accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
Q5X9P6
|
PRSA2_STRP6
|
Foldase protein PrsA 2
|
Streptococcus
|
MKQMNKLITGVVTLATVVTLSACQSSHNNTKLVSMKGDTITVSDFYNETKNTELAQKAMLSLVISRVFETQYANKVSDKEVEKAYKQTADQYGTSFKTVLAQSGLTPETYKKQIRLTKLVEYAVKEQAKNETISKKDYRQAYDAYTPTMTAEIMQFEKEEDAKAALEAVKAEGADFAAIAKEKTIAADKKTTYTFDSGETTLPAEVVRAASGLKEGNRSEIITALDPAISKRTYHIIKVTKKATKKADWKAYQKRLKDIIVTGKLKDPDFQNKVIAKALDKANVKIKDKAFANILAQFAKPNQKQPAQK
|
Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
|
Q5X9P6
|
B8E7R0
|
DXR_SHEB2
|
2-C-methyl-D-erythritol 4-phosphate synthase
|
Shewanella
|
MQNMVILGATGSIGASTLSVISANPLAYSVYGLVANASVDKMLALCVAHKPKVAHMVDEAAAKQLRAVLPATLNIQVTTGMNDLLGLVTAAEVDTVMAAIVGAAGLVPTLEAVKAGKRVLLANKEALVMSGELFIEATKRSGAVLLPVDSEHNAIFQCLPQEVQANLGRCDLAASGISHILLTGSGGPFLRSDLATLAAMTPAQACKHPNWSMGPKISVDSATMMNKGLEFIEARWLFNTQAEQLKVVIHPQSVIHSMVQYRDGSVIAQMGNPDMRTPIAHCMAYPQRIHSGVEPLDFFKVGQLSFYEPDFERFPCLALAMDACAQGQEATTVLNAANEIAVEAFLQGQIGFTQIAKVNEACLVTVPKRPMGSIEDILALDAQTRVYARETLASIA
|
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
B8E7R0
|
B9M594
|
TRMD_GEODF
|
tRNA [GM37] methyltransferase
|
Geotalea
|
MKFDVLTLFPGMFEGPLTESILKRAREKGLIDVALHNIRDFAFDRHSVTDDYPYGGGAGMVMKVEPLAACVEHAQAGSPEARVILTTPHGRPFSHAVAAELAREEALIIICGRYEGVDERVRELFVDDEISLGDFVLTGGEMAAMVIIDAVSRLVPGVLGSEESAINDSFADGLLEYPQYTRPSEFRGLEVPKVLLSGNHQEIEMWRRHKSLEATALLRPDLLQSAKLTNGDRKYLEKSSKDAR
|
Specifically methylates guanosine-37 in various tRNAs.
|
B9M594
|
P24385
|
CCND1_HUMAN
|
PRAD1 oncogene
|
Homo
|
MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI
|
Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition . Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase . Hypophosphorylates RB1 in early G(1) phase . Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals . Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity . Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex . Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner .
|
P24385
|
Q9Z8H0
|
ISPG_CHLPN
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Chlamydia
|
MTLITPAINSSRRKTHTVRIGNLYIGSDHSIKTQSMTTTLTTDIDSTVEQIYALAEHNCDIVRVTVQGIKEAQACEKIKERLIALGLNIPLVADIHFFPQAAMLVADFADKVRINPGNYIDKRNMFKGTKIYTEASYAQSLLRLEEKFAPLVEKCKRLGKAMRIGVNHGSLSERIMQKYGDTIEGMVASAIEYIAVCEKLNYRDVVFSMKSSNPKIMVTAYRQLAKDLDARGWLYPLHLGVTEAGMGVDGIIKSAVGIGTLLAEGLGDTIRCSLTGCPTTEIPVCDSLLRHTKIYLDLPEKKNPFSLQHSENFVSAAEKPAKTTLWGDVYGVFLKLYPHHLTDFTPEELLEHLGVNPVTKEKAFTTPEGVVVPPELKDAPITDVLREHFLVFHHHQVPCLYEHNEEIWDSPAVHQAPFVHFHASDPFIHTSRDFFEKQGHQGKPTKLVFSRDFDNKEEAAISIATEFGALLLDGLGEAVVLDLPNLPLQDVLKIAFGTLQNAGVRLVKTEYISCPMCGRTLFDLEEVTTRIRKRTQHLPGLKIAIMGCIVNGPGEMADADFGFVGSKTGMIDLYVKHTCVKAHIPMEDAEEELIRLLQEHGVWKDPEETKLTV
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
Q9Z8H0
|
C0MBK6
|
OTC_STRE4
|
Ornithine carbamoyltransferase
|
Streptococcus
|
MTQVFQGRSFLAEKDFTREEFEYLIDFAAHLKDLKKRGIPHHYLEGKNIALLFEKTSTRTRAAFTTAAIDLGAHPEYLGANDIQLGKKESTEDTAKVLGRMFDGIEFRGFSQRMVEELAEFSGVPVWNGLTDEWHPTQMLADYLTVKENFGKLEGLTLVYCGDGRNNVANSLLVAGTLLGVNVHIFSPKELFPAEDIVKLAEGYAKASGAHVLVTDNADEAVKGADVLYTDVWVSMGEEDKFEERVKLLKPYQVNMELVKKAANDNLIFLHCLPAFHDTNTVYGKDVAEKFGVEEMEVTDEVFRSKYARHFDQAENRMHTIKAVMAATLGNLFIPKV
|
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
|
C0MBK6
|
P07678
|
ATPE_BACP3
|
F-ATPase epsilon subunit
|
Bacillus
|
MKTIHVSVVTPDGPVYEDDVEMVSVKAKSGELGILPGHIPLVAPLEISAARLKKGGKTQYIAVSGGFLEVRPDNVTILAQAAERAEDIDVLRAKARKSGRTPLQSQQDDIDFKRAELALKRAMNRLSVAEMK
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
P07678
|
Q9U6Y7
|
GFPL_DISST
|
GFP-like fluorescent chromoprotein dsFP483
|
Discosoma
|
MSCSKSVIKEEMLIDLHLEGTFNGHYFEIKGKGKGQPNEGTNTVTLEVTKGGPLPFGWHILCPQFQYGNKAFVHHPDNIHDYLKLSFPEGYTWERSMHFEDGGLCCITNDISLTGNCFYYDIKFTGLNFPPNGPVVQKKTTGWEPSTERLYPRDGVLIGDIHHALTVEGGGHYACDIKTVYRAKKAALKMPGYHYVDTKLVIWNNDKEFMKVEEHEIAVARHHPFYEPKKDK
|
Pigment protein that is green in color.
|
Q9U6Y7
|
A0A0H3KB22
|
QUEE_BURM1
|
Queuosine biosynthesis protein QueE
|
Burkholderia cepacia complex
|
MTYAVKEIFYTLQGEGANAGRPAVFCRFAGCNLWSGREEDRAQAVCRFCDTDFVGTDGENGGKFKDADALVATIAGLWPAGEAHRFVVCTGGEPMLQLDQPLVDALHAAGFGIAIETNGSLPVLESIDWICVSPKADAPLVVTKGNELKVVIPQDNQRLADYAKLDFEYFLVQPMDGPSRDLNTKLAIDWCKRHPQWRLSMQTHKYLNIP
|
Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.
|
A0A0H3KB22
|
A8LC67
|
RL1_FRASN
|
50S ribosomal protein L1
|
unclassified Frankia
|
MKRSKAYRAAAEKIDATALYSPLDAARLARETSSTKYDATVEVAIRLGVDPRKADQMVRGTVNLPHGTGKSPRVAVFAAGEKAAEATAAGADVVGSDDLVARIQEGFLDFDATVATPDQMAKVGRIARILGPRGLMPNPKTGTVTLDVAKVVGDIKGGKINFRVDKQGNLHIVIGKVSFSEAQLIENYTVALDEIVRVKPSAAKGRYLKKVTFATTMGPGIPVDPNRTRNLLEDAPA
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
A8LC67
|
H6LGM8
|
CARE_ACEWD
|
Electron transfer flavoprotein subunit alpha
|
Acetobacterium
|
MAIKVIEEKCIGCSKCQKSCPFDAITIENKIAVIGDACTNCGTCIDVCPTEAILQEGTEKIVRDLSMYKGVWVFAEQREGKIMPVVFELLGEGKKLANEIGTELCAILCGSNVAELTDELFAYGADKVYLADAPELEKYTTDGYSKIINEAIGLYKPEIVLYGATHIGRDLAPCLAVKVNTGLTADCTKLEIDPDDKKIRQTRPAFGGNLMATIVCPGSRPQMSTVRPGVMDKAAYDPSQKGEVIKLDATFNEGDIRTKVLEIVKTTTDNISISDADFIVSGGMGLGKPEGFELLKQLADKLGGTVATSRACVDAGWADHAQQVGQTGTTVKPQIYFACGISGAIQHIAGMQDSDIIIAINKNENAPIFEVADYGIVGDLYKVIPAIIEELDKIGK
|
Caffeyl-CoA reductase-Etf complex catalyzes the reduction of caffeyl-CoA to yield hydrocaffeyl-CoA. It couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant. It uses the mechanism of electron bifurcation to overcome the steep energy barrier in ferredoxin reduction. The electron transfer flavoprotein (Etf) mediates the electron transfer between the different donors and acceptors. The iron-sulfur cluster may be involved in electron transport, possibly in the intramolecular electron transfer from the Etf protein subunit to the caffeyl-CoA reductase subunit inside the complex. The complex can also reduce 4-coumaroyl-CoA and feruloyl-CoA.
|
H6LGM8
|
A4QK75
|
NU1C_ARAHI
|
NADH-plastoquinone oxidoreductase subunit 1
|
Arabis
|
MIIYATEVETINSFVRLESLKELYSLVWIFVPIFSLVLGIITGVLVIAWIERELSAGIQQRIGPEYAGPLGILQALADGTKLLFKEDLRPSRGNTPLFSIGPSIAVISILLSYSVIPFSNHLVLADLNIGIFLWIAISSIAPIGLLMSGYGSNNKYSFLGGLRAAAQSISYEIPLTLCVLSISLLSNSLSTVDIVEAQSKYGFWGWNLWRQPIGFIIFLISSLAECERLPFDLPEAEEELIAGYQTEYSGIKFGLFYVASYINLLISSLFVTILYLGGWNISIPYISIPYISILELFERDPIFGTTIGIFITLAKTYLFLFISIATRWTLPRLRMDQLLNLGWKFLLPISLGNLLLTTSFQLFSL
|
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
|
A4QK75
|
P14319
|
QACC_STAAU
|
Quaternary ammonium determinant C
|
Staphylococcus
|
MPYIYLIIAISTEVIGSAFLKSSEGFSKFIPSLGTIISFGICFYFLSKTMQHLPLNITYATWAGLGLVLTTVVSIIIFKEQINLITIVSIVLIIVGVVSLNIFGTSH
|
Multidrug exporter. Is implicated for the resistance to bacteriocidal quaternary ammonium compounds and ethidium bromide.
|
P14319
|
B0BWA7
|
RL10_RICRO
|
50S ribosomal protein L10
|
spotted fever group
|
MLRSEKPVAVEDIVNIYKESPSIIITHYHGLTVSQVSVLREALKSKEAGFKVVKNTLAKIAANQTGLNSIANLFAGPTAIVYSKEPVEMAKLVVNFAKANDNLKIIGGIVDNHVLDEHSIKELSKLLTLNELRGKIIGLLQAPATQVVGVLQAPSSSMARVIQAYASKN
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
B0BWA7
|
Q6DE23
|
KISHB_XENLA
|
Transmembrane protein 167B
|
Xenopus
|
MTNVYSLDGLLVFALLFVCTCAYFRKVPRLRSWLLSEKKGVWGVFYKAAVIGSRLHLAVSISCIAMAFYVLFIK
|
Involved in the early part of the secretory pathway.
|
Q6DE23
|
Q8KP10
|
ACT_BACMT
|
MDH activator
|
Bacillus
|
MGKLFEEKTIKTEQIFSGRVVKLQVDDVELPNGQTSKREIVRHPGAVAVIAITNENKIVMVEQYRKPLEKSIVEIPAGKLEKGEDPRVTALRELEEETGYECEQMEWLISFATSPGFADEIIHLYVAKGLSKKENAAGLDEDEFVDLIELTLDEALQYIKEKRIYDSKTVIAVQYLQLQEALKHK
|
Involved in the activation of the NAD-dependent methanol dehydrogenase (MDH). MDH activation by Act involves hydrolytic removal of the nicotinamide mononucleotide (NMN) moiety of the NAD cofactor, changing its ping-pong type of reaction mechanism into a ternary complex reaction mechanism. It requires the presence of magnesium ions and is also able to use ADP-ribose.
|
Q8KP10
|
Q8TIR7
|
NIKR3_METAC
|
Putative nickel-responsive regulator 3
|
Methanosarcina
|
METELMRIGVSLPDTLLSKFDEIIEKRGYSSRSEGIRDAIRSYISYYEWMGDIKGHRVGTVAVIYDHTKRGLSNALADIQHHYSHLIKSSVHIHLDHDNCFEVIVLDGDGEEIKELAEAIMALKGVKFSKLTTVASNEKI
|
Transcriptional regulator.
|
Q8TIR7
|
A0RVX8
|
RL22_CENSY
|
50S ribosomal protein L22
|
Cenarchaeum
|
MGDFGYSFEGYDPTRHVRASLREKQISHKHAREISLHIRGMTVEKARDFLQAVIEKKRAVPFRRFKRQVGHRSDPGVMAGRYPEKSAAEFIKLLDNLESNAEYKGMDLDRLTIVGAVAHKGILIKRFIPRAMGRSTPKNNVLTHVELVAREA
|
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
|
A0RVX8
|
P0DUJ1
|
APOE_PTEGI
|
Apolipoprotein E
|
Pteropus
|
MKFLWAALVVTLLAGCQADVEEEVKLGQEPDRWQAKQPWEQALGRFWEYLRWVQTLSNKVKEELLNSQVTEELKLLIEETMKEVKAYKEELEKQVGPIAQETQARLSKELQAAQARLESDMEDVRTRLAQYRSEAQAALGQNTDDLQGRLASHLRKLRKRLLRDAEDLQKRLAVYQAGTREAAERGVSAVHERLGPLMMEGPLQAIPPSQQLRERAEAWGQKVRGRLESVGSQARDRLDDMRDQMEELKAKVEEQASQVRLQAEAFQTRLKSWFEPLVQDMQRQWASLVEKVQSSLGISPSTKPSKTK
|
APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells.
|
P0DUJ1
|
Q5FM85
|
RL22_LACAC
|
50S ribosomal protein L22
|
Lactobacillus
|
MAEQISSAKAEARTVRIAPRKARLVIDLIRGKSVAEALAILEFTPRAASPIVEKVLRSAIANAEHNYDLESANLYVSEAYVNEGATLKRFRPRAKGMASPINKRTSHVVVVVSEKND
|
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
|
Q5FM85
|
A1L224
|
CR3L2_DANRE
|
Processed cyclic AMP-responsive element-binding protein 3-like protein 2
|
Danio
|
MEIMDSGEPFLQWDKNLSELSEAGENDILYSTHFTDLLDDLSQEALLGQLLSDPFLSGRGDAMDTEEELTRASPVPPHIQAEHSYSLCGDSRPQSPLSHLPGEPGSDAADSESDEWPMEQEDKGIKMEPLLCVPLPALTLTVTPAGSAPEPVIDSCDSAQSLSLPQVKEDSNSPQIKLEPHEVDQFLNLSPKGLECLQMPPTPPSSVGSDSEGSQSPVHPCAPASPTQTPAVLKVAPRAPSSLSSSPLLTAPHKLQGSGPLLLTEEEKRTLIAEGYPVPTKLPLSKAEEKALKKIRRKIKNKISAQESRRKKKEYVDALEKKVETCSNENHELRRKVENLECTNKSLLQQLHSLQAVVAGKVPRSCRVTGTQTSTCLMVVVLCFSLFLGSFYPGLSPCSSITKADLSREISIHDSYTTTVKSRSLLSIQEPGGLDEPHPIGLGGEYPEWDRQADVMAAWRFEQQHKEEEAELHKAEHRPLLLSTNETHAQKAILIDLHTHRSNETAKVIQLDRTVNETS
|
Transcription factor involved in unfolded protein response (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/mbtps1 and S2P/mbtps2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in chondrogenesis. May protect neuroblastoma cells from ER stress-induced death. In vitro activates transcription of target genes via direct binding to the CRE site.
|
A1L224
|
Q2LZ59
|
MOB2_DROPS
|
Mps one binder kinase activator-like 2
|
Sophophora
|
MKETLSSKVPTTRTVGVTFDSVSESKSKLKSGSVQGTTATATATGPPSPPSSYVIKCLLKTARFMWQVTTIPAKIGDTLGTLYRYAQDSVDTFLCVAGKARRKERDGDQNSTDTKLYLEESVLERKLPEADLKALVDLPAGLDYNEWLASHTLALFEHVNLVYGTISEFCTQSGCADMTGPGNRTYLWFDEKGKKTRVAAPQYIDYVMTFTQKTVSDESIFPTKYANEFPGSFESIARKILRLQFHVIAHLYAAHFREIALLGLHTHLNLTFAHLTALHRRFNLIDEKETDVLRDLEVALRLTDDTSGQDSSSSVHEHSSSSSSPPVQHQQHQHQQQHNNSSSTSNSTSPAEALHVNSQSNSNSHSNSSNSHTTTASASASLIDGDSAAPPICTQPEAGAGCKPAGSSGLLGGILGDLTSGEFGDTTRYCTSAVPQAAASSSASAAGPGADGAASAALNNGAGALHLNFSNNNNNNHNLNHLNHHHHHHHHQHHHQHHPHGHHGHQGHQGHQGHHQAPASTTVPHSGLIQCNAAGAVGASAGGGGNAVSAATGGATSASSTA
|
Required for the normal morphogenesis of a variety of polarized outgrowths including epidermal hairs, bristles, arista laterals, and dendrites.
|
Q2LZ59
|
P14614
|
GLUB4_ORYSJ
|
Glutelin type-B 4 basic chain
|
Oryza sativa
|
MATIAFSRLSIYFCVLLLCHGSMAQLFGPNVNPWHNPRQGGFRECRFDRLQAFEPLRRVRSEAGVTEYFDEKNEQFQCTGTFVIRRVIEPQGLLVPRYSNTPGMVYIIQGRGSMGLTFPGCPATYQQQFQQFLPEGQSQSQKFRDEHQKIHQFRQGDIVALPAGVAHWFYNEGDAPVVALYVFDLNNNANQLEPRQKEFLLAGNNNREQQMYGRSIEQHSGQNIFSGFNNELLSEALGVNALVAKRLQGQNDQRGEIIRVKNGLKLLRPAFAQQQEQAQQQEQAQAQYQVQYSEEQQPSTRCNGLDENFCTIKARLNIENPSHADTYNPRAGRITRLNSQKFPILNLVQLSATRVNLYQNAILSPFWNVNAHSLVYIVQGHARVQVVSNLGKTVFNGVLRPGQLLIIPQHYVVLKKAEHEGCQYISFKTNANSMVSHLAGKNSIFRAMPVDVIANAYRISREQARSLKNNRGEELGAFTPRYQQQTYPGFSNESENEALE
|
Seed storage protein.
|
P14614
|
O74844
|
CENPQ_SCHPO
|
Sim4-mal2-associated protein 7
|
Schizosaccharomyces
|
MEMKRRVRAVRRDQIQKRWRPLEDKQRQEIIIIFRTCSRLVLNTIKSETRKSLAEEWFMNILLKIEAPLRNLPVPRKRKESILFSQLLSSNMQLEQQLYSDLDHINVLQQELKVETARLENEQKSYEEMKQNMAINNSRLADLKSKLHPYLKKGLKISHDNFSDSNDFSFQKKLNTEDSNTSKTSTLDMYKEKLKPFTKTMQIHANKTVQLSQTIQKATLLLQRLNNTKNIGLNKSSKLKIKNI
|
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore COMA complex, which connects centromere-associated proteins and the outer kinetochore. COMA interacts with other inner kinetochore proteins to form the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
|
O74844
|
A1SYY2
|
UREE_PSYIN
|
Urease accessory protein UreE
|
Psychromonas
|
MLQVFERLDHTHDEISDSITLDQDTRKKSRIKSVTDKGANIGIFVERGHPLLVGEILKTECGLLIEVKGKAEDVSTAVANDWLNFSKVCYHLGNRHTTLQIGELWVRFKPDHVLEQLAENYGLSVNSIPAVFEPENGAYGVRSHGHSHAHDS
|
Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.
|
A1SYY2
|
Q2NRH3
|
TYSY_SODGM
|
Thymidylate synthase
|
Sodalis
|
MKQYLDLMRRVRAQGTPKADRTGTGTLSIFGHQMRFDLRQGFLLVTTKRCHLRSIIHELLWFLNGDTNIAYLQQNNVSIWDEWADDNGDLGPVYGRQWRAWGTSDGRQIDQLAEVVRQLKQDPDSRRIIVSAWNVGELDKMALAPCHALFQFYVANGTLSCQLYQRSCDIFLGLPFNIASYALLVHMLAQQCDLQVGDFVWTGGDTHLYSNHLQQADLQLTRDPLPLPQLLIKRRPATLFDYRFEDFELTGYDPHPAIKAPVAV
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
|
Q2NRH3
|
Q3A9Q4
|
RL10_CARHZ
|
50S ribosomal protein L10
|
Carboxydothermus
|
MKPIIEQKAKVVAEIEEMIKSSQAAILVDYRGLTVAEMTELRRKLKEKGAEIKVVKNTLAKRAAHNLGITGLDPYLEGPTALAVAKEDPASAAKVLFDFAKDHPNLEIKVGILENIVLEKDQVKAIADLPPRNVLLAKLLGGMQAPLYGFAGALAGMLRKFVYALEAIRKQKAGEE
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
Q3A9Q4
|
Q3AC01
|
PYRC_CARHZ
|
Dihydroorotase
|
Carboxydothermus
|
MGMLIKNGNVVMVEDGKIRKMDVLIDKGIIVEISPEINRSDVEVIDIEGKFLIPGLIDMHVHFRDPGYTHKEDIHSGSNAALAGGFTGVLMMPNTDPPPDNATVIYYWKEKSKSIPLNILFSGCITKNRAGKELSKFYELKEAGAVAITDDGNWVADGAVFRHAMEYAAALDLLVITHPEEPTIANRGVINEGYWSTVLGLRGIPKAAENIAIYRDIEIAKMTGAKLHVAHLSTAEGVRLVAAAKKLGLKVTAEVTPHHLVLTDEALAGYDTNLKVNPPLREAEEQKALLKGLLEGVIDVIATDHAPHASYEKNVEFNDAPFGIEGLETAFPVLYTELVLKKKITLEKLLLKMTVNPAKILQLPKQGDIKKGNYANLTVIDPKLTLKVSEELLVGKSKNNPFLGRTLTGWPVMTVYQGIVAYQRLLKGVQ
|
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
|
Q3AC01
|
B4SU91
|
SPEE_SALNS
|
Spermidine synthase
|
Salmonella
|
MAENTMWHETLHDQFGQYFAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGHAKHVLIIGGGDGAMLREVTRHKNVETITMVEIDAGVVSFCRQYLPNHNAGSYDDPRFTLVIDDGVNFVNQTHQTFDVIISDCTDPIGPGESLFTSAFYEGCKRCLNPGGIFVAQNGVCFLQQDEALDSHRKLSHYFSDVGFYQAAIPTYYGGIMTFAWATDNGALRHLSSEIIQARFHAAGLKCRYYNPAIHAAAFALPQYLHDALSAQ
|
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
|
B4SU91
|
Q12T12
|
PCKA_SHEDO
|
Phosphoenolpyruvate carboxykinase (ATP)
|
Shewanella
|
MTDGAPRTFLNPTSAELVEIALQRGEGRLTANGALVALTGARTGRSPADRFIVKEPSSEADIEWGPVNKPFDAGAFDALWGRVEAYLSEKELFVSELEVGADDEHYLPVRVTTEYAWHQLFARNLFITPEHFNRGDKGVWQIINAPGFVCDPSRDGTHSDAVVILNFAERKVLLAGLKYAGEMKKSMFSVQNFLLPAKGVLPMHCSANVGQDGDTTLFFGLSGTGKTTLSADPKRFLIGDDEHGWAKGGVFNIEGGCYAKCIDLSQKNEPVIWDAIRFGTVLENVMLDENRVPNYKDSSLTENSRAAYPLEHIAQRKVENRGNEPHAVVFLTCDVSGVLPPVSILTKEQAAYHFLSGYTAKVGSTEMGSTSAIQSTFSTCFGAPFFPRPAGVYAELLIERIESFNSQVYLVNTGWTGGPHGVGKRFDIPTTRAIVDAIVSGSLKDAPTEHLATLNLAVPLAIEGVDSTLLNPINTWADKDMYAKYAKQLAQEFNSNFAKYQVSEAIKQAGPKA
|
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
|
Q12T12
|
Q03RR0
|
NUSB_LEVBA
|
Antitermination factor NusB
|
Levilactobacillus
|
MTLTRHQIRERAFQMLFALNANPEADHDALYQRVLTDDPNQLVPVPDYLATLVNGVLAHQSELDAQIDQYLSTGWQLKRIAKTDLVILRMAFYEIEHVDDVPNRVAVNEALELAKNFSDDRSRRFINGVLAHTLDDETDTQA
|
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
|
Q03RR0
|
Q9NPI6
|
DCP1A_HUMAN
|
Transcription factor SMIF
|
Homo
|
MEALSRAGQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEFQLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVVEEETRRSQQAARDKQSPSQANGCSDHRPIDILEMLSRAKDEYERNQMGDSNISSPGLQPSTQLSNLGSTETLEEMPSGSQDKSAPSGHKHLTVEELFGTSLPKEQPAVVGLDSEEMERLPGDASQKEPNSFLPFPFEQLGGAPQSETLGVPSAAHHSVQPEITTPVLITPASITQSNEKHAPTYTIPLSPVLSPTLPAEAPTAQVPPSLPRNSTMMQAVKTTPRQRSPLLNQPVPELSHASLIANQSPFRAPLNVTNTAGTSLPSVDLLQKLRLTPQHDQIQTQPLGKGAMVASFSPAAGQLATPESFIEPPSKTAAARVAASASLSNMVLAPLQSMQQNQDPEVFVQPKVLSSAIPVAGAPLVTATTTAVSSVLLAPSVFQQTVTRSSDLERKASSPSPLTIGTPESQRKPSIILSKSQLQDTLIHLIKNDSSFLSTLHEVYLQVLTKNKDNHNL
|
Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay . Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP . Contributes to the transactivation of target genes after stimulation by TGFB1 . Essential for embryonic development .
|
Q9NPI6
|
A6VN13
|
ORN_ACTSZ
|
Oligoribonuclease
|
Actinobacillus
|
MAQDKENLIWIDLEMTGLDPEQERIIEIATIVTDKNLNILAEGPVLAVHQPNQLLDKMSDWCIKTHTANGLVERVKASKLTERAAELQTIDFLKLWVPKGASPICGNSVAQDKRFLFKYMPDLADYFHYRHLDVSTLKELARRWKPEISDGFQKANTHLALDDIRESIKELAYYREHFIKLD
|
3'-to-5' exoribonuclease specific for small oligoribonucleotides.
|
A6VN13
|
A2S6L0
|
MNMG_BURM9
|
Glucose-inhibited division protein A
|
pseudomallei group
|
MLYPTEFDVIVVGGGHAGTEAALASARMGAKTLLLTHNIETLGQMSCNPSIGGIGKGHLVKEVDALGGAMAAATDEGGIQFRILNSSKGPAVRATRAQADRVLYKQAIRRRLENQPNLWLFQQAVDDLMVEGDRVVGAVTQVGVRFRARAVVLTAGTFLDGKIHVGLNHYTGGRAGDPAAVSLSSRLKELNLPQGRLKTGTPPRIDGRTIDFSKLDEQPGDLDPIPVFSFLGRAEQHPQQLPCWVTHTNERTHDIIRSGLDRSPMYTGVIEGVGPRYCPSIEDKIHRFASKDSHQIFLEPEGLTTNEFYPNGISTSLPFDVQLALVHSMRGLEQAHILRPGYAIEYDYFDPRALKSSLETKAIGGLFFAGQINGTTGYEEAAAQGLLAGINAGRYAQEKDAWCPRRDQAYLGVLVDDLVTRGVSEPYRMFTSRAEYRLSLREDNADMRLTEIGRELGVVDDVRWDAFNRKRDAVSRETERLRTTWVTPKTLPADEATALLGKPIDHEYSLAELLRRPGVSYDGVCGLRGGECGPSEPLAEDELLLAQIKEQIEIGIKYQGYIERQAGEIERNGANENTRLPDGIDYTEVRGLSFEVSQKLNQFRPETIGQASRISGMTPAAISLLMVHLKKRGLGRRKGADSVPGADVQADNTAAQQ
|
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
A2S6L0
|
A0LUE6
|
POTA_ACIC1
|
Spermidine/putrescine import ATP-binding protein PotA
|
Acidothermus
|
MTDYTPDETPGIALRDISKVYSSRTGDVVAVHALTLAVRSGEFFSLLGPSGCGKTTTLRMIAGFEEPTTGRILLEGRDVTDVPPHRRDVNMVFQNYALFPHLTVWENVAFGPKRKKLPREEIRRRVGEALELVDLVGREKRRPDELSGGQQQRVALARALVNRPRALLLDEPLGALDLKLRQAMQLELKRIQREAGVTFVYVTHDQGEALTMSDRIAVMNAGRVEQLGTPREIYETPSTPFVAGFIGTSNVISAPLARIEGAIALLATSADERVLVPLRVPVPPGASISATVRPEKIRLSLHPPDGDRCRLLGVVREVVYLGTATQYVVATSVAEQLVVYAQNDGTADLVPAPGDRIWLWWRPEHGYQLIHADATDVPEEAAP
|
Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
|
A0LUE6
|
P35634
|
FLA2_BARBA
|
Flagellin
|
Bartonella
|
GAAILTNDNAMDALQDL
|
Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. Flagella are an important component in the invasiveness of B.bacilliformis.
|
P35634
|
B8DJT5
|
DAPB_DESVM
|
4-hydroxy-tetrahydrodipicolinate reductase
|
Desulfovibrio
|
MSTSIIVTGAGGRMGSTICRMAQEDPVLTLAAVVERPERLASLDVWKCPSGSDPDAVFATVPGGVVVDFTSPEASMANARAAARAGVSHVIGTTGLTAEQKAELADLARTARIFWAPNMSIGVNVLLKILPQLVQQLGEQYDLEMVELHHNRKKDSPSGTALRLAECLAEARGWNLPDVANYHREGIIGERPKDEIGIQTIRGGDVVGVHTIYAMGPGERIEITHQAHSRENFAQGALRAAKWLPQQQPGTLYSMLDML
|
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
|
B8DJT5
|
P27214
|
ANX11_BOVIN
|
Calcyclin-associated annexin-50
|
Bos
|
MSYPGYPPPAGGYPPGAPGGGAWGGAGYPPPTMPPIGLDNVANYAGQFNQDYLSGVAANMSGTFGGANVPNLYPGAPGGGYPPVPPGGFGQPPPAQQPVPSYGMYPPPGGNPTSGMPSYPPYPGAPVPGQPMLPPGQQPPGVYPGQPPMTYPGQSPVPPPGQQPVPSYPGYSGSGTVTPAVSPAQFGNRGTITDASGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILALMKTPVLFDAYEIKEAIKGAGTDEACLIEILASRSNEHIRELNRVYKTEFKKTLEEAIRSDTSGHFQRLLISLSQGNRDESTNVDMTLVQRDVQELYAAGENRLGTDESKFNAILCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEQGMLAVVKCLKNTPAFFAERLNKAMRGAGTKDRTLIRIMVSRSEIDLLDIRAEYKRLYGKSLYHDITGDTSGDYRKILLKICGGND
|
Binds specifically to calcyclin in a calcium-dependent manner. Required for midbody formation and completion of the terminal phase of cytokinesis.
|
P27214
|
A1WBI7
|
PANB_ACISJ
|
Ketopantoate hydroxymethyltransferase
|
unclassified Acidovorax
|
MTDSPTAGTPYGTLPPASPLPQRRPVSLPRLAQMREAGEKITMLTAYDATFAAVADAAGVECILVGDSLGMVCQGLPSTVGVTLEHMAYHTASVARGLHRVQGTAWLIADLPYGSYAESREQALRSACQLMQAGAHMVKLEGGGWTAPTVQFLVERGVPVCAHLGLTPQTVHALGGYRVQGKGDQAAQQLRRQALELQDAGAAMLVLEMVPTPLARDLTQALPRCHTIGIGAGSGTAGQVLVMHDMLGINLGKNPKFVHDFMRDAGSVRGAIEAYVQAVKQGRFPDDALHAWN
|
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
|
A1WBI7
|
Q6P8Y0
|
CF161_MOUSE
|
Cilia- and flagella-associated protein 161
|
Mus
|
MAQNVYGPGVRMGNWNEDVYLEEERMRHFLEKREKGELLIQRNRRVKKNILRPMQLSVSEDGYVHYGDKVIIVNPDQVLGEEAGKFMRGDLSLCMSPDEVKAQLSDDLEIPCGVSAVQTIAPMGRNTFTILSDGANSCEMGQVVVYGQNFCLGIAAGLEGKMLYLTSDHRTLLKSSLKSGLQEVTLTDEVTHLNCWQAAFLDPQLRLEYEGFPVRANEKIVIYHRHTNRALAVHRNLFLRTYFGKEMEVVAHTYLDSHKVEKPKNQWMLVTGNPRNKSNTMLDISKPITEDTRALEQAMGINT
|
Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
|
Q6P8Y0
|
Q9M0G7
|
MIK1_ARATH
|
Protein PHLOEM INTERCALATED WITH XYLEM-LIKE 2
|
Arabidopsis
|
MKMKIIVLFLYYCYIGSTSSVLASIDNVNELSVLLSVKSTLVDPLNFLKDWKLSDTSDHCNWTGVRCNSNGNVEKLDLAGMNLTGKISDSISQLSSLVSFNISCNGFESLLPKSIPPLKSIDISQNSFSGSLFLFSNESLGLVHLNASGNNLSGNLTEDLGNLVSLEVLDLRGNFFQGSLPSSFKNLQKLRFLGLSGNNLTGELPSVLGQLPSLETAILGYNEFKGPIPPEFGNINSLKYLDLAIGKLSGEIPSELGKLKSLETLLLYENNFTGTIPREIGSITTLKVLDFSDNALTGEIPMEITKLKNLQLLNLMRNKLSGSIPPAISSLAQLQVLELWNNTLSGELPSDLGKNSPLQWLDVSSNSFSGEIPSTLCNKGNLTKLILFNNTFTGQIPATLSTCQSLVRVRMQNNLLNGSIPIGFGKLEKLQRLELAGNRLSGGIPGDISDSVSLSFIDFSRNQIRSSLPSTILSIHNLQAFLVADNFISGEVPDQFQDCPSLSNLDLSSNTLTGTIPSSIASCEKLVSLNLRNNNLTGEIPRQITTMSALAVLDLSNNSLTGVLPESIGTSPALELLNVSYNKLTGPVPINGFLKTINPDDLRGNSGLCGGVLPPCSKFQRATSSHSSLHGKRIVAGWLIGIASVLALGILTIVTRTLYKKWYSNGFCGDETASKGEWPWRLMAFHRLGFTASDILACIKESNMIGMGATGIVYKAEMSRSSTVLAVKKLWRSAADIEDGTTGDFVGEVNLLGKLRHRNIVRLLGFLYNDKNMMIVYEFMLNGNLGDAIHGKNAAGRLLVDWVSRYNIALGVAHGLAYLHHDCHPPVIHRDIKSNNILLDANLDARIADFGLARMMARKKETVSMVAGSYGYIAPEYGYTLKVDEKIDIYSYGVVLLELLTGRRPLEPEFGESVDIVEWVRRKIRDNISLEEALDPNVGNCRYVQEEMLLVLQIALLCTTKLPKDRPSMRDVISMLGEAKPRRKSNSNEENTSRSLAEKHSSVFSTSPVNGLL
|
Involved in the regulation of procambium maintenance and polarity during vascular-tissue development . Involved in the pollen tube perception of the female signal . Phosphorylates MDSI1 .
|
Q9M0G7
|
Q7MAE2
|
CH10_WOLSU
|
Chaperonin-10
|
Wolinella
|
MNFKPLGQRVLVERLEEDTKTASGIIIPDNAKEKPLMGTVKALSEEVAKEGLLKAGSQVVFAKYSGTDVKLEGKEYLILKVEDLLGTIE
|
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
|
Q7MAE2
|
Q634Q3
|
END4_BACCZ
|
Endonuclease IV
|
Bacillus cereus group
|
MLKIGSHVSMSGKKMLLAASEEAVSYGATTFMIYTGAPQNTRRKPIEELNIEAGRKHMEQNGIEEIIVHAPYIINVGNTTKPETFQLGVDFLRMEIERTSALGVAKQIVLHPGAHVGAGADAGIQQIIKGLNEVLTPDQTVNIALETMAGKGTECGRSFEEIAKIIDGVKYNEKLSVCFDTCHTHDAGYDIVNDFDGVLNEFDKIVGIDRLQVLHINDSKNVRGAGKDRHENIGFGHIGYKALHHIVHHPQLTHVPKILETPYVGEDKKDKKPPYKLEIEMLKNGTFDEGLLEKIKAQ
|
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.
|
Q634Q3
|
B8ZPZ6
|
FUCI_STRPJ
|
FucIase
|
Streptococcus
|
MIQHPRIGIRPTIDGRRQGVRESLEVQTMNMAKSVADLISSTLKYPDGEPVECVISPSTIGRVPEAAASHELFKKSNVCATITVTPCWCYGSETMDMSPDIPHAIWGFNGTERPGAVYLAAVLASHAQKGIPAFGIYGRDVQEANDTDIPEDVKEKLLRYARAALATGLMRDTAYLSMGSVSMGIGGSIVNPDFFQEYLGMRNESVDMTEFTRRMDRGIYDPEEFERAMVWVKEHIKEGVDRNREDLILSKEEKEKQWEFVIKMFMIGRDLMVGNPRLAELGFEEEAVGHHALVAGFQGQRQWTDHFPNGDFMETFLNTQFDWNGIRKPFVFATENDSLNGVSMLFNYLLTNTPQIFADVRTYWSPEAVERVTGYTLEGRAAAGFLHLINSGSCTLDGTGQATRDGKPVMKPFWELDESEVQAMLENTDFPPANREYFRGGGFSTRFLTKGDMPVTMVRLNLLKGVGPVLQIAEGYTLELPEDVHHTLDNRTDPGWPTTWFAPRLTGKGAFKSVYDVMNNWGANHGAITYGHIGADLITLASMLRIPVNMHNVPEEDIFRPKNWSLFGTEDLESADYRACQLLGPLHK
|
Converts the aldose L-fucose into the corresponding ketose L-fuculose.
|
B8ZPZ6
|
Q1LSE1
|
GATA_CUPMC
|
Glutamyl-tRNA(Gln) amidotransferase subunit A
|
Cupriavidus
|
MPFSADSVTSLRQIADALAARSVSAEELAREYLARIEAGRALNAFVAVDPELTLAQARAADERRAQGQATPLTGVPIAHKDVFVTRGWKSTAGSKMLANYESPFDATVVERLAAAGMVTLGKTNMDEFAMGSSNENSFFGPVSNPWDTSRVPGGSSGGSAAAVAAGLAPAATGTDTGGSIRQPASFSGITGIKPTYGRVSRYGMIAFASSLDQGGPMAHSAEDCALLLNGMAGFDPKDSTSLTPELGGVTEDFTRLLGQPRAGATASQPLAGLRIGLPREYFGKGLSADVEQALRAALAEYEKLGATLVDVTLPKTELSIPVYYIIAPAEASSNLSRFDGVRYGHRAAQYGDLLDMYKKSRAEGFGPEVKRRIMVGTYVLSHGYYDAYYLQAQKIRRIIADDFQRAFTQCDVIMGPVAPTVAWKLGEKTADPVQMYLADIFTLSTSLAGLPGMSVPCGFGEGNMPVGLQLIGNYFDEAQLLQTAHAFQQATDWHLRRPA
|
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).
|
Q1LSE1
|
Q7N8L0
|
CYSN_PHOLL
|
Sulfate adenylate transferase
|
Photorhabdus
|
MSALAQNETIAHQIKQQGGVEAYLHAQQEKGLLRFLTCGSVDDGKSTLIGRLLHDTRQIYEDQLSTLQNDSKRIGTQGEKLDLALLVDGLAAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLSILLIDARKGVQEQTRRHSFISTLLGIRHLVVAVNKMDLMEYRQEVFNQIKQDYMNFAGQLPTNLDVHFVPISALDGDNIVTISRNMDWYEGPTLLDILETVDVKKEASKQLLRFPVQYVSRPDLDFRGYSGTLSSGILRKGQKVKVMPSGICSQVERIVTFDGDLDFAVPGEAITVVLKDEIDISRGDLLISADDEMMVTRHALVDVVWMSEQPLVQGQNLDIKVAGKKSRGKVENIQYQVDITHLTQRVAVDLPLNAIGSVEFSFEEPLMLDSYQQNSDTGGIILVDRLTNVTVGAGLVREIQTDVYEGPKEFSEFELELNRLIRRHFPHWGARDLLGGK
|
With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
|
Q7N8L0
|
P0DMS5
|
APOA1_OCTDE
| null |
Octodon
|
MKAVVLAVAVLFLTGSQARHFWQRDDPQTSWDRVRDFATVYVDAVKESGRDYVAQLEASLGKHLNLKLLDNWDTLSTTFSKLRSELGPVTQEFWDNLEKDTEWLRQEMNKDLVEVKEKVQPYLKNFQEKVQLELEHYRKKVEPLGTDLRDGARQKLQELQEKLTPLGEDLRDRARQHVDELRAQLGPYSDQMRQRLTQRLEALKDSASLAEYQAKAQEHLKTFSEKAKPALEDLRLGLLPVLESLKASFLSSIDEVSKKLSAQ
|
Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.
|
P0DMS5
|
B9JA09
|
LPXK_AGRRK
|
Lipid A 4'-kinase
|
Agrobacterium tumefaciens complex
|
MVSEAPPFWWRKPDWRAWGLSPFSFLYGRVAGHRMVHGRRASVPVPVICVGNFTVGGAGKTPTALALARAAKTKGLKPGFLSRGYGGSLDVTTVVDPHDHHATAVGDEPLLLAREALTVIARRRADGAERLVREGADLIIMDDGFQSAQLAIDYALVVIDATRGIGNGHLVPGGPVRAPLRTQLGYTSGLLKVGDGNAADRIVRLAARAGKPFFSASIKTLGQEDLQGRKVLAFAGIADPTKFFRTVETLGAGIAVRRSFGDHEHLEEDEIADILDVADRDGLEIVTTSKDYVRLIGHHGRADELLARCRVIEIAMVFDDPHAPELIIDRAIAAARERRLREGWTGKTLLPSGEK
|
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
|
B9JA09
|
P49279
|
NRAM1_HUMAN
|
Solute carrier family 11 member 1
|
Homo
|
MTGDKGPQRLSGSSYGSISSPTSPTSPGPQQAPPRETYLSEKIPIPDTKPGTFSLRKLWAFTGPGFLMSIAFLDPGNIESDLQAGAVAGFKLLWVLLWATVLGLLCQRLAARLGVVTGKDLGEVCHLYYPKVPRTVLWLTIELAIVGSDMQEVIGTAIAFNLLSAGRIPLWGGVLITIVDTFFFLFLDNYGLRKLEAFFGLLITIMALTFGYEYVVARPEQGALLRGLFLPSCPGCGHPELLQAVGIVGAIIMPHNIYLHSALVKSREIDRARRADIREANMYFLIEATIALSVSFIINLFVMAVFGQAFYQKTNQAAFNICANSSLHDYAKIFPMNNATVAVDIYQGGVILGCLFGPAALYIWAIGLLAAGQSSTMTGTYAGQFVMEGFLRLRWSRFARVLLTRSCAILPTVLVAVFRDLRDLSGLNDLLNVLQSLLLPFAVLPILTFTSMPTLMQEFANGLLNKVVTSSIMVLVCAINLYFVVSYLPSLPHPAYFGLAALLAAAYLGLSTYLVWTCCLAHGATFLAHSSHHHFLYGLLEEDQKGETSG
|
Divalent transition metal (iron and manganese) transporter involved in iron metabolism and host resistance to certain pathogens. Macrophage-specific membrane transport function. Controls natural resistance to infection with intracellular parasites. Pathogen resistance involves sequestration of Fe(2+) and Mn(2+), cofactors of both prokaryotic and eukaryotic catalases and superoxide dismutases, not only to protect the macrophage against its own generation of reactive oxygen species, but to deny the cations to the pathogen for synthesis of its protective enzymes.
|
P49279
|
B7UNT3
|
ARGE_ECO27
|
N-acetylornithinase
|
Escherichia
|
MKNKLPPFIEIYRALIATPSISATEEALDQSNADLITLLADWFKDLGFNVEVQPVPGTRNKFNMLASCGQGAGGLLLAGHTDTVPFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLAKPLYILATADEETSMAGARYFAETTALRPDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYDAFTVPYPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRLTVDELHPPIPGYECPPNHKLVEVVEKLLGAKTEVVNYCTEAPFIQTLCPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVIHHFCWH
|
Catalyzes the hydrolysis of the amide bond of N(2)-acetylated L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to form L-ornithine, an intermediate in L-arginine biosynthesis pathway, and a branchpoint in the synthesis of polyamines.
|
B7UNT3
|
Q52331
|
KORC2_ECOLX
|
Transcriptional repressor protein KorC
|
Escherichia
|
MSDVNIRLECLRPAERWVQPTGAEIREVLHLAGLTGGQAARILGLGAKGDRTVRRWVGEDSPIPYAAWAILCDLAGIGAIWKGQG
|
Acts with KorA as corepressor in the control of the kilC and kilE operons.
|
Q52331
|
A5UE39
|
TPIS_HAEIE
|
Triose-phosphate isomerase
|
Haemophilus
|
MARRPLVMGNWKLNGSKAFTKELIEGLKAELHDVTGCDVAIAPPVMYLGTAEAALSGCGCNCGGKSVIQLGAQNVDINVKGAFTGDISTEMLKDFGAKYIIIGHSERRTYHKESDEFVAKKFGALKEAGLVPVLCIGESEAENEAGKTEEVCARQIDAVINALGVEAFNGAVIAYEPIWAIGTGKSATPAQAQAVHAFIRGHIAAKSQAVAEQVIIQYGGSVNDANAAELFTQPDIDGALVGGASLKAPAFAVIVKAAAAAKN
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
A5UE39
|
C4L1C9
|
TYSY_EXISA
|
Thymidylate synthase
|
unclassified Exiguobacterium
|
MKQYHDLCRHILDQGVVKEDRTGTGTTSVFGYQMRFNLQEGFPLITTKKLHIRSIIHELLWFISGETNVRYLQDNGVRIWNEWADEEGNLGPVYGSQWRSFPRPDGSSVDQLAQVIEQIKTNPDSRRLIVSAWNPGQLEEMALPPCHLLFQFYVADGKLSCQLYQRSADTFLGVPFNIASYALLTHMVAHVTGLEVGDFVHTLGDAHIYHNHLEQVELQLSRDPRPLPKLNIVRDVSSIESFRFEDFEILGYDPHPHIKGEVSV
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
|
C4L1C9
|
Q1LSZ8
|
FETP_BAUCH
|
Probable Fe(2+)-trafficking protein
|
Candidatus Baumannia
|
MSKNIYCVFLRKQAEGQDFQSYPGELGKHIFNNISKEAWAKWQQKQTMLINENKLNLISNTDRNFLEKEMIKFLFKS
|
Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes.
|
Q1LSZ8
|
Q34800
|
COX1_SYMSY
|
Cytochrome c oxidase polypeptide I
|
Symphalangus
|
MFADRWLFSTNHKDIGTLYLLFGAWAGVLGTALSLLIRAELGQPGNLLGNDHIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASAMVEAGAGTGWTVYPPLAGNYSHPGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTHYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGSDTKWSAAVLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLDQTYAKIHFAIMFVGVNLTFFPQHFLGLSGMPRRYSDYPDAYTTWNILSSVGSFISLTAVMLMIFMIWEAFASKRKILMIEQPSTNLEWLYGCPPPYHTFEEPVYMKP
|
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.
|
Q34800
|
B3QYF4
|
GUAA_CHLT3
|
Glutamine amidotransferase
|
Chloroherpeton
|
MNSVIVLDFGSQYTQLIARRIRELGIYSEILPYHTSAEALRERNPKALILSGGPTSVYDAFAPMPDEKIYELDIPILGICYGLQAIAKHFGGEVAASPKREFGRAQMNIVRQNELAESLLFKNIPDSTVWMSHSDKLTCLPKGFHITAQTANSELCAIEVTEGEGAHRIFGLQFHPEVHHTEFGEKLLSNFLINIAGITPDWSPQSFIDSEIARIKELVGDQTAICAISGGVDSSVAAVLVSRALGDKLHCIFVDNGLLRKNEAEKVQEKLKQLGLNLTTVDASELFLSRLKNVVSPERKRKIIGRTFIKVFEEHIHNEKFLVQGTLYPDVIESVSVKGPSQTIKTHHNVGGLPKRMKLKLIEPLRELFKDEVRKVGKLLDVPDEILTRHPFPGPGLAVRVLGSVSKERLDVLREADAIFIDELKKHDLYLQIWQAFTVLLPVQTVGVMGDNRTYENAVALRAVNSTDGMTADWARLPNDFLAHVSNRIINEVRGINRVTYDISSKPPATIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
B3QYF4
|
Q9UU96
|
GRC3_SCHPO
|
Polynucleotide 5'-hydroxyl-kinase grc3
|
Schizosaccharomyces
|
MVKRQRIESSNVPLSAFAVRQLTLSKAARKKDNSSGKKRSVSEEESQDKYEDEMKTEGEFPSYKHTLVQVVVPGVDHRTKLHSESSKNDSEITPDINRSKVNPQEYSEFSVASPQTISPSLPLNLDDETVSENVPHSPQSSNDAIPVIKITEENSFRVKDTLYVGLHKDQKLAMVGTFIFRSVRGKFQLFGATYSSACMSWFPLNAPLAFATPVFSAIDNALPAMQISEYEEDSLNLRSFAVPSYSPKEHEYELEPKDILPNFETVIAFRENENGLSKIARVLPFAKRLFSFKNLLQDASSISNNFEITPESWCSFSNQLLFSTSKSDYVVPRLMVCGPKGSGKSSFSRYITNRLLQQYRHIAYLDLDPGQPEVVPSGHISLYYINSPLQGPVFARMLFPTYMLRLHLGDISPQKDPDHYIACVTRLFAEYKDYIFNQEISQKEIIPLIINCPGWIRGGGAELLSSIVDICQPTEVVYMSREDMKSSHREKKSIYQHKEYMPDFLSSRDEFQLTLLESTWQYLPDPNVNKVTSADNRMLGLLSYLYFNCNLQRWDFTTSLTACQPIATAFKGSSKGIDAVNIIGEPLNVNDVAKTINGTLMALYACDTASLDNSNTQRIVSSPEGIPLIINDGLPLDPNTSHCLGLIVLRTIDLKRNEFHFVGPLNLELIKDAYAKSLKIVLERGRLELPVYAMLDHRLAQYSELPYLDRNHDRVAVGAHRRRVRRNIIRRSTFVG
|
Polynucleotide 5'-kinase required for both rRNA processing and heterochromatic gene silencing.
|
Q9UU96
|
Q6DGB6
|
CC103_DANRE
|
Protein schmalhans
|
Danio
|
MENSDVINFSCLEKELHSALQADRKYQRENDAKFRALNQKVASYEEFRDIVLASHLKPLDRNDISGSPRKQPWNPVACRTNYVCASSEQVQPQLSEVQPRSASEFIRDWRRFAGCSFEKYSLLVSLGGEALQKIFSTEIGLGLLGEFLLILSQCLKSGDEDRVTGVLDGLSKTGRFSINLSLLSQAEQEACEELFNKLKVAAGECHPYKDNSNTSVVCEAGLTHMEDNKTDITTTLKELAGKYGTEK
|
Dynein-attachment factor required for cilia motility.
|
Q6DGB6
|
Q6B8W7
|
RK6_GRATL
|
50S ribosomal protein L6, chloroplastic
|
Agarophyton tenuistipitatum
|
MSRIGKKPINLPQNINITIIENNVQIQGPKGELSYKIPKLIQIKQDTKNNKLFLYKTEDNKEAQKLHGLCRTLINNMIIGVSQGFEKKLQIQGVGYRSQLDGDNLLLNVGYSHTVIVKPPKNIILEVENNTSITIKGIQKEQVGEIAAQIRRIRPPEPYKGKGIRYLNETINLKVGKSGK
|
Binds 23S rRNA.
|
Q6B8W7
|
Q4R6H1
|
NDUAD_MACFA
|
NADH-ubiquinone oxidoreductase B16.6 subunit
|
Macaca
|
MAVAVCHFRLGPEVWNTASMEMPKVKQDMPPPGGYGPIDYKRNLPRRGLSGYSMLAIGIGTLVYGHWSIMKWNRERRRLQIEDFEARIALMPLFQAETDRRTLQMLRENLEEEAIIMKDVPDWKVGESVFHTTRWVPPLIGELYGLRTTEETIHANYGFMWYT
|
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes.
|
Q4R6H1
|
Q18B40
|
FABH_CLOD6
|
3-oxoacyl-[acyl-carrier-protein] synthase III
|
Clostridioides
|
MNTKAGILGVGSYLPEQSYDNFHFEKIMDTSDEWISTRTGIKERRFAKESEATSDLASKAALKAIECAKLNVEDIELIILATITPDMSLPSTACIVQDAIGAVNATAFDISAACSGFVYGVTIAKQFVETGCYKNVLVIGAETCSKFLNYDDRTTAVLFGDGAGAAVIGPVNEGGILSTHMGSDGKGKDCLKVPAGGSRLKASKETVEANLHTIEMAGSDVFKFAVRKMAETSLRALEKANLNTTDIDYLVPHQANIRIIQASSKRLELDMKKVYVNIDKYGNMSAASIPVALDEAYREGKIKKGDNVVLVGFGGGLTWGASVVKWTL
|
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
|
Q18B40
|
A1TPZ6
|
FOLD_ACIAC
|
Methenyltetrahydrofolate cyclohydrolase
|
Acidovorax
|
MTAQLIDGNALSRQLRADVARRAALLKERGTTPGLAVVLVGDNPASQVYVRNKVKACEESGLHSVLEKYDAAMSEAELLARVDALNNDPSIHGILVQLPLPAHIDAQKVIEAISPAKDVDGFHIASAGALMTGMPGFWPCTPYGCMKMLEHIGYDLRGKHAVVIGRSNIVGKPMALMLLAKDATVTVCHSRTADLKAQTLQADVIVAAVGRRNVLTADMVKPGAVVIDVGMNRNDEGRLCGDVDFDGVREVAGHITPVPGGVGPMTITMLLVNTLEAAERAAG
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
A1TPZ6
|
Q7V0G7
|
LNT_PROMP
|
Apolipoprotein N-acyltransferase
|
Prochlorococcus
|
MINTQNKKFNKYFVPCLGGIFGGIATSTHFWLLFMPLSLFILWSRSDKKLANFLWGFFFILVSHSWLYELHPLTWLGFSWISSLIISISILFGCSIIGGILVYLWGLLVKKILQKKEISNMNSLRLTIKVLLLSFAWGIGEFILSQTPLFWIGLGEGIVPGDLYLAGLARWIGASGLCVVQLTIGFWIYLIYEKWKRKYHFKKTFLFGLLILVILHFLGGLTNPIERNNDYPVALWQTNMPTREKTNFKNQFINDKLISAQKIALSNDAKLLITPEGTLNNNFNLNFKSKIRMLAGGFRNSKNGLRSSLLGYQIGDKTYSSFIDKHRLVPLGEKIPGFLNIFSRGLSAVGGIQPGSDSRFFKWKFTQPLAIAICYEITDGFKIRNAVKSGAELIISAANLDPYPRKLHYQFLSLARVRSIENKKDNIIISNTGPSGLISEEGKIIKLFDPNTEQNDVVNPNFSIEKTFYTTYGERPLFLLCLFLIGLNLYFGKFTN
|
Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
|
Q7V0G7
|
P29386
|
AGL6_ARATH
|
Agamous-like MADS-box protein AGL6
|
Arabidopsis
|
MGRGRVEMKRIENKINRQVTFSKRRNGLLKKAYELSVLCDAEVALIIFSSRGKLYEFGSVGIESTIERYNRCYNCSLSNNKPEETTQSWCQEVTKLKSKYESLVRTNRNLLGEDLGEMGVKELQALERQLEAALTATRQRKTQVMMEEMEDLRKKERQLGDINKQLKIKFETEGHAFKTFQDLWANSAASVAGDPNNSEFPVEPSHPNVLDCNTEPFLQIGFQQHYYVQGEGSSVSKSNVAGETNFVQGWVL
|
Probable transcription factor. Forms a heterodimer via the K-box domain with AG, that could be involved in genes regulation during floral meristem development.
|
P29386
|
A8Q2H5
|
RSSA_BRUMA
|
40S ribosomal protein SA
|
Brugia
|
MSAGLETFALKEEDAIKLLACQTHVGAANCDFQMEQYVWKRRADGIHIIHLRKTWEKLLLAARAIAAIDNPGDVCVVSARPYAQRALLKFAAHTGSTPIFGRFTPGCLTNQIQKQFKEPRLLIVSDPRVDHQAVTEASYVGVPVISFCNTDSPLKFIDIAIPCNNKGVQSIGLMWWLLAREVLLIKGKMTRQTGFVLDDKEIMPDLYFYRNPEEQEKEELAEPREVKEPWPGVPPPEVAKIDEVVRSIGMYQTIGGVEPAKKLDFSMVEPVSDWAQETERAVQLDAAQQQEWGASTQNSNW
|
Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.
|
A8Q2H5
|
P26572
|
MGAT1_HUMAN
|
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
|
Homo
|
MLKKQSAGLVLWGAILFVAWNALLLLFFWTRPAPGRPPSVSALDGDPASLTREVIRLAQDAEVELERQRGLLQQIGDALSSQRGRVPTAAPPAQPRVPVTPAPAVIPILVIACDRSTVRRCLDKLLHYRPSAELFPIIVSQDCGHEETAQAIASYGSAVTHIRQPDLSSIAVPPDHRKFQGYYKIARHYRWALGQVFRQFRFPAAVVVEDDLEVAPDFFEYFRATYPLLKADPSLWCVSAWNDNGKEQMVDASRPELLYRTDFFPGLGWLLLAELWAELEPKWPKAFWDDWMRRPEQRQGRACIRPEISRTMTFGRKGVSHGQFFDQHLKFIKLNQQFVHFTQLDLSYLQREAYDRDFLARVYGAPQLQVEKVRTNDRKELGEVRVQYTGRDSFKAFAKALGVMDDLKSGVPRAGYRGIVTFQFRGRRVHLAPPLTWEGYDPSWN
|
Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
|
P26572
|
Q07UP2
|
MNME_RHOP5
|
tRNA modification GTPase MnmE
|
Rhodopseudomonas
|
MHASDQTIFALSSGRPPSAIAIVRVSGSRGAKIVEALAGRLPTPRMAMRALIKDRDGEPIDDAVVLWFPGPASATGEDVAEFHIHGGRAVLAALMATLSSFENVRAAEPGEFTRRAFEHGKIDLTEAEGLDDLIHADTDRQRRQALRQLNGLLGDRARDWRAQIIEAQALIEAGIDFADEGDVPDDLLAPALAKIEALAGEIEALLAAQGRSERLRDGLVVAIVGPPNVGKSTLMNQLARREVAIVSPHAGTTRDVIEVHLDLDGYPVTVIDTAGIRDSDDPVEQEGVRRAQARAAEADLVLWLLADDQVAAPAAIESDAPVWLVRNKVDLAGAATGVKPAKNLEANLGQNVPQPSFAISAKRGDGIADLVGALGGFAAEFFGAGEAGAITRQRHRDLLRDALVMLQCSKRGRAEELVAEDLRSASRSLGRLLGQVDVEDVLDALFRDFCIGK
|
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
Q07UP2
|
Q30RQ5
|
MDH_SULDN
|
Malate dehydrogenase
|
Sulfurimonas
|
MNQGKRVGIIGAGNVGATVAYSLAMLGSCHEIILRDNKIDVAKGKALDMSQAAAAVRSHTIVSVAEEMADLTNCDVVVVTAGSPRLPGMSRDDLLMINANITKDVIAGVAKYSPDAIIIMVSNPLDAMTYVALKESGFDRSRVIGMAGILDSARMASFIQEKLGYGGGQIRASVMGGHGDDMVPLARYSTVAGVPLTDLMSTSEINEIVIRTRNGGAEIVGHLKTGSAYYAPAKATALMVEAILKDTKQIHPCAVFLEGEYGHSDVVSGVPVMLGANGAEKIIEISLDESEKIMFEGSCNSVRTLIDTLNKNKFFDKGE
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
Q30RQ5
|
Q67FQ3
|
ARHB_XENLA
|
Autosomal recessive hypercholesterolemia protein homolog beta
|
Xenopus
|
MDALKSAGRAIIRSPSIAKQSWGGGKHKKLPENWTDTRETLLEGMLFHLKYLGMTLVEQPKGEELSATAVKRIVATAKASGKKLQKVLLKVSPRGIILYDSASNQLIENVSIYRISYCTADKMHDKVFAYIAQSQQNETLECHAFLCTKRKMAQAVTLTVAQAFKVAFEFWQVSRENKDKREKSGSDGEGASSSQSDGSSSITSLKASASANLLDFEDCTKAFDVLNASDNHIEDLFRQNSTNENNNIVWELDDGLDEAFARLAESRTNPQVLDIGLTANDLQSEECLSPTSWDKLELNPAEADELFMF
|
Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR). Also involved in the vitellogenin receptor mediated endocytosis of nutrients during oogenesis.
|
Q67FQ3
|
Q31FG4
|
HLDD_HYDCU
|
ADP-L-glycero-beta-D-manno-heptose-6-epimerase
|
Hydrogenovibrio
|
MIVVTGGAGFIGSNIVKALNAQGRTDILVVDNLKNGKKFINIADCDIADYLDKEDFQSRIFAEEGLPDIDCVFHEGACSATTEWDGKYMMDNNYEYSKDLLNYCLNRKIPFLYASSAAVYGDGPTFIEERQYEKPLNVYGYSKFQFDQYVRRILPLAESQVAGFRYFNVYGPREQHKGDMASVAFKLHNQVLAGEKLKLFGAYDGYEAGMQTRDFVFIEDVVNVNLWFMENPEQSGIFNLGPAAAEPFKHIADAVIDFHGQGEIEYIPFPDRLKGAYQSFTQADNTRLRDAGYDKPFHTVSEGVQKYLRWLSDNPRVLDFTKK
|
Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
|
Q31FG4
|
P59149
|
RR4_EXSCR
|
30S ribosomal protein S4, chloroplastic
|
Exsertotheca
|
MSRYRGPRVRIIRRLGTLPGLTNKTSQLKSSSINQSISNKKISQYRIRLEEKQKLRFHYGITERQLLNYVRIARKAKGSTGEVLLQLLEMRSDNVIFRLGMAPTIPGARQLVNHRHILVNDCIVDIPSYRCKPQDFITIKNQRKSETMISKNIELYQKSKIPNHLTYSSLEKKGLVNQILDRESIGLKINELLVVEYYSRQA
|
With S5 and S12 plays an important role in translational accuracy.
|
P59149
|
A5D145
|
MURG_PELTS
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
Pelotomaculum
|
MRFLVSGGGTGGHIYPALAIARGLKNRYPGAEILYMGTSNGMEADIVPAEGFPFTGISASGLERKLSPRNLLALWQAVRGFCQAVEIIGRWRPEAVIGTGGYVCGPVVLAAVLKRIPTLIHEQNALPGVTNRILSRFASRVAITFADSLKYFPDQSKVRLTGLPVRPEILQADRKTGLQKLGIKEGRFFLLSFGGSRGARSINGAMLTVIKAFAGNPDVEILHATGKAGYQKFLDGCRAAGIELDKIGNVTVKEYIYNMQDALAAADLVVSRAGAATLAELTALGIPSILVPYPYASENHQEFNARALEKEGAALVILDRQLNGGLLSRTITELINDRARLQAMAAASRKMGKNRALEDIIDCIDELIRSKRRHF
|
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).
|
A5D145
|
A6V8H8
|
ACEK_PSEA7
|
Isocitrate dehydrogenase kinase/phosphatase
|
Pseudomonas
|
MVQSAPASEIAALILRGFDAYREQFREITDGARARFEQAQWQEAQRASAQRINLYEEKVAETVAGLRAGLADSELLDVERWPIIKSAYIAQIDLRLDDELAETWFNSIFCGLFSHDNISDGTMFVHTTRPSLRAHARAPYTRTYRPGGDLRQALEKIFDDYRFDVPYDDRERDLERIDALLHSNLPDWVCKDPDLAIELIGSVFYRNKGAYLVGRLFTPDEQWPLVFPLLHREGHGIQFDTVITDEAEVSIIFSFTRSYFMVDVPVPAELVAFLKRLLPGKHLAELYTSIGFYKQGKSEFYRALINHLATTDDRFVMAPGVRGMVMSVFTLPGFNTVFKIIKDRFNPSKSVDHATVIQKYQLVKNHDRVGRLADTQQFADFRFPVSKFEPECLAELLEVAPSTVVVEGDVVLIRHCWTERRMTPLNIYLENASEAQTREALNDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEICYLTEVNFRYIPEPRFPEDEMSSEPWYSVGPNDVFPEEFPRFLFVDLDQRRLFAKLHGNLYDAKYWQGLQQQIREGKVIDVFPYRRQETPEQLLK
|
Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
|
A6V8H8
|
P71010
|
ALBB_BACSU
|
Antilisterial bacteriocin subtilosin biosynthesis protein AlbB
|
Bacillus
|
MSPAQRRILLYILSFIFVIGAVVYFVKSDYLFTLIFIAIAILFGMRARKADSR
|
Involved in the production of the bacteriocin subtilosin. Required for maximal production and for optimal immunity to subtilosin.
|
P71010
|
B1WRN9
|
CCS1_CROS5
|
Cytochrome c biogenesis protein CcsB
|
Crocosphaera subtropica
|
MTISDSPQTPENLSLPKQGFRQLIKIVADLRLAIVLLLAIALFSISGTVIEQGETISFYQQNYPEDPALFGFLTWKVILILGLNHVYTTWWFLSLLVLFGTSLTTCTFTRQFPALKAARKWNFYQKARQFEKLALSTELAINDLKFVNNLLEQKGYKTFQENQAIYARKGIIGKIGPIVVHAAMLIILGGAIWGALTGFLAQAMVPTGSEFKVNNIIEAGPLSQPQIPKDWGIRVNRFWIDYTPDGTIDQFYSDLSVINNDGEELKHKTIYVNEPLRYHGVTFYQTDWGIAGVQAQVNNSPIFQLPMALLNTNGNGRIWGTWIPTKPDLSEGVSLLAKDLQGTMMVYDQKGDLYSAVRPGMILDINGVRLKIYQLIGSTGLQIKADPGIPFVYTGFGLLMMGVIMSYVSHSQIWVLQEDEHCYIGGKTNRSQVTFERELLGIIESLEPEKT
|
Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
|
B1WRN9
|
B7GYL4
|
MINC_ACIB3
|
Probable septum site-determining protein MinC
|
Acinetobacter calcoaceticus/baumannii complex
|
MADIRITGRMVNFSRITFDTNDHDVIRQQLSNILNEGSYQGTVVIIDSTVEQELIALIQLLVSLGLQPMAVIDGILGDEARAIQFPVLPADQPLQRIKPTAEQVAIVEKPSSAQASVETKKPLNNNAVAHITSYHDEILRTGQSLVQDQGDIILKAAMNSGSEVIASGNIHIYGTVRGRVIAGAGGHAAARIFCQSLEAELVSIAGTYCVADDIPKHVVKKPVHIYLNEKQELEFEALEL
|
Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.
|
B7GYL4
|
A5DBJ8
|
LOC1_PICGU
|
60S ribosomal subunit assembly/export protein LOC1
|
Meyerozyma
|
MATRQSKTAKRNKTQNQKRNVESEVFTDSAARNLLENQPKLTPKSKVKKPSKLAVKKQQAKVRLYGAKNGREYKESELQIPVLNKAVVPGVKAKKGKKGKVFVDDNDNLTMERLVKSINDKYDKVNESKLEKSRRLEEIREVKRREMEKKEEQKKNKLDDKKKELKNKASVARANRRKNAKEAAKEAESDEPRKKKVSFA
|
Required for efficient assembly and nuclear export of the 60S ribosomal subunit.
|
A5DBJ8
|
Q6FYM0
|
ATPD_BARQU
|
F-type ATPase subunit delta
|
Bartonella
|
MSDSFALIPLPLVDQRYAQALFDFVQEARSVENVEKAVASFLVVLDQHEDLKRFVQSPFFSIKEQIKVMRSVCENIKFADQGAGQILSNFLRVITVNRRLCALSGILQAFQHRVALSRREVSAQIISARPLSSHQEEELRVALEGVVRGKVLLHMCVDPTILGGLIIRLGSSQIDTSLVTKLSSLKLALKKEVS
|
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.
|
Q6FYM0
|
P75052
|
TYPH_MYCPN
|
TdRPase
|
Mycoplasma
|
MNIVNLISKKQRGKALTETEINWFVHSVNNKSLADYQVSAFLMAVWFQGMNSKELFCLTKAMVKSGESLHFNHHSKLSVDKHSTGGIGDKVSIALIPILTALDYSVAKLSGRGLGYTGGTIDKLEAVGVKTDFTPTEAQNLLDQNDCFIIGQSEGIAPVDKVLYALRDTTATVDSLPLIASSVMSKKLAINNDYIFIDLKYGKGAFCKTKTMAKELAQYMYSIAKQFKRKLYIKLSDMNQVLGKTIGNALEVLEVVHFLKRNWTEVGADFIQLMEQIVTEILIETKRAPNKRAAVALYHATLEGEKPWQRFLKFIELQGSSWERFLDLKELFNPQYKAPVLASQSGTLSYTSPVDLAMVSISLGAGRMVKTDLIDPMAGIKLVKQANEVVKAGDTVLELYSSKPITPAHIEAAQHTIIIKQ
|
The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis.
|
P75052
|
Q74CB9
|
PYRDB_GEOSL
| null |
Geobacter
|
MQKPDLSVEIAGITLRNPVMTASGTFGYGEEFSEYVNLEAIGAIITKGLSLKPKAGNPTPRIVETTGGMLNAIGLQNVGIDAFVEKKVPFLRTVATPVIVNFFGNTLEEYAELAERLDLIPEVAAVEINISCPNVKHGGIVFGTDPKAAYSVVKAVREATIKPVIVKLSPNVTDIVEMAWACADAEADALSLINTLTGMAIDLDKRRPILANVTGGLSGPAVKPIALRMVWQVARAVKIPVIGIGGIMTGIDALEFMLAGATAVQVGTANFLDPGAAGRIAAEMERYLADNGIADVKEMIGALEV
|
Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
|
Q74CB9
|
Q9LPK6
|
AEE9_ARATH
|
AMP-binding protein 9
|
Arabidopsis
|
MELLLPHPSNSTPLTVLGFLDRAASVYGDCPSILHTTNTVHTWSETHNRCLRIASALTSSSLGINRGQVVSVVGPNVPSVYELQFAVPMSGAILNNINPRLDAHALSVLLRHSESKLVFVDPNSISVVLEAVSFMRQNEKPHLVLLDDDQEDGSLSPSAASDFLDTYQGVMERGDSRFKWIRPQTEWQPMILNYTSGTTSSPKGVVLSHRAIFMLTVSSLLDWHFPNRPVYLWTLPMFHANGWGYTWGTAAVGATNVCTRRVDAPTIYDLIDKHHVTHMCAAPMVLNMLTNYPSRKPLKNPVQVMTAGAPPPAAIISRAETLGFNVGHGYGLTETGGPVVSCAWKAEWDHLDPLERARLKSRQGVRTIGFAEVDVRDPRTGKSVEHDGVSVGEIVLKGGSVMLGYYKDPEGTAACMREDGWFYSGDVGVIHEDGYLEVKDRSKDVIICGGENISSAEVETVLYTNPVVKEAAVVAKPDKMWGETPCAFVSLKYDSNGNGLVTEREIREFCKTRLPKYMVPRKVIFQEELPKTSTGKIQKFLLRQMAKSLP
|
May act as an acid--thiol ligase that activates carboxylic acids by forming acyl-CoAs.
|
Q9LPK6
|
D2Y2D6
|
H2A14_CYRHA
|
Peptide F8-20.15
|
Haplopelma
|
MKVTLIAIPTCAAVLVLHTTAAEELEESQLMEVGMPDTELAAVDEERLFECSVSCEIEKEGNKDCKKKKCKGGWKCKFNMCVKV
|
Postsynaptic neurotoxin.
|
D2Y2D6
|
Q9H6Q3
|
SLAP2_HUMAN
|
Src-like adapter protein 2
|
Homo
|
MGSLPSRRKSLPSPSLSSSVQGQGPVTMEAERSKATAVALGSFPAGGPAELSLRLGEPLTIVSEDGDWWTVLSEVSGREYNIPSVHVAKVSHGWLYEGLSREKAEELLLLPGNPGGAFLIRESQTRRGSYSLSVRLSRPASWDRIRHYRIHCLDNGWLYISPRLTFPSLQALVDHYSELADDICCLLKEPCVLQRAGPLPGKDIPLPVTVQRTPLNWKELDSSLLFSEAATGEESLLSEGLRESLSFYISLNDEAVSLDDA
|
Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins.
|
Q9H6Q3
|
Q0P8W4
|
PSEB_CAMJE
|
UDP-GlcNAc-inverting 4,6-dehydratase
|
Campylobacter
|
MFNKKNILITGGTGSFGKTYTKVLLENYKPNKIIIYSRDELKQFEMASVFNAPCMRYFIGDVRDKERLSAAMRDVDFVIHAAAMKHVPIAEYNPMECIKTNIHGAQNVIDACFENGVKKCIALSTDKACNPVNLYGATKLASDKLFVAANNIAGNKQTRFGVTRYGNVVGSRGSVVPFFKKLISEGAKELPITDTRMTRFWISLEDGVKFVLSNFERMHGGEIFIPKIPSMKITDLAHALAPNLSHKIIGIRAGEKLHEIMISSDDSHLTYEFENYYAISPSIKFVDKDNDFSINALGEKGQKVKDGFSYSSDNNPLWASEKELLEIINHTEGF
|
Catalyzes the first step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Has both C6 dehydratase and C5 epimerase activities that result in the production of both UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose.
|
Q0P8W4
|
Q47F76
|
PSRP_DECAR
|
Pyruvate, water dikinase regulatory protein
|
Dechloromonas
|
MPTTIKRTVFFVSDGTGLTVEALGHSLMTQFEDIEFKQIRIPFLTSVEQAQEAVARINGQGESDGMRPIVFTTLVNPELSSIVHQADAFCLSYFDTFLAPLEAELGIKSNHTVGRSHGSAESSEYKKRIESINYTLAHDDGITDRDLEEADVILVAVSRCGKTPTSLYLAMQFGLKAANFPLIPEDFDRGRLPGTLEKHRSKLFGLTIQPERLHQIREERRAASNYASLANCRFEIAEAEKMMRREGIRWLDSSTKSIEEISTTILQELKLR
|
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
|
Q47F76
|
Q754Q2
|
ACH1_ASHGO
|
Acetyl-CoA deacylase
|
Eremothecium
|
MTVSQLLKQRVRYAPYLSKVRRAEELLPLFKHGQYIGWSGFTGVGAPKVIPTALADHVEKNGLQGQLAFNLFVGASAGPEENRWADLDMILRRAPHQVGKPIARAINDGRIKFFDKHLSMFPQDLTYGYYTRERTDGKILDYAIVEATAIKEDGSIVLGPSVGGSPEFMSAADKLIVEVNTATPSFEGLHDIDMPVLPPHRVPYPYTRVDERSGLDAVPVDPARVVALVESTERDKVGPNTPSDEGSRAIAGHLVEFFENEVRHGRLPANLLPLQSGIGNIANAVIEGLAGASFRNLTVWTEVLQDSFLDLFENGSLEFATATSIRLTEAGFEKFFANWDEYSSKLCLRSQVVSNSPEMIRRLGVIAMNTPVEVDIYAHANSTNVSGSRMLNGLGGSADFLRNAKLSIMHAPSARPSKTDPTGISTIVPMASHVDQTEHDLDVLVTDQGLADLRGLCPRERAREIIRQCAHPDYKPILTDYLDRAEHYAQRSRSMHEPHILQQALRFHTHLAEKGTMKVPSWD
|
Presumably involved in regulating the intracellular acetyl-CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation.
|
Q754Q2
|
Q49UQ2
|
RS18_STAS1
|
30S ribosomal protein S18
|
Staphylococcus
|
MAGGPRRGGRRRKKVCYFTANGITHIDYKDTELLKRFISERGKILPRRVTGTSAKYQRMLTLAIKRSRHMALLPYVKEEQ
|
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
|
Q49UQ2
|
Q755A2
|
KXD1_ASHGO
|
KxDL homolog
|
Eremothecium
|
MSDDVDSETRSRTPSISSRQFIIPEDELATLDSENSSLDSGGEEASSGGSDAYSAAGGSTPVFSRLGQHPSTFFTGSQVAPIFDTSLYLFESLTQSLDSVDFSEALSLQTKTSATINSKSRELQLLVGEVQTHLRRLQTAFEQGQHTAQRVRHNLRDITRGVESLKQTFARSYPIEYHQALERAYERRAE
|
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in endosomal cargo sorting.
|
Q755A2
|
P51563
|
TCR7_VIBAN
|
Tetracycline resistance protein, class G
|
Vibrio
|
MRSSAIIALLIVGLDAMGLGLIMPVLPTLLRELVPAEQVAGHYGALLSLYALMQVVFAPMLGQLSDSYGRRPVLLASLAGAAVDYTIMASAPVLWVLYIGRLVSGVTGATGAVAASTIADSTGEGSRARWFGYMGACYGAGMIAGPALGGMLGGISAHAPFIAAALLNGFAFLLACIFLKETHHSHGGTGKPVRIKPFVLLRLDDALRGLGALFAVFFIIQLIGQVPAALWVIYGEDRFQWNTATVGLSLAAFGATHAIFQAFVTGPLSSRLGERRTLLFGMAADGTGFVLLAFATQGWMVFPILLLLAAGGVGMPALQAMLSNNVSSNKQGALQGTLTSLTNLSSIAGPLGFTALYSATAGAWNGWVWIVGAILYLICLPILRRPFATSLVI
|
Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.
|
P51563
|
Q1GBK5
|
RS14Z_LACDA
|
30S ribosomal protein S14 type Z
|
Lactobacillus
|
MAKTSQKVRNHRPAKFSSREYTRCERCGRPHSVYRKFGLCRICLKELGHKGQIPGLKKASW
|
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
|
Q1GBK5
|
A0QJL0
|
DNLI_MYCA1
|
Polydeoxyribonucleotide synthase [ATP]
|
Mycobacterium avium complex (MAC)
|
MSPSHAKLATVLLFDVATASADVGGTPSRLTKVARIADLLRRAAPDAALVAIVVSWLSGELRQRQIGVGWAALRSRPPAAAHPTLTVVAVDAAFAEIGAVAGKGAQARRAALLNALFAAATETEQTFLLRLLGGELRQGALAGIMADAVARAAGIPAAAVQRAAMLGGDLPAVAAAALSGEAAALSGEASALDAFTLRVGRPVAPMLAQTAAGVAEAIERHGGQAIFEAKLDGARVQIHRAGDQVTVYTRSLDDVTARLPEVVTATLALPVEALIADGEAIALRPDNSPQRFQVTASRFGRSVDVAAAVAAQPLSVFFFDILHCDGVDLLDAPTTDRLAALDALVPPAQRVDQLLTADPDAAGRFLEATLAAGHEGVMAKAPGAPYQAGRRGAGWLKVKPVHTLDLVVLAVEWGSGRRRGKLSNIHLGARDPATGEFVMVGKTFKGMTDAMLDWQTARFTELAVGGTDGYVVRVRPEQVVEVAVDGVQKSSRYPGGLALRFARVLRYRDDKGPAEADTIDAVRALY
|
DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
|
A0QJL0
|
B2UVE0
|
FABZ_HELPS
|
Beta-hydroxyacyl-ACP dehydratase
|
Helicobacter
|
MEQNHQNLQSQFFIEHILQILPHRYPMLLIDRVVELEANKKIVAYKNITFNEDVFNGHFPDKPIFPGVLIVEGMAQTGGFLAFTSLWGFDPEIAKTKIVYFMTIDKVKFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMIAERD
|
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
|
B2UVE0
|
Q3AQ12
|
ACP_CHLCH
|
Acyl carrier protein
|
Chlorobium
|
MTAAEIKDKVFDIIVSRMGVNKDQIKMESKFSDDLGADSLDTVELIMELENAFDVQIPDEDAEKIATVQQAVDYIVSKQ
|
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
|
Q3AQ12
|
A8F4Q8
|
EFG_PSELT
|
Elongation factor G
|
Pseudothermotoga
|
MLEIEALYVPLSKLRNIGIMAHIDAGKTTTTERILYYTGRKHVLGSVDEGTATMDWMEQEKERGITIKAAATTCFWKEHRINIIDTPGHVDFTVEVERALRVLDGAVAVFDATAGVEPQSETVWRQAERYSVPRIAFMNKMDKTGADFFMSIKSMVEKLHAKPVAIQVPIGAEKDFIGVVDLIEMKAITWTSEDGSEFIKHEIPENMLDLAEEMREEMISMLAEEDEELLELYLEEQELPVEKIKDILRKATINNKLVPVLCGAAARNKGIQPLLDAVVDYLPSPIDIPAVKAITPSGEEIQIPPSVEGDFAGLAFKIQTDPYVGKLAYVRVYSGKLEKGSYVYNSTKQIRERVARLIFMHADKREDAEYARAGDIVAIIGLKNTTTGDTLCSQERPVLLEKMSFPEPVISIAIEPLTRDDEERMVKAVAALSEEDPTLRINVDRETGQVVLSGMGELHLEIVTDRLKREFGVNVRVGRPQVSYRETIRQTGTAEGKYVRQTGGRGQYGHVIMKFEPLPLDGEKQFEFINKTVGGVIPREYIPAIEEGVKEAMEMGVLAGYPMIGVRAVLLDGSYHEVDSSEIAFKVAASLAFKNAMKICQPVLLEPVMKLEVVVPEEYVGGIIADLNARRAQIESLESRINLRVIKAFVPLSELFGYATTLRSLSQGRAVHVAQFSHYKEAPDKVVEKVLKVV
|
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
|
A8F4Q8
|
Q2FZL3
|
SSPB_STAA8
|
Staphylopain B
|
Staphylococcus
|
MNSSCKSRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLPGNVKEKESAKTVSAKLKQELKNTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCATFPNQMIEYGKSQGRDIHYQEGVPSYEQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVGNAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY
|
Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S.aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin.
|
Q2FZL3
|
B0SCK5
|
LPXD_LEPBA
|
UDP-3-O-acylglucosamine N-acyltransferase
|
Leptospira
|
MTQIKLSTLQTLLPDATFQNSETLKDINFSGLTSLTLAGPSDISFVASKTFVNEAKASKASLLVVSQETAEALSDKAIIIVSKVELTTAKIIRLFFPEKQPSGKRSAQVAIDPSAKIGSNTDIGHFVTIGKDSIIGNDCIIEDGVKIGDRVQIGDGARIGKNCVFFDDTIVGKRFIAFGNSTFGGDGFGFVYAEGKHNKIPQVGRVVIGDDVEVGSNCTIDRGALTDTTIGNGCKFDNMVHVAHNCKVGDHVIIAGQSGLAGSVTLGNNVIIGGACAISDHLTLVDGTIIAGGSSLRTSPKTKDVYVGWDLGLTFPEFQKYRVNIKNIVNLNKWLKRIENIEKKVGIETKES
|
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
B0SCK5
|
A8MLM7
|
SPED_ALKOO
|
S-adenosylmethionine decarboxylase alpha chain
|
Alkaliphilus
|
MLGLEKKLTLYGFNNLTKTLSFNIYDVCYAKSEKAQKAYIEYIDEQYNSERLTKILCDVTEMIGAHVLNISKQDYEPQGASVNILITEEALPLHLIDESCNKGEGIAAQRDTIHAHLDKSHVTVHTYPEYHPDNAISTFRVDIDVSTCGMISPLNALDYLIGSFDSDIITIDYRVRGFTRDVEGKKFYIDHNITSIQDYIDDETLKKYDAIDVNVYQSNIFHTKMLIKEIELQNYLFNKDVNELLPKQRLEITNNLRKEMIEIFSGMNIY
|
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
|
A8MLM7
|
C3N5U6
|
RL18_SULIA
|
50S ribosomal protein L18
|
Sulfolobus
|
MANGPNYKIKPRRRREGKTNYYKRYVYVISKQIRFIVRITNKYVIVQIAKIDPKGDIMVASAHSSELTKKFEWKGDENNTPSAYLTGYLAALRAVKKGVTECVADIGLHVPSKGNKVFYAIKGAIDAGLKIPIGDISIENDRIKGEHIAKYAEKLKSENLDLYNKLFSRYLGRGLNPENLPSHFEEILNKIKSSGG
|
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.
|
C3N5U6
|
B1J143
|
LIPB_PSEPW
|
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
|
Pseudomonas
|
MSLCLGFRELGLQPYEPVLEAMRRFTEQRSPDSQDEIWLVEHPAVFTQGQAGKAEHLLVPGDIPVVQTDRGGQVTYHGPGQLVAYLLLDVRRLGFGVRELVSRIEQTLIELLASYGVSAAAKPDAPGVYVDGAKIASLGLRIRNGRSFHGLALNVDMDLAPFRRINPCGYAGLAMTQLRDLAGPIELDEVRTRLRGQLVKHLDYAEQTTLTGGID
|
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.
|
B1J143
|
P53608
|
ARGI_BACCD
|
Arginase
|
Geobacillus thermoleovorans group
|
MKPISIIGVPMDLGQTRRGVDMGPSAMRYAGVIERLERLHYDIEDLGDIPIGKAERLHEQGDSRLRNLKAVAEANEKLAAAVDQVVQRGRFPLVLGGDHSIAIGTLAGVAKHYERLGVIWYDAHGDVNTAETSPSGNIHGMPLAASLGFGHPALTQIGGYSPKIKPEHVVLIGVRSLDEGEKKFIREKGIKIYTMHEVDRLGMTRVMEETIAYLKERTDGVHLSLDLDGLDPSDAPGVGTPVIGGLTYRESHLAMEMLAEAQIITSAEFVEVNPILDERNKTASVAVALMGSLFGEKLM
|
Controls arginine catabolism.
|
P53608
|
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