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2.75k
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5.51k
AlphaFoldDB
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Q1RH88
SODF_RICBR
Superoxide dismutase [Mn/Fe]
belli group
MTYCDKSNQTSYPFVLPNLPYEKESFKPHFTAETFEYHHGKHHNAYVQNLNNLLKDKEELQKKNLEEIIDWSSQNQNIAIFNNAAQVWNHTFFWHSIKPNGGGKPSGKILKQINEDFGSFEEFCEQFKAEATGQFGSGWAWLVYHNNRLQIVKTANAGTPIANGMQPLLACDVWEHAYYIDYRNKRPDYVDIFIKHMINWEFVENNLTK
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 by successive reduction and oxidation of the transition metal ion at the active site.
Q1RH88
A1VJ32
RS5_POLNA
30S ribosomal protein S5
Polaromonas
MAKFQAKSQNDAPDDGLKEKMIAINRVTKVVKGGRILGFAALTVVGDGDGRVGMGKGKSKEVPAAVQKAMEEARRNMTKVSLKNGTLHHNVFGHHGAANVMMAPAPKGTGIIAGGPMRAVFEVMGITDIVAKSHGSSNPYNMVRATMDALKNSTTASDIAAKRGKSVEEIFG
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
A1VJ32
Q2YS95
NAGB_STAAB
Glucosamine-6-phosphate isomerase
Staphylococcus
MKVLNLGSKKQASFYVACELYKEMAFNQHCKLGLATGGTMTDLYEQLVKLLNKNQLNVDNVSTFNLDEYVGLTASHPQSYHYYMDAMLFKQYPYFNRKNIHIPNGDADDMNAEASKYNDVLEQQGQRDIQILGIGENGHIGFNEPGTPFDSVTHIVDLTESTIKANSRYFENEDDVPKQAISMGLANILQAKRIILLAFGEKKRAAITHLLNQEISVDVPATLLHKHPNVEIYLDDEACPKNVAKIHVDEMD
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Q2YS95
A8AU71
RECF_STRGC
DNA replication and repair protein RecF
Streptococcus
MWLKSLTLKHFRNYQDAEINFHSGLNIFLGQNAQGKTNILESIYFLALTRSHRTRSDKDFIHFQEKDLKVSGILEKKTGTIPLDIELTAKGRITKINHLKQNRLSDYIGAMNVVLFAPEDLQLIKGSPSLRRKFIDIELGQIKPIYLADLSNYNHVLKQRNSYLKNSQNIDENFLSVLDEQLIEYGCRVVKHRLDFLKKLEIFAQEKHLDISQKKETLTIDYLSSVPLQDIDSIEESFRLSLSKNRKRDLFKQNTGVGPHRDDIAFFINQMDANYGSQGQHRSVVLSLKLAEIKLIENITKESPILLLDDVMSELDNDRQLKLLETISQEIQTFITTTTLEHLKNLPKDIKIFEISNGNIK
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.
A8AU71
B5Z677
GLMM_HELPG
Phosphoglucosamine mutase
Helicobacter
MKIFGTDGVRGKAGVKLTPMFVMRLGIAAGLYFKKHSQTNKILIGKDTRKSGYMVENALVSALTSIGYNVIQIGPMPTPAIAFLTEDMRCDAGIMISASHNPFEDNGIKFFNSYGYKLKEEEEKAIEEIFHDEELLHSSYKVGESIGSAKRIDDVIGRYIVHLKHSFPKHLNLQSLRIVLDTANGAAYKVAPVVFSELGADVLVINDEPNGCNINEQCGALHPNQLSQEVKKYRADLGFAFDGDADRLVVVDNLGNIVHGDKLLGVLGVYQKSKNALSSQAIVATSMSNLALKEYLKSQDLELKHCAIGDKFVSECMRLNKANFGGEQSGHIIFSDYAKTGDGLVCALQVSALVLESKQASSVALNPFELYPQNLVNLNVQKKPPLESLKGYSALLKELDQLEIRHLIRYSGTENKLRILLEAKDEKLLESKMQELKEFFEGHLC
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
B5Z677
Q88VS1
RECO_LACPL
Recombination protein O
Lactiplantibacillus
MVTNFNGILLFRRDYRERDMLIKFLTAEYGKKMFFIRGARRRGFKMAAELLPFTMGEYVGDLRDQGLSYINSVKSVQYLEHISQDIALNAYATYVMNLMDVAFPDNQPVGRWYQQLTSALQLIDQDVAPALVANVVEIQLLQPFGVAPELRWCTVCGRSDLPLDYSESYGGLLCQQHWHLDPHRLHASPAAIFYLRQFSVLDLAKVHSIKVKPRTAAELRRILDEIYQNSVGVRLKSKRFIDQMGSWYQPLAPRKNED
Involved in DNA repair and RecF pathway recombination.
Q88VS1
P27132
ACT2_NAEFO
Actin II
Naegleria
VQALEVDNGSGMCKAGFAGDDAPGAVFPSIIGRPKQKSIMVGMGNKDAYVGDEVQSKRGILIFKYPIQHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFSVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLIEDSHGTCYSFNTTAERECQRDIKGKALLYCFDFEQEMKIAAESSSVEKLYELPDGNVITVGNERFRCPEVLFQPNFIGMEAAGVHETTFNSIGKCDIHIRKDLYGNVVLSGGTTMFEGIAERMTKELTNMAPASMKIKVVAPPERKYSVWIGGSILASLSTFQQMWITKEEYEDAGPGIVHRESF
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
P27132
Q88RK5
ENGB_PSEPK
Probable GTP-binding protein EngB
Pseudomonas
MQVKNPILGLCQKAKFALSAAKVEQCPDDQGYEVAFAGRSNAGKSSALNTLTHASLARTSKTPGRTQLLNFFSLDDERRLVDLPGYGYAKVPIPLKQHWQKHLEAYLGSRECLRGVILMMDVRHPMTDFDKMMLDWAKASSMPMHILLTKADKLTHGAGKNTLLKVQSEIRKGWGDGVTIQLFSAPKRLGVEDAYRVLADWMELEDKPVV
Necessary for normal cell division and for the maintenance of normal septation.
Q88RK5
Q1H2K1
RS4_METFK
30S ribosomal protein S4
Methylobacillus
MSRFTGPRLKVMRALGIDLPGLSRKTIEARPTPPGQHGAKNTRRKKSDFGVKLQEKQKLRFNYGLSEKQLRRLMVDARKGKSPTGETLLQLLERRLDNVVFRAGFAPTIAAARQLVTHRHVMLNGKSVNIPSIRVRVGDEISLKASSTKLPIVVETLANPPLTRPEWISWAEQSQQAKVAHLPAAEDVPFPVDVQQVVEYYANRL
With S5 and S12 plays an important role in translational accuracy.
Q1H2K1
Q81TU9
CPFC2_BACAN
Coproporphyrin III ferrochelatase 2
Bacillus cereus group
MKKKKIGLLVMAYGTPDSLDEVEAYYTHIRHGRKPSEEALQDLIGRYKAIGGISPLAKITKEQAHKLTDSMNNMFTEYEFNCYLGLKHTAPFIEDAVEEMKRDGIEQAISIVLAPHYSTFSIKAYNERAIRLSEEIGGPVIKPIDQWYDEPKFISYWADQIKETFTKIEDKEKAVVIFSAHSLPEKIIAAGDPYVEQLQHTADLIAAAANIQNYTIGWQSAGNTPDPWIGPDVQDLTRDLFEEYRYESFIYCPVGFVAEHLEVLYDNDYECKVVTDELNAAYFRPNMPNAQSTFIDCLATIVSRKMKEIVDKELILNNN
Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Q81TU9
Q2KCH7
CHEY_RHIEC
Probable chemotaxis protein CheY
Rhizobium
MSIAEKIKVLIVDDQVTSRLLLSDALTQLGFKQITSAGDGEQGMKIMTEQPHHLVISDFNMPKMDGIGFLQAVRTNPNTKKAAFIILTAQGDRALVQRAAQLGANNVLAKPFTIEKMKAAIEAVFGALK
Putative member of a two-component regulatory system.
Q2KCH7
A0B5L3
NEP1_METTP
16S rRNA (pseudouridine-N1-)-methyltransferase Nep1
Methanothrix
MISMLLADSELELVPREIVGYPAVRLNARKRNKSPAKSILDASLHHSAMRALPMGDRRGRPDIVHVFLLVALESVLNRVGQLRVYIHTRNNEMITIDPTTRIPKNYPRFVGLMESLFEKGSVPEREPLIVMQRDRDIGACIGEIPHEKVILLSPKGRRVRLSDYVKECDNALFILGGFPKGEFISDVLSEADDTISIYEESLSVWTVASEILVNYENHVLEASAPS
Methyltransferase involved in ribosomal biogenesis. Specifically catalyzes the N1-methylation of the pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA.
A0B5L3
Q8K2P2
FA83A_MOUSE
Protein FAM83A
Mus
MSRSRHVGKIRKRLEDVKNQWTRPARADFSDNESARLATDALLDGGPEAYWRALSQEGEVDFLSSAEAQYIQAQAKEPPDAPDSAGGAESGPRGLDSCSLQSGTYFPVASEGSEPALLHTWTLAEKPYLKEKSSATIYFQMDKHNNIRDLVRRCISRASQVLAILMDVFTDVEILCDILEAANKRGVFVCVLLDQGGVKLFQEMCDKVQISDIHLKNISIRSVEGEVYCAKSGRKFAGQIQEKFIISDWRFVLSGSYSFSWLCGHVHRNILSKFTGQAVELFDEEFRRLYASSKPLMGLKSPRLVAPFQPNKGPEAPNGRLSGTSDSASDRTSSNPFSSLSTGSNAHNQSLSTSSGPSSPLAPIPPTVPRLQPYHSTRRAVAPQPLLVPMRPHEGAPAPYSSLMAYRPTRLQLQQLGLVPRVTHPWRPFLQALPHF
Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both RAS/MAPK and PI3K/AKT/TOR signaling cascades downstream of EGFR. Required for the RAS/MAPK signaling cascade activation upon EGFR stimulation, it also activates both signaling cascades independently of EGFR activation.
Q8K2P2
Q5F831
RPIA_NEIG1
Phosphoriboisomerase A
Neisseria
MTTQDELKRIAAEKAVEFVPENEYIGIGTGSTINFFIEALGKSGKKIKGAVSTSKKSGELLARYDIPVVSLNEVSGLAVYIDGADEVNHALQMIKGGGGAHLNEKIVASASEKFVCIADESKYVSRLGKFPLPVEAVESARSLVSRKLLAMGGQPELRIGYTTFYGNQIVDVHGLNIDQPLTMEDEINKITGVLENGIFARDAADVLILGTEEGAKVIYPCQG
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Q5F831
B2HVF8
DCUP_ACIBC
Uroporphyrinogen decarboxylase
Acinetobacter calcoaceticus/baumannii complex
MTTLKNDRFLRALLREPVDTTPIWMMRQAGRYLPEYRETRSKAGDFLSLCKNTEFACEVTLQPLRRYDLDAAILFSDILTIPDALGLGLYFETGEGPKFHKTVRTEQDVANLPKLNAKADLDYVMNAVSTIRSALGGQVPLIGFSGSPWTLATYMVEGGSSKEFRFTKQMMYAQPEVLHALLDHLADSVIDYLNAQIDAGAQAIQIFDSWGGALAHREYVEFSLNYMNKIIAGLQREKDGRRIPVIVFTKGGGQWLEPMIASGADALGLDWTTPLNTARNVVSGRVALQGNLDPAVLYGSAASIEKAVKAMLDDAYANGEKTGYVANLGHGITQWVDPAQPKIFVDTVHEYSAKYLG
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
B2HVF8
B7VT10
RIBB_VIBA3
3,4-dihydroxy-2-butanone 4-phosphate synthase
Vibrio
MNQSSLLAEFGEPITRVENALQALREGRGVLLLDDEDRENEGDIIYSVEHLTNAQMALMIRECSGIVCLCLTDEQANQLELPPMVVDNNSANQTAFTVTIEAKVGVTTGVSAADRVTTIKTAANPTAKPTDLARPGHVFPLRARKGGVLARRGHTEGTVDLMQMAGLQSAGVLCEVTNPDGTMAKAPEIVAFGKMHNMPVLTIEDMVMYRTEFDLKLA
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
B7VT10
Q1QIJ1
RNH2_NITHX
Ribonuclease HII
Nitrobacter
MTRRNNGHSARFLVASASWFSHHSGMIREPSRDRPGRSPAVAPSFQHERALLKRGVWPVAGCDEVGRGPLAGPVVAAAVVLDPKRIPKGIDDSKRLTAARREELFEEITATASFAVAFASTARIDRDNILRASLWALARAVHALPDMPRHVFVDGRDRIEIACACEPVIGGDGIVLSIAAASIVAKVTRDRLMCKLAQDCPGYGFETHKGYGVPAHLEALGRLGPSPHHRSFFAPVVAARERHRAPPIGESASATETSAGISIEATI
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Q1QIJ1
A1APM0
PYRF_PELPD
OMP decarboxylase
Pelobacter
MNRDEARKKIIFALDVNGIAEIDRYAGLLSDRVGMFKIGKELFTACGPEAVATVRRHGGQVFLDLKYHDIPNTVAKAMLEAARLGVQLANLHALGGLEMMETAASAVRREFGDDRPRLLAVTILTSSTAETLRRVGIDHPVEEMVVRLACLAREAGMDGVVASPREIGLIRQACGPDFLIVTPGVRPSFASQDDQKRIMSPDDAVREGADYLVIGRPIAKADDPVRAVDMIVDEIVAGCP
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
A1APM0
B2S746
MNMA_BRUA1
tRNA-specific 2-thiouridylase MnmA
Brucella
MSLNSLDLPGKPEDTRVVVAMSGGVDSSVVAGILKREGYDVVGVTLQLYDHGAAVHRAGSCCAGQDIEDARRVSESLGIPHYVLDYEARFREAVIDPFANSYVSGETPIPCVSCNQTVKFADLLQTARDLGADALATGHYIRSRANGAHRALYRPVDTDRDQSYFLFATTQEQIDYLRFPLGHLPKAQVREIAEELGLTVAKKQDSQDICFVPQGKYSDIISRLKPEAANPGDIVHIDGRTLGRHDGIVHYTVGQRRGIGVATGEALYVVHLDAANARVIVGPREALETHKVFLRDVNWLGDTPIADLPKSGMEVFAKVRSTRPPRPAVLRHADGQTWVELVDGESGIAPGQACVLYSDDSNAARVFGGGFIGRSEREPQAEEMLRRLMANADKASAA
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
B2S746
Q8WXH2
JPH3_HUMAN
Trinucleotide repeat-containing gene 22 protein
Homo
MSSGGRFNFDDGGSYCGGWEDGKAHGHGVCTGPKGQGEYTGSWSHGFEVLGVYTWPSGNTYQGTWAQGKRHGIGLESKGKWVYKGEWTHGFKGRYGVRECAGNGAKYEGTWSNGLQDGYGTETYSDGGTYQGQWVGGMRQGYGVRQSVPYGMAAVIRSPLRTSINSLRSEHTNGTALHPDASPAVAGSPAVSRGGFVLVAHSDSEILKSKKKGLFRRSLLSGLKLRKSESKSSLASQRSKQSSFRSEAGMSTVSSTASDIHSTISLGEAEAELAVIEDDIDATTTETYVGEWKNDKRSGFGVSQRSDGLKYEGEWASNRRHGYGCMTFPDGTKEEGKYKQNILVGGKRKNLIPLRASKIREKVDRAVEAAERAATIAKQKAEIAASRTSHSRAKAEAALTAAQKAQEEARIARITAKEFSPSFQHRENGLEYQRPKRQTSCDDIEVLSTGTPLQQESPELYRKGTTPSDLTPDDSPLQSFPTSPAATPPPAPAARNKVAHFSRQVSVDEERGGDIQMLLEGRAGDCARSSWGEEQAGGSRGVRSGALRGGLLVDDFRTRGSGRKQPGNPKPRERRTESPPVFTWTSHHRASNHSPGGSRLLELQEEKLSNYRMEMKPLLRMETHPQKRRYSKGGACRGLGDDHRPEDRGFGVQRLRSKAQNKENFRPASSAEPAVQKLASLRLGGAEPRLLRWDLTFSPPQKSLPVALESDEENGDELKSSTGSAPILVVMVILLNIGVAILFINFFI
Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH3 is brain-specific and appears to have an active role in certain neurons involved in motor coordination and memory.
Q8WXH2
Q8R9D0
MUTS2_CALS4
Endonuclease MutS2
Caldanaerobacter
MKGMREKTLKSLEFDKIVKLIANECDSELGREKVFDIEIKKDLKAIEFELDLLNEAVKFIYSYGDISFSFQDIREHVKKAQIDYILYNRELLGIKNFLSLVEEVKAHFKSLYDREDFLLLKEFDKRLVPLKSLKEKIENTVISEDEISDEASPVLKAIRRQKASINEKIKSTLNSIISTRQKELQEPIITMRQGRYVVPVKQEYRNVFKGIIHDQSSTGATLFIEPIQVVDLNNELRELELKEQKEIERILFELSQEVKKNAEAIFKDVEVVSELDFLFAKARYSIKIKASRPELNTSGYVNLKKARHPLIDPEKVVPIDIHIGREFTTLVITGPNTGGKTVTLKTVGLLTLMAMAGINIPAEEKSQISIFEDVFVDIGDEQSIEQSLSTFSSHMTNIVSILKKVNKNSLVLLDELGAGTDPLEGSALAMSILDFLHRTGCRTIATTHYSELKQYALKTKGVENASVEFDVETLRPTYRLIIGIPGRSNAFEISRRLGLSEEIIENAKSYMSGEAIRFEDVIKDVEEKRKDLENAYQEVERLKKEVEVLKEELEKEKRKLESQKDKILKEAKEKAREIIKEAKQTAEEVIKRIKEAEEKEKNKDRAIQEIREKIKKNLEELEEEVLKPKEFSYGKIPDSLKAGQTVYIVPLDQNGIVLSPPDASGNVEVQAGILKMTVHISNLRVKEEQEQEEVKKGYSRFINEKAKSISPSLDVRGMTLDDALLEVEKYIDDAYLAGLNQVTIIHGRGTGVLRTGIAKFLRNSKYVKSFRLGRYGEGGDGVTIVELHSR
Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity.
Q8R9D0
P58366
ANKH_RAT
Progressive ankylosis protein homolog
Rattus
MVKFPALTHYWPLIRFLVPLGITNIAIDFGEQALNRGIAAVKEDAVEMLASYGLAYSLMKFFAGPMSDFKNVGLVFVNSKRDRAKAVLCMVVAGAIAAVFHTLIAYSDLGYYIINKLHHVDESVGSKTRRAFLYLAAFPFMDAMAWTHAGILLKHKYSFLVGCASISDVIAQVVFVAILLHSHLECREPLLIPILSLYMGALVRCTTLCLGYYRNIHDIIPDRSGPELGGDATIRKMLSFWWPLALILATQRISRPIVNLFVSRDLGGSSAATEAVAILTATYPVGHMPYGWLTEIRAVYPAFDKNNPSNKLANTNNTVTSAHIKKFTFVCMALSLTLCFVMFWTPNVSEKILIDIIGVDFAFAELCVIPLRIFSFFPVPVTVRAHLTGWLMTLKKTFVLAPSSVLRIIVLITSLVVLPYLGVHGATLGVGSLLAGFVGESTMVALAACYVYRKQKKKMENESATEGEDSAMTDMPPAEEVTDIVEMREENE
Regulates intra- and extracellular levels of inorganic pyrophosphate (PPi), probably functioning as PPi transporter.
P58366
Q6P9A3
ZN549_HUMAN
Zinc finger protein 549
Homo
MAEAALVITPQIPMVTEEFVKPSQGHVTFEDIAVYFSQEEWGLLDEAQRCLYHDVMLENFSLMASVGCLHGIEAEEAPSEQTLSAQGVSQARTPKLGPSIPNAHSCEMCILVMKDILYLSEHQGTLPWQKPYTSVASGKWFSFGSNLQQHQNQDSGEKHIRKEESSALLLNSCKIPLSDNLFPCKDVEKDFPTILGLLQHQTTHSRQEYAHRSRETFQQRRYKCEQVFNEKVHVTEHQRVHTGEKAYKRREYGKSLNSKYLFVEHQRTHNAEKPYVCNICGKSFLHKQTLVGHQQRIHTRERSYVCIECGKSLSSKYSLVEHQRTHNGEKPYVCNVCGKSFRHKQTFVGHQQRIHTGERPYVCMECGKSFIHSYDRIRHQRVHTGEGAYQCSECGKSFIYKQSLLDHHRIHTGERPYECKECGKAFIHKKRLLEHQRIHTGEKPYVCIICGKSFIRSSDYMRHQRIHTGERAYECSDCGKAFISKQTLLKHHKIHTRERPYECSECGKGFYLEVKLLQHQRIHTREQLCECNECGKVFSHQKRLLEHQKVHTGEKPCECSECGKCFRHRTSLIQHQKVHSGERPYNCTACEKAFIYKNKLVEHQRIHTGEKPYECGKCGKAFNKRYSLVRHQKVHITEEP
May be involved in transcriptional regulation.
Q6P9A3
Q30QP2
FMT_SULDN
Methionyl-tRNA formyltransferase
Sulfurimonas
MKIIFMGTPDYAAHILEKLLNTKNIEVVALYTQPDKPVGRKKILTPPAAKNIALKYGIAISQPSRLRDKETVAEVTSIECDYIVVAAYGQILPLEILKHAPCINLHASILPHYRGASPIQQTLLHGDVKTGVTAMLMNEGLDTGDILKIKEIEVDADEMSESLFSRLTEVASDLTIDVLENFVQYTPKIQDDSLSSHCKKITKQDGEVEFDNATAIFNKYRAFTPWPGIYLTSGLKLKKIELFEKESQNESGRILDIQKDSIIVGCKKGSIKVITLQPESKNEMSALSYINGKRLNIADTLS
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.
Q30QP2
Q9G5S9
COX2_TAMQA
Cytochrome c oxidase polypeptide II
Tamias
MAYPFELGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINDPSLTVKTMGHQWYWSYEYTDYEDLNFDSYMVPTSDLSPGELRLLEVDNRVVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQATLTSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKHFENWSSSML
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Q9G5S9
Q8DMM0
RL5_THEVB
50S ribosomal protein L5
Thermosynechococcus
MSQRLKDHYNKTVVPQLMQQFQYKNIHQVPKIVKVTVNRGLGEAAQNAKALEATLAEIATITGQKPVVTRAKKAIAGFKIRKGMPVGVAVTLRSERMYAFLDRLINLALPRIRDFRGVNPKSFDGRGNYTLGLREQLIFPEVNYDDIDQIRGMDVSIITTANTDEEGRALLKAMGMPFREN
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.
Q8DMM0
Q8D2Z5
FTSW_WIGBR
Peptidoglycan polymerase
Wigglesworthia
MNNKKKIVKIFFYDKILFFLLISLSIIGIIIVSSASISFGIRLHNDYFYFAKRNLLYFFLSFFLFFQIIRIPINQLEKYNKIALLINLFLLIIVFIIGNSINGAIRWIKIGFFSIQPSECSKLILFFYISDYIVKKNKELKNKLWGFLKPIIIMLIFVILLLMQPDLGNSLILFLTTLLLFFLAGINLWKCCFMFLFGLLTIFILIIFKPYRIRRILSFLDPWEDPFNSGYQLTQSLMALGRGKIIGTGLGNSIQKLEYLPEAYTDFIFSILGEELGYIGSIIILIMLFFVIFRIFLIGKNSFIQKKFFSGYFSFSVGIWISLQTIMNVGGVIGILPIKGLTLPFISYGGSSLITIFSAIAIVIRSDFELRINKYQAYLKQ
Peptidoglycan polymerase that is essential for cell division.
Q8D2Z5
Q7WJ81
LPXB_BORBR
Lipid-A-disaccharide synthase
Bordetella
MSLRIGMVAGEPSGDLLAGRIIAGLQARAPGVHCAGIGGPQMAARGFEAWHPMHALTVFGYIDAFKRIPSLLSTYGDVKRRLLAEPPSVFVGIDAPDFNLRLEHQLRQAGTPTVHFVGPSIWAWRYERINKIRAAVSHMLVLFPFEEALYRKEGIPVTYVGHPLAGVIPMQPDRAAARARLGIDADARVLAILPGSRSSEIRLLAPRFLQAAAELVRRDPRLQCVVPMVNPQRRAEFEAIAAQHPVPGLRCVTAAEGQGETPVAWSVMEASNAVLVASGTATLETALYKRPMVISYVLSPWMRRIMAWKSGQQRPYLPWVGLPNVLLRDFAVPELLQDEATPAALAEATWQALTDEAGAARIEARFTALHQDLLRDTPALAAQAILEVADGAA
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Q7WJ81
B2U513
NAGZ_SHIB3
N-acetyl-beta-glucosaminidase
Shigella
MGPVMLDVEGYELDAEEREILAHPLVGGLILFTRNYHDPAQLRELVRQIRAASRNHLVVAVDQEGGRVQRFREGFTRLPAAQSFAALLGMEEGGKLAQEAGWLMASEMIAMDIDISFAPVLDVGHISAAIGERSYHADPEKALAIASRFIDGMHEAGMKTTGKHFPGHGAVTADSHKETPCDPRPQAEIRAKDMSVFSTLIRENKLDAIMPAHVIYSDVDPRPASGSSYWLKTVLRQELCFDGVIFSDDLSMEGAAIMGSYAERGQASLDAGCDMILVCNNRKGAVSVLDNLSPIKAERVTRLYHKGSFSRQELMDSARWKASSTRLNQLHERWQEEKAGH
Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
B2U513
P04254
HCYA_PANIN
Hemocyanin A chain
Panulirus
DALGTGNAQKQQDINHLLDKIYEPTKYPDLKEIAENFNPLGDTSIYNDHGAAVETLMKELNDHRLLEQRHWYSLFNTRQRKEALMLFAVLNQCKEWYCFRSNAAYFRERMNEGEFVYALYVSVIHSKLGDGIVLPPLYQITPHMFTNSEVIDKAYSAKMTQKQGTFNVSFTGTKKNREQRVAYFGEDIGMNIHHVTWHMDFPFWWEDSYGYHLDRKGELFFWVHHQLTARFDFERLSNWLDPVDELHWDRIIREGFAPLTSYKYGGEFPVRPDNIHFEDVDGVAHVHDLEITESRIHEAIDHGYITDSDGHTIDIRQPKGIELLGDIIESSKYSSNVQYYGSLHNTAHVMLGRQGDPHGKFNLPPGVMEHFETATRDPSFFRLHKYMDNIFKKHTDSFPPYTHDNLEFSGMVVNGVAIDGELITFFDEFQYSLINAVDSGENIEDVEINARVHRLNHKEFTYKITMSNNNDGERLATFRIFLCPIEDNNGITLTLDEARWFCIELDKFFQKVPKGPETIERSSKDSSVTVPDMPSFQSLKEQADNAVNGGHDLDLSAYERSCGIPDRMLLPKSKPEGMEFNLYVAVTDGDKDTEGHNGGHDYGGTHAQCGVHGEAYPDNRPLGYPLERRIPDERVIDGVSNIKHVVVKIVHHLEHHD
Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
P04254
Q4J978
DHYS_SULAC
Probable deoxyhypusine synthase
Sulfolobus
MKREDLLTNVVDDLSLEDLRDLKNLEIIFDKVYGFSAENVVKAVEILRDLIKEADLRFLSFTANLVSTGLRGLLADLIRREYFNVVITTGGTIDHDIARSFGGKYYKGSFEFDDTMLKELEIHRLGNIFIPFENYGKVIEEVVRKYIPEIVSVRKDWSVYELLWEFGKRINDQHSILKACYEKKVPLIVPGVVDGSFGTNLFIVSQFNGLKIDLFQDMRLIKDLIFSSEKSGALIIGGGISKHHTIWWNQFKDGLDYAIYITTAQEYDGSLSGARPREAISWNKVRPSARSVTIYADATIILPILSASLLR
Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Q4J978
P36442
PSBE_MESCR
PSII reaction center subunit V
Mesembryanthemum subgen. Cryophytum
MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESRQGIPLITGRFDSLEQLDEFSKSF
This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
P36442
C1CW40
MURG_DEIDV
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
Deinococcus
MSLVVMATGGTGGHIYPAVATARELNARGHETLLLGQRGGMEERVAAEQGLSFEGVDAGKLARSGQGRPDPRELFRAVRGVVEARRVLQARRPALVVGYGGFASLPGVLAAQSLGIATVLHEQNARLGLTQRVAVGRARAVGTAYEQVLGLPAGEGTLVGMPVREERLSREEAQRRLGLHSGPLTVFVMGGSQGSLFLNNSVPDTLRNILGKEGLLSGLGSEAGQIDLDFTHPRAGGAAVQVLHSTGPRWLADVAPRVHDLEWYHAVGYVDTVAAWAAADLAITRAGTGTLAEAAFHGVPLVMVPLPESSENHQYHNALSVQQAGAGRVVEQKNVQEALGAAVLECAEPGTRMAMRDAALARAQIGAAARFADLIEQHLPRS
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
C1CW40
Q7ZAN7
XERC_BRUSU
Tyrosine recombinase XerC
Brucella
MATNSEFLIPARADLAAAREEWLKSLKTMRRLSDNTLIAYERDTRQFLQFLTGHLGEPPSLKEIGNLRIADLRSFLANRRNDGAGARTLGRGLAGVRSLLRHLEKRGLVNAAGASAMRAPRQPKSLPKPLTADDARRVVSADGQMAEEPWIAARNAAVLTLLYGCGLRISEALGLSGDALSDPSARSMTITGKGSKTRLVPLLPAVHKAVAQYRALCPFDLSAGQPLFRGAKGGPLHAAIIQREMQKLRAGLGLPDSATPHALRHSFATHLLGRGGDLRTIQELLGHASLSTTQVYTGVDTQRLLEVYDKTHPRA
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
Q7ZAN7
A4WCR7
NUOA_ENT38
NUO1
Enterobacter
MSMSTSTEVVAHHWAFAIFLIVAIGLCCLMLIGGWFLGGRARARHKNTPFESGIDSVGTARLRLSAKFYLVAMFFVIFDVEALYLFAWSTSIRESGWVGFVEAAIFILVLLAGLVYLVRIGALDWTPTRSRRELVNPENSNSNRQQ
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
A4WCR7
P39371
NANM_ECOLI
Sialic acid epimerase
Escherichia
MNKTITALAIMMASFAANASVLPETPVPFKSGTGAIDNDTVYIGLGSAGTAWYKLDTQAKDKKWTALAAFPGGPRDQATSAFIDGNLYVFGGIGKNSEGLTQVFNDVHKYNPKTNSWVKLMSHAPMGMAGHVTFVHNGKAYVTGGVNQNIFNGYFEDLNEAGKDSTAIDKINAHYFDKKAEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEAKPGLRTDAVFELDFTGNNLKWNKLAPVSSPDGVAGGFAGISNDSLIFAGGAGFKGSRENYQNGKNYAHEGLKKSYSTDIHLWHNGKWDKSGELSQGRAYGVSLPWNNSLLIIGGETAGGKAVTDSVLITVKDNKVTVQN
Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers. Probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses . Forms linear aceneuramate during interconversion of Neu5Ac anomers .
P39371
Q2JQL7
PURL_SYNJA
Phosphoribosylformylglycinamidine synthase subunit II
unclassified Synechococcus
MTSASAPPDLKAHGLSPEEYRQIQQQLGRDPNPTELAMFGVMWSEHCCYKNSRPLLKHFPTTGERVVVGPGENAGVVDLGDGDWLAFKIESHNHPSAVEPFQGAATGVGGILRDIFTLGARPIALLNSLRFGPLTDPRNRRLMARVVEGIAHYGNCVGVPTVGGEVAVDPCYSGNPLVNVMALGLLETPAVVKSAARGVGNPILYVGATTGRDGIRGASFASAELKEDAQQDRPAVQVGDPFLGKCLIEACLEAFATVAVVAAQDMGAAGITCSTAEMAAKGGVGIRFDLDRVPARESGMAAWEYLLSESQERMLLVVQKGREAEVMEIFHRWGLQASVAGEVIAEPLVEIWHQGSCVVRVPARALAEDTPVYVRPLLPEPPEYVQAAWQWDPSTLPPCDRQGIHLPQKTLAWEQVLLQLLASPTLASKAWIYRQYDHQVQNNTVLWPGQGDAAVIRIRSQKFGVGEVPPLQAARKAIAATLDGNGRWVYLDPYEGAKAAVAEAARNLSCVGADPLAITDNLNFGSPENPVVYWQLALACRGIAEACRALGTPVTGGNVSLYNEKGSQAIYPTPVIGMVGLIPDLKFICGQGWQQEGDLVYLLGSQAVTSLGGSEYLAAIYNKVTGRPAPVDLELEKRVQGACRHGIRQGWVRSAHDCSEGGLAVALAEACLSGGRGASVSLAPGSLPWDQALFGEGSSRILVSVDPAQRSPWEAYLESQLPGQWQLLGQVGGPADPLVLTTAEGDPLLSVSLAALQGAYYSAFAD
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Q2JQL7
Q5QY51
IXTPA_IDILO
Nucleoside-triphosphate pyrophosphatase
Idiomarina
MSQNTLVLATGNAGKVAELRHMLSQTHATADWLVRPQSEWDFAEADETGTTFVENAIIKARHACQQTGLPAIADDSGLAVTALNGAPGVYSARYAGGNATDSDNINKLLKALEGVEESQRQASFHCVLVYMQSAEDPTPIICQGRWDGHILTHPVGEEGFGYDPVFWVKEKNCSAAQLSKTEKQALSHRGQALKQLLEQLAK
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Q5QY51
Q9A7Y1
TGT_CAUVC
tRNA-guanine transglycosylase
Caulobacter
MAAFPFEIEATDGKARTGVLKTPRGDIRTPAFMPVGTAATVKAMTVDQVKDTGADIILGNTYHLMLRPSAERVKRLGGLHKFMRWDKPILTDSGGFQVMSLSGISKLTEEAVTFSSHVDGSKHVLTPERSIEIQADLLGSDIVMQLDECVAWPAEEARARKGMELSARWAKRSKDAFGTRDTQVLFGIQQGSTFENLRRESSERLREIGFDGYAIGGLAVGEGHQAMCEVLDYAPGFLPEDRPRYLMGVGKPIDLVEAVARGVDMFDCVLPTRSGRHGQAWTWDGPINLKNAKYAEDETPLDPDSDCPASRDYSKAYLRHLFKAEEILGQVLLSWHNIAFFQALTAAMRAAIAEGRFEQFRRDFAARHLGG
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Q9A7Y1
A7ELE2
MDM12_SCLS1
Mitochondrial inheritance component mdm12
Sclerotinia
MSIDLNWETLTTGPDGIALAEKIRDFVHAKFQTVTLPRFIKGVKVHTFDFGSIAPEVELKDICDPLPDFYEDLDDDDGGSDEDDEGSNSCQTDEENEAAKTLRERRKMDRVERTANGSSNVSNPPSYTDTRYPGLRSMQASGDNGSPFLGVSTPGIPGGTSNLSYFHSQLASGFSGTQTPLAAVAGAHLPQGWPDRPSPSLHMSALRNQSHTSLSHTASERPMTPPQIADLSQQSIREKASASTLAVSSSTTGPVTRGGATEKTIPEEQTSEGEEPTSPPRRFREPKPEDLQTVFRVRYSGNIRLSLTVDILLDYPMPSFVGIPVRLNITGLSFDGVAVLAYIRKRAHFCFLSPEDAYAAIGADEKEAGGSGGMKMGALLHEIKVESEIGQRENGKQVLKNVGKVEKFVLEQVRRIFEDEFVYPSFWTFLV
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. Mdm12 is required for the interaction of the ER-resident membrane protein mmm1 and the outer mitochondrial membrane-resident beta-barrel protein mdm10. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
A7ELE2
P0A445
PSBA1_SYNEL
Photosystem II Q(B) protein 1
Synechococcus
MTTTLQRRESANLWERFCNWVTSTDNRLYVGWFGVIMIPTLLAATICFVIAFIAAPPVDIDGIREPVSGSLLYGNNIITGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLIIFHFLLGASCYMGRQWELSYRLGMRPWICVAYSAPLASAFAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHQLGVAGVFGGALFCAMHGSLVTSSLIRETTETESANYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGVWFTALGISTMAFNLNGFNFNHSVIDAKGNVINTWADIINRANLGMEVMHERNAHNFPLDLASAESAPVAMIAPSING
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
P0A445
Q9TUA8
OR1D2_PANTR
Olfactory receptor 1D2
Pan
MDGGNQSEGSEFLLLGMSESPEQQRILFWMFLSMYLVTVVGNVLIILAISSDSCLHTPMYFFLANLSFTDLFFVTNTIPKMLVNLQSQNKAISYAGCLTQLYFLVSLVALDNLILAVMAYDRYVAICCPLHYTTAMSPKLCILLLSLCWVLSVLYGLIHTLLMTRVTFCGSRKIHYIFCEMYVLLRMACSNIQTNHTVLIATGCFIFLIPFGFVIISYVLIIRAILRIPSLSKKYKAFSTCASHLGAVSLFYGTLCMVYLKPLHTYSVKDSVATVMYAVVTPMMNPFIYSLRNKDMHGALGRLLDKHFKRLT
Odorant receptor.
Q9TUA8
Q4FNM8
RBFA_PELUB
Ribosome-binding factor A
Candidatus Pelagibacter
MADRIGKPVSQRQLRVGEMIRQSLGMIFARNEAKVPNLETNTITVTEVKMSQDLKIAKAYVLPLGGKDSELVIKKLKECSFLIRKALSKKIIMKYLPKILFAKDDSFEYAEKIENLIKQTNK
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.
Q4FNM8
B0TR40
YBEY_SHEHH
Endoribonuclease YbeY
Shewanella
MNDNQTVIDLDLQIAVEGFELPSQAELELWVKTALRDTMSEAELTIRIVDVEESQELNSTYRGKDKPTNVLSFPFEAPPGIELPLLGDLVICAAVVKQEAMDQNKPLIAHWAHMVVHGCLHLLGYDHIDDSEAEEMESLETHLIESLGYINPYKEQ
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
B0TR40
Q7Y1C5
BRC2A_ARATH
Protein BREAST CANCER SUSCEPTIBILITY 2 homolog A
Arabidopsis
MSTWQLFPDSSGDGFRWEVAGRILQSVSDSTPTKALESTAPLPSMADLLLQGCSKLIAREEAMPGEIPMFRTGLGKSVVLKESSIAKAKSILAEKVTYSDLRNTNCSIPQMRQVDTAETLPMFRTASGKSVPLKESSIAKAMSILGSDKIIDSDNVLPRESGFGVSNSLFQTASNKKVNVSSAGLARAKALLGLEEDDLNGFNHVNQSSSSSQQHGWSGLKTHEEFDATVVKHHSGTPGQYEDYVSGKRSEVLNPSLKVPPTKFQTAGGKSLSVSAEALKRARNLLGDPELGSFFDDVAGGDQFFTPEKDERLSDIAINNGSANRGYIAHEEKTSNKHTPNSFVSPLWSSSKQFSSVNLENLASGGNLIKKFDAAVDETDCALNATHGLSNNRSLASDMAVNNSKVNGFIPRGRQPGRPADQPLVDITNRRDTAYAYNKQDSTQKKRLGKTVSVSPFKRPRISSFKTPSKKHALQASSGLSVVSCDTLTSKKVLSTRYPEKSPRVYIKDFFGMHPTATTRMDYVPDHVRRIKSSNADKYVFCDESSSNKVGAETFLQMLAESGASLQHASRKWVTNHYRWIVWKLACYDIYYPAKCRGNFLTITNVLEELKYRYEREVNHGHCSAIKRILSGDAPASSMMVLCISAINPKTDNDSQEAHCSDSCSNVKVELTDGWYSMNAALDVVLTKQLNAGKLFVGQKLRILGAGLSGWATPTSPLEAVISSTICLLLNINGTYRAHWADRLGFCKEIGVPLALNCIKCNGGPVPKTLAGIKRIYPILYKERLGEKKSIVRSERIESRIIQLHNQRRSALVEGIMCEYQRGINGVHSQNDTDSEEGAKIFKLLETAAEPEFLMAEMSPEQLRSFTTYKAKFEAAQQMRKEKSVAETLEDAGLGERNVTPFMRIRLVGLTSLSYEGEHNPKEGIVTIWDPTERQRTELTEGKIYMMKGLVPINSDSEILYLHARGSSSRWQPLSPKDSENFQPFFNPRKPISLSNLGEIPLSSEFDIAAYVVYVGNAYTDVLQKKQWVFVTDGSAQHSGEISNSLLAISFSTSFMDDSSVSHISHNLVGSVVGFCNLIKRAKDVTNEIWVAEAAENSVYFINAEAAYSSHLKTSSAHIQTWAKLSSSKSVIHELRQRVLSIIGACKSPSC
Involved in double-strand break repair and/or homologous recombination by mediating RAD51- and DMC1-facilitated DNA repair. Plays an essential role in both somatic and meiotic homologous recombination. Is crucial for the formation of RAD51 and DMC1 foci during male meiotic homologous recombination in prophase I.
Q7Y1C5
P21373
UTR1_YEAST
Unknown transcript 1 protein
Saccharomyces
MKENDMNNGVDKWVNEEDGRNDHHNNNNNLMKKAMMNNEQIDRTQDIDNAKEMLRKISSESSSRRSSLLNKDSSLVNGNANSGGGTSINGTRGSSKSSNTHFQYASTAYGVRMLSKDISNTKVELDVENLMIVTKLNDVSLYFLTRELVEWVLVHFPRVTVYVDSELKNSKKFAAGELCEDSKCRESRIKYWTKDFIREHDVFFDLVVTLGGDGTVLFVSSIFQRHVPPVMSFSLGSLGFLTNFKFEHFREDLPRIMNHKIKTNLRLRLECTIYRRHRPEVDPNTGKKICVVEKLSTHHILNEVTIDRGPSPFLSMLELYGDGSLMTVAQADGLIAATPTGSTAYSLSAGGSLVCPTVNAIALTPICPHALSFRPIILPESINLKVKVSMKSRAPAWAAFDGKDRIELQKGDFITICASPYAFPTVEASPDEFINSISRQLNWNVREQQKSFTHILSQKNQEKYAHEANKVRNQAEPLEVIRDKYSLEADATKENNNGSDDESDDESVNCEACKLKPSSVPKPSQARFSV
Specifically phosphorylates NAD in the presence of ATP, dATP, or CTP as phosphoryl donors.
P21373
Q76MH8
MATK_ZINOF
Intron maturase
Zingiber
MEELQGYLEEDRSRQQQFLYPLLFQEYIYVFAYDHGLNSSIFYEPQNSLGYDNKFSSVLVKRLIIRMYQKNYLIYSVNDIYQNIFVGHNNYFYFNFFSQILSEGFAVIVEIPFSLQLISSLEEKEIPKSHNLQSSHSIFPFLEDKLLHLNYLSDILIPYPVHMEILVQILQSWIQDVLSLHLLQFLLHEYYNWNSLIIPKKSIYVFSKENKRLFWFLYNLYIYEYEFLLVFPCKQSSFLRLISSGVLLERIHFYVKIEHLGVYRIFCQKTLWIFKDPFIHYIRYQGKSILGSRGTHFLMKKWKYHLVNFWQYYFHFWSQPYRIDIKKLSNYSFYFLGYFSSVQINSSMVRNQMLENSFLMDTLTKKFDTIIPIIPLIRSLFKAQFCTVSGYPISKPIWTDLADCDIINRFGRICRKLTHYHSGSSKKQSLYRMKYILRLSCARTLARKHKSSARSFLQRLSSGLLEEFFTEEEQVIFLIFPKIISFYLYGSYRERIWYLDIIRINDLVNCLLVTT
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
Q76MH8
B0T193
GATA_CAUSK
Glutamyl-tRNA(Gln) amidotransferase subunit A
unclassified Caulobacter
MSSLTSLTLKGALDGLEKGDFTSVELTRAHIDAIEAARGLNAFLLETPEQALSMAAASDARRALDAARPLDGIPLGIKDLFCTQGVRTTAASKILEPFVPQYESTVTSQLWRDGAVMLGKLNLDEFAMGSSNETSAYGPVVNPWRKAGSNQALTPGGSSGGSAAAVAADLCLGATATDTGGSIRQPAAFTGTVGIKPTYGRCSRWGVVAFASSLDQAGPIAKTVTDAALLLTSMSGHDPKDSTSLDVPVPDFSAFVGKSIKGLRIGVPQEYRVDGMPAEIEKLWADGIAWLKDAGCEIVEISLPHTKYALPAYYIVAPAEASSNLARYDGMRYGLRAEGSNLTEVYENTRAEGFGDEVKRRILIGTYVLSAGYYDAYYLKALKVRRRIAEDFDNAWERCDAILTPTAPSAAFGLGENSSDPIAMYLNDVFTVTTNLAGLPGLSLPAGLDANGLPLGLQIIGKPLDEGTVFSVAGVLEKAAGFTAKATKWW
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
B0T193
Q28385
IL1A_HORSE
Interleukin-1 alpha
Equus
MAKVPDLFEDLKNCYSENEDYSSEIDHLSLTQKSFYDASYDPLPEDCMDTFMSLSTSETSKTSKLNFKESVVLVAANGKTLKKRRLSLNQFITNDDLEAIANDPEEGIIRPRSVHYNFQSNTKYNFMRIVNHQCTLNDALNQSVIRDTSGQYLATAALNNLDDAVKFDMGAYTSEEDSQLPVTLRISKTRLFVSAQNEDEPVLLKEMPDTPKTIKDETNLLFFWERHGSKNYFKSVAHPKLFIATKQGKLVHMARGQPSITDFQILDNQF
Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex. Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways. Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage. In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as signal for genotoxic stress without loss of cell integrity.
Q28385
B3PK30
RPOB_CELJU
Transcriptase subunit beta
Cellvibrio
MAYSYTEKKRIRKNFGKLPHVMDVPYLLAIQLDSYRKFTQADLSANKREDVGLHAAFRSVFPIVSYSGNAALEYVSYSLGKAAFDVNECILRGVTYAVPLRVKVRLIIYDRESANKAIKDIKEQEVYMGEIPLMTDNGTFVINGTERVIVSQLHRSPGVFFDHDKGKTHSSGKLLYSARIIPYRGSWLDFEFDPKDLLYVRIDRRRKLPATILLRALNYSSQEMLSMFFETSSFTLGKDGQFSYEVVPSRLRGDVATFDIKDDKGNIIVEEGRRITARHIRQLEKAGVDQMEVPSEYLLGRSLAKDIVDTRTGELLFECNTEITSDVLSKIVAAGVEKVETLYTNELDCGPFISETLRIDPTRTQLEALVEIYRMMRPGEPPTKESAEALFQNLFFSQERYDLSAVGRMKFNRRLGRETETGEGTLSNDDIVDVMKTLISIRNGKGVVDDIDHLGNRRVRSVGEMAENQFRVGLVRVERAVKERLSMAESEGLMPQDLINAKPVAAAVKEFFGSSQLSQFMDQNNPLSEITHKRRVFALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLATYARTNNYGFLESPYRKVIEGKVTDQIEYLSAINESEYVIAQASASLDDNGRLTEELVSVRHQNEFTLKAPTDVQYMDVSARQVVSVAASLIPFLEHDDANRALMGSNMQRQAVPTLRSQKPLVGTGMERNVAADSGVCVVAKRGGVIDSVDAGRIVVKVHDAEVEAGDAGVDIYNLIKYTRSNQNTCINQRPIVSMGDIVSRGDILADGPSVDMGELALGQNMRIAFMPWNGYNFEDSILVSERVVQEDRFTTIHIQELTCIARDTKLGSEEITADIPNVGESALSKLDESGIVYIGAEVGGGDILVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDTSLRVPSGTKGTVIDVQVFTRDGLEKDQRSLEIEKAQLDEVRKDLNEEFRIVETATFERLRAALVGQIVASGKGVKKGEALTHDILDGLEKDQWFKLRMNEDALNEQIDRAEEQLAERRKILDERFEDKKRKLSTGDDLAPGVLKIVKVYLAIKRRIQPGDKMAGRHGNKGVISVIMPVEDMPYDENGETVDIVLNPLGVPSRMNVGQVLEMHLGMAAKGLGVKINKLIQEQKAVADIRSFLEEIYNSTGDVAAKEDLVSFSDREVIDLAKNLVDGVPMATPVFDGAKEHEIKALLRLASLSDTGQTTLFDGRTGDQFSRSVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVAGRTKMYKNIVDGDHRMEPGMPESFNVLVKEIRSLGINIELEQED
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
B3PK30
Q83HX2
GATA_TROW8
Glutamyl-tRNA(Gln) amidotransferase subunit A
Tropheryma
MIRRAPFLILLRFCRMGKMACSGYPPFQGRIVLSEMPAHRLAALIRSKEVSALEVAESFIDNIEASDSRICAFLYTDFSYTRDVARRVDEELKSATKLSPLAGVPIAVKDMILTRDMPTTAGSKILEGWIPPYNATVIERISRARMPILGKTNQDEFGMGSSTEYSAYKTTRNPWDLSRTAGGSGGGSSAAVSASQAPLALGTDTGGSIRLPAHCTGTVGIRPTYGSVSRYGVIALASSFDQVGPCSSNILDAALLHEVIAGYDPADAVSIKDQDLNFSQAAYEGANRGISGVRLGFVNPSNWCNSKITDLFGRTLKSLESEGAVLHEVQFPNFDHAVQAYYLIMQAEASSNLSRYDSIRFGPQEMAASASGTVSKTRSIRFGPEVKRRILLGTHILSAGYYDDFYMSAQKIRSLVKRDFAKIFSLVDVLLLPTAPTPAFKLGEKIDHHTSMYKSDTATTPASLAGLPAGSIPMGVIDGLPVGLQIIAPGQFDSRVYSTGAAIEQIIGDIHAMKNTKHNTGQTA
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Q83HX2
Q4PEV8
EIF3M_USTMA
Eukaryotic translation initiation factor 3 subunit M
Ustilago
MSAADLVTVLAEGTFEEQIVEVSAFLSRSQPEASRNDFISKFQQLALDAEPAEPAEPAVSTEATEPASAPDAAKKQQTVQQLVSEIVTLGEGSDRELEGVYNLIFSLISSTDQQTQLVPQLLSAVSKDSAAAATGAGGADKSNVRYRILSNLFNSLEATSALRLQTFNALLSLVAANDDLDYLTSALTALPQWLAQWSVSETEKASCLESVAKALEGAEKEHGQTSKAYQFLVLHLRYISTLPASASTKEAAERTVAAALRLPRLYEFEDLLHVQAVLDLKSASSPIFDLLKIFVGGTTADFSAFASSHSSEFQRLNLSHDDLLHKIRLLDLADLCALRVSADVSYASIAKTLNIEHDQVELWVIDVIRAGLVSGKLSQVNDAFRVYKSTHRQFGKEQWQSLEQRLVQWQNSISSIIESIAATRGGKLPDGAPVAAELATA
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.
Q4PEV8
O04397
FENR2_TOBAC
Ferredoxin--NADP reductase, root-type isozyme, chloroplastic
Nicotiana
MAHSALSQVSVAVPLQTDSSFRRSTFKATSITFSDRSSWISMPPIDLKAAPSRNQHIVCMSVQQASKAKVSVSPLSLEDAKEPPLNIYKPKEPYTATIVSVERLVGPKAPGETCHIVIDHDGNLPYWEGQSYGVIPPGENPKKPGNPHNVRLYLIASTRYGDSFDGKTASLCVRRAVYYDPETGKEDPSKNGVCSNFLCDSKPGDKVKITGPSGKIMLLPEEIPNATHIMIGTGTGVAPFRGYLRRMFMESVPTKFNGLAWLFLGVANTDSLLYDDEFTKYLNDYPGNFRYDRALSREQKNNKGGKMYVQDKIEEYSDEIFKLLDEGAHIYFCGLKGMMPGIQDTLKRVAERRGESWEQKLSQLKKNKQWHVEVY
May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. Is involved in nitrate assimilation.
O04397
Q15JG1
VLDE_STRHL
Trehalose 6-phosphate synthase-like enzyme VldE
Streptomyces violaceusniger group
MTGSEIFLASKRAAITYDTDPATGEPRAWLAPGGTGNVVAEQAGVLNISWIASADSEDDRRASALNPDGVTMELHSGREILVRLIRHDPAVFRNVQNFMTANLMWAANNYGWDRWTQPSFGSDAREGWADFGRFTRDFADAILKSSAQSADPVYLVHDYQLVGVPALLREQRPDAPILLFVHIPWPSADYWRILPKEIRTGILHGMLPATTIGFFADRWCRNFLESVADLLPDARIDREAMTVEWRGHRTRLRTMPLGYSPLTLDGRNPQLPEGIEEWADGHRLVVHSGRTDPIKNAERAVRAFVLAARGGGLEKTRMLVRMNPNRLYVPANADYVHRVETAVAEANAELGSDTVRIDNDNDVNHTIACFRRADLLIFNSTVDGQNLSTFEAPLVNERDADVILSETCGAAEVLGEYCRSVNPFDLVEQAEAISAALAAGPRQRAEAAARRRDAARPWTLEAWVQAQLDGLAADHAARTATAERFDTAPAVSTRADL
Involved in the biosynthesis of the antifungal agent validamycin A . Catalyzes the condensation between GDP-valienol and validamine 7-phosphate via a nonglycosidic C-N bond formation to yield validoxylamine A 7'-phosphate .
Q15JG1
O22891
Y2044_ARATH
Putative BTB/POZ domain-containing protein At2g40440
Arabidopsis
MATETNKELFVGGFAKILKEQRQVDVRLKAGDSGDEGASTSAHKLVLSARSEVFKKMLESDEIKASAQLETITLCEMKHEELEAFIEFIYSDGSMLSAKEKQHVRSLYIAGDKYEIPHLRDLCRIELISSLKSSNALDILELAQIPFDKALHDSAFFFFFFFFFG
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
O22891
Q9ZLW3
RL9_HELPJ
50S ribosomal protein L9
Helicobacter
MKVLLLEDVKNLGKAGEVCEVKDGYGNNFLIANQKAKLATNEVINKYKAEVKKKAEKEALEKAQKLQMVETLQTITLTIHKKVGANGSLFGAITKEEITERLKEQHASLNLDKKDIELKHPIKSTGIYEIEVKLGSGIAGVFKIDVVAE
Binds to the 23S rRNA.
Q9ZLW3
Q5RFB6
RPN1_PONAB
Ribophorin-1
Pongo
MEAPAARLFLLLLLGTWAPAPGSASSEAPPLINEDVKRTVDLSSHLAKVTAEVVLAHLGGGSTSRATSFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVRLPVALDPGAKISVIVETVYTHVLQPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASRNVESYTKLGNPTRSEDLLDYGPFRDVPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWGNIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGISSIRSFKTILPAAAQDVYYRDEIGNVSTSHLLILDDSVEMEIRPRFPLFGGWKTHYIVGYNLPSYEYLYNLGDQYALKMRFVDHVFDEQVIDSLTVKIILPEGAKNIEIDSPYEISRAPDELHYTYLDTFGRPVIVAYKKNLVEQHIQDIVVHYTFNKVLMLQEPLLVVAAFYILFFTVIIYVRLDFSITKDPAAEARMKVACITEQVLTLVNKRIGLYRHFDETVNRYKQSRDISTLNSGKKSLETEHKALTSEIALLQSRLKTEGSDLCDRVSEMQKLDAQVKELVLKSAVEAERLVAGKLKKDTYIENEKLISGKRQELVTKIDHILDAL
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Q5RFB6
P31287
WNT6_XENLA
Protein Wnt-6
Xenopus
QECKCHGLSGSCTFTTCWKKMPHFREVGDRLLERFNGAFKVMGGNDGKTIIPVGHNIKPPDKQDLIYSAESPDFCQANRKTGSPGTRGRVCNSTALDVGGCDLLCCGRGQREETVVVEENCLCRFHWCC
Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters.
P31287
P75457
END4_MYCPN
Endonuclease IV
Mycoplasma
MPKLLGSFISFKSPHYLVGSVRDAVSIKAQAFMIFLGAPHTALRVDPNRMQIDEGHTLMEQHNLSKSGMVVHAPYIINCASKDPVKQTFAIDVLTREVKLCHAVGAKLIVLHPGSAVEQTQTQALDHLIKVLNTVIANTKEVIICLETMAGKGNEIGRDLDQLKYVINHIEQQERIGVCLDTCHFHDSGNDFNNTAEIMETIDTKLGFEFLKVIHLNESKNVCGSKKDRHANLGEGMIGFDNLMRFIAQPQIKQIPIVLETPSDKHNYPAVYGAEIERIRAWFGAR
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
P75457
Q3A2U7
MNTP_SYNC1
Putative manganese efflux pump MntP
Syntrophotalea
MDMITLFGLALALAMDAFAVALGCGLTLERLTGRHLFRLGWHFGLFQAMMPIIGWLAGLTVQKWIETYDHWVAFGLLVCVGGKMIHEAFQDEETRESRDDPTRGMSLIMLSVATSIDALAVGLSLAIVGISVWFPALIIGIIAGVMTVIGMLLGRRAGARWGQRVEIAGGLILIGIGLKILWEHTLGM
Probably functions as a manganese efflux pump.
Q3A2U7
O21332
NU3M_DASNO
NADH dehydrogenase subunit 3
Dasypus
MNIMITLFINMSLASLLVLIAFWLPQLNTYTEKSSPYECGFDPMGSARLPFSMKFFLVAITFLLFDLEIALLLPLPWATQANTMTPMLTTALVLILLLALGLAYEWLQKGLEWNE
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 of complex I.
O21332
O25792
NUPC_HELPY
Nucleoside permease NupC
Helicobacter
MIFSSLFSVVGMAVLFLIAWVFSSNKRAINYRTIVSAFVIQVALGALALYVPLGREMLQGLASGIQSVISYGYEGVRFLFGNLAPNAKGDQGIGGFVFAINVLAIIIFFASLISLLYYLKIMPLFINLIGGALQKCLGTSRAESMSAAANIFVAHTEAPLVIKPYLKSMSDSEIFAVMCVGMASVAGPVLAGYASMGIPLPYLIAASFMSAPGGLLFAKIIYPQNETISSHADVSIEKHVNAIEAIANGASTGLNLALHVGAMLLAFVGMLALINGLLGVVGGFLGMEHLSLGLILGTLLKPLAFMLGIPWSQAGIAGEIIGIKIALNEFVGYMQLLPYLGDNPPLILSEKTKAIITFALCGFANLSSVAMLIGGLGSLVPKKKDLIVRLALKAVLVGTLSNFMSATIAGLFIGLNAH
Involved in purine nucleosides uptake. Could also be involved in uptake of nucleobases.
O25792
A6VZF8
OADC_MARMS
Oxaloacetate decarboxylase
Marinomonas
MATPSQHDLRNDFRALLASGKCYYTASTFDPMSARIAADLGFEVGILGGSVASLQVLAAPDFALITLSEFTEQATRIGRVARLPIIADADHGYGNALNVMRTIVELERAGVAALTIEDTLLPAKYGHKSTDLIPVEEAVGKLKAALEARIDPIMSIIARTNAGQLSTEETISRVKAYQAVGVDGICMVGIRDFAHLEEISQHISIPIMLVAYDNPELRDRERLAANGVRIVVNGHAAYFAAIKATYDCLREQRGIAEGTLDASELSTRYSTLEENRVWANKYMDVQE
Catalyzes the decarboxylation of oxaloacetate into pyruvate. Seems to play a role in maintaining cellular concentrations of bicarbonate and pyruvate.
A6VZF8
P56100
CYDX_ECOLI
Cytochrome d ubiquinol oxidase subunit X
Escherichia
MWYFAWILGTLLACSFGVITALALEHVESGKAGQEDI
Required for correct functioning of cytochrome bd-I oxidase. This protein and AppX may have some functional overlap.
P56100
P04088
INHBB_PIG
Activin beta-B chain
Sus
MDGLPGRALGAACLLLLAAGWLGPEAWGSPTPPPSPAAPPPPPPPGALGGSQDTCTSCGGFRRPEELGRLDGDFLEAVKRHILNRLQMRGRPNITHAVPKAAMVTALRKLHAGKVREDGRVEIPHLDGHASPGADGQERVSEIISFAETDGLASSRVRLYFFISNEGNQNLFVVQASLWLYLKLLPYVLEKGSRRKVRVKVYFQEPGHGDRWDVVEKRVDLKRSGWHTLPLTEAIQALFERGERRLNLDVQCDGCQELAVVPVFVDPGEESHRPFVVVQARLVDSRHRIRKRGLECDGRTNLCCRQQFFIDFRLIGWSDWIIAPTGYYGNYCEGSCPAYLAGVPGSASSFHTAVVNQYRMRGLNPGTVNSCCIPTKLSTMSMLYFDDEYNIVKRDVPNMIVEECGCA
Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
P04088
Q3MA16
RL7_TRIV2
50S ribosomal protein L7/L12
Trichormus
MSAATDQILDQLKSLSLLEAAELVKQIEEAFGVSAAAPVGVAVAAPAAAAAAEPVEEQTEFDVILESVPADKKIAVLKIVREITGLGLKEAKDLVEAAPKAVKEAIAKDAAEDAKKRIEEAGGKVTIK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Q3MA16
Q9JL99
CLC1B_MOUSE
C-type lectin-like receptor 2
Mus
MQDEDGYITLNIKPRKQALSSAEPASSWWRVMALVLLISSMGLVVGLVALGIMSVTQQKYLLAEKENLSATLQQLAKKFCQELIRQSEIKTKSTFEHKCSPCATKWRYHGDSCYGFFRRNLTWEESKQYCTEQNATLVKTASQSTLDYIAERITSVRWIGLSRQNSKKDWMWEDSSVLRKNGINLSGNTEENMNCAYLHNGKIHPASCKERHYLICERNAGMTRVDQLL
C-type lectin-like receptor that functions as a platelet receptor for the lymphatic endothelial marker, PDPN. After ligand activation, signals via sequential activation of SRC and SYK tyrosine kinases leading to activation of PLCG2.
Q9JL99
A5UEY7
FABA_HAEIG
Trans-2-decenoyl-[acyl-carrier-protein] isomerase
Haemophilus
MQNACTLNKKSSYSYDDLLASGRGELFGKEGPQLPAPTMLMMDRIIEMNEETGAFGKGYIEAELDIKPELPFFGCHFIGDPVMPGCLGLDAMWQLVGFYLGWIGGKGKGRALGVGEVKFTGQILPTAKKVVYRIHMKRVINRKLVMGMADGEVEVDGRVIYTATDLKVGLFQDTSTF
Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length.
A5UEY7
Q5RCZ2
CY561_PONAB
Cytochrome b561
Pongo
MEGGAAASTPAALPYYVAFSQLLGLTLVAMTGAWLGLYRGGIAWESDLQFNAHPLCMVIGLIFLQGDALLVYRVFRNEAKRTTKVLHGLLHIFALVIALVGLVAVFDYHRKEGYADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLLSVGTALLGLKEALLFKLRDKYSAFEPEGVLANVLGLLLACFGGAVLYILTRADWKRPSQAEEQALSMDFKTLTEGDSPGSQ
Transmembrane reductase that uses ascorbate as an electron donor in the cytoplasm and transfers electrons across membranes to reduce monodehydro-L-ascorbate radical in the lumen of secretory vesicles. It is therefore involved the regeneration and homeostasis within secretory vesicles of ascorbate which in turn provides reducing equivalents needed to support the activity of intravesicular enzymes.
Q5RCZ2
Q2RP11
ENGB_RHORT
Probable GTP-binding protein EngB
Rhodospirillum
MADLPETPAFGAAFSDEEEAARALEAGRWLFSQTCSFVMGCVSLDTLPDHDLSEIAFAGRSNVGKSSLVNALTGRKTLARTSNTPGRTQELNYFRLGPEAQDPALMMVDLPGYGFAEAPKDAVKRWTRLIMAYLRGRPALRRVCLLIDSRHGIKENDRDVMRMLDEAAVSYQIVLTKADKLKAAEITDVLARVVAETAKHVAAHPDVIVTSSQSGAGIDLLRAQLAALASP
Necessary for normal cell division and for the maintenance of normal septation.
Q2RP11
Q1G9A0
MURC_LACDA
UDP-N-acetylmuramoyl-L-alanine synthetase
Lactobacillus
MLDKTKQIWFIGIKGTGMASLALILHDLGYKVAGSDIDKYTFTQDPLEAAGIEVASFSKDNIKESGQVIVKGNAFKSDNIEVAACEEKGVKWQSYPDTVEEIVQQYTSIGVAGSHGKTSTTGLLATVLGEAAPTSFLIGDGMGKGVKDSRFFVYEADEYRRHFLAYHPDYQIMTNVDFDHPDYFKDRDDYASAFQTAADQTKKGLFVWGDDERLQKIHPKTAKKYTYGLKDSDDFQAFDVVKTTEGAKFHVRANGEDLGEFTIHLFGDHNVMNATAVIAIAFTEGIDLDVVRKGLVKYTGAKRRFSEKDFGDTVVIDDYAHHPTELRATIQAARQKFPDRKLVTIFQPHTYSRTKEFEEEYVEILKGVDKAFLTPIYGSAREAAGDIKSEDIASQIPGAEVIDFDNLKDLLAYKGDCIVFMGAGDIPKYEVAFEEMLGK
Cell wall formation.
Q1G9A0
Q8SAS8
TBSYN_HYPAN
Benzophenone synthase
Hypericum
MAPAMEYSTQNGQGEGKKRASVLAIGTTNPEHFILQEDYPDFYFRNTNSEHMTELKEKFKRICVKSHIRKRHFYLTEEILKENQGIATYGAGSLDARQRILETEVPKLGQEAALKAIAEWGQPISKITHVVFATTSGFMMPGADYVITRLLGLNRTVRRVMLYNQGCFAGGTALRVAKDLAENNEGARVLVVCAENTAMTFHAPNESHLDVIVGQAMFSDGAAALIIGACPDVASGERAVFNILSASQTIVPGSDGAITAHFYEMGMSYFLKEDVIPLFRDNIAAVMEEAFSPLGVSDWNSLFYSIHPGGRGIIDGVAGNLGIKDENLVATRHVLGEYGNMGSACVMFILDELRKSSKVNGKPTTGDGKEFGCLIGLGPGLTVEAVVLQSVPILQ
Type III polyketide synthase involved in the biosynthesis of benzophenones and xanthones. The preferred substrate is benzoyl-CoA, but can also use 3-hydroxybenzoyl-CoA with a lower activity.
Q8SAS8
Q6ZN04
MEX3B_HUMAN
RING finger protein 195
Homo
MPSSLFADLERNGSGGGGGGSSGGGETLDDQRALQLALDQLSLLGLDSDEGASLYDSEPRKKSVNMTECVPVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPVFVVTGRKEDVAMARREIISAAEHFSMIRASRNKNTALNGAVPGPPNLPGQTTIQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEAHIALRTGGIIELTDENDFHANGTDVGFDLHHGSGGSGPGSLWSKPTPSITPTPGRKPFSSYRNDSSSSLGSASTDSYFGGGTSSSAAATQRLADYSPPSPALSFAHNGNNNNNGNGYTYTAGGEASVPSPDGCPELQPTFDPAPAPPPGAPLIWAQFERSPGGGPAAPVSSSCSSSASSSASSSSVVFPGGGASAPSNANLGLLVHRRLHPGTSCPRLSPPLHMAPGAGEHHLARRVRSDPGGGGLAYAAYANGLGAQLPGLQPSDTSGSSSSSSSSSSSSSSSSGLRRKGSRDCSVCFESEVIAALVPCGHNLFCMECANRICEKSEPECPVCHTAVTQAIRIFS
RNA-binding protein. May be involved in post-transcriptional regulatory mechanisms.
Q6ZN04
A4WNL5
RNH2_CERS5
Ribonuclease HII
Cereibacter
MEIACPDWSHESAAFAEGFTCIVGVDEVGRGPLAGPVTAAAVRLFPGRIPEGLNDSKKLPAARREALAAEILAVAEVSVAHASVEEIDRLNILQASHLAMARALAGLPCPPDFALIDGHLIPKGLAHRCRAIVKGDALCLSIAAASIVAKVARDRIMVDLEQQHPGYGWRTNAGYGTRDHLQALLNLGLTPHHRRSFKPVHNILYQEASVSP
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
A4WNL5
A1WUX1
SYP_HALHL
Prolyl-tRNA synthetase
Halorhodospira
MRVTRFPLSTTRETPADAEIVSHQLMLRAGMIRRLSSGLYTWLPLGLRVLQKVERIVREEMNRAGALEVLMPAVQPAELWQESGRWEKYGPELLRIRDRHDREGCFGPTHEEVITDLFRREIRSYRQLPVNYYQIQTKFRDEIRPRFGVMRAREFLMKDAYSFHLDDDDLRAEYQRMHEAYCRIFQRTGLAFRPVEADTGAIGGSVSHEFMVLADSGEDAIAVCEASGYAANVELAPAVAPTEPRPAPQAERAEVATPGQRTIAEVAAYLGLPEARNLKTLLVEGADGGLVALLLRGDHELNELKAEKHPAVKAPLTFAEAERVERQLGCPFGSLGPVGLTGVTLIADHAAAHLADFACGANREGYHLTGVNWGRDLPEPETADLREVTAGDPSPDGEGTLTLRRGIEVGHIFQLGTTYSEAMGASVLDEQGQERTVTMGCYGIGVSRVVAAAIEQNHDDRGICWPAPIAPFQVALVAIKAEDPAVAEAAEALYADLTASGIDVLYDDRDARPGVKFADMELIGIPHRVVVSPRAIQEGSVEYKGRQDADPTHVPRAEIVTWLKNRLT
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
A1WUX1
Q73NV5
RS12_TREDE
30S ribosomal protein S12
Treponema
MPTINQLIKKGRKSAAVKTKSPALQSCPQKRGVCTSVKTITPKKPNSALRKVARIRLSNGIEVTAYIPGIGHNLQEHSVVLVRGGRVKDLPGVRYHIIRGTKDALGVEDRKRGRSKYGAKRPKA
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
Q73NV5
Q9KDI4
YAJC_HALH5
Sec translocon accessory complex subunit YajC
Halalkalibacterium (ex Joshi et al. 2022)
MEGLGGFLIPLILMFAIFYFLLIRPQQKRQKQIQEMHNNLQRGDKIVTIGGLHGTIDSLDESTVVILVNDNRKLTFDRSAIREVVNPD
The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions.
Q9KDI4
Q6D0G7
LEU3_PECAS
Beta-IPM dehydrogenase
Pectobacterium
MTKSYHIAVLPGDGIGPEVMAQAHKVLDAVRQRFGIRITTSEYDVGGIAIDRQGTPLPQATVAGCEQADAILFGSVGGPKWEHLPPAEQPERGALLPLRKHFKLFSNLRPARLYQGLEAFCPLRSDIAAKGFDILCVRELTGGIYFGQPKGREGSGQYERAFDTEVYHRFEIERIAHIAFESARKRRSIVTSIDKANVLQSSILWREIVTEVAKAYPDVKLSHLYIDNATMQLIKDPSQFDVMLCSNLFGDILSDECAMITGSMGMLPSASLNEQGFGLYEPAGGSAPDIAGKDIANPIAQILSLALLLRYSLGADDAAEAIEKAVNTALAEGYRTADLASASNAIGTSEMGDVIARFVAQGA
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Q6D0G7
Q2JX22
RIMP_SYNJA
Ribosome maturation factor RimP
unclassified Synechococcus
MVHPLIPQLESLARPLAARLGYELVQMVFHTNQYPPVLRVDIRPLDPEQETSHADCEAMSQALEVELDRVDLIPGHYVLEVSSPGISNLLISDRDFVVFKGFAVEVTVDPPYKGKAVWSGHLLGRDEEKVALSLKGRRVQLPRASVQRVVLSGAETE
Required for maturation of 30S ribosomal subunits.
Q2JX22
A4XSS4
PLSX_PSEMY
Phosphate-acyl-ACP acyltransferase
Pseudomonas
MSASIIAIDAMGGDFGPHCIVPACISALAEFPSLHLALVGQAPLIEEQLARQSGVDRSRLQVHHASEVIAMDERPAQALRGKPDASMRVALELVRQRQAHACVSAGNTGALMALSRYVLKTLPGIDRPAMVSPIPTERGHCYLLDLGANVDCSAEHLYQFAIMGAVAAETLGVARPRVALLNVGTEDIKGNQQVKLAASLLLQARGLNFIGYIEGDGVYRGEADVVVCDGFVGNILLKASEGLAKMITGRVETLFNEGLFAQAVGALAMPLLRRLKADLAPARHNGASFLGLQGIVVKSHGAAGQESFQSAIRCALREVQENLPQRLHGRLEDLLL
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
A4XSS4
A4QNX6
CTL2B_DANRE
CTD small phosphatase-like protein 2-B
Danio
MRLRMRKDSQQPTLARRACPARTKRKSSEVEECTGESKALLSSIKKFIHGSSIKVEQDNPAKTSHLSCELITSTPQRKNDLQRKSIYRARRRTSINGETTNHDTNKPNGKLEVTEEVVSSPPRTTLLGTIFSPVFNFFSPANKNASNSPDQVVEAEEIVKQLEMEQVEEMPTCTATSREPLSVPLYTSAMTSAFRPPPTAHTPEQESENTPHPDLPPLTAPGSPATGGYVDASITVPAEGSYEEEWEVFDPYFFIKHVPPLTEEQLTRKPALPLKTRSTPEFSLVLDLDETLVHCSLNELDDAALTFPVLFQDVIYQVYVRLRPFFREFLERMSQIYEIILFTASKKVYADKLLNILDPRKQLVRHRLFREHCVCVQGNYIKDLNILGRDLSKTIIIDNSPQAFAYQLSNGIPIESWFMDRNDSELLKLVPFLEKLVELNEDVRPHVRERFRLHDLLPPD
Probable phosphatase.
A4QNX6
Q61656
DDX5_MOUSE
RNA helicase p68
Mus
MSSYSSDRDRGRDRGFGAPRFGGSRTGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVDTYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSNLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSNVANMHNGMNQQAYAYPLPQAAPMIGYPMPTGYSQ
Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms.
Q61656
A0B7D6
EF1A_METTP
Elongation factor Tu
Methanothrix
MADTKPHLNLAFIGHVDHGKSTLVGRMMYEMGAIDEHIIEQYRKEAAAKGKATFEFAWVMDSLKEERERGVTIDIAHQRFDTDKYYFTVVDCPGHRDFVKNMITGASQADAAVLVVAAPDGVMAQTKEHVFLARTLGVNQLIVAINKMDATEPPYDEKRYNEVKEEVGKLLRMVGYKIDEVPFIPVSAYNGDNVVKHSDRTKWYTGPTVLDALNALKEPQKPVNLPLRIPVQDVYSISGVGTVPVGRVETGVLKKGDKVIFEPAHVSGEVKSIEIHHQEIPEAYPGDNIGWNVRGIGKNDIRRGDVCGHVDNPPTVAKEFTAQIVVLQHPSAISAGYTPVFHCHTAQVACTITEIKAKLDPRTGSVKEQNPAFIKTGDAAIISVRPTKPMVIEKVKEIPQLGRFAIRDMGMTIAAGMCQNVTPR
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
A0B7D6
C3MDH9
COBT_SINFN
N(1)-alpha-phosphoribosyltransferase
Sinorhizobium
MSASGLPFDDFRELLRNLPGPDAAALVAARERDAQLTKPPGALGRLEEIAFWLAAWTGRPPAVNRPLVAIFAGNHGVTRQGVTPFPSSVTAQMVENFAAGGAAINQICVTHDLGLKVFDLALDYPTGDITEEAALSERDCAATMAFGMEAIAGGTDLLCIGEMGIGNTTIAAAINLGLYGGTAEEWVGPGTGSEGEVLKRKIAAVERAVALHRDHLSDPLELMRRLGGREIAAMAGAILAARMQKVPVIIDGYVATAAAAILKAANPAALDHCLIGHVSGEPGHIRAIEKLGKTPLLALGMRLGEGTGAALAAGIVKAAAACHGGMATFAQAGVSNKD
Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
C3MDH9
A5UIZ2
PURA_HAEIG
IMP--aspartate ligase
Haemophilus
MGKSVVILGAQWGDEGKGKIVDLLTDRVKYVVRYQGGHNAGHTLIINGEKTVLRLIPSGMLHPNVTCLIGNGVVVSPEALMKEMGELESRGIKVRERLLISEACPLILPYHVAMDHAREAALGKKAIGTTGRGIGPAYEDKVARRGLRIGDLFNKEAFAEKLKNILEYYNFQLVNYYKVEPVDYQKTLDDVMAIADVITGMVADITTILDTARKNGEHILFEGAQGTMLDIDHGTYPYVTSSNTTAGGVATGSGFGPRNLDYVLGIIKAYCTRVGGGPFTTELFDDVGAEIARKGNEFGAVTGRPRRCGWFDAVAIRRAIQLNSISGFCMTKLDVLDGFDEVKICVAYKMPNGEIVEYAPLAAKDWDGVEPIYETLPGWKENTFRITDVNKLPQNCINYIKRIEEVTGVPIDILSTGPDRVETMILRDPFAA
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.
A5UIZ2
Q0S2N2
MOAA_RHOJR
Molybdenum cofactor biosynthesis protein A
Rhodococcus
MTAVAMGIPTVRSSVSLAGRPDVDQLVDRFGRVARDLRVSITEKCSLRCTYCMPEEGLPAIPAENLLTANEIVRLVDIAVHRLGVREVRFTGGEPLMRVDLEQMIAGCAERAPGIPLAMTTNAVGLEHRAAGLARAGLTRVNVSLDSVDREHFARLTRRDRLPSVIAGIRAAARAGLAPLKINAVLMPETLSGAADLLEWCLSEGVALRFIEEMPLDADHEWARENMVAADRLLAVLGERFTLTEHGREDPSAPAEEWLVDGGPATVGIIASVTRSFCSDCDRTRLTAEGTVRSCLFSDQEIDLRAALRSGAGDEELAQLWRGAMWNKWAGHGINADGFAPPQRSMGAIGG
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Q0S2N2
Q3YT18
SSRP_EHRCJ
Small protein B
Ehrlichia
MDVIIENRKVRFNYFIIQEFDAGIVLIGSEVKSLRQRKVSIAEAYVTEKNMELWLCNLHISEYNHASTKNHNPTRPRKLLLRKKQIYKISGNIKNDGFTVVPLSLYFNEKGLAKAKIVIVKGKKLHDKRETIKTRDWNREKSRVLRGN
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Q3YT18
O29511
DAPF_ARCFU
PLP-independent amino acid racemase
Archaeoglobus
MRIAFTKMHGNGNDFVLIDEFEGVIVGEEEKPRFVRAVCHRNFGVGADGALFVQPSQKADVRFRYFNSDGSEAAMCGNGIRCFSRYVVEEGYAGERLRVETLAGILELEVKRENGWWVKVDMGKPKFGREEIPAKTDVWGYEVEHDGRKFRIYAANTGVPHVAVFVDSLDFDIVPLARKIRYSEIFPEGTNVNFAKVDGDTITVRTYERGVEGETLSCGTGSVAVAAIANRLGLTGSKVDVVTKGGLLKIELTEDTAYMTGGASRVFDGILRLNELRYDI
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.
O29511
Q9AWZ8
PANB1_ORYSJ
Ketopantoate hydroxymethyltransferase 1
Oryza sativa
MMMMMRRAFRHLARQQRRPLSHVPESAVYGGPRPQDVGAAAGAGAGAGATRRVTVTTLRGKHRRGEPITVVTAYDYPSAVHVDSAGIDVCLVGDSAAMVVHGHDTTLPISLDVMLEHCRAVARGATRPLLVGDLPFGCYESSSTRAVDSAVRVLKEGGMDAIKLEGGAPSRISAAKAIVEAGIAVMGHVGLTPQAISVLGGFRPQGKTVDSAVKVVETALALQEAGCFSVVLECVPAPVAAAATSALQIPTIGIGAGPFCSGQVLVYHDLLGMMQHPHHAKVTPKFCKQFGNVGHVINKALSEYKQEVETRSFPGPSHTPYKIAAADVDGFANALQKMGLDEAANAAAAAAENAEKDGELPENK
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Q9AWZ8
A6Q4V8
PRMA_NITSB
Ribosomal protein L11 methyltransferase
unclassified Nitratiruptor
MDRYYYEYTVDIDAFKDEIESFLMDRFYNGIEESDGKLILRSEKSLDDIMDELRTYVDSLIKLFDTEIHLKITKEKKENIDWIEKYKKSITPVEVGEFYIHPSWYEPKEGKTNIKIDPALAFGSGHHETTRGCLNAIQKYVQPGMELLDVGCGSGILSIAAAKKGAVVDICDTDALALEESQKNFSLNGVEFREGWVGSAANAKKKYDIVIANIVADVLIMIAKDLQETTKEGGILILSGIIEKYRNKVKNRFDFSILEELQEGEWITMILRNDRGTDGK
Methylates ribosomal protein L11.
A6Q4V8
Q05FK2
RS13_CARRP
30S ribosomal protein S13
Candidatus Carsonella
MNINICGVLISKKKNIVFGLTKIYGIGYSMSLKICSKIENFKNKKFKDLTNEEKAKIENFINKINVENNLKTIIKENFKKKLNLNSYKSLRHKKKLPCRGQRTKTNAKTRKKMNHEII
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
Q05FK2
Q21RW7
RS17_ALBFT
30S ribosomal protein S17
Rhodoferax
MTEAKKSLKRTLVGKVVSDKRAKTVTVLIERRVKHELYGKIVGKSSKYHAHDETGEYKLGDIIEITESRPISKTKNWVATRLVQKAAVV
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Q21RW7
Q2T9W0
BACD1_BOVIN
BTB/POZ domain-containing protein KCTD13
Bos
MSAEASGPAAAEAPSLEVAKPSELEPGSAAYGLKPLTTNSKYVKLNVGGSLHYTTLRTLTGQDTRLKAMFSGRAEVLTDAGGWVLIDRSGRHFGTILNYLRDGSVPLPESTRELGELLGEARHYLVQGLIEDCQLALQQKRENVSPLCLIPTVTSPREEQQLLASTSKPVVKLLHNRSNNKYSYTSTSDDNLLKNIELFDKLALRFHGRLLFLKDVLGDEICCWSFYGQGRKIAEVCCTSIVYATEKKQTKVEFPEARIFEETLNILIYETPRGPDPALLEATGGAAGGGGASRGEDEDNREHRVRRIHVRRHITHDERPHGQQIVFKD
Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for synaptic transmission. The BCR(KCTD13) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and promoting synaptic transmission.
Q2T9W0
B7IUX9
GATA_BACC2
Glutamyl-tRNA(Gln) amidotransferase subunit A
Bacillus cereus group
MSLFDHSVSELHKKLNNKEISVTDLVEESYKRIADVEDNVKAFLTLDEENARAKAKELDAKIGAEDNGLLFGMPIGVKDNIVTNGLRTTCASKMLANFDPIYDATVVQKLKAADTITIGKLNMDEFAMGSSNENSGFYATKNPWNLDYVPGGSSGGSAAAVAAGEVLFSLGSDTGGSIRQPAAYCGVVGLKPTYGRVSRYGLVAFASSLDQIGPITRTVEDNAYLLQAISGIDRMDATSANVEVGNYLAGLTGDVKGLRIAVPKEYLGEGVGEEARESVLAALKVLEGMGATWEEVSLPHSKYALATYYLLSSSEASANLSRFDGVRYGVRSDNVNNLLDLYKNTRSEGFGDEVKRRIMLGTFALSSGYYDAYYKKAQQVRTLIKNDFENVFANYDVIIGPTTPTPAFKVGEKVDDPMTMYANDILTIPVNLAGVPAISVPCGFGANNMPLGLQIIGKHFDEATIYRVAHAFEQATDYHTKKASL
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
B7IUX9
B1VZM4
LIPB_STRGG
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
Streptomyces
MSELRFVRLGFGEQAVEYTEAWQKQREVHADRFEDRVPDTCLLLEHPPVYTAGRRTAESERPLDGTPVVDVDRGGKITWHGPGQLVGYPIQKLPRPVDVVAHVRRLEEALIRTAADFGVETSRIEGRSGVWVLGDPVERRQALGGLSLDFDPRLQDEEFDPRLNGPEYAPSNAGQRREDRKLAAIGIRVAKGVTMHGFALNVNPDNTWFDRIVPCGIRDAGVTSLSAELGREVTVEEVLPVAERHLRDILENAELAPRAVEQPKAAAPAPAPA
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.
B1VZM4
Q1LT59
HSPQ_BAUCH
Heat shock protein HspQ
Candidatus Baumannia
MIASKFGIGQQVRHKLFGYLGVIIDVDPEYSLDKPYIDKIAADDSLRTAPWYHVVMEDEDGKPVHTYLAEAQLGYEAFLEHPEQPTLDELAESIRLQLQAPRLRN
Involved in the degradation of certain denaturated proteins, including DnaA, during heat shock stress.
Q1LT59
Q6GIC2
ADDB_STAAR
ATP-dependent helicase/nuclease AddB
Staphylococcus
MTLHAYLGRAGTGKSTKMLTEIKQKMKADPLGDPIILIAPTQSTFQLEQAFVNDPELNGSLRTEVLHFERLSHRIFQEVGSYSEQKLSKAATEMMIYNIVQEQQKYLKLYQSQAKYYGFSEKLTEQIQDFKKYAVTPEHLESFIADKNMQTRTKNKLEDIALIYREFEQRIQNEFITGEDALQYFIDCMPKSEWLKRADIYIDGFHNFSTIEYLIIKGLIKYAKSVTIILTTDGNHDQFSLFRKPSEVLRHIEEISNELNISIERQYFNQLYRFNNQDLKHLEQEFDALQINRVACQGHINILESATMREEINEIARRIIVDIRDKQLRYQDIAILYRDESYAYLFDSILPLYNIPYNIDTKRSMTHHPVMEMIRSLIEVIQSNWQINPMLRLLKTDVLTTSYLKSAYLVDLLENFVLERGIYGKRWLDDELFNVEHFSKMGRKAHKLTEDERNTFEQVVKLKKDVIDKILHFEKQMSQAATVKDFATAFYESMEYFELPNQLMTERDELDLNGNHEKAEEIDQIWNGLIQILDDLVLVFGDEPMSMERFLEVFDIGLEQLEFVMIPQTLDQVSIGTMDLAKVDNKQHVYLVGMNDGTMPQPVTASSLITDEEKKYFEQQANVELSPTSDILQMDEAFVCYVAMTRAKGNVTFSYSLMGSSGDDKEISPFLNQIQSLFNQLEITNIPQYHEVNPLSLMQHAKQTKITLFEALRAWLDDEIVADSWLDAYQVIRDSDHLSQGLDYLMSALTFDNETVKLGETLSKDLYGKEINASVSRFEGYQQCPFKHYASHGLKLNERTKYELQNFDLGDIFHSVLKYISERINGDFKQLDLKKIRQLTNEALEEILPKVQFNLLNSSAYYRYLSRRIGAIVETTLSALKYQGTYSKFMPKHFETSFRRKPRTNDELIAQTLTTTQGIPINIRGQIDRIDTYTKNDTSFVNIIDYKSSEGSATLDLTKVYYGMQMQMMTYMDIVLQNKQRLGLTDIVKPGGLLYFHVHEPRIKFKSWADIDEDKLEQDLIKKFKLSGLVNADQTVIDALDIRLEPKFTSDIVPVGLNKDGSLSKRGSQVADEATIYKFIQHNKENFIETASNIMDGHTEVAPLKYKQKLPCAFCSYQSVCHVDGMIDSKRYRTVDETINPIEAIQNININDEFGGEQ
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddB nuclease domain is not required for chi fragment generation; this subunit has 5' -> 3' nuclease activity.
Q6GIC2
P66327
RS10_COREF
30S ribosomal protein S10
Corynebacterium
MAGQKIRIRLKAYDHEAIDASARKIVETVTRTGARVVGPVPLPTEKNVYAVIRSPHKYKDSREHFEMRTHKRLIDILDPTPKTVDALMRIDLPASVDVNIQ
Involved in the binding of tRNA to the ribosomes.
P66327
A9BFX6
ATPD_PETMO
F-type ATPase subunit delta
Petrotoga
MKASYFLASKYAQALLGTLEEKGEISRLDEYVEAFQRLKKALESSESLRDMVYSPLIPPKHIVSRMKDVSEFDDTIFVQFLEVLADKRRQNLIPFMSHILYQESLEREKVVEVRLVLPNEVSNTIINQVKQAIQNKTGRKIKLRTQFNEDLIGGLQLYIGDKFFDYSVKGFLQDIQSAYAPIGGGEIFES
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
A9BFX6
Q5M8Y2
UBE2F_XENTR
Ubiquitin-conjugating enzyme E2 F
Silurana
MLTLASKLKRDDGVKGSRTSSTTSDSTRRVSVRDRLLVKEVAELEANLPCTCKVNFPDPNKLHYFHLTVSPDESYYQGGRFQFEIEVPDAYNMVPPKVKCLTRIWHPNITETGEICLSLLREHSIDGTGWAPTRTLKDVVWGLNSLFTDLLNFDDPLNIEAAEHHLRDKDEYRNKVEDYIKRYAR
Accepts the ubiquitin-like protein NEDD8 from the uba3-nae1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase rbx2, but not rbx1, suggests that the rbx2-ube2f complex neddylates specific target proteins, such as cul5.
Q5M8Y2