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Full Name
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taxon
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sequence
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2.75k
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5.51k
AlphaFoldDB
stringlengths
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10
Q3B6G3
EFTU_CHLL3
Elongation factor Tu
Pelodictyon
MAKESYKRDKPHVNIGTIGHVDHGKTTLTAAITSVLSKKGFAESRAFGDIDKAPEERERGITISTAHVEYQTEKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVAGTDGPMPQTREHILLARQVNVPALVVFLNKVDIADPELLELVEMELRELLTEYGFPGDDIPIIKGSALKALEGDPEGEKAILELMDAVDNYIPEPVRDVDKPFLMPVEDVFSISGRGTVGTGRIERGRIKINEEVEIVGIKDTRKSVVTGIEMFQKLLDEGQAGDNAGLLLRGVDKTELERGMVIAKPGTIKPHTKFKAEVYILKKEEGGRHTPFFTNYRPQFYFRTTDVTGAVTLPEGVEMVMPGDNLSVDVELIAPIAMDEGLRFAIREGGRTVGAGSVTKISE
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Q3B6G3
B3PPU4
RECA_RHIE6
Recombinase A
Rhizobium
MSQNSLRLVEDKSVDKSKALEAALSQIERSFGKGSIMKLGSNENVIEIETISTGSLGLDIALGVGGLPKGRIIEIYGPESSGKTTLALQTIAESQKKGGICAFVDAEHALDPVYARKLGVDLQNLLISQPDTGEQALEITDTLVRSGAVDVLVVDSVAALTPRAEIEGEMGDSLPGLQARLMSQALRKLTASISKSNTMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGSVKEREEVIGNQTRVKVVKNKMAPPFKQVEFDIMYGEGVSKTGELVDLGVKAGIVEKSGAWFSYNSQRLGQGRENAKTFLRDNPDLAREIELALRQNAGLIADRFLQNGGPDADDGDAAADM
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.
B3PPU4
Q8N5M9
JAGN1_HUMAN
Protein jagunal homolog 1
Homo
MASRAGPRAAGTDGSDFQHRERVAMHYQMSVTLKYEIKKLIYVHLVIWLLLVAKMSVGHLRLLSHDQVAMPYQWEYPYLLSILPSLLGLLSFPRNNISYLVLSMISMGLFSIAPLIYGSMEMFPAAQQLYRHGKAYRFLFGFSAVSIMYLVLVLAVQVHAWQLYYSKKLLDSWFTSTQEKKHK
Endoplasmic reticulum transmembrane protein involved in vesicle-mediated transport, which is required for neutrophil function. Required for vesicle-mediated transport; it is however unclear whether it is involved in early secretory pathway or intracellular protein transport. Acts as a regulator of neutrophil function, probably via its role in vesicle-mediated transport: required for defense against fungal pathogens and for granulocyte colony-stimulating factor (GM-CSF) signaling pathway; possibly by regulating glycosylation and/or targeting of proteins contributing to the viability and migration of neutrophils.
Q8N5M9
Q17Z49
PYRE_HELAH
Orotate phosphoribosyltransferase
Helicobacter
MDVKACYQNAKALLEGHFLLSSGFHSNYYLQSAKVLENPKLAEQLALELAKQIQNARLNIECVCSPAIGGILAGYELARALGVRFIFTERVNGVMALRRGFEVKPNEKILVCEDIITTGKSAMECAKVLEEKGAHIVAFAALANRGICKRTHSSLKAQEDACLPSELPLFALEDFVFDMHEPKHCPLCTTSVAIKPGSRGN
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Q17Z49
P0A2B8
RMUC_SALTI
DNA recombination protein RmuC
Salmonella
MDITLMISAVVALAAGAVIGWLATKAHADQIRADLIEERRELDIELSAARQQLAQEAHWRSECELLNNELRSLHSINTSLEADLREVTTRLEATQQHAEDKIRQMINSEQRLSEQFENLANRIFEHSNRRVDEQNRQSLNSLLTPLREQLDGFRRQVQESFGKEAQERHTLAHEIRNLQQLNAQMAQEAINLTRALKGDNKAQGNWGEVVLARVLEASGLREGYEYETQVSIENDARSRMQPDVIVRLPQGKDVVIDAKMTLVAYERYFNAEDDYTREAALQEHIASVRNHIRLLGRKDYQQLPGLRSLDYVLMFIPVEPAFLLALDKQPELITEALKNNIMLVSPTTLLVALRTIANLWRYEHQSRNAQHIADRASKLYDKMRLFVDDMSAIGQSLDKAQDNYRQAMKKLASGRGNVLAQAEAFRGLGVEIKREINPDLAEQAVTQDEEYRLRSIPEGRQDEHYPNDERVKQQLS
Involved in DNA recombination.
P0A2B8
B6V866
MCPB_TRITO
Carboxypeptidase MCPB
Trichophyton
MVAYRFLTLISLGLGSHCASALQYGYNQVSTHKDSAVVAGAFPAINGTHLQSPAFTSPGTVPRGFSDGTSGPTRDETMEGFMRRLARSNSWMTYHKADFKSEEGRKFPYMYLSASKSSIEKPSSHKLRVWLQGGVHGNEPAGDQSMLALLGDLAANQKWAAKLLEKMDILVLPRYNPDGVFYFQRYLATNFDPNRDHIKLARQQTRDIKELFARFSPHIATDMHEFTAGRAFGPKKDIIYAADALFSSAKNLNIDEGIRQLSEKLFAKRMGKDIEAAGLRWDPYIIQGESSSSKLLLREAGTDAKIGRNAMGLSQCVVFLCETRGIGIADQHFERRTLSGLVMVKSILQTAVDNFDEVYNTIERGIRRFTNSRNDIVLTDRSPIMERTFGMLNTTDATLFDYPIDFATTTPAQAVLTRSRPRAYLIPPSWPDIVKRLEVFGVKADKLPHSYVGPVEALNVTSVTFDKEYYEGVVTTTVETKLVERNIRLPAGSYLVKTNQKNAALAFVALEPENIDSFASFGVIPVSTGDQYPIFRVE
Extracellular metalloprotease that contributes to pathogenicity.
B6V866
Q1LNF7
EFTS_CUPMC
Elongation factor Ts
Cupriavidus
MAAITASMVAELRAKTDAPMMECKKALTEADGDLGKAEELLRVKLGNKASKAASRVTAEGIVVSYIDGTTGALVELNCETDFVSKNDDFLGFGAKVAELVAKQNPADVAVLSALEMDGSTVDAVRSALIGKIGENMTIRRFVRYTNGGKLVSYLHGTRIGVMVEFDGDEAAAKDVAMHVAAMKPVSLSADQVPAELIAKERSIAEQKAAESGKPAEIVAKMVEGSVQKYLKEVSLLNQSFVKNDKQTVEQMLKGVNTTVKGFTLYVVGEGIEKKQDDFAAEVAAQVAAAQKA
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Q1LNF7
B0SXC3
SYY_CAUSK
Tyrosyl-tRNA synthetase
unclassified Caulobacter
MSAAASFKSEFLQTLQARGYIHQITHPDELDAAAAGGIVTAYIGFDATAPSLHVGSLIQIMMLRRLQQAGHKPIVLMGGGTTKVGDPTGKDESRKLLSDADIAANIAGIKQVFAKFLTFGDGPTDAIMVDNDVWLSKFGYVQFLRDYGVHFTVNRMLAFDSVKLRLEREQPMTFLEFNYMLMQAVDFLELNRAHGCVLQMGGSDQWGNILNGVELTRRVDHKAAFGLTTPLLATASGAKMGKTMSGAVWLNAEQLSPYDYWQFWRNTEDADVGRFLKLFTDLPLDEIARLEALPGAQINDAKKVLADEATRMAHGEDEARKARDAAEKAFEQGALSADLPTFEIAAAELKAGIVLANLFADAGLAASRGEARRLAQGGGVKVNDKAEPDANRVVTEADLVEGVVKLAAGKKKIVLVKPI
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
B0SXC3
A1U1Q6
MASZ_MARN8
Malate synthase G
Marinobacter
MTERVQVGGIQIAKNLYDFVNNEAIPGTGIEADKFWAEFDKIVNELAPRNRELLLKRDEIQEKMDTWNREHKGQKLDMAEYKAFLKDIGYLVDEPADFKISTSNVDPEIATMAGPQLVVPVMNARFALNAANARWGSLYDALYGTDAISEENGAEKGRGYNPVRGAKVIEWARNLLDGSAPLASGSHKDAAKYYIDGGKLAVKLQNGDVTGLKDESGFVGYTGAADAPTGVLLVKNGMHFEIQIDASHPIGKDDGAHVKDVLMESALTTIMDCEDSVAAVDADDKVVAYKNWLGLMKGDLEESFEKGGQMMTRRMNGDRTYTGADGSELTLKGRSLLFVRNVGHLMTNPAILLKDGSEIPEGLMDGLVTSLIAIHDLKGDGKFQNSTKGSVYIVKPKQHGPEEVAFTNEFFGRVEDALGLPRFTLKVGIMDEERRTTVNLKACIHAAKERTVFINTGFLDRTGDEIHTSMELGPFIRKGPMKQAAWINAYEQWNVDIGLEAGLSGVAQIGKGMWAMPDLMAGMLEAKIGHPKAGANTAWVPSPTAATLHATHYHQVNVFDVQKELANRQRASLDDILTVPVMEDPSSLSAEDIQQELDNNAQGILGYVVRWIDQGVGCSKVPDINDVGLMEDRATLRISSQLLTNWLYHGICSEEQIMETMKRMAAVVDKQNAGDAAYRNMAPNFDDSIAFQAAVDLVLKGREQPAGYTEPLLHAYRQKAKAKYGQ
Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
A1U1Q6
A0E3W6
NNRE_PARTE
NAD(P)HX epimerase
Paramecium
MQQLNKISYLNQIQSQQFDVELMSEEVGFTLDQLMELAGQSIANTVVQLNKEGKSYNKILVLCGPGNNGGDGIVSARHLKQFGLQPEIALFREVKNPFFNRLLNQCKYNLIPIHYELQDLEKYDLLIDAILGFSFKPPLREPYDKPIQQLKTTKTPILSVDIPSGWDVEQGNAQDFFTPQYLISLTLPKLGVKSFKGRHFIGGRFIPLKLQEKYNFIVPEYQGSDTILELSNL
Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
A0E3W6
Q58141
ISF1_METJA
MCJ-1
Methanocaldococcus
MKVFGISGSPRLQGTHFAVNYALNYLKEKGAEVRYFSVSRKKINFCLHCDYCIKKKEGCIHKDDMEEVYENLIWADGVIIGTPVYQGNVTGQLKTLMDRCRAILAKNPKVLRGRVGMAIAVGGDRNGGQEIALRTIHDFFIINEMIPVGGGSFGANLGATFWSKDRGKKGVEEDEEGLRVLRKTLNRFYEVLKEKRGL
Redox-active protein probably involved in electron transport.
Q58141
Q7WFN9
SYP_BORBR
Prolyl-tRNA synthetase
Bordetella
MRASKYHLNTLKEAPAEAEIASHQLMTRAGMIRKLAGGIYTYMPLGLKVIRKIEGIVREEMNAAGAIELLMPVVQPAELWMESGRWEQYGAELLRIKDRHQRDFVLQPTSEEVITDIARNEIQSYRQLPLNFYHIQTKFRDERRPRFGLMRGREFTMKDAYSFDRDEAGAQRSYDIMYAAYQRIFQRLGLEFRAVAADTGSIGGSRSHEFQVIADTGEDLIVYNPESDYAANIELAEAPALLATRAAPGQDLEAVPTPGAAKCEDVAKLLDLPLARTIKSIVLAVDQPEGPAQVWLLLLRGDHELNEIKAGKLPGLAGFRFATETEILDHFGCKPGYLGPIKTARPVHVVADRTVANMADFVCGANREDYHYQGANWARDLPEPELVADLRNVVEGDPSPDGKGALSIQRGIEVGHVFFLGTKYSEALKATFLDDNGKPAVLQMGCYGIGVTRIVGAAIEQNHDARGIIWPRAIAPYEVVICPVGWGKSETVRDTALALYEALRARGVDVMLDDRDSRPGVMFAEWELIGVPLRVTVGERGLNEGVVELQARREAEAAKVPVDQALAQTLAKLDLL
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Q7WFN9
Q12084
DAS2_YEAST
Regulator of rDNA transcription 3
Saccharomyces
MDRKAVEEKRIVISIGGGHATGVGAIALDLQNTFKSLYNSINIRVINLDNMIEGNIKSYNNNDYDFDNILNLVYEKHAVTSQNDMIQHDYEDPIDLIIVCGCYALYDKRINEISQLKVFLDSDADKRLISLIKKKNVGSNEQLAQLITEYMDHLRPEMQQYIEPTRTFADLIIPSTNENLGRAVLVDGIVKAIEDTKSQIEGNNTNNKIRPRLWDFEAETMDLEKDRYYDLS
Putative uridine kinase identified in a screen for mutants with increased levels of rDNA transcription.
Q12084
Q8WVK2
SNR27_HUMAN
U4/U6.U5 tri-snRNP-associated protein 3
Homo
MGRSRSRSPRRERRRSRSTSRERERRRRERSRSRERDRRRSRSRSPHRRRSRSPRRHRSTSPSPSRLKERRDEEKKETKETKSKERQITEEDLEGKTEEEIEMMKLMGFASFDSTKGKKVDGSVNAYAINVSQKRKYRQYMNRKGGFNRPLDFIA
May play a role in mRNA splicing.
Q8WVK2
Q1DCA3
GATA_MYXXD
Glutamyl-tRNA(Gln) amidotransferase subunit A
Myxococcus
MQLTDLTMLELAAKLAAGEASSEEATRASLARIQQVDPKVRAFLRVDEAGALAAARASDARRKSGSPASALDGVPLGLKDIFLTEGVETTAGSRILEGFVPPYDATVVRLLKEAGLPLVGKLNMDEFAMGSSNESSAFFPSHNPWDVSRTPGGSSGGSAAAVAAREVFGALGTDTGGSIRQPAALTNTVGLKPTYGRVSRFGVIAFASSLDQPGPMTRTVADAAALLQVIARPDAQDATSADAPVPDYSADLEAGVRGLKLGVPREYFTEGMDPEVEAAVREALREYERLGATLVDVSLPHTKYALATYYLIAPAEASSNLARYDGVRFGLRAKDARSLRDVYALTREQGFGAEVKRRIMLGTFALSSGYYDAHYLRAQKVRTLIREDFTRAFQQVDALLSPTSPVPAFKLGEKVEDPLSMYLMDIYTLPCNLAGLPGLSVPCGFTKAGLPVGLQILGRPFDEAGLLRIARAYEREHDFFRRSAPL
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).
Q1DCA3
B0BN28
SKA1_RAT
Spindle and kinetochore-associated protein 1
Rattus
MASDLEQLCSYVNEKIENIKKILSLRKLGQDPTLKTTLSKIGDEIITVNELLNQFELEIQYQEQTNSSLKELCKSLEEEFKDVEHLKEHIPSHLPQVTVTQSSTHKPDLDPKESVKAEEPVLPKKPPKEQRVIKEMHFITTDEFSGVPAYMKSRLTYCQINDVIKEINKAVVSKYKIIHQPKASMSSVKRNLYQRFINEETKDTKGRHFIVEADIKEFTTLKVDKKFHVIMNILRHCQRLSEVRGGGLTRYVIT
Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. Affinity for microtubules is synergistically enhanced in the presence of the ndc-80 complex and may allow the ndc-80 complex to track depolymerizing microtubules. In the complex, it mediates the interaction with microtubules.
B0BN28
Q39FQ7
RLMN_BURL3
tRNA m2A37 methyltransferase
Burkholderia cepacia complex
MTSETTVNLLDFDAEGLVAYCGSLGEKPFRAKQLQRWIHQYNAGDFDGMTDLAKSLREKLKGRASIGMPEIASDHVSTDGTRKWLIDVGNGNAVETVFIPEETRGTLCVSSQAGCAVNCRFCSTGKQGFSRNLSTAEIIGQLRMAEFALRASLGRAPGPNGKAERVVTNVVMMGMGEPLLNYSAVVPAMRLMLDDNAYGLSRRRVTLSTSGVVPMMDRLGAELPVALAVSLHAPNDPLRDELVPLNKKYPLRELMAACQRYLKVAPRDFITFEYCMLDGVNDTEAHARELLAVTRDVPCKFNLIPFNPFPESGLIRSKPEQIKRFAQVLIDAGVVTTVRKTRGDDIDAACGQLAGAVKDRTRLAERTGAAGKIIEVRAI
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
Q39FQ7
Q11T75
ACPS_CYTH3
4'-phosphopantetheinyl transferase AcpS
Cytophaga
MIQGIGVDIVDIARMQQRIDAASGFRELVFSPAEITYCESKANKYESYAARFAAKEAFLKAVGIGIDFSIDLNQIEITNNKAGKPYFVYTKQVEALLLTHIGFVPDAQVSLSHSREQAIAFVLFNKN
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Q11T75
Q8BUK6
HOOK3_MOUSE
Protein Hook homolog 3
Mus
MFNVESVERVELCESLLTWIQTFNVDAPCQTAEDLTNGVVMSQVLQKIDPVYFDDNWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSKESPVSAGHDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQILMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARGQLETYKRQVVELQNRLSDESKKADKLDFEYKRLKEKVDGLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEDSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLRIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQRDMEEKYIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATSTRRSYPGHVQPATAR
(Microbial infection) Serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking.
Q8BUK6
Q0TV32
SELO_CLOP1
Protein adenylyltransferase SelO
Clostridium
MDNKNFQSKTGFNLENTYLTLPNIFFSEQNPKGSKNPKLIKFNTSLAEELGLNEEVLNSDFGLNIFAGNETFPGIVPIAQAYAGHQFGHFTMLGDGRALLLGEHVTKDSKRYDVQLKGSGRTIYSRGGDGKAALAPMLREYIISEGMHGLGIPTTRSLAVVNTGEEVLRERFEQGAILTRIASSHIRVGTFAYAAQWGTLEDLKSLADYTIKRHFPNIAKSENKYILFLEEVINRQAELIVKWQSVGFIHGVMNTDNMVISGETIDYGPCAFMDTYDTNTVFSSIDYAGRYAYGNQPNMALWNLARFSEALLPLLNPNLDEAVNIAKKSISNFSKLYKKYWFNKMRAKLGLFTEKENDELLIEGLLSTMQKYEADFTNTFVSLTLNKFEDEKVFSSDEFKTWYALWQNRLKEENRSQEEVRNLMMNNNPYIIPRNHLVEKALKNAEKGDFTFMDNLLEALKNPYSYSKDLEKYTKLPEKSDTPYVTYCGT
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Q0TV32
A4SHL4
CYSG1_AERS4
Sirohydrochlorin ferrochelatase 1
Aeromonas
MDYLPIFCRLDNKPVLLVGGGEVAERKARLLLDAGARLTVVSPALDPELAALATSGTIDWLAAEFEPAHLTGKWLVVAATDRREVNALVYQSANQAGIFANVVDDPKRSSFIMPSIIDRSPLMVAISSGGKAPVLARLLREKLEALLPQHLGAVAAFAGGLRARVKARFASMGERRQFWERLLSADRLGQALARGDKASANQLADTLFAEETGAKGEVILVGAGPGDPGLLTLHALRHMQQADLVVYDQLVSDEVMALVRRDARRIFVGKQAGNHCVPQEGINQLLLEEASKGQRVVRLKGGDPFIFGRGGEELETLVGSGVGFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTAHGKGGTQDLDWPLLARDQQTLVFYMGLSSCATIRQKLTAHGKAGTTPVALIERGTQLNQRVIRGTLDQLPELAVGVESPALIMVGSVVTLADKLAWFGQTNHGVQAAALA
Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
A4SHL4
Q5WLW2
RSMA_ALKCK
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
Alkalihalobacillus
MNLNKDIATPARTNAILKKHGFTLKKSLGQNFLIDLNILAKIVEASGFDEQDGIVEIGPGIGALTEQLAKKADKVVAFEIDGRLIPVLEDTLSAYPNVKIIHSDVLKADLPGVLDAEFSKGQAIHVVANLPYYVTTPILMKLLEDRLPFKSITVMIQAEVAERIAAKPGSKEYGALSIAAQYYAEAKPMVVVPASVFVPQPRVDSSVLKLTIREKPLVEVIDERWFFNVFHASFANRRKTILNNLVHNLAGKDAKAAIEQALSEAGIDPKRRGETLSPQEFARLSDALYSTLRKAD
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.
Q5WLW2
Q0RDP3
RIMM_FRAAA
Ribosome maturation factor RimM
Frankia
MTEPIVVGRIGRPHGVRGDVTIEVRTDLPQRRFALGAVLGREGGGAPLTVAEARWHSGRLLLRFQGVEDRGAAEALRDVLLTIDSAEAGPPVDDDEDAEGEGGDIWWDRDLVGLEAVTTAGATLGRVTDVIHAPAGDLLAVGRPGGGEHLVPFVREIVPTVDPAAGRIVVDPPPGLLDLD
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Q0RDP3
C4K8P2
RIBB_HAMD5
3,4-dihydroxy-2-butanone 4-phosphate synthase
Candidatus Hamiltonella
MNQICLEYFGNSVARVKKALENLKNGHGVMVLDDENRENEGDFVFAAETMTVEQMALTIRHGSGIVCLCLTEERCQQLELPMMVEKNSSTFQTPFTVSIEAAKGVTTGVSASDRITTIKAAISQTAKPADLHRPGHVFPLKGHPKGVLGRSGHTEAAIDLARLAGLKPAGVLCELTNDNGTMARAPEVIAFAKKHKMTVLSIEDLIEYRQTHMETNFS
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
C4K8P2
A4F7R9
RS14_SACEN
30S ribosomal protein S14
Saccharopolyspora
MAKKSKIARDAQRRAVVARYAQRRAELKRIIAAPGSSPEERAAAQQELRRQPRDASATRLRNRDAVDGRPRGYFRKFGLSRVRLRQLAHSGELPGVTKSSW
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.
A4F7R9
Q65EM1
LUTC_BACLD
Lactate utilization protein C
Bacillus
MTNGTIHNKDGFLNRIAERLGRNRRSAGVTVPDYIHQPQHRVYQGYTQDELVGVLKDHCRKIHTELIETDVIGLHDALYEQAARFGGGPVMIPKDDRFKEYGLSGLLTDKWPNEGTKVWEWDAAAGDENIQRAEQANIGVTFSEITLAESGTVVLFSSKDKGRSVSLLPTTYIAIVPKSTIVPRMTQASAIIKQKIADGDVIPSCINYVTGPSNSADIEMDLVVGVHGPVKAAYIVVEDR
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source.
Q65EM1
Q9WYU3
PDXT_THEMA
Pyridoxal 5'-phosphate synthase glutaminase subunit
Thermotoga
MKIGVLGVQGDVREHVEALHKLGVETLIVKLPEQLDMVDGLILPGGESTTMIRILKEMDMDEKLVERINNGLPVFATCAGVILLAKRIKNYSQEKLGVLDITVERNAYGRQVESFETFVEIPAVGKDPFRAIFIRAPRIVETGKNVEILATYDYDPVLVKEGNILACTFHPELTDDLRLHRYFLEMVK
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Q9WYU3
B7UIC1
LEUD_ECO27
Isopropylmalate isomerase
Escherichia
MAEKFIKHTGLVVPLDAANVDTDAIIPKQFLQKVTRTGFGAHLFNDWRFLDEKGQQPNPDFVLNFPQYQGASILLARENFGCGSSREHAPWALTDYGFKVVIAPSFADIFYGNSFNNQLLPVKLSDAEVDELFALVQANPGIHFDVDLEAQEVKAGEKTYRFTIDAFRRHCMMNGLDSIGLTLQHDDAIASYEEKQPAFMR
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
B7UIC1
Q2G8K8
PYRH_NOVAD
Uridine monophosphate kinase
Novosphingobium
MSLPSCVPGYRRILLKLSGEVLMGEQQFGIDTDYVARVAQEVKDARDSGLEICLVIGGGNIFRGMAGAAKGMDRAQADYMGMLATVMNALAMQSALEQLGVPTRVQSAIEMDKVCEPVIRRRAERHLEKGRIVIFAAGVGAPYFTTDSGAALRAAEMKCDALLKGTSVDGVYNADPKKDPAAKRYETVDYDTVLADNLKVMDASAVALCRDNNIPIVVFSIRERGNLARVLAGEGTQTTVKKEA
Catalyzes the reversible phosphorylation of UMP to UDP.
Q2G8K8
A0RKF7
LIPA_BACAH
Sulfur insertion protein LipA
Bacillus cereus group
MTKQTEYKRKPEWLKIKLNTNENYTGLKKMMRSKNLHTVCEEAKCPNIHECWAVRKTATFMILGAVCTRACRFCAVKTGLPTELDLQEPERVADSVVQMGLKHVVITAVARDDLKDGGAAVFAETVRAVRRKNPFTSIEVLPSDMGGVEENLKMLMDAKPDILNHNIETVRRLSDRVRARAKYDRSLEFLRRAKEMQPDIPTKSSIMVGLGETREDLIEAMDDLRANNVDILTLGQYLQPSKKHLPVLKYYPPAEFAELKEIALSKGFSHCEAGPLVRSSYHADEQVRSAKEKTAEAK
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.
A0RKF7
Q7YC75
CYB_CHRGO
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Chrotomys
MTNIRKTHPLIKIINHSFIDLPAPSNISSWWNFGSLLGLCLMIQIITGLFLAMHYTSDTTTAFSSVAHICRDVNYGWLIRYMHANGASMFFICLFLHVGRGMYYGSYTFMETWNIGVILLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALVIVHLLFLHETGSNNPTGLNSDADKIPFHPYYTIKDLLGALILILSLMTMVLFFPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILILAFLPFLHTSKQRSMMFRPITQVLYWLLVANLLVLTWIGGQPVEHPFIIIGQLASISYFSIILILMPISGIIEDKLLKWSL
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Q7YC75
Q2A5L1
CYOE_FRATH
Heme O synthase
Francisella
MYFKRYLQLAKPGIIFGNLITLTGGFLLATHREIGFEYLPLFVYVMIGVALMIAAGCVFNNIYDQDIDSSMTRTQNRPLVTGDISVIQATIYGTILLILSCLVLYYLVNLLTLWIIIIGFIVYVGIYTVSKRLTIHATVLGGISGAIPPVAGYTAVVNILDYNALALFLILFFWQIPHSYAIAMLYIDDYKKVKLPMLPIVKGIAYTKKIMLFYLALFVVSCALPAVLGSADLFSFIVCMLVALFWMYKSIQSYRTDTDRVFAKTVFKFSIIVITAICLTMG
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Q2A5L1
O80809
CLV2_ARATH
Receptor-like protein 10
Arabidopsis
MIKIADFTLFFFIFVFSPSLPLAQSQLPDLDPQDKASLLIFRVSIHDLNRSLSTWYGSSCSNWTGLACQNPTGKVLSLTLSGLNLSSQIHPSLCKLSSLQSLDLSHNNFSGNIPSCFGSLRNLRTLNLSRNRFVGSIPATFVSLKELREVVLSENRDLGGVVPHWFGNFSMNLERVDFSFCSFVGELPESLLYLKSLKYLNLESNNMTGTLRDFQQPLVVLNLASNQFSGTLPCFYASRPSLSILNIAENSLVGGLPSCLGSLKELSHLNLSFNGFNYEISPRLMFSEKLVMLDLSHNGFSGRLPSRISETTEKLGLVLLDLSHNSFSGDIPLRITELKSLQALRLSHNLLTGDIPARIGNLTYLQVIDLSHNALTGSIPLNIVGCFQLLALMISNNNLSGEIQPELDALDSLKILDISNNHISGEIPLTLAGLKSLEIVDISSNNLSGNLNEAITKWSNLKYLSLARNKFSGTLPSWLFKFDKIQMIDYSSNRFSWFIPDDNLNSTRFKDFQTGGGEGFAEPPGKVEIKISAAVVAKDELSFSYNLLSMVGIDLSDNLLHGEIPEALFRQKNIEYLNLSYNFLEGQLPRLEKLPRLKALDLSHNSLSGQVIGNISAPPGLTLLNLSHNCFSGIITEKEGLGKFPGALAGNPELCVETPGSKCDPANIDASQEEIYQNELVEGPISIWIFCLSAFISFDFGVLGIFCSARARSYILQTKA
Involved in the perception of CLV3 and CLV3-like (CLE) peptides, that act as extracellular signals regulating meristems maintenance. Required for the sensing of the root CLE peptides (e.g. CLE8, CLE9/CLE10, CLE11, CLE13, CLE14, CLE16, CLE17, CLE18, CLE20, CLE21, CLE25, CLE26, CLE40, CLE41/CLE44 and CLE45), which involves also CRN and leads to root growth regulation, mostly in the phloem and protophloem . Involved in controlling the stem cell population size in shoot and root apical meristems, and during organ development. Promotes the formation of CLV1 multimers. In complex with CRN, perceives secreted CLV3-like effector proteins from plant-parasitic cyst nematodes as ligand mimics of the plant CLE signaling pathway . This recognition is required for proper feeding structure (syncytium) development and ultimately successful nematode infection . CLE14 perception by CLV2/CRN complex triggers root meristem differentiation .
O80809
C0ZYQ1
NRDR_RHOE4
Transcriptional repressor NrdR
Rhodococcus erythropolis group
MHCPFCRHPDSRVVDSREADEGQAIRRRRSCPECGRRFTTVETAVLSVVKRSGVTEPFSREKVVKGVRRACQGRQVDNDSLNLLAQQVEDAVRASGSAEIPSNEVGLAILDPLRNLDEVAYLRFASVYKSFSSAADFEREITDMREHAETRAADKASGAETVSVD
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
C0ZYQ1
Q9F5X1
MNMG_PSEU2
Glucose-inhibited division protein A
Pseudomonas syringae
MVDFPSRFEVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGQMSCNPAIGGIGKSHLVKEIDALGGAMAMATDKGGIQFRVLNSRKGPAVRATRAQADRVLYKAAIRETLENQPNLWIFQQACDDLIVDQDQVRGVVTQMGMRIFADSVVLTTGTFLGGLIHIGMQNYSGGRAGDPPSIALAQRLRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFLGNKEQHPPQVSCWITHTNARTHEIIASNLDRSPMYSGVIEGIGPRYCPSIEDKIHRFADKESHQVFIEPEGLTTHELYPNGISTSLPFDVQLQIVRSIRGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRDSWCPRRDEAYIGVLVDDLITLGTQEPYRMFTSRAEYRLILREDNADLRLTEKGRELGLVDDARWAAFCIKRESIELEEQRLKSTWVRPGTEQGDAIAAHFGTPLTHEYNLLNLLTRPEIDYASLISITGQGCTDPQVAEQVEIKTKYAGYIDRQQDEIARLRASEDTRLPEDIDYAAISGLSKEIQSKLGITRPETLGQASRIPGVTPAAISLLMIHLKKRGAGRQLEQSA
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.
Q9F5X1
C6E229
CMOB_GEOSM
tRNA U34 carboxymethyltransferase
unclassified Geobacter
MSNYDALYSQLVAMGQERWAEQLQATLPDKLALESTAKMAGWQSAMQSLPEIRPSRIELKENVTIGTSDDLGDINREELIALLQAFHPWRKGPYNFFGIEIDTEWRSDWKWERLLPHIQPLAGRRVLDVGCGNGYHGWRMRGAGADFVLGIDPFLLSVQQFQVMQRYLRDPQHHVIPIGIEEVPPNLACFDSVFSMGVLYHRRSPLDHLFELKGCLRPGGELILETLIVEGKRETIFMPPGRYAKMRNVWFIPSIEAMTLWLERCGFTDIGCVDTNRTSREEQRSTGWMRFESLADFLDPNDAEKTIEGHPAPLRAIFTATKL
Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
C6E229
B3PK36
RS10_CELJU
30S ribosomal protein S10
Cellvibrio
MQNQRIRIRLKAFDHKLIDASTQEIVETAKRTGAQVRGPIPLPTRKERFTVLISPHVNKDARDQYEIRTHKRLLDIVEPTEKTVDALMKLDLAAGVEVQISLG
Involved in the binding of tRNA to the ribosomes.
B3PK36
Q962S7
RL37_SPOFR
60S ribosomal protein L37
Spodoptera
MTKGTSSFGKRRNKTHTLCRRCGRSSYHIQKSKCAQCGYPAAKLRSYHWSVKAKRRKTTGTGRMRHLKIVRRRFRNGFKEGKPTPKKAVASS
Binds to the 23S rRNA.
Q962S7
Q9LXJ1
BIC1_ARATH
BLUE-LIGHT INHIBITOR OF CRYPTOCHROMES 1
Arabidopsis
MMNIDDTTSPMAHPIGPSQPPSDQTKQDPPSLPQEAASSVSADKKDLALLEEKPKQSQEEDRVDTGRERLKKHRREIAGRVWIPEIWGQEELLKDWIDCSTFDTCLVPAGISSARTALVEEARRAASASGGLHNRCLILR
Regulates the blue-light dependent dimerization of CRY2 and formation of photobodies. Interacts with photoexited CRY2 to inhibit its activity. Inhibits CRY phosphorylation.
Q9LXJ1
P46491
CRCB_HAEIN
Putative fluoride ion transporter CrcB
Haemophilus
MQALLFISYGAILGASLRWAIGLLFNPLFSSFAFGTLIANLFGCLIIGVLLGLFWQFPQISAEWRLFLITGFLGSLTTFSSFSSEVVELFFNDKWLNGFCVLMMHLFGCLAMTVLGIWIYKICLNFYLNPIHFGFAQLNQQIHRYEIRVIAYIAKFFVSF
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
P46491
B8D9Q1
TIG_BUCA5
PPIase
Buchnera
MNFFMEKNKDAGHRVTIKIPKTTVNNSLLQEFIKIRKTTKINGFRKGKTPIRVIQEKYGSAIYYDIFKKLMQKFFYEFIKTEKIKIIGSPKFYIHQDEDKKKEYFEYSVIYELYPQFQIKDIKQIKVNKINVEITEEDIKKNIETNKNKKNIWNPVNKAVKSYDRVTINYCIYEKNKKIKKFDKDNISFIVSKNTLIPQLNYKIINHFVNDIIFFKIKFHAFHPEKELQNKDITFKIKIIKIEKKQELESEKSNKKNITEKKTIQTDYQTIKNNLHSQINIITDKYLENQIIQKIVEKNILLLPPLLFQKEIKNLYKQYTKQYQEENSNILEKKYHMSLDSEVKKRLYFQIIIEQIILNNKLFADENNIQKLIKKISSNYKNPMEIIKLYNKNKNLKNTMKNIELERQAMLLLKKSIKIEKQNWNFERFLNYNWASHEELML
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
B8D9Q1
Q8YC99
LIVB6_BRUME
Leu/Ile/Val-binding protein homolog 6
Brucella
MKKIALTALAVFSLAASAAYADVVKVGVIGPFSGPFALQGKNFKAGIDAYMAEHGNKVGDDTVEVVYRDVPQADPAQSKALAQELVVKEGVQYLAGFYFTPDAMAVTPILKQGNVPMVVMNAATSSIVTKSPYVVRTSFTTWQTSTPIARVALDKGVKKVISVVSDYGPGVDAENAFKAAFTDAGGEVVEAIRMPLATNDFSPIMQRIKDSGAQGVFAFLPSGPTTLGFMKAYVDNGLKSSGIQLFAPGDLTQESDLPALGENALGVLTTFHYAVSHDSPENRKFVEEARKAIGNPAELSFPSVGAYDGMHVIYKMIEATGGKKDAAKAVEAVKGMEWVSPRGPVSIDPESRHITQNIYLREVAKADDGTYYNKEIQTFEKQGDPGLKAQ
Component of an amino-acid transport system.
Q8YC99
A0RXV1
PSB2_CENSY
Proteasome core protein PsmB 2
Cenarchaeum
MSNNVEEKILHGTTTVGIKATDGVVLCADMRASAGYFIANNNTMKIQRIDDHAGLTLAGGVADAQNIVDVLRYHASLHRIRKQGPIPIKSLARLTSLIFHQNRGYPFMADILMGGFDAVGPALYNIDMFGSVEEKSYVTTGSGSPVAYGTLEEEYRADLTADEAKGVALRAVKAAITRNIGTGDGINVAVINGNGFELLTREQKKAVIAL
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
A0RXV1
P43631
KI2S2_HUMAN
p58 natural killer cell receptor clone CL-49
Homo
MSLMVVSMACVGFFLLQGAWPHEGVHRKPSLLAHPGPLVKSEETVILQCWSDVRFEHFLLHREGKYKDTLHLIGEHHDGVSKANFSIGPMMQDLAGTYRCYGSVTHSPYQLSAPSDPLDIVITGLYEKPSLSAQPGPTVLAGESVTLSCSSRSSYDMYHLSREGEAHERRFSAGPKVNGTFQADFPLGPATHGGTYRCFGSFRDSPYEWSNSSDPLLVSVTGNPSNSWPSPTEPSSKTGNPRHLHVLIGTSVVKIPFTILLFFLLHRWCSNKKNAAVMDQEPAGNRTVNSEDSDEQDHQEVSYA
Receptor on natural killer (NK) cells for HLA-C alleles. Does not inhibit the activity of NK cells.
P43631
Q92T28
MGSA_RHIME
Methylglyoxal synthase
Sinorhizobium
MADRKCLALIAHDQKKDDLAAFAKANEAVLSKWKIVATGTTGGRVLDVCPALDIVRLKSGPLGGDQQIGALIATGDVDCLIFFVDPLTAMPHDVDVKALMRLAIVYDIPMALNRATAEQLIDFRRN
Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Q92T28
Q69Z69
ESCO1_MOUSE
Establishment of cohesion 1 homolog 1
Mus
MSIQEKSKENSSIVTKESEDENLEEEVESSQNSPTKKSGSKEAVKTPVRFSNKSKTNESEFGMRMSTRSASCSADKTATNSFNKNTVTLKGQSQESSKTKKLCQEKLSLGILKGNEQLHRRSQRLQQLTECTTRSLRSREIHGQIQTVKQNQQSARREQCNSTQSKCNKVKVNQKHVKRKVLEIKSDCKEDRHSVTNEVINSPKGKKRKVQHQTTSTCSSQCNQGSEKCLQKTSRKEEIKPVPVTADIRKLKAATSVVSKKNELRKSAHTQVSTSTKRPQIPLPLVPEHSDDQELEQAGKSKRGSILQLCEEIAGEIESDTVEVKKESSCVESVKEEKPAEVKLQGTDAERQILHHKEANQDVRSNRFFPSRKTKPVKCVLNGINSSTKKNSNWTKIKLSKFNSVQQHKLDSQVSPKLNLLQTGLSTSVLEMPHPVSQSTFLEMKAHGNVTCQRDKMKGIKSEEVKINNIAIEINKATKRDPGNCNLDNHIKPSPDSSLDNQMKLSCESAPDQNFSICSASEVETNPLENTAAASTLLSQAKIDEDRTFPGSAPNQQHSVLSDEASINRKNRDVPPNHSQLKHDSHLEITIPKSLKLKDSEKVDEKQLVIDAGHKRFGAVSCNICGMLYTASNPEDETQHLLFHNQFISAVKYVGWKKERILAEYPDGRIIMVLPEDPKYALKKVDEIREMVDNDLGFQQAPLMCYSRTKTLLFISNDKKVVGCLIAEHIQWGYRVIEEKLPVIRSEEEKVRFERQKAWCCSTLPEPAICGISRIWVFSMMRRKKIASRMIECLRSNFIYGSYLSKEEIAFSDPTPDGKLFATQYCGTGQFLVYNFINGQNTT
Acetyltransferase required for the establishment of sister chromatid cohesion. Couples the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. Acts by mediating the acetylation of cohesin component SMC3.
Q69Z69
Q6MIR9
NUOI_BDEBA
NDH-1 subunit I
Bdellovibrio
MSVMQNNSEKSKWFLPGILGGLATTMKHLLKNLFNQKKMMTLNYPEEKYEYSPRFKGNHVLTVKKDGSLRCTACMLCATNCPAECIKITAAEHNDPTVEKFPISYEIDILRCVFCGFCEEACPVDAIRLGPEWQTPGVNGANFIYDINHLAYRPNLKGGILTHVDDEERHKAGI
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Q6MIR9
Q08048
HGF_MOUSE
Hepatocyte growth factor beta chain
Mus
MMWGTKLLPVLLLQHVLLHLLLLHVAIPYAEGQKKRRNTLHEFKKSAKTTLTKEDPLLKIKTKKVNSADECANRCIRNRGFTFTCKAFVFDKSRKRCYWYPFNSMSSGVKKGFGHEFDLYENKDYIRNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQCSEVECMTCNGESYRGPMDHTESGKTCQRWDQQTPHRHKFLPERYPDKGFDDNYCRNPDGKPRPWCYTLDPDTPWEYCAIKTCAHSAVNETDVPMETTECIQGQGEGYRGTSNTIWNGIPCQRWDSQYPHKHDITPENFKCKDLRENYCRNPDGAESPWCFTTDPNIRVGYCSQIPKCDVSSGQDCYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNKNYCRNPDDDAHGPWCYTGNPLIPWDYCPISRCEGDTTPTIVNLDHPVISCAKTKQLRVVNGIPTQTTVGWMVSLKYRNKHICGGSLIKESWVLTARQCFPARNKDLKDYEAWLGIHDVHERGEEKRKQILNISQLVYGPEGSDLVLLKLARPAILDNFVSTIDLPSYGCTIPEKTTCSIYGWGYTGLINADGLLRVAHLYIMGNEKCSQHHQGKVTLNESELCAGAEKIGSGPCEGDYGGPLICEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKVILTYKL
Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization.
Q08048
A9WT08
DCDB_RENSM
DCD-DUT
Renibacterium
MLISDRDIRTQIDSGRIVLDPFEPSMVQPSSVDVRIDKLFRLFDNHKYAHIDPAEEQPELTRLVEVAADEPFILHPGEFVLGSTYEAVTLPDDVAARLEGKSSLGRLGLLTHSTAGFIDPGFSGHVTLELSNMATLPIKLWPGSKIGQLCFFQLSSPAEHPYGSGAYGNRYQGQRGPTASRSHQNFHRTEI
Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
A9WT08
Q7YWU9
UBXN5_CAEEL
UBX domain-containing protein 5
Caenorhabditis
MPTNNHVQKEKFAEDRALLSQQNKEYAESLAKDIAKKEEKDKIRFEAEQKELRKKTIQDYREKLKGTVSQGPLRLLVRYPNGSRLILSFSPSQPMTSLFDAIILNPACPDYFSVRSVYPRAEIHCYPAWYHTIFNAEFKDETEKGANNVAKETNEVKCLETIPNNSILYVNLIQ
Probably acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity. Unlike other UBX domain-containing protein does not bind 'Lys-48'-polyubiquitinated chain.
Q7YWU9
Q8X5V6
DUSA_ECO57
tRNA-dihydrouridine synthase A
Escherichia
MHGNSEMQKINQTSAMPEKTDVHWSGRFSVAPMLDWTDRHCRYFLRLLSRNTLLYTEMVTTGAIIHGKGDYLAYSEEEHPVALQLGGSDPAALAQCAKLAEARGYDEINLNVGCPSDRVQNGMFGACLMGNAQLVADCVKAMRDVVSIPVTVKTRIGIDDQDSYEFLCDFINTVSGKGECEMFIIHARKAWLSGLSPKENREIPPLDYPRVYQLKRDFPHLTMSINGGIKSLEEAKAHLQHMDGVMVGREAYQNPGILAAVDREIFGSSDTDADPVAVVRAMYPYIERELSQGTYLGHITRHMLGLFQGIPGARQWRRYLSENAHKAGADINVLEHALKLVADKR
Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs.
Q8X5V6
B6EPT9
RS8_ALISL
30S ribosomal protein S8
Aliivibrio
MSMQDPISDMLTRVRNGQSANKVAVKMPSSKLKVAIAALLKAEGYIADFAVEGDIKPELEITLKYFQAKQVIEQIQRVSRPGLRVYKKNDALPSVMGGLGIAVISTSKGLMSDRAARKAGLGGEIICYVA
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.
B6EPT9
Q11QE1
ENO_CYTH3
2-phosphoglycerate dehydratase
Cytophaga
MSLIEEIVARQIFDSRGNPTIEVDVITENGLIGRAAVPSGASTGKHEAVELRDNDKSIYMGKSVLKAVANVNDIIAPELIGSHVFEQNLIDRLMIDLDGTANKGKLGANAILGVSLALAKAAAQEAGLPLYRYVGGVSANTLPVPMMNIINGGSHADNSIDFQEFMIMPTGAKSFTEAMRMGSEIFHNLAKVLKSKGMSTNVGDEGGFAPNIASNEDALITVIQAIEAAGYRPGEDVMIAFDAASSEFYDSETKLYHFKKSTGDKLTSSQMASYWADLVKRYPIVSIEDGMDEDDWSGWAELTKLVGDKVQLVGDDLFVTNVSRLQQGIDQGIANSILVKVNQIGSLTETISAVNLAKRNSYTSVMSHRSGETEDNTIADLAVALNCGQIKTGSCSRSDRMAKYNQLLRIEEELGEAAYFPGKNMRK
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Q11QE1
O15442
MPPD1_HUMAN
Adult brain protein 239
Homo
MWRSRWDASVLKAEALALLPCGLGMAFSQSHVMAARRHQHSRLIIEVDEYSSNPTQAFTFYNINQGRFQPPHVQMVDPVPHDAPKPPGYTRFVCVSDTHSRTDPIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYKIVIAGNHELTFDQEFMADLIKQDFYYFPSVSKLKPENYENVQSLLTNCIYLQDSEVTVRGFRIYGSPWQPWFYGWGFNLPRGQALLEKWNLIPEGVDILITHGPPLGFLDWVPKKMQRVGCVELLNTVQRRVQPRLHVFGHIHEGYGVMADGTTTYVNASVCTVNYQPVNPPIVIDLPTPRNS
May have metallophosphoesterase activity (in vitro).
O15442
Q9KTF9
LIPA_VIBCH
Sulfur insertion protein LipA
Vibrio
MSKPIQMERGVKYRDADKMALIPIKNMPTEQKEVLRKPEWMKIKLPADSQRIQDIKAAMRKNNLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPNAPEAEEPKKLAQTIHDMKLKYVVITSVDRDDLRDGGAQHFADCNREIRALNPHIKIETLVPDFRGRMEVALEALKDNPPDVFNHNLETAPRLYRKVRPGANYKWSLELLRQFKEQHPHVPTKSGLMMGLGETKEEIVEVLKDLRAHGVTMLTLGQYLAPSRHHLPVERYVPPAEFDELKEVALELGFTHAACGPFVRSSYHADLQAKGLEVK
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.
Q9KTF9
Q2KPA3
HBB_SCAOR
Hemoglobin beta chain
Scapanus
MVHLSAEEKGLVTGLWGKVNVDDVGAEALGRLLVVYPWTQRFFDSFGDLSSAGAIMGNPKVKAHGKKVANSISDGIKNLDNLKGTYAKLSELHCDKLHVDPENFRLLGNVLVCVMARTLGKEFTPHAQAAFQKMVLGVATALAHKYH
Involved in oxygen transport from the lung to the various peripheral tissues.
Q2KPA3
Q318B0
CRCB1_PROM9
Putative fluoride ion transporter CrcB 1
Prochlorococcus
MKIKIYIYILLACYIASFLRLFINNNFIVSIIGSLLFGFFIDKRLSYSIEKIILSGFFSCFTSFSGFIYFLYKVFNQGDLMKFIIFCNLIIIINLLVMYFGFWISRKIT
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Q318B0
Q3Z977
RS19_DEHM1
30S ribosomal protein S19
Dehalococcoides
MSRSVKKGPALCPKLMKKVEVASATNQKSIIKTWARWSTITPLMVGLNVGVHDGRRHVPIYITENMVGHRLGEFTTTRNFRGHAKAEKVSQVK
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Q3Z977
Q3SIM3
PLSX_THIDA
Phosphate-acyl-ACP acyltransferase
Thiobacillus
MRNITVAIDVMGGDHGPHVTVPAAIRCLARHPDLNVILVGPQDIIAAELRAHRSGPGPRLIVRHASQVVAMDEAPALALRGKKDSSMRVAIDLVKSGEADACVSAGNTGALMATARFVLKTLPGIDRPAIAAVMPTVSGHALVLDMGANVDCTAEHLLQFGIMGAMLVSAVEHKQNPSVGLLNVGEEDIKGNEMVKRAAELLRDSHLNFYGNVEGNDIFKGTTDVVVCDGFVGNVTLKASEGLAKMISTVLKAEFKRNWLTRIAGLIALPVLKAFKRRLDPRRYNGATLLGLKGVVVKSHGSADRYAFEHAIETAGDEVRNNVLKRITDQIQLLQRVAA
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Q3SIM3
Q06850
CDPK1_ARATH
Calcium-dependent protein kinase isoform AK1
Arabidopsis
MGNTCVGPSRNGFLQSVSAAMWRPRDGDDSASMSNGDIASEAVSGELRSRLSDEVQNKPPEQVTMPKPGTDVETKDREIRTESKPETLEEISLESKPETKQETKSETKPESKPDPPAKPKKPKHMKRVSSAGLRTESVLQRKTENFKEFYSLGRKLGQGQFGTTFLCVEKTTGKEFACKSIAKRKLLTDEDVEDVRREIQIMHHLAGHPNVISIKGAYEDVVAVHLVMECCAGGELFDRIIQRGHYTERKAAELTRTIVGVVEACHSLGVMHRDLKPENFLFVSKHEDSLLKTIDFGLSMFFKPDDVFTDVVGSPYYVAPEVLRKRYGPEADVWSAGVIVYILLSGVPPFWAETEQGIFEQVLHGDLDFSSDPWPSISESAKDLVRKMLVRDPKKRLTAHQVLCHPWVQVDGVAPDKPLDSAVLSRMKQFSAMNKFKKMALRVIAESLSEEEIAGLKEMFNMIDADKSGQITFEELKAGLKRVGANLKESEILDLMQAADVDNSGTIDYKEFIAATLHLNKIEREDHLFAAFTYFDKDGSGYITPDELQQACEEFGVEDVRIEELMRDVDQDNDGRIDYNEFVAMMQKGSITGGPVKMGLEKSFSIALKL
May play a role in signal transduction pathways that involve calcium as a second messenger. Phosphorylates the Ca(2+)-ATPase ACA2 resulting in the inhibition of its calcium activation.
Q06850
Q96QF0
RAB3I_HUMAN
SSX2-interacting protein
Homo
MGLKKMKGLSYDEAFAMANDPLEGFHEVNLASPTSPDLLGVYESGTQEQTTSPSVIYRPHPSALSSVPIQANALDVSELPTQPVYSSPRRLNCAEISSISFHVTDPAPCSTSGVTAGLTKLTTRKDNYNAEREFLQGATITEACDGSDDIFGLSTDSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAALKTLVLSSSPTSPTQEPLPGGKTPFKKGHTRNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKDEPTMDRTCPFLDKIYQEDIFPCLTFSKSELASAVLEAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQQGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKEEL
Guanine nucleotide exchange factor (GEF) which may activate RAB8A and RAB8B . Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form . Mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5 . Modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface . Together with RAB11A, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis .
Q96QF0
Q4JF28
IRF3_BOVIN
Interferon regulatory factor 3
Bos
MGTQKPRILPWLISQLDRGELEGVAWLGESRTRFRIPWKHGLRQDAQQEDFGIFQAWAVASGAYTPGKDKPDLPTWKRNFRSALNRKEVLRLAEDHSKDSQDPHKIYEFVNSGVRDIPEPDTSQDNGRHNTSDTQEDTLEKLLSDMDLSPGGPSNLTMASEKPPQFLQSPDSDIPALCPNSGLSENPLKQLLANEEDWEFEVTAFYRGCQVFQQTVFCPGGLRLVGSEAGDRMLPGQPIRLPDPATSLTDKSVTDYVQRVLSCLGGGLALWRAGQWLCAQRLGHCHVYWAIGEELLPSCGHKPDGEVPKDREGGVFNLGPFITDLITFIEGSRRSPLYTLWFCVGQSWPQDQPWIKRLVMVKVVPMCLRVLVDIARQGGASSLENTVDLHISNSDPLSLTPDQYMACLQDLAEDMDF
Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.
Q4JF28
A0PRX9
THIG_MYCUA
Thiazole synthase
Mycobacterium
MVESKLMIADRSFASRLIMGTGGASNLAVLQEALVASGTELTTVAIRRVDAEGGTGLLDLLNRLGITPLPNTAGCRSAAEAVLTAQLAREALATNWVKLEVIADERTLLPDAIELVRAAEQLVDDGFVVLPYTNDDPVLARRLEDTGCAAVMPLGSPIGTGLGITNPHNIEMIVASAGVPVVLDAGIGTASDAALAMELGCDALLLATAVTRAADPAAMAAAMSAAVTAGYLARCAGRIPKRFWAQASSPTLVTTQSPGAESGN
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
A0PRX9
Q49XC6
PHNC_STAS1
Phosphonates import ATP-binding protein PhnC
Staphylococcus
MSQIEFKDVRKVYSNGHVGLDRINLNIEKGDFAVIVGLSGSGKSTLLRSINRLHDITEGEILIDGKSMTKASGNQLLEMRRNIGMIFQNFNLVKRSSVMRNVLSGRVGYHPTWKMVLGLFPKEDKIKALEALDRVNILDKYKSRSDELSGGQQQRISIARALCQEPAIILADEPVASLDPLTTKQVMDDLKRINQELGITIIINLHFVDLAREYGTRIIGLRDGQLVFDGPVERATDEAFNEIYGRSIQDEEKLGVN
Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
Q49XC6
Q96F44
TRI11_HUMAN
Tripartite motif-containing protein 11
Homo
MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSPQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCPAHREPLAAFCGDELRLLCAACERSGEHWAHRVRPLQDAAEDLKAKLEKSLEHLRKQMQDALLFQAQADETCVLWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQRLEEEELEVLPRLREGAAHLGQQSAHLAELIAELEGRCQLPALGLLQDIKDALRRVQDVKLQPPEVVPMELRTVCRVPGLVETLRRFRGDVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGSGDTLAPQ
E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle.
Q96F44
P38574
UPK3A_BOVIN
Uroplakin III
Bos
MPPLWVVLALGCLRLGSGVNLQPQLASVTFATNNPTLTTVALEKPLCMFDSSAALHGTYEVYLYVLVDSASFRNASVQDSTKTPLSSTFQQTQGGRTGPYKAAAFDLTPCSDSPSLDAVRDVSRASEILNAYLIRVGTNGTCLLDPNFQGLCNPPLSAATEYRFKYVLVNMSSGLVQDQTLWSDPIRTDRLTLYSAIDTWPGRRSGGMIVITSILGSLPFFLLIGFAGAIVLSLVDRGDADGATSHDSQITQEAVPKSLGTSEPSYTSVNRGPSLDRAEVYASKLQD
Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx which may play an important role in preventing bacterial adherence.
P38574
B2IF94
RS11_BEII9
30S ribosomal protein S11
Beijerinckia
MAKEATRVRRRERKNIVSGVAHVNSTFNNTMITITDAQGNTISWSSAGMMGFKGSRKSTPYAAQMAAEDCARKAVEHGMRTLEVEVSGPGSGRESALRALQAAGFTVTSIRDVTPIPHNGCRPRKRRRV
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
B2IF94
Q1LND7
SSRP_CUPMC
Small protein B
Cupriavidus
MTIADNKKAFFDYFIEERYEAGIVLEGWEVKAIRAGRVQIKEGYVVVRDAEMFLIGAHISPLQSASTHINPDPVRTRKLLLKADEIKKLIGKVEQRGYTLVPLNLHYTRGRVKCEIGLAKGKKQFDKRETEKNRDWDREKARIMKGGVKE
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Q1LND7
B4SRK3
NAGZ_STRM5
N-acetyl-beta-glucosaminidase
Stenotrophomonas maltophilia group
MLLIGVAGTELTAQERDWLQHDAVAGVVLFKRNFASRQQVTDLSAAIRAAAPRPQLICVDQEGGRVQRFREGYSELPPLQDIGALYATDPQQALALAEQHAWLMASEVRASGLDLSFAPVVDLGRGNRAIGNRAFSEDPQVVAAFTAAYVRGMHAVGMAATLKHFPGHGTVLEDTHVDTAIDPRALDELRAQDLVPFQAGIAAGADAVMMAHVVYPQVAPEPAGYSPRWIQDILRGELGFRGVVFSDDIGMAASHSAGGVPARVHAHLDAGCDVVLVCHPELVDEALHAVQGRSLNTAALLGLLGRGALGWDGLLADARHGDTQSHLLETLGRTV
Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
B4SRK3
B6JND5
RS11_HELP2
30S ribosomal protein S11
Helicobacter
MAKRNVVAKKKVVKKNIARGVVYISATFNNTNITITDEMGNVICWSTAGGLGFKGSKKSTPYAAQQAVESALSKAKEHGVKEVGIKVQGPGSGRETAIKSVGATEGVKVLWIKDITPLPHNGCRPPKRRRV
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
B6JND5
A4F9N6
RS20_SACEN
30S ribosomal protein S20
Saccharopolyspora
MANIKSQMKRIKTNEANRQRNKAVKSSLKTAIRKFREAADAGDKAKAVELQATAGRALDKAVSKGVIHSNQAANKKSAMAKRANQL
Binds directly to 16S ribosomal RNA.
A4F9N6
Q9CR46
SKA2_MOUSE
Protein FAM33A
Mus
MEAEVDKLELMFQKADSDLDYLQYRLEYEVKTNHPHSAGEKNAVTVLKELSAIKSRYQALCARFKAVSVEQKETKSCICATLNKTMTMIQELQKQTNLELTLLTEEEKAATEPLKSHMPD
Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex, it is required for SKA1 localization. Affinity for microtubules is synergistically enhanced in the presence of the ndc-80 complex and may allow the ndc-80 complex to track depolymerizing microtubules.
Q9CR46
A6L2R5
ARAA_PHOV8
L-arabinose isomerase
Phocaeicola
MEKAFDQYEVWFVTGAQLLYGGDAVIAVDAHSNEMVNGLNESGKLPVKVVYKGTANSSKEVEAVFKAANNDEKCIGVITWMHTFSPAKMWIHGLQQLKKPLLHLHTQFNKEIPWDTMDMDFMNLNQSAHGDREFGHICTRMRIRRKVVVGYWKDEDTQHKIAVWMRVCAGWADSQDMLIIRFGDQMNNVAVTDGDKVEAEQRMGYHVDYCPASELMKYHKNIKDTDVEALVATYFNEYDHDASLEDKSTEAYQKVWNAAKAELALRAILKAKGAKGFTTNFDDLGQTDGSYFDQIPGLASQRLMAEGYGFGAEGDWKSAALYRTVWVMNQGLSKGCSFLEDYTLNFDGANSAILQSHMLEVCPLIAASKPRLEVHFLGIGIRKSQTARLVFTSKVGSGCTATVVDLGNRFRLIVNDVECIESKPLPKLPVASALWIPMPNFEVGAGAWILAGGTHHSCFSYDLTAEYWEDYAEIAGIEMIRIDKDTTISNFKKELRMNEVYYMLNKALC
Catalyzes the conversion of L-arabinose to L-ribulose.
A6L2R5
P21525
FOSLA_DROME
Fos-related antigen
Sophophora
MKNLNGRTHNACYHPYYHQSLHFAQQQQQQQQHHLQQQQQHMQQQQQQQQAPQQQLRHQQRQLPTQPAYQQSQSVAHNAFPLRSSSNNYGHVASSAYAASSGSHNSNNAAAMAAVCQMQNFFNQQQQQQQQLEFNNNCMPINYYQQQQQQHYPSESQSSASGWNPETPGQAQLALTATTCNTTAAATCNTTAAATTSTTATSAAAGSDNNHSDNFAMDASEIATFLANELFLQQLGNFETGQSVLTLTTPTLTPTTTRNIEDTLGHLLSDTQTDRVAGCAGFAVPKVLPNAIDVLGMGIPTGVSSLPLQQTFDLSLGQGSESEDSNASYNDTQMNEEQDTTDTSSAHTDSTSYQAGHIMAGSVNGGGVNNFSNVLAAVSSSRGSASVGSSNANTSNTPARRGGGRRPNRSTNMTPEEEQKRAVRRERNKQAAARCRKRRVDQTNELTEEVEQLEKRGESMRKEIEVLTNSKNQLEYLLATHRATCQKIRSDMLSVVTCNGLIAPAGLLSAGSSGSGASSHHNHNSNDSSNGTITGMDATLNSTGRSNSPLDLKPAANIDSLLMHIKDEPLDGAIDSGSSLDQDGPPPSKRITLPPMSTMPHVHLSTILTPTGASSGSLQTPITSTAPGGFGSAFPVTSNGSSINNINSIGNNMNSPTLNAHNKVPKERPNTLAFQRPLGQMHLTMANNKAGGPTQIQGVPIQTPSTGTFNFDSLMDGGTGLTPVSGPLVPNSSSTNKHPLELPTPTAEPSKLVSL
Developmentally regulated transcription factor AP-1 binds and recognizes the enhancer DNA sequence: 5'-TGA[CG]TCA-3'. May play a role in the function or determination of a particular subset of cells in the developing embryo. It is able to carry out its function either independently of or in conjunction with Jra.
P21525
B3QR32
NDK_CHLP8
Nucleoside-2-P kinase
Chlorobaculum
MERTLTILKPDCVRKQLIGAVTDKIERAGFRIVAMKKTRLTKETAGAFYAVHKERPFYGELVEFMSSGPCVPMILEKENAVADFRTLIGATDPAEAAEGTVRKLYADSKGENIVHGSDSAENAAIEGAFFFAAEEVVRVD
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
B3QR32
Q9CBA8
MENG_MYCLE
Demethylmenaquinone methyltransferase
Mycobacterium
MSRAALDKDPRDVVAMFDDVAHRYDLTNTVLSLGQDRYWRRATRSALRIGPGQKVLDLAAGTAVSTAELSKSGAWCVAADFSVRMLATGGARKVPKVAADATQLPFSDGVFDAVTISFGLRNIADYQAALREMARVTRPGGQLVVCEFSTPTNALVANVYTEYLMRALPQVARLVSSNPDAYIYLAESIRAWPDQVTLACQLSRTGWASPRWRNLTGGIVALHAADKPVR
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Q9CBA8
P00311
PHCB_GALSU
C-phycocyanin beta chain
Galdieria
MLDAFAKVVAQADARGEFLSNTQLDALSKMVSEGNKRLDVVNRITSNASAIVTNAARALFSEQPQLIQPGGNAYTNRRMAACLRDMEIILRYVSYAIIAGDSSILDDRCLNGLRETYQALGVPGASVAVGIEKMKDSAIAIANDPSGITTGDCSALMAEVGTYFDRAATAVQ
Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod.
P00311
Q6M154
ARGB_METMP
NAG kinase
Methanococcus
MEDYTKAEILIEALPYICKFHDQKILIKYGGHAMVNEQAKNWIAKDLVLLKYVGINPIVVHGGGPEINRAMEKMGKTPEFIHGLRVTDEETLDIVKMVLIGKINGDIVSKLERYGGKSVGLSGKSGQLIKAKKKIQYLMKDSQKIEVDLGMVGEVEHVDTKLIDILVEKRYIPVISPIGVDHQGNDLNLNADIAAGDIAGAMNAQKLIMVTDVDGIMDDVNDPSTLHRRLTIPQIEDMIEKGLITGGMIPKIEACVNALDKGVQSVHIVNGKTPHAVLLEIFTEDGVGTMVVRE
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Q6M154
Q5KUJ9
NUOH_GEOKA
NDH-1 subunit H
Geobacillus thermoleovorans group
MMEQWLESTPGWSNIALFFGLGALLLAVVLAFVTYGILAERKVMGFMQGRIGPNQVGGRFGLLQTVADVLKLLLKEDTIPKAADRPLYVLAPIIAFVPSFMVLAVLPFTDAFRFADIGVGLLYYIAVSGLTTVGVVAGGWASNNKYALLGGMRAAAQMISYEIPLVMSALGVVLLAGSMNLVDIVAAQKDVWFIFAQPLAFLIFLIAAVAELNRTPFDLPEAESELVAGFHVEYSGFRWAFFMLAEYVYLFAMAALVTILFLGGWHPVAFLGWIPGAVWFALKFCAVVFVLIWFRATFPRVRADQLMEFAWKVLLPLSLVNIVLTAVVKAWFF
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
Q5KUJ9
P0AAG4
GLTL_ECO57
Glutamate/aspartate import ATP-binding protein GltL
Escherichia
MITLKNVSKWYGHFQVLTDCSTEVKKGEVVVVCGPSGSGKSTLIKTVNGLEPVQQGEITVDGIVVNDKKTDLAKLRSRVGMVFQHFELFPHLSIIENLTLAQVKVLKRDKAPAREKALKLLERVGLSAHANKFPAQLSGGQQQRVAIARALCMDPIAMLFDEPTSALDPEMINEVLDVMVELANEGMTMMVVTHEMGFARKVANRVIFMDEGKIVEDSPKDAFFDDPKSDRAKDFLAKILH
Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Probably responsible for energy coupling to the transport system.
P0AAG4
Q8N5F7
NKAP_HUMAN
NF-kappa-B-activating protein
Homo
MAPVSGSRSPDREASGSGGRRRSSSKSPKPSKSARSPRGRRSRSHSCSRSGDRNGLTHQLGGLSQGSRNQSYRSRSRSRSRERPSAPRGIPFASASSSVYYGSYSRPYGSDKPWPSLLDKEREESLRQKRLSERERIGELGAPEVWGLSPKNPEPDSDEHTPVEDEEPKKSTTSASTSEEEKKKKSSRSKERSKKRRKKKSSKRKHKKYSEDSDSDSDSETDSSDEDNKRRAKKAKKKEKKKKHRSKKYKKKRSKKSRKESSDSSSKESQEEFLENPWKDRTKAEEPSDLIGPEAPKTLTSQDDKPLNYGHALLPGEGAAMAEYVKAGKRIPRRGEIGLTSEEIASFECSGYVMSGSRHRRMEAVRLRKENQIYSADEKRALASFNQEERRKRENKILASFREMVYRKTKGKDDK
Acts as a transcriptional repressor . Plays a role as a transcriptional corepressor of the Notch-mediated signaling required for T-cell development . Also involved in the TNF and IL-1 induced NF-kappa-B activation. Associates with chromatin at the Notch-regulated SKP2 promoter.
Q8N5F7
Q9ZZ51
COX2_SQUAC
Cytochrome c oxidase polypeptide II
Squalus
MAHPSQLGFQDAASPVMEELLHFHDHTLMIVFLISTLVLYIIMAMVSTKLTNKYILDSQEIEIVWTILPAVILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIQTQDLTPGQFRLLETDHRMVVPMESPIRVLVSAEDVLHSWTVPALGVKMDAVPGRLNQTAFIISRPGVYYGQCSEICGANHSFMPIVVEAVPLEHFESWSSLMLEEA
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.
Q9ZZ51
Q7NNJ8
IF1_GLOVI
Translation initiation factor IF-1
Gloeobacter
MAKQDVIEMEGTVVESLPNAMFRVELDNSFNILAHISGKIRRNYIKILPGDRVKVELTPYDLTKGRITYRLRK
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Q7NNJ8
A9VT80
RIMM_BACMK
Ribosome maturation factor RimM
Bacillus cereus group
MTKWFNVGKIVNTHGVKGEIRVISRTDFPEERYKVGNTLYIWDEKGTDYLTVKVTSHRQHKTFDLLTLEGYNNVDEVEKLKGSLIKVPEEQLGELAEGEYYYHEIIGCNVVTEEGEALGTIKEILSPGANDVWVIKRPKGQDLLIPYIDDVVLQVNIENKLVTIHVMEGLL
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
A9VT80
Q927E6
DHAK1_LISIN
PTS-dependent dihydroxyacetone kinase 1, dihydroxyacetone-binding subunit DhaK
Listeria
MKKILNGTDQVVEQMVEGLVKSHADVVHRVEGTRVIARNDKRPGKVGLVSGGGSGHEPAHAGYVGRGMLSAAVCGDVFTSPTPDQIYEGIKAADQGAGVLLIVKNYTGDVMNFEMAADLADADDIKVEQIVVDDDIAVEDSTFTTGRRGVAGTVLVHKIIGAAAEAGASLEELKALGEKVIASVKTLGVALSPCTVPEVGHPGFELGDDEIELGIGIHGEPGFTREKIMPSARLAKQLYERISSESKLLAGDKVVVLVNGMGATPLMEQYVFANDVHELLKNAGVQVEKTLVGDYMTSLEMAGLSLTILKLEDEKWVDMLKLPVDTIAW
Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP.
Q927E6
A7H2B2
MNMC_CAMJD
FAD-dependent cmnm(5)s(2)U34 oxidoreductase
Campylobacter
MKKAKLIFKDNTPFSLDFDDFYFNSKDGLNESKFVYTHSFEWKNQENFIITESGFGIGLNFFLTLKRFLETTPSKRPKKLFYISVEAFYIEKEQLREIYQKLRFYEEFKELLEHFLKFYPKAKEGIYRFYFEDCFLDLVFEDITILKELDFKADVWYLDGFSPNKNSQMFDENLIFEVARLSKKNTQICTFSSASFLQKNLKKYGFRVEKTKGFRKREMIKAYLENELEFKDKEAYFSRTFSSLKNKKVAIIGAGISSAVLAYELSLRGFKIDVFEKHLELGKGASGNESGILSSLILKSKVKLGEFSELSFIEASRFYRQILDLNFKGVVEFAHNDLMQERFDTQRENVLFKISKNQAFLEEGGVIFPKNLVKNLFEKSKACIYFNHEFQAYKFENECFTLKFKNDIVKSDYAVLIYAMGADTKDFVFYDEMKLSKVRGQVTHLKPFLDTQFPLSSKAYICPIKDDLQVIGASYDRLDASLESKEEDDKQNIENIAEFIDKNTKLEIIGSKVGFRSYSSDRFMIVGNAYDEAFYKEEYKALLWTKDKEQKPAKMSCNLYFNFAHGSRGFSTSVLAARYLCALINNEPLCLEKKYIHAIHPARFLVRKLKKGL
Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
A7H2B2
P01717
LV325_HUMAN
Ig lambda chain V-IV region Hil
Homo
MAWIPLLLPLLTLCTGSEASYELTQPPSVSVSPGQTARITCSGDALPKQYAYWYQQKPGQAPVLVIYKDSERPSGIPERFSGSSSGTTVTLTISGVQAEDEADYYCQSADSS
V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen .
P01717
Q1WUF8
RIMP_LIGS1
Ribosome maturation factor RimP
Ligilactobacillus
MSSVVETVTNLVTPILDENHFELVDVEFVKEGKSWYLRVYIDKPNGINIEECALVSDKLSEKLDSCDPDPIPQAYYLEVSSPGAERPLKKEKDYERALNKYIHISLYQAIDGQKVYEGTMVDLNKETLTLEYRVKTRTVTKTFDRNKIAKARLAIKF
Required for maturation of 30S ribosomal subunits.
Q1WUF8
Q9RTN7
ACNA_DEIRA
RNA-binding protein
Deinococcus
MSDKAMNLFGARDTLQVPGSDKKLYFYNLNKLQGHDVSRLPVSIKVLLESVLREANDYDVRREDVETVAGWSATNPEVEIPFKPARVILQDFTGVPAVVDLAAMRSAMVKLGGDPSKINPLIPVDLVIDHSVQVDEFGTEFALANNMALEFERNRERYEFLRWGQQAFDNFGVVPPASGIVHQVNLEYLAKGVQSRAEDDGEVVYPDSLVGTDSHTTMINGLGIVGWGVGGIEAEAVMLGQPIYMLMPEVIGFKITGAMPEGATATDLALRVTQMLREKGVVGKFVEFYGAGLSNMTLPDRATIANMAPEYGATMGFFPVDDEALRYLRRTGRLEDEIGLVEAYYKAQGMFRTDETPDPVFTDTIELDLATIVPSLAGPKRPQDRVNLSDMHSVFNEALTAPVKNRGFELGSDKLDAQGTIGGTDIKIGHGAVTLASITSCTNTSNPSVLIAAGLVAKKAVEKGLKTKPWVKTSLAPGSRVVTEYLETAGLQQYLDQIGFNTVGYGCMTCIGNSGPLPEPVVEAIQEGDLVVASVLSGNRNFEGRVNPHIKANYLASPPLVVAYALAGTVVNDIVNDAIGQDSNGQDVFLKDIWPTNAEIQEAMDRSINAEMFKKVYDGIEKSNADWNAIPVAEGALFDWKEDSTYIQNPPFFDTLAGGAHEIESIKGARALVKVGDSVTTDHISPAGSFKADTPAGRYLTERGIAPKDFNSYGSRRGNDRIMTRGTFANIRLKNQLAPGTEGGFTTNFLNGEVTSIFDASTAYKEAGVPLVVLAGKDYGMGSSRDWAAKGTFLLGVKAVIAESFERIHRSNLVGMGVLPLQYKNGETADSLGINGDETFEFVLPGDLKPRQDVTVKVTGKDGNTRDITVMCRIDTPVEIDYYKNGGILQTVLRGILSKSQGEVKA
Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein.
Q9RTN7
Q8VGR9
O1044_MOUSE
Olfactory receptor 185-4
Mus
MAQINCTQVTEFILVGLTDREELKMPLFVVFLSIYLFTTLGNLGLILVIRTDARLHTPMYFFLSNLAFVDFCYSSVITPKMLGNFLYKQNMISFNACAAQLGCFLAFMTAECLLLASMAYDRYVAICNPLLYMVLMSPGICFQLVAAPYSYSFLVALFHAILTFRLCYCHSNAINHFYCDDMPLLRLTCSDTHSKQLWIFVCAGIMFISSLLIVFISYTFIISAILRMRSAEGRRKAFSTCGSHMLAVTIFYGTLIFMYLQPSSNHSLDTDKMASVFYTVIIPMLNPLIYSLRNKEVKDALKKLIASKNQMLSS
Potential odorant receptor.
Q8VGR9
P02836
HMEN_DROME
Segmentation polarity homeobox protein engrailed
Sophophora
MALEDRCSPQSAPSPITLQMQHLHHQQQQQQQQQQQMQHLHQLQQLQQLHQQQLAAGVFHHPAMAFDAAAAAAAAAAAAAAHAHAAALQQRLSGSGSPASCSTPASSTPLTIKEEESDSVIGDMSFHNQTHTTNEEEEAEEDDDIDVDVDDTSAGGRLPPPAHQQQSTAKPSLAFSISNILSDRFGDVQKPGKSMENQASIFRPFEASRSQTATPSAFTRVDLLEFSRQQQAAAAAATAAMMLERANFLNCFNPAAYPRIHEEIVQSRLRRSAANAVIPPPMSSKMSDANPEKSALGSLCKAVSQIGQPAAPTMTQPPLSSSASSLASPPPASNASTISSTSSVATSSSSSSSGCSSAASSLNSSPSSRLGASGSGVNASSPQPQPIPPPSAVSRDSGMESSDDTRSETGSTTTEGGKNEMWPAWVYCTRYSDRPSSGPRYRRPKQPKDKTNDEKRPRTAFSSEQLARLKREFNENRYLTERRRQQLSSELGLNEAQIKIWFQNKRAKIKKSTGSKNPLALQLMAQGLYNHTTVPLTKEEEELEMRMNGQIP
This protein specifies the body segmentation pattern. It is required for the development of the central nervous system. Transcriptional regulator that represses activated promoters. Wg signaling operates by inactivating the SGG repression of EN autoactivation.
P02836
Q2KBW4
KUP1_RHIEC
Probable potassium transport system protein kup 1
Rhizobium
MSDESHPHERHMTPRKLFYLALGSVGVVYGDIGTSPLYAFREALKPVAHDGVTRFEVISLISLMIWALTIIVTIKYVLFLLRADNDGEGGTLSLLALLMKTANGHTALLMLLGLMGAALFLGDAMITPALSVLSAVEGLKLVTPSLAEYIVPISVVILALLFVVQSRGTGAVAKFFGPITAVWFLVMAAAGISHISDDFGILAAFNPYYAVSFLLHEGFYGVVVLGAVFLTVTGAEALYADLGHFGRRPIQWAWFLLVFPALTLNYLGQGALVLGKPETMSDPFYLMYPQWALLPVVILATAATIIASQAVITGAFSLVRQGINLGFLPRMEILFTSETNTGQIFLPSVNAVLFFGVIFLVLSFKTSDALATAYGISVTGAMVVTSIMAFEFVRARWNWSLPVAVIALAPLVVLEMIFLGANLLKIHDGGYIPILIATAFTVVMWTWRRGTAILMEKTRHTDIPLASFVSSIERKSEHSPAQVPGTAIFLTSDPESAPAALLHNLKHNHVLHDRNVILTIRTVNKPRVPSHDRYKVEPISERFSRVELLFGFMESQNVSQALATLRKTGLKFDIMSTSFYLGRRKLVPDAKSGMPYWQDRLYIALANAAANPSDYFRLPANRVVELGSHVII
Transport of potassium into the cell.
Q2KBW4
A1SX61
DNLJ_PSYIN
Polydeoxyribonucleotide synthase [NAD(+)]
Psychromonas
MITLSKSQEEVFKKLAVELSMSKLIEACNKSVDFSSLNSNEQLDVLKVTNAFYRSAEQIINDSTYDAFLSEFSTYNPDHPYLLTVEPEVLADSKTVPLPKKMLSTDKAYSFEEIKKWIDRLLKAAIEVGVSESEIQIKVTPKLDGYAAYDDGISLYTRGDGARGQDITRAFNKGLQVANNGDRGLGPGEIVIKKSYFDTVLSDKFENSRNIQAAIIAEKKVDESIQKAIDVGACVFFPFLSLENWIGHYTEILVDFESIVEKMWSAVDYDIDGVVLEVTNETLKEHMGATRHHHRWQIAFKVNAESAEVKVLNVTPQTSRTGRVTPVAELEPTKLSGATISRATVHHYNMVKTNGVGPGAIVQLVRSGLVIPKIEKVIKAVEPQLAKECPSCGTHLIWESDHLVCPNKTDCPAQTENTLVHFFKTLGNNDGFGPKVIEKLHEFGIKKIHEIYELKQESFVSFGFGDKTAQNLVEQLQVSRDVEIEDWRFLAAFGVSRLAGGNCEKLLQHHSLDSLFEATVEDLVQLDGFAQVSADAIVEGLANIKEEFLKLSALNFNLTITPKASEKSPGETPVFGKIIVFTGAMTQGSRGDMEKQAKALGAKVAKSVTGKTSLLVTGDKVGANKINAARDKGVQVLSELDYLALISTY
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
A1SX61
Q06328
YPQ2_YEAST
PQ-loop repeat-containing protein 2
Saccharomyces
MSCSNGIWPTVSNLCGSLSFFTSVISLFPQIIETYRDKSVDGLSPYFLLAWLCGDITSLIGAKLTGQLLFQILLAIYFLLNDSFVCGQYYYYGVLHENKLATVGHEPKPLLPELVENGELLREEEDMIQGGSSAESPRSSRRRSAITAALAIAHTISTASAYPLNVGSTQSQVGPPGDGKNSQLGTILSWIGASFYVGARIPQLIKNYNRKSTDGLSPFLFATTLLCNITYNLSIFTSCRFLDNQNKREFIVNELPFIFGSAGTIAFDLIYFYQYYILYATDMQLRELERELYSPEEDSAAQLVTERTSLLSGETQT
May function as an amino acid transporter mediating the export of cationic amino acids from the vacuole.
Q06328
A5UKS9
EF1B_METS3
aEF-1beta
Methanobrevibacter
MGEVVATLKIMPESPDVDLEALKAAIQAAMPAEAEFHKIEEEPIAFGLVALNLIFIIEDGEGGTESTEEAMAKLADVASVEITDTRRLM
Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus allowing the regeneration of EF-1-alpha/GTP that could then be used to form the ternary complex EF-1-alpha/GTP/AAtRNA.
A5UKS9
Q9CXK8
NIP7_MOUSE
kDa93
Mus
MRPLTEEETRVMFEKIAKYIGENLQLLVDRPDGTYCFRLHNDRVYYVSEMMLKLAANISGDKLVSLGTCFGKFTKTHKFRLHVTALDYLAPYAKYKVWVKPGAEQSFLYGNHVLKSGLGRITENTSQYQGVVVYSMADIPLGFGVAAKSTQDCRKVDPMAIVVFHQADIGEYVRHEETLT
Required for proper 34S pre-rRNA processing and 60S ribosome subunit assembly.
Q9CXK8
Q3SVP3
UBIG_NITWN
3-demethylubiquinone 3-O-methyltransferase
Nitrobacter
MTMQVDPSANSSAASSAAPGTTVDRAEIEKFSKLSQEWWDPTGKMAPLHRINPLRLQFIRDAACRKFDRNARSLNCLAGLRLLDIGCGAGLLCEPFTRLGAQVIGVDPSASNIAAAKLHAEKAHLSIDYRCTTVEDMDVRERFDIILAMEVVEHVADVGLFLDRCAAMLKPGGMMAASTLNRNWKSFALGIVAAEYVLRWLPRGTHQWDKFVTPDELARHFERNGLGITEQSGVVYSPFGDRWSLSSDMDVNYMVVAEAVG
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Q3SVP3
Q28641
MYH4_RABIT
Myosin heavy chain, skeletal muscle, juvenile
Oryctolagus
MSSDADMAIFGEAAPYLRKSEKERIEAQNKPFDAKSSVFVADPKESFVKATVQSREGGKVTAKTEAGATVTVKEDQVFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAHFSLVHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAFLFTGTAAAEAEGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQLITRTQAMCRGFLARVEYKKMVERRESIFCIQYNIRAFMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKEEFEKTKESLAKAEAKRKELEEKMVALMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALAMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQVSELKTKEEEHQRLINDLSAQRARLQTESGEFSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKHKYEETHAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKVKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEAEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE
Muscle contraction.
Q28641
B7K5H5
SYI_RIPO1
Isoleucyl-tRNA synthetase
Rippkaea orientalis
MTEPKSYKDTVNLPQTDFSMRANAVQREPEIQQFWTENCIYEQLSQNNPEDLFILHDGPPYANGSLHMGHALNKTLKDIINKYKLLRGHKVRYVPGWDCHGLPIELKVLQSMKSEEREGLTPLKLRRKARDFALKTQQEQAEGFKRYGVWGDWENPYLTLTPEYEAAQIGVFGQMALKGYIYRGLKPVHWSPSSRTALAEAELEYPEGHTSQSIFAAFPIIKSSKDAQEILDPFLSNLGVAIWTTTPWTLPGNLAVALNPELTYAIVEQTSNLCNYQYIIVAADLVERLSATFSTELTVKATLPGQILEHTIYRHPLYDRESEIVIGGDYVTTESGTGLVHTAPGHGQEDYIVGQRYGLQVLSPVDDAGNFTEEAGQFSGLNVLKDANQAIINELKNKGSLLKEEPYLHKYPYDWRTKKPTIFRATEQWFASVEGFREAALEAIKSVNWIPPQGENRITPMVSDRSDWCISRQRSWGVPIPVFYNEETNEPLLTEETINHVQAIIAKQGSDAWWELSIEELLPEQYKKDAHKYRRGTDTMDVWFDSGSSWAAVAKQREELKYPVDIYLEGSDQHRGWFQSSLLTSVAVNGIAPYKTVLTHGFVLDEKGHKMSKSLGNIVDPLVIINGGKNQKQEPPYGADVLRLWVSSVDYSSDVPIGQTILKQLSDVYRKIRNTARFLLGNLHDFDPEKDTVSYDQLPELDQYMLHRITEVFTEVTDAFEKFQFFRFFQTVQNFCVVDLSNFYLDIAKDRLYISDTNSLRRRSCQTVLKVAVESLAKAIAPVLCHMAEDIWQFLPYKTPYQSVFASGWVEMQKQWERPELTASWGKLRQIRTEVNKVLEQARNEKAIGSSLDAKVLLYVSDQDFKKQLESFNPNDSLKGNQVDELRYLVLASQVELVDSLEAIKKADYQSESELVSVGVVKAEGQKCDRCWNYSTKVGEFSDDPTICERCNAALVGEF
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).
B7K5H5
A7S338
LIS1_NEMVE
Lissencephaly-1 homolog
Nematostella
MVLTPRQKEELNKAIADYLHQCGFEDTLNAFKQDANMPGELDKKYTGLLEKKWTSVIRLQKKVMDLETRLSEAEKEVHHGGGPKKTRSPEDWIPRPPERYTLTGHRSPITKVLFHPVYSVMVTSSEDATVKVWDYETGDFERTLKGHTDAVQDLAFDHTGKFLASSSADMTIKLWDFQGFECIRTLHGHDHNVSSISFLPSGDHLVSASRDKTIKMWEIATGYCVKTFQGHGEWVRRVRPNADGSLIASCSNDQTIRVWVVASRECKCDLRDHDHVIEDLNWAPESATPVINEAAGVEGGKKAMSPGPFLVSASRDKSIKIWDVSAGVCLVTLVGHDNWVRAVMFHPGGKFIVSCSDDKTLRIWDYKNKRCAKTLVAHEHFVTTLDFHKSAPFVATGSVDLTLKVWECR
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes.
A7S338