLAGLASKIEDRVYEPLEAIALVKDNATAKFDETMEAHVRLGIDPKYTDQQLRTTVALPNGTGQTVRIAVVTRGEKVAEAKAAGAELAGDEDLVETIAKGEMEFDLLIATPDMMPKVAKLGRVLGPRGLMPNPKAGTVTIDLAGAIQEFKAGKLEFRADRTGIVHVRFGKASFTAEALLQNLKTLQETIDRNKPSGAKGRYWKSLYVTSTMGPSVEVDFSALQDIEQGS
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
Q7U3T7
C0RGM7
RNPH_BRUMB
tRNA nucleotidyltransferase
Brucella
MRPSKRAADEMRTISFERGVSKHAEGSCLVKFGDTHVLCTASLEEKVPGWMRNTGKGWVTAEYGMLPRSTGERMRREAAAGKQGGRTQEIQRLIGRSLRAVVDMQALGEMQITVDCDVIQADGGTRTAAITGGWVALHECLRWMEARQMVRVEKVLKDHVAAISCGIYEGVPVLDLDYAEDSVAETDSNFVMTGKGGIVEIQGTAEGVPFSEEEFGALMKLARSGIDRLVSLQKMAVA
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.
C0RGM7
B2VGS4
RIMP_ERWT9
Ribosome maturation factor RimP
Erwinia
MGLSTLEQKLTELISAPVEALGYELVGIEFVRGRTSTLRIYIDSEDGINVDDCADVSHQVSAVMDVEDPITVAYNLEVSSPGLDRPMFTAEHYARFTGEEVSLVLRMAVQNRRKWQGIIKSVEGEMITVAVEGNDEVFALSNIQKANLVPHF
Required for maturation of 30S ribosomal subunits.
B2VGS4
A4IFD0
KAD5_BOVIN
ATP-AMP transphosphorylase 5
Bos
MNTNEAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKELGGCDKVKWDTFVSQEKKTLPPLNGGQSRRSFLRNVMPENSNFPYRRYDRLPPIHQFSIESDTDLSETAELIEEYEVFDPTRPRPKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKWSLIAKIITTGELAPQETTITEIKQKLMQMPDEVGIVIDGFPRDVAQALSFEDQICTPDLVVFLACTNQRLKERLLKRAEQQGRPDDNLKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDISMAVDSKLFPNKEAAAGSSDLDPSMMLDTGEVIDTGSDYEDQGDDQLNVFGEDTMGGFMEDLKKCKIIFMIGGPGSGKGTQCGKLAEKYGFTHLSTDELLQNELSSESGRSKLIRDIMERGELVPSGIILELLKEAMVASLSNTKGFLIDGYPREVKQGEEFGRRIGDPHLVICMDCSADTMTNRLLQRSRNSPQADDNTTTIAKRLETYYRASIPVVAYYETKTQLHKINAEGTPEEVFLQLCTAIDSIF
Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. Also displays broad nucleoside diphosphate kinase activity.
A4IFD0
Q0AQE4
PANB_MARMM
Ketopantoate hydroxymethyltransferase
Maricaulis
MSAQSKSPTKARRITAPDIRARKGGEPLVCLTAYDAPMARILDPHCDLLLVGDSVGMVVHGLDSTVGVTLDMMILHGQAVMRGARQALVAVDMPFGSYEQSPEQAFANAARVMAETGCQAIKIESGTYAADTIRFMAARSIPVIGHIGLRPQAALADGGFRAKGRTQAERQRVIDEALATAEAGAFAIVIEGVAEDLAREITETVDVPTIGIGASAACDGQILVTQDMLGVFDWTPKFVKRYDNMAERTDAAVAQFASDVRDRSFPSQREVYTMKRSDG
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Q0AQE4
P56668
KNX11_MAIZE
Homeobox protein knotted-1-like 11
Zea
ADRELKEMLLKKYSGCLSRLRSEFLKKRKKGKLPKDARSALMDWWNTHYRWPYPTEEDKVRLAAATGLDPKQINNWFINQRKRHWKPS
Probably binds to the DNA sequence 5'-TGAC-3'.
P56668
C1C6B0
RLMN_STRP7
tRNA m2A37 methyltransferase
Streptococcus
MKPSIHSLAHQTMQEWVLEQGEKKFRADQIWEWLYRKRVQSFEEMTNLSKDLIAKLNDQFVVNPLKQRIVQESADGTVKYLFELPDGMLIETVLMCQHYGLSVCVTTQVGCNIGCTFCASGLIKKQRDLNNGEIVAQIMLVQKYFDERGQDERVSHIVVMGIGEPFDNYNNVLNFFRTINDDKGMAIGARHITVSTSGLAHKIRDFADEGVQVNLAVSLHAPNNELRSSIMKINRAFPIEKLFAAIEYYIETTNRGVTFEYIMLNEVNDGVEQALELTELLKNIKKLSYVNLIPYNPVSEHDQYSRSPKERVLAFYDTLKKKGVNCVVRQEHGTDIDAACGQLRSNTMKRDRQKAVSAVNP
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
C1C6B0
A1YER7
HXD4_GORGO
Homeobox protein Hox-D4
Gorilla
MVMSSYMVNSKYVDPKFPPCEEYLQGGYLGEQGADYYGGGAQGADFQPPGLYPRPDFGEQPFGGSGPGPGSALPARGHGQEPGGPGGHYAAPGEPCPAPPAPPPAPLPGAPACSQSDPKQPPPGTALKQPAVVYPWMKKVHVNSVNPNYTGGEPKRSRTAYTRQQVLELEKEFHFNRYLTRRRRIEIAHTLCLSERQIKIWFQNRRMKWKKDHKLPNTKGRSSSSSSSSSCSSSVAPSQHLQPMAKDHHTDLTTL
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
A1YER7
A5W6U4
NADK_PSEP1
ATP-dependent NAD kinase
Pseudomonas
MEQFRNIGIIGRLGSSQVLDTIRRLKKFLLDRHLHVILEDTIAEVLPGHGLQTSTRKLLGEVCDLVIVVGGDGSLLGAARALARHNIPVLGINRGNLGFLTDIRPDELEQKVAEVLDGHYLVENRFLLQAEVRRHHEAIGQGDALNDVVLHPGKSTRMIEFEIYIDGQFVCSQKADGLIVATPTGSTAYALSAGGPIMHPKLDAIVIVPMYPHTLSGRPIVVDGNSELKIVVSKDLQIYPQVSCDGQNHFTCAPGDTITVSKKPQKLRLIHPLDHNYYEVCRTKLGWGSRLGSSDD
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
A5W6U4
Q8E9P9
FTSQ_SHEON
Cell division protein FtsQ
Shewanella
MSWSDKRRHWRARKSQVNWYLWSGIGFLSLVIGSFVFGGYLLHKFLNDASTLPIEAVAIKGERTYTTDKDIQIALQDLMQRSFFSADITLVQQALEALPWVYRASVRREWPAKLRVYLQEQQPAAHWNGTAWLNVHGEVFEAPSHPELEHLPHLSGPDDMGTEVLTAYAQVNSLLKINGFTLASLNLTPRHAWHATLGNGIVLDLGREDKMARIQRFITVYPLLAKQDKPIARVDLRYDTGLAVGWGDAQTREPIINDEKPR
Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Q8E9P9
A1WX31
DNAK_HALHL
Heat shock protein 70
Halorhodospira
MGKIIGIDLGTTNSCVAVMEGNKTRVIENAEGDRTTPSVVAFAEDGEVLTGAPAKRQSVTNPENTIHAVKRLIGRRFDEDVVQRDIKEMPYKIVKADNGDAWVEAQGKKMAPPEVSARTLQKMKSTAEDYLGEEVTEAVITVPAYFNDSQRQATKDAGKIAGLEVKRIINEPTAAALAYGLDKEGGDKKVAVYDLGGGTFDVSIIEIAEVDGEKQFEVLSTSGDTFLGGEDFDKRIIDYLIQEFKKDQGIDLAQDHLALQRLREAAEKAKVELSSSQQTEINLPYITADQSGPKHMAIKLTRAKLESLVEDLVERTIEPCKTALKDAGLAAGDIQDVILVGGQTRMPKVQEKVKEYFGQDPRKDVNPDEAVAVGAAIQAGVLGGDVKDVLLLDVTPLSLGIETLGGVMTKIIEKNTTIPTKGTQTFSTAEDNQTAVTVHVLQGEREMAKDNKSLGRFDLTDIPPSPRGVPQIEVAFDIDANGILNVSAKDKATGKETGIEIKASSGLTEDEIERMVKEAEENAEEDRRQRELVEARNQAENMIHSTRKSLSDLGEQVGDAEKQEIESAISELEQVKDGEDKDAIEQKTQELATKAGELAQKAYQQAGGGDEASADAGAGETASGEQKEDVVDADFEEVKDEDGNSRK
Acts as a chaperone.
A1WX31
O14121
NDH1_SCHPO
Probable NADH-ubiquinone oxidoreductase C3A11.07, mitochondrial
Schizosaccharomyces
MLFSRSILRGMPKAGIPKSPLALSASRNLRLANSVRFASDAASSPKSTTSKWKILKRTTLGLFATAVVLYGANVYRFRHPDPHQPLPDPSKKTLVVLGAGWGATSILRTIDTSLFNVIVVSPRNYFLFTSLLPSTATGSVHTRSIVQPIRYMLRHKSCYVKFYEAECTDVDADKKVIHIKKTTTDGVDLEQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIWDAQKIRARILHCLEQAQFKDLPAETRRRYVHTVVVGGGPTGMEFAGEMADFIEDDLKSWYPELADDFAVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTALKKVTAENIHVEVKNPDGSKQEEVIPYGLLVWAGGNRARPLTKKLMEGSEEQNNRRGLVVDEYLKLKGYKDIFALGDCTHTAYAPTAQVASQQGAYLGQLFNKLGSLNFEKPSEDRHIALGDEMDSSTLISLANEKHASTKVFLPFKYSHQGSLAYVGHEKAIADIEVPWFGKQLHASGALAFYFWRSVYLSELYSLRNRTNVTLDWIRVKLFGRDISSL
Catalyzes the oxidation of NADH.
O14121
B5RM48
RL5_BORDL
50S ribosomal protein L5
Borrelia
MSYIPELKRRYRDNIVKELVSEFQYKSIMQAPKIEKIVVSMGVGDAVKNKKLLDSAVMELSQITGQKAVKTKAKKAISGFKIRQGQEIGAKVTLRGNMMYEFLYKLVNLALPRVKDFRGINGNAFDGNGNCSFGIAEQIIFSEIDYDKIERISGLNVTIVTTALNDKEGKALLAKFGMPFSN
This is 1 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. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
B5RM48
Q9K8N1
PHNC3_HALH5
Phosphonates import ATP-binding protein PhnC 3
Halalkalibacterium (ex Joshi et al. 2022)
MIEFKNVSLVYPNGTQGLKDVNLKINEGEFVVIVGLSGAGKSTLIRSMNRLVTPTEGELLIDGENILPYSSRQLRKLRTKVGMIFQNYNLVKRSSVMKNVISGRLGHVGTFASLLNLYPKEDVALAYRSLQRVNIAEKVYQRADQLSGGQQQRVAIARVLTQQPKIILADEPVASLDPPTSHQVMTYLRKINKEDKITTIVNLHFIDMAMEYADRIIGMRAGEVVFDGPASDVSEETFEEIYGRKIREDDLVGGQDNE
Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
Q9K8N1
A0A0H2ZGW2
DPPA2_PSEAB
Di/tripeptide-binding protein 2
Pseudomonas
MRPRSALRYSLLLLAFAASAAIQAQPKTLAVCTEAAPEGFDPARYTSGYTFDASAHPLYNALAAFAPGSATVIPALAESWDVSADGLVYTFRLRQGVKFHSTDYFKPSREFNADDVLFSFQRMLDPQHPAHDLSPSGYPYADAMQLRDIIERIEKIDEHQVRFVLKHPEAPFLADLAMPFGSILSAEYAGQLIARGKGDELNSKPIGTGPFVFTRYRKDAQVRYAANPDYWKGKPAIDHLVLAITLDPNVRVQRLRRNECQIALTPKPEDVAALRQDPQLTVLEEAAMITSHAAINTRHEPFDDPRVRRAIAMGFNKSSYLKIVFGDQARPAIGPYPPMLLGYDDSIRDWPYDPERAKALLKEAGVAPDTPLNLYISTGSGPGGNPARVAQLIQSDLAAIGIRVNIHQFEWGEMVKRTKAGEHDMMLYSWIGDNGDPDNFLTHNLGCASVESGENRARWCDKGFDEAIRKARMSNDESQRVALYKEAQRIFHEQMPWLPLAHPLMFDAQRKNVSGYRMSPMSARDFSRVKLD
Part of the ABC transporter DppABCDF involved in the uptake of various di/tripeptides . Shows high flexibility on substrate recognition. Efficiently uses tripeptides .
A0A0H2ZGW2
Q4WB03
PSOE_ASPFU
Pseurotin biosynthesis protein E
Aspergillus subgen. Fumigati
MVFGTLYTFPGDQCRTIAIKAVAKANGLDLDIRETPRTPDHLSISKLGKVPAFQGADSFKLFECMAIALYITSQNEQTTLLGKDKKEYAEIIKWMSFFNTEIVILMTQQLLPQLGVIPYDRDQVEFFANMTQRSVDVVEEYLQDRTFLVGDQLSLADLFCAGNISLGFQFFYGKAWRQQNPNVSRWYEMVCHQPIYAAVTDKFQLLDEPKLTNNPPEKKPETVPKNGAAVAIEATQA
Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation . The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule . The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold . Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE . The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol . Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D .
Q4WB03
Q5BK30
DAW1_RAT
WD repeat-containing protein 69
Rattus
MKLKSLLLRYYPPGIMLEYEKGGELKTKSIDLLELSPSTDVNTLVGEIQKVEPLITASRTKQVRLLVQRLQEKLRQHCDHNFYLFKVLRAHILPLTNVALNKAGSCFITGSYDRTCKVWDTASGEELHTLEGHRNVVYAIAFNNPYGDKIATGSFDKTCKLWSAETGKCYHTFRGHTAEIVCLSFNPQSTVVATGSMDTTAKLWDIQSGEEVVTLTGHLAEIISLSFDTSGDRIITGSFDHTVVVWDASTGRKVHTLIGHCAEISSALFSWDCSLILTGSMDKTCMLWDATSGKCVATLTGHDDEILDSCFDYTGKLIATASADGTARVYNATTRKCITKLEGHEGEISKISFNPQGNRLLTGSSDKTARIWDVQTGQCLQVLEGHTDEIFSCAFNYKGNIVITGSKDNSCRIWR
May play a role in axonemal outer row dynein assembly.
Q5BK30
D4D8C1
PFF1_TRIVH
FXNA-related family protease 1
Trichophyton
MVSSRRGFNPIAFTPWPVTILSSLVYLALIIPIIVVHHLVPPAPKESPAGVDLEEAWHDLQHLTRQYHPYNSHSNDEVHQWLLKRIHAISATSARSESQSGPEVFVFDDNQTNLTFSSAGVAATAITGVYFESRNIVVYIRGTEDEPGEWWKSPDGEPSGKGGVLVNAHYDSVSTGYGATDNGVGVITTLQLLKYFTTPGHYPRKGLVLLFNNGEEDFLNGAYAYSQHPMSKFTHTFLNLEGAGAGGRAVLFRSTDTEVTRFYGKSEHPFGTVLARDAFKLKFIRSETDYHVFDGVFGMRGLDVAFMEPRSRYHTDQDDARHTSIDSVWHMLSAAITTTEGLVSYTGDAFDGDSGDGGKLNNGIGTLGVWFDFFGSSFAVFQLNTLFGHSVALLVVAPLLLIITSVALFAVDKMYMFSMYTYISESGGQVSLYGLRGMFRFPLILGISTALTIALAFLIMKVNPFIIYSSPYAVWSMMLSTCMFFAWFISCVADFARPSALHRAYAFSWMFGIMWVFLVIATVYQKQHGIASSYFIVFYFAGVAVATWISYLELFGLPKTQDYARRQGRLSDRTPSSDSHFLAPSADELPSSSSAAGRDFNPEDVEDEEPTESTSLLRGQQRTTFANYASARGSQESNISNQGNNSLHPKDHRLEQKWSIYLMSSAWILQFLLVAPIVIILLGQLGLFLTSATYQIGADGGSQLVIYIGIAVLSVLILLPLFPFIHRFTYHIPTFLLFILIGTLVYNLTAFPFSHSNRLKLAFVQEMDLATGNNQASLVGVEPYIHDAVHAIPSVQDGKISCTSHGYGGRTKCSWPGLKPKVAEGPYKDWVSYNISQTKDDKITRFEVSGKNTRACKLLFDSPIADFHVQGSVVDKRIPHTGPKGVSEIRLWSRNWENTWTVDVEWTKKNSERTGKVMCLWSDDNDLHVIPELDLARKFAPWWVAITKLRDGLVEGSYSFEL
May be involved in vacuolar sorting and osmoregulation.
D4D8C1
P83063
RL10_BACCE
50S ribosomal protein L10
Bacillus cereus group
MSKVIETKQQVVTEIADKLRA
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
P83063
A1BHJ1
TPIS_CHLPD
Triose-phosphate isomerase
Chlorobium
MRKKIVVGNWKMNKTVTESLVLAAEVTAALGEGFTGCDVGIAPPFTALYEVGKLTGSRLALVAQNCHFEPDGAFTGEVSASMVREAGCSAVIAGHSERRHCFGETNAIVNRKVKHALSEGLQVIMCAGETLEQREGGVTGDVVTAQVREGLLGIDDISNIVIAYEPVWAIGTGKTATSEQAEEVHLLIRNTVSDLFGEEAAGRLRIQYGGSVKPSNAKELFSMPNIDGGLIGGASLNAADFVAIVKAAV
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
A1BHJ1
B8E7F1
HYPA_SHEB2
Hydrogenase maturation factor HypA
Shewanella
MHEYSIVSALIEQCEQHALANHAAKITRVDIKLGVMSGVEPSLLQTAFDTFKLDGICNAAQLNIQIQPLVILCQDCQSESVLSERTIVCPACQSYRTRVLDGEDMLLMQLEMEQEED
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
B8E7F1
Q0RPD5
NHAA1_FRAAA
Sodium/proton antiporter NhaA 1
Frankia
MLNPQTRRVRLFARGSWAETRRIAGILRDETISGGLLLAATVLALGWANSPWSGTYDSLLATDFGPAALHLDLSVQQWAADGLLAIFFFVAGLELKREFVAGDLRDPSRAVVPVAAAAGGVAVPAVLYSLLNLHSGALRGWAIPTATDIAFALSVLAVVGRCLPTALRTFLLTLAVVDDLLAIVIIAVAYTGELSVVPLVAAVVPLAAFTLLVQRRVRAWWLLLPLAVLTWALVHASGVHATVAGVLLAFAVPVLRSEGAGGPQAGPGLAEHFEHRWRPLSAAVAVPVFAFCSAGVTVGGLGGLGDALSDRAALGVVVGLVVGKAIGIFTTTWLVARFTGASLERGLAWVDVAGLALLGGVGFTVSLLIGELAFGPGSARDDHVKVGVLTASVTAALLATVVLRLRNRAYARIHELETADDDHEDGPDA
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Q0RPD5
O27731
HMT2_METTH
Archaeal histone A2
Methanothermobacter
MAELPIAPVGRIIKNAGAQRISDDAREALAKILEEKGEEIAKEAVKLAKHAGRKTVKASDIELAAKKL
Binds and compacts DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils.
O27731
Q8WUA7
TB22A_HUMAN
TBC1 domain family member 22A
Homo
MASDGARKQFWKRSNSKLPGSIQHVYGAQHPPFDPLLHGTLLRSTAKMPTTPVKAKRVSTFQEFESNTSDAWDAGEDDDELLAMAAESLNSEVVMETANRVLRNHSQRQGRPTLQEGPGLQQKPRPEAEPPSPPSGDLRLVKSVSESHTSCPAESASDAAPLQRSQSLPHSATVTLGGTSDPSTLSSSALSEREASRLDKFKQLLAGPNTDLEELRRLSWSGIPKPVRPMTWKLLSGYLPANVDRRPATLQRKQKEYFAFIEHYYDSRNDEVHQDTYRQIHIDIPRMSPEALILQPKVTEIFERILFIWAIRHPASGYVQGINDLVTPFFVVFICEYIEAEEVDTVDVSGVPAEVLCNIEADTYWCMSKLLDGIQDNYTFAQPGIQMKVKMLEELVSRIDEQVHRHLDQHEVRYLQFAFRWMNNLLMREVPLRCTIRLWDTYQSEPDGFSHFHLYVCAAFLVRWRKEILEEKDFQELLLFLQNLPTAHWDDEDISLLLAEAYRLKFAFADAPNHYKK
May act as a GTPase-activating protein for Rab family protein(s).
Q8WUA7
P0CS33
EIF3I_CRYNB
Eukaryotic translation initiation factor 3 39 kDa subunit homolog
Cryptococcus neoformans species complex
MKPIILQGHERSLNQIVFNSEGDLLFSASKDSVVNAWYTSNGERLGTYGGIKGGDGHNGSVWTVAVDSQTRFLLTGGADNAMKLWEVKTGECLYTWEFLTAVKRVAWNEDDDMFLSITEQRSGQPSVIRIFSINREDPRSQSTTPITEMRLSGSRATVAIWAPLSDYIITGHESGKIAKYDVKTGEEVQAVEDEHSALISDIQLSPDGTYFITASKDKTARLWDIETLEVMKVYTTETPVNSAVITPDRPYIILGGGQDAMNVTTTSQRAGKFESRFFHKLFEEEVGRVKGHFGPINTLSVHPQGRAYASGAEDGFVRVHWFEESYFRSRPFGDLEPEPEV
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
P0CS33
B3PJB0
ISPF_CELJU
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Cellvibrio
MSMRIGQGYDVHAFGEGEKIVIGGVVIPHHHGLVAHSDGDVLLHALCDALLGAVALGDIGKHFPDTDMQYRNADSRSLLRMVYAKVSQHGWKLANADMTIVAQAPRMASYIPHMVEVIASDLQSSASQINVKATTSERLGFTGREEGIACYAVVLLESR
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
B3PJB0
B4IF39
UBE2S_DROSE
Ubiquitin-protein ligase S
Sophophora
MSSQYSNVENLSPQTIRQVMRELQEMETTPPEGIKVLINESDVTDIQALIDGPAGTPYAAGIFRVKLTLNKDFPLTPPKAYFLTKIFHPNVAANGEICVNTLKKDWKPDLGIKHILLTIKCLLIVPNPESALNEEAGKMLLERYDDYSQRARMMTEIHAQPAKCGVGATGDAKDDGGPSTKKHAGLDKKLQDKKKEKLLKEKKRMLKRL
Catalyzes the covalent attachment of ubiquitin to other proteins. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by specifically elongating polyubiquitin chains initiated by the E2 enzyme vih/UbcH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit.
B4IF39
B7J1W4
RL1_BORBZ
50S ribosomal protein L1
Borreliella
MSKKGKKYIEAFSKVDKNKFYNIEDAILLLKEIKFAKFDETIDISINLNLKKNHTVRDTIVLPNQFMKPKRILVFAKGDRADEARAFGATHVGDDDLINKIKSGWDEFDVVVATPDMMKDVGRLGPILGKRGLMPNPKTQTVTNNLKDAINSLKKGRTEFRANKNGVISFSFGKSSMDNEKIKENYEEFVKEVVKKRPSDLKGAFIDSIYISSTMGPSIKVNFVWR
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
B7J1W4
Q92268
TBB_PLESA
Beta-tubulin
Lentinus
MREIVHLQTGQCRNQIGAKFWEVVSDEHGIEPDGLYKGNNDLQLERISVYYNEVGANKYVPRAVLVDLEPGTMDSVRSGPLGSLFRPDNFVFGQSGGGNNWAKGHYTEGAELVDAVLDVVRKEAEGTDCLQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPKVSDTVVEPYNATLSVHQLVENSDETFCIDNEALYDICFRTLKLTTPTYGDLNHLISIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMPGVCPLTARGSQQYRAVTVPELTQQMFDAKNMMAASDPRHGRYLTVAAVFRGKVSMKEVEEQMQNVQNKNSAYFVEWIPNNVLTAQCDIPPRGCKMAVTFLGNSTAIQELFKRVNDQFAAMFKRKAFLHWYTQEGMDEMEFTEAESNMQDLVAEYQQYQDATADEEEGEYEEEPAEEEQ
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.
Q92268
Q5NZS0
RBFA_AROAE
Ribosome-binding factor A
Aromatoleum
MPKEFSRSQRVAEQVRRELAELIRLEVKDPRVGFITLTDVEITPDYAHAKVFFTSMKGEEGLDEILTGLHRASGFLRRELGKRVRIHTLPELHFHYDSSVERGSRMSQLIDQVVRDDDARHKDDPES
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
Q5NZS0
Q492E6
URED_BLOPB
Urease accessory protein UreD
Candidatus Blochmannia
MSDELSQNFIDGWLGELRLNFALRGGRSVLTRCKHVGPFYVKKVFYSENDNTPHVYLLHPPGGLVGGDKLVLDVKLESDSRVLLTTPGAAKFYRSNGLYSEQKHIFRLERNTALEWVPQSSIFFPKSKAKIDTTFIIEQGSRVISFDMLCFGNLSLGSSTYPEEVDIHLNICLSDSIGLQERLRINELNCVMKLGGFRISALLFAVPSDEKTLYKVRKLITSVKHFQVGGATLLDEILVVRLLGNDNQYLKKMLHHIWYTIRPFIIGKKAMLPRIWLT
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
Q492E6
Q44493
ALGE4_AZOVI
Poly(beta-D-mannuronate) C5 epimerase 4
Azotobacter
MDYNVKDFGALGDGVSDDRASIQAAIDAAYAAGGGTVYLPAGEYRVSAAGEPGDGCLMLKDGVYLAGAGMGETVIKLIDGSDQKITGMVRSAYGEETSNFGMRDLTLDGNRDNTSGKVDGWFNGYIPGGDGADRDVTIERVEVREMSGYGFDPHEQTINLTIRDSVAHDNGLDGFVADYLVDSVFENNVAYANDRHGFNVVTSTHDFVMTNNVAYGNGSSGLVVQRGLEDLALPSNILIDGGAYYDNAREGVLLKMTSDITLQNADIHGNGSSGVRVYGAQDVQILDNQIHDNAQAAAVPEVLLQSFDDTAGASGTYYTTLNTRIEGNTISGSANSTYGIQERNDGTDYSSLIDNDIAGVQQPIQLYGPHSTVSGEPGATPQQPSTGSDGEPLVGGDTDDQLQGGSGADRLDGGAGDDILDGGAGRDRLSGGAGADTFVFSAREDSYRTDTAVFNDLILDFEASEDRIDLSALGFSGLGDGYGGTLLLKTNAEGTRTYLKSFEADAEGRRFEVALDGDHTGDLSAANVVFAATGTTTELEVLGDSGTQAGAIV
Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G), but introduces almost exclusively MG blocks, producing a polymer with non-gel-forming capacity.
Q44493
A7NDP3
PNP_FRATF
Polynucleotide phosphorylase
Francisella
MKIFREVFELGNKEIILETGGMARQADGSVTVSCGNNVVLVTTVVKKSVADGTDFFPLSVHYLEKTYAAGKIPGGFLRREGRPSEEQILISRLIDRSIRPSFPDGFFNEIQIVATVLSYDGAFSPDILALIGASASLAISGAPYDDVVAGVRVGYTNGKYILNPNKQDLRDSDLDLVVSGTYDAILMVESEANSLPESVMLGGILYAHKHLKTIINSINRLAKVASKPRIEYSIYQINKFLKSQIKSQFFGEIKNTYTIASKQERNLKLNAIRKNVLEYIFSSDVDGNEYTEKEILEAFHDIEKDLVRSNILEGKPRIDGRCTETIRPINVKIGVLPGVHGSALFTRGETQALVVTTLGSDRDAQLVESLDGIEKCRYMLHYNFPPYSVGECGMVGMAPKRREIGHANLAKRATQAVFPNEEAYPYVVRVVSEILESNGSSSMATVCGSSLSMMDAGVPIAEPVAGIAMGLIKDGAKYAVLSDILGDEDHLGDMDFKVAGTRYGVTALQMDIKIKGISREILEQALEQARVGRLHILGIMNEVIKEHKEAVSDVAPQIHVMNINPAKIKDVVGRGGATVKGIVEKTGAQIDTSDSGEVKVFAKDKKSMDMAVAMIEEIVAEVEEGQVYKGKIVKLLDSGVFVNLLGSQDGYLPFSEIEQAGMKTNSLVEGQGLEVLVQNIDRGGRVKLSLVAR
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
A7NDP3
A1UH85
SYY_MYCSK
Tyrosyl-tRNA synthetase
unclassified Mycobacterium
MSSILDELDWRGLIAQSTDRDALAAELAAGPMTLYSGFDPTAPSLHAGHLVPLLTLRRFQQAGHRPIVLAGGATGMIGDPRDTGERTLQTADTVADWADRIRGQLERFVEFDESPTGAIVENNLSWTGALSTIEFLRDVGKYFSVNVMLDRDTVRRRLEGEGISYTEFSYMLLQANDYVQLRKRHGCALQIGGSDQWGNIVAGVRLVRQKLGDTVHAMTTPLVTDSEGKKFGKSTGGGNLWLDPEMTTPYAWYQYFINTADADVVNYLRWFTFLEAGELAELEEATRDRPHQRTAQRRLARELTTLVHGEDATRSVEHASQALFGRGELAALDEPTLAAALREASVAELTPSGPDLITDLLVATGLSASKGAARRTIAEGGVSVNNMKIDSDEWTPQASDFLHGRWLVLRRGKRNIAGVQRVG
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).
A1UH85
A5CWR5
LIPB_VESOH
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
Candidatus Vesicomyosocius
MRVINLGRQDYLNIWDKMKTFTNTRDKNTKDELWIVEHNPVFTQGVSSKPEHILSNTDIPIVQTDRGGQVTYHGPGQVIIYCLFDLKRLGMGVKRIIEIIENSIIDLLRTYTIKAHLKSGAPGVYIDNAKIAALGLRIKQSRIYHGLSLNIDMDLSPFIQINPCGYQNLKVTQLCDLTDSRDTLNIIAKKLSQILINYVSRNRH
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
A5CWR5
A9M3P7
PURA_NEIM0
IMP--aspartate ligase
Neisseria
MAKNVVVIGAQWGDEGKGKIVDWLAEEAGGVVRFQGGHNAGHTLVVGGKKTILRLIPSGILHESLDCFIGSGVVVSPEALLGEIDELNAAGVKNVEGRLKIAPTCPLILPYHIALDQAREASRGKGKIGTTGRGIGPAYEDKVARRAIRAADLLHPEKLREKLDAVLAYYNVQLQHLHNAEPVKAEDVMAVIEKVAPRIAPMITDVSRVLNEKNKNGEKLLFEGAQGALLDIDYGTYPFVTSSNCLAGAASAGAGVGPQMLDYVLGIVKAYTTRVGSGPFPTELFDEVGAGLAERGHEFGSVTGRARRCGWFDAAALKRSIQINGISGMCITKLDVMDGVETINICVGYELPDGGKTDILPCGSDAVETCKPIYETMEGWKESTFGIKNYEELPDNAKAYLKRIEEVCGAPVAIVSTGPDREETIVLHHPFA
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
A9M3P7
A4SCS3
RS8_CHLPM
30S ribosomal protein S8
Chlorobium
MPVTDSIADYITRLRNAGRAKNKTTDIPYSKLRENISQLLLEKGYIKGFTVITTEKFPFIRVEMKYTAAGVPSIKEITRVSRPGRRMYEGKDIKKYLGGLGLYIISTSKGVITDKEAREQGVGGEILFRIY
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.
A4SCS3
O03074
ATPB_MICPL
F-ATPase subunit beta
Microlepia
PVGETTLGRISNVLGEPVDNPGPVQSNTIFPIHRSAPAFTQLDTKLSIFETGIKVADLLAPYRRGGKIGLFGGAGVGKTVLITELINNIAKAHGGVSVSGGVGERTREGNDLYMEMKESKVINEQNISESKVALVYGQMNEPPGARMRVGSTASTMAEYFRDVNKQDVLLFIDNILRFVQAGSEVSALLGRMPPAVGYQPTLGTEMGSLQERITSTKEGSTTSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMSQPWIVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFPSQPFFVAEVFTGSPGKYVSLPETIKGFQMILPGELDSLPEQAFYLVGNVDEATAKAAALQVEGQ
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
O03074
Q9LQ10
1A110_ARATH
Probable aminotransferase ACS10
Arabidopsis
MTRTEPNRSRSSNSDSDKNSGNVGGGRTTGMRVIVPLQGVVQGRGGLFLGSVIPCAFFYFLQFYLKRNRKNDESDNSGEQNSSASSSSSPNSGLPDPTRSQSAGHLTELTGLPRSLSRILLSPRNSGGAVSVSGRVNCVLKGGDSSPYYVGQKRVEDDPYDELGNPDGVIQLGLAQNNKLSLDDWVLENPKEAISDGLSISGIASYEPSDGLLELKMAVAGFMTEATKNSVTFDPSQLVLTSGASSAIEILSFCLADSGNAFLVPTPCSPGYDRDVKWRTGVDIIHVPCRSADNFNMSMVVLDRAFYQAKKRGVRIRGIIISNPSNPMGSLLSRENLYALLDFARERNIHIISNEIFAGSVHGEEGEFVSMAEIVDTEENIDRERVHIVYDLSKDLSFRGLRSAAIYSFNESVLSASRKLTTLSPVSSPTQHLLISAISNPKNVQRFVKTNRQRLQSIYTELVEGLKELGIECTRSNGGFYCWADMRGLISSYSEKGEIELWNKLLNIGKINVIPGSCCHCIEPGWFRICFSNLSERDVPVVMNRIRKVCETCKSQN
Probable aminotransferase. Does not have 1-aminocyclopropane-1-carboxylate synthase (ACS) activity, suggesting that it is not involved in ethylene biosynthesis.
Q9LQ10