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
|
|---|---|---|---|---|---|---|
P15223
|
SCX1_CENNO
|
Toxin II.14
|
Centruroides
|
MNSLLMITACFVLIGTVWAKDGYLVDAKGCKKNCYKLGKNDYCNRECRMKHRGGSYGYCYGFGCYCEGLSDSTPTWPLPNKTCSGK
|
Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
|
P15223
|
Q9ZHZ4
|
RBL2_HALNC
|
Form II RuBisCO
|
Halothiobacillus
|
MDQSARYADLSLKEEDLIAGGKHILVAYKMKPKAGHGYLEASAHFAAESSTGTNVEVSTTDDFTKGVDALVYYIDEATEDMRIAYPMDLFDRNVTDGRMMLVSVLTLIIGNNQGMGDIEHAKIHDIYFPERAIQLFDGPSKDISDMWRILGRPIENGGYIAGTIIKPKLGLRPEPFAAAAYQFWLGGDFIKNDEPQGNQVFCPLKKVLPLVYDSMKRAQDETGQAKLFSMNITADDHYEMMARADFGLETFGPDADKLAFLVDGFVGGPGMITTARRQYPNQYLHYHRAGHGMITSPSAKRGYTAFVLAKISRLQGASGIHVGTMGYGKMEGEGDDRNIAYMIERDEAQGPVYFQKWYGMKPTTPIISGGMNALRLPGFFENLGHGNVINTAGGGSYGHIDSPAAGAISLKQAYECWKAGADPIEFAKEHKEFARAFESFPKDADAIFPGWREKLGVHK
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.
|
Q9ZHZ4
|
P20853
|
CP2A7_HUMAN
|
Cytochrome P450 IIA4
|
Homo
|
MLASGLLLVALLACLTVMVLMSVWQQRKSRGKLPPGPTPLPFIGNYLQLNTEHICDSIMKFSECYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVAFSNGERAKQLLRFAIATLRDFGVGKRGIEERIQEESGFLIEAIRSTHGANIDPTFFLSRTVSNVISSIVFGDRFDYEDKEFLSLLSMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFKLLQGLEDFIAKKVEHNQRTLDPNSPQDFIDSFLIHMQEEEKNPNTEFYLKNLMMSTLNLFIAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRTKMPYMEAVIHEIQRFGDVIPMSLARRVKKDTKFRDFFLPKGTEVFPMLGSVLRDPSFFSNPQDFNPQHFLDDKGQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVVFATIPRNYTMSFLPR
|
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
|
P20853
|
Q733D6
|
PHNC_BACC1
|
Phosphonates import ATP-binding protein PhnC
|
Bacillus cereus group
|
MIEFRNVSKVYPNGTKGLNHINLKIQKGEFVVMVGLSGAGKSTLLRSVNRLHEITEGEIMIEGESITAAKGKGLRRMRRDIGMIFQSFNLVKRSTVLKNVLAGRVGYHSTLRTTLGIFPKEDLELAFQSLKRVNILEKAYARADELSGGQQQRVSIARALAQEAKIILADEPVASLDPLTTKQVLDDLKKINEDFGITTIVNLHSIDLARQYATRIIGLHAGEIVFDGLVEEATDEKFAEIYGDVAQKSELLEVAVK
|
Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
|
Q733D6
|
A8LQ30
|
BCHL_DINSH
|
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
|
Dinoroseobacter
|
MSPLDTAPPVLKGEDGEGSVQVHQDDSMKIEGAKVFSVYGKGGIGKSTTSSNLSAAFSKLGKRVLQIGCDPKHDSTFTLTGSLVPTVIDILKEVDFHAEELRPEDFVFEGFNGVKCVEAGGPPAGTGCGGYVVGQTVKLLKQHHLLEDTDVVIFDVLGDVVCGGFAAPLQHADRALIVTANDFDSIYAMNRIIAAVQAKSKNYSVRLAGCVANRSRETDEVDRYCKTVGFNRIAHMPDLDAIRRSRLKKKTLFEMEDAEDVVQVRKEYIRLAETLWNGTEPLAPAPLPDREIFELLGFD
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
|
A8LQ30
|
B2S6E8
|
COBQ_BRUA1
|
Cobyric acid synthase
|
Brucella
|
MARAIMFQGTGSDVGKSVLVAGLCRVARNRGLKVRPFKPQNMSNNAAVSDDGGEIGRAQWLQALACGVPSSVHMNPVLLKPQTDMGSQLIVQGQVRGEARGRYYQELKPQLMAAVMESFAKVGDGADLVLVEGAGSPAEINLRAGDIANMGFATHADVPVVLVGDIDRGGVIASLVGTHTILPQEDRAMVRGFLINKFRGDISLFDDGLAAITRFTGWRSFGVVPWLKAVSRLPAEDSVVLERAVRGDKKALIVAVPMLPRIANFDDLDPLKAEPAVEVVMVPPGSSLPADAGLVVLPGTKSTIADLLALRENGWDRELVAHVKRGGHVLGICGGFQMLGRRISDPAGIEGNVRDIEGLGLLDIETMTEPEKVVRNVEAVSLLHDEPLEGYEIHIGRTSGPDMARPFARIGDHDDGAVSPDGRIMGTYLHGIFSADRFRHHFLRALGVEGGQMNYRESVEEALGELAEGLEASLDIDGLFALA
|
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
|
B2S6E8
|
B5FTK8
|
NUDL_SALDC
|
Uncharacterized Nudix hydrolase NudL
|
Salmonella
|
MDTSRLTLDHFLSRFQLLRPQMTHKTLNQRQAAVLIPVVRRPQPGLLLTQRAIHLRKHAGQVAFPGGAVDSTDASLIAAALREAQEEVAIPPQAVEVIGVLPPVDSVTGFQVTPVVGIIPPNLPWRASEDEVSAVFEMPLAQALQLGRYHPLDVYRRGNSHRVWLSWYEHYFVWGMTANILRELALQIGVKP
|
Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.
|
B5FTK8
|
A7FLJ3
|
NQRF_YERP3
|
NQR-1 subunit F
|
Yersinia
|
MEIILGVVMFTLIVLALTVMILFAKSKLVNTGDITVEINEDEDKSFTAPAGDKLLNMLSSHGIFVSSACGGGGSCGQCRVTIKEGGGDILPTELSHISKREAKEGCRLACQVNVKQNLKIELPEEIFGVKKWTCEVISNDNKATFIKELKLKIPDGDVVPFRAGGFIQIEAEPHTVKYADFDVPTEYRGDWDKFNLFRFESVVTEPTVRAYSMANYPEEHGIILLNVRIATPPPSVPDAPPGIMSSYIWSLKPGDKVVISGPFGEFFAKDTDAEMVFIGGGAGMAPMRSHIFDQLKRLHSKRKISFWYGARSRREMFYEEDFDQLQAENDNFRWHVALSDPQPEDNWTGYTGFIHNVLLENYLKDHPAPEDCEFYMCGPPMMNAAVIKMLKDLGVEDENIMLDDFGG
|
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway.
|
A7FLJ3
|
P46467
|
VPS4B_MOUSE
|
Suppressor of K(+) transport growth defect 1
|
Mus
|
MASTNTNLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGDKAKQSIRAKCTEYLDRAEKLKEYLKKKEKKPQKPVKEEQSGPVDEKGNDSDGEAESDDPEKKKLQNQLQGAIVIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSAIRRRFEKRIYIPLPEAHARAAMFRLHLGSTQNSLTEADFQELGRKTDGYSGADISIIVRDALMQPVRKVQSATHFKKVRGPSRADPNCIVNDLLTPCSPGDPGAIEMTWMDVPGDKLLEPVVSMWDMLRSLSSTKPTVNEQDLLKLKKFTEDFGQEG
|
(Microbial infection) In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (lentiviruses).
|
P46467
|
B0KCI8
|
RL11_THEP3
|
50S ribosomal protein L11
|
Thermoanaerobacter
|
MAKKVAAVVKIQLPAGKATPAPPVGTALGPHGVNIMAFCKEFNERTAKDAGLIIPVVITIYADRSFSFITKTPPAAVLLKKAAGIESGSPQPNKQKVGKITREQLREIAEIKMKDLNASDIEAAMRMIAGTARSMGIEIV
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
B0KCI8
|
P0C7N5
|
OR8U9_HUMAN
|
Olfactory receptor 8U9
|
Homo
|
MTQINCTQVTEFILVGLTDRQELKMPLFVLFLSIYLFTVVGNLGLILLIRTDEKLNTPMYFFLSNLAFVDFCYSSVITPKMLGNFLYKQNSISFNACAAQLGCFLAFMTAECLLLASMAYDRYVAICNPLMYMVVMSPGICIQLVAAPHSYSILVALFHTILTFRLSYCHSNIVNHFYCDDMPLLRLTCSDTRFKQLWIFACAGIMFISSLLIVFVSYMFIISAILRMHSAEGRQKAFSTCGSHMLAVTIFYGTLIFMYLQPSSSHALDTDKMASVFYTVIIPMLNPLIYSLQNKEVKEALKKIIINKN
|
Odorant receptor.
|
P0C7N5
|
Q6NTP2
|
IREB2_XENLA
|
Iron-responsive element-binding protein 2
|
Xenopus
|
MTENPFHYLVETLSGTSDKTFFNVSKLKATEYDSLPYCIRVVLEAVVRNCDGVLVKEQDAFNILNWKTKCEFKEIPFLPARVMLQDFTGIPAMVDFAAMRDAISKFGKDPKQVNPACPTDLIADHSLQLDFTKCIAAQNVSGLPAVETHRPTTTPGKTPGRKAQCRSQGGCKGACDLGAANGSSREQIENTPMLCPFHLQPIAEPETALKSLEIEFNRNKERLQFFKWCSKAFQNVAVIPPETGTVHQVNLEFLSRVVMEEKGCIYPDSVLGTDSHTTMVNGLGILGLGVGGIESEAAMLGVPITLTLPEVVGCELTGTINPIATSIDVVLSITKHLKQAGVAGTFVEFFGNGVSQLSVADRTTIANMCPEYGATVAFFPVDSVTLQHLKQTGVDLQCVKTFENYLKAVKLLRQENVQQPLYSKVLQINLNSIVPYVSGPKRPQDRISVMDMKKDFETCLKEKTGLKGFQIPEEKQNIMVPVTYGNSEYSLSHGCVVIAAVTSCTNNCNPSVMLTAGLLAKKAVEAGLTVKPYIKTSLSPGSGTVTYYLSASGVLPYLSKLGFDIIGYGCARCVGNTNPLPESIVTAIKEGELVACGVFSGNKHFEGNRCSCVCANYLASPPLVVAYALAGTVNIDLQTEPLGENAQGKKIFLQDIWPSREEVLEVEETLVIPSMFSELKLKIEKQNTRWNLLDAPESTLFPWDLRSTYIRSPPFFHKLEKIPPPIQPIERAYVLLYLGDSVTTDHMSPAGSIPRTSPAAKYLMQKNLVPREFNSYGARRGNDAVMTRGTFANMKLFNKLVGKTGPKTIHLPSGQTMDVFDAAELYQRSEIPLIIIAGKKYGLGNSRDWAAKGPFLLGVRVVIAESYEKIHKDHLVGMGIAPLQFLSGENAETLGLSGKEQYSLSLPVDLTPGHKVEIKTNTGKIFHVIAAFDNEAEVTLYKHGGILSYVARKYL
|
RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA.
|
Q6NTP2
|
Q5FAF7
|
SYY_NEIG1
|
Tyrosyl-tRNA synthetase
|
Neisseria
|
MSVIQDLQSRGLIAQTTDIEALDALLNEQKIALYCGFDPTADSLHIGHLLPVLALRRFQQAGHTPIALVGGATGMIGDPSFKAAERSLNSAETVAGWVGSIRSQLTPFLSFEGGNAAIMANNADWFGSMNCLDFLRDIGKHFSVNAMLNKESVKQRIDRDGAGISFTEFAYSLLQGYDFAELNKRHGAVLEIGGSDQWGNITAGIDLTRRLNQKQVFGLTLPLVTKSDGTKFGKTEGGAVWLNAKKTSPYQFYQFWLKVADADVYKFLKYFTFLSIEEIGVVEAKDKASGSKPEAQRILAEEMTRLIHGEEALAAAQRISESLFAEDQSRLTESDFEQLALDGLPAFEVSDGINAVEALVKTGLAASNKEARGFVNAKAVLLNGKPAEANNPNHAAERPDDAYLLIGEYKRFGKYTILRRGKRNHALLVWK
|
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).
|
Q5FAF7
|
Q0TB40
|
NEPI_ECOL5
|
Purine ribonucleoside efflux pump NepI
|
Escherichia
|
MSEFIAENRGANAITRPNWSAVFSVAFCVACLIIVEFLPVSLLTPMAQDLGISEGVAGQSVTVTAFVAMFASLFITQTIQATDRRYVVILFAVLLTLSCLLVSFANSFSLLLIGRACLGVALGGFWAISASLTMRLVPPRTVPKALSVIFGAVSIALVIAAPLGSFLGELIGWRNVFNAAAAMGVLCIFWIIKSLPSLPGEPSHQKQNTFRLLQRPGVMAGMIAIFMSFAGQFAFFTYIRPVYMNLAGFGVDGLTLVLLSFGIASFVGTSLSSFILKRSVKLALAGAPFVLALSALVLTLWGSDKIVATGVAIIWGLTFALIPVGWSTWITRSLADQAEKAGSIQVAVIQLANTCGAAIGGYALDNIGLTSPLMLSGTLMLLTALLVTAKVKMKKS
|
Involved in the efflux of purine ribonucleosides, such as inosine and guanosine.
|
Q0TB40
|
O44390
|
ACO11_TRINI
|
Acyl-CoA Delta-11 desaturase
|
Trichoplusia
|
MAVMAQTVQETATVLEEEARTVTLVAPKTTPRKYKYIYTNFLTFSYAHLAALYGLYLCFTSAKWETLLFSFVLFHMSNIGITAGAHRLWTHKTFKAKLPLEIVLMIFNSLAFQNTAITWAREHRLHHKYSDTDADPHNASRGFFYSHVGWLLVKKHPDVLKYGKTIDMSDVYNNPVLKFQKKYAVPLIGTVCFALPTLIPVYCWGESWNNAWHIALFRYIFNLNVTFLVNSAAHIWGNKPYDKSILPAQNLLVSFLASGEGFHNYHHVFPWDYRTAELGNNFLNLTTLFIDFCAWFGWAYDLKSVSEDIIKQRAKRTGDGSSGVIWGWDDKDMDRDIKSKANIFYAKKE
|
Catalyzes the formation of Delta(11) fatty acyl precursors in the pheromone gland.
|
O44390
|
P67702
|
HIGA_ECOL6
|
Antitoxin HigA
|
Escherichia
|
MIAIADILQAGEKLTAVAPFLAGIQNEEQYTQALELVDHLLLNDPENPLLDLVCAKITAWEESAPEFAEFNAMAQAMPGGIAVIRTLMDQYGLTLSDLPEIGSKSMVSRVLSGKRKLTLEHAKKLATRFGISPALFID
|
Antitoxin component of a type II toxin-antitoxin (TA) system. Functions as an mRNA interferase antitoxin.
|
P67702
|
Q9D676
|
CLC2G_MOUSE
|
Osteoclast inhibitory lectin-related protein 1
|
Mus
|
MNITRASLPMLNTTCSCRREKWNFLGRYEGTFDYWIGLHRASSKHPWMWTDNTEYNNMFVYHMNAQCLKKPEEGESSPGTGGVHSYKILQRNSLRAISPESSAKLYCCCGVIMVLTVAVVALSVALPATKTEQILINKTYAACPKNWIGVGNKCFYFSEYTSNWTFAQTFCMAQEAQLARFDNEKELNFLMRYKANFDSWIGLHRESSEHPWKWTDNTEYNNMIPIQGVETCAYLSGNGISSSRHYIPRIWICSKLNNYSLHCPTPVPV
|
Inhibits osteoclast formation.
|
Q9D676
|
Q5NRC5
|
LEUC_ZYMMO
|
Isopropylmalate isomerase
|
Zymomonas
|
MTKNPRTLYEKIWDAHIVERREDGSALIYIDRHLVHEVTSPQAFEALRQAGRPLRRPDRTLAVPDHNVPTTARVDSEGHLLPIADPQSAKQLAALAKNAPEFGVRYISATDPEQGIVHVVGPEQGFTLPGTTLVCGDSHTAAHGALGALAFGIGTSEVEHVMATQTLILTPAKTMEVRVEGKLSPDVSAKDLILHIIHSLGTAGGTGYAIEYTGEAIRNLSIEERLTVSNMSIEAGARTGLIAADEKTFAYLFGRPMAPKGADWEKAVQWWKSLATDKGAVYDKTVIIKAEDVQPSVTWGTSPEDVVPITGVVPDPASFADPAKQAAARRSLEYMGLEPGQKMEGLAVENVFIGSCTNSRIEDLRAAASVVWGRHVADNVKQALVVPGSGLVKRQAEAEGLDEVFKAAGFEWREPGCSMCLAMNPDKVPAGERCASTSNRNFVGRQGPGARTHLVSPAMAAAAAVTGHLTDLRHLEPVKMGEKA
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
Q5NRC5
|
Q02721
|
TO6BL_YEAST
|
Meiotic recombination protein REC102
|
Saccharomyces
|
MARDITFLTVFLESCGAVNNDEAGKLLSAWTSTVRIEGPESTDSNSLYIPLLPPGMLKIKLNFKMNDRLVTEEQELFTKLREIVGSSIRFWEEQLFYQVQDVSTIENHVILSLKCTILTDAQISTFISKPRELHTHAKGYPEIYYLSELSTTVNFFSKEGNYVEISQVIPHFNEYFSSLIVSQLEFEYPMVFSMISRLRLKWQQSSLAPISYALTSNSVLLPIMLNMIAQDKSSTTAYQILCRRRGPPIQNFQIFSLPAVTYNK
|
Required for formation of the SPO11-mediated double-strand breaks (DSBs) that initiate meiotic recombination. May mediate the interaction between SPO11 subunits during meiosis. Also needed for homolog chromosome pairing, synaptonemal complex formation, and for the proper timing of the first meiotic division. Not required for mitosis and mitotic DNA repair mechanisms.
|
Q02721
|
A1U2U9
|
RLMD_MARN8
|
23S rRNA(m5U1939)-methyltransferase
|
Marinobacter
|
MSKRRRKVLPKEPVRCEIETLSHDGRGIARADGKTQFVDGALPGETVMAKMVRTRSRFDELRTTEVLEAAPDRQQPPCEFADLCGGCSLQHMSADAQIRFKENTLREHFAHFGGIEPEQWVAPMRSPDSLGYRRKARLGVRYVKARESVLVGFREKRNSFLTDIDRCVVLDPRIGERIEPLRELLHGMAAFDRIAQVEVACGDDTAAMVFRNMDDLVPDDREKLIAFGQAHDLHIYLQPKGPDTVHRIWPESGGRDDERLTYRMDEFDLTMAFHPMDFTQVNAGINRNMVHRAVEWLDVQPGERVLDLFCGLGNFTLPLARKGGQVVGVEGDDAMVVRGRENARLNDLSNVEFHGADLHGDFTGQSWAKEGFDKILIDPPRSGAEEICKYLTAFGANRIVYVSCNPATLARDAGVMVRNGYRLVQAGVMDMFPHTTHVESIALFERSAD
|
Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
|
A1U2U9
|
Q0TMS8
|
ECFA2_CLOP1
|
Energy-coupling factor transporter ATP-binding protein EcfA2
|
Clostridium
|
MSIKIENLNHIYMPKTPFEKIALNNINCEIEDGEFVALIGHTGSGKSTFIQHLNGLLSPTSGNIIVDGVNIADKKVKLSDIRKKVGLVFQYPEYQLFEETIEKDIEYGPRNLGISEEEISKRVKKSMEMVGLDYETYKDKSPFDLSGGQKRRVAIAGVIAMEPKVLILDEPTAGLDPKGREDILAQIRLLHKEYGMTIIMVSHSMEDVAKIADRVIVMNSGEIVLDGKIAEVFKEVETLEKIGLAVPQVTYLIRELRNKGFNISEEIFTISQAKEALLEIIRNNN
|
ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
|
Q0TMS8
|
Q6L0A8
|
MPTA_PICTO
|
GTP cyclohydrolase IV
|
Picrophilus
|
MIELKDVQGFRPDYEIPIKRAGIKSFKRRVKLNYNNESFDSYVDVSISVSLNPDRKGLDMSRTIESVRSSYNLNDVAYDIYNDLFSRINYSSSGYVNVSFDFYYNNKIYPVSLIAEGDKNDVKRYVEVSAEGMTVCPCAMETIRSIMLYDYNVSYGDIGISHNQRNKASLKIQYIKDAHLERLIDILESSFSYPVRNMLKRYDEGKMIIEAHKRPKFVEDVVREIAYKAAFMEPEMNLYMDVRSESFESIHPHNAYAEIEDYTANIRSYLKNR
|
Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin.
|
Q6L0A8
|
A2SKL7
|
ERPA_METPP
|
Putative iron-sulfur cluster insertion protein ErpA
|
Methylibium
|
MSAVAEHIATQMPAPIVFTDSAAGKVKELVEEEGNPELKLRVFVQGGGCSGFQYGFTFDEIVNDDDTKMEKNGVMLLIDAMSLQYLVGAEIDYKEDLEGAQFVIKNPNATTTCGCGSSFST
|
Required for insertion of 4Fe-4S clusters.
|
A2SKL7
|
Q5L8D5
|
RS4_BACFN
|
30S ribosomal protein S4
|
Bacteroides
|
MARYTGPKSRIARKFGEGIFGADKVLSKKNYPPGQHGNSRKRKTSEYGIQLREKQKAKYTYGVLEKQFRNLFEKAATAKGITGEVLLQMLEGRLDNIVFRLGIAPTRAAARQLVGHKHITVDGQVVNIPSYAVKPGQLIGVRERSKSLEVIANSLAGFNHSKYAWLEWDEASKVGKLLHIPERADIPENIKEHLIVELYSK
|
With S5 and S12 plays an important role in translational accuracy.
|
Q5L8D5
|
Q9CA40
|
NUDT1_ARATH
|
NADH pyrophosphatase
|
Arabidopsis
|
MSTGEAIPRVAVVVFILNGNSILLGRRRSSIGNSTFALPGGHLEFGESFEECAAREVMEETGLKIEKMKLLTVTNNVFKEAPTPSHYVSVSIRAVLVDPSQEPKNMEPEKCEGWDWYDWENLPKPLFWPLEKLFGSGFNPFTHGGGD
|
Mediates the hydrolysis of some nucleoside diphosphate derivatives. Its substrate specificity is unclear. In vitro, it can use NTP, dNTP, 8-oxo-GTP, 8-oxo-dGTP, dGTP, dATP, dTTP or dihydroneopterin triphosphate (DHNTP) as substrate. Has some NADH pyrophosphatase activity in vitro; however, such activity may not be relevant in vivo due to the high concentration of manganese used during the experiments. Plays an important role in protection against oxidative DNA and RNA damage by removing oxidatively damaged form of guanine.
|
Q9CA40
|
Q6N4T7
|
RL23_RHOPA
|
RRP-L23
|
Rhodopseudomonas
|
MKSIDPRHYDVIVAPVVTEKSTMASEHNKVVFKVQGGATKPQIKEAVEKLFDVKVKSVNTLVRKGKTKAFRGTFGTQSDVKRAVVTLEEGHRIDVTTGL
|
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
|
Q6N4T7
|
P11398
|
PYR1_MASLA
|
Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod
|
Mastigocladus
|
MAITAAASRLGTEPFSNAAKIELRSDASREEVEAVINAVYRHVLGNDYIMASERLVSAESLLRDGNLTVREFVRSVAKSELYKKKFFYNSFQTRFIELNYKHLLGRAPYDESEIVFHLDLYQNKGYDAEIDSYIDSVEYQNNFGDNIVPYYRGFETQPGQKTVGFNRMFRLYRGYANSDRAQIEGTKPRLARELATNKASSIVGPSGSNPAWGYRPSVDITPRKTLGNAVGENDRVYRIEVTGVRSPGYPSVRRSSYAIIVPYERLSEKIQQIHKLGGKIVSITSA
|
Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
|
P11398
|
Q7U8C3
|
DXR_PARMW
|
2-C-methyl-D-erythritol 4-phosphate synthase
|
Parasynechococcus marenigrum
|
MLGSTGSIGTQTLQIAEEFPEQFRVVALTAGQNLDLLVQQIQRHQPELVALANADLLPELQQRLDALGTDRKRPQLVGGPDGLNIAASWESADLVVTGIVGCAGLLPTLAAVRAGKDLALANKETLIAAGPVVLPELKKSGSRLLPADSEHSAIFQCLQGTPWAENARLSTGVPTPGLRRIQLTASGGAFRDWKAEDLENATVADATSHPNWSMGRKITVDSASLMNKGLEVIEAHYLFGLDYDHIEIVIHPQSIIHSMIELADSSVLAQLGWPDMKLPILYCLSWPSRLETPWRRLDLTEVGQLSFRAPDPAKYPCMQLAYAAGRAGGTMPAVMNAANEEAVAQFLEEKIHFLDIPVVIEAACERHKADLIAHPQLEDVLAVDQWARMAVREQVKRGTTRVPLAALAA
|
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q7U8C3
|
Q9U2G5
|
MRP7_CAEEL
|
Multidrug resistance protein mrp-7
|
Caenorhabditis
|
MLSSFCGDGHPFSTGLPNVSICAQHTVLVWVPAAFFLLTLPFLSAQCHLTAQRFARLPFSAHFIIKLLLVAFLAANSLATWCYVLFSKNSYAAAYYVYPGLWVLVWTGTFLVHLIRLRCGLVSSGIQHVTSLIFLLCGAPEFYQWIRMENSNSFPNDLTTTDSAQFLSIAYLSWYSALILYTFSLCFADPRGAKTDDEKASSKSAASPELQSSFLNRLTLWWFNSIPWTGARRDLEIDDIFELNERSGTEFLSELWESFWEPKRLKYIHDTSIWAKKDPSEQEKDPVVIPSVVSSLFMMFRWEFLLASTLKFVSDTMQFASPFLLHELLNFISAKNAPFWKGMALSILMFSVSELRSLILNGYFYIMFRMGTKIQTSLTAAVYKKTLLISNSARRDRTVGEIVNLMAIDVERFQMITPQIQQFWSCPYQITFALVYLFITLGYSALPGVVIMVIFVPMNIISSMIVRKWQIEQMKLKDERTKMVNEVLNGIKVVKLYAWEVPMEAYIDEIRTKELALIKKSAMVRNILDSFNTASPFLVALFSFGTFVLSNPSHLLTPQIAFVSLALFNQLRSPMTMIALLINQAVQAVVSNKRLKEFLVAEELDEKCVDRSVNIERSHNAVRVENLTASWDPEEAAGEKTLQDVDLTAPRNSLIAVVGKVGSGKSSLLQALLGEMGKLRGRIGVNGRVAYVPQQPWIQNMTLRDNITFGRPFDRKRYDQVLYACALKADIKILPAGDQTEIGEKGINLSGGQKARVSLARAVYQNLDVYLLDDPLSAVDAHVGRHIFEKVIGPNGLLREKTRILVTHGLTYTKMADEILVMLEGKIEESGTFEHLIKRRGLFFDFMEEYKSGSDNSSEAGGSQDDDFEAIGGEIQDYMNPEDVVLTVTNDLDETIRTPELTTQISTMSSPEKPPTGTSPAAATESQNKLIKKEGIAQGKVEIATYQLYVKAAGYLLSIAFIGFFIVYMTLQILRSFWLSAWSDEYDPDSPSAHPMAKGWRLGVYGALGFSETACFFVALLALVFVGQRASKNLHGPLIHNLMRSPMSFYDTTPLGRILNRCAKDIETIDMMLPMNFRYLVMCVLQVAFTLIVIIISTPLFAVVILPLALIYLIFLRYYVPTSRQLKRLESVHRSPIYSHFGETIQGAASIRAFGKVDEFRQDSGRILDTFIRCRYSSLVSNRWLAVRLEFVGNCIIFFAALFAVLSKEFGWITSPGVIGVSVSYALNITEVLNFAVRQVSEIEANIVSVERVNEYTNTPNEAPWRIEGREPAPGWPSRGVVKFDGYSTRYREGLDLVLHDISADVAAGEKIGIVGRTGAGKSSFALALFRMIEAAGGRIVIDDVEVSQIGLHDLRSNITIIPQDPVLFSGTLRFNLDPFFTYSDDQIWRALELAHLKHFAAGLPDGLLYKISEAGENLSVGQRQLVALARALLRHTRVLVLDEATAAVDVATDALIQETIREEFKECTVFTIAHRLNTIMDYDRIMVLDKGSILEFDTPDALMADKNSAFAKMVADAAEQDKHE
|
Negatively regulates cellular toxicity by mediating the export of environmental toxicants such as methylmercury out of the cell . Plays a role in inhibiting methylmercury-induced dopamine (DA) motor neuron degeneration . Not involved in Mn(2+)- or Al(3+)-associated toxicity .
|
Q9U2G5
|
P15802
|
AATA_PENCH
|
Acyl-coenzyme A:6-aminopenicillanic acid acyltransferase 29 kDa subunit
|
Penicillium chrysogenum species complex
|
MLHILCQGTPFEIGYEHGSAAKAVIARSIDFAVDLIRGKTKKTDEELKQVLSQLGRVIEERWPKYYEEIRGIAKGAERDVSEIVMLNTRTEFAYGLKAARDGCTTAYCQLPNGALQGQNWDFFSATKENLIRLTIRQAGLPTIKFITEAGIIGKVGFNSAGVAVNYNALHLQGLRPTGVPSHIALRIALESTSPSQAYDRIVEQGGMAASAFIMVGNGHEAFGLEFSPTSIRKQVLDANGRMVHTNHCLLQHGKNEKELDPLPDSWNRHQRMEFLLDGFDGTKQAFAQLWADEDNYPFSICRAYEEGKSRGATLFNIIYDHARREATVRLGRPTNPDEMFVMRFDEEDERSALNARL
|
Isopenicillin-N N-acyltransferase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic . AatA catalyzes the exchange of the alpha-aminoadipyl side chain of isopenicillin N for phenylacetic acid to yield penicillin . This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively . The penicillin biosynthesis occurs via 3 enzymatic steps, the first corresponding to the production of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin in the peroxisomal matrix (Probable).
|
P15802
|
A0S0B0
|
IL6_PAROL
|
Interleukin-6
|
Paralichthys
|
MASKHNADLSSAAMLAALLLCALGAPVEYEPTDSPAGDFSGEEQEVTPDLLSASPVWDLIIGVTAHHQKEFEDEFQQEVKYRFLNHYKLSSLPADCPSANFSKEACLQRLAEGLHTYMVLFKHVEKEYPSSSILLHARYHSGALIGLIKEKMRNPGQVTVPTSRQEQQLLQDMDNPSTFHRKMTAHNILRQLHNFLRNGKVAIRKREMPKQKRRKDDGIIPPIHPSYQMT
|
Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway. The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells.
|
A0S0B0
|
A0RTP4
|
PDXT_CENSY
|
Pyridoxal 5'-phosphate synthase glutaminase subunit
|
Cenarchaeum
|
MSGPSIGVLSLQGDVRENIGMIHTAISRAGVGGSVEQVNDASAIKELDGLIIPGGESTVIGGLAGGELLDVIRTKVRGGMPAFGICAGLILLSKGATDRTVGRTGQPLLDLLDVRVERNAFGRQKESFETELSMTSCGIEEFRGVFIRAPVITEAGPGVQVIAEYDNKKVAVQQGSVLGVSFHPELTNDPSLHQYFLKMCA
|
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.
|
A0RTP4
|
Q5DRC2
|
PCDG1_PANTR
|
Protocadherin gamma-A1
|
Pan
|
MKIQKKLTGCSRLMLLCLSLELLLEAGAGNIHYSVPEETDKGSFVGNIAKDLGLQPQELADRGVRIVSRGRMPLFALNPRSGSLITARRIDREELCAQSMPCLVSFNILVEDKMKLFPVEVEIIDINDNTPQFQLEELEFQMNEITTPGTRISLPFGQDLDVGMNSLQSYQLSSNPHFSLDVQQGADGPQHPEMVLQSPLDREEEAVHHLILTASDGGEPVRSGTLRIYIQVVDANDNPPAFTQAQYHINVPENVPLGTQLLMVNATDPDEGANGEVTYSFHNVDHRVAQIFHLDSYTGEISNKEPLDFEEYKMYSMEVQAQDGAGLMAKAKVLIKVLDVNDNTPEVTITSVTTAVPENFPPGTIIALISVHDQDSGDNGCTTCFIPGNLPFKLEKLVDNYYRLVTERTLDRELISGYNITITAIDQGTPALSTETHISLLVTDINDNSPVFHQDSYSAYIPENNPRGASIFSVRAHDLDSNENAQITYSLIEDTIQGAPLSAYLSINSDTGVLYALRSFDYEQFRNLQLKVMARDSGDPPLSSNVSLSLFVLDQNDNPPEILYPALPTDDSTGVELAPRSAEPGYLVTKVVAVDRDSGQNAWLSYRLLKASEPGLFSVGLHTGEVRTARALLDRDALKQSLVVAVQDHGQPPLSATVTLTVAVADRIPDILADLGSLEPSAKPNDSDLTLYLVVAVAAVSCVFLAFVIVLLAHRLRRWHKSRLLQASGGSLTGMQSSHFVGVDGVRAFLQTYSHEVSLTADSRKSHLIFPQPNYADTLISQESCEKKDFLSAPQSLLEDKKEPFSQQAPPNTDWRFSQAQRPGTSGSQNGDDTGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
|
Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
|
Q5DRC2
|
P59795
|
BPT_SPHEL
|
Aspartate/glutamate leucyltransferase
|
Sphingomonas
|
MTALSRFPRFFVTSPSPCPYLPGRQERKIFTELSGQQAGELNDALSRIGFRRSQSVAYRPSCAGCTACVSVRVVTEGFQPNATQRKLLKRYGDLEVTACKPWATGEQYELLKRYLDSRHPGGGMAAMDESDYADMVEQSPVSSYVIEYREPSVNGERGRLVGACITDQQGDGLSMIYSYFVTDDEARPGMGNFIIMDHILRARAAGLPYVYLGYWVKGSARMAYKTRYRPIEVLGPTGWALLEDEDMVGAMPSAVAAALA
|
Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
|
P59795
|
A0A348B794
|
STS29_POSPM
|
Terpene cyclase 29
|
Postia
|
MSAVTQVVETAIGCVIPSCIEFGSSMRIATSLGSPSVTQSPCVNRDVEDIARTARESIRFFLAELSIECVPYTQDPALEAQVASATRCWPDRERLAPHIRTGIVIAATAYAHNSLATRTLIALYTAIGVALDEPDILESANAIGFHHSLCTETSERPSAILDEWRRILARMWDHFPRFGASCILTSTLQFLNMTMLENETKGKVLNRTAMPFVEYRRMTDGFPEVYTAFIWEKGRFPDVQVYMQAIPNAMRFINFGNDILSFYKEEAAGETGTYIHDRARLTGLSSVETLREVVEETVSAWRQVCEILGEGIARDAWNSFVRGYVTFHVHNPRYRLSELL
|
Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to a single major terpene scaffold whose chemical structure is still unknown.
|
A0A348B794
|
A1AAB6
|
EMTA_ECOK1
|
Peptidoglycan lytic endotransglycosylase
|
Escherichia
|
MKLRWFAFLIVLLAGCSSKHDYTNPPWNAKVPVQRAMQWMPISQKAGAAWGVDPQLITAIIAIESGGNPNAVSKSNAIGLMQIKASTSGRDVYRRMGWSGEPTTSELKNPERNISMGAAYLNILETGPLAGIEDPKVLQYALVVSYANGAGALLRTFSSDRKKAISKINDLDADEFLDHVARNHPAPQAPRYIYKLEQALDAM
|
Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Preferentially cleaves at a distance of more than two disaccharide units from the ends of the glycan chain.
|
A1AAB6
|
Q46I99
|
GCST_PROMT
|
Glycine cleavage system T protein
|
Prochlorococcus
|
MKLLQTPLYQECKELGGKMVPFANWEMPVSFSGLIEEHNAVRKNVGMFDISHMGVVQLKGKNIKSALQNLVPSDVFRIGPSEACYTVFLKENGGIQDDLIIYDQGVLDTNEESIVLVINAARKESDIEWLSSNLFKKEITISEFMPEGALIAIQGPESISTLEKILEEPLSNLPRFGHRTITSNPNLINSQESIFIARTGYTGEEGFEFLSSPETAKSIWKSLIASGVTPCGLGARDTLRLEASMHLYGNDINLDTTPFEAGLGWLVHLEMPNDFIGRKALEKQAEVGTQKKLVGIQVLDKGIARKGYPVLYNSETVGIVTSGTWSPTLQKPIALAYVPSEIAKVNTQIEVEIRRKKHPAIIVKRPFYRKGF
|
The glycine cleavage system catalyzes the degradation of glycine.
|
Q46I99
|
B1WU69
|
HISZ_CROS5
|
ATP phosphoribosyltransferase regulatory subunit
|
Crocosphaera subtropica
|
MIHQPPAGARDLLPLEVVQKAWINDTLQQVFGQWGYQRIVTSTIERLDTLKAGGAIEDETVIQLHNNSREQLGLRPELTASVARAAVTRMANTSYPQRLCYRANVFRNPPSGHHGRQLEFYQAGVELLFSGGTLADAEILLLVAECLQKLQIPSWYLILGDAGLTRSLLSPFPEALRQEVRHCLATLDYVKLDNLSYPNEELKHRASLLFNLRGKPEDVLSKVVDLTLDQTGKHCLNNLKSLIELVNHSTSYKLPLTLDLSLIQTFDYYTGIIFKAIGQTNHKLQNLGQGGRYDQLLGVYHPQKKSAPGIGFSLNVGALHRCLLSTDILPQKPLLIDYLVVAKTSESQIEALKYAQQLRKDDNSLRVTIDLENRNEEEIKKYAQENGIKTIVWIEKGKEAIIN
|
Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
|
B1WU69
|
A8H745
|
GLMM_SHEPA
|
Phosphoglucosamine mutase
|
Shewanella
|
MKQRQFFGTDGIRGKVGAGKMTPELALKLGWAAGRVLSRSGTQKVIIGKDTRISGYLFESALEAGLSAAGLDVMLIGPMPTPAVAYLTRTFRAEAGIVISASHNPYYDNGIKFFANDGSKLDDEVELEIEAELEKPLTCVESHLLGKVNRIDDAAGRYIEYCKSHFPAEQTLSGLKIVVDCAHGATYHIAPSVFRELGAEVIAIGDKPNGLNINDKVGATSMGQICETVLAENADLGIALDGDGDRIMMVNRHGRVIDGDEILYILACDAQKRGVLRGGVVGTLMSNLGLDLALQALEIPFVRSKVGDRYVMELLKEHDWRIGGENSGHILNLDHGTTGDGIVAGILVLAAMQRQNASLEALTANITMLPQVLVNVRFEGDNDPLASEVVLAAQAEVEQKLGARGRVLLRKSGTEPLLRVMVEGDEQEAVTEYANYIADAVRNLV
|
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
|
A8H745
|
P41191
|
RL10_LIBAF
|
50S ribosomal protein L10
|
Liberibacter
|
MNRQEKSVEISELSKIFSSSGSVVVAHYKGISVAQIKDLRKKVREAGGGVKVAKNRLVKIAVSDTSLKGVSDLFVGQSLIVYSVDPIVAPKISVSFANDNKQFVVLGGILEKDILDQDSIKRIASLPNIDGIRSMIISAIQFNSTRLVNLLNAPQTKIVRAISAFVDKNQQS
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
P41191
|
B8D6X9
|
DNLJ_BUCAT
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Buchnera
|
MTSTKDKIEKLRKILLKYEYFYHTLNQSIISDAEYDYLFRQLYELELKNKELIPSDSPTQKVGSHILQKFKKIKHFSPMLSLENTFDVNGYLNFKKRIKKSIHNNEPLSFCCELKLDGVAISIIYEEGIFVRAATRGDGFEGENITSNARMIDSIPLKLKGIDIPKRLEIRGEVFMLKSNFIKLNKKYKLNQNKYFSNPRNAAAGSLRHIDPNITAERKLIFSCHGCDFFVKTNKELTTHYQRLMKCLSWGIPVNKEIVICSSDIEIIQFYKKIAQKRNFLDFDIDGIVIKVNSLELQKKIGSTTKSPRWAIAFKFSPKERITTLNDVKFQVGRTGVITPVAYFNPVYISGVMISKASLHNKNEIERLNLHFNDTITICRSGDVIPRLLNVIEIRRCDNAKKIIFPSFCPVCNTELLENIEEKLIRCHSGLTCDAQKKQALYHFFSKKSLYVVGLGPKIINELVEKGLVKNPIDFFYLKDIDLIQLKNVGKRKSIKIINSIKKCKKTTLKCFIYALGIPGVGEVVAGKIANYFIKLDKLMNSNILELNCISGVGKIISNNIFNYFSTISNREMVVKLIKQAGIFLNDQEIHKINSEKTYFFNKKIVLTGVFKSFSRIELKTILLSLGAKISNNISRKTDFLIYGNNFGSKFFRAKDLDVKIINQEELNSLIRIKEQ
|
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.
|
B8D6X9
|
Q93QY7
|
MPRF_STAXY
|
Multiple peptide resistance factor
|
Staphylococcus
|
MTKELRSKLFTILKIAFALTLFTIVAITLYKELSHINLKDAIKSFSKINRFWLVALFLSGGASIIVLSIYDVILAKTLKLKIGLAKTIRIGYIVNALNAVVGFGGFIGASVRFLFYKNTTDDKKALFHTISIVLISMLTGLSLLSILVVIHVFDISHIFTPYPWVKWLMYVVALFLPIFVVFTIIKPVQKTHRLLGVYCTIVSGVEWFVAALVLYMSMAIVGVQIPFATFMGIFILAALSGLISFIPGGFGTFDLVVLLGLKALNVNEEAIVLGLSLYRFAYYLFPVLIALILSTFEFRSTAKRYWEDSRILVPVKDMTSLLGSYQKDIIARIPSFAIALLLLFTSLVFFLNNLTIIYDGLYDPNHYIYYIIVSIHTCACLLLLLNVIGVYKLSKRAILFSIISVLFIFIATAYTYASFILLSWLTVIFILLLVFYRRARVIKRPFRYSKLLLSVITGAIILYINHLVIKSTFYSLEIYHIEMLTSILRYYFWITILLVAIIVGVIVWWFEYRYRSSNSRDNIATCESIIDKYNGNYLSHLMYSGDKKFFINDNKDAFVMYRYHNNTYIILGDPIGNSESFYSLLEAFYKEAEYLGYDIIFYQVTDKYMSLYHSFGNQFFKLGEEAVINLTSFTTSGKKKRGLRATLNKLDDLGYSFEVLEPPFSQQMITDLKAISDDWLADKNEMHFSVGSFDEHYISQAPIGVLKDNEQSVIAFCTLMPTYYNGVISVDLIRWKQDIELPLMDSLYLNMLLWSKDNNYEHFNMGMATLSNVGQIPYSFYGERIAGRVFEHFNGLYRFQGLRRYKEKFNPKWEPRFLVYRKHQSLWVSMLKVMRVIRKNN
|
Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides.
|
Q93QY7
|
B9KE78
|
GLMM_CAMLR
|
Phosphoglucosamine mutase
|
Campylobacter
|
MKLFGTDGVRGKAGEFLDSFLAMRLAMAAGIYFKDKALTNNILVGKDTRRSGYMIENAIVSGLTSIGYNVIEIGPMPTPAIAFLTEDMRCDAGIMISASHNPYYDNGIKFFDAHGNKLDEQAEAKIEEIYFNDKLIEEARTTKSQIGQAKRIDDVIGRYIVSIKNSFPKELTLKSLRVVLDVAHGASYKVAPTVFRELGADVIVINDKPNGLNINENCGALHPLNLALEVKKFRADVGFAFDGDADRLVVVDEKGEVAHGDSLLGVLALFLKKQGKLKSSVVSTIMSNGALKEFLTKYKIPHETCNVGDKYVLEKLKECGGNFGGEQSGHIIFSDYAKTGDGLVAALQFSALMLSEAKSASEILNQVKPYPQLLHNLKISEKKDLSKLAGLEELKKDLEKKGIASLFRYSGTENLIRLLLEAKDIKLLEKEMKVVESFFMKVLNA
|
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
|
B9KE78
|
Q02WZ5
|
PNP_LACLS
|
Polynucleotide phosphorylase
|
Lactococcus cremoris subsp. cremoris
|
MAKETFSIEFAGRTLTVETGQVAKQANGAVVVRYGDTTVLTAATMGKMATGDFFPLQVNYEEKMYAAGKFPGGFNKREARPSTDATLTARLIDRPIRPMFAEGFRNEVQVINTVLSYDENASGRVAAMFGSSLALAISDIPFDGPIAGVEVAYIDGKYVINPTVAEKESSSLELSVAGNINAINMVESGAKELSEEVMLGALLAGHNAVKELIEFQNEIVAKVGKEKAEVELLHVDEDLKAEVIAAYNSDLQKAVQVEEKLAREAATKAVKEAIISVYSAKYENDENLSIILRDLAEILEGMEHAEVRRLITEDKIRPDGRKIDEIRPLDAEIDFTPRSITHGTGLFTRGQTQALSTLTLAPMNEAQIIDGLNDEYKKRFMHHYNFPQYSVGETGRYGAPGRREIGHGALGERALEQVLPSLEEFPYAIRLVAEVLESNGSSSQASICAGTLALMAGGVPIKAPVAGIAMGLISDGTNYTVLTDIQGLEDHFGDMDFKVAGTREGITALQMDIKISGITPEILAEALAQAKTARFQILDVIEATIAQPREELAPSAPKIDTIMIPVDKIKVVIGKGGEQIDKIIAETGVKIDIDDEGLCSIFSSDQSAIDRAKEIIAELVREAKVGEVYEAKVVRIESFGAFVNLFGKQDAMVHISEMAWARTAKVEDVMKLGDVVKVKIMKIDDKGRVDASMRALVEKPEGYVEPERKPRERRDNKDRRNGNGFDRRNNDRNNHNNHNNNSGNHSFELRERKSHVDHEFPELSTKKPE
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
Q02WZ5
|
P73618
|
DEOC_SYNY3
|
Phosphodeoxyriboaldolase
|
unclassified Synechocystis
|
MEKSRQFDLAPYIDHAALDPATTREAIATCCAQALHHKFVAVCVYPSALSQAVELLRGKKVEICAVIGFPSGASTSGSKLYEAQEAAELGATELDVVINLGLLKDGNTEAVYNDIAPIVEATGLTVKAILEMGRLTESEKRLAAEICLDAGVQYLKTSTGWGKGATVADVRLLHQISQGRVGIKASGGIRTVEQAIALIEAGATRLGTSRGVELIQQQQQLWEQG
|
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
|
P73618
|
A0L4K6
|
SURE_MAGMM
|
Nucleoside 5'-monophosphate phosphohydrolase
|
Magnetococcus
|
MLILLTNDDGIASPGLQALKDALKERHDVVTLAPVKDMSGTAHAISRGEDIKLTRIAEYEVAINGTPTDCVMAGLRMVLRRPPDLLVSGINMGANVAEDLSYSATAGAAWEGALSGIPSMAVSLCGSAAPWHFESAIKVTHMVIRQWLENPLPPGTFLNVNVPNVPEYELKNPKPTRQGLRFNWPPPPVTAAGNPAFWDPTIPTPREEEFQLATDEEALRDGFTSVTALHCLFRHPHATERLKAWSLFR
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
|
A0L4K6
|
A7X5M5
|
UREF_STAA1
|
Urease accessory protein UreF
|
Staphylococcus
|
MIDHTHLRLFQFCDSQFPTGAFSHSFGLETYIQRNIIHDDHTFIAWLKMFLQEQLTYSDGLAMRLVYDALENDDTQKVLHIDKLMFVQNLPKETRVGAKQMGTRMVKLALELYNSPWIAWYHQQMQDKKAKLNPAICFTMLGHHLGVDIETIIDYYLYQNVSSLTQNAVRAIPLGQTAGQKIVTHMIPYIEETRKQIFELKEADFGMTAPGLELNQMAHENVNVRIFIS
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
A7X5M5
|
B9KMG1
|
PTH_CERSK
|
Peptidyl-tRNA hydrolase
|
Cereibacter
|
MKLFVGLGNPGARYAGNRHNIGYMAVEAIAADHGFGPWRARFQGLTSEGRLGSEQVLLLKPETFMNLSGQSVGEAMRFYKLTPADVIVFHDELDLAPGKLRLKQGGGHAGHNGLRSIHAHVGEAYGRVRLGIGHPGHKDAVAAYVLNDFAKADQDWLADLLRGISDGAEALARGDGAKFQNAVALRMQPPKPEKPKPAAKAPEAQAPEAAPDARSALQKLADRFR
|
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
|
B9KMG1
|
P21992
|
FLAB3_TREPA
|
Flagellar filament 31 kDa core protein
|
Treponema
|
MIINHNMSAMFAQRQGGINGLAIAKNIEKLSSGYRINRAGDDASGLAVSEKMRSQIRGLNQAGQNIQNGISFIQATEGYLAETTEIVQRLRELAIQAANGIYSAEDRMQIQVEVSQLVDEVDRIASQAQFNGMNLLTGRFSRESALGPMQLHVGANMDQNEKIFINTMTASALGFFSDEGTDGSRSISIATVDGANKVIGTLDSALKEINKQRADLGAYQNRFETAYQGIAIAAENLQAAESRIRDADLAQQMVDYTKNQILEQSTMAMLAQANTQPQAVLRLMQ
|
Component of the core of the flagella.
|
P21992
|
Q3IYC6
|
GPH_CERS4
|
Phosphoglycolate phosphatase
|
Cereibacter
|
MPGVVFDLDGTLVHSAPDIHAAVNKALAEEGGAPFTLAEITGFIGNGVPVLIQRVLAARGEAPDAHRQAELQGRFMAHYEADPATLTSVYPGAEAAIRHLRAEGWRIGLCTNKPVGASRQILSLFGLLELFDAIIGGDSLPQRKPDPAPLRATAAALNEEVVLYVGDSEVDAATAEAAGLRFALFTEGYRHAPVHELPHHGLFSHHDELQDLLRRLLA
|
Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.
|
Q3IYC6
|
B1IAM6
|
PYRF_STRPI
|
OMP decarboxylase
|
Streptococcus
|
MREHRPIIALDFPSFEVVKEFLALFPAEESLYLKVGMELYYAAGPEIVSYLKGLGHSVFLDLKLHDIPNTVKSAMKILSQLGVDMTNVHAAGGVEMMKAAREGLGSQAKLIAVTQLTSTSEAQMQEFQNIQTSLQESVIHYAKKTAEAGLDGVVCSAQEVQVIKQATNPDFICLTPGIRPAGVAVGDQKRVMTPADAYQIGSDYIVVGRPITQAEDPVAAYHAIKDEWTQDWN
|
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
|
B1IAM6
|
P93472
|
DIM_PEA
|
Cell elongation protein diminuto
|
Pisum
|
MSDLEAPLRPKRKKIWVDYFVKFRWILVIFVVLPISFTLYFLTYLGDVRSEWKSFKTRQKEHDENVQKVVNRLKKRNPSKDGLVCTARKPWVAVGMRNVDYKRARHFEVDLSPFRNILDIDKERMIARVEPLVNMGQITRVTVPMNLALAVVAELDDLTVGGLINGYGIEGSSHKYGLFSDTVVAFEIILADGSLVKATKDNEYSDLFYAIPWSQGTLGLLVAAEVKLIPIKEYMKLTYKPVVGNLKDIAQAYSDSFAPRDGDQDNDEKVPDFVETMIYSPTRAVCMTGRYASKEEAKKKGNKINNVGWWYKTWFYQHAETALKKGLFVEYIPTREYYHRHTRCLYWEGKLILPFGDQFSFRFLFGWLMPPKVSLLKATQGEAIRNYYHEMHVIQDMLVPLYKVGDALEWSDREMEIYPIWLCPHKLFKLPIKTMIYPEAGFELQRRQGDTQNAQMFTDVGVYYAPGPVLRGEVFDGAEAVRKMESWMIENHCFQPQYAVSELNEKNFWRMFDAGLYEHCRRKYGAVGTFMSVYYKCKKGRKTEKEVREAEQAHLDTAYPEVDQPPD
|
Plays a critical role in the general process of plant cell elongation.
|
P93472
|
Q48NU4
|
CCA_PSE14
|
Phosphatase
|
Pseudomonas
|
MQIYKVGGAVRDRLLGQPVTDIDWVVVGASTEDMLVKGYRPVGTDFPVFLHPLTNEEYALARTERKSGVGYGGFVFHASPEVTLEQDLIRRDLTINAMAEDKDGNLTDPYNGQKDLEARILRHVSPAFAEDPLRVLRVARFAARYARYGFTIAPETLGLMRQLSESGELKALTAERSWKEISRALMEEQPQVFIQVLHDCGALKELMPEVEALFGVPQPAAHHPEIDTGVHVLSVLEQSAIHKHPLTVRWACLLHDLGKGLTPEAEWPRHIAHEHTGLRLIKAVNERFRVPRECQELALLVGQYHTHGHRALELKPSTLLELLQSFDVYRRPQRFEEFIAACEMDARGRHGFEQRSYPQADYLRGAAQAARTVSVQPLLEKGFKGKELGDALKNERLKALKIYKAEHVA
|
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.
|
Q48NU4
|
A1RQ57
|
HUTU_SHESW
|
Imidazolonepropionate hydrolase
|
Shewanella
|
MDKRHDPSRRIIAPHGTQLSCKSWLTEAPMRMLMNNLHPDVAERPEDLVVYGGIGRAARDWDCYDKIIEVLQRLEDDETLLVQSGKPVGVFRTHADAPRVLIANSNLVPHWANWEHFNELDKLGLAMYGQMTAGSWIYIGTQGIVQGTYETFVSVAKQHFEGISKGKWILTGGLGGMGGAQTLAGTMAGFSVLACEVDETRIDFRLRTRYVDKKATSLDEALAMIEAANQAGKPVSVGLLANAADVFAELVKRGVTPDVVTDQTSAHDPLNGYLPQGWTMAEAAAMRKTDEAGVVKAAKASMAVQVQAMLNLQTAGAATLDYGNNIRQMAFEMGVENAFDFPGFVPAYIRPLFCEGIGPFRWVALSGDPEDIYKTDAKVKELIPDNPHLHNWLDMARERIAFQGLPARICWIGLKDRARLALAFNEMVKNGELSAPVVIGRDHLDSGSVASPNRETESMLDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHSGVVIVCDGTDAAAKRVGRVLWNDPATGVMRHADAGYEIAKNCAKEQGLDLPMQD
|
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
|
A1RQ57
|
A5UN95
|
PURA_METS3
|
IMP--aspartate ligase
|
Methanobrevibacter
|
MTCSILVGGAWGDEGKGKCITYLCGNDKPDIIARAGVGPNAGHSVEFNGEKYGLRLIPSGFVHTDAKLMIGAGVLVDKDVLFKEFEDLKKYNVKERTFVDPRCAIITKDHRERDKKSEHLAKKIGSTGSGCGPANSDRVLRTVKLANDVPELEDYLADVSLETNDVLDNGGDVFIEGSQGFALSLYYGTYPFVTSKDTTASTFAADVGVGPTKVDEVINVFKAYITRVGEGPFPTEISQEEAESKNIEEYGVVTGRRRRVGLFDMELAKESCRINGATQIALTCVDRLYPDCARTQSYDDLSAETKKFVEEIQSETGVPVTIISTGPDLKDTIDLRKELL
|
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
|
A5UN95
|
Q5VZK9
|
CARL1_HUMAN
|
Leucine-rich repeat-containing protein 16A
|
Homo
|
MTEESSDVPRELIESIKDVIGRKIKISVKKKVKLEVKGDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVVCSKSAQMIVETEKCSISMKMASPEDVSEVLAHIGTCLRKIFPGLSPVRIMKKVSMEPSERLASLQALWDSQTVAEQGPCGGFSQMYACVCDWLGFSYREEVQWDVDTIYLTQDTRELNLQDFSHLDHRDLIPIIAALEYNQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLENAGLRTDFAQKLASALAHNPNSGLHTINLAGNPLEDRGVSSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSLSQSLSANPLTASTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIVHLDLSNTECSLDMVCGALLRGCLQYLAVLNLSRTVFSHRKGKEVPPSFKQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNHNLKGVSLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLESDLSTLIVWLSKNRSIQHLALGKNFNNMKSKNLTPVLDNLVQMIQDEESPLQSLSLADSKLKTEVTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFMPIPMYDASQALKTNPEKTEDALQKIENYLLRNHETRKYLQEQAYRLQQGIVTSTTQQMIDRICVKVQDHLNSLRNCGGDAIQEDLKSAERLMRDAKNSKTLLPNLYHVGGASWAGASGLLSSPIQETLESMAGEVTRVVDEQLKALLESMVDAAENLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSHCHHKLADHFSRRGKTLPQQESLEIELAEEKPVKRSIITVEELTEIERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEMEFDLDKALEEVPIHIEDPPFPSLRQEKRSSGFISELPSEEGKKLEHFTKLRPKRNKKQQPTQAAVCAANIVSQDGEQNGLMGRVDEGVDEFFTKKVTKMDSKKWSTRGSESHELNEGGDEKKKRDSRKSSGFLNLIKSRSKSERPPTILMTEEPSSPKGAVRSPPVDCPRKDTKAAEHNGNSERIEEIKTPDSFEESQGEEIGKVERSDSKSSPQAGRRYGVQVMGSGLLAEMKAKQEKRAACAQKKLGNDAVSQDSSSPALSGVERSDGGGAVPKLHPGLPENRFGLGTPEKNTKAEPKAEAGSRSRSSSSTPTSPKPLLQSPKPSLAARPVIPQKPRTASRPDDIPDSPSSPKVALLPPVLKKVPSDKERDGQSSPQPSPRTFSQEVSRRSWGQQAQEYQEQKQRSSSKDGHQGSKSNDSGEEAEKEFIFV
|
Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments . Plays a role in lamellipodial protrusion formations and cell migration .
|
Q5VZK9
|
A8FQ86
|
LEUD_SHESH
|
Isopropylmalate isomerase
|
Shewanella
|
MNPFTSHTGLAVMIDSANVDTDQIIPKQFLSKVTRDGFGVHLFHDWRYLDEAGDEPNPGFSLNLPRYKGASILISKENFGCGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLTDVEVQQLMDEVEASEGAEITVDLEELTVTSPSGAVFNFEIAGSARHNLLNGLDAIGLSLACADQIARYEAQLPTWKA
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
A8FQ86
|
Q80X66
|
BTBDA_MOUSE
|
Glucose metabolism-related protein 1
|
Mus
|
MAGRPHPYDSNSSDPENWDRKLHSRPRKLYKHSSSASRVAKGGVDHTKMSLHGASGGHERSRDRRRSSDRSRDSSHERAESQLTPCIRNVTSPTRQHHIEREKDHSSSRPSSPRPQRASPNGSMSSAGNSSRNSSQSSSDGSCKTSGEMVFVYENAKEGARNVRTSERVTLIVDNTRFVVDPSIFTAQPNTMLGRMFGSGREHNFTRPNEKGEYEVAEGIGSTVFRAILDYYKTGIIRCPDGISIPELREACDYLCISFEYSTIKCRDLSALMHELSNDGARRQFEFYLEEMILPLMVASAQSGERECHIVVLTDDDVVDWDEEYPPQMGEEYSQIIYSTKLYRFFKYIENRDVAKSVLKERGLKKIRLGIEGYPTYKEKVKKRPGGRPEVIYNYVQRPFIRMSWEKEEGKSRHVDFQCVKSKSITNLAAAAADIPQDQLVVMHPTPQVDELDILPSHPASGNNDLDPDAQNPML
|
Plays a major role as an activator of AKT family members by inhibiting PPP2CA-mediated dephosphorylation, thereby keeping AKTs activated. Plays a role in preventing motor neuronal death and in accelerating the growth of pancreatic beta cells.
|
Q80X66
|
P36421
|
SYYC_YEAST
|
Tyrosyl-tRNA synthetase
|
Saccharomyces
|
MSSAATVDPNEAFGLITKNLQEVLNPQIIKDVLEVQKRHLKLYWGTAPTGRPHCGYFVPMTKLADFLKAGCEVTVLLADLHAFLDNMKAPLEVVNYRAKYYELTIKAILRSINVPIEKLKFVVGSSYQLTPDYTMDIFRLSNIVSQNDAKRAGADVVKQVANPLLSGLIYPLMQALDEQFLDVDCQFGGVDQRKIFVLAEENLPSLGYKKRAHLMNPMVPGLAQGGKMSASDPNSKIDLLEEPKQVKKKINSAFCSPGNVEENGLLSFVQYVIAPIQELKFGTNHFEFFIDRPEKFGGPITYKSFEEMKLAFKEEKLSPPDLKIGVADAINELLEPIRQEFANNKEFQEASEKGYPVATPQKSKKAKKPKNKGTKYPGATKTNEIATKLEETKL
|
Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two-step reaction: L-tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) . The specificity determinants on tRNA(Tyr) are the base pair C1-G72, the discriminator residue A73, and the three anticodon bases G34, U35 and A36 . Also involved in nuclear tRNA export . Also attaches D-Tyr to tRNA(Tyr), this reaction is about 150-fold less efficient than attachment of L-Tyr .
|
P36421
|
A1WMN6
|
HISZ_VEREI
|
ATP phosphoribosyltransferase regulatory subunit
|
Verminephrobacter
|
MSAWVLPDHIADVLPSEARHIEELRRGLLDTARCYGYELVMPPLMEHLESLLTGTGEALDLQTFKLVDQLSGRSLGLRADTTPQVARIDAHLLNRKGVTRLCYCGPVLHTRPDRPHATREPLQFGAEIYGHSGLEADLEALQLARECLRVAGVRDTTIDLADMRIVRKLLAGVALSPQRLSRIHAALAAKDAGELAALTHCFAADSRAALLALLQLYGDEAVLAEAEKALQRIDGISPVLANLRWLASRLEGAQVTFDLADLRGYAYYSGARFAIYARGASDALVRGGRYDEVGAVFGRNRPAVGLSLDIKQVVGVVPPQTLKAAIRAPWGEAADVNAAIAELRAAGETVVCVLPGHESEVDEFHCDRELAQVSGRWVVQAV
|
Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
|
A1WMN6
|
B1YNS0
|
BIOF_BURA4
|
8-amino-7-ketopelargonate synthase
|
Burkholderia cepacia complex
|
MTRTAPSSLRSLPAEGAAATDLLDTLQRGLAELDAQGLRRVRRTADTACDAHMRVDGRDIVGFASNDYLGLAAHPALVAAFAEGARRYGSGSGGSHLLGGHSRAHATLEDELAGFAGGFSDAPRALYFSTGYMANLAAMTALTGKHATIFSDALNHASLIDGIRLSRANVQVYPHADMAALAALLDASDAETKLIVSDTVFSMDGDIAPLAELVALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLIYVGTLGKAAGVAGAFVIAHETVIEWMIQRARSYIFTTAAPPAVAHAVSASLKVIAGDEGDARRAHLAALIERTRALLRMTRWQPVDSHTAVQPLVIGSNDATLAAMRSLDAHGLWVPAIRPPTVPAGTSRLRVSLSAAHSFDDLARLEAALIEASEGQTRRDAEQPPRSLRSLPPEGAAASLGAARRETAA
|
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
|
B1YNS0
|
Q8Y0V3
|
RSGA_RALSO
|
Small ribosomal subunit biogenesis GTPase RsgA
|
Ralstonia
|
MTRGKPGRAGHDRRHASTGEHGLVIAAHGRHYLVERKGGGLLQCFPRGKRSECAVGDRVIFEATAVDQGVVVRVEERRNLLHRSDQFKSKQLAANIDQVLIMLGTEPGFSEDLLGRALVAAESLGITPLILLNKIDLTARLETARARLALYRALGYAVVELSVHAAPEAAHAVLAAHVAGRSSILIGQSGMGKSSLLNLLIPGVDAQTREISEKLDSGKHTTTFTRLYHLPSGWGHGGTLIDSPGFQEFGLHHLTEGMLERAFPEFRPRLTECRFYNCRHLQEPGCGILGAMAEGKIDPRRHALYAQLLHESEQQKPW
|
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
|
Q8Y0V3
|
A0A067XMK8
|
PTAJ_PESFW
|
Pestheic acid biosynthesis cluster protein J
|
Pestalotiopsis
|
MAASTAAQVQLSEEALGLARIFENPKGSLEAASKLLQKNHDEFHVFWRDVGGHNHIPHSVLSILALGGGPAELQRAWDDGVAIQRPTPPLDEDVVKKLENPAEFRARIGSIPNYTNFLHFFRNQMDKKGWQAVVSEYAFSRTPLAETIFAQLFEGAYHPFIHIGFGIEFNLPSIIAEGLAQAATHDSAGIEGFFLEAERQAAQSKGPGKSLVQLLDEVRTTEKIKTAARLPDGPVRVRDGVIGRAGAEIAALASQFRVPADQLSRGAAESINISAYTAGAAQRAGKARKIDFFHMHNTTSSLFLTVFLNQPWISTEDKVRIVEWKGRLDLVWYAACSAPDLNVDHVIGYKPAQSAGWGWKELYEAINVAHDDGHLAKIVRALKNGEEVSRPFESGEGAEAFPIKGDSWLKLAQMSYDTTLDLPDDDKWIWGAGFLPLWNKVPSL
|
Baeyer-Villiger oxidase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes . The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA . As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain . The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and the intermediate to release atrochrysone carboxylic acid, which is spontaneously dehydrated to form endocrocin anthrone . Endocrocin anthrone is then converted to endocrocin, catalyzed by the anthrone oxygenase ptaC . Spontaneous decarboxylation of endocrocin occurs to generate emodin . An O-methyltransferase (ptaH or ptaI) could methylate emodin to form physcion . PtaJ could then catalyze the oxidative cleavage of physcion, and rotation of the intermediate could then afford desmethylisosulochrin . PtaF, a putative NADH-dependent oxidoreductase, might also participate in the oxidative cleavage step . Desmethylisosulochrin is then transformed by another O-methyltransferase (ptaH or ptaI) to form isosulochrin . Chlorination of isosulochrin by ptaM in the cyclohexadienone B ring then produces chloroisosulochrin . PtaE is responsible for the oxidative coupling reactions of both benzophenones isosulouchrin and chloroisosulouchrin to RES-1214-1 and pestheic acid respectively, regardless of chlorination.
|
A0A067XMK8
|
B1KHG7
|
SYD_SHEWM
|
Aspartyl-tRNA synthetase
|
Shewanella
|
MRSQYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGIVQVVYDPDLPEVFDVASTLRSEFCVQVTGLVRARPDSQVNQDMRTGGIEILGKGLTILNSSAPLPINMDKNQHNTEEQRLKYRYLDLRRPEMADRIVFRSKVTSAVRRFLDDSGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSSEQVMAKTEEMVRGLFNDLLNVDLGEFPKMTFAEAMRRFGSDKPDLRNPLELIDIADIVKEVEFAVFNGPANDPEGRVAVLSIPGGAKLSRKQLDEYAKYVTIYGAKGLAWMKVNDLDQGMEGIQSPVLKFLSEDVVKALLDRTGAQTGDLILFGADKANIVAEAMGALRLKAGEDFDLLQGEWKPLWVVDFPMFERTSDGGLHAMHHPFTAPTGISPEQLEADPTAAISDAYDMVLNGCELGGGSVRIHNSEMQSAVFRILGIEEEEANEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPAQLIELGIEVIENQESKEEQA
|
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
|
B1KHG7
|
Q99570
|
PI3R4_HUMAN
|
Phosphoinositide 3-kinase adaptor protein
|
Homo
|
MGNQLAGIAPSQILSVESYFSDIHDFEYDKSLGSTRFFKVARAKHREGLVVVKVFAIQDPTLPLTSYKQELEELKIRLNSAQNCLPFQKASEKASEKAAMLFRQYVRDNLYDRISTRPFLNNIEKRWIAFQILTAVDQAHKSGVRHGDIKTENVMVTSWNWVLLTDFASFKPTYLPEDNPADFNYFFDTSRRRTCYIAPERFVDGGMFATELEYMRDPSTPLVDLNSNQRTRGELKRAMDIFSAGCVIAELFTEGVPLFDLSQLLAYRNGHFFPEQVLNKIEDHSIRELVTQMIHREPDKRLEAEDYLKQQRGNAFPEIFYTFLQPYMAQFAKETFLSADERILVIRKDLGNIIHNLCGHDLPEKAEGEPKENGLVILVSVITSCLQTLKYCDSKLAALELILHLAPRLSVEILLDRITPYLLHFSNDSVPRVRAEALRTLTKVLALVKEVPRNDINIYPEYILPGIAHLAQDDATIVRLAYAENIALLAETALRFLELVQLKNLNMENDPNNEEIDEVTHPNGNYDTELQALHEMVQQKVVTLLSDPENIVKQTLMENGITRLCVFFGRQKANDVLLSHMITFLNDKNDWHLRGAFFDSIVGVAAYVGWQSSSILKPLLQQGLSDAEEFVIVKALYALTCMCQLGLLQKPHVYEFASDIAPFLCHPNLWIRYGAVGFITVVARQISTADVYCKLMPYLDPYITQPIIQIERKLVLLSVLKEPVSRSIFDYALRSKDITSLFRHLHMRQKKRNGSLPDCPPPEDPAIAQLLKKLLSQGMTEEEEDKLLALKDFMMKSNKAKANIVDQSHLHDSSQKGVIDLAALGITGRQVDLVKTKQEPDDKRARKHVKQDSNVNEEWKSMFGSLDPPNMPQALPKGSDQEVIQTGKPPRSESSAGICVPLSTSSQVPEVTTVQNKKPVIPVLSSTILPSTYQIRITTCKTELQQLIQQKREQCNAERIAKQMMENAEWESKPPPPGWRPKGLLVAHLHEHKSAVNRIRVSDEHSLFATCSNDGTVKIWNSQKMEGKTTTTRSILTYSRIGGRVKTLTFCQGSHYLAIASDNGAVQLLGIEASKLPKSPKIHPLQSRILDQKEDGCVVDMHHFNSGAQSVLAYATVNGSLVGWDLRSSSNAWTLKHDLKSGLITSFAVDIHQCWLCIGTSSGTMACWDMRFQLPISSHCHPSRARIRRLSMHPLYQSWVIAAVQGNNEVSMWDMETGDRRFTLWASSAPPLSELQPSPHSVHGIYCSPADGNPILLTAGSDMKIRFWDLAYPERSYVVAGSTSSPSVSYYRKIIEGTEVVQEIQNKQKVGPSDDTPRRGPESLPVGHHDIITDVATFQTTQGFIVTASRDGIVKVWK
|
Regulatory subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 .
|
Q99570
|
Q6G1D3
|
ACCD_BARQU
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
|
Bartonella
|
MNWITNYVRPKINSILRRREIPDNLWIKDPTSGEMVFHKDLEVNQYVIPNSGYHMRISAKNRLMHFFDDGIYTPLENPKVVIDPLKFRDEKRYIDRLKDYRSKLGVDDNILSAQGTIEGLPIVATVQDFAFMGGSLGMASGEAIIKAFDTAIANKCPLVLFSASGGARMQEGTLSLMQMPRTTVAIEMMKEAKLPYIVVLTNPTTGGVTASYAMLGDIHIAEPGAMIGFAGPRVIQQTIRETLPEGFQSSEYLLEHGMIDMVVSRLEMKATIARLLRLIMKCPPAVNPSNPSPTDSQPPLSKAEAA
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
|
Q6G1D3
|
P0CU17
|
RPN51_SCHPO
|
26S proteasome regulatory subunit rpn501
|
Schizosaccharomyces
|
MEQKPEVDYSEKFAELQKSLNNLNTIDIDANLEKLLIFEKQVRQASDTSTNTKVLIYIADLLFRAGDFQGLNEQLVSLFKKHGQLKQSMTSLVQHVMTYLPGIDDLKTKINLIETLRTITDGKIYVEVERARLTQLLSQIKEEQGDIKSAQEILCNEPVETYGSFDLKEKVAFILDQVRLFLLRSDYYMASTYTKKINVKFFEKEDVQSLKLKYYEQKIRIGLHDDAYLDVCKYYRAVYDTAVVQEDPEKWKEILENVVCFALLTPYDNEQADLLHRINADHKLNSLPLLQQLVKCFIVNELMRWPKIAEIYGSALRSNPVFAENDEKGEKRWSELRKRVIEHNIRVVANYYSRIHCSRLGVLLDMSPSETEQFLCDLIAKHHFYAKIDRPAQVISFKKSQNVQEQLNEWGSNITELLGKLEKVRQLIIKEEMMNSIQQAVAK
|
Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Required for proper proteasome assembly.
|
P0CU17
|
P95399
|
AROE_NEIPO
|
Shikimate dehydrogenase (NADP(+))
|
Neisseria
|
MTALPRYAVFGNPVAHSKSPQIHQQFTLQEGVDIEYGRICADIDGFAQAVSTFFETGGCGANVTVPFKQEAFALADEHSDRALAAGAVNTLILLKNGKLRGDNTDGIGLVNDITQVKNIAIEGKTILLLGAGGAVRGVIPVLKEHRPARIVIANRTHAKAEELARLFGIEAVPMADLNGGFDIIINGTSGGLSGQLPAVNPEIFRSCRLAYDMVYGDAAQTFLNFAQSNGAAEVSDGLGMLVGQAAASYHIWRGFTPDIRPVIEYMKAL
|
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
|
P95399
|
C3KV13
|
UVRC_CLOB6
|
Excinuclease ABC subunit C
|
Clostridium
|
MFDLEYQLKNLPDKPGVYLMKNNLGEIIYVGKAKILKNRVRQYFQKSQKHSEKVKAMVKNIEEFEYIITDSEIEALILECNLIKKYRPKYNILLKDDKHYPFIKVTLAEDFPRVISTRKVTKDGSKYFGPYVDGSSVKDIIELIKKTFPIRTCKKNIVEGAKAIRPCLNYQIGLCKAPCAQYIKKSEYREIIDDVIKLLSGKHLDIVENFKLNMEKAAGNLEFEKAAMLRDKINIIEKIGEKQKIILNNFDNEDYISLYSDGKDTCFQVFFLRNGKIVGREHFIIEDTFDTNSSTLISNFLKEFYGGTAYIPKTIYVPNIEDEVLLEQWLTLKKESKSTIKIPIKGEKKNILDLVEKNAKTTLENFKLKYLQEKALYDNVLKDLKNILRLQEEPIRIEAFDISNIQGFDSVGSMVVFEKGRAKPSDYRRFKINTVKGADDYKSMKEILTRRFQHGLSEIKSIQDRKLEFSSGKFSVFPDLILMDGGKGQINIALEVLNTFNINIPVCGMVKDNKHRTRGLIYNGEEIIINKYGSVMKFITRVQDEVHRFAISYHRSLRGKNSFHSLLDDIPNIGEKRKKDLLFNFKSIDNIKKATYEELLSISSMDKKSAESILEFFK
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
C3KV13
|
A1T0R0
|
HEM3_PSYIN
|
Pre-uroporphyrinogen synthase
|
Psychromonas
|
MTAQKIRIATRHSPLAMWQANFIKSELLKYHPNLIVELLPMKTKGDIILDTPLAKVGGKGLFVKELEVAILEGRADIAVHSIKDVPVDFPEGLGLTTICKREDPHDAFVSNHYKQLDELPEGAIVGTCSLRRQCQILALRPDIIIKNLRGNVNTRLRKLDEGEYDAIILAAAGLMRLEMQHRITSLIAPEVSLPAVGQGAVGIECRLDDEQTITLLKPLEDPETRIRITAERAMNLKLQGGCQVPIGSFAILENEQLFLRGLVGSVDGKQIIRKEITGHQNDAQQLGITLAEQLLACGAEEILAEVYKNQ
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
A1T0R0
|
Q8UD80
|
HEM6_AGRFC
|
Oxygen-dependent coproporphyrinogen-III oxidase
|
Agrobacterium tumefaciens complex
|
MERPILPKGLPEDIEDKKAVAQAWFQHLRDTIVASFETLEDELTGPLSDQEPGRFVQKDWLRDNGEGGGGKMSMMEGRVFEKVGVHTSTVYGEFSPEFRKQIPGAEEDPRFWASGLSLIAHPVNPNVPAVHMNTRMVVTTSHWFGGGADLTPVLGRRRTQQDPDTQLFHRAFEITCNRHPIADYPRYKSWCDEYFFLKHRDEPRGTGGIFFDWLHPDEEKGGWDANFTFVQDVGRAFNLVYPKIVRANFNQNWTEEDRDEQLIRRGRYVEFNLLYDRGTIFGLKTGGNVESILSSLPPVVRWP
|
Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
|
Q8UD80
|
Q6MCW1
|
SURE_PARUW
|
Nucleoside 5'-monophosphate phosphohydrolase
|
Candidatus Protochlamydia
|
MSSKPLILVTNDDGVHAKGIRHLWQSIQDLADLIIVAPQQEQSAVSLSITVRRPLHIEKVDWLNAQADVWSVNGTPADCVKLALNVVLPKRPQLIVSGINRGTNAGRNIFYSGTVAAIMEGVMQGIPGIAFSYGDYFNPSYHLIESFIPGIVNYALQNAMQEGTFLNVNFPKTEHGPIKGIRLTTQGKEYWAENPEKRQHPAEQNSYYWLGSKLAEYDEREDSDIFLLRKGFATVVPLHIGDLTNHSHLLKEKLAFETFVN
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
|
Q6MCW1
|
A8H0Q6
|
RPIA_SHEPA
|
Phosphoriboisomerase A
|
Shewanella
|
MTQDEMKKAAGWAALQYVEENSIVGVGTGSTVNHFIDALATMKFDIEGAVSSSEASTEKMKALGIPVFDLNSVNELSVYVDGADEINSQMDMIKGGGAALTREKIVAAVADKFICIVDNTKQVDILGEFPLPIEVIPMARSYVARQIVKLGGDPVYREGCVTDNGNIIIDVYNMKIMKPKELEQQIDGIVGVVTNGLFAKRGADILLVGTPEGVKTVTF
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
A8H0Q6
|
A1S8D5
|
GRPE_SHEAM
|
HSP-70 cofactor
|
Shewanella
|
MSNESTNPQQEPLEQVQDTEVVTDEAALVDELTQANFRIEELEQALAAAEAKVEEQKDSVVRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALAGTNAEDEATKAMYEGVSLTMKTLVNAVEKFGVKVVDPMGQPFNPEQHQAIGMQPNPEVPANHVMVVLQKGYELNGRLLRPAMVMVSQGGGVDTQA
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
|
A1S8D5
|
P0CY97
|
CH601_CUTAK
|
Heat shock protein 60 1
|
Cutibacterium
|
MAKLIEFNIEARRGLEAGMNTLADAVKVTLGPKGRNVVLEKSWGAPTITNDGVSIAKEIELDDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQAMVREGLRNVTAGANPMGLKKGIEAAVQAVSARLSDMAIDIETKDQIASTASISAADPTVGEIIAEAMDKVGKEGVITVEESNTFGLELELTEGMRFDKGYISPYFVTDTERMEAVLEDPYILIVNSKISSLKDLLPVLEKVMQSGKPLFVIAEDVEGEALAGLIVNKIRGTFKSVAVKAPGFGDRRKAMLNDIAILTGGQVISEEVGLSLDAVTLDLLGRARQVVVTKDEATIVDGAGDSEQIAGRVSQIRKEIENSDSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKHRIEDAVRNAKAAVEEGIIPGGGVALLQASKAAEIEGLEGDELTGAQIVLAACTAPLKQIAINAGLEGGVVAEKVAGLPAGQGLNAANDEYVDMVEAGIIDPAKVTRSALQNAASIAALFLTTEAVIADKPEPVKAPAGGGDMDGMGGMGGMM
|
Together with its co-chaperonin GroES, 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.
|
P0CY97
|
A9SR33
|
M2K1B_PHYPA
|
PpMKK1b
|
Physcomitrium
|
MSRRHRTGGLRVAVPKQENSIHRFLTANGVFHDDDIQLDHMGLRVVSSESTAYANPPDAQLSLADLEAVRVLGKGAGGSVQLVRHKWTNDIYALKGIQMNINETVRKQIVQELKINQLTLHQCPYIVKCYHSFYHNGIISIVLEYMDRGSLADIIKQTKQIPEPYLAVISNQVLKGLNYLHQVRHIIHRDIKPSNLLINQKGEVKISDFGVSAVLISSMAQRDTFVGTYTYMSPERLGGQSYAYDSDIWSLGLTILECALGYFPYRPPGQEEGWNNFFMLMELVINQPPVAAPPDKFSPEFCSFIAACIQKRPGDRLSTADLLKHPFLQKYSEEEYHLSNLR
|
The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for full defense response to fungal pathogen chitin.
|
A9SR33
|
Q1GYZ3
|
RSMH_METFK
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Methylobacillus
|
MSAGISHVPAAQVSQHVTVLLEEAVEALSIKPDGVYVDGTFGRGGHSRKILEKLGAQGRLVALDRDLAAIQAAQGIQDARFKIVHSHFAAMAQVLASLNIQQVDGVLLDLGISSPQIDEGERGFSFRFDGPLDMRMDQSRGQTAAEFIATATEQELTRVIKEYGEERFAKQIARAIVAQRAGGMDISTTGQLAKIVAGAVPKVEPGQDPATRTFQALRIFINQELEELSLTLPQCLSLLAPQGRLAVISFHSLEDRIVKRFIRGEQDRDNLPAHFPVRASDLPQPRLVAIGRAVRPSEDEVRRNPRSRSAVLRVAERTAVL
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
Q1GYZ3
|
P81244
|
CYC6_PROHO
|
Soluble cytochrome f
|
Prochlorothrix
|
AASGASIFSAKCAQCHLGGKNIINPTKTLSLADLQANGKDTVSAI
|
Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
|
P81244
|
P24980
|
NU6M_BALPH
|
NADH dehydrogenase subunit 6
|
Balaenoptera
|
MMMYIVFILSIIFVISFVGVSSKPSPIYGGLGLIVGGGVGCGVILSFGGSFLGLMVFLIYLGGMLVVFGYTTAMATEQYPEVWVSNKVVLGAFVLGLVVEFLIVIYALKSGEVKIMFEFDGLGDWVVYDTGGSGVFSEEATGIAALYSYGVWLVIVTGWSLFISVVIIMEITRGS
|
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
|
P24980
|
A5UJB8
|
CPGS_METS3
|
Cyclic 2,3-diphosphoglycerate synthetase
|
Methanobrevibacter
|
MKSISKMLCLVDGEHYLPVTQESIDVLNNLEHIDIVAAVFIGGTEKLRDDSEESYSKVLGVPVQFAKNEDIPYDIIVEMINRYDVDTVMDLSDEPILDYPKRFKIACKTLAQGVSYQGPDFKFDPVTQYEIMEKPSIKIIGTGKRIGKTAVSGFVSRLIDKNGYEPCVIAMGRGGPQEPEIVHGEQLEITPEFLLEQSEKGVHAASDHWEDALMSRILTIGCRRCGGGMAGEVFLTNMKKGAKLANQVDSKFAIFEGSGAAIPPIKTNKNIVLIGANQPLNNIIDYFGPYRIGLGDLIILTMCEEPMCNEEKREYIEKFIKEINPKAKIISTVFRPKPLADISGKKVLFATTAPKSIEHELVDYLETNYNCEIVGTTPHLSNRPLLKKDIEKYMDEADIMLTELKAAAVDVATKDSIKAGLDVVYCDNIPVPINYKYPDLSKSVLEIVDEAIEDFNKD
|
Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.
|
A5UJB8
|
P9WPG2
|
PGSA_MYCTO
|
CDP-diacylglycerol--glycerol-3-phosphate phosphatidyltransferase
|
Mycobacterium tuberculosis complex
|
MSRSTRYSVAVSAQPETGQIAGRARIANLANILTLLRLVMVPVFLLALFYGGGHHSAARVVAWAIFATACITDRFDGLLARNYGMATEFGAFVDPIADKTLIGSALIGLSMLGDLPWWVTVLILTRELGVTVLRLAVIRRGVIPASWGGKLKTFVQAVAIGLFVLPLSGPLHVAAVVVMAAAILLTVITGVDYVARALRDIGGIRQTAS
|
Probably catalyzes the synthesis of phosphatidylglycerophosphate by transferring a phosphatidyl group from CDP-diacylglycerol to glycerol 3-phosphate.
|
P9WPG2
|
A5FYS5
|
RLMH_ACICJ
|
rRNA (pseudouridine-N3-)-methyltransferase RlmH
|
Acidiphilium
|
MTAPGARLRIIAIGRDSKGPEADLVARYAARLQPRPEVVALPDGTGSPAEIKRREADAILRRLAAEDLVIALDLGGKAPDSAAFAAMLASWRETSRPLAFVIGGAEGLERRIIERADAVLSLGNLTLPHLLARAVLAEQLYRAQCILAGHPYHRAGRP
|
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
|
A5FYS5
|
P73289
|
RL25_SYNY3
|
50S ribosomal protein L25
|
unclassified Synechocystis
|
MALSIECQQRPEKVNPRALRREGLIPATLYGHNGAESISLVVDHKTAITMLRSVTVKETPIEVKIPHLSWEGEAVVQEIQCHPWRRNLYHLAFFAGKK
|
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
|
P73289
|
B6J7Q0
|
MDH_COXB1
|
Malate dehydrogenase
|
Coxiella
|
MAKHVKVAVTGAAGQIGYALLFRLASGQAFGLDTTVDLHLLEIEPALPALKGVVMELEDCAFPLLRNMVVTSDPRVAFNDVNWALLVGAAPRKAGMERKDLLEKNGSIFAGQGKAINENAASDVRIFVVGNPCNTNCLIAMNNAPDIPKDRFYAMTRLDQNRAIGQLALKAGVDVPSVKNMIIWGNHSSTQYPDFYHATIDGKPATEVIRDKNWLLNDFIPVIQQRGAAVIKARGASSAASAANAALDSVWSLINTTPADDNYSVALCAQGQYGVDEGLIFSFPCRTENGVVSVIEEIEHNEFGQQKLKETLDELREERDAVEALGLI
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
B6J7Q0
|
Q9TLS1
|
PREA_CYACA
|
Prenyl transferase
|
Cyanidium
|
MKVNSKTLQSVKEDLLNIEQTLNKLIKVNNPILSAAAKHLLIVESKKIRPAIVLLVAKAIDKNKKIKTSQQRLAEVTEIIHTATLLHDDVVDESIIRRGTKSVNKTFGNKIAVFAGDFLFAQSSWYLANINNLEVVKAISKVITDLAEGELQQNLTQFNTYYSIIKYLEKSFNKTASLIAASCKSCCLLSDFDQSLNSKFYNYGKNLGLAFQIIDDILDITSSSTALGKMTTSDLKLGNLTAPVLFALTKNSKLFKIIEREFCEKSDISEAINIIKETNAIEESFDLAYEHIEAAINSIKDLPTSSEKDSLIEIAYDLLNRYK
|
Possible role in synthesis of the nonaprenyl side chain of plastoquinone or in synthesis of other prenyl chains such as undekaprenyl pyrophosphate.
|
Q9TLS1
|
C0ZG01
|
RPOZ_BREBN
|
Transcriptase subunit omega
|
Brevibacillus
|
MLYPSIDELTEKAESKYILVTVASKRARQLRENSEVQVVRPKSKKFVGLALEEFISDELVHEFLDGRK
|
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
|
C0ZG01
|
Q3B8R1
|
EMARD_RAT
|
Endoplasmic reticulum membrane-associated RNA degradation protein
|
Rattus
|
MEILTGDSITTCLSPLVHDLICNLGFELTEICDINSIVTQNGEVRWKAITDRVSYAELGHSLDYRQSVQRLGPVCEAIHLHISSLSRAQFETQYSPWYQWTTSPELFLEIYDALESSQSAAISLSVMKLASCLERALGDVFLLIGNECPFLLRDLLASAELAHVFGHAVMDVLKVFIGSPCGLNLRNVLWHGFASPQDIPPKYCSALLLLTAGLGQLLKSYLHHTKVQLAHRPFVTLTNLEDVIVFPGVTDKVLSALETVMTKSSFLLKIMLPYWELAVSKFKSHRFADCTMLLLSQLEAGLRRVFATVNKCPDRLLTAESTILYTTFDEILAKHMSDGSINQLPCFLGEPAMDFLWDFLNYQEGPRIRDRLSHGEINIREFPKAAASQLLTFCLVLLLRFTEEDTLSELKEEAAIQLLVSLAERYRSRCHPAFQLQKQVLSCEKSLRMWPVLPLPEECCQEAGRSEGNSEACACNSLISKILCELCHYLPASACAINGLDGLPSEKWSQLLNELCNTRIPTLFCPKIVLEVLVVLRGISSQCQRVSDQVIASLQLRHRQWVEHTLRSRQRQNYVRMLSSVGLLCPVLSLILLLLALELVSVHAVHGKDAQERQQYLRFLKLILQYTENLVAYTSRQKNKWNEAVSLTRAVLLRIWTFSEKKQMLIHLTKNTNKVDTG
|
May play a role in neuronal migration during embryonic development.
|
Q3B8R1
|
Q15YB1
|
RPOB_PSEA6
|
Transcriptase subunit beta
|
Pseudoalteromonas
|
MVYSYSEKKRIRKDFGKRPQVLEIPYLLSIQLDSFKKFIDLDVDGQHGLEAAFRSVFPIKSYSGNAELQYVSYRLGEPVFDVKECQIRGVTFSAPLRVKLRLVLFDREAAPGTVKDIKEQEVYMGEIPLMTENGTFVINGTERVIVSQLHRSPGVFFDHDKGKTHSSGKVLYNARVIPYRGSWLDFEFDPKDNLYVRIDRRRKLPATIMLRALEIPTEEILGMFFEKNQVRIDGNRFMSDIVPDRLRGETAQFDILDSDGNVLVEAGRRISARHTRALEKAGIVELEVPAEYLVGRVFACDYVDQETGELVVAANDLLTLENVLALKEAGYTTFETLYINELDHGAYISDTLRIDSSTNRLEALVEIYRMMRPGEPPTKDAAETLFTNLFFSEDRYDLSSVGRMKFNRRLGRETSIGAGTLDKDDIVDVMKQLITIRDGKDDVDDIDHLGNRRIRSVGEMAENQFRVGLVRVERAVKERLSLGDLDAVMPQDLINAKPISAAVKEFFGSSQLSQFMDQNNPLSEVTDKRRISALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLASFARTNDFGFLETPYRKIVDGVVTDEIDYLSAIEEGQFSIAQANVVLDETGRLADDLIPCRHRGETTLKESSEITYMDVSPQQIVSIAASIIPFLEHDDANRALMGANMQRQAVPTLIADKPLVGTGMEKTVAVDSGVTVVAKRGGRVDYVDASRIVIKVNEEETVAGEAGIDIYNLTKYTRSNQNTCINQRPTCNVGEPIVAGDVLADGPSTDLGELALGQNMRIAFMPWNGYNFEDSILISERVAMEDRFTTIHIQELSCVARDTKLGPEEISSDIPNVGESALGKLDESGVVYIGAEVKGGDILVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDTSLRVPNSVRGTVIDVQVFTRDGVEKDKRALEIEGMQLRQVKKDLSDEFNILADGIFARAKNLLIKSGIEESRLESAQREKWFDLTLTDEDAQTELDQIAEQFVEIKADFDKKFEIKRRKITQGDDLQPGVLKIVKVYLAVKRQIQPGDKMAGRHGNKGVISTIKPVEDMPYDVNGTPVDIVLNPLGVPSRMNIGQILETHLGMAAHGIGVKIDRMLKEHEEMAKLRSFLKEVYGAGTTHQEVDLDNFSDDEITRLADNLRKGVPMATPVFDGATEAEIKHMLTLADLPESGQIALFDGRTGREFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVDGDHRMEPGMPESFNVLLKEIRSLGINIELEEQ
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q15YB1
|
P21842
|
CMA1_CANLF
|
Mast cell protease I
|
Canis
|
MHCLPLTLLLLLLCSRAEAEEIIGGTESKPHSRPYMAHLEILTLRNHLASCGGFLIRRNFVLTAAHCAGRFIMVTLGAHNIQKKEDTWQKLEVIKQFPHPKYDDLTLRHDIMLLKLKEKANLTLAVGTLPLSPQFNFVPPGRMCRVAGWGKRQVNGSGSDTLQEVKLRLMDPQACRHYMAFDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGQNDAKPPAVFTRISHYRPWINKVLKQNKA
|
Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion.
|
P21842
|
P61037
|
LNT1_TREDE
|
Apolipoprotein N-acyltransferase 1
|
Treponema
|
MKNKFIFFTLNLLLAVLGAVLFALSHPNYLNLNGFPFFAYIALIPFFLLLKRTKLKFSFLWGAFSGALSYFIFNFWIIFFHPLAIYIIIAKYCILYSVLFFVLKIIDSYFSRYSFIFQTIAWVAFEYLNTLGFLGYSYGIMGYTQWNFPILIRVSSIFGVWGISFLLVFFSACSASFLFEFYKEKDIKNVYQRYKLPMMIWVGTFFAFILYGAFTKIDLSEAQRARIALVQPNRDPWLGNLEVYRNNYEELKNLSEKALKNFPDIELVVWPETAFIPMIRWHYKYTSTYNPNSLLVRELLHFLDNQKVPFLIGNDDGVLDEKFSDNNFDNLEDKRLDYNAALLFIPKKNVSPPEPQTYRKMHLVPFTEHFPYQKLFPRFYEFLKENDTHFWEKGKEANLLEFNNFKIGTPICFEDTFGYISKAFSKKGANIIINLTNDAWANSAVSQYQHLSMAVFRAVENRLPVLRATSSGQTAFIDQNGNIQEMLPPFIKDILVADVTVLTEGHKTVYSYLGDFFGVLCTIVLILNLCFIIINKFIKRSEVK
|
Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
|
P61037
|
A1WUM8
|
TIG_HALHL
|
PPIase
|
Halorhodospira
|
MQVSVETTEGLGRRMTVQVPAERVENEVERRLKDLSGRVKMDGFRPGKVPVKVVRKQYGAQVRSEVLSEVVQQTYSEALEQESLRPAGNPHIEPKRTGEGEDLEYEASFDVLPEIEVAGLDQIQVERPQVEITDADLDNVLERLRKQHADYQEVDRAAQDEDRVVIDFHGTIDGEAFTGNSAEDAPLILGAGQLPEAFEQGLQGAKAGQELTVEHKFPDELAEPSIAGKTAVFQVTVKRVEEPQLPELDDDFAARLGIQEGGVEALREAVRGNLERERHQAVRQRLKRQVLDQLADQNELELPKSLIDGEIQALRQQSGASAEGELPESERSAYEDVASRRVKLGLLVNELVRSQGIQLDRERMMTQLREMAANSGQDPSEALQQIAQDRQMMQSLEASVIEEQVVDWLLEQVQTEDKTLSFDELMNSEDGDQASA
|
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.
|
A1WUM8
|
A6WYK4
|
LEPA_BRUA4
|
Ribosomal back-translocase LepA
|
Brucella
|
MSTPLDHIRNFSIVAHIDHGKSTLADRLIQLTGGLDTREMKDQVLDSMDIERERGITIKAQTVRLSYKAKNGEDYVLNLIDTPGHVDFAYEVSRSLAACEGSLLVVDASQGVEAQTLANVYQAIDNNHEIVVVLNKIDLPAAEPERVKQQIEEVIGIDAAQAVHISAKTGIGIEDVLEAIVTQLPAPKEGDRNAPLKAMLVDSWYDSYLGVIVLVRIIDGVLKKGQTIRMMGTGAKYPVERTGVFTPKMVQVDELGPGELGFITASIKEVADTRVGDTITEDRRPTNKMLSGFKPAQPVVFCGLFPVDAADFEDLRAAMGKLRLNDASFSFEMETSAALGFGFRCGFLGLLHLEIIQERLEREFNLDLITTAPSVVYRLNMQDGSQKELHNPADMPDVVKINAIEEPWIRATIMTPDDYLGAIMKLCQERRGLQIDLTYVGPRAMITYDLPLNEVVFDFYDRLKSISKGYASFDYNLSDYREGDLVKMSILVNEEPVDALSMLVHRSAAEKRGRALCEKLKELIPQHMFKIPIQAAIGGRIVARETISALRKDVTAKCYGGDVTRKRKLLEKQKEGKKRMRQFGKVEIPQEAFIQALKMGDD
|
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
|
A6WYK4
|
P86327
|
LACC2_CERUI
|
Urishiol oxidase C2
|
Cerrena
|
AIGPVADLDIVNDQLTDASMIKWDCLPYDVRSPNPLGTTGFAGGNYRSVPADLHLTTLADPR
|
Lignin degradation and detoxification of lignin-derived products (Probable). Oxidation of a broad range of substrates including mono-, di- and polyphenols, aromatic amines and methoxy-substituted phenols accompanied by reduction of oxygen to water.
|
P86327
|
Q12MJ8
|
RSMF_SHEDO
|
rRNA (cytosine-C(5)-)-methyltransferase RsmF
|
Shewanella
|
MLQINPNFIKHIEQELPSHLSMDEFILACNRPLRQSIRVNTLRISSEDFIALMTPRGWSFSPVPWCSDGFWITLTHDEQLGNCLEHIQGLFYIQEASSMLPPTALFTNDDADERAPLRVLDMASAPGSKTTQMAALMNNNGLLIANEYSASRVKVLHANVLRMGVSNCALTHFDGRVFGEYQYEAFDAVLLDAPCGGEGTVRKDQNALKEWQLDDVIAIADTQKDLIEAAFLALKPGGALVYSTCTLSQLENQAICQHLLSRYPEAVAFESLATLFDGAAKACTEEGFLHVWPQIYDSEGFFVAKMRKTASVPRIKSQPKAQKNFPFSPAPEKQIAALQDYIQQSFALSLPPGAQVYLRDDEFWLFPAPFSDFIGTMRFQRIGIKLADVLKKGFKIKHEAVIALGAKLGTNANNNSNTNPNNNANTNPNNNSNTNPRCIPLNQAQAEQFLMGRDIDTASFDGKLDLTPKGEMMVSYHGAAIGVVKHLGHRLKNSLPRELVRDNLG
|
Specifically methylates the cytosine at position 1407 (m5C1407) of 16S rRNA.
|
Q12MJ8
|
Q2QM59
|
PCF8_ORYSJ
|
Transcription factor PCF8
|
Oryza sativa
|
MEEVVVGGKERKRPRGALVGVGGGGASAATAAAWRTSRVARAAAGGKDRHSKVVTSRGLRDRRVRLSVPTAIAFYDIQDRLGVDQPSKAIEWLIRAAAAAIDALPSLDCSFALPAAASSPPPPAADDAEVSTSETSKSSVLSLANAPCDNGGGAFAELLHCSNTNGSKPLQQQQQATLAYYAAAQSAHMAAPMSFEVMAMPPHLAFSQEQQQHATVAAFDRGTLQSNASLWPPPPQPPPSQHPFLLQRFAAAPAEVAGLPFFLAGGVGGAAAAAPAATTNGGERRLQLWDFKEERKT
|
Transcription activator. Binds the promoter core sequence 5'-GGNCC-3'.
|
Q2QM59
|
Q9PWL7
|
HXBAA_DANRE
|
Homeobox protein Hox-B10a
|
Danio
|
MALHRHPFVHGAASWDGEQPSPVQLPHISACPFTSSGRKEDPFYFTLDPTGQARQPLDISAFSRIMTDMGSLNSADDHRPETSFYSGHKLLSLNTDTDPESPSLSSHSDSQHLHSLSLSAPCSETDNKHDMQYLAMESTKYPSQWSESRTNRSIITTLSISQRSKDDIEPNNLQTDFTRGDKTPREKTQDVTLENAANGWLSAKAGRKKRCPYSKHQILELEKEFLFNMYLTRERRLEISRSINLTDRQVKIWFQNRRMKLKKMTREHRTRDPGTSFTV
|
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
|
Q9PWL7
|
Q8K947
|
RS12_BUCAP
|
30S ribosomal protein S12
|
Buchnera
|
MATVNQLVRKPRLRKIVKTNVPALEGSPQKRGVCTRVYTTTPKKPNSALRKVCRVRLTNGFEVTAYIGGEGHNLQEHSVILIRGGRVKDLPGVRYHIVRGSLDCAGVKERKKGRSKYGVKKAKV
|
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
|
Q8K947
|
O94260
|
G3BP_SCHPO
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Putative G3BP-like protein
|
Schizosaccharomyces
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MTAENATLLEPVLGKDEIGWMFVQEYYTYLNKEPNRLHCFYTKKSTLIHGDEGESISLCHGQQEIHNKILDLDFQNCKVLISNVDSLASSNGGIVIQVLGEMSNKGKLSRKFAQTFFLAEQPNGYFVLNDIFRFLREDVEEEEESPDAVEKEKKDVASEPYVNGVQSQEHLPSAKEEGHYQDPAATENNFATAALISNETDSLNQATLAVPEEPVIQVTEASVPSFVSQQENQLQDEALTSNSKNADAIGASDANVATAPKSWADLIARNHPDVKSQASVSSTASTTGQTVKGVNADQTQQPTAPYTQSNELLETSVFVKNIPPETSDVSLKSAMSIFGPVKAIEFARRKGTAYVDFVNHECVQLALNKKTLQINNATLNIEERRRLFSGKFNKSGDKKSNDNYNGMKRNFRKGNRGAFDGRSKEVTTSKKQNN
|
Probable scaffold protein that may be involved in mRNA transport.
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O94260
|
Q5M821
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PPM1H_RAT
|
Protein phosphatase 1H
|
Rattus
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MLTRVKSAVANFMGGIMAGSSGSEHGGSGCGGSDLPLRFPYGRPEFLGLSQDEVECSADHIARPILILKETRRLPWATGYAEVINAGKSTHNEDQASCEVLTVKKKVGTITSTPNRNSKRRSSLPNGEGLQLKENSESEGISCHYWSLFDGHAGSGAAVVASRLLQHHITQQLQDIVEILKNSAILPPTCLGEEPESTPAHGRTLTRAASLRGGVGAPGSPSTPPTRFFTEKKIPHECLVIGALESAFKEMDLQIERERSAYNISGGCTALIVVCLLGKLYVANAGDSRAIIIRNGEIIPMSSEFTPETERQRLQYLAFMQPHLLGNEFTHLEFPRRVQRKELGKKMLYRDFNMTGWAYKTIEDDDLKFPLIYGEGKKARVMATIGVTRGLGDHDLKVHDSNIYIKPFLSSAPEVRVYDLSKYEHGADDVLILATDGLWDVLSNEEVAEAITQFLPNCDPDDPHRYTLAAQDLVMRARGVLKDRGWRISNDRLGSGDDISVYVIPLIHGNKLS
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Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation.
|
Q5M821
|
P29380
|
CYC_ARATH
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Cytochrome c
|
Arabidopsis
|
MQVADISLQGDAKKGANLFKTRCAQCHTLKAGEGNKIGPELHGLFGRKTGSVAGYSYTDANKQKGIEWKDDTLFEYLENPKKYIPGTKMAFGGLKKPKDRNDLITFLEEETK
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Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
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P29380
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