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
|
|---|---|---|---|---|---|---|
Q8S8X4
|
PSAA_ATRBE
|
PsaA
|
Atropa
|
MIIRSPEPEVKILVDRDPVKTSFEEWARPGHFSRTIAKGPDTTTWIWNLHADAHDFDSHTSDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIGPSAQVVWPIVGQEILNGDVRGGFRGIQITSGFFQIWRASGITSELQLYCTAIGALVFAALMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQVHVSLPINQFLNAGVDPKEIPLPHEYILNRDLLAQLYPSFAEGATPFFTLNWSKYADFLTFRGGLDPVTGGLWLTDIAHHHLAIAILFLIAGHMYRTNWGIGHGLKDILEAHKGPFTGQGHKGLYEILTTSWHAQLSLNLAMLGSLTIVVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTRYNDLLDRVLRHRDAIISHLNWACIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPVFAQWIQNTHALAPGATAPGATASTSLTWGGGDLVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPERGGTCQVSAWDHVFLGLFWMYNAISVVIFHFSWKMQSDVWGSVSDQGVVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPATQPRALSIIQGRAVGVTHYLLGGIATTWAFFLARIITVG
|
PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
|
Q8S8X4
|
P55238
|
GLGS_HORVU
|
Alpha-D-glucose-1-phosphate adenyl transferase
|
Hordeum
|
MAMAAAASPSKILIPPHRASAVTAAASTSCDSLRLLCAPRGRPGPRGLVARPVPRRPFFFSPRAVSDSKSSQTCLDPDASTSVLGIILGGGAGTRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYGSNIGGYKNEGFVEVLAAQQSPDNPDWFQGTADAVRQYLWLFEEHNVMEYLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEERATAFGLMKIDEEGRIIEFAEKPKGEQLKAMMVDTTILGLEDARAKEMPYIASMGIYVISKHVMLQLLREQFPGANDFGSEVIPGATSTGMRVQAYLYDGYWEDIGTIEAFYNANLGITKKPIPDFSFYDRSAPIYTQPRHLPPSKVLDADVTDSVIGEGCVIKNCKIHHSVVGLRSCISEGAIIEDTLLMGADYYETEADKKLLAEKGGIPIGIGKNSHIKRAIIDKNARIGDNVMIINVDNVQEAARETDGYFIKSGIVTVIKDALLPSGTVI
|
This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
|
P55238
|
Q9LYE5
|
CID5_ARATH
|
Protein INCREASED POLYPLOIDY LEVEL IN DARKNESS 1
|
Arabidopsis
|
MKPGAFALNPHAASYVPISKRVDYGGGDDGLVFAAKSPTVEVSMPKKSSEMAYKQIRDDDLDLEMDIDMDIEYLLVTFSGLSQESITDVYLANGGDLEATIEMLNQLEIYSTESEENLPETLDIGDISESGPSTSKSTEVAASTSSVIPNAPVSA
|
Promotes polyploidy in dark-grown seedlings. Regulates the endocycle leading to hypocotyl elongation.
|
Q9LYE5
|
Q9RRL7
|
ACSA_DEIRA
| null |
Deinococcus
|
MTHPNDHIDAMLHETRVIHPSAEFQAGTRVSRAEYERRYRQSLDQPDDFWSEVAHDLHWMKDWDRVLDWQEPHAQWFVGGQTNIAYNALDRNVQRGLGDKRAIIWEGEDGEVRTYTYAELLREVCKAANALEELGVVAGDRVTLYMPLIPEAAIAMLACARIGAVHSIVFGGFSVSALADRINNAQSKLLITADAGYRRGKPVTLKINADEAAKLAPCLEHVLVVKRAGIPLEWWTEGRDLWWHDVVDRQSDQHEATALDSEHPLFILYTSGSTGAPKGVQHTTGGYMVGTYLTTQTVFDLRDDDIYWCTADIGWITGHSYSVYGPLLNGATVVMYEGAPNQPDWGRFWDIVQKHRVTILYTAPTAIRSFMQHGDEIPGRYDLASLRLLGSVGEPINPEAWMWYYRVIGGERCPVVDTWWQTETGSIMLTTLPGAFPSKPGSAGLPMFGVEPALMTRDGEEIGDDDGGLLVIKRPWPSMLRTVYGDDERYRKSYWGEIPHVYFAGDGARRDHDGYYTIVGRVDDVLNVSGHRLGTMEIESALVAHPDVSEAAVVGRPDPVKGESVVAYVLLQDGHTADPAALRAHVSSEIGALARPDAIYIADALPKTRSGKIMRRFLRQLAAGQPVQGDTSTLEDPTVLERLQASPAL
|
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
|
Q9RRL7
|
A0A1B0GUS4
|
UB2L5_HUMAN
|
Ubiquitin-protein ligase L5
|
Homo
|
MAASRRLMKELEEIRKCGMENFRNIQVDEANLLTWQGLIVPDNPPYNKGAFRIEINFPAEYPFKPPRITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSNDRKKFCKNAEEFTKKYGEKRPVD
|
Catalyzes the covalent attachment of ubiquitin to other proteins.
|
A0A1B0GUS4
|
Q47LJ7
|
RS19_THEFY
|
30S ribosomal protein S19
|
Thermobifida
|
MPRSLKKGPFVDHHLMKKVLEQNEKGTKNVIKTWSRRSMVVPEMIGHTIAVHDGRKHVPVFITEAMIGHKLGEFAPTRTFRSHVKEDRRSRR
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
Q47LJ7
|
Q59468
|
HMDH_HALVD
|
3-hydroxy-3-methylglutaryl-coenzyme A reductase
|
Haloferax
|
MTDAASLADRVREGDLRLHELEAHADADTAAEARRLLVESQSGASLDAVGNYGFPAEAAESAIENMVGSIQVPMGVAGPVSVDGGSVAGEKYLPLATTEGALLASVNRGCSVINSAGGATARVLKSGMTRAPVFRVADVAEAEALVSWTRDNFAALKEAAEETTNHGELLDVTPYVVGNSVYLRFRYDTKDAMGMNMATIATEAVCGVVEAETAASLVALSGNLCSDKKPAAINAVEGRGRSVTADVRIPREVVEERLHTTPEAVAELNTRKNLVGSAKAASLGFNAHVANVVAAMFLATGQDEAQVVEGANAITTAEVQDGDLYVSVSIASLEVGTVGGGTKLPTQSEGLDILGVSGGGDPAGSNADALAECIAVGSLAGELSLLSALASRHLSSAHAELGR
|
Catalyzes the NADPH-dependent reductive deacylation of (S)-3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to (R)-mevalonate. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids. Is also able to catalyze the reduction of mevaldehyde to mevalonate and the oxidative acylation of mevaldehyde to HMG-CoA.
|
Q59468
|
Q3MD46
|
MURI_TRIV2
|
Glutamate racemase
|
Trichormus
|
MYSSSSIEGNLYGFSEQEPQRAPIGVFDSGVGGLTVLRQIYRQLPNESVIYFGDTARLPYGIRSQAEILTFVRDILDWMQQQHVKMVVMACNTSSALALDIVREEYDFPILGVILPGAKAAVQQGKRIGVISTPATAKSNAYRQAIWEIDPNVEVWQVGCPEFVPLIEQNRIQDPYTTEVARAYLEPLIQQDIDTLVYGCTHYPLLAPVLRSLLPPQVKIIDPAVHVVTACTQELDILGLSNTHPPLPTRFAVSGCPQQFSQSGVNWLGYTPLVEAVDFTGIPVSQLQQDLA
|
Provides the (R)-glutamate required for cell wall biosynthesis.
|
Q3MD46
|
A9MWU8
|
RNB_SALPB
|
Exoribonuclease II
|
Salmonella
|
MFQDNPLLAQLKQQLHSQTPRAEGVVKATEKGFGFLEVDAQKSYFIPPPQMKKVMHGDRIVAVIHTEKERESAEPEELIEPFLTRFVGKVQGKNDRLSIVPDHPLLKDAIPCRAARGVQHEFKEGDWAVAEMRRHPLKGDRSFYADLTQYITFADDHFVPWWVTLARHNLEKEAPNGVATEMLDEGLERQDLTALNFVTIDSASTEDMDDALYAEELADGRLQLTVAIADPTAWIAEGSKLDNTAKIRAFTNYLPGFNIPMLPRELSDDLCSLRANEVRPALACRMIIAADGTIDDDIAFFAATIESKAKLAYDNVSDWLENNGTWQPDNEGIAQQIRLLHRICLSRSEWRHHHALVFKDRPDYRFVLGEKGEVLDIVAEPRRIANRIVEESMIAANLCAARVLRDKLGFGIYNVHTGFDPANADALAALLKTHGLHVDAEEVLTLEGFCKLRRELDAQPSGFLDSRIRRFQSFAEISTEPGPHFGLGLEAYATWTSPIRKYGDMINHRLLKAVIKGEAIARPQEDITQQMAERRRLNRMAERDVGDWLYARFLNDKAGTNTRFAAEIIDVSRGGMRVRLVDNGAIAFIPAPFLHAVRDELVCSQENGTVQIKGETVYKVTDVIDVTIAEVRMETRSIIARPAA
|
Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction.
|
A9MWU8
|
B7ZS96
|
TTHY_XENLA
|
Prealbumin
|
Xenopus
|
MASFKSFLLLALLAIVSEAAPPGHASHGEADSKCPLMVKVLDAVRGIPAANLLVNVFRQTESGKWEQITSGKTTELGEIHNLTTDEQFTEGVYKIEFATKAFWGKLGLSPFHEYVDVVFTANDAGHRHYTIAVLLTPYSFSSTAIVSEPHDDL
|
Thyroid hormone-binding protein, with a much higher binding affinity for triiodothyronine (T3) than for thyroxine (T4). Probably transports triiodothyronine from the bloodstream to the brain.
|
B7ZS96
|
Q75K18
|
SRP54_DICDI
|
Signal recognition particle 54 kDa protein
|
Dictyostelium
|
MVLADLGNQLSSALRSLNETTIVNEDTINQLLKEVGNALSKSDVSMSLIIQMRKNIKDKIKLDQMAAGLNKRKIIKQVVFDELIRLLDPGVPLWKPTKGKSNIVMFVGLQGAGKTTSVTKLAYFYKKKGFSTAIVCADTFRAGAFDQVRHNAAKAKIHYYGSETEKDPVVVARTGVDIFKKDGTEIIIVDTSGRHKQDSELFEEMKQIETAVKPDNCIFVMDSSIGQAAYEQATAFRSSVKVGSIIITKMDGNSMGGGAISAVAATNTPIIFIGTGEHLTDLELFDPSTFVSKLLGYGDMKGMLEKIKEVIPEDSTSLKEIAQGKFTLRSMQQQFQQIMQLGPIDKLVQMIPGMNQLPQLQGNEGGLKLKAYINILDSLSEKELDGKKPITQKRIITIAQGSGRHPNEVVELLEQHKTFEKLIGKGGPGGGLGSLMAGKGGPKNMEQAMKQMNANGGMQGLMNSLKGMGGMGDLAKMFGGGGGGGGGMPSMGDLAKMMGGMGGGGRGGGGMPNMGDLAKMMGGMGGGAGKGGQNGFPNLDLD
|
Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein).
|
Q75K18
|
Q1AXL7
|
GLMU_RUBXD
|
Glucosamine-1-phosphate N-acetyltransferase
|
Rubrobacter
|
MAQAGSASPLFAVVLAAGKGTRMKSNRAKVLHTLCGVPMVNYVIGAIRPLVPERLLVVVGHQAEQVRAVLPEDAEPVLQPEQRGTGDAVRVALEAIPEEEGVLLVVNGDGPLISDRTLGELLERHRSAGVGATVLVAELPDPSGLGRVREDAGVVRITEERDATEAERRNRLCNLGLYAFELPELRRAIREISSGAGRGELYLTDVLEIIGRRSRAVTYRLKDLEEANLVNDRSQLARAEEILRRRILDAHMKEGVTVRDPVSTHIEASVEIGRDTVILPGTFLRGRTRIGSDCVIGPSTDLVDTVVEDGATVEHSVGRGARVGRGAAVGPYAYLRPGTVLEEGSKVGAFCEVKNTRVGARSKVPHLSYVGDAEIGEDANLGAGTITANYDGAKKHRTVIEDGAFTGINTNLIAPVTIGQGAYLGAGSVVNKDIPPGKLAVGAPARVIRDAPGARSSSGDRRRARTEG
|
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
|
Q1AXL7
|
B0KBA3
|
CLPX_THEP3
|
ATP-dependent Clp protease ATP-binding subunit ClpX
|
Thermoanaerobacter
|
MAKYDNQKQLKCSFCGKTQDQVKRLVAGPGVYICDECIELCQEIINEEFEEDMDMGIGELPKPKEIKEFLDQYVIGQEKAKKALAVAVYNHYKRINSRIKPDDVELQKSNILLLGPTGSGKTLLAQTLAKLLNVPFAIADATSLTEAGYVGEDVENILLKLIQAADYDIEKAEKGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTIANVPPQGGRKHPHQEFIQIDTTNILFICGGAFEGIEKIIESRIGKKSLGFGAEVQSRKEKDLSEILSHIMPQDLLKFGMIPEFIGRVPIVVTLDPLSKDDLVRILTEPKNALTKQYEKLFELDGVKLEFDKKALGLIADMALERKTGARGLRAILEEIMLDVMYEIPSSDNIEKCIITEETVLKKAPPTLVYSDAQKAKKKIKKTESVS
|
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
|
B0KBA3
|
Q8JGS0
|
RU1C_DANRE
|
U1 small nuclear ribonucleoprotein C
|
Danio
|
MPKFYCDYCDTYLTHDSPSVRKTHCSGRKHKENVKDYYQKWMEEQAQSLIDKTTAAFQQGKIPPTPFPGAPPPGGSLLPHPSIGGPPRPGMLPAPPMGGPPMMPMMGPPPHAMMPGGPGPGMRPPMGGPMQMMPGPHMMRPPARPMMPAVRPGMVRPDR
|
Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. snrpc/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
|
Q8JGS0
|
B2IK83
|
KAD_BEII9
|
Adenylate monophosphate kinase
|
Beijerinckia
|
MRLILLGPPGAGKGTQSERLREQCKIPQLSTGDMLRAAVKAGTPIGLKAKAVMDAGGLVSDDIVVGIVADRIEEPDARNGFILDGFPRTVKQAEALTTMLHEKKMDLDAVIELVVDENALLARIEKRAKETLAAGGTVRADDNPAAFKTRIDTYREQTAPVSAYYASQGVLKTVDGMADIDTVTAAIDKILKA
|
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
|
B2IK83
|
Q29PU2
|
SAU76_ARATH
|
Protein SMALL AUXIN UP RNA 76
|
Arabidopsis
|
MAKGGNKLMKLKSVLKKLNSFNTKPNQPPAQTNHSRSSAVSAFPSEDLQTVYVGRTRRTYHVSSDVVSHPLFQQLAAVDGGCGSEDGSISVSCEVVLFEHLLWMLENADADESRPESVYELVEFYAC
|
May be involved in the regulation of ethylene receptor signaling. Promotes cell expansion and plant growth (Probable). Involved in the regulation of cell elongation .
|
Q29PU2
|
O66435
|
RS19_AQUAE
|
30S ribosomal protein S19
|
Aquifex
|
MGFKGAWNKRNRLIENPEEYYRLYKKLQRAYKLVREAIKRYGSFELLKGKNTLPELEALLEERKLVLENLKKQLKEAHKGKPKIEAEGDEKLKELIREVNKAQAEVRALEIIVNRVRKYEELYAQYKQMTEKKAYVDPKLWVRIRKMNETGERKVVRTYSRATTIIPEFVGHTIAVHNGKTFVPVYITQDMVGHKLGEFAPTRTFKGHPEKTAKVVKKK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
O66435
|
B9KL95
|
RS19_CERSK
|
30S ribosomal protein S19
|
Cereibacter
|
MARSTWKGPFVDGYLLKKAEKSRESGKNEVIKIWSRRSTILPQFVGLTFGVYNGKKHVPVNVTEEMIGQKFGEYSPTRTYYGHAADKKAKRK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
B9KL95
|
Q06922
|
TGFA_PIG
|
TGF type 1
|
Sus
|
MVPSAGQFALFALGILLAVCQALENSTSALSADPPIAAAVVSHFNDCPDSHSQFCFHGTCRFLVQEDKPACVCHSGYVGARCEHADLLAVVAASQKKQAITALVVVSIVALAVLIITCVLIHCCQVRKHCEWCRALICRHEKPSALLKGRTACCHSETVV
|
TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar.
|
Q06922
|
P0CAQ7
|
CA16B_CONLE
|
Alpha-conotoxin-like Lp1.6b
|
Lithoconus
|
VVLGPASDGRNAAANNKASDLIRQICCGYGDCGFVPNVCV
|
Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
|
P0CAQ7
|
A9EXF3
|
THIG_SORC5
|
Thiazole synthase
|
Sorangium
|
MTSDALTIGRYTFTSRLFVGTGKYKDLDETRRALEASGAEVVTVALRRVNLKERGEGSMMSLLQQGRVTILPNTAGCYTVEDAVRTCRLARELGLSDLVKLEVIGDERTLFPDNEATLEAARILVKEGFTVLPYCMDDPIVCRKLEDIGCAAVMPLAAPIGSGLGIRNPYNLMIIRETAKVPVIVDAGVGTASDAAVAMELGCDGVLMNTAIAGARDPILMAQAMKDAVRAGRMAYLAGRMPKKLYATASSPEQGKIAAL
|
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
|
A9EXF3
|
Q1AYH3
|
HUTU_RUBXD
|
Imidazolonepropionate hydrolase
|
Rubrobacter
|
MTDGKTTTVRAPRGTELSCKGWHQEGALRMLMNNLDPEVAERPEELVVYGGTGKAARSWECFWAIVEALRGLDGDETLLVQSGKPVAVFRTHPWAPRVLIANSLLVPEWADWETFRELERAGLTMFGQMTAGSWIYIGTQGILQGTYETFAALAEQRFGGTLRGRVCLTAGLGGMGGAQPLAITMNEGVALCVEVDPRRIDRRLEHRYLDERIDDLDAAVERAEEARREGEPLSIGIPGNAAEVFPALLERGYVPDAVTDQTSAHDPLGGYIPAGYTLEEAAELREADPGRYVREARASMARHCAAMVGFMERGAEVFDYGNNLRGEARLGGFERAFSYPGFVPAYIRPLFCEGKGPFRWAALSGDPDDIAATDEAVLELFPENGRLVRWIRQARERVRFQGLPARICWLGAGERHRAGLRFNELVAGGTISAPIVIGRDHLDSGSVASPYRETEGMRDGSDAIADWPVLNALLNTASGASWVAVHHGGGVGIGKSIHAGAQVVVDGTEEGAARIERVLTNDPSLGVVRHADAGYERAREAARALGIRMPMLGR
|
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
|
Q1AYH3
|
B1WR90
|
PDXH_CROS5
|
Pyridoxal 5'-phosphate synthase
|
Crocosphaera subtropica
|
MDLTALREEYTRHGLTRDDLEDNPFKQFEKWFQQATEAELSEPNAMSLATASAKGEPSIRTVLLKYFDEKGFVFFTNYESRKAQQIEENPHVALLFLWLPLERQVKIQGTATKVSTAESLNYFTSRPRGSQLGAWCSAQSSVISSRKLLEMKFEELKYKFQHGEIPLPSFWGGYRVKPTRFEFWQGRPNRLHDRFSYTLTETDDTTWGIHRLAP
|
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
|
B1WR90
|
Q96DR5
|
BPIA2_HUMAN
|
Short palate, lung and nasal epithelium carcinoma-associated protein 2
|
Homo
|
MLQLWKLVLLCGVLTGTSESLLDNLGNDLSNVVDKLEPVLHEGLETVDNTLKGILEKLKVDLGVLQKSSAWQLAKQKAQEAEKLLNNVISKLLPTNTDIFGLKISNSLILDVKAEPIDDGKGLNLSFPVTANVTVAGPIIGQIINLKASLDLLTAVTIETDPQTHQPVAVLGECASDPTSISLSLLDKHSQIINKFVNSVINTLKSTVSSLLQKEICPLIRIFIHSLDVNVIQQVVDNPQHKTQLQTLI
|
Has strong antibacterial activity against P. aeruginosa.
|
Q96DR5
|
O17611
|
NH100_CAEEL
|
Nuclear hormone receptor family member nhr-100
|
Caenorhabditis
|
MNIPFNSVSKIQWRNPSPVSDTSCLVCGDPHGKRHYGAMSCNGCKGFFRRSIWEKRTYKCSFNNECIIEFKYRNRCRACRLKRCLHVGMDANAVRSERTRKIKTEIDGDVKLEIKEEPADSEDADDECPLDIKPDIAMAWQTKEIIAHMLYEEDRVLNWEEPYNKLRYYTMDSEVLQAIKDPSQVCARTKINWNSHSRPLITIEALRFNWCRTFTLTIDWFETLPEYRALIDDDKELLVKFSLMPVGWLWYAYKSYEYRCDGIVFVDGSWFPRDKTIQQQVCPTCVLYYGRITESFMADVVNSMKELEMDETEMVLLKAICHLQPDYRLTRRGNDVISTGREKYKRALCEYIRMKSNGFMDASFRLCKLMQILPVVDILGKYEDESALLVSLGETEFNGSGGGLPYDIHASDSHFARKNRRKSDNQYHQQHVPLHIQ
|
Orphan nuclear receptor.
|
O17611
|
Q55G32
|
EXPL6_DICDI
|
Expansin-like protein 6
|
Dictyostelium
|
MIKIIYLIVLLVLLFKNNHIIIKADDCPFPQIPIKTLSGTWYDDPDHASCGFEKLTGPLGPGNRLVVALGSKLFDKGANCGQCYDVTSPFNNKTITVMATDSCHDAGYCQADNHFDFYKEAFDLLGSPSGVISGNSGLSYIKVPCPTYGNVKIMMKDGSNEFWTSFLIFNSRILIKQVSIKLSNSQQFIDLNRQPQGNYWPSTNMVSGEFEVRIESIGGEFIYVKIPSIESRKIYDTGNQFSADGCVGNKYDPYAPFQITSNSNNILPPSLYIIFLISILFLIINNIFSNKY
|
May serve to lubricate the movement of the cellulose microfibrils during cell growth and wall extension and/or may serve to maintain the fluid state of the slug cell wall.
|
Q55G32
|
Q8DST6
|
UPP_STRMU
|
UPRTase
|
Streptococcus
|
MGKFQIISHPLIQHKLSILRRKDTSTKHFRELVNEIAMLMGYEVSRELPLEEVEIETPITKTVQKQLTGKKLAIVPILRAGIGMVDGLLSLVPAAKVGHIGMYRDEETLEPVEYLVKLPEDIDQRQIFVVDPMLATGGSAVLAIDSLKKRGAANIKFVCLVSAPEGLKKLQEAHPDIDIYTAALDEKLNEKGYIVPGLGDAGDRLFGTK
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
Q8DST6
|
A0Q3H1
|
KHSE_CLONN
|
Homoserine kinase
|
Clostridium
|
MIKVKVPGTTANMGPGFDSFGMALDIYNEITVEEIESGFEMLQEGELSEIPLAENLIYTTFLNTLNKHNYKYKGFRINLSKCDVPMSRGLGSSATCIVGGIFAANSIMGNVMSFDEIIKEAVSIEGHPDNVVPAIVGGMTVSIMDKDNVIYSNVTVPDRLRAFVMIPNYKLGTEEARGVLPDSYTREECVFNISRAAMLVNVMNNGEIEKLRLCMQDKIHQKYRGALIRNIDDIFKKAYEFGSLAEFISGSGSTLIAFIDKDNNEFYDRMKNFLDTLEDEWTVHLLKPNFTGAEIIKNR
|
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
|
A0Q3H1
|
A8FSF3
|
HCP_SHESH
|
Prismane protein
|
Shewanella
|
MFCIQCEQTIRTPAGNGCSYSQGMCGKLAETSDLQDLLIYVLQGVSAYAVKAREFDIIDHEIDTFVPKAFFATLTNVNFDDARLVEYVEQANAYRGRLQDAYETACTAKGVTPEQMSAPAQLILATSKPEMITQAAQAAPNRGDVHEDILGLRLLCLYGLKGAAAYMEHARVLSQTNDEVAGQFHEIMAFLGEDSVDVDKLFATSMEIGQLNYKVMAMLDEGETESFGHPEPTQVNTVAVKGKAILVSGHDMVDLELILKQTEGKGINVFTHGEMLPALAYPEFKKYPHLVGNYGSAWQNQQKEFANFPGAVVMTSNCIIDPNVGSYADRIFTRSIVGWPGVTHLVGDDFTPVIEKALALDGFIYDEIPHLITIGFARNALMAAAPAVIDNVKNGSIKHFFLVGGCDGDKAERSYFTDIATQAPDDSVILTLGCGKYKFNKLEFGDINGIPRLLDIGQCNDSYSAIQLAIALSEAFECEINELPLSIVLSWFEQKAIVVLLTLLSLGVKNIRTGPTPPAFLTPNLLKILEDKFGLRNTTTVEEDLKTILNVA
|
Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
|
A8FSF3
|
Q02780
|
NFIA_MOUSE
|
TGGCA-binding protein
|
Mus
|
MKLADSVMAGKASDGSIKWQLCYDISARTWWMDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKEEERAVKDELLSEKPEVKQKWASRLLAKLRKDIRPEYREDFVLTVTGKKPPCCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKSPQCSNPGLCVQPHHIGVSVKELDLYLAYFVHAADSSQSESPSQPSEADIKDQPENGHLGFQDSFVTSGVFSVTELVRVSQTPIAAGTGPNFSLSDLESSSYYSMSPGAMRRSLPSTSSTSSTKRLKSVEDEMDSPGEEPFYTGQGRSPGSGSQSSGWHEVEPGLPSPSTLKKSEKSGFSSPSPSQTSSLGTAFTQHHRPVITGPRASPHATPSTLHFPTSPIIQQPGPYFSHPAIRYHPQETLKEFVQLVCPDAGQQAGQVGFLNPNGSSQGKVHNPFLPTPMLPPPPPPPMARPVPLPMPDTKPPTTSTEGGAASPTSPTYSTPSTSPANRFVSVGPRDPSFVNIPQQTQSWYLG
|
Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.
|
Q02780
|
A8AMR3
|
CUTA_CITK8
|
Divalent-cation tolerance protein CutA
|
Citrobacter
|
MLDDNSQDISIPEAVVVLCTAPDEATAQDLAAKVLAEKLAACATLLPGATSLYYWEGKLEQEYEVQMILKTTVSHQQALLECLKSHHPYQTPELLVLPVTHGDTDYLSWLNASLR
|
Involved in resistance toward heavy metals.
|
A8AMR3
|
A7H2Z6
|
THIG_CAMJD
|
Thiazole synthase
|
Campylobacter
|
MQENLKNDKLKIGKYEFDSRFILGSGKYSLELIKSSIEEAKAQIITLALRRANTGEIANILDYIPKNITLLPNTSGARNADEALRIARLSRELGCGELIKIEVISDSRYLLPDNYETIKACELLAKEGFTPLPYMHADLYAARAMRDVGAAAIMPLAAPIGSNKGLCAKEFIQILLNEIDLPIIVDAGIGTPAQACEAMQMGVSAVMVNTAIAEAKDIALMARAFSLAVNAGRAAFLAGLASVSEAKASSPLTGFLRD
|
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
|
A7H2Z6
|
Q7MGZ2
|
GPMI_VIBVY
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
|
Vibrio
|
MSAKKPLALVILDGYGYREDTASNAIANAKTPVMDALIANQPNTLISASGMDVGLPDGQMGNSEVGHTNIGAGRVVYQDLTRITKSILDGEFQQTAALVEAIDTAVKAEKAVHIMGLMSPGGVHSHEDHILAAVEMAAERGAEKIYLHCFLDGRDTPPRSAEGSLQRFQDLFAKLGKGRVASLVGRYYAMDRDNNWDRVQVAYDLLTQAKADFTYDSAVAGLAAAYERGENDEFVKATEIKAEGQESAAMQDGDAVIFMNYRADRARQITRTFVADFAGFERAAFPAVNFVMLTQYAADIPLAIAFPPASLENTYGEWLSKQGQTQLRISETEKYAHVTFFFNGGVETEFAGEERQLVASPKVATYDLQPEMSSTELTEKMVAAIKSGKYDTIICNYPNADMVGHTGVYEAAEKAIEALDASVGQVVEAIKEVGGQLLITADHGNAEMMVDPETGGIHTAHTSLPVPLIYVGDKAVEFKEGGKLSDLAPTMLSLAGLEIPAEMTGQVLVK
|
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
|
Q7MGZ2
|
A8AJ37
|
GAL1_CITK8
|
Galactose kinase
|
Citrobacter
|
MSLKEKTQSLFAEIFGYPATHTIQAPGRVNLIGEHTDYNDGFVLPCAIDYQTVISCATRDDRKVRVIAADYDNQVDEFSLDAPIVTHDSQQWSNYVRGVVKHLQKRNNAFGGADLVISGNVPQGAGLSSSASLEVAVGTVFQQLYHLPLDGAQIALNGQEAENQFVGCNCGIMDQLISALGKKDHALLIDCRTLGTKAVSMPEGVAVVIINSNFKRTLVGSEYNTRREQCETGARFFQQPALRDVSLAAFNAVASELDPIVAKRVRHVLTENARTVEAASALEKGDLKRMGELMAESHASMRDDFEITVPQIDTLVEIVKATIGDKGGVRMTGGGFGGCVVALLPEALVPAVQQAVATQYEAKTGIKETFYVCKPSQGAGQC
|
Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
|
A8AJ37
|
P42444
|
RECA_ENTFA
|
Recombinase A
|
Enterococcus
|
MADDRKVALDAALKKIEKNFGKGSIMKLGEKADQKISTIPSGSLALDVALGVGGYPRGRIIEVYGPESSGKTTVSLHAIAEVQRNGGTAAFIDAEHALDPQYAEKLGVNIDELLLSQPDTGEQGLEIADALVSSGAIDIVVIDSVAALVPRAEIDGEMGASHVGLQARLMSQALRKLSGSINKTKTIAIFINQIREKVGVMFGNPETTPGGRALKFYATVRLEVRRAEQLKQGTDIVGNRTKIKVVKNKVAPPFKVAEVDIMYGQGISQEGELLDMAVEKDLISKSGAWYGYKEERIGQGRENAKQYMADHPEMMAEVSKLVRDAYGIGDGSTITEEAEGQEELPLDE
|
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
|
P42444
|
Q5ASK9
|
TRM44_EMENI
|
tRNA (uracil-O(2)-)-methyltransferase
|
Aspergillus subgen. Nidulantes
|
MARALALSRSVQVCKSRLFTVASKSAITKRCLSNPIQYRSVSLFATTYAPSKDLNSRLHSEHIGDTALYLLLNPGLTSSVLFRADILAQSGKCPTLAALEAQKQQETEEASTATAMTMAQNVIEEEKEVKEPVVEIPAREVPGFELHKTLIRRLIPRNQQLDMPVDQTCHLYSHAGAVEQIEKEKELGIPHSRAPKERFMVIYTPHVSSKEELPYYHPLVRSMAFVYEFGYTGEFEGPENSIPRIAENPKGTMSIHFLPYENDVDSISARLERSLTKLIEVQIRTTKGRLDPCRPSTSSPYALIKDNVIPRNRVQDTYSRLKNKYAANLNERWIESTEPSKHVFEDLSIAAFLIELWRDLYGAVPGDEREQQKQQSSTSKVGSGQFPGFVDIACGNGVLVYILISEGYSGWGFDARRRKTWSIFPTDVQERLKEEIYIPKPFMDVLAAQNQGPIQNKNQDASMQSPLSEPQSGQSNGPNSGTSTSTSLSNLPKDTFIISNHADELTLWTPILSTLLNPANPPPFLAIPCCSHSLSGARHRFRPQSARPSATQNPQKQQGENGTHSQDEEGSSEDMKERKGEEKEKNPETGDLEQMRKDKLAAQNPH
|
Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
|
Q5ASK9
|
B9MDP9
|
LEPA_ACIET
|
Ribosomal back-translocase LepA
|
Diaphorobacter
|
MNHIRNFSIIAHIDHGKSTLADRIIQRCGGLADREMEAQVLDSMDIEKERGITIKAQTAALQYKARDGKVYNLNLIDTPGHVDFSYEVSRSLSACEGALLVVDASQGVEAQTVANCYTALDLGVEVLPVLNKMDLPQADPDTAKAEIEDVIGIDASEAIAISAKTGMGIDDVLEQIVAKVPAPRGKPDAPLRAMIIDSWFDSYVGVVMLVRVVDGRLQKGERFKMMASGAAYEANNLGVFTPAQQSRDALEAGEVGYIIAGIKELKAAKVGDTITLEKKLPNNLGPATEALPGFKEIQPQVFAGLYPTEANQYDALRDALEKLQLNDASLHFEPEVSQALGFGFRCGFLGLLHMEIVQERLEREFDQDLITTAPSVVYEVVKGDGEVIMVENPSKMPDQGKIQEIREPIVTVHLYMPQDYVGPVMTLANQKRGVQMNMQYHGRQVMLTYELPLGEIVLDFFDKLKSVSRGYASMDYEFKEYRPSDVVKVDILLNGEKVDALSIIVHRSQSQYRGRAVAAKMREIISRQMFDVAIQAAIGANIIARETIKALRKNVLAKCYGGDITRKRKLLEKQKAGKKRMKQIGSVEVPQEAFLAILQVED
|
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
|
B9MDP9
|
Q493T7
|
IF2_BLOPB
|
Translation initiation factor IF-2
|
Candidatus Blochmannia
|
MTDTTIQSFAAEMKMSVDQLIQWFSYIGILKTEIGIVTQREKEILFKYMNDNKSDISKKLILQRKTRSILSVSSVGGKNKKVQIEIRKKLTYVQSTLQETEFIDVKNKMVLDANREASSLIVRNNRLVNKKISNTLGPSSLTKISKKNHRYSELIEHKEKVIGKISRKFEDKSLQDSDETQLLKKKTKNCWDIELNNTNAISSNLGDSSSNSKLYCMPELLEKNNNQKLENERRNRSRVRTRYRNGGKLTKQHKRGNHHRLYEATSDEFGMEEELYIPNRVNKSKRKQSALVQVFNKPVQTITRDIIIGQTISVAELANKMSIKSSRVIKTMMQLGIIATINQIIDQDTAQLVAEEMGHNVILRRENELEELIMNDRDIDITSSDTTLANRAPIVTIMGHVDHGKTSLLDRIRSTKIASSEVGGITQSIGAYHVSTDNGMITFLDTPGHAAFTAMRARGVQITDIVVLVVAADDGVMPQTIEAIEHIKAANVPVVVAINKIDKSEANPERIKNDLNNHGLIPEEWGGDTQFIHVSATSGNGIDNLLDAILLQSDMLELKVVHHGMARAIVIESFLDKGRGPVVAVLVREGTLKCGDIILCGTEYGRVRAMRNEFGHEITSAGPSIPVELLGLSGSPASGESVIVVRNEKKAREVALYRQGKSREIKLARQKEPNIENIFSSIKNTSVVSELNLIVKSDTKGSSEAIRESLENLSTGGDVTIKILSSSIGGITETDVALAAASNAVIVGFNVRADPTARRIIEADQLDVRYYSVIYDLIDEVKQAVHGMLAPRYKHEIIGLAKVRNVFRSPKYGNVAGCMVVEGMIKRYKKIRVIRDNIVVHEGELESLRRFKDDVNEVRSGIECGIGIKNYKNIHSGDMIEVFDMVKISHV
|
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.
|
Q493T7
|
P84570
|
PLS2_PITOR
|
Phylloseptin-5
|
Pithecopus
|
FLSLIPHAINAVSAIAKHS
|
Has antiprotozoal activity against T.cruzi.
|
P84570
|
B7NNT8
|
ARNF_ECO7I
|
Undecaprenyl phosphate-aminoarabinose flippase subunit ArnF
|
Escherichia
|
MGLMWGLFSVIIASAAQLSLGFAASHLPPMTHLWDFIAALLAFGLDARILLLGLQGYLLSVFCWYKTLHKLALSKAYALLSMSYVLVWIASMVLPGWEGTFSLKALLGVACIMSGLMLIFLPTTKQRY
|
Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane.
|
B7NNT8
|
Q1IWP0
|
VATE_DEIGD
|
V-ATPase subunit E
|
Deinococcus
|
MALDKLLEHEAQAEIERIRAEARDRAQQILASARERADALLESRRRLLETQRQAALVRARSAADLELSAARLTASEQGMAEVYRLVEGHLREITGLPEYREILARLIAEARQAIPEAEAVEVNPADLALARELVTDLSVRENPAIQGGVRVVARGGKSGITNTLAGRLDRLRGELAPQVSRLLAE
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
Q1IWP0
|
Q1LTT8
|
RL31_BAUCH
|
50S ribosomal protein L31
|
Candidatus Baumannia
|
MQKNIHPKYFEIRAICSCGNIIPTYSTLDQHLNLDVCSACHPFYTGKQRRVNTRGRVERFNKRFSLSIMNSKKKE
|
Binds the 23S rRNA.
|
Q1LTT8
|
Q96W72
|
XYNB_TALPU
|
1,4-beta-D-xylan xylanohydrolase B
|
Talaromyces sect. Talaromyces
|
MKVTAAFAGLLATTLAAPATELVTRSINYVQNYNGNLGAFSYNEGAGTFSMYWQQGVSNDFVVGLGRSTGSSNPITYSASYSASGGSYLAVYGWVNSPQAEYHVVEAYGNYNPCSSGSATNLGTVSSDGGTYQVCTDTRVNQPSITGTSTFTQFFSVRQGSRTSGTVTIANHFNFWAKHGFGNSNFNYQVVAVEAWSGTGTASVTVSA
|
Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
|
Q96W72
|
A8MEA3
|
RECF_ALKOO
|
DNA replication and repair protein RecF
|
Alkaliphilus
|
MIVEELKLINYRNYEQMNLKFHPRLNVFIGDNAQGKTNLIESIYLCSAGKSFRTNHDQELINMNKKQAYIHVKVKKVHSDVHIEVRLNSERKKDLKVNQIPLVKMGELLGNLNVVLFSPEDLKLVKEGPSERRRFMDREISQISTKFYYTLSQYNKILQHRNKLLKYNKGKEIDIEVWDEQLAAAGAWLIVYRRNFIKKISILAKLMHRKITESIENLEVIYEPNVKVKENDEVDVIKEKILQNLKENFNVDKQRGLTTCGPHRDDMILKINGLDVKTYGSQGQQRTAVLSLKLAELELVKGEVGEYPILLLDDVMSELDSKRQHYLIHNLKSVQTFITTTMMETLKDLKPEDRAVFYVNKGQID
|
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
|
A8MEA3
|
C5Y210
|
NNRD_SORBI
|
ATP-dependent NAD(P)HX dehydratase
|
Sorghum
|
MSRPTGACPHAWRHQQQPLRGRMWAASPAFRRQLVLLRSLLPSPPAPSSVAGFPPSCPSCSSFLRVRTNHAMAASAGTVYEADAEAVVRRITPPLDRARHKGQAGKIAVIGGCREYTGAPYFAAISALKVGADLSHVFCTKDAATVIKSYSPELIVHPILEESYSVRDDERASVSSKILTEVGKWMERFDCIVVGPGLGRDSFLLDCVSNIMRHARQANIPTVVDGDGLFLVTNNLSLVEGNPLAILTPNVYEYKRLVQKVLNCDVDEETASEQLITLCQKIGDVTIMQKGKADVISDGKTVTQVSTFGSPRRCGGQGDILSGSVAVFASWARHFVLTNEQPTEKRKAASHAFEKNKRSTVTSDIIEFLGKSLEDICPAEH
|
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
|
C5Y210
|
A9B426
|
RL6_HERA2
|
50S ribosomal protein L6
|
Herpetosiphon
|
MSRIGRKPIEVPAGVTVNVDSNNLVTVKGPKGTLSESIRPEVTVNINGATVEITRVNDSRQARAFHGLSRTLVANMVDGVTKGFEKTLEMNGTGYRATLDGKTLVLSLGFSHPVRVEPYEGNSFEVAERRVVIKGPNKQKVGDQAANIRKLRPPEPYLGKGIKYSDEVIRRKAGKAGKK
|
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
|
A9B426
|
A0A286YFG1
|
SCGR8_HUMAN
|
Keratin-associated protein 28-8
|
Homo
|
MGCCGCGGCGGGCGGCSGGCGGGCGGGCGGGGCGGGCGSCTTCRCYRVGCCSSCCPCCRGCCGGCCSTPVICCCRRTCSSCGCGYGKGCCQQKGCCQQKCCCQKQCCC
|
In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
|
A0A286YFG1
|
Q6YXN2
|
CYB6_PHYPA
|
Cytochrome b6
|
Physcomitrium
|
MGRVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFASVQYIMTEVNFGWLIRSVHRWSASMMVLMMILHIFRVYLTGGFKKPRELTWVTGVILAVLTVSFGVTGYSLPWDQIGYWAVKIVTGVPEAIPVIGSPLVEILRGSVSVGQSTLTRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
|
Q6YXN2
|
P01353
|
GAST_CANLF
|
Gastrin
|
Canis
|
MQRLCVYVLILALALATFSEASWKPRSRLQDAPSGPGANRGLEPHGLDQLGPASHHRRQLGLQGPPQLVADLSKKQGPWMEEEEAAYGWMDFGRRSAEEGDQRP
|
Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine.
|
P01353
|
C4LD55
|
NQRE_TOLAT
|
NQR-1 subunit E
|
Tolumonas
|
MEHYLSLFVKSIFIENLALSFFLGMCTFLAVSKKVKTAMGLGIAVVVVQAIAVPANNLVFTYVLKENALVQGMDLTFLGFITYIGVIAALVQILEMFLDRYVPSLYSALGIFLPLITVNCAIFGGVSFMVQREYNFPESVVYGVGSGISWALAIVLMAAIREKMKYSDVPPGLRGLGITFITAGLMALGFMSFSGISL
|
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
|
C4LD55
|
A4XES9
|
CARDI_NOVAD
|
NACOX1
|
Novosphingobium
|
MVTKGVVVVSSFRRSRQDANRPHAFLTGIHAPVKEERTIEDLAVTGTIPAELSGRYVRIGPNPFRADPRGHHWFVGDGMVHGVCMKGGKALWYRNRYVRSRNLQDAGGPAAAPGPRRSTFDTVNTNVIQHAGRTFALVEAGSFPVELTHDLESFAYSDLGGTLKGPFSAHPHLDPLTGELHAVTYDGQTLDTVWHVVVDREGRVRREEPVPVAHGPSIHDCAITAKYVLILDLPVTFSMAALVGGARFPYRWNPAHRARVGLLPREGTAADVIWCDVDAAYVFHVANAFDNPDGTVTVDLAAYETMFAHGPDGPNGKSLGMERWTVDPAARKVARKTLDAAPQEFHRPDERFFGQPYRFAWSMGLPAENAEDFLGHAPIYGYDLATGQRSAHDFGPGKIPGEFVFIPRRADAEEGDGWLMGYVIDLASETTDLAILDARNLAAPPLALIHIPCRIPPGFHGNWLPDAAD
|
Catalyzes the conversion of 8'-apo-beta-carotenal to 13-apo-beta-carotenone and C12-dialdehyde. Has also weak activity with 4'-apo-beta-carotenal and gamma-carotene.
|
A4XES9
|
C3KE92
|
YACG_PSEFS
|
DNA gyrase inhibitor YacG
|
Pseudomonas
|
MSQPLTVDCPTCGAPVEWTAANLNRPFCSDRCKLIDLGAWAAEEHKIPVAPDAEDELFSEDLPPRH
|
Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase.
|
C3KE92
|
P0A316
|
PHEA2_PARMW
|
C-phycoerythrin class II alpha chain
|
Parasynechococcus marenigrum
|
MKSVITTVVGAADSASRFPSASDMESVQGSIQRAAARLEAAEKLAGNYDQVAQEAVDAVYNQYPNGATGRQPRKCATEGKEKCKRDFVHYLRLINYCLVTGGTGPLDELAINGQKEVYKALSIDAGTYVAGFSHLRSRGCAPRDMSAQALTAYNQLLDYVINSLG
|
Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.
|
P0A316
|
Q9FMP0
|
MD19A_ARATH
|
Mediator of RNA polymerase II transcription subunit 19a
|
Arabidopsis
|
MEPERLKFGGPRELCGAADLISQFKLVQHHEFFCKKSLPVSLSDSHYLHNVVGDTEIRKGEGMQLDQLIESISQSRETNIRIQPFDIDELQESFQLNDMTPVELPPAEKGAPTIPSKSKSESKDRDRKHKKHKDRDKDKDREHKKHKHKHKDRSKDKDKDKDRDRKKDKNGHHDSGDHSKKHHDKKRKHDGDEDLNDVQRHKKNKHKSSKLDEVGAIRVAG
|
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
|
Q9FMP0
|
Q9MIY1
|
NU4M_DANRE
|
NADH dehydrogenase subunit 4
|
Danio
|
MLKVLIPTIMLFPTIWLSSSKWLWTTTTMNSFLIAFISLTWLKWTSDTGWNASNSYMAADPLSTPLLVLTCWLLPLMILASQNHINSEPVNRQRMYITLLASLQTFMIMAFGATKIIMFYIMFEATLIPTLIIITRWGNQAERLNAGTYFLFYTLAGSLPLLVALLLLQQSTGTLSMLVLQYSDPLLLNSWGHKIWWAGCLIAFLVKMPLYGMHLWLPKAHVEAPVAGSMILAAVLLKLGGYGMMRMMVMLDPLSKQLAYPFIILALWGVIMTGLVCLRQTDLKSLIAYSSVGHMGLVAGGILIQTPWGFTGAIILMIAHGLTSSALFCLANTSYERTHSRTMILARGLQMVLPLATVWWFIANLANLALPPLPNLMGELMIITALFNWSPWTIIITGMGTLITANYSLYMFLTSQRGSIPEHITNLSPSHTREHLLMTLHLIPIILLMLKPELMWGWCN
|
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
|
Q9MIY1
|
Q5NVI3
|
RED_PONAB
|
IK factor
|
Pongo
|
MPERDSEPFSNPLAPDGHDVDDPHSFHQSKLTNEDFRKLLMTPRAAPTSAPPSKSRHHEMPREYNEDEDPAARRRKKKSYYAKLRQQEIERERELAEKYRDRAKERRDGVNKDYEETELISTTANYRAVGPTAEADKSAAEKRRQLIQESKFLGGDMEHTHLVKGLDFALLQKVRAEIASKEKEEEELMEKPQKETKKDEDPENKIEFKTRLGRNVYRMLFKSKAYERNELFLPGRMAYVVDLDDEYADTDIPTTLIRSKADCPTMEAQTTLTTNDIVISKLTQILSYLRQGTRNKKLKKKDKGKLEEKKPPEADMNIFEDIGDYVPSTTKTPRDKERERYRERERDRERDRDRDRERERERDRERERERDREREEEKKRHSYFEKPKVDDEPIDVDKGPGSAKELIKSINEKFAGSAGWEGTESLKKPEDKKQLGDFFGMSNSYAECYPATMDDMAVDSDEEVDYSKMDQGNKKGPLGRWDFDTQEEYSEYMNNKEALPKAAFQYGIKMSEGRKTRRFKETNDKAELDRQWKKISAIIEKRKKMEADGVEVKRPKY
|
Involved in pre-mRNA splicing as a component of the spliceosome. Auxiliary spliceosomal protein that regulates selection of alternative splice sites in a small set of target pre-mRNA species. Required for normal mitotic cell cycle progression. Recruits MAD1L1 and MAD2L1 to kinetochores, and is required to trigger the spindle assembly checkpoint. Required for normal accumulation of SMU1.
|
Q5NVI3
|
Q750W3
|
RKM5_ASHGO
|
Ribosomal lysine N-methyltransferase 5
|
Eremothecium
|
MLQLCPLDEDTLYTHVYERYVELDRHAETLAQDLGIHASDAETLVVDIAPAQPTKSSDTYSLTVSQSLASLRSSTVNNNSTTGYVLWSGTPFFLCWLLYAPSAAPLRDGGRVPVTDSAAQFLQLPPLFSAPARPVCVVELGSGAAGVAAIVLANYVDRYLVSDQKAILKPLRANLLANISEVSRRTVCSKQTPELSSNRRTPARCELELIALDWERIATVPAALRPTDAAHVHVLALDVVYNDFLIPPLLTAIKRLLRWYADEHAVKATAYVLVHLRAQDILQTFLEHAIIDLRLRCYYMDEERLRSSRFALYYVTL
|
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates 60S ribosomal protein L1.
|
Q750W3
|
Q7AP31
|
FLOA_LISIN
|
Flotillin-like protein FloA
|
Listeria
|
MTMIGPIIIAVLIIIFLIVFFTLVPVGLWISALSARVPVGLGTLIGMRLRRVVPSRVVKPLIKAVKAGLDLEVNQLESHYLAGGDVDNTVDALIAAHRANIELDFSRAAAIDLAGRDVLEAVQTSVTPKVIRTPEFTGVAQNGVEVKVITQITVQSNIERIVGGAGEDTVIARVGEAVVSTVGETREHTDVLENPNSISKKVQEQGLGDGTAYTILSIDIAEMRIGDNIKAKLDIEKANADMEVAQAAASKRKAEAIALEQENRAAVVAAEAEVPRALSRALEEGNLGVMDYYKMENVQSDTAMRESIAHEDEK
|
Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity.
|
Q7AP31
|
A7INJ8
|
LEXA_XANP2
|
LexA repressor
|
Xanthobacter
|
MLTRKQYDLLRFIHERLKETGVPPSFDEMKEALDLRSKSGIHRLITALEERGFIRRLPNRARALEVVRLPDSVAPGLATPRSASRGFSPSVIEGSLGKVRPAADDDEGAGQVVTVPVMGRIAAGSPISAIQTRSHTLNIPPEMLGSGEHFALEVRGDSMIEAGILDGDTVLIRKCDTADTGDIIVALVDDEEATLKRLRKKGASIALEAANPAYETRIFGPDRVRIQGRLIGLMRRY
|
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
|
A7INJ8
|
B2U9W0
|
PURA_RALPJ
|
IMP--aspartate ligase
|
Ralstonia
|
MSAPAVSQGRNVVVIGTQWGDEGKGKIVDWLTDHAQGVVRFQGGHNAGHTLIIGGKKTILRLIPSGIMRDGVACYIGNGVVLSPEALFKEIDELESAGVQVQNRLRISEATNLILPYHVAIDKAREAKRGAAKIGTTGRGIGPAYEDKVARRGLRVQDLFDPAYFAERLRENLDFHNFVLTQYLNHPALDFQQTLDEMLSYAGRLAPMVTDVSAELFAANAAGKNLMFEGAQGTLLDIDHGTYPFVTSSNCVAGNAAAGAGVGPGQLHYILGITKAYCTRVGSGPFPSELYDADNPARQDPIGVRLANVGKEFGSVTGRPRRTGWLDAAALRRAIQINGVSGLCMTKLDVLDGLETLKLCVGYMLDGKQIDILPRGSDAVARCQPIYEEFPGWNTSTFGLKEWDALPQTAQAYLKRVEEVAGIPIAMISTGPDRDETILLRHPYKD
|
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.
|
B2U9W0
|
P22314
|
UBA1_HUMAN
|
Ubiquitin-activating enzyme E1
|
Homo
|
MSSSPLSKKRRVSGPDPKPGSNCSPAQSVLSEVPSVPTNGMAKNGSEADIDEGLYSRQLYVLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCHNRGIKLVVADTRGLFGQLFCDFGEEMILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKKISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVALAQAVNARALPAVQQNNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEVLTEDKCLQRQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDPKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTGSQDRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSRLEELKATLPSPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQYYNQEWTLWDRFEVQGLQPNGEEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRYTIR
|
Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system . Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP . Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites .
|
P22314
|
B9K884
|
EFTU_THENN
|
Elongation factor Tu
|
Thermotoga
|
MAKEKFVRTKPHVNVGTIGHIDHGKSTLTAAITKYLSLKGLAQYVPYDQIDKAPEEKARGITINITHVEYETEKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTREHVLLARQVEVPYMIVFINKTDMVDDPELIELVEMEVRDLLSQYEYPGDEVPVIKGSALKALEAPDDPNHEAYKPIQELLDAMDNYIPDPQRDVDKPFLMPIEDVFSITGRGTVVTGRIERGRIRPGDEVEIIGLSYEIRKTVVTSVEMFRKELDEGIAGDNVGCLLRGIDKDEVERGQVLAAPGSIKPHKRFKAEVYVLKKEEGGRHTPFTKGYKPQFYIRTADVTGEIVGLPEGVEMVMPGDHVEMEIELIYPVAIEKGQRFAIREGGRTVGAGVVTEVIE
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
B9K884
|
P96095
|
HCP_ACIFI
|
Prismane protein
|
Acidithiobacillus
|
MMFCYQCEQTTRSPAGIGCTSEPGTCGKDEATAVLQDILTHLMKGIASMRAGRAMGVADRRTDDFIFYGLFTTLTNVNFTATRFVHLIQEASKRRERIKLLYEEAAREQGKTPEILSGPALFQPADSLEQLLRQAPSVAINADVEHLGSDVIGARALILYGMKGVALIAQHARVLGYQSDEVMPQAEEILDYLASNPTDLDEMLEESLEVGRLNLKVMELLDVANTDSFGAQEITSVRISPIQGKAILVSGHDLHDLKQILEQTKDQGINVYTHGEMLPANAYPLLKAYPHLAGNLGGAWQDQQREFADFPGPIVMTSNCIIEPGRSYKNRIFTLGPVGWPGVRHIDNGDFTPVIQAAKALPGFTADAKEQRITIGFGHHTLLGVADKIVDAVKHGDIRHFFLVGGCDGVSPARNYFTEVADNAPADSVVMTLGCGKYRFNKHEFGDIGGIPRLLDIGQCNDAHSAIRVAGALAEAFNCGVNDLPLSIMLSWFEQKATAIHLSLLALGIKGIKLGPTLPAYLTPTLVQKLQSRFDLDLDLIGEAQADLQAALAHTA
|
Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
|
P96095
|
B7KHC2
|
TRMD_GLOC7
|
tRNA [GM37] methyltransferase
|
Gloeothece citriformis
|
MRFDIITLFPDFFTSPLQSGLLGKALDKQIAQVNLVNPRDFALDKHHRVDDEPYGGGVGMLLKPEPIFAAVESLEILPRREVVLMTPQGQPLSQPILRELATDFDQLVLICGHYEGVDERVTQYLVTREISLGDFVLTCGEIPALTVLNGVIRLLPGTVGKEESLKLESFEADLLDYPQYTRPALFRDWEVPAVLRSGNHQAIEQWRKQQQIERTKERRPDLWEKWTINNG
|
Specifically methylates guanosine-37 in various tRNAs.
|
B7KHC2
|
P31353
|
PMM_CANAL
|
Phosphomannomutase
|
Candida
|
MSFANKQDPKTLVLFDVDGTLTPARLTISEEMKKTLEKLREKVVIGFVGGSDLSKQVEQLGPNVLNDFDYCFSENGLTAYKLGKELASQSFINWIGNEKYNKLVKFILRYLSDIDLPIRRGTFIEFRNGMINVSPIGRNASTQERNDYEKFDKQHHIRETMVEALKKEFPDFGLTYSIGGQISFDVFPTGWDKTYCLQHVEDEHFENIHFFGDKSYKGGNDYEIYNDPRTIGHAVNSPDDTIRILNETFKLQ
|
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
|
P31353
|
B7KHD0
|
FMT_GLOC7
|
Methionyl-tRNA formyltransferase
|
Gloeothece citriformis
|
MKVVFFGTPQFAVPSLERLLEHSDIDVVAVVTQPDKPRGRGKQLIPSPIKKVALDHQIPIWQPKRVKKNAQTLTKLRETNADAFAVVAYGQILSAEILQMPKLACINVHGSILPKYRGAAPIQWSIYHGETQTGITTMLMDEGMDTGAMLLKAYTPIQLLDNADKIATTLANQGADLLIETLLKLEQGELNPESQNSELATYAPLIQKEDYLINWTRHALQIHNQVRGFYPNCFTTFREQPLKILATAPLGEAYWEHLPSNIAQKIQPQWTTLSSLTSSPGEVVNLIKNLGPIVQTGEGLLLLLQVQLSGKRPQSGWDFVNGTRLSVGEKFLMV
|
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
|
B7KHD0
|
A5FLE3
|
HEM11_FLAJ1
|
Glutamyl-tRNA reductase 1
|
Flavobacterium
|
MENNNVPKHLYFYSVGLSYKKADAEVRGQFSLDAVAKTRLLEQAKNDGIESLLVTSTCNRTEIYGFAEHPFQLIKLICDNSNGSVDAFQKVGFVYKNQEAINHMFRVGTGLDSQILGDFEIISQIKTSFTHSKSMGLANAFMERLVNAVIQASKRIKTETEISSGATSVSFASVQYILKNVEDISNKNILLFGTGKIGRNTCENLVKHTKNEHITLINRTKDKAEKLAGKLNLIVKDYSELHLELQKADVVVVATGAQNPTVDKAILNLKKPLLILDLSIPKNVNENVEELEGVTLIHMDYLSQLTDETLENRKLHIPAAEAIIEEIKEEFVTWMKGRKFAPTINALKEKLNAIKASELDFQSKKIADFNEEQAEIISNRIIQKITTHFANHLKDDDTMVDESIEWIEKVFKIKAS
|
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
|
A5FLE3
|
A1AU58
|
DDL_PELPD
|
D-alanylalanine synthetase
|
Pelobacter
|
MNDIRSRKIAVLMGGLSAEREVSLASGAAVCQALVARGFDALSVDVARDLPLVLSREGIGAAFIALHGRYGEDGCVQGLLELMAIPYTGSGVLASALAMHKLYSKQAFVSAGILTAPFHHFRRGERVSLSHLSFGLPLVVKPVQEGSSVGISIVKEESQLAAAVKLAFRHDDEILVEQFIKGQEVQVGILDDRPMGAIEIVSRNEFYDFEAKYTDGMAEHFFPARLEKGLYEEALRVGLAAHHALGCRCYSRVDLLVTPAGECYVLEVNTLPGMTALSLLPEIAAKGADLPFEELVERIILSADLSVKTG
|
Cell wall formation.
|
A1AU58
|
Q85FW3
|
RK3_CYAM1
|
50S ribosomal protein L3, chloroplastic
|
Cyanidioschyzon
|
MSLLMSLLATKIGMSQLFDEKGNALPVTWVKSGVHEVIDHRTPEKHGYTALVVRYQHWIREFRVKHLSAYPIGRRLDLSTCFQIGQKVSVKAKTIGKGFAGYQKRHHFARGPMSHGSKNHRQPGSIGAGTFPGRVFPGTRMAGRLGGNFCTIKGLEILQIQNDQMALKGAVPGKVGNLLRIE
|
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
|
Q85FW3
|
Q91V13
|
LEAP2_MOUSE
|
Liver-expressed antimicrobial peptide 2
|
Mus
|
MLQLKLFAVLLTCLLLLGQVNSSPVPEVSSAKRSRRMTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE
|
Has an antimicrobial activity.
|
Q91V13
|
Q8P1C8
|
ENGB_STRP8
|
Probable GTP-binding protein EngB
|
Streptococcus
|
MAEEQVLNTHNASILLSAANKSHYPQDDLPEIALAGRSNVGKSSFINTILGRKNLARTSSKPGKTQLLNFFNIDDKLRFVDVPGYGYAKVSKSERAEWGKMIEEYLTSRDNLRAVVSLVDLRHAPSKEDIQMYDFLKYYDIPVIVVATKADKIPRGKWNKHESVVKKALNFDKSDTFIVFSSVERIGIDDSWDAILEQV
|
Necessary for normal cell division and for the maintenance of normal septation.
|
Q8P1C8
|
A4FYA5
|
PSB_METM5
|
Proteasome core protein PsmB
|
Methanococcus
|
MISNSEYHKEYMKGTTTVGLLCKDGVVLATDKRATMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQSLIRIISAEAKIHKMRTGNNMTPLSCTTLISNVLHGNRHYPLLTQLILGGYDLINGAKLFSLDPVGGINEESSFTATGSGSPTAYGVLEAEYRSDVTIDKGLLVAVKALSSAMQRDAYSGNGISLAHINKDGVKLYSDAEIEGFLKKINKKR
|
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
|
A4FYA5
|
P26223
|
XYNB_BUTFI
|
1,4-beta-D-xylan xylanohydrolase B
|
Butyrivibrio
|
MNLKTAYEPYFKIGAAISRWNLHTPAHTKLLAEQFNSFTCENDMKPMYYLDREANKKDPEKYNLSPALTFENAIPYLEFAKDNKIAMRGHTLVWHNQTPKWFFCERYNENFPMADRETILARLESYIHGVLDFVQTNYPGIIYAWDVVNEIVDEGAFRKSIWTETVGEDFFIKAFEFARKYAAPEVSLFYNDYETAQPWKRDFILEKVLGPLIDKKLIDGMGMQSHLLMDHPDISEYRTALEMYGSTGLQIHITELDMHNADPSEESMHALATRYQEFFQTYLDAKKSGKANITSVTFWNLLDENSWLSGFRRETSYPLVFKGKCEAKEAYYAVLKAAVSDDSIDKWVPDYSEEDYKLQGMPTPDIKRFRENIWQENEYNYEASYGFIPNLFAYLHNDDVKRDCMLVIPGGGYCMCCSHEGELAAMEFYNRGMNAFVLSYTTDITMSVPLHKQPLEDISRAVRFIRKNASKYNIDGKKLVIMGFSAGSHVCGSLAVHFDDVKDNNPEYADISGRPDGVILSYPVITTGRYTHADSVRTLLGANPTDEELTYFSLEKQVKDNTPPCFIWQTEEDSVVPVENSYLFANALREKKIPFAHYVFPRGFHGLTVANDEFFSGWSGGEYSMEQTMRARFAV
|
B.fibrisolvens is located in the rumen of ruminant animals, where it contributes to the animal's digestion of plant material by hydrolyzing hemicellulose with its xylanases.
|
P26223
|
Q5LNP2
|
ATPE_RUEPO
|
F-ATPase epsilon subunit
|
Ruegeria
|
MANTMQFDLVSPERLLASLQVSAVQIPGADGDMTAMPDHAPTITTLRPGVLKVEGPEGTSEYLVTGGFAQIGADSLSVLAEKAIPVTEVTRAHLDELIAEARSSHEAAKGQEHTSVVDDAAKLLADMEALGTHMGL
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
Q5LNP2
|
Q9LE63
|
MY106_ARATH
|
Transcription factor NOEK
|
Arabidopsis
|
MGRSPCCDKAGLKKGPWTPEEDQKLLAYIEEHGHGSWRSLPEKAGLQRCGKSCRLRWTNYLRPDIKRGKFTVQEEQTIIQLHALLGNRWSAIATHLPKRTDNEIKNYWNTHLKKRLIKMGIDPVTHKHKNETLSSSTGQSKNAATLSHMAQWESARLEAEARLARESKLLHLQHYQNNNNLNKSAAPQQHCFTQKTSTNWTKPNQGNGDQQLESPTSTVTFSENLLMPLGIPTDSSRNRNNNNNESSAMIELAVSSSTSSDVSLVKEHEHDWIRQINCGSGGIGEGFTSLLIGDSVGRGLPTGKNEATAGVGNESEYNYYEDNKNYWNSILNLVDSSPSDSATMF
|
Functions as a repressor of epidermal cell outgrowth and negatively regulate trichome branch formation . Acts as both a positive and negative regulator of cellular outgrowth. Promotes both trichome expansion and branch formation . Coordinately with WIN1/SHN1, participates in the regulation of cuticle biosynthesis and wax accumulation in reproductive organs and trichomes. Functions in cuticle nanoridge formation in petals and stamens, and in morphogenesis of petal conical cells and trichomes . May play a role in the regulation of cuticle formation in vegetative organs .
|
Q9LE63
|
Q09504
|
YQI2_CAEEL
|
Uncharacterized tRNA-dihydrouridine synthase-like protein C45G9.2
|
Caenorhabditis
|
MVRYSKLAFRQLVRVYDVDVCFTPMIYAKNFIESEKCRSSELSVCEGDSPLIVQFATDDPFVLSEAAEMVYKCSTGVDLNCGCPKHDVRSKGFGSALLSKPELLADMVRQTRARIPDPDFSVSLKIRINHDIEKTVDLCRKAEAAGVTHLTVHGRTPSQRAEPIDIQALRIVKDSVSVPIIANGGITTREEALFLAEQTGVDGIMAANGLLDNPALFAGHEHTPSDCVENFMRLSREYGLDWLLYHQHLQYMLRPVFSAQQRRVFNELNGRLAIDHFLNNLLDI
|
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs.
|
Q09504
|
A9MCK4
|
DADA_BRUC2
|
D-amino acid dehydrogenase
|
Brucella
|
MQITILGSGVIGVTTAYYLAKLGHEVTVIDREEGPAPETSFANAGQVSPGYASPWAAPSIPLKAAKWLFQKHAPLILRLTTDPVQYRWLLQMLANCTDSRYKINKTRMVRVAEYSRDCLIELRKDTGIEYDQRSQGTLQLFREQYQLDGIGKDIEVLRQDGVPFEVLDRDGCVNVEPALAHAKDKFVGGLRLPNDETGDCFKFTNALAKIAEGLGVKFRFGVNIKSLLMSGGKISGVETSEGIVTAERYVVALGSYTPALIKALGLNAPIYPVKGYSITAPIVDESRAPVSTVLDESYKIAITRLGDRIRVGGMAEVSGFTDDLPAARRATLDLSVTDLFPGGDLKAATFWSGLRPMTPDSTPIIGGTRYDNLFINAGHGTLGWTMACGSGRLLADLISGNKADIRADDLGIARYN
|
Oxidative deamination of D-amino acids.
|
A9MCK4
|
Q97SQ2
|
DPO3_STRPN
|
DNA polymerase III PolC-type
|
Streptococcus
|
MSNSFEILMNQLGMPAEMRQAPALAQANIERVVVHKISKVWEFHFVFSNILPIEIFLELKKGLSEEFSKTGNKAVFEIKARSQEFSNQLLQSYYREAFSEGPCASQGFKSLYQNLQVRAEGNQLFIEGSEAIDKEHFKKNHLPNLAKQLEKFGFPTFNCQVEKNDVLTQEQEEAFHAENEQIVQAANEEALRAMEQLEQMAPPPAEEKPAFDFQAKKAAAKPKLDKAEITPMIEVTTEENRLVFEGVVFDVEQKVTRTGRVLINFKMTDYTSSFSMQKWVKNEEEAQKFDLIKKNSWLRVRGNVEMNNFTRDLTMNVQDLQEVVHYERKDLMPEGERRVEFHAHTNMSTMDALPEVEEIVATAAKWGHKAVAITDHGNVQSFPHGYKAAKKAGIQLIYGMEANIVEDRVPIVYNEVEMDLSEATYVVFDVETTGLSAIYNDLIQVAASKMYKGNVIAEFDEFINPGHPLSAFTTELTGITDDHVKNAKPLEQVLQEFQEFCKDTVLVAHNATFDVGFMNANYERHDLPKISQPVIDTLEFARNLYPEYKRHGLGPLTKRFGVALEHHHMANYDAEATGRLLFIFIKEVAEKHGVTDLARLNIDLISPDSYKKARIKHATIYVKNQVGLKNIFKLVSLSNTKYFEGVPRIPRTVLDAHREGLILGSACSEGEVFDVVVSQGVDAAVEVAKYYDFIEVMPPAIYAPLIAKEQVKDMEELQTIIKSLIEVGDRLGKPVLATGNVHYIEPEEEIYREIIVRSLGQGAMINRTIGHGEHAQPAPLPKAHFRTTNEMLDEFAFLGEELARKLVIENTNALAEIFESVEVVKGDLYTPFIDKAEETVAELTYKKAFEIYGNPLPDIVDLRIEKELTSILGNGFAVIYLASQMLVQRSNERGYLVGSRGSVGSSFVATMIGITEVNPLSPHYVCGQCQYSEFITDGSYGSGFDMPHKDCPNCGHKLSKNGQDIPFETFLGFDGDKVPDIDLNFSGEDQPSAHLDVRDIFGEEYAFRAGTVGTVAAKTAYGFVKGYERDYGKFYRDAEVERLAQGAAGVKRTTGQHPGGIVVIPNYMDVYDFTPVQYPADDVTAEWQTTHFNFHDIDENVLKLDVLGHDDPTMIRKLQDLSGIDPNKIPMDDEGVMALFSGTDVLGVTPEQIGTPTGMLGIPEFGTNFVRGMVDETHPTTFAELLQLSGLSHGTDVWLGNAQDLIKQGIADLSTVIGCRDDIMVYLMHAGLEPKMAFTIMERVRKGLWLKISEEERNGYIEAMKANKVPEWYIESCGKIKYMFPKAHAAAYVMMALRVAYFKVHHPIYYYCAYFSIRAKAFDIKTMGAGLEVIKRRMEEISEKRKNNEASNVEIDLYTTLEIVNEMWERGFKFGKLDLYCSQATEFLIDGDTLIPPFVAMDGLGENVAKQLVRAREEGEFLSKTELRKRGGLSSTLVEKMDEMGILGNMPEDNQLSLFDELF
|
Required for replicative DNA synthesis. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
|
Q97SQ2
|
P96065
|
PHNV_SALTY
|
Putative 2-aminoethylphosphonate transport system permease protein PhnV
|
Salmonella
|
MLIWSPKGRAAAGVVASVLFIVFFFLPLAVILMSSLSQQWNGILPSGFTLNHFVNALHGAAWDALLASLTIGFCASLFALLCGVWAALALRQYGVKTQKWLSMVFYLPSAIPSVSVGLGILVAFSQGPLQMNGTLWIVLTAHFVLISAFTFSNVSTGLARISADIENVASSLGASPWYRLRHVTLPLLMPWMMSALALSLSLSMGELGATMMIYPPGWTTLPVAIFSLTDRGNIADGAALTIVLVAITLLLMMKLERIAKRLGQK
|
Probably part of the PhnSTUV complex (TC 3.A.1.11.5) involved in 2-aminoethylphosphonate import. Probably responsible for the translocation of the substrate across the membrane.
|
P96065
|
O46427
|
CATH_PIG
|
Cathepsin H light chain
|
Sus
|
MWAVLSLLCAGAWLLGPPACGASNLAVSSFEKLHFKSWMVQHQKKYSLEEYHHRLQVFVSNWRKINAHNAGNHTFKLGLNQFSDMSFDEIRHKYLWSEPQNCSATKGNYLRGTGPYPPSMDWRKKGNFVSPVKNQGSCGSCWTFSTTGALESAVAIATGKMLSLAEQQLVDCAQNFNNHGCQGGLPSQAFEYIRYNKGIMGEDTYPYKGQDDHCKFQPDKAIAFVKDVANITMNDEEAMVEAVALYNPVSFAFEVTNDFLMYRKGIYSSTSCHKTPDKVNHAVLAVGYGEENGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLAACASYPIPLV
|
Important for the overall degradation of proteins in lysosomes.
|
O46427
|
A8I3B5
|
RNC_AZOC5
|
Ribonuclease III
|
Azorhizobium
|
MSETQDFAALEARLGHSFADRSHLVLALTHISSVKGQAVRVRSYQRLEFLGDHVLGSVVSHMLYAAFPKAEEGELSRRLAELVREEACAEVAQDMGLGPYLRLGPGEAQSGARQRRAILADVAEAVVAAVYLDGGYEAASALVERFWRGRLEAPRRPLRDPKTVLQEWAQARGLPPPVYRDVERSGPDHAPRFRVAVDLPGLECAEAEGGSKQTAQKAAASAFLAREGVVTESGE
|
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.
|
A8I3B5
|
P46161
|
DEFB3_BOVIN
|
BNDB-3
|
Bos
|
LALLFLVLSAGSGFTQGVRNHVTCRINRGFCVPIRCPGRTRQIGTCFGPRIKCCRSW
|
Has bactericidal activity. Active against E.coli ML35 and S.aureus 502A.
|
P46161
|
Q6GFY8
|
RS4_STAAR
|
30S ribosomal protein S4
|
Staphylococcus
|
MARFRGSNWKKSRRLGISLSGTGKELEKRPYAPGQHGPNQRKKLSEYGLQLREKQKLRYLYGMTERQFRNTFDIAGKKFGVHGENFMILLASRLDAVVYSLGLARTRRQARQLVNHGHILVDGKRVDIPSYSVKPSQTISVREKSQKLNVIVESVEINNFVPEYLNFDADSLTGTFVRLPERSELPAEINEQLIVEYYSR
|
With S5 and S12 plays an important role in translational accuracy.
|
Q6GFY8
|
Q9UPY8
|
MARE3_HUMAN
|
RP3
|
Homo
|
MAVNVYSTSVTSENLSRHDMLAWVNDSLHLNYTKIEQLCSGAAYCQFMDMLFPGCVHLRKVKFQAKLEHEYIHNFKVLQAAFKKMGVDKIIPVEKLVKGKFQDNFEFIQWFKKFFDANYDGKDYNPLLARQGQDVAPPPNPGDQIFNKSKKLIGTAVPQRTSPTGPKNMQTSGRLSNVAPPCILRKNPPSARNGGHETDAQILELNQQLVDLKLTVDGLEKERDFYFSKLRDIELICQEHESENSPVISGIIGILYATEEGFAPPEDDEIEEHQQEDQDEY
|
Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton . Promotes microtubule growth . May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes . Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement . Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules .
|
Q9UPY8
|
Q7SHZ2
|
GATA_NEUCR
|
Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial
|
Neurospora
|
MSARIGRLRGLCLRHVSSTRQTSPIQRRSLNQFISRVQQHDQPALEQRQFRLAVKDNIATVSPNSEEETPLTTTCGSNFLANYRSPFEATIVSQLRSRGALLVGKTNLDEFGMGSHSVHTAFGAVAQEGEHEQQAVKHSAGGSSGGSAVAVATGEADIALGTDTGGSVRLPAGYTGVVGFKPSYGMLSRYGVVPYANSLDTVGLLAKEVRPIAELILGGADKVTRGLWAEHDPLDPTSLSHGARRRCASQRDCYTGPLPKDPYPLKNLKFGLPLEYNITELSPSIRHSWSAAAAKLQSLGARLVPVSLPSTRHALSAYYVIAPAEASSNLAKYDGIRYGTRFTSPTESDAAISEGPEGREEEEEGILYARARTAGFGDEVKRRILLGAYTLSSAAMDNYFLKAQKVRRLVRRDFNRVFALPNPLLDKPERFELSELPETVGLEDKWGPTEVDFLLCPTAPTTAPRLDEVLSEEEKDPVSAYMNDVFTVPASLAGLPAISVPMRVEDKEGAGMAGLQLIGQYWDDARLLAVAETVADVVREEL
|
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
|
Q7SHZ2
|
C5CJH0
|
THIG_VARPS
|
Thiazole synthase
|
Variovorax
|
MTTASAIPDNDPLVLYGQTFHSRLLLGTARYPSPDLLEAAVKRAKPAMLTASLRRQSASPGASDSGNGFWELLRRLAVPVLPNTAGCHSVQEVIATAQMARELFDTPWIKLELIGDDYTLQPDTLNLVDAASQLIRDGFQVLPYCTEDLVLCQRLVDVGCQAVMPWAAPIGTGRGPVNPYALQLLRERLSVPMLVDAGLGLPSHACQVMEWGYDGVLLNTAVALAQDPVSMAGAFADAVQAGRAAHRAGAMAAQDSAQPSTPVLGTPFWHHAP
|
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
|
C5CJH0
|
P63085
|
MK01_MOUSE
|
Mitogen-activated protein kinase 2
|
Mus
|
MAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
|
Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity.
|
P63085
|
Q0ID34
|
RF1_SYNS3
|
Peptide chain release factor 1
|
unclassified Synechococcus
|
MDTTTLISRLEAASSSFHNLERQLADPDVAADPQRLETIARERSRLEPLVLDYTSLQKVEAEQVQAKSLLKESRGDAAMEELAQQELQELDRHHADLIQRITLALLPKDPRDERSVMLEIRAGAGGDEACLWAGDLARMYERFSSRRGWSVTPVSANEADLGGYKELILSVKGDAVFSELKFEAGVHRVQRVPSTESQGRVHTSTATVAVMPEADPVEVQIDPRDLDISTARSGGAGGQNVNKVETAVDLMHKPTGIRVFCTQERSQMQNRERALEILRAKLYERQLAEANASERSARRSQVGTGDRSEKIRTYNAKDNRMTDHRLGRNFSLDPVLEGQMDDVIDACIAEEQRGKLADLSEQAD
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
Q0ID34
|
B3EK39
|
PYRG_CHLPB
|
UTP--ammonia ligase
|
Chlorobium
|
MARPKNVKHIFVTGGVVSSLGKGILSASLGLLLKSRGLRVAIQKYDPYINVDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFLDEPTSQASNLTMGRVYKAVIDKERQGEYLGGTVQVVPHVIDEIKAKMNELAKNANLDVLITEIGGTIGDIESLPFLEAMRQLKLDLGTKNLLNIHLTLVPYIKAACEMKTKPTQHSVKMLLETGIQPDILVCRSEKPLSREIKNKVGHFCNLHEADVIGLSDCETIYGVPIMLLDEQLDKRVLKKLGIKKFQDPELSYWTEFCDKVKHPEDGEVTIAVCGKYTEYPDAYKSILESFVHAGAVNNVKVTVRFIRSEDAEESGCDIATAMKDVHGLLVAPGFGDRGIEGKISFIRYARENNIPFLGICLGMQCATIEFARNVCGLSEANSTEFSKRCRQPVIDLMEHQKKVKEKGGTMRLGSYPCILKEDTIANKAYGKFLINERHRHRYEFNNEYRELLEQNGMLFSGTSPNGDLVEIIEISGHPWFVGVQFHPEYKSRVRSAHPLFVGFVAAAKAFAFGDRQLSFEPDTLPLGEPERTLEG
|
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.
|
B3EK39
|
B2S679
|
RL3_BRUA1
|
50S ribosomal protein L3
|
Brucella
|
MRSGVIAQKLGMTRVYNDAGEHVPVTVLRMENCHVVAQRTVEKNGYTAVQLGVGMAKVKNTSKAMRGHFAKAEVEPKAKLAEFRVSPDNLLEVGVEITAEHFVAGQKVDVTGTSIGKGFAGVMKRHNFGGHRASHGNSITHRSHGSTGQRQDPGKVFKGKKMAGHMGQTRVTTQNIEVVSTDSDRGLILVRGAVPGSKGAWILVRDAVKASLPENAPKPAGLRAGAKAEAAATEGGE
|
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
|
B2S679
|
B3PK52
|
RL6_CELJU
|
50S ribosomal protein L6
|
Cellvibrio
|
MSRVAKSPVEVPAAVTVTLNGQSLSVKGGKGTLALEVHANVEVKHEGNVLTFTPRDGAKQSDALAGTTRALVNNMVVGVSQGFEKKLTLVGVGYRVKAEGNTVNLSLGYSHPVNYVLPQGVSVETPSQTEIVLKSADKQLLGQVAAEIRAFREPEPYKGKGVRYSDEVVLRKEAKKK
|
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
|
B3PK52
|
B6I9D2
|
TRHO_ECOSE
|
tRNA hydroxylation protein O
|
Escherichia
|
MPVLHNRISNDALKAKMLAESEPRTTISFYKYFHIADPKVTRDALYQLFTALNVFGRVYLAHEGINAQISVPASNVETFRAQLYDFDPALEGLRLNIALDDDGKSFWVLRMKVRDRIVADGIDDPHFDASNVGEYLQAAEVNAMLDDPDALFIDMRNHYEYEVGHFENALEIPADTFREQLPKAVEMMQAHKDKKIVMYCTGGIRCEKASAWMKHNGFNKVWHIEGGIIEYARKAREQGLPVRFIGKNFVFDERMGERISDEIIAHCHQCGAPCDSHTNCKNDGCHLLFIQCPVCAEKYKGCCSEICCEESALPPEEQRRRRAGRENGNKIFNKSRGRLNTTLGIPDPTE
|
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first step in 5-carboxymethoxyuridine (cmo5U) biosynthesis. May be part of an alternate pathway, which is able to bypass cmo5U biogenesis in a subset of tRNAs under aerobic conditions.
|
B6I9D2
|
A0A2K1J5A5
|
SOK3_PHYPA
|
Protein SOSEKI 3
|
Physcomitrium
|
MARGEDSSSVQVLYQLSWDGKLEHPHMIEVHYPPNQGGLRLRDVKKRLTTLRGHGINDSFSWSSKRNYKNEFIWNDLCDDDVIQPLRGSGEYVLRASELFDTFTNKPWEHPSKHSNERMQSSRTMSVDNVTLQQGLINVKLHSGALAREDDQPSGEKLCCSGRRSCINLEDCSSKGVAIDIPKNLQNLSVDQETIDVEKSDFCLSSSDNEVSPRLKTAADCITPVKDVGLVVMTRSTTVHGLHTPAPRSLTSPTEPPFSPGSAKRMWKKEIRKSLFRTSRNSSNVNPVLSGENAALDVDVPPITLSTQEDVSFWRDGRSKSASPSSLNELREVQNEKEKEAEQSTSQLIRLLWARWTGGSSKGKRTPQSTCEDPLPKSPEAKQMPRSRTKTPCKEIRSTNHIAGSLPVTCPSPAVDNKAHSSLDRQEIPPQEECKNRPSPMTLQSCEEITSPVTEIEQDVEIGDIKAIVEEQASNKFPEPEFQQNLRTEQIVLSVQIPDLHIDALDSPTSDTQGSPAEADIPKSATARVKTSNSLPRVKTTTSPKPLPPGFHKGTNDTKPVQIITPRRTPRTSIPLASPPPLVRTFNRVSVRSLSSIAAITLSPENDSAASNLSPENPIVKKRINFRERDEMPLIPGLTTLDWEKALQEAVTDCLPPPNFREILQECSTCGRTFKPDSLQVHMRGCHPPQYARAFSARASPHVVRSRAS
|
SOSEKI proteins locally interpret global polarity cues and can influence cell division orientation to coordinate cell polarization relative to body axes.
|
A0A2K1J5A5
|
Q13UB5
|
ANMK_PARXL
|
AnhMurNAc kinase
|
Paraburkholderia
|
MAQDPADGVYFGLMSGTSMDGVDGVAVRFAQGKPSVVLAEAFVGFAAGLRDALFALQQPGDNEIEREALAANALATRYAVCCHDLLHNSRVPAAEVRAIGVHGQTVRHRPEKGYTRQINNPALLAEMMHIDVIADFRSRDVAAGGQGAPLVPAFHATVFGAKNETRVVCNLGGISNITILNATGSVRGFDCGPANALLDEWAQRHLGKPFDENGHFAAGGQVDRTLLNALLDEPFFGQQPPKSTGRDLFNADWLDAKLPPFAALDHADVQATLVALTAVTVAREIERHASDAKAVYVCGGGARNPEILKALQQALEDSGVSGVPVMTTDALGVPPSQVEPLAFAWLAMRCVARLPGNLPAVTGASAERVLGAIYPR
|
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
|
Q13UB5
|
Q0C0Y0
|
RF2_HYPNA
|
Peptide chain release factor 2
|
Hyphomonas
|
MSAEIRSLIEKIESSAALLRRRLDWDTATKRLDELTALSERPNFWDDPQEAQAMMRERQKLADGIALVQTLEKDVADAPELMELAEGDASMLADLEATLRRAAARAAEAELAALLSGEADGNDCYLQINAGEGGTESQDWASILRRMYVRWAEKRGYGVELLDERDGEEAGIKSATLQIKGENAYGWLKSEQGVHRLVRISPFDSSARRHTSFSSVAVSPVIDDKIDVEINPSDVRTDTYRASGAGGQHVNRTDSAVRLTHIPTNTVVQCQAGRSQHQNRDEAWKMLRSKLYELELQKRRAVADAQYADKSAIGFGHQIRSYVLQPYQMVKDLRTEVETSDTSGVLDGDIDRFLSAALAASVSKDQDA
|
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
|
Q0C0Y0
|
B8DCW3
|
RHAD_LISMH
|
Rhamnulose-1-phosphate aldolase
|
Listeria
|
MTKDIMDAVFIKEMAKTTSNLYRLGWDERNGGNITYLLDEKEVVEYLDVKQIIRTIPMDFDGEKLAGKYFLVTGSGKYFKNVEEAPAVNLGVIQVSEDGKAVHLLWGYTDGGLPTSELPAHFMSHIARLSVDPENRVVMHCHATHLLAMTFTHELTEREFTRTLWQMCTECLVVFPEGVGIIPWLVPGTNEIGEATSEKMKENRLIVWPHHGIYGAGKSMDETFGLIETAEKAAEVYTIVMSQGGIKQAITDEQLKALGERFSVEAKAGYLNN
|
Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
|
B8DCW3
|
Q21MH7
|
RSMH_SACD2
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Saccharophagus
|
MNESPHFSVLLQESVESLVVDPAGTYVDGTFGRGGHSRAILAKLGPEGKLFGIDKDPEAVAVGKALEAEDSRFRIVHGSFADLKHIDLLQADFAAGGLSGVLVDLGVSSPQLDVAERGFSFMNDGPLDMRMNTEAGMTAAEWINTAKQEDIAQVLWEYGEERFSRHMAKAIVERREIKPFTRTHDFAEVVKAANRKWEKGKHPATRAFQAVRIFINRELEDLRQLLDDSVSVLAPGGRFVVISFHSLEDRMVKRFFRDQSMGKQFPKGLPVTEEMKKQNLKIIGKALKAGDTELTQNIRSRSAVMRVGERLG
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
Q21MH7
|
Q17VC7
|
CH10_HELAH
|
Chaperonin-10
|
Helicobacter
|
MKFQPLGERVLVERLEEENKTSSGIIIPDNAKEKPLMGVVKAVSHKISEGCKCVKEGDVIAFGKYKGTEIVLDGTEYMVLELEDILGIVNAGSCCHANSHDHKDHKHAEACCHDHKKH
|
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
|
Q17VC7
|
P44466
|
DACA_HAEIN
|
Penicillin-binding protein 5
|
Haemophilus
|
MLKRTTKIAFLSSFVALSAFSVSAEDMQFGVTPPQITAQTYVLMDYNSGAILTALNPDQRQYPASLTKMMTSYVVGVALKQGKIHNTDMVTIGESAWGRNFPDSSKMFLDLNTQVSVADLNRGVIVVSGNDATVALAEHISGNVPNFVETMNKYVQQFGLKNTNFTTPHGLDDPNQYSSARDMAIIGAHIIRDLPEEYKIYSEKNFTFNKIKQANRNGLLWDKTINVDGMKTGHTSQAGYNLVASATTSNNMRLISVVMGVPTYKGREVESKKLLQWGFANFETFKTLEAGKEISEQRVYYGDKNSVKLGALMDHFITIPKGKQSEVKARYELADKNLQAPLVKGQVIGKVVYQLDGKDIASANLQVMNDVGEAGIFGKLWDWLVLTVKGLFS
|
Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
|
P44466
|
Q3KKS6
|
MIAA_CHLTA
|
Isopentenyl-diphosphate:tRNA isopentenyltransferase
|
Chlamydia
|
MSSSSSSGAATGFAVCSDPQKSFSKMFKRTVILLAGPTGSGKTAVSLKLAPLVDGEIISVDSMQVYQGMDIGTAKVSLADRKEVPHHLIDVCHVQESFNAVDFYYHAVQACQDILSRNKVPILVGGTGFYFHTFLSGPPSGPSPDFVLREQLTLEAQERGISALYQELELLDPVYAATITKHDKNKIIRALEIIRKTGSKVSSYAWQSTVNESKEYHCRGWLLSPDPELLRHNILERCDQMLEEGLLDEVQALLAAGIKGNSSASRAIGYREWIEFLDLGSPPDLFEITKQKFITNTWRYTKKQRTWFKRCSLFRELRPMGMTLDDMAKKIAQDYFLCG
|
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
|
Q3KKS6
|
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