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Full Name
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2.75k
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5.51k
AlphaFoldDB
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C4L660
RIMP_EXISA
Ribosome maturation factor RimP
unclassified Exiguobacterium
MSKITEVVESIALPIVERENMELVDVEFVKEGPDWFLRVYIDKPGGVDLDDCVNINEQLSEKLNETDPIEQAYYLDVSSPGAERPLKKPSDFERAVGKNVYMKTFAPIDGAKEFEGILTAYDGETVVIETRIKTRKKAVSLPVDKIAQARLAVTFS
Required for maturation of 30S ribosomal subunits.
C4L660
Q6MSP1
RL18_MYCMS
50S ribosomal protein L18
Mycoplasma
MKFTKAEARKRRHFRVRQKVVGTAERPRLNVFKSNTNFYAQIIDDTKGVTLVSASTLKMDLKSKSNTLAAQKVAEEIAKKALAANITQVVFDRNGYLYHGKIKAFAETARENGLKF
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
Q6MSP1
Q5W676
HXK5_ORYSJ
Hexokinase I
Oryza sativa
MGKAAAVGTAVVVAAAVGVAVVLARRRRRRDLELVEGAAAERKRKVAAVIEDVEHALSTPTALLRGISDAMVTEMERGLRGDSHAMVKMLITYVDNLPTGNEQGLFYALDLGGTNFRVLRVQLGGKEKRVVQQQYEEVSIPPHLMVGTSMELFDFIASALSKFVDTEGDDFHLPEGRQRELGFTFSFPVSQTSISSGTLIKWTKGFSINDAVGEDVVSELGKAMERQGLDMKIAALVNDTVGTLAGGRYADNSVVAAIILGTGTNAAYVENANAIPKWTGLLPRSGNMVINTEWGSFKSDKLPLSEFDKAMDFESLNPGEQIYEKLISGMYLGEIVRRILLKLAHDAALFGDVVPSKLEQPFVLRTPDMSAMHHDSSHDLKTVGAKLKDIVGVPDTSLEVRYITSHICDIVAERAARLAAAGIYGVLKKLGRDKMPKDGSKMPRTVIALDGGLYEHYKKFSSCLESTLTDLLGDDVSSSVVTKLANDGSGIGAALLAASHSQYAEID
Fructose and glucose phosphorylating enzyme.
Q5W676
Q6CK58
MSC3_KLULA
Meiotic sister-chromatid recombination protein 3
Kluyveromyces
MVFGMNLGNRRKATRVPDLSRYDYHYNGSGGNSVNQGDNYLKSHELSADAAFAASARAGSLVNYPERGYTNISRANSLRMGHPGQQQQQSSYIPRSYSFTARGAYAPRTGNVGNRRSVSAIPRTGTASSRGVGSRTGSMTGSVARVGSRTGSFAGGGNGSIIIKTQEVKDMMGRTQSITTQTIRRINGMEYVETTTQTAGLVEDPQFHFQQFAENDEFPISDELSATPPAAPLSESQPRTNQRLANFNSNAINNSAANNIRSDSEEEGEEHFTDASDVVEESGAFAEDDQDHFLAKVNKVDVDNNSKSYTSRKPLVQKQGVQQQQEVQHQGISQVQNTEAKSVGRKSTMSKRMTLRDTPNAQLEPEKDTTDQATPDNNATKRKSIFKSKKRNEAVAVPTVPTSDQKTLSQEEMYAIALEIAQQKYGHPTKTVSHSTDNGSRNEMTPILEDADVEQPHVLPTTLHLPTREEQIQHEQLQQPTAAIPTNEKSRHPKKKVKSILDRVVQFSQENSGNQPPKQHRGKQYSQQPPDVAPSNGTTDNFDTNASGHNINHNNNNHNNNNNTSSSSSLRHESGANPVVVTEDTTVLAASTAATPVDVNEPGNPDHVIPASSPSIDNTPRINEKTKSKKKNEKGSFFKRLFKSNKTHINTK
May be involved in the control of meiotic sister-chromatid recombination.
Q6CK58
Q62838
MUSK_RAT
Muscle-specific tyrosine protein kinase receptor
Rattus
MRELVNIPLLQMLTLVAFSGTEKLPKAPVITTPLETVDALVEEVATFMCAVESYPQPEISWTRNKILIKLFDTRYSIRENGQLLTILSVEDSDDGIYCCTANNGVGGAVESCGALQVKMKPKITRPPINVKIIEGLKAVLPCTTMGNPKPSVSWIKGDSALRENSRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGTAYSKLVKLEVEVFARILRAPESHNVTFGSFVTLRCTAIGMPVPTISWIENGNAVSSGSIQENVKDRVIDSRLQLFITKPGLYTCIATNKHGEKFSTAKAAATVSIAEWSKSQKESKGYCAQYRGEVCDAVLVKDSLVFFNTSYPDPEEAQELLIHTAWNELKAVSPLCRPAAEALLCNHLFQECSPGVLPTPMPICREYCLAVKELFCAKEWLAMEGKTHRGLYRSGMHFLPVPECSKLPSMHQDPTACTRLPYLDYKKENITTFPSITSSKPSVDIPNLPASTSSFAVSPAYSMTVIISIMSCFAVFALLTITTLYCCRRRREWKNKKRESAAVTLTTLPSELLLDRLHPNPMYQRMPLLLNPKLLSLEYPRNNIEYVRDIGEGAFGRVFQARAPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDNPNIVKLLGVCAVGKPMCLLFEYMAYGDLNEFLRSMSPHTVCSLSHSDLSTRARVSSPGPPPLSCAEQLCIARQVAAGMAYLSERKFVHRDLATRNCLVGENMVVKIADFGLSRNIYSADYYKADGNDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGLQPYYGMAHEEVIYYVRDGNILACPENCPLELYNLMRLCWSKLPADRPSFCSIHRILQRMCERAEGTVGV
Receptor tyrosine kinase which plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between the motor neuron and the skeletal muscle . Recruitment of AGRIN by LRP4 to the MUSK signaling complex induces phosphorylation and activation of MUSK, the kinase of the complex. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. May regulate AChR phosphorylation and clustering through activation of ABL1 and Src family kinases which in turn regulate MUSK. DVL1 and PAK1 that form a ternary complex with MUSK are also important for MUSK-dependent regulation of AChR clustering. May positively regulate Rho family GTPases through FNTA. Mediates the phosphorylation of FNTA which promotes prenylation, recruitment to membranes and activation of RAC1 a regulator of the actin cytoskeleton and of gene expression. Other effectors of the MUSK signaling include DNAJA3 which functions downstream of MUSK. May also play a role within the central nervous system by mediating cholinergic responses, synaptic plasticity and memory formation.
Q62838
P08897
COGS_HYPLI
Hypodermin C
Hypoderma
MKFLLVFALALATTSAFQHPASIFELREGRIINGYEAYTGLFPYQAGLDITLQDQRRVWCGGSLIDNKWILTAAHCVHDAVSVVVYLGSAVQYEGEAVVNSERIISHSMFNPDTYLNDVALIKIPHVEYTDNIQPIRLPSGEELNNKFENIWATVSGWGQSNTDTVILQYTYNLVIDNDRCAQEYPPGIIVESTICGDTCDGKSPCFGDSGGPFVLSDKNLLIGVVSFVSGAGCESGKPVGFSRVTSYMDWIQQNTGIIF
This enzyme is a serine protease capable of degrading the native triple helix of collagen. Also cleaves the B chain of insulin at the 15-Leu-|-Try-16 and 22-Arg-|-Gly-23 bonds. Hydrolyzes casein, but not Px-Pro-Leu-Gly-Pro-DArg, BzArgNHPh, AcTyrNHPh, 2-naphthyl phosphate, 2-naphthyl butyrate, 2-naphthyl caprylate, 2-naphthyl myristate, L-leucine 2-2-naphthylamide, L-valine 2-naphthylamide, L-cysteine 2-naphthylamide or L-glutarylphenylalanine 2-naphthylamide.
P08897
Q8F5I5
TPIS_LEPIN
Triose-phosphate isomerase
Leptospira
MRKTIIAGNWKMNLSLKEAVFLAHSIREKIPSISKDKVSMVFPSTLHLENVSKILEGSSVIVGAQNCYHSGLAAFTGETSPDQLKEIGVKVVMVGHSERRQFLGESNFFCNDKIRFLLKNEFTVLYCVGETLSERESGKTLEVLSSQIREGLKGIDSVFFSNLILAYEPVWAIGTGKVATPSQAQEVHSFIRKEISGLFVGASSISESISILYGGSVKPDNIQDLLKEKDIDGGLVGGASQKISSFAELF
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Q8F5I5
Q0IFL2
RUVB1_AEDAE
Pontin
Stegomyia
MKIEEVKSTVKTQRIAAHSHVKGLGLDENGVPLQMAAGLVGQKDAREAAGIVVDLIKSKKMSGRALLLAGPPGTGKTAIALAIAQELGNKVPFCPMVGSEVFSSEIKKTEVLMENFRRSIGLRIRETKEVYEGEVTELTPVETENPMGGYGKTISNVVIGLKTAKGTKQLKLDPSIYESLQKEKVEVGDVIYIEANSGAVKRQGRSDTFATEFDLETEEYVPLPKGDVHKKKEVVQDVTLHDLDVANARPQGGQDVLSMVGQIMKPKKTEITDKLRMEINKVVNKYIDQGIAELVPGVLFIDEVHMLDLECFTYLHKSLESAIAPIVIFATNRGRCVIRGTDDIISPHGIPLDLLDRLLIVRTAPYNLSEIEQIIKLRAQTEGLSVEDSAIQALSEIGDNTTLRYAVQLLTPAHQNCKVNGRTQITKDDIVEVNGLFLDAKRSAKFLQEENTKYMM
Proposed core component of the chromatin remodeling Ino80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.
Q0IFL2
P0DM36
LECG_AGKPI
C-type lectin APL
Agkistrodon
NNCPHDWLPMNGLCYKIFDELKAWEDAERFCRKYKPGCHLASFHTYGESLEIAEYISDYHKGQAEVWIGLWDKKKDFSWEWTDRSCTDYLTWDKNQPDVYQNKEFCVELVSLTGYRLWNDQVCESKNAFLCQCKF
Beta-galactoside lectin that agglutinates rabbit and human erythrocytes in a calcium-dependent fashion (MHC is 0.21 ug/ml on rabbit erythrocytes). Galactose (15 mM), lactose (20 mM), rhamnose (20 mM) and EGTA strongly inhibit this activity.
P0DM36
Q1CS16
RS6_HELPH
30S ribosomal protein S6
Helicobacter
MRHYETMFILKPTLVEEEIKSKIEFYKEVITKHHGVIETSLDMGMRNLAYEIKKHKRGYYYVAYFKAEPSMILELERLYRINEDVLRFIVIKYESKKEVEAWHALVDRANKKPSHAKEKHEKTEHTHSHHLEEAESVGSHSE
Binds together with S18 to 16S ribosomal RNA.
Q1CS16
Q1QVG8
MURC_CHRSD
UDP-N-acetylmuramoyl-L-alanine synthetase
Chromohalobacter
MTASSVHSPVRQNRTGLGMRRIRHIHFVGIGGAGMCGIAEVLANQGYIVSGSDLRESAVTRHLRDCDIRVYIGHVDEHAHGADVLVVSTAVDLENPEIRWAREHRIPVVRRAEMLAELMRFRHGIAVAGTHGKTTTTSLTSTLLAEGGLDPTFVIGGKLTSAGTNARLGEGDYLVAEADESDASFLHLQPMVSIVTNIDADHMATYAGDFARLKDTFLEFLHNLPFYGLAVLCLDDDNVRGLLPRVQRQFVTYGFAEDADYRLRDFVQRGGEVQFTAERPPGMAPLEIRLGMPGRHNALNALAAIAVASDAGVDDAAIQQGLLHFAGVGRRFQVHGHYPAPGGEGDVMLVDDYGHHPREVEMVIDAVRAGWPERRLVMLYQPHRYSRTRDLYEDFVRVLSGVDTLLLLDVYSAGESSIPGAEGRTLAGSIRQRGQVDPIFVESKQELPALLSRVLRPDDILITQGAGDIGGISLRLAAGQLDLNGMEL
Cell wall formation.
Q1QVG8
A6UWH7
MTRA_META3
N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit A
Methanococcus
MADKKAPASGWPIVSGEYVVGNPESCVAVVTLGSHGLDEAAIEAGAAISGPCHTENLGIEKVVANYISNPNIRFMLVTGSEVQGHITGQCFKALYENGIGDDGGIIGAKGAIPFLENAGQDAISRFQNQLVEIVDLIDVEDTGKISSAIKDCISKDPGAFEEDPMILDLEGGGGEAGADESTSIKPAAPETVLLEARMRMISEKINDAALIAKFNSGYYNGKIQGIAIGLFLSLLIFSLL
Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
A6UWH7
F4JP52
PQT3_ARATH
null
Arabidopsis
MAIYYKFKSARDYDTISMDGPFITVGLLKEKIYETKHLGSGKDLDIVISNAQTNEEYLDEAMLIPKNTSVLIRRVPGRPRIRIITREEPRVEDKVENVQADMNNVITADASPVEDEFDEFGNDLYSIPDAPAVHSNNLCHDSAPADDEETKLKALIDTPALDWHQQGADSFGPGRGYGRGMAGRMGGRGFGMERTTPPPGYVCHRCNVSGHFIQHCSTNGNPNFDVKRVKPPTGIPKSMLMATPNGSYSLPSGAVAVLKPNEDAFEKEMEGLTSTTRSVGEFPPELKCPLCKEVMRDAALASKCCLKSYCDKCIRDHIIAKSMCVCGATHVLADDLLPNKTLRDTINRILESGNSSAENAGSMCQVQDMESVRCPPPKALSPTTSAASGGEKKPAPSNNNETSTLKPSIEIAEITSAWASAEIVKVEKPVDASANIQGSSNGKEAAVSQLNTQPPKEEMPQQVASGEQGKRKKKKPRMSGTDLAGPDYMMPMGPGPGNQYFNGFQPGFNGVQHGFNGVQPGFNGFHHGFNGFPGPFPGAMPPFVGYGFGGVIHPDPFAAQGFGFPNIPPPYRDLAEMGNRMNLQHPIMGREEFEAKKTEMKRKRENEIRRSEGGNVVRDSEKSRIMNNSAVTSSPVKPKSRQGPPPPISSDYDRRRRSDRSSPERQSSRRFTSPPRSSSRKSERDRHHDLDSEHDRRRDRPRETDRKHRKRSEKSSSDPTVEIDDNNKSNVFTRISFPEESSGKQRKTSKSSPAPPESSVAPVSSGRRHHSRREREMVEYDSSDDEDRHFKRKPSRYKRSPSVAPSDAGDEHFRHSKRSKGERARA
E3 ubiquitin ligase acting as a negative regulator of oxidative stress tolerance, probably by mediating 26S proteasome-mediated degradation of PRMT13/PRMT4B, thus preventing APX1 and GPX1 accumulation via the reduction of histone H3 methylation (H3R17me2a). Confers sensitivity to cadmium CdCl(2) and salt NaCl stresses.
F4JP52
P55311
CATA_SOLME
Catalase
Solanum
MDLSKYRPSSAYDTPFLTTNAGGPVYNNVSSLTVGPRGPVLLEDYHLIEKLATFDRERIPERVVHARGASAKGFFEVTHDVSHLTCADFLRAPGVQTPVICRFSTVVHERGSPESIRDIRGFAVKFYTREGNFDLVGNNVPVFFNRDAKSFPDTIRALKPNPKSHIQENWRILDFFSFLPESLHTFAFFYDDVCLPINYRHMEGFGVHAYQLINKAGKAHYVKFHWKPTCGVKSMTEEEAIRVGGTNHSHATKDLYDSIAAGNYPEWKLFIQIMDPEDVDKFDFDPLDVTKTWPEDILPLMPVGRLVLNRNIDNFFAENEQLAFNPGHIVPGVYYSEDKLLQTRIFAYADTQRHRIGPNYMQLPVNAPKCAHHNNHRDGAMNFMHRDEEVDYLPSRFDPCRPAEQYPIPSCVLTGRREKCVIPKENNFKQAGERYRTWEPDRQDRYINKWVESLSDPRVTHEIRSIWISYLSQADKSCGQKVASRLLVKPTM
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
P55311
P05709
SIM_DROME
Protein single-minded
Sophophora
MTNHRRVRKDCYESRLHDIAKTCAMKEKSKNAARTRREKENTEFCELAKLLPLPAAITSQLDKASVIRLTTSYLKMRQVFPDGLGEAWGSSPAMQRGATIKELGSHLLQTLDGFIFVVAPDGKIMYISETASVHLGLSQVELTGNSIFEYIHNYDQDEMNAILSLHPHINQHPLAQTHTPIGSPNGVQHPSAYDHDRGSHTIEIEKTFFLRMKCVLAKRNAGLTTSGFKVIHCSGYLKARIYPDRGDGQGSLIQNLGLVAVGHSLPSSAITEIKLHQNMFMFRAKLDMKLIFFDARVSQLTGYEPQDLIEKTLYQYIHAADIMAMRCSHQILLYKGQVTTKYYRFLTKGGGWVWVQSYATLVHNSRSSREVFIVSVNYVLSEREVKDLVLNEIQTGVVKREPISPAAQAAQAAQAAQAAQAAQAAQAAQAAQAAQAAHVAQAVQAQVVVVPQQSVVVQPQCAGATGQPVGPGTPVSLALSASPKLDPYFEPELPLQPAVTPVPPTNNSSSSSNNNNGVWHHHHVQQQQQSGSMDHDSLSYTQLYPPLNDLVVSSSSSVGGGTASSAGGGSSASASSSGVYSTEMQYPDTTTGNLYYNNNNHYYYDYDATVDVATSMIRPFSANSNSCSSSSESERQLSTGNASIVNETSPSQTTYSDLSHNFELSYFSDNSSQQHQHQQQQQHLMEQQHLQYQYATW
Transcription factor that functions as a master developmental regulator controlling midline development of the ventral nerve cord. Required to correctly specify the formation of the central brain complex, which controls walking behavior. Also required for correct patterning of the embryonic genital disk and anal pad anlage. Plays a role in synapse development.
P05709
Q2FPC7
G1PDH_METHJ
sn-glycerol-1-phosphate dehydrogenase
Methanospirillum
MSTDPVQVLQPDGFNKSRWTQLPRDVLIGHQAIMQLPDIIADIKPGRSVLLISGGTTREVAGNTVADILKDQYEVRRFVAGKLDADTLEACSQASSSADFLIGVGGGRVIDCAKIVSYKQGKPFISVPTAASHDGIISGRATLPTETGSVSVGAHPPIAVVADTGIISQAPHRLMASGCADVISNYTAILDWELAHRLRGEQISEYAIALSKMTAEILVKDANLIKPGQEEAAWIVVKALVSSGVSMAIAGSSRPASGGEHKFGHALERLMPGAALHGEACGIGSIMTMYLHGGDWREIRSSLARIGAPTTPRELNIPDEVIVEALMKARDIRPERFTILDMGLTRESAEHLVQMLYEE
Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.
Q2FPC7
P39662
HMP_CUPNH
Nitric oxide dioxygenase
Cupriavidus
MLTQKTKDIVKATAPVLAEHGYDIIKCFYQRMFEAHPELKNVFNMAHQEQGQQQQALARAVYAYAENIEDPNSLMAVLKNIANKHASLGVKPEQYPIVGEHLLAAIKEVLGNAATDDIISAWAQAYGNLADVLMGMESELYERSAEQPGGWKGWRTFVIREKRPESDVITSFILEPADGGPVVNFEPGQYTSVAIDVPALGLQQIRQYSLSDMPNGRSYRISVKREGGGPQPPGYVSNLLHDHVNVGDQVKLAAPYGSFHIDVDAKTPIVLISGGVGLTPMVSMLKVALQAPPRQVVFVHGARNSAVHAMRDRLREAAKTYENLDLFVFYDQPLPEDVQGRDYDYPGLVDVKQIEKSILLPDADYYICGPIPFMRMQHDALKNLGIHEARIHYEVFGPDLFAE
In the presence of oxygen and NADH, FHP has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2), both in vitro and in vivo, and it has been suggested that FHP might act as an amplifier of superoxide stress. Under anaerobic conditions, FHP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.
P39662
P80711
CLAVB_STYCL
Clavanin-B
Styela
VFQFLGRIIHHVGNFVHGFSHVF
Has antimicrobial activity.
P80711
Q7UK56
GATB_RHOBA
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Rhodopirellula
MTASAILACQKYPVTTIIGLEVHVQLKTQTKLFCGCTTEFGAPPNTQVCPVCLGMPGALPVMNREAIALSVKTGLALNCDIPPLTKWDRKQYFYPDLPKGYQISQFDLPICADGHLAISTDDGETERRIGLVRAHLEEDAGKSMHDEASGISDTKIDLNRCGTPLLEIVSQPDLRSADEAKAYLSELKLLLTHLKVSDCEMQEGSLRVDANVNLHIDVEGKKIATPIVEIKNLNSFRNVQRAIDYEVQRQLVDWEENRQTIDDAPKTTRGWDDSAEQTFAQREKEESADYRYFPDPDLLPVRLPREYVESISESLGELPAVTRERLQTQHGIKPYDADVIVNQGPDVIDYFETAVGASGDGRRTSSWMMQDVMRTMKERSIDIDAFPIPAERLGELIRMIADGKLDNNRARDVFEHLLTHDESIEQATKSLGIEAVDDDALESLCKELLAANPQVVEDVKGGKQQAVGALIGQAKKKNPNASPQAVRQLLIDLIAKM
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Q7UK56
A0PTP9
AMPA_MYCUA
Leucyl aminopeptidase
Mycobacterium
MTAESGDQIPTVHVATSLPKRRVSSSVLIVPVVSTGDDEQSGERPGAVVASAEPFLSADAIAEIEAGLRALDATGASDQVHRLVVSSLPVSSVLTVGLGKPRYEWTPDAVRRAAGAAARALGTAKAVVTTLADLPGDGVCAAAVEGLILGSYRFSAFRSAKTAPKDAGLHKITVLTTTKDARKHCAHGAAVATAVATARDLVNTPPSHLYPAELARRAKVLGESVGLEVQVLDEKALQKAGYGGLVGVGQGSSRPPRLVRLTHRGSRLAKNPRRAKKVALVGKGVTFDTGGISIKPAASMHYMTSDMGGAAAVIATVALAAQLELPINVIATVPIAENMPSATAQRPGDVLTQYGGTTVEVLNTDAEGRLILADAIVRACEDNPDYLIETSTLTGAQTVALGARIPGVMGSDEFRDRVAAISQQVGENGWPMPLPDELKDDLKSTVADLANVSGQRFAGMLVAGVFLREFVADAVDWAHIDVAGPAYNTGSAWGYTPKGATGVPTRTMFAVLEDIAANG
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
A0PTP9
Q3B1A2
RECO_CHLL3
Recombination protein O
Pelodictyon
MIVKTRAVVLREIKYRDQSKILTLYTREFGRLACILKGGRNPKNRLSGIFSAGNVLDIVLYRKPEREVQLISDGSLVSCPMVPGPDIERFGVLYRIIDLVRLTTEHDGRSPRLFSLLESTLLELNRERVAYRTLYAWFLLRFISLQGFAPELCRCVFSGREIAADAAGGPRGELLFVMNPGGLALPGTACTDGRNVRPILPEAADLLAALSRTSTAESAAGGSGIPEGSAALFCGTLLQEYCRHHLEHTGGQKNLAVISQLLAE
Involved in DNA repair and RecF pathway recombination.
Q3B1A2
P56551
ECNA_CITFR
Entericidin A
Citrobacter freundii complex
MMKRLLGLVMLLLFTCTLLTGCNTARGFGEDIKHLGNSISHAAS
Acts as antidote to the effect of entericidin B.
P56551
B9DVB6
RBFA_STRU0
Ribosome-binding factor A
Streptococcus
MANHRIDRVGMEIKREVNAILQKKVRDPRVEGVTITEVQMLGDLSAAKVYYTVMSDLASDNQKAQLGLEKATGTIKRELGKNLTMYKIPDLIFEKDNSIAYGNKIDQLLRALDKKS
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.
B9DVB6
Q48NU0
GLPE_PSE14
Thiosulfate sulfurtransferase GlpE
Pseudomonas
MTEFKRIPPEQAQALREQGAVLVDVRDAQTFQSNHIPDSVHLDNHSIADFIAKADLDKPLVVVCYHGNSSQSAAAYLVGQGFSDVYSVDGGFELWRATYPDETVQG
Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Q48NU0
A1U613
DNAJ_MARN8
Chaperone protein DnaJ
Marinobacter
MAKRDYYEVLGISRDADEKEIKRAYRKLAMKYHPDRNPDDKDAETKFKEASEAYEILADSSKRAAYDQFGHAGVDGQAGGGFGGGGASFSDIFGDVFGDIFGGGGRGRTTRGADLRYTLELDLEEAVKGKTVKINIPGHKECEACDGSGAEKGSRPETCGTCQGMGQVRMQQGFFTVQQACPTCRGSGQIIKNPCKSCHGQGRVRQEKTLSVKVPPGVDTGDRIRLSGEGEMGVDGGPPGDLYVQVAVREHSIFTRDGRNLYCEVPISIVDATLGGELEVPTLDGRVKLKIPPETQTGKLFRLRNKGVSPVRGGPAGDLLCRVIVETPVNLTKRQKELLEEFQQTLDGNNGTHHAPKKTSWFEGVKNFFDEMKF
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
A1U613
Q049P0
FMT_LACDB
Methionyl-tRNA formyltransferase
Lactobacillus
MNSVIFLGTPQFGATVLEGLIKAGYHILAVVTQPDKKVGRKQKVVYSPVKEVALANDLPLYQPVRLSKSDELDELLQLDADFIITAAFGQFLPTKFLKSAKIAAVNVHGSLLPKYRGGAPIQYAVRNGDAETGVTIMEMVKEMDAGDMYAQASLPIRPDETSGEVFEELAPLGRDLLLETLPKIASGEIVKKPQDPSQVVFSPTISKAEERISLKLTAKEAKNLIRALNPDPGAYLVIKGQRLKVWKAEVADDNTSLPAGHLLTNQGRFAISFAGNTVLNLLEVQPNGKKAMAIKDFLNGQGKKFAAGEKIVDED
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.
Q049P0
A4WWS0
HSLU_CERS5
Unfoldase HslU
Cereibacter
MTDLTPREIVSELDRFIIGQKDAKRAVAVALRNRWRRKQLSDDIRDEVYPKNILMIGPTGVGKTEISRRLARLAKAPFLKVEATKFTEVGYVGRDVDSIIRDLVDAAIVETRARMREDVKSRAVKAAEDRVIEAIAGRDAREQTREMFRGKLKRGELDATVIEVEVADTSNPMQMLDPTGQGQMGMMNLGEIFGKAFGGRTTRRKMTVAESHDILMNEEADKLLDDEVVKATALEAVQENGIVFIDEIDKVCARSDMRGADVSREGVQRDLLPLIEGTTVSTKYGPVKTDHILFIASGAFHIAKPSDLLPELQGRLPIRVELRALTEEDFVRILSETDNALTRQYKALMKTEKVGITFTEEGIKALASIAAEVNRSVENIGARRLYTVMERVFEELSFHAPDRSGEEVTVDAAYVEKNLGELARSTDLSRYVL
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
A4WWS0
Q5E2Y4
KHSE_ALIF1
Homoserine kinase
Aliivibrio
MSVVVYAPASIGNVSVGFDVLGAAVSPIDGTLLGDRVLVELGSEAFTLATAGSFVDKLPENPKDNIVYDCWCVFSRELNKKNVALKNVHMILEKNMPIGSGLGSSACSIVAALDALNQFHDNPLNDMELLALMGEMEGQISGGIHYDNVAPCYLGGLQLMVEELGIISQEVPCFDEWYWVMAYPGIKVSTAEAREILPSQYRRQDVIAHGRNLAGFIHACYSKQPELAAKMIKDVVAEPYRERLLPNFAKAREYAASAGALTTGISGSGPTLFSICKDKDVADRVSRWLQENYVQNNEGFVHVCRLDKQGSQVTGSKL
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Q5E2Y4
Q7UKV4
RL9_RHOBA
50S ribosomal protein L9
Rhodopirellula
MSKSATSHFKRLPKGQNGGIELLLIHNVEHLGRQGDLVEVKAGYALNYLLPQGLATIATDHHKRMVEKHREKLRAIELEKLKSYREQADELAKQSITIEANANDEGHLYGSVGPHEIVDALKASGITLAQDQIRLEGPLKELGLYTVKIHLHSEVDASLKVWVVPTVAAEGGEPGAS
Binds to the 23S rRNA.
Q7UKV4
P19595
UGPA_SOLTU
UDP-glucose pyrophosphorylase
Solanum
MATATTLSPADAEKLNNLKSAVAGLNQISENEKSGFINLVGRYLSGEAQHIDWSKIQTPTDEVVVPYDKLAPLSEDPAETKKLLDKLVVLKLNGGLGTTMGCTGPKSVIEVRNGLTFLDLIVKQIEALNAKFGCSVPLLLMNSFNTHDDTLKIVEKYANSNIDIHTFNQSQYPRLVTEDFAPLPCKGNSGKDGWYPPGHGDVFPSLMNSGKLDALLAKGKEYVFVANSDNLGAIVDLKILNHLILNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLSAIKRLVEADALKMEIIPNPKEVDGVKVLQLETAAGAAIKFFDRAIGANVPRSRFLPVKATSDLLLVQSDLYTLTDEGYVIRNPARSNPSNPSIELGPEFKKVANFLGRFKSIPSIIDLDSLKVTGDVWFGSGVTLKGKVTVAAKSGVKLEIPDGAVIANKDINGPEDI
Plays a central role as a glucosyl donor in cellular metabolic pathways.
P19595
Q0HMX6
AROQ_SHESM
Type II DHQase
Shewanella
MNHKVLLINGPNLNLLGRREPSVYGHQTLADIVATLSEQAQAAGVELEHIQSNAEFELINAIHATDAQMIIINPAAFTHTSVALRDALLGVDIPFFEVHLSNVHAREPFRHHSYLSDKAIGVICGFGAQGYEFALAAAIKRLKA
Catalyzes a trans-dehydration via an enolate intermediate.
Q0HMX6
G3MJ83
E1182_AMBMU
Evasin P1182
Amblyomma
MALNWSFRVIFVSTMWCALLKFATLGEPKDDNDYGGGCPFVVLGNGTHAKPAGCSHLCNGAPETLDNIECYNVTEEVAKRMTPGIPYACWLGWCNKGECKRGNRTEVCYRGSEEE
Salivary chemokine-binding protein which binds to host chemokines CCL2, CCL3, CCL4, CCL8 and CCL18.
G3MJ83
Q09MG0
PETL_CITSI
Cytochrome b6-f complex subunit VI
Citrus
MPTITSYFGFLLAALTITSALFIGLSKIGLI
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
Q09MG0
Q0C4M2
OTC_HYPNA
Ornithine carbamoyltransferase
Hyphomonas
MTIRHFLDIWPLESAELRAILDQAHAMKKARAGWPKGKIDAGAPLDGHTLAMIFEKSSTRTRFSFDMAMRQLGGSSITATSNDMQLGRGETVEDTAKVLSRFVDAVMIRANDHADVEAFADAASVPVINGLTDRSHPCQIMADLMTLEEHGLTLRGARLAWVGDGNNVCASFIHAAPKFGFSLAVGTPKRFAPDEDDLEIAAELQGRIDLYETAEEAVAGADVVIADTFVSMGDVDAERRLEILDPYAVTEELMELAAGGAKFLHCLPAHRGEEVDAEVIDGPASLVFDEAENRLHAQKAILRWCLGK
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Q0C4M2
A7XRY3
TDIB_EMENI
Terrequinone biosynthesis protein B
Aspergillus subgen. Nidulantes
MATEYWSRHLRSVLAPLFAAAGTYSPEDQESHLAFIDEHIAPNLGPLPWEPHGPYSTPSSLVGSPFDPSINIVSSGKAKVRFDFDVISPPDRTGPDPFAEGSAREILHRLADLVGADTQWMGYLMDALYLTPAEAEVAKTKLPPGVAIPPSSVGFDFDGPERTLKFYIPSVRKALATGQDVSELMLKTLRGLQPLGSELVPAMDLIASYLSTRTNDAMLPLVGIDCLDPRTHKNARVKCYLHTSSNSFAVVRDVLTLGGRLSDDTSLKRVETLKSVWPLLINELEGPQSDAATMDESWSKPERLNRTGYSGIQYTIEITPGQAIPDTKIYVPLFQYTDSSEVAERNFESALKKLGNEWGLSGKYRSVMQEIFKDVENYGQTYASFSYTEGKGVYTTSYVAMPIKDEGGGSLAGDFGFRN
Indole prenyltransferase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent . The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD . The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules . The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain . TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 . Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 .
A7XRY3
Q5E2M9
RL13_ALIF1
50S ribosomal protein L13
Aliivibrio
MKTFVAKPAAVKRDWYVVDAEGKTLGRIATEIASRLRGKHKAEYTPHVDTGDYIIVINAEKVRVTGKKASDKIYYRHSEFPGGLKSISFEKLIDRKPEMVIELAVKGMLPRGPLGRAMYRKLKVYAGAEHNHTAQQPQVLDI
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
Q5E2M9
Q6XMH6
MAP2_ENCHA
Peptidase M
Encephalitozoon
MKFILMNQAAELPIEFLPRDGAYRKGRLLDSKNAEVENTTESDILQDARRAAEAHRRVRYKVQSIIKPGMTLLEIVKSIEDSTRILLSGERNNGIGFPAGMSMNSCAAHYSVNPGEKDIILTENDVLKIDFGTHSNGRIMDSAFTIAFKEEFEPLLMAAKEGTETGIRSLGIDARVCDIGRDINEVISSYEMEVDGKKWAIRPVSDLHGHSISQFKIHGGISIPAVNNRDPTRITGDTFYAVETFATTGEGFINDRSPCSHFMINTHKSRKLYNKDLIKVYEFVRDSFGTLPFSPRHLDYYNLVEGSALKSVNLLTMMGLFTPYPPLNDIDGSKVAQFEHTVYLSESGKEILTRGDDY
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Q6XMH6
A0M584
RS8_GRAFK
30S ribosomal protein S8
Gramella
MNTDPIADYLTRIRNANAANHRVVEIPASNVKKEITKILFDQGYILSYKFEDTTAQGTIKIALKYDKLTKEPVIKKIQRISKPGLRKYAGSTEIPRILNGLGIAVVSTSHGVMTGKQAKANKVGGEVLCYVY
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
A0M584
Q5SBP3
LLOS_OCIBA
R-linalool synthase, chloroplastic
Ocimum
MSCARITVTLPYRSAKTSIQRGITHCPALLRPRFSACTPLASAVPLSSTPLINGDNSPLKNTHQHVEERSSKRREYLLEETARKLQRNDTESVEKLKLIDNIQRLGIGYYFEDAIDAVLRSPFSAEEEEDLFTAALRFRLLRHNGIQVTPEIFLKFKDERGEFDESDTLGLLSLYEASNLGVTGEEILEEAMEFAEPRLRRSLSELAAPLRSEVAQALDVPRHLRMARLEARRFIEQYGKQSDHDGDLLELAILDYNQVQAQHQSELTEITRWWKQLGLVEKLGFGRDRALECFMWTMGILPHPKYSSSRIESAKAAALLYVIDDIFDTYGKMDELILFTDAIRRWDLEAMEGLPEYMKICYMALYNTTNEICYRVLKDTGRIALPYLKSVWIETIEAYMVEVKWFSGGSAPKLEEYIENGASTVGAYMVLVHLFFLIGEGLTHQNVLFFKQKPYHKPFSAAGRIFRLWDDLGTSQEEEERGDMASSIRLFMKEYKLSTVEEARSCVLEEISRLWKDLNEGLISIKDALPLTIVKVALNIARTSQVVYKHEQHTYMLSVDNYVEALFFTPLLSS
Monoterpene synthase that catalyzes the formation of (3R)-linalool from geranyl diphosphate.
Q5SBP3
A4IJT3
ACPS_GEOTN
4'-phosphopantetheinyl transferase AcpS
Geobacillus
MIVGIGIDIVELERIQSLLERNRKFLDRILTPREREQFDQLAPARQVEFLAGRFAAKEAYAKALGTGIGRHVSFQDIEIVSDEYGKPSIAARRDGEVIHLSISHSRDYAIAQVIIERFGPAKPSDACHG
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
A4IJT3
P9WJ02
SIR_MYCTO
Sulfite reductase [ferredoxin]
Mycobacterium tuberculosis complex
MTTARPAKARNEGQWALGHREPLNANEELKKAGNPLDVRERIENIYAKQGFDSIDKTDLRGRFRWWGLYTQREQGYDGTWTGDDNIDKLEAKYFMMRVRCDGGALSAAALRTLGQISTEFARDTADISDRQNVQYHWIEVENVPEIWRRLDDVGLQTTEACGDCPRVVLGSPLAGESLDEVLDPTWAIEEIVRRYIGKPDFADLPRKYKTAISGLQDVAHEINDVAFIGVNHPEHGPGLDLWVGGGLSTNPMLAQRVGAWVPLGEVPEVWAAVTSVFRDYGYRRLRAKARLKFLIKDWGIAKFREVLETEYLKRPLIDGPAPEPVKHPIDHVGVQRLKNGLNAVGVAPIAGRVSGTILTAVADLMARAGSDRIRFTPYQKLVILDIPDALLDDLIAGLDALGLQSRPSHWRRNLMACSGIEFCKLSFAETRVRAQHLVPELERRLEDINSQLDVPITVNINGCPNSCARIQIADIGFKGQMIDDGHGGSVEGFQVHLGGHLGLDAGFGRKLRQHKVTSDELGDYIDRVVRNFVKHRSEGERFAQWVIRAEEDDLR
Catalyzes the reduction of sulfite to sulfide, a step in the biosynthesis of sulfur-containing amino acids and cofactors.
P9WJ02
Q42560
ACO1_ARATH
Citrate hydro-lyase 1
Arabidopsis
MASENPFRSILKALEKPDGGEFGNYYSLPALNDPRIDKLPYSIRILLESAIRNCDEFQVKSKDVEKILDWENTSPKQVEIPFKPARVLLQDFTGVPAVVDLACMRDAMNNLGGDSNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSNAFHNMLVVPPGSGIVHQVNLEYLARVVFNTNGLLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLTGKLRDGMTATDLVLTVTQMLRKHGVVGKFVEFHGEGMRELSLADRATIANMSPEYGATMGFFPVDHVTLQYLRLTGRSDDTVSMIEAYLRANKMFVDYSEPESKTVYSSCLELNLEDVEPCVSGPKRPHDRVPLKEMKADWHSCLDNRVGFKGFAVPKEAQSKAVEFNFNGTTAQLRHGDVVIAAITSCTNTSNPSVMLGAALVAKKACDLGLEVKPWIKTSLAPGSGVVTKYLAKSGLQKYLNQLGFSIVGYGCTTCIGNSGDIHEAVASAIVDNDLVASAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDFETQPIGTGKDGKQIFFRDIWPSNKEVAEVVQSSVLPDMFKATYEAITKGNSMWNQLSVASGTLYEWDPKSTYIHEPPYFKGMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRRDFNSYGSRRGNDEIMARGTFANIRIVNKHLKGEVGPKTVHIPTGEKLSVFDAAMKYRNEGRDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVISKSFERIHRSNLVGMGIIPLCFKAGEDAETLGLTGQELYTIELPNNVSEIKPGQDVTVVTNNGKSFTCTLRFDTEVELAYFDHGGILQYVIRNLIKQ
Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. Contributes to oxidative stress tolerance . May have a role in respiration .
Q42560
A8H2P5
APT_SHEPA
Adenine phosphoribosyltransferase
Shewanella
MVMNTDSLALIKNSIKTIPNYPKEGILFRDVTSLLEDPQAYKLTIGLLVEHYKDQGFTKVVGTEARGFLFGAPLALELGIGFVPVRKPGKLPRETISESYELEYGHDVLEIHVDAINADDKVLVIDDLLATGGTIEATVKLIRKLGGSVNDAAFVISLPDLGGEERLKAMDLKLISLCEFEGE
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
A8H2P5
A9BDY5
FPG_PROM4
DNA-(apurinic or apyrimidinic site) lyase MutM
Prochlorococcus
MPELPEVETVRKGLEKRLKNFYIDNVEVLSERSIASNGGSNVFIFNLKDLVFGRWSRRGKYLIASLCKESDLIEEIPSGTLVVHLRMTGYFEWHQNTKAPCTHTRVRFWNKKGSEIRFIDIRNFGQMWWIPPNKLPSEVINGLKNLGPEPFSKDFNPEYLKYCLKGRKRSIKSSLLDQSILAGVGNIYADESLFEAGITPIKASGDLNGCELKKLCKSLTRILKASIGKGGTTFSDFRDLEGLNGTYGGYAWVYRRNQKPCRKCGTLIEKTKVAGRSTHWCPNCQN
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
A9BDY5
Q9CGD7
KHSE_LACLA
Homoserine kinase
Lactococcus
MKIIVPATSANLGAGFDSIGIAVNLYLTVEVLEESNDWKIDHDLGNNIPTDEKNLLLTTLSAVLKAKNSSLSAKYHLKMTSEVPLARGLGSSSSVIIAGIELANQLAKLNLTTEEKLELACEIEGHPDNVAPALLGNLVIASTVADKTNYVSSDFPSCKLLAFVPDYELKTVESRKVLPKELAYKEAVAASSIANVLTASLLTKNLKVAGQMIESDHFHENYRASLVPELKILREIGHEFGAYGTYLSGAGPTVMLLLPDDKLNLLTEKINEQNLSGQLYSLEVDSNGLQVKESVL
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Q9CGD7
Q9EQ45
V1R46_MOUSE
Vomeronasal type-1 receptor B8
Mus
MNKANIFCTDTNMKVILFSEVSVGISANSILFISHLCMFLGESRPKPIDLYIAFFSLTHLMLLVTMGLIAVDMFMPGGRWDSTTCTFLMYLHIVLRGPTLCATCLLNVLWTITLSPRNSCLTKFKHKSPHHISGAFLFLCVLYMSLSSELLSITASLNLTSENFLYVSQSCSILPMSYSIKSMFSTKMAIREAFLIGLMVLSSGYMVALLWSHKKQAQHLHSNSLSLKASPEQRATRTIMLLMSFFVVFYILDSVIFYSRMKFKDDSIFVCVQIIVSHSYVTVSPFVFICTEKHIIKFFWSLCGRIVNI
Putative pheromone receptor implicated in the regulation of social and reproductive behavior.
Q9EQ45
Q2INJ8
CHEB1_ANADE
Protein-glutamate methylesterase/protein-glutamine glutaminase 1
Anaeromyxobacter
MAPRILVVDDSAVVRMALSQILGRAGLEVETAIDPLVAMDKMRRARPDAIVLDIEMPRMDGLTFLDRVMAQDPVPVVVCSGLAGPGSEVALHALEHGAVDVIEKPRLGVKGFLEDSARRIVEVVRAATQARLRARVRALRPLPRPPAGAQPRPAPRLAPRAGRAELVVVGASTGGTEALRVLLEAMPADAPAIAVVQHMPEVFTAQFAKRLDKLCRIEVKEAADGDRLLPGRALVAPGNRHLSVKRAGGLVAVVSDGPPVSLHRPSVNVLFHSAARVAGPGTLGILLTGMGDDGADGLLELRRAGAHTVAQDESTSVVFGMPKEAIARGAAVEVLPLPRVASAVLAWAR
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
Q2INJ8
A0QUX1
GATB_MYCS2
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Mycolicibacterium
MTAATTAELVDFDDVVARYEPVMGMEVHVELSTATKMFCGCANRFGAEPNTLVCPVCLGLPGALPVLNEAAVESAIRIGLALNCEITPWGRFARKNYFYPDQPKNYQISQYDEPIAVDGYLDVPLEDGTTWRVEIERAHMEEDTGKLTHLGSDTGRIAGATTSLADYNRAGVPLIEIVTKPIEGAGARAPEIARAYVTALRQLMRALDVSDVRMDQGSMRCDSNVSLKPKGAKEFGTRTETKNVNSLRSVEVAVRYEMRRQAAVLDAGGTVTQETRHFHEDGYTSPGRSKETAQDYRYFPEPDLEPVAPSPELVERLRTTIPELPWLARKRIQDDWGVSDEVMRDLVNAGAVELVAATVDHGVSSEAARAWWGNFLVQKANEAGVELDELPISPAQVAAVVKLVDEGKLSNKLARQVVEGVLAGEGEPEQVMTDRGLALVRDDSVIQAAVDEALAANPDIVEKIRGGKVQAAGAIVGAVMKATKGSADAARVRELVLAACGQS
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
A0QUX1
Q3IMY5
RL2_NATPD
50S ribosomal protein L2
Natronomonas
MGRRILGQRRGRGTSTFRAPSHRYKADLSHRNVEESDLVTGEVVDIEHDPARSAPLADVQFDDGDRRLVLAPEGVTVGDEIQIGVSAEIAPGNTMPLAEIPEGVPVCNVERQPGDGGKFARASGVSATLLTHDRNAAVVQLPSGEMRRLSPECRATIGVVAGGGRTEKPFVKAGNKHHKMKSRGGKWPRVRGVAMNAVDHPFGGGGRQHPGKPKSVSRDTPPGRKVGDIASKRTGRGGKGGQE
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
Q3IMY5
Q8Y4L8
METN2_LISMO
Methionine import ATP-binding protein MetN 2
Listeria
MITLQNVVKEYTSRNNKVLAVDHVDLEIEQGEIFGVVGYSGAGKSTLIRMFNGLELPSAGTVEVDNLLISQIRGSKLRKARQQIGMIFQHFNLLWSRTVAENIAFPLEIAGVRGEKRRFRVNELIRLVGLEGKENAYPAELSGGQKQRVGIARALANNPKVLLCDEATSALDPQTTDEVLELLLDINKRLNLTIIVITHEMHVIRKICNRVAVMENGKVVELGDVLDVFRHPQEKVTQRFVRQVTDSDETEELIHLLLDNYAEGKIVKLLFMSENATQPVISQVAKENDVMLNVLHGNLTQTQNGAYGTLYVQVLGTEDAINASLTQLRQLKVETEVLER
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Q8Y4L8
P22781
DDC_CAVPO
DOPA decarboxylase
Cavia
MNASEFRRRGKEMVDYVANYLEGIESRLVYPDVEPGYLRPLIPSSAPEEPETYEDIIGDIERIIMPGVTHWNSPYFFAYFPTANSYPSMLADMLCGAISCIGFSWAASPACTELETVMLDWLGKMLRLPDAFLAGNAGMGGGVIQGSASEATLVALLAARTKVIRRLQAASPELTQAAIMEKLVAYASDQAHSSVERAGLIGGVRMKLIPSDSNFAMRASALREALERDKAAGLIPFFVVATLGTTNCCSFDSLLEVGPICNQEEMWLHIDAAYAGSAFICPEFRHLLDGVEFADSFNFNPHKWLLVNFDCSAMWVKQRTDLIGAFKLDPVYLKHGHQDSGLITDYRHWQIPLGRRFRSLKMWFVFRMYGIKGLQAHIRKHVQLAHEFESLVRQDPRFEICMEVTLGLVCFRLKGSNQLNETLLKRINSARKIHLVPCHLRDKFVLRFRICSRQVESDHVQQAWQHIRQLASSVLRLERA
Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin.
P22781
Q601M6
TILS_MESH2
tRNA(Ile)-lysidine synthetase
Mesomycoplasma
MQIKIKSKEKYLIGVSGGSDSMFLLNKYKNQDVIVAHINYNLRPEAIFETLLVSKFCQKYNLELKILSFDSFKIKKNLQSGLRLGRYQFFEKIYKEFNCTKLLVGHHRDDFLETVFLQKKQKKIVTFWGIHKKNNLFNMEILRPFLYWRTKKQIIRICQQKKIPYLDDQSNFTGKYQRNQIRFLLEKKSDFSLFFLFLFYYLINIFKLIILKNQKKILQNWQKTGYNINFFKKIKIKSKIIFLFVNQNFDNVKLTRGKINEIINFICGKSTSGAFLLKKNNYIIKKKWKILPKSSKI
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Q601M6
B7IHI2
GUAA_THEAB
Glutamine amidotransferase
Thermosipho
MNTVVVLDYGSQYTQLIVRRVREKGYYAELLPWDASKEEVQNLNPAAIILSGGPASVFEKDAPFVPDYILELNIPILGICYGLQSLVHKFGGIVEKSPKREFGHAVLKVKDDPLFEGLPKEFDVWMSHSDRVEKLPEGFLVIGESENSPYAAIRNKDGTIYGVQFHPEVTHTSFGDKILENFVSKVAKMEKNWKMTDFIEEKINEIRKVVGNDKVILGLSGGVDSSVVALLLDKAIGKNSIPIFVDTGLLRLNERQEVEENFRKLGIDIVVVDAKERFLSNLKGVEDPEEKRKIIGHTFIDVFYEASMKLLEKHGNIKYLAQGTLYPDIIESKVSERKAAAKIKTHHNVGGLPEKLPFKIIEPFRYLFKDEVRKIGKILGLPDEMINRHPFPGPGLAVRIIGEVTNEAIKILQHADHIFIEELKKNDLYDKVWQAFAVFLPIRSVGVMGDYRTYDNVIALRAVNSFDGMTADWSKLPHEFLNKVAKRIVNEVDGVNRVVYDITSKPPATIEWE
Catalyzes the synthesis of GMP from XMP.
B7IHI2
Q4QSC5
NQO9_RHOMR
NDH-1 subunit 9
Rhodothermus
MPGKPVNLASPNERKLNFWERLYLPAVVQGLAYTWRKMRSPRYTFQYPDELWYPPDSYRGRPVLVEENGRPRCVACGLCARACPPLAISMQAKEVDDVKEREPAWFEINMLRCIYCGYCEEVCPEEAIVMSKEYDLTFQSRDEAIFGLEKLLVPAERLKDRLEWLDRYKDPQYGQHWEFRKENNLHSLKDRPFLKWLLEEEGMEELKSTHLRPEEPVAAERSWGGVRAEG
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 menaquinone. 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.
Q4QSC5
P00559
PGK1_HORSE
Phosphoglycerate kinase 1
Equus
MSLSNKLTLDKLNVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDVGPMPDKYSLQPVAVELKSLLGKDVLFLKDCVGPEVEKACADPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIETFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLFDEEGAKIVKNLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGTESSKKYAEAVARAKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNV
Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). May play a role in sperm motility.
P00559
Q9ZLD6
UVRA_HELPJ
Excinuclease ABC subunit A
Helicobacter
MQHKTIMDKIIIQGARENNLKNIFLEIPKNQFVVFTGLSGSGKSTLAFDTLYAEGQRRYLESLSSYARQFLDKVGKPNVDKIEGLTPAIAIDQKTTSKNPRSTVGTITEIYDYLRLLFARVGEQFCPTCLEPISSMSASDIISQICHLEENSKIIILAPIIKDKKGSFNDKLESLRLKGYVRAFVDGVMVRLDEEIHLHKTKKHTIEAVVDRVVINSENASRIASAVEKALKESYGELEVEILQDNAPSIRKHYSEHKACFKCKMSFEELEPLSFSFNSPKGACESCLGLGTKFSLDISKILDPNTPLNQGAIKVIFGYNRSYYAQMFEGFCTYNGIDSALCFNELNKEQQDALLYGNGTEISFHFKNSPLKRPWKGIIQIAYDMFKEQKDLSDYMSEKTCSSCNGHRLKASSLSVQVAGLKMADFLTKPIEEVYHFFNDPTHFNYLNEQEKKIAEPILKEILERVFFLYDVGLGYLTLGRDARTISGGESQRIRIASQIGSGLTGVLYVLDEPSIGLHEKDTLKLINTLRNLQKKGNTLIVVEHDKETIKHADFVVDIGPKAGRHGGEVVFSGSVKDLLQNNHSTALYLNGTKKIERPKFEPPKEKHFLEIKNVNINNIKNLSVQIPLKQLVCITGVSGSGKSSLILQTLLPTAQTLLNHAKKNQSLNGVEIVGLEYLDKVIYLDQAPIGKTPRSNPATYTGVMDEIRILFAEQKEAKILGYSTSRFSFNVKGGRCEKCQGDGDIKIEMHFLPDVLVQCDSCKGAKYNPQTLEIKVKGKSIADVLNMSVEEAYEFFAKFPKIAVKLKTLIDVGLGYITLGQNATTLSGGEAQRIKLAKELSKKDTGKTLYILDEPTTGLHFEDVNHLLQVLHSLVALGNSMLVIEHNLDIIKNADYIIDMGPDGGDKGGKVIASGTPLEVAQNCEKTQSYTGKFLALELK
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.
Q9ZLD6
Q2N814
RUVB_ERYLH
Holliday junction ATP-dependent DNA helicase RuvB
Erythrobacter
MTDPIPLHTPDRQPEDPDVALRPKSLAEFVGQAAAKDNLAVFIEAARSRGEAMDHTLFFGPPGLGKTTLAQIIARELGVGFRATSGPVIAKAGDLAALLTNLEPHDVLFIDEIHRLNPVVEEVLYPAMEDRALDLIIGEGPAARSVRIDLPPFTLIGATTRQGLLTTPLRDRFGIPVRLNFYTEEELEKVVTRGAGLMGLAIDAAGAREIARRSRGTPRVAGRLLRRVRDFAEVQKAGTVTSPIADAALTRLEVDGLGLDAMDRRYLTMIADIYKGGPVGVETLAAGLAEPRDTIEDVVEPYLIQLGLVARTARGRCLNDRGWEHLERQPPAGSQTGLFDGKS
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
Q2N814
Q1LTQ3
RECA_BAUCH
Recombinase A
Candidatus Baumannia
MAIDENKQKALAAALSLIEKQFGTGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIATAQKEGKICAFIDAEHALDPIYAKNLGVDIDNLLCSQPDTGEQALEICDVLTRSGAVDVIIVDSVAALTPKAEIEGEIGDSHIGLAARMMSQAMRKLTSNLKNANTLLIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSVKEGDVVVGSETRVKVVKNKVAAPFKQADFQITYGKGINIHGELVDLGVKNNLIEKAGSWYSYNGNKIGQGKNNVCNFLKYHPQLAAELDKKLREMLLHNTTRTESNSLVRDDEGTFDE
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.
Q1LTQ3
P14489
BLO10_PSEAI
Beta-lactamase PSE-2
Pseudomonas
MKTFAAYVIIACLSSTALAGSITENTSWNKEFSAEAVNGVFVLCKSSSKSCATNDLARASKEYLPASTFKIPNAIIGLETGVIKNEHQVFKWDGKPRAMKQWERDLTLRGAIQVSAVPVFQQIAREVGEVRMQKYLKKFSYGNQNISGGIDKFWLEGQLRISAVNQVEFLESLYLNKLSASKENQLIVKEALVTEAAPEYLVHSKTGFSGVGTESNPGVAWWVGWVEKETEVYFFAFNMDIDNESKLPLRKSIPTKIMESEGIIGG
Hydrolyzes both carbenicillin and oxacillin.
P14489
A5ERK2
RUVC_BRASB
Holliday junction resolvase RuvC
unclassified Bradyrhizobium
MKAQPIRAAVRIIGIDPGLRRTGWGVIESEGNRLIYVGCGSVEPPDDLPLANRLLAIHEGLAKVLNDFQPLEAAVEQTFVNKDGVATLKLGQARGIAMLAPAMFGISVAEYAPNQVKKTVVGAGHADKGQIAVMLKILLPKAEPPSADAADALAIAITHAHHRQGQALRMKVAGL
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
A5ERK2
A6VXM7
GCSH_MARMS
Glycine cleavage system H protein
Marinomonas
MSTIPENLKYADSHEWVLDNGDGTVTVGITDHAQDLLGDVVYVELPEVGTEVTATEQFSLVESVKAASDIYAPVNGEVIEVNDALNDAPELINEAPFEGAWIAKIKLSNAADLDKLLDAAGYSATIA
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
A6VXM7
Q9QZI8
SERC1_MOUSE
Tumor differentially expressed protein 2
Mus
MGSVLGLCSVASWIPCLCGSAPCLLCRCCPSGNNSTVTRLIYALFLLVGVCVACVMLIPGMEEQLNKIPGFCENEKGVVPCNILVGYKAVYRLCFGLAMFYLLLSLLMIKVKSSSDPRAAVHNGFWFFKFATAVAIIIGAFFIPEGTFTTVWFYVGMAGAFCFILIQLVLLIDFAHSWNESWVEKMEEGNSRCWYAALLSATALNYLLSLVAVVLFFVYYTHPASCAENKAFISVNMLLCIGASVMSILPKIQESQPRSGLLQSSVITVYTMYLTWSAMTNEPETNCNPSLLSIIGFNTTRPIPKDGQSVQWWHPQGIIGLVLFLLCVFYSSIRTSNNSQVNKLTLTSDESTLIEDGNGRSDGSLDDGDGIHRAVDNERDGVTYSYSFFHFMLFLASLYIMMTLTNWYRYEPSREMKSQWTAVWVKISSSWIGLVLYVWTLVAPLVLTNRDFD
Enhances the incorporation of serine into phosphatidylserine and sphingolipids.
Q9QZI8
Q11XX4
RL21_CYTH3
50S ribosomal protein L21
Cytophaga
MYAIVEIGGKQYKVEKDHFIYVYRLEGAEGSAVTFDNVLLLADNNQYQVGAPSVAGASVSGKILEHLKDDKVTAFKKKRRKGFRKTVGFRQSLTKVLITSLN
This protein binds to 23S rRNA in the presence of protein L20.
Q11XX4
Q46VX0
RSMG_CUPPJ
16S rRNA 7-methylguanosine methyltransferase
Cupriavidus
MGGQRHTMIDDAAQRRRLEAGLAEIGLALPPDRIDTLFAYLALLRKWNGVYNLTAIRHPDEMLTHHLLDSLAAVPALAEMARSSEVGGAARGRVLDVGSGGGMPGLPLAISCPDVSVLMVDIVQKKTAFLTQCRAQLGLSNAAAHWGPVERLEDPDKFAVITSRAFAELTDFVNLSGHLLAPHGRLIAMKGVYPQAELDRMEAAGLMAAWQVEEVRRLTVPGLDAERHLVLLSRK
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Q46VX0
Q49136
CAPP_METEA
Phosphoenolpyruvate carboxylase
Methylorubrum
MTKTLHARPSAATDTTFAPPVITGTATEDALEILFHALLDVARRHDPELEDVLHGRADISSFTPEMLARALQVQGIWFQLVSIAEQNAAMRRRRHVERDQGREALNGSFAKVLAEASARGIGPQQIHALLKDLRIRPTITAHPTEGKRVTVLEKLRRIYLVLRELELPRWTERERNGLMNELRDQIELIWMTGELHLEKATVEREVAWGLHFFDETLFEMLPEMLLSLEESLAQYYPDETFEVPPFFQFGSWIGGDRDGNPYVTASVTRETLQRNALASLRRYRDGITHLGRVLSITERSLPVPETFRSELAHMLAESGDARAIANRNPGEAYRQFLSCVLRKLEATIARNKGARSVGPDYPSADGLINDLRTLEKGLADAKCGALATDIVRPVRRMVEIFRFSTVRLDLRENSTRTTKTLHALWKLRNGDREPPALDSPAWKDWLLTELARPRTPETSFEDFADRLPDDARETLATFALVGEMRDTLDREAFGAFILSMTRSTVDVLGAYLLAKEAGIFLDTTGTEICPLPIVPLFETIDDLRAAPAIMKELLGIPVVRRSTRWQGGVQEVMIGYSDSNKDGGFIASNWELYKAQVRLTTLGNHLGVPIAFFHGRGGSVSRGGVPTHRGIAAQPPGSIQGRFRITEQGEVVSFKYANRGTAAYQMELLAASVFEHALLSEGNGNGSRAEFDDALEALSGASRAAYVNLLQAEGLVDYFQAASPLDEISLLNIGSRPARRFGAKSLSDLRAIPWVFAWSQNRHVITGWYGVGSGLKSFIDVRGEAGEALLRRLFRDCRVFRLVLDEVEKTLLMVDLEIARDYAGLVEDAGIRARIFGMIEAEYALTREMVLRVSGDSELAQRFPQFSERLRGRLPTINQVSREQVELLRRYRSETDEDKREAVKSALLLSINCIAVGFGATG
Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Q49136
O94368
PPR1_SCHPO
Pentatricopeptide repeat-containing protein 1, mitochondrial
Schizosaccharomyces
MLKRAHYVALHVTLNHNGLSYQRVFSCLTQFPMLRHSSTAAKNNVSMISKFQAPEDKFFPSFSLKSMPKQSSHMSASLLNSLNTSMKKSFSRKKYREAVSLFRKNLWKYEESWIRNQDFIDCCIIACSAYEKLCQPLRIKKTFIILSQLCPKLPAELCRVFLSYATGCVNYGHNVALTCFENSPKELIDYNYWLSWLSFSKSSPVVLWLTFTRISSAGLSPNAETFEILLVAFASQKNFWFFEKTYDLFMQSKLTWRPFTYRVLIESFMKFGNFEEAEKLAYSYVKNKIDSLSSDVFFSAILKFYAVGGDFQGFKKLLSFMTDYNVNFSVSTLNQLLRLNLYHAMDEKISTFSSEHITKLIEQQIKPDLESMLIISEYLNEYKPSPKMRELINWLYSNFHLPKTVSLHFLREVQSLVFRYPLLHSKIHLAISTLKDSGCDWNVGLSYLNWLFVNKRITEAINFFYTITINAGTRPPNELFDVFISNLLKFTSAETTSSAIRKVQSKYPSMCGSSPAIKLILFSKSFSVLQSTSEKIEQLLVSFQRNPSAYSKSFTLALAEWLFSRRLFQSALLYSFKVSDVDDSHFSFRSQILICWCYYRLNDFKSLIQHTNNLLQSNNASLLRRLAATLYRIQIRENNGYKRVLLDRLRKKAILRAFPSRTLNRTEKVKLYNEDAKFRSIFSRVLLHQSHLGNVIS
Mitochondrial RNA-binding protein required for the stability of the cox2 and cox3 mRNAs.
O94368
C6E7E7
QUEC_GEOSM
Queuosine biosynthesis protein QueC
unclassified Geobacter
MQKKAVILYSGGLDSTTCLAIAKKQGFAPYALSFSYGQRHQQELEVAKLNARPMGAVDHLLVEFDLRKMGGSALTSDIEVPKEGVGEEIPVTYVPARNTIFLSFALGWAETLDCFDIFIGVNALDYSGYPDCRPEFISAYETMANLATKAGVEGKRLQIHTPLISLTKAEIIQKGISLGVDYSKTHSCYDPAEDGAACGRCDSCRLRLKGFAEAGVTDPVRYQKL
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
C6E7E7
P83310
RDPA_DELAC
Mecoprop/alpha-ketoglutarate-dioxygenase
Delftia
MHAALSPLSQRFERIAVQPLTGVLGAEITGVDLREPLDDSTWNEILDAFHTYQVIYFPGQAITNEQHIAFSRRFGPVDPVPLLKSIEGYPEVQMIRREANESGRVIGDDWHTDSTFLDAPPAAVVMRAIDVPEHGGDTGFLSMYTAWETLSPTMQATIEGLNVVHSATRVFGSLYQAQNRRFSNTSVKVMDVDAGDRETVHPLVVTHPGSGRKGLYVNQVYCQRIEGMTDAESKPLLQFLYEHATRFDFTCRVRWKKDQVLVWDNLCTMHRAVPDYAGKFRYLTRTTVGGVRPAR
Involved in the degradation of the phenoxypropionate herbicides. Catalyzes the enantiospecific cleavage of the ether bond in the herbicid R-dichlorprop ((R)-2-(2,4-dichlorophenoxy)propionate)(R-2,4-DP) and R-mecoprop ((R)-2-(4-chloro-2-methylphenoxy)propionate)(R-2,4-MCPP). It can also accept (RS)-2-(2,4,5-trichlorophenoxy)propionate, (RS)-2-(4-chlorophenoxy)propionate, (RS)-2-(m-chlorophenoxy)propionate, however it can only accept 2-oxoglutarate as oxygen acceptor.
P83310
Q42652
SUS_BETVU
Sucrose-UDP glucosyltransferase
Beta
AGGKQILSDGPFSEVLRSAQEAIVVPPFVAIAVRPRPGVWEYVRVNVSELNVEQLTVSEYLHFKEELVDGKADDHYVLELDFEPFNESVPRPTRSSSIGNGVQFLNRHLSSSMFCNKDCLEPLLDFLRVHKHKGVVMMLNDRIQTIQRLQSALSKAEDYLIKLPADTPYSEFEFVIQGMGFERGWGDTAERVLEMMHLLLDILQAPDPSTLETFLGRLPMVFNVVILSVHGYFGQAHVLGLPDTGGQIVYILDQVRSLEHEMLQRIKKQGLDVTPRILIVSRLIPDAKGTTCNQRMEKVSGTEHASILRVPFRSEKGILRKWISRFDVWPYLETFTEDAAGEIIGELQGRPDLIIGNYSDGNIVASLLSHKMGVTQCNIAHALEKTKYPDSDIYWKRFEDKYHFSCQFSADLMAMNHADFIITSTYQEIAGTKNTVGQYESHKAFTFPGLYRVVHGIDVFDPKFNIVSPGADMAIYFPFSEKDVTCLTSLHRLIEQLLFKPEQNEEHIGVLDDTSKPIIFSMARLDRVKNITGLVECYGKNAKLRELANLVVVAGYNDVKKSNDREEIAEIEKMHRLIQEYNLRGQFRWIASQTNRVRNGELYRYICDKGGIFAQPAFYEAFGLTVVEAMTCGLPTFATCHGGPAEIIEDGVSGFHIDPYHADQAEKMTEFFVKCREDPNYWTKISAGGLLRIKERYTWQKYSERLMTLAGVYGFWKYVSKLERRETRRYLEMFYILKFRDLANSVPLATDEEPSTTDAVATFRGP
Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways.
Q42652
P22195
PER1_ARAHY
PNPC1
Arachis
MALPISKVDFLIFMCLIGLGSAQLSSNFYATKCPNALSTIKSAVNSAVAKEARMGASLLRLHFHDCFVQGCDASVLLDDTSNFTGEKTAGPNANSIRGFEVIDTIKSQVESLCPGVVSCADILAVAARDSVVALGGASWNVLLGRRDSTTASLSSANSDLPAPFFNLSGLISAFSNKGFTTKELVTLSGAHTIGQAQCTAFRTRIYNESNIDPTYAKSLQANCPSVGGDTNLSPFDVTTPNKFDNAYYINLRNKKGLLHSDQQLFNGVSTDSQVTAYSNNAATFNTDFGNAMIKMGNLSPLTGTSGQIRTNCRKTN
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
P22195
Q5SK82
TLBP_THET8
TRAP transporter lactate-binding subunit P
Thermus
MKRVSRRAFLRRLGVGVAATAAFSPLAVAQARRYRWRIQTAWDAGTVGYSLFQKFTERVKELTDGQLEVQPFPAGAVVGTFDMFDAVKTGVLDGMNPFTLYWAGRMPVTAFLSSYALGLDRPDQWETWFYSLGGLDIARRAFAEQGLFYVGPVQHDLNIIHSKKPIRRFEDFKGVKLRVPGGMIAEVFAAAGASTVLLPGGEVYPALERGVIDAADFVGPAVNYNLGFHQVAKYIIMGPPETPAIHQPVDLMDFTINLNRWRSLPKPLQERFIAAVHEYSWIHYAGIQKANLEAWPKYRQAGVEVIRLSNEDVRKFRRLAIPIWFKWAKMDKYSREAFASQLEYMKGIGYVTDEELKGLSL
Part of the tripartite ATP-independent periplasmic (TRAP) transport system involved in the uptake of lactate. This protein specifically binds L-lactate.
Q5SK82
C3K222
MSRQ_PSEFS
Flavocytochrome MsrQ
Pseudomonas
MRYPIWRVGVFIAAAVWPLFWLYEAWSAVLGPDPGKVLVDRLGLGTLILLLITLAMTPLQKLSGWAGWIAVRRQLGLWCFAYVVLHLAAYCVFVLGLDWSQLGVELRKRPYIIVGALGFLLLLVLAVTSNRYSQRRLGSRWKKLHRLVYVVLGLGLLHMLWIVRADLKEWAIYASIGALLLVLRIPPVMRRIPRLIAKKPLSATKA
Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
C3K222
B0BV26
LIPA_RICRO
Sulfur insertion protein LipA
spotted fever group
MANLNKRPDWIKVKAPNSTEYYNTKDLIKNLRLNTVCEEAACPNIGECWSKKHTTVMILGSVCTRACRFCNVKTGRPDLLDPYEPQRLAEAVQKLNLKHVVITSVDRDDLEDGGASHFAECISEIRKSSPNTTIEILTPDFLRKEGAAEIIANAKPDVFNHNVETVPSLYKTIRPGARYYNSLSLLHNIKKLSPEIFTKSGMMVGLGEEINEVVQVIDDLREAKVDFLTIGQYLQPTKNHAEVAKYVTPEEFKYLERLAKTKGFLMVSASPLTRSSYHADEDFQKLKENYQQKLVS
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
B0BV26
Q6AK45
SYI_DESPS
Isoleucyl-tRNA synthetase
Desulfotalea
MDYRDSLNLPKTNFKMKANLAQREPMILKRWEKEGLYQMLQERAQDRPLFVLHDGPPYANGHIHLGHAFNKILKDIILRSKRASGFNAPYVPGWDCHGLPIEHNVDKELGEEKKKTIPILAKRAACRKYANKWIKTQKPEFKRLGVLGDWEDPYLTINYSYEAAIAREFNKFLLSGSVVRNRKPVYWCSTCTTALAEAEVEYHDHTSPSIYVKFPVIEDFSDVDPALAGDKTFVVIWTTTPWTLPSNTAVAFHPKFQYAAVAVGEETWVLAEDLVEKFMQEVGIEDYSIKSTFTAEKLENRNCRHPFMDRDSRLVFADYVTTEAGTGCVHTAPGHGADDYATGLRYGLEVLSPVDGDGIYTKEAGPYAGRQVPEVNSDIIADLAESGLLVFKKDINHSYPHCWRCRKPVMYRATPQWFISMENNDLRKKALKNIESVSWTPSWGMNRIHSMVESRPDWCLSRQRTWGVPLTVISCKDCGEVVKSEEVVAKIDELFLKEGADAWFSHPVEDFLPEGHVCTCGCATFIKEEDILDVWFDSGSSFAAVCELRDDLVAPADLYLEGSDQHRGWFQSSLITATGTRGYAPFKGVLTHGYVVDGQGKKMSKSVGNVVAPQEVIDEYGAEILRLWVSSEDYRDDVKVSKEILKQVSDSYRKIRNTIRYFLGNLNDFDPSKDRIAVSEMSELDRWALARFEELRAKITESYDKYEFHAINQSLNYFCGTTMSAFYLDIIKDRLYVEGTDSTIRRASQTVLYDILDGLLRLMSPVLSFTAADAWNALYSLGEKDSLEKSVFFADFPVAIDPQFDAEQEARWQRLIKIRSELTKALELARRDKVIGHSLEAEVLVKGEGELGEFIHAEWQHLREISIVSAMSEIEGAPEESAYVSEEVEGLVVSVKLAPGVKCDRCWIRSTTVGDSVEHPQLCSRCLAIVEDMDLEMDA
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
Q6AK45
A1BFE5
MIAA_CHLPD
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Chlorobium
MHDSDRQKTILAILGPTASGKSALAFSIAKEINAEIISADSRQIYRELNIGTAKPSQETLRQIKHHFVNELSIGDPFTAGNFAREASARIRNILHSGKNVLIAGGSTLYLEALLNGFADLPPADTEKRQQLAIELETFGSKHLFERLRQLDPLQAATLDHTKTQRLVRSLEIIELSGHTVTEMQKKHIQPLADINVITCGLSLPRPLLYEKINRRTDQMLASGLLQEAVALFTKYYPYCDVITTNALQTVGYQELFAYLDEKTDFKTAITLIKQHTRNYAKRQLTFFKNRLNVNWMDAPENEHELSMLTTSCCRMITGN
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).
A1BFE5
Q1KVW6
PSBD_TETOB
Photosystem Q(A) protein
Tetradesmus
MTIAIGSTYQEKRTWFDDADDWLRQDRFVFVGWSGLLLFPCAYFALGGWFTGTTFVTSWYTHGLATSYLEGCNFLTAAVSTPANSMAHSLLFLWGPEAQGDFTRWCQLGGLWTFVALHGSFGLIGFMLRQFEIARSVNLRPYNAIAFSAPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLLVPVTGLWMSAIGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHERLVFPEEVLPRGNAL
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. D2 is needed for assembly of a stable PSII complex.
Q1KVW6
Q32BW1
YGFZ_SHIDS
tRNA-modifying protein YgfZ
Shigella
MAFTPFPPRQPTASARLPLTLMTLDDWALATITGADSEKYMQGQVTADVSQMTEDQHLQAAHCDAKGKMWSNLRLFRDGDGFAWIERRSVREPQLTELKKYAVFSKVTIAPDDERVLLGVAGFQARAALANLFSELPSKEKQVVREGATTLLWFEHPAERFLIVTDEATANMLTDKLRGEAELNNSQQWLALNIEAGFPVIDAANSGQFIPQATNLQALGGISFKKGCYTGQEMVARAKFRGANKRALWLLAGSASRLPEAGEDLELRMGENWRRTGTVLAAVKLEDGQVVVQVVMNNDMEPDSIFRVRDDANTLHIEPLPYSLEE
Folate-binding protein involved in regulating the level of ATP-DnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication.
Q32BW1
P95778
RMLA_STRMU
dTDP-glucose synthase
Streptococcus
MKGIILAGGSGTRLYPLTRAASKQLMPVYDKPMIYYPLSTLMLAGIKDILIISTPQDLPRFKELLQDGSEFGIKLSYAEQPSPDGLAQAFIIGEEFIGDDHVALILGDNIYYGPGLSRMLQKAASKESGATVFGYQVKDPERFGVVEFDNDRNAISIEEKPEHPKSHYAVTGLYFYDNSVVDIAKNIKPSPRGELEITDVNKAYLDRGDLSVEVMERGFAWLDTGTHESLLEAAQYIETVQRMQNLQVANLEEIAYRMGYITADQVRELAQPLKKNEYGQYLLRLIGEA
Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.
P95778
A5FS52
RSMA_DEHMB
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
Dehalococcoides
MGKDVPLLVASAPSLMAQAKEMMEGYTLKARKGLGQHFLISQGVLNKILAAADLKPTDTVIEVGPGLGVLTEELLKRAGQVIAVEVDDKLIDALTEKFKGYPNFRLIHSDILKTSPEEILGQNVPYKLVANLPYYITSAVLRQFLEAKLKPESMVVMVQKEVAKNIVAKTGDMGLLTLSIRFYGNPSLVSVVPGGAFYPPPEVDSAIVKIVIPQTTIMEGVSEVDFFKLARAGFGTRRKTLLNALAQGLGISKPVILSLLNGAGIDPARRAETLSMEEWKKLCLEYAGNPC
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
A5FS52
Q8BQC8
RBAK_MOUSE
Zinc finger protein 769
Mus
MSRSKGPLSFKDVAVAFSQEEWQQLDPEERTTYRDVMLETYSNLVSVGYDVTKPNMIIKLEQGEEPWTVEGDRHAQRHLEISKVYDPREGIEEIGEKHLQCDDDPYCWRAEKGAAFDEAYTLETALISPSSGAHSCVSCGETLESVSELISSDGSYALEKPSMCFECGKAYGESLEDFNQDEGNSSQHDENILQKVTILEKPFAYECMEALDSESVFMARERAYMGEKPYDWGDSGPDFIQMSDFSTYPRSQMELKPFECTQCGKSFCKKSKFIIHQRAHTGEKPYACSVCGKSFSQKGTLTVHRRSHLEEKPYKCNECGKTFCQKLHLTQHQRTHSGEKPYECSECGKSFCQKTHLTLHQRNHSGERPYPCNECGKSFSRKSALNDHQRTHTGEKLYKCNECGKSYYRKSTLITHQRTHTGEKPYQCSECGKFFSRVSYLTIHYRSHLEEKPYECTECGKTFNLNSAFIRHWKVHAEERVQECGECGKPSPLQCAPDHTGDLGEKRYECNECGKTFLDSSAFHRHQSVPEGEKTYECNICGKSFSDSSCYTVHYRGHSEEKPFGCSECGKTFSHNSSLFRHQRVHTGEKPYECYECGKFFSQKSYLTIHHRIHSGEKPYECSKCGKVFSRMSNLTVHYRSHSGEKPYECNECGKVFSQKSYLTVHYRTHSGEKPYECNECGKKFHHRSAFNSHQRIHKRGTVNVLTVEKL
May repress E2F-dependent transcription. May promote AR-dependent transcription.
Q8BQC8
P01354
GAST_FELCA
Gastrin
Felis
MQRLCVCVLILALALTAFSEASWKPRSQLQDAPSGPGANGGLEPHWLNRLGPASHHRWQLGLQGPPQQVADLSKKQGPWLEEEEAAYGWMDFGRRSAEDGDQHP
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.
P01354
Q9CHT8
RNZ_LACLA
tRNase Z
Lactococcus
MEIQFLGTGAGQPSKSRNTQAIALKMLDERNEIWLFDCGEATQHQILNTTIKPRKITKIFITHLHGDHIFGLPGFLSSRSFQSSDEQTDLELYGPVGIKDFVLTALRISGSRLAYRINFHEIDSAGKIFEDDSFEVHTDLLDHTIFCLGYRVVEKNRIGELDANALKEAGLPFGPLFGKIKKGEIVQYEGKTFDPKDYIGADKAGKIVTILGDTRKSNVAVRLAYGADLLVHEATYEANESKMAKAHGHSTTKQAADVAKEAGVNRLLLTHISARYVGPLVGQLVREAQTVHSNTFVVKDFYEEKIG
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Q9CHT8
C1KYW2
KHSE_LISMC
Homoserine kinase
Listeria
MRIRVPATTANLGPGFDSCGLALTLYLTLDIGAEADSWYIEHNIGGGIPHDETNVIIETALNLAPNLTPHHLVMTCDIPPARGLGSSSAAVVAGIELANTLAELKLSKEEKVRIAAEIEGHPDNVAPAVLGNWVVGAKLDGEDFYVRHLFPDCALIAFIPKAELLTSESRGVLPDTLPFKEAVQASSIANVMIAAILRNDMALAGEMMERDLWHEKYRSQLVPHLTQIRDVAKSQGAYAACLSGAGPTVLVFAPRNLANTLQTSLQTLEIDADVLLLDVEGSGAEVFR
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
C1KYW2
Q5P3T7
TTCA_AROAE
tRNA 2-thiocytidine biosynthesis protein TtcA
Aromatoleum
MTPLSAVATPTPAPAEAADSRFSNTFLRLKKKLERGVGKAIADFNMIGDGDTVMVCVSGGKDSYTLLSCLLALRERAPVDFRIIAMNLDQKQPGFPAEVLPAYFESIGVEYRIVTEDTYSIVKDKIPEGKTTCSLCSRLRRGIIYRVARELGATRIALGHHRDDMLETLFLNLFFGGKIKAMPPKLVSDNGEHVVIRPLAYCTEADIAKFARTMEFPIIPCNLCGSQENAQRKQIKTMLQGWAREHPGRIESIATALGQVVPSHLADASLFDFRNLTRDTLVAEGDIAFDRAELPPASAAVMPTVMQLTDHRTDGK
Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
Q5P3T7
Q3AC15
RPOZ_CARHZ
Transcriptase subunit omega
Carboxydothermus
MNQPSLDILMKKADSRYTLVVATAKRARQITAGESSKLKHISNKPVTIALHEIGNDLITYQRLKSSQNK
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Q3AC15
Q4L7B0
RISB_STAHJ
6,7-dimethyl-8-ribityllumazine synthase
Staphylococcus
MNFEGKLVGTDLKVAIVVSRFNDFITNRLLDGAKDTLVRHGVEDSNIDVAYVPGAFEIPLVSKKLAQKGEYDAVITLGCVIRGATSHYDYVCNEVAKGVSKANDVSDIPVIFGVLTTESIEQAVERAGTKAGNKGAEAAVSAIEMANLLKQF
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Q4L7B0
P86013
LANPA_PAEPO
Lantibiotic paenibacillin
Paenibacillus
MKVDQMFDLDLRKSYEASELSPQASIIKTTIKVSKAVCKTLTCICTGSCSNCK
Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Lacks antibacterial activity against Gram-negative bacteria.
P86013
A6UVG7
DAPA_META3
4-hydroxy-tetrahydrodipicolinate synthase
Methanococcus
MQGVFPAIITPFKNGGVDYEGLEQNINFLIDNGVNGIVSVGTTGESPTLSHDEHKKIIEKSVSVCDGKVDVIAGAGSNSTEEAIALSQFAEDVGADSVLLITPYYNKPTQEGLKQHFSKIAESINIPIVLYNVPSRTAVNLQPETIKYLYEEYSNITTVKEANPDLSHISDVINSCDISVLSGNDELTLPVISLGGNGVISVVANIVPNEFVQMVNYANEGKFKEAREIHYKLFNLMKSLFIETNPVPIKTAMNLLNMPAGDLRLPLCKMEEENKFKLETALKEYGLL
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
A6UVG7
Q2JD94
RUVB_FRACC
Holliday junction ATP-dependent DNA helicase RuvB
Frankia
MSDDGLVSAAASPEERAFEAGLRPRTLAEFVGQRKVREQLTIMLEGARARGRPPDHVLLSGPPGLGKTSLAMIMAQELEVPLRMTSGPAIERAGDLVAILTALSPGEVLFLDEIHRIARPAEELLYAAMEDFRVDVILGKGPGATAIPLDVSPFTLVGATTRSGLLTGPLRDRFGFTAHLDFYDADELARVLTRSAGLLGVTLTAEGAAEVAGRSRGTPRIANRLLRRVRDYAEVRADGVVTREIAQAALRIYDVDGLGLDRLDRAVLEALVTRFGGGPVGLTTLAVSVGEEPETVEDVAEPFLLRAGLLIRTARGRMATPAAFEHLGLDPVTDPLGRTQVSLFTEGE
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
Q2JD94
A4Y2Q5
UBIE_SHEPC
Demethylmenaquinone methyltransferase
Shewanella
MSEGESKSTHFGYKTVEADKKAELVAGVFHSVAAKYDIMNDVMSFGIHRFWKRHTIEVSGARPGMKVLDLAGGTGDLTAKFSHLVGDKGEVVLADINDSMLKVGRTKLRDKGIVNNVSYVQANAEALPFPDNHFDIITIAFGLRNVTDKDAALRSMNRVLKPGGKLLVLEFSKPQHEIMRKVYDLYSFKVLPKMGELITKDADSYEYLAESIRMHPDQDTLKQMMVDAGFEQVDYTNMTDGIVALHRGYKF
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
A4Y2Q5
C7NST3
HPRL_HALUD
HGPRTase-like protein
Halorhabdus
MDRLKQSLLDAPVIEKEEYQYFVHPISDGVPMLRPELLREIVIRIIRKAELEDVDKIVTPAAMGIHISTAVSLMTDIPLVVIRKRQYGLEGEVSLQQVTGYSESEMYVNDVYEGDKVLVLDDVLSTGGTLAGITGALEEIGAEIVDIVAVIKKVGGENKIDDSDFDVKTLINVDVEDMEVIIVDEQGDG
May catalyze a purine salvage reaction, the substrate is unknown.
C7NST3
Q3KL68
TRHO_CHLTA
tRNA hydroxylation protein O
Chlamydia
MEKNYYALAYYYFGPVSNPHEEIALHKQLFKTMDVSCRIYISEEGINGQFSGYQPDAERYMAWLKQRPDFASIKFKIHHIEENIFPRVTVKYRKELVALGCSVDTTKQGKHISPEEWHEKLQENRCLVLDVRNNYEWKIGHFENAVLPDIETFREFPDYADRLAKEHDPAKTPVMMYCTGGIRCELYSALLLEKGFKEVYQLDGGVIAYGLKMGTGKWRGKLFVFDDRMAMPIDEADPNVSPIARCSLCNTDSDTYYNCANTDCNNLFICCESCIATHKGCCSEECSQAPRIRAFSAERGNKPFRRKHLCPTIEQSCCLKEQENQPA
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Q3KL68
P40302
PSA6_YEAST
Proteinase YSCE subunit PRE5
Saccharomyces
MFRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLDTFIKIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI
The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
P40302
Q03QY5
ATPD_LEVBA
F-type ATPase subunit delta
Levilactobacillus
MSLNRATVAKRYSQALFDLLSEKDQLESGYTELQELRRIFQDNPQLSTMLSDASLQVADREALLQPLLKQASPYIKNLIQMVYDYGRMENMVDIIDQFQVLYDELHHTVYAEVTTAVELSAEQKSQIEAVYAKRVGAEKVVLSSKVDPDVIGGVIVKAADTILDGSLRTKINRLRQQLLA
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.
Q03QY5
Q9NP78
ABCB9_HUMAN
TAP-like protein
Homo
MRLWKAVVVTLAFMSVDICVTTAIYVFSHLDRSLLEDIRHFNIFDSVLDLWAACLYRSCLLLGATIGVAKNSALGPRRLRASWLVITLVCLFVGIYAMVKLLLFSEVRRPIRDPWFWALFVWTYISLGASFLLWWLLSTVRPGTQALEPGAATEAEGFPGSGRPPPEQASGATLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQMLGLQPAADFTAGHNEPVANGSHKA
ATP-dependent low-affinity peptide transporter which translocates a broad spectrum of peptides from the cytosol to the lysosomal lumen for degradation . Displays a broad peptide length specificity from 6-mer up to at least 59-mer peptides with an optimum of 23-mers . Binds and transports smaller and larger peptides with the same affinity . Favors positively charged, aromatic or hydrophobic residues in the N- and C-terminal positions whereas negatively charged residues as well as asparagine and methionine are not favored .
Q9NP78
Q9ANP1
HYPD1_BRADU
Hydrogenase maturation factor HypD1
Bradyrhizobium
MKYSSEFRDKTIAQGLARAIDAEVSSQRAYRFVEFCGGHTHAISRYGLEDLLPANVRMIHGPGCPVCVLPASRIDMAIRLAERPEVILCVYGDLMRAPGSQGQSLLLAKALGAHIRMVYSTLDAIRLAEQTPGREVVFFAIGFETTTPPTAVMIRIAEHKRLEGLSVFCNHVLTPSAMHRILENPKIRNTGGVPIDGFIGPAHVSTIVGTQPYEPMAEQFEKPIVVAGFEPLDVLQAVLMLVRQVNQNRHEVENQYSRAVTREGNRRAKEEVSQVFELREQFEWRGLGLVPNSGLKLKQSYAKFDAETRFAIHDLRVADNPACECCAILRGAKRPIDCKLFGNICTPETPIGACMVSSEGACAAYWTYRRVRDEQARQTS
Involved in the maturation of [NiFe] hydrogenases. Involved in the biosynthesis of the Fe(CN)(2)CO cofactor.
Q9ANP1
A5EXG1
RUVC_DICNV
Holliday junction resolvase RuvC
Dichelobacter
MAICRILGIDPGSRITGYGIIDVRGTAIDYVDSGCIRLATQLMPQRLMTIHQGIFELVQQYHPQQFAIEAIFVHKNPNSALKLGQARGVAICAAVLSGLSINEYAAKSIKQAVVGKGGADKIQVQHMVKILLNRQGAIQSDAADALAVAITHAHHLQTLACQRPRQTDYWVNGNAS
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
A5EXG1
Q9FZ32
FB60_ARATH
F-box protein At1g55000
Arabidopsis
MALYCRDTLIIIFQKLTVADLARASCVCKVWNSVATEDDLVVSAFTAPWRIKELVGRPASVSFWRDNGIWKFAISHRICRGDSVTSLAVKYAVQVMDIKRLNNMMSDHGIYSRDRLLIPISNPEILANTTCYVELDKYAKREVAVLYLEGAPKREQPVPGTNQQSNLSADGKRRLIESLRRSMQVDDGTALYYLAIAEGDPRSALSEFSADLRWERQAGLN
Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Q9FZ32
C4Z563
TGT_LACE2
tRNA-guanine transglycosylase
Lachnospira
MYKILKTDGRAKRAEFTTVHGTVQTPVFMNVGTVAAIKGAVATTDLQQIGTQIELSNTYHLHVRPGDKIIKQLGGLHKFMNWDKPILTDSGGFQVFSLAGLRKIKEEGVTFQSHIDGHKIFMGPEESMQIQSNLGSTIAMAFDECAPAKADRKYIQNSVDRTYRWLERCKKEMARLNSLPDTVNPDQMLFGIDQGGVFNDIRIDHAKRISELDLDGYAVGGLAVGETHEEMYDVLDNVVPYLPQDKPTYLMGVGTPANILESVDRGIDFFDCVYPSRNGRHGHVYTKFGKINLFNAKYETDTAPIEEGCGCPCCQNYSRAYVRHLLKAKEMLGMRLCVLHNLYYYNHLMTDIRAAIEEGRYAGFKEEALYQMKTYDKQ
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).
C4Z563
Q2K9D7
XGPT_RHIEC
Xanthine phosphoribosyltransferase
Rhizobium
MSLPDKAFPVSWDQFHRDARALAWRLAGLDQTFKAIVCITRGGLVPAAIISRELNIRLIETVCIASYHDYVNQGDMVLLKGIAPELAENGGEGVLVVDDLTDTGKTAAQVRTMLPKAHFACVYAKPKGVPTVDTFITEVSQDTWIYFPWDMGFTYQEPIAKGAR
Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine.
Q2K9D7