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
|
|---|---|---|---|---|---|---|
A5E8J8
|
PYRF_BRASB
|
OMP decarboxylase
|
unclassified Bradyrhizobium
|
MPTEIAPRDRLIVALDLPGVAEAEAMITRLGDAVTFYKIGMELTYAGGLGLAERLAADGKQVFMDLKLHDIPNTVERATRQIARLGARFLTVHGFSQSMTAALAGAAGSPLELLAVTVMTSYDDADLAAAGYAMGVKELVARRAVQAKQIGIHGLILSPEETQLVRPLVGPDMQLVTPGIRPAGSDVGDQKRIMTPALAIAGGADRLVVGRPVTGAADPAAAAESIVADIASALALVGKTNRT
|
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
|
A5E8J8
|
A1AV74
|
HIS6_RUTMC
|
ImGP synthase subunit HisF
|
Candidatus Ruthia
|
MPLAKRIIPCLDVCNGRVVKGTKFVDIKDAGDPVEVAKRYDFECADEITFLDITASIEGRDTMIHMVEAIAEQVFIPLTVGGGIRKAVDVRAMLNAGADKVAINSAAIFNPNLINQLSEEFGSQCIVIAIDAKKVSDNKWEIFTHGGRKSTGIDAIEWAVKMTKGDNGAGEVLLTSMDCDGVKTGFDLLLTKAASDAVDVPIIASGGVGNLEHLSEGVLQGGADAVLAASIFHFGEYTIQQAKQAMQENGIEVRL
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
|
A1AV74
|
B2TIX0
|
CH60_CLOBB
|
Chaperonin-60
|
Clostridium
|
MAKMLKFGEDARRSMQVGVDKLADTVKVTLGPKGRNVVLDKKFGSPLITNDGVSIAREIELEDPYENMGAQLVKEVATKTNDVAGDGTTTATLLAQAIIREGLKNVTAGANPMLIRNGIRMAVDKAVEEIKKISKPVEGKEDIARVAAISAADEEIGKLIADAMEKVGNEGVITIEESKSMGTELDVVEGMQFDRGYVSPYMSTDTEKMEAILDTPYILITDKKITNIQEILPILEQIVQAGRKLLIIAEDIEGEAMATLVVNKLRGTFTCVAVKAPGFGDRRKEMLEDIAILTGGTVIAEELGRDLKEVTLDMLGQAESVKVSKDNTVVVNGKGNPENIKDRISQIKAQIEETSSEFDKEKLQERLAKLAGGVAVIKVGAATETELKERKLRIEDALAATKAAVEEGIVPGGGTAYINVIKEVEKLTSDVQDTELGIKIIVKSLEEPLRQIASNAGVEGSVIIEKVKNSEVGTGYDALYGKYVNMIKSGIVDPTKVTRSALQNAASVSATFLTTEAAVAEIPQKEPAMPAPGMGMDGMY
|
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.
|
B2TIX0
|
A2SMC9
|
GMHA_METPP
|
Sedoheptulose 7-phosphate isomerase
|
Methylibium
|
MGMLEQRIQRHFFDSADLKNQAAEVLSKPIADAVQAVLGCITAGGKVLACGNGGSASDAQHFAAEFVGRFERERPGLAAIALNTDTSIITALGNDYDFSAIYAKQVQALGNPGDVLLAITTSGNSANVVAAVDAAHDKDMTVIALTGRGGGKLGARLTETDVHICVPHERTARIQEVHILAIHCLCDAVDVQLLGEQDLT
|
Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
|
A2SMC9
|
Q9URM2
|
TKT_SCHPO
|
Probable transketolase
|
Schizosaccharomyces
|
MTSSSYTDIDTLAINTIRTLAVDTTAHAKSGHPGAPMGLAPAAHVLFSRIMKFNPAHPKWLNRDRFILSNGHACVLQYIMCHLLGYKLTIEDLKQFRQVGSKTPGHPETHNPDLNIETGAGPLGQGIASAVGLAIGKAHSAAVYNKPGFDLFSNYTFCFLGDGCLQEGVSSEACSLAGHLKLSNLIAVWDNNKITIDGATSMSFDEDVEKRFEAYGWNIVRVANGDTDLDGIEKGFREAMSCTDKPTLINLKTTIGYGSELQGTHSVHGSPLKPEDCVHVKKLFGFDPTKTFQVPPEVYAYYKERVAIASSAEEEYKKMYASYKQSYPDLSNQLERILSRKFPEGWEKHLPVYKPGDKAVATRKLSEIVLDALCPVLPELVGGSADLTPSNLTRWEGAADFQPPSSKLGTYAGRYIRYGIREHGMAGIMNGLAVYGPIIPYGGTFLNFVSYAAGAVRMAALNNSRVIYVATHDSIGLGEDGPTHQPIETFAHFRAMPNINCWRPADGNETSAAYYSALTSDSTPSILALTRQNLPQLENSTIENALKGGYVMLENKEADITLVGTGSEVSLCIDTVKTLETEYNLKARVVSLPCWEVFEQQPESYRLSVIPDGIPAMSVEVWATNGWRRYVHEAFGMHTFGDSGPAPKLYEKFHFTTSGVAQRAKKTVDAYKDIPYIRSPVRRAF
|
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
|
Q9URM2
|
Q9T6H8
|
CCMF1_ARATH
|
Cytochrome c biogenesis orf382
|
Arabidopsis
|
MSISIYEFFHYSLFLGLFVAFTYNKKQPPAFGAALAFWCILLSFLGLLFCHISNNLSNYNVLTANALFFYQISGTWSNHEGSILLWCWILNFYGFFFCYRGRPQSHNVLKQGGYRESLFFFFVLNFVKNSILSLLRYEQESGLKNQLYTPFVLRTLVDSELCSRRNRTFDGPALFYAPLYPERKIKNPLDAWRFRGSREGKRTHPLLHLARDDKERASSIDEQRIDGALGIALFFSFFLLASSDPFVRNFFVCTEPLAELNPVLQDPILAIHPPCIYAGDVASAEGFGLCRSKMMNGIVALHSPPMRKDAAEKNGTLLCSAGCVGSRITSELFTLKFKHVGAKCYPALLLRSNRSPLMLLRRRFFAFSSFWAGARSHSTKRY
|
Forms a complex with CCMFC, CCMFN2 and CCMH that performs the assembly of heme with c-type apocytochromes in mitochondria.
|
Q9T6H8
|
Q1J4W9
|
TIG_STRPF
|
PPIase
|
Streptococcus
|
MISRIKSFKNALNYDKMNCIEIILRRNDLMSTSFENKATNRGVITFTISQDKIKPALDKAFNKIKKDLNAPGFRKGHMPRPVFNQKFGEEVLYEDALNIVLPEAYEAAVTELGLDVVAQPKIDVVSMEKGKEWTLSAEVVTKPEVKLGDYKNLVVEVDASKEVSDEDVDAKIERERQNLAELIIKDGEAAQGDTVVIDFVGSVDGVEFDGGKGDNFSLELGSGQFIPGFEDQLVGAKAGDEVEVNVTFPESYQAEDLAGKAAKFMTTIHEVKTKEVPELDDELAKDIDEDVDTLEDLKVKYRKELEAAQETAYDDAVEGAAIELAVANAEIVDLPEEMIHEEVNRSVNEFMGNMQRQGISPEMYFQLTGTTQEDLHNQYSAEADKRVKTNLVIEAIAKAEGFEATDSEIEQEINDLATEYNMPADQVRSLLSADMLKHDIAMKKAVEVITSTASVK
|
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.
|
Q1J4W9
|
Q8KDE3
|
ARGC_CHLTE
|
N-acetyl-glutamate semialdehyde dehydrogenase
|
Chlorobaculum
|
MNHIPMQNKKVTVSVIGASGYSGAELVKLLMKHPGIVIEELYAHTQAGKRFTELYPSIPCDKTFQTYAGQTNSDVYLLALPHGEALQLVPGIVAAGKKVIDLSGDFRLKNTAEHKRFYGGDKSAEDVLQYGMPELFRDEIAGSTAISNPGCYATSIILGLAPLFLGGMAGLDVESVNVTAVSGISGAGRSAKLELSFSEMSGNMRAYKVGKHQHTPEIMQTLGTSVTDPSFRFVFTPMIAPYVRGIYSVLNVRLASPVAMEPVRELYAGFYANAPFVRLRDGVTEVSHVAYTNFCDISLAFESDGSLVIITAIDNLVKGAAGQAVQNMNLMLGFGETTALL
|
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
|
Q8KDE3
|
Q49SP7
|
TPSCS_POGCB
|
PatTpsA
|
Pogostemon
|
MAAFTANAVDMRPPVITIHPRSKDIFSQFSLDDKLQKQYAQGIEALKEEARSMLMAAKSAKVMILIDTLERLGLGYHFEKEIEEKLEAIYKKEDGDDYDLFTTALRFRLLRQHQRRVPCSVFDKFMNKEGKFEEEPLISDVEGLLSLYDAAYLQIHGEHILQEALIFTTHHLTRIEPQLDDHSPLKLKLNRALEFPFYREIPIIYAHFYISVYERDDSRDEVLLKMAKLSYNFLQNLYKKELSQLSRWWNKLELIPNLPYIRDSVAGAYLWAVALYFEPQYSDVRMAIAKLIQIAAAVDDTYDNYATIREAQLLTEALERLNVHEIDTLPDYMKIVYRFVMSWSEDFERDATIKEQMLATPYFKAEMKKLGRAYNQELKWVMERQLPSFEEYMKNSEITSGVYIMFTVISPYLNSATQKNIDWLLSQPRLASSTAIVMRCCNDLGSNQRESKGGEVMTSLDCYMKQHGASKQETISKFKLIIEDEWKNLNEEWAATTCLPKVMVEIFRNYARIAGFCYKNNGDAYTSPKIVQQCFDALFVNPLRI
|
Sesquiterpene synthase involved in gamma-curcumene biosynthesis.
|
Q49SP7
|
B5XJ09
|
MUTL_STRPZ
|
DNA mismatch repair protein MutL
|
Streptococcus
|
MTNIIELPEVLANQIAAGEVVERPASVVKELVENAIDAKSSQITVEIEESGLKMIQVTDNGEGMSHEDLPLSLRRHATSKIKSQSDLFRIRTLGFRGEALPSVASISKITIKTATKEVTHGSLLIATGGEIETLEAISTPTGTKIKVENLFYNTPARLKYMKSLQAELAHIVDVVNRLSLAHPEVAFTLISDGRQLTQTSGTGDLRQAIAGIYGLNTTKKMLAISNADLDFEVSGYVSLPELTRANRNYMTILVNGRYIKNFLLNRAILDGYGSKLMVGRFPIVVIDIQIDPYLADVNVHPTKQEVRISKERELMALISTAISESLKEQDLIPDALENLAKSSTRHFSKPEQTQLPLQSRGLYYDPQKNDFFVKESAVSEKIPETDFYSGAVDNSIKVEKAELLPHSEEVIGPSSVKHASRPQNIFTETDHPNLDLKNRQKLSQMLTRLENEEKSVFPELDYFGQMHGTYLFAQGKDGLFIIDQHAAQERVKYEYYRDKIGEVDSSLQQLLVPYLFEFSGSDFINLQEKMALLNEVGIFLEVYGHNTFILREHPIWMKEEEIASGVYEMCDMLLLTNEVSIKTYRAELAIMMSCKRSIKANHSLDDYSARNLLLQLAQCQNPYNCPHGRPVLINFSKADMEKMFRRIQENHTSLRELGKY
|
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
|
B5XJ09
|
Q14FF9
|
RR14_POPAL
|
30S ribosomal protein S14, chloroplastic
|
Populus
|
MARKSLIQREKKRQKLEQKYHLIRRSSKKEISKVPSLSDKWEIHGKLQSPPRNSAPTRLHRRCFLTGRPRANYRDFGLSGHILRAKVHACLLPGATRSSW
|
Binds 16S rRNA, required for the assembly of 30S particles.
|
Q14FF9
|
P35575
|
G6PC1_HUMAN
|
Glucose-6-phosphatase alpha
|
Homo
|
MEEGMNVLHDFGIQSTHYLQVNYQDSQDWFILVSVIADLRNAFYVLFPIWFHLQEAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPSGHAMGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETFSHIHSIYNASLKKYFLITFFLFSFAIGFYLLLKGLGVDLLWTLEKAQRWCEQPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMYRESCKGKLSKWLPFRLSSIVASLVLLHVFDSLKPPSQVELVFYVLSFCKSAVVPLASVSVIPYCLAQVLGQPHKKSL
|
Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production in the terminal step of glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels.
|
P35575
|
Q8PH57
|
PEPQ_XANAC
|
Proline dipeptidase
|
Xanthomonas
|
MPQPSLSSLYSDHLRTLTARADEALQRGGFEHLVVPSGSTHYQLFDDRDYPYAVNPQFKAWVPLTRVPDSWLVYTPGKRPTVIFYQPFDYWHVVPDAPSGWWVDHCDIHIIRTPDQALALLPKHAERCAILGEPHSTLGAYVPNNPQPVLDYLEYQRAFKTPYELALLRIAQQLAVRGHRAAEAAFRAGQSEFGIHMAYCAAVGQDANDLPYGNIIALNEHGAVLHYTELGQQPPQPLRSFLIDAGASAYGYASDITRTYAADPDSDFQALIDAVDAAQLRMGQNVRAGVDYKQLHIDAHLALMGILKEFGILTVSPEAALATGVSAAFFPHGLGHLIGLQVHDVAGFAASDRGGRIERPPGHPYLRLTRVLEPGMVVTIEPGVYFIDMLLDEVKKNGHAASVDWQRVEAFKPYGGIRIEDEVVCTDGSAENLTRPVFAAA
|
Splits dipeptides with a prolyl residue in the C-terminal position.
|
Q8PH57
|
Q52666
|
BZTD_RHOCB
|
Glutamate/glutamine/aspartate/asparagine transport ATP-binding protein BztD
|
Rhodobacter
|
MSEPSYDHQVDRSHMQVSDEIAIQISQMNKWYGQFHVLRDINLTVHRGERIVIAGPSGSGKSTMIRCINRLEEHQSGKIIVDGIELTSDLKNIDKVRSEVGMVFQHFNLFPHLTILENLTLAPIWVRKVPKREAEETAMYYLEKVKIPEQAQKYPGQLSGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMIKEVLDTMIQLAEEGMTMLCVAHEMGFAQAVANRVIFMADGQIVEQNNPHDFFRNPQSERTKQFLSQILGH
|
Part of a binding-protein-dependent transport system for glutamate, glutamine, aspartate, asparagine. Probably responsible for energy coupling to the transport system.
|
Q52666
|
F4JWS8
|
QCR72_ARATH
|
Ubiquinol-cytochrome c oxidoreductase subunit 7-2
|
Arabidopsis
|
MASFLQRLVDPRKNFLARMHMKSVSNRLRRYGLRYDDLYDPLYDLDIKEALNRLPREIVDARNQRLMRAMDLSMKHEYLPDNLQAVQTPFRSYLQDMLALVKRERAEREALGALPLYQRTIP
|
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of 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. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
|
F4JWS8
|
Q737Z5
|
PLSY1_BACC1
|
Lysophosphatidic acid synthase 1
|
Bacillus cereus group
|
MINSMQFLYLVASYLFGNILTAYIVTKWRHDVDIRNEGSGNPGARNMGRVYGKGYFIVTFLGDAIKGAIVVSIAEYLFGDSTFVMLALLAVLLGHIYPIVFKGKGGKGISTFIGGLIAFDYLIALTLVAVFIIFYLIFKGFTKPGLITIACLPVCMILYSYSIVTTILSALIIVLILYVNRD
|
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
|
Q737Z5
|
A1ANL2
|
COWN_PELPD
|
CO weal-nitrogenase
|
Pelobacter
|
MQKMTETDRYVTFKGIDGDGNARRLVAMLRRHIDDPAKTNLFWEKFKEKLELAESPDTNNTRRLDELFLIHSYINNIYDLLEEHGDQEALTLLHQIEVESC
|
Is required to sustain N(2)-dependent growth in the presence of low levels of carbon monoxide (CO). Probably acts by protecting the N(2) fixation ability of the nitrogenase complex, which is inactivated in the presence of CO.
|
A1ANL2
|
Q2RB33
|
NAC45_ORYSJ
|
NAC domain-containing protein 45
|
Oryza sativa
|
MVETSTSLVKLEQDGSLFLPPGFRFHPTDAEVILSYLLQKFLNPSFTSLPIGEVDLNKCEPWDLPSKAKMGEKEWYFFSHKDMKYPTGMRTNRATKEGYWKATGKDREIFNLQPTSYGGSSNNKNNKQLVGMKKTLVFYMGRAPKGTKTNWVMHEFRLHANLHNDNPNLRLNLKDEWVVCKVFHKKGDDREAINKQQAQAAAVDQYSAGTPNNGSSVEAGDDDDDLFQLDSIIDPSIYFSNSSAANILSAPPNMSNSVVAANYGASTTTTGTASAGSFQQQPNYCSLINKSISSSNVSSWNNMPPPPPVAEGGVHGIGSSYSLQHQAAMVKALRDVIRLPNPLGMPQYKLDDAYLWDSS
|
Transcription activator involved in responses to drought stress and salt stress. Transactivates the stress response genes LEA19 and PM19L.
|
Q2RB33
|
M5BGY5
|
DID_ATHCH
|
Disintegrin DS-AC
|
Atheris
|
MIQVLLVIICLAVFPYQGSCIILESENVNDYEIVYPKKLTVLPTGAMNSPHPCCDPVTCKPKKGEHCISGPCCRNCKFINSGTICKKARGDDMNDYCTGTTPDCPRNPYKD
|
Inhibits ADP-induced platelet aggregation in human platelet-rich plasma (IC(50) is 6 uM).
|
M5BGY5
|
Q2RTB8
|
GLYA2_RHORT
|
Serine hydroxymethyltransferase 2
|
Rhodospirillum
|
MTAYTPWTGFFSASVAQADPELDRVLRAELSRQQDQIELIASENIVSRAVLEAAGSVLTNKYAEGYPGKRYYGGCEEVDVAEELAIERAKALFGCSYVNVQPHSGAQANGAVMMALVKPGDTIMGMSLAAGGHLTHGAPPAQSGKWFNAVQYGVRLQDASIDFDEVATLAETHKPKLIIAGGSAYPRIIDFAKFREIADRVGALFMVDMAHFAGLVAAGLHPSPLPYADIVTTTTHKTLRGPRGGMVLSNNPDIGKKINSAVFPGLQGGPLMHIIAAKAVAFGEALRPEFKVYAQAVIDNAKALTDALAAGGLNIVSGGTDTHLALVDLRPKALTGNIVEKSLERANITTNKNGIPFDPEKPAITSGIRVGTPAGTTRGFGTAEFTEIGKLIVEVLDGLAANGEDNSQAEAAVREKVAVLCRRFPIYGGL
|
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
|
Q2RTB8
|
Q02643
|
GHRHR_HUMAN
|
Growth hormone-releasing factor receptor
|
Homo
|
MDRRMWGAHVFCVLSPLPTVLGHMHPECDFITQLREDESACLQAAEEMPNTTLGCPATWDGLLCWPTAGSGEWVTLPCPDFFSHFSSESGAVKRDCTITGWSEPFPPYPVACPVPLELLAEEESYFSTVKIIYTVGHSISIVALFVAITILVALRRLHCPRNYVHTQLFTTFILKAGAVFLKDAALFHSDDTDHCSFSTVLCKVSVAASHFATMTNFSWLLAEAVYLNCLLASTSPSSRRAFWWLVLAGWGLPVLFTGTWVSCKLAFEDIACWDLDDTSPYWWIIKGPIVLSVGVNFGLFLNIIRILVRKLEPAQGSLHTQSQYWRLSKSTLFLIPLFGIHYIIFNFLPDNAGLGIRLPLELGLGSFQGFIVAILYCFLNQEVRTEISRKWHGHDPELLPAWRTRAKWTTPSRSAAKVLTSMC
|
Receptor for GRF, coupled to G proteins which activate adenylyl cyclase. Stimulates somatotroph cell growth, growth hormone gene transcription and growth hormone secretion.
|
Q02643
|
A7MJ90
|
NFI_CROS8
|
Deoxyribonuclease V
|
Cronobacter
|
MDLATLRAQQIELASNVVREDRLNVDPPTIIGGADVGFEQGGEVTRAAMVLLKYPSLELLEYQVARIPTTMPYIPGFLSFREYPALLTAWEMLSRKPDLLFVDGHGISHPRRLGVASHFGMLVDVPTIGVAKKRLCGKFEPLSDEPGAVSPLMDKGEQLAWVWRSKARCNPLFVSTGHRVSIDTALGWVQRCTKGYRLPEPTRWADAVASGRPAFLRWQEIQG
|
DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
|
A7MJ90
|
O84799
|
DNAG_CHLTR
|
DNA primase
|
Chlamydia
|
MYYTEESLETLKHSIDIVSVLGEYVHLKRSGADYKACCPFHDEKTPSFIVYPTRGHYHCYGCGEHGDAINFLMKQQGYSFSEAVLFLAKKFHVDLVVRTKETSGQDSKDSLRRINREAERFFQYCLLHLPEGEEALAYLYKRGFSPDTIDRFQIGYAPEQRLFIQAMEERNISVKQLEWAGYLAKDWFLFAQRIMFPIQDALGYTIGFSSRRFKEGGRGGKYINSPETILFKKSRVLYGLQFSRKRIAKERRVILVEGQADCLQMIDFGFNCTLAAQGTSFTETHVHELVKLGVSKAYLLFDGDAAGEKASLRVGDLCQAAGITAIVCRLPSGQDPDSFLMQRGPEELRELLDRGEDYLSFLVWHKIHSYEQFTPREKARVIEEVIQQVRCWGSPITIHEYLRQLASLVKVPEPAVLSYLSSITSAAEDKGKKVSAKEPSSESKQTSTEGKISKKISPRMILEADVIRCLLFAKPEDEFVPATVKQYLSPEEFHCAEYRAIFVMAMNHYNDRQTLPSMDEMMSLVVGTEAMTLLVARRMNTELMRDIVVQSIQKLLDKHWRDKKRKLCHQTGKGLDSLQEYVRLSGERVKVSLVS
|
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
|
O84799
|
B4TYW7
|
UVRC_SALSV
|
Excinuclease ABC subunit C
|
Salmonella
|
MSEIFDAKAFLKTVTSQPGVYRMYDAGGTVIYVGKAKDLKKRLSSYFRSNLASRKTEALVAQIQHIDVTVTHTETEALLLEHNYIKLYQPRYNVLLRDDKSYPFIFLSGDTHPRLAMHRGAKHAKGEYFGPFPNGYAVRETLALLQKIFPIRQCENSVYRNRSRPCLQYQIGRCLGPCVAGLVSEEEYTQQVEYVRLFLSGKDDQVLTQLIARMEKASQDLAFEEAARIRDQIQAVRRVTERQFVSNAGDDLDVIGVAFDAGMACVHVLFIRQGKVLGSRSYFPKVPGGTELGEVVETFVGQFYLQGSQMRTLPGEILLDFNLSDKTLLADSLSELAGRRIHVQTKPRGDRARYLKLARTNAATALITKLSQQSTITQRLTALAAVLKLPAIKRMECFDISHTMGEQTVASCVVFDANGPLRAEYRRYNIAGITPGDDYAAMNQVLRRRYGKAIEESKIPDVILIDGGKGQLAQAKAVFAELDVPWDKHRPLLLGVAKGADRKAGLETLFFEPEGEGFSLPPDSPALHVIQHIRDESHDHAIGGHRKKRAKVKNTSTLETIEGVGPKRRQMLLKYMGGLQGLRNASVEEIAKVPGISQGLAEKIFWSLKH
|
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.
|
B4TYW7
|
C8V3Y7
|
ATND_EMENI
|
Aspercryptin biosynthesis cluster protein D
|
Aspergillus subgen. Nidulantes
|
MANPERSYLSRFFSSQFSKLPYPSQSFKDAVILVTGGNTGLGLEAARHFVRLQAATVILAVRDLKKGEQAKLSIEESTKVQGVVEVWQVDLEDVRSVQSLAAKASSLPRLDVVVANAGISTNKWALVGDMERTIQVNVLSTFLLILALLPKMQEQDIEGQIRARPRVVVVSSEGHETTAFAERKAARIFDALRDQRQANMDERYDTSKLIQLYLVRALAERLSRSDKPPVTLNAVSPGLCKTGLLRETPLVARLLTGPVMAILARNAEEGSRTLVHAAAANDGETNGKYLRDYLQRLYAAKKATPRRRDCCRSF
|
Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) . The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol . The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM . The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps . First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ . the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains . The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr . Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr . After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide . Further reduction would generate aspercryptins . The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version . AtnB seems to be involved in the selectivity for Ile versus Val by the third module . Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively .
|
C8V3Y7
|
Q4KJF1
|
NHAP2_PSEF5
|
Potassium/proton antiporter NhaP2
|
Pseudomonas
|
MNATTINSLFLIGALLVGASILVSSLSSRLGIPILVIILAVGMTAGVDGGGIIFDNYPTAYLVGNLALAVILLDGGLRTRVASFRVALWPALSLATVGVLITTGLTGMAAAWLFDLNLIQGLLIGAIVGSTDAAAVFSLLGGKGLNERVTASLEIESGSNDPMAVFLTVTLIDMLASGHTGLHWSLLTDLIREFGIGAVIGLGGGWLMLQLVNRIHLATGLYPILVVAGGLVVFALTNALHGSGFLAVYLCGLVIGNRPVRSRHGILHMLDGMAWLAQIGMFLVLGLLVTPHDLLPIALPALGLALWMILFARPLSVLVGLAPFKAFHGREKAFISWVGLRGAVPIILAVFPLMAGLPNAQLYFNLAFFIVLISLLVQGTSLPWVAKWLKVTVPPEPAPISRAALEVHVTSEWELFVYRLGAEKWCIGAALRELKMPEGTRIAALFRGQQLLHPSGSTVLEADDLLCVIGHEHNLPALGKLFSQAPERGLDLRFFGDFVLEGDAQLGAVSALYGLKLDGQDADMPLGAFIAQKVGGAPVVGDQVEWNNTIWTVAVMDGNKIGKVGVRFPEGSRPGPGLFL
|
K(+)/H(+) antiporter that extrudes potassium in exchange for external protons and maintains the internal concentration of potassium under toxic levels.
|
Q4KJF1
|
Q1QH71
|
ARGB_NITHX
|
NAG kinase
|
Nitrobacter
|
MSDASRISPLDQARILSEALPHMQQYDEETIVIKYGGHAMGAEDVARQFARDIVLLEQTAINPVVVHGGGPQIATMLQRLGIKSEFAAGLRITDAATIEIVEMVLAGSINKQLVGYINEAGGKAVGLCGKDGNMVTASKATRTIADPDSNIEKVVDLGFVGEPEKVDLTLLNQLIGHELIPVLAPLATSKGGQTFNVNADTFAGAVAGALKAKRLLLLTDVPGVLDKSKKLIPDLSIGDARKLIADGTISGGMIPKVETCIYALEQGVGGVVIIDGKTPHAVLLELFTDQGTGTLIHK
|
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
|
Q1QH71
|
B5XKQ0
|
ATPG_STRPZ
|
F-ATPase gamma subunit
|
Streptococcus
|
MAGSLSEIKAKIISTEKTSKITSAMRMVSSAKLVKSEQAARDFQIYASKIRQITTDLLKSELTIGSDNPMLVSRPVKKTGYIVITSDKGLVGGYNSKILKSVMDMITEYHADGDYEIISIGSVGSDFFKARGMNVAFELRGLADQPSFEQVRQIISQSVDMFVNEIFDELYVCYNHHVNSLTSQVRVQQMLPISDLVADEAAEEGVTGFELEPNRQDILDQLLPQFTESLIYGAIIDAKTAEHAAGMTAMQTATDNAKNVINDLTIQYNRARQAAITQEITEIVAGANALE
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
|
B5XKQ0
|
Q0C2D0
|
PTH_HYPNA
|
Peptidyl-tRNA hydrolase
|
Hyphomonas
|
MLILSGQGNPGAKYAKNRHNAGFLVIDRIHDAYGFGPWRTKFDAEISEGTVETANGRQRVLLIKPQTFYNETGRSVSKAVTFYKLQPEDVTVFHDEIDLAPGRLRVKRGGGHSGNNGARSMMAHLGENFRRIRIGVGHPGDKAMVMPHVLSDFHKVDLEWFEPMTEAVCKALPFLLAGDDERFQTEVMRLAPAPKHDPKQTARKGEA
|
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
|
Q0C2D0
|
B7H746
|
MURC_BACC4
|
UDP-N-acetylmuramoyl-L-alanine synthetase
|
Bacillus cereus group
|
MTVYHFVGIKGTGMSSLAQILHDMKHTVQGSDYEKRFFTQTALEKRSISILPFDKNNVEEGQVIIAGNAFPDTHEEIVAAKELNIPVHRYHHFLGDLMSQYTSVAVTGAHGKTSTTGLLAHVMQGAHPTSYLIGDGTGHGVENSKYFVFEACEYRRHFLSYNPDYAIMTNIDFDHPDYFADINDVFSAFQEMALQVKKGIIACGDDEELQKIQAKVPVIFYGFGEDNDFQARNIQKRTDGTIFDVFVRNTYYDTFKITGYGNHSVLNALAVIALCHYENVDVEAVKHQLTTFEGVKRRFNEKPMGEQVIIDDYAHHPTEINATIEAARQKHPEREIVAVFQPHTFSRTEKFLDEFAESLSKADQVYLCDIFGSARENKGELTIEDLQKRIDGAELITDTTTDVLKKHKNGVLIFMGAGDIQKFEAAYVKEVQVAEK
|
Cell wall formation.
|
B7H746
|
Q834D8
|
LSPA_ENTFA
|
Signal peptidase II
|
Enterococcus
|
MTRLLVVYFLISALLVGLDQWSKYLTVQNISLGETKEFIPGFLSLTHLRNTGAAWSLLEGKMIFFYVITVIVSVVIIYLLIKNYKKSIWYSVGLSFVLAGAIGNFIDRVRLGYVVDMLQTDFMNFPIFNVADSTLVVGVICIFIYLILDEKAAKEGKNGTN
|
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
|
Q834D8
|
Q8KLG1
|
NODI_RHIEC
|
Nodulation ATP-binding protein I
|
Rhizobium
|
MPVNGARRSDERMFMTAIDFSDVSKTYGDKAVVSALSFRVSPGECFGLLGPNGAGKSTIARMILGMTAPDAGKITVLGVPVPAQARLARKGIGVVPQFDNLEPEFTVRENLLVYSRYFGMNTRKVEAVMSSLLEFARLESKVNARVSELSGGMKRRLTLARALINDPQLLVMDEPTTGLDPHARHLIWERLRSLLTRGKTIILTTHFMEEAERLCDRLCVLEGGRSIAEGRPHDLIDELIGCEVIEIYGGDPHELESLVGPYADRIEISGETLFCYVSDPEQVRVRLRQRAGLRILQRPPNLEDVFLRLTGREMEK
|
Part of the ABC transporter complex NodIJ involved in the export of the nodulation factors (Nod factors), the bacterial signal molecules that induce symbiosis and subsequent nodulation induction. Nod factors are LCO (lipo-chitin oligosaccharide), a modified beta-1,4-linked N-acetylglucosamine oligosaccharide. This subunit is responsible for energy coupling to the transport system.
|
Q8KLG1
|
Q4L7C3
|
CRCB2_STAHJ
|
Putative fluoride ion transporter CrcB 2
|
Staphylococcus
|
MQYLFVFIGGLFGALLRYVLSTLNVDSGLPLGTLIANIVGAFLMGYLSSLSIHFFKNNPLIKKGVTTGLLGALTTFSTFQFELVTMSQNNSIALLFIYGLTSYIGGILFCWFGVKLGGQPT
|
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
|
Q4L7C3
|
Q99NA5
|
IDH3A_RAT
|
NAD(+)-specific ICDH subunit alpha
|
Rattus
|
MAGSAWVSKVSRLLGAFHNTKQVTRGFAGGVQTVTLIPGDGIGPEISASVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPPEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAENCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTQSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAAKIEAACFATIKDGKSLTKDLGGNSKCSDFTEEICRRVKDLD
|
Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
|
Q99NA5
|
Q7F2L3
|
NAC48_ORYSJ
|
Protein STRESS-RESPONSIVE NAC 2
|
Oryza sativa
|
MSGGQDLQLPPGFRFHPTDEELVMHYLCRRCAGLPIAVPIIAEIDLYKFDPWQLPRMALYGEKEWYFFSPRDRKYPNGSRPNRAAGSGYWKATGADKPVGSPKPVAIKKALVFYAGKAPKGEKTNWIMHEYRLADVDRSARKKNSLRLDDWVLCRIYNKKGGLEKPPAAAVAAAGMVSSGGGVQRKPMVGVNAAVSSPPEQKPVVAGPAFPDLAAYYDRPSDSMPRLHADSSCSEQVLSPEFACEVQSQPKISEWERTFATVGPINPAASILDPAGSGGLGGLGGGGSDPLLQDILMYWGKPF
|
Transcription activator that binds to the promoter of the stress response gene LEA19. Involved in tolerance to abiotic stresses . Transcription activator involved in response to abiotic and biotic stresses. Involved in drought and salt stress responses, and defense response to the rice blast fungus . Transcription activator involved tolerance to cold and salt stresses . Transcription activator involved in tolerance to drought stress. Targets directly and activates genes involved in membrane modification, nicotianamine (NA) biosynthesis, glutathione relocation, accumulation of phosphoadenosine phosphosulfate and glycosylation in roots . Controls root growth at early vegetative stage through chromatin modification and histone lysine deacytaltion by HDAC1 .
|
Q7F2L3
|
Q05974
|
RAB1A_LYMST
|
Ras-related protein Rab-1A
|
Lymnaea
|
MSTMNPDYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDFTTAKEYADQLGIPFLETSAKNATNVEQAFMTMAAEIKNRMGPITAASDSKPSVKINSSTPVSANKGGCC
|
Probably required for transit of protein from the ER through Golgi compartment.
|
Q05974
|
Q28E95
|
SH3R1_XENTR
|
SH3 domain-containing RING finger protein 1
|
Silurana
|
MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVSSRNELRCPECRTLVECGVDELPSNILLVRLLDGIKQRPRKAGVGGSAGNSTNVLRAQGSLTTNCGLNDAQNIHGGQQRIQARSPPVRGVPQLPCAKALYNYEGKEPGDLKFNKGDIIVLRRQVDENWYHGEINGIHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFLKDDILTVIRRVDENWAEGMLGDKIGIFPISYVEFNSAAKQLIELDKPSGVDTGEGSSGTTHSSNSQKQADAKKNTKKRHSFTSLTMSNKSSQSVQNRHSMEISPPVLISSSNPTAAARISELTGLSCSAPSQVHISTTGLIVTPPPSSPVVSGPAFTFPPEVTYQAALGDLNPPLLPPPPLATPVITSTSSGAAAAVQRSISGPAEQVTHLRTSTRPSVFVAIYPYIPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFPGNYVAPVTRALTTATPAKVAMATASSSNVVNLVTPTPPGAPCQKLQGNGAEFAKTVSTNGVPPAGIPGSHIQSSPQAKVLLHMSGQMTVNQARNAVRTAAAHSQDRPTAAVTPIQAQIPSASVLPQQAATSQQMPPPLSGPAAYINAAMNISRPSVPVASAASSSVSSAAFETECNWKSGSGLAACSFPENVSAPLNSAANKQDKDSKKEKKGLLKLLSGASTKRKPRSSPPHSPTQELEQTNSEAALEGAVGPDILPVNGNGRVASCTVDCDLVSASALVQDNRKPASLDTNVPIAPPPRQPCSSLGTVLNDSRPCERYRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI
|
Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Acts as a scaffold protein that contributes to the effective activation of the JNK signaling pathway.
|
Q28E95
|
A6TGJ0
|
CYAY_KLEP7
|
Iron-sulfur cluster assembly protein CyaY
|
Klebsiella
|
MNDSEFHRLADSLWMTIEERLDDWDGDSDIDCEINGGVLTISFENGSKIIINRQEPLHQVWLATKQGGYHFDLKGDEWICDRSGETFWDLLEQAASQQAGETVKFR
|
Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis.
|
A6TGJ0
|
Q31CU1
|
GLMM_PROM9
|
Phosphoglucosamine mutase
|
Prochlorococcus
|
MQSIFGTDGIRGRFNEEITYSLAYKVGYALGSNLENNNPILIGRDTRISGDILLHAITKGINASGKKFINLGICPTPAIPFLIKQEQLSSGIMISASHNPPEYNGIKIFDHNGQKITKNFENKIQKFIEESNQNISVTTKEISLKANKELMDIYMKSLIQSMGGENLSGMKIILDTCYGSATTCAKKIFQSLGADVRVLNNSKNGLKINVNCGSTNLEPLKKALRQSPADMGFSFDGDSDRVIGLDSKGNVLDGDHILFLWGRELMEQKILTNNLLISTQMANLGFEEAWNKIGGLLYRTDVGDKYVHDAIKEKRAVLGGEQSGHILSKINNFSGDGILTALQISKYCKKKNITLNNWLKTSFEPFPQKLTNINLNFNINKVNQKTRILINQTTENFQKIYSDNCRIYIRPSGTEPLMRVLVEAKSHKKVDSLSSEIANKLILEINKIMN
|
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
|
Q31CU1
|
A6VCL8
|
DNAK_PSEA7
|
Heat shock protein 70
|
Pseudomonas
|
MGKIIGIDLGTTNSCVAILENGNVKVIENAEGARTTPSIIAYTNDGETLVGQPAKRQAVTNPQNTLYAVKRLIGRRFEENVVQKDIQMVPYSIVKADNGDAWVEVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGLDKAKGDHTVIVYDLGGGTFDVSVIEIAEVDGEHQFEVLATNGDTFLGGEDFDIRLIDYLVDEFKKESGINLKGDPLAMQRLKEAAEKAKIELSSTQQTDVNLPYVTADASGPKHLNVKVSRAKLESLVEDLVQRTIEPCRTALKDAGLDVSDIHEVILVGGQTRMPLVQKTVAEFFGKEARKDVNPDEAVAVGAAIQGAVLAGDVKDVLLLDVTPLTLGIETLGGVMTGLIEKNTTIPTKKSQVFSTADDNQGAVTIHVLQGERKQAAQNKSLGKFDLADIPPAPRGVPQIEVTFDIDANGILHVSAKDKATGKQQSIVIKASSGLSEDEIQQMVRDAEANAEEDRKFEELAAARNQGDALVHATRKMITEAGDKATAEDKATIEKALGELEVAVKGDDKAEIEAKMNALSQASAPLAQKMYAEQAQQGEGAAQGEQAKSADDVVDAEFEEVKDNK
|
Acts as a chaperone.
|
A6VCL8
|
A9A079
|
PYRR_DESOH
|
Uracil phosphoribosyltransferase
|
Desulfosudis
|
MEMEKRTPVLDGQGINTVLIRLAREIIQRHTNLEPLVIIGVHTRGVHLARRLADTIAEINGRAIPTGDIDITLYRDDWTKIGYSPVVQSTQIGFPIDDKTVILVDDVLFTGRTTRAALDALTDFGRPAKVELAVLVDREGMRELPIQADYVGMFVKTDKAEMVNVLLSETDGEDAVVVNTP
|
Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant.
|
A9A079
|
A4SNI2
|
CDD_AERS4
|
Cytidine aminohydrolase
|
Aeromonas
|
MHPRFAKPLDTLSAPLKAALLPMLDNDFQARFTPQQVATLKAATGLEDRALRLALLPLAAACSVAPISKFFVGAIACGLSGTWYFGANMEFAGQGLFHSVHAEQSAISNAWLGGETGISEITVNYTPCGHCRQFMNELSTAKTLQVSLPDDLSALQSFLPHSFGPADLDITDALMSPQAHDELVLESEDPIWRAALAAARQSYAPYSQGYAAVALLFADGRLFCGRYAENAAFNPSLPPMQMACAHAVLCGEDLASIRRAVLLESKNGQISQRDSAQSTLKALGSVELEYQAV
|
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
|
A4SNI2
|
Q6DAQ3
|
TATB_PECAS
|
Sec-independent protein translocase protein TatB
|
Pectobacterium
|
MFDIGFGELLLVMVLGLIVLGPERLPVAVRTVASWIRTLRSLASTVQNELSQELKLQEFQESLKKVEKASLQNLSPELKASMDELKDAAEAMKRGYTETPSPQKSDDPKKSGDHSATVEPQSNIPLNDPEAAYDGVIEAETAVRPADSQQKPENAAVAENHNDGRHATSDEAVGNNNVKPEQSQPSAASARQPSDSR
|
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
|
Q6DAQ3
|
A3QF19
|
HIS5_SHELP
|
ImGP synthase subunit HisH
|
Shewanella
|
MSNPDTIIIDTGCANLSSVRYAFERIGADVEVSDDIDKIKAATRVVLPGVGTARAAMKALKDKKLIDTICSLTQPVLGVCLGMQMLTKASQERGGLSYGNSSKDCQCLGLIDTNIEQLDAKGLPLPHMGWNQISPSEHPLFAGVAEGSYVYFVHSYRAPLGDFTIAKCEYGEGFSAAIAKDNFMGVQFHPEKSAAVGATILRNFMKMNAGSFAGNHKSTQESAQ
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
|
A3QF19
|
B2ILG7
|
NUOD2_BEII9
|
NDH-1 subunit D 2
|
Beijerinckia
|
MDEAGFRNFTVNFGPQHPAAHGVLRLVLELDGEVVERADPHIGLLHRGTEKLIEYRTYLQALPYFDRLDYVAPMNQEHAFCLAIEKLLQMPVPRRGQLIRVLFCEIGRLLSHLLNITTQALDIGALTPPLWGFEEREKLMVFYERASGARMHANYFRVGGVHQDLPEKLLDDIWNFCEPFLKVCNDLEELLSYNRIFKQRNVDVGVISLDEAWTRGFSGVMVRGSGAAWDLRKAQPYECYDELQFDIPVGKHGDCYDRYLIRMEEMRQSVRIMKQCLEKLSSVDGKGPIIEQNHKVTPPRRSEMKRSMEALIQHFKLYTEGHHVPAGEVYAAVEAPKGEFGVYLISDGSNIPYRCKIRAPSFAHLQAIDFLSHKHMLADVSAIIGSLDIVFGEIDR
|
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.
|
B2ILG7
|
Q6LT55
|
CMOA_PHOPR
|
Carboxy-S-adenosyl-L-methionine synthase
|
Photobacterium
|
MRMAGQDNIFAAPIEKLGDFTFDQKVAEVFPDMIQRSVPGYSNIISAIGMLAERFAKPHSKIYDLGCSLGAATLSMRRSIQQEGCEIIAVDNSAAMVERCRLHIDAYRSDTPVQVVEADIRNIDIADASVVVLNFTLQFLVPEDRQMLLEKIYAGLRPGGILILSEKYIFDDEQAHELLINLHHDFKRANGYSELEISQKRSAIENVMRPDSIDTHKKRLTEIGFSSTEVWFQCFNFGSMFAIK
|
Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
|
Q6LT55
|
Q5ASI4
|
NACB_EMENI
|
Beta-NAC
|
Aspergillus subgen. Nidulantes
|
MDQAKLARMQASVRIGGKGTPRRKVKKVHKTSGADDKKLQATLKKMNVQPIQAIEEVNMFKEDGNVIHFAAPKEERALTVGCEIKVHASVPSNTFALYGNGEEKELTELVPGILNQLGPDSLASLRKLAESYQNMQKNQAGEKKDDDEDDIPDLVEGENFEKSVD
|
Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. EGD1 may act as a transcription factor that exert a negative effect on the expression of several genes that are transcribed by RNA polymerase II.
|
Q5ASI4
|
Q6NJ52
|
RL13_CORDI
|
50S ribosomal protein L13
|
Corynebacterium
|
MSTYHPKSGDITRKWYVIDATDVVLGRLATHAADLLRGKGKPQFAPNVDCGDHVIVINADKVHVSSNKREREMRYRHSGYPGGLKTMTLGRSLEVHPERVVEESIRGMMPHNRLSRASVKKLHVFAGSEHPYAAQKPETYEFKQVAQ
|
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
|
Q6NJ52
|
Q888Q6
|
PANC_PSESM
|
Pantoate-activating enzyme
|
Pseudomonas
|
MNTVKTVLELRAAVARARSEGKRIALTPTMGNLHSGHAALVSKAAQRADFVVASIFVNPLQFGPNEDLATYPRTLAADQEKLLQAGCNLLFTPGVEEMYPHGMADQTLVSVPHLSQGLCGASRPGHFEGVATVVSKLFNMVQPDLAIFGEKDFQQLAVIRAMVRDLNMPIQIIGEPTVRADDGLALSSRNGYLDEAQRAAAPALYQAIRQTAEAISAGEQDFETLLNSKKQQLQAAGFRIDYLEIRNADSLRPTTAEDPDLVILAAAFMGKTRLIDNLHLTRG
|
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
|
Q888Q6
|
A5WVX0
|
ITPA_DANRE
|
Nucleoside-triphosphate pyrophosphatase
|
Danio
|
MAVPTGRALVFVTGNAKKLEEVVQILGDKFPYKLISKKIDLPEYQGEPDDISIQKCKEAARQVDGPVLVEDTCLCFRALEGLPGPYIKWFLDKLKPEGLYKMLAGFEDKSAWALCTFAFCAGKEEPVQLFRGITEGHIVEPRGPRDFGWDPCFQPEGYDKTYAELPKEVKNSISHRYRALAALSEHFCQDNGAPETKRSKHQD
|
Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
|
A5WVX0
|
A1YQ94
|
ODAM_PANTR
|
Apin
|
Pan
|
MKIIILLGFLGATLSAPLIPQRLTSASNSNELLLNLNNGQLLPLQLQGPLNSWIPPFSGILQQQQQAQIPGLSQFSLSALDQFAGLLPNQIPFPGQASFAQGAQAGHVDPLQLQTPPQTQPGPSHVMPYVFSFKMPQEQGQMFQYYPVYMLLPWEQPQQTVPRSPQQTRQQQYEEQIPFYAQFGYIPQLAEPATSGGQQQLAFDPQLGTAPEIAVMSTGEEIPYLGKEAINFRHDSAGVFMPSTSPKPSTTNAFTSAVDQTITPELPEEKDKTDSLREP
|
Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface.
|
A1YQ94
|
P06259
|
NU3C_MARPO
|
NADH-plastoquinone oxidoreductase subunit 3
|
Marchantia
|
MFLLQKYDYFFVFLLIISFFSILIFSLSKWIAPINKGPEKFTSYESGIEPMGEACIQFQIRYYMFALVFVIFDVETVFLYPWAMSFYNFGISSFIEALIFILILIIGLVYAWRKGALEWS
|
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
|
P06259
|
O59726
|
FNX2_SCHPO
|
Vacuolar membrane amino acid uptake transporter fnx2
|
Schizosaccharomyces
|
MSNPRTKSPNTNRGQGLRSERSALLNDSLSSLNGNSSYDSIKDSSKNNKDVAEVNEYPRRPESSVSVVSNSPHRQDAATTNTVSTVSVSKVLPALLLGVVLAALDNTIVASTYTKIGAEFGKFSQVSWTATAYMISCTAFQPLFGKFCDIYGRKKTLLAAYCVFGIGCFLCGTSRSLWQLVAARAIAGIGGGGMNSTVSILMSDIVPLKQRGTYQGIINVFFAIGSSLGGPVGGYFADQYTWRIGFLIQVPLIAIAFLCVYFTLNLPHHNHVSFMTRFRKIDLKGLILLIIGVTTMTCAFTLGGNVREWNDPVVISLLIASSISYLSFVYVEAFVAFEPLAPMDVLTERTCLSSYLCNFFHSVANFGWIYGMPLFFQSIKNEGAEKSGIRLIPMIIGSSLGSLLGGAVISLTGNYKKITVGSYFFGSVAALFMLRYGYSNFNWEYAVYPFSGGLGNGIAVTTTLVAIIHASPSAFQASAIATSYLFRSNGCVLGVSISSSIVQTVLGIKLRKSLDFDVDELLHHLRKDISYVHRLPEEIRQTVLDALLGSIHYSFLFVSFMFFCAFVCSMFIKNRNL
|
MFS-type transporter involved in vacuolar amino acid uptake.
|
O59726
|
B6J1C6
|
DNLJ_COXB2
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Coxiella
|
MNGVEVPAKIQKRIERLRQEINDHNYRYYVLSQPTIPDSVYDELFHELQKLEKKYPETITPSSPTQRVGAEPLKVFEPVHHEIPMLSLDNVFDEKGLRAFDKRIRQRLKLDKPFEYVCEPKMDGVALSLLYENGELIRAATRGDGYTGENVTQNTRTIASVPLQLRGNDYPELVEIRGEVLMPREGFAKFNREAEKRGDKTFANPRNAASGSLRQLDPRITAKRPLIFYGYLIGLLKGKDFPKNHCDVLKWFKDWGIPVISEIKVVGGIEGCLDYYEHLVKTREKMPFDIDGIVIKVNSLQVQAELGFVSRAPRWAIAYKFPAQEKMTVVKAIEFQVGRTGAVTPVARLEPVSVSGVTVSNATLHNFDELYRKDVRVGDTVIVRRAGDVIPEVVGPILAKRPKKAKLIKIPSRCPVCHAEVIKPEGEAVARCVGGLYCRAQLRESIKHFASRRALDIEGLGDKLVELFIQEKLIKDITGIYQLKKSAITALPRMGEKSAENLLTAIEKSKKTTLPRFLYALGIRGVGDTTARTLARHFHELDLLMKASIETLQEIRDIGPVAAENIHAFFHQKHNAELINKLIHLGVHWPQEKAVVKSEIAGKTFVLTGALKSLTREEAEEKIERSGGKATSSVSKNTDYVIVGENPGSKYEKAKALGISLIDEEAFLKLLKSKGVF
|
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.
|
B6J1C6
|
O19001
|
CDN1B_FELCA
|
p27Kip1
|
Felis
|
MSNVRVSNGSPSLERMDARQAEYPKPSACRNLFGPVNHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGNRQAVPLIGSQANTEDTHLVDQKTDTSDNQTGLAEQCPGIRKRPATDDSSPQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT
|
Important regulator of cell cycle progression. Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry.
|
O19001
|
P57193
|
FABB_BUCAI
|
Beta-ketoacyl-ACP synthase I
|
Buchnera
|
MRRVVITGIGIVSSIGNNKKEVLASLYKGVSGIVSSEEMKKLGMRSAVWGNIKLESINIITQKLSRFMNNASRYSFVAMMEAIKDAKIDREYYQKNPRVGLISGSGCSFSKNTLTSDIHLMKNKHISKGISPYLAVKTMPSGISACLSTLFKIYGVTYSISSACATSAHCIGNAFELIQFGRQDLIFAGGGEEISLELAMQFDAMRALSTCFNNDPKKASRVYDVYRDGFVISGGAGMLVIEELNSALSRSAYIYAEIIGYAATSDGSNIVVPSGDGAIRCMNLARKGKNIPIDYLNVHGTGTKIGDLIELEAIRKVFLNEKKPMISATKSMTGHGLGASGVHEMIYTLLMLKYNFIAPTINIENLEPCAENMNIIQKTTNIEINTAMSNSFGFGGTNVSLIVKKY
|
Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can also use unsaturated fatty acids. Catalyzes a key reaction in unsaturated fatty acid (UFA) synthesis, the elongation of the cis-3-decenoyl-ACP produced by FabA.
|
P57193
|
B0TJY5
|
GLYA_SHEHH
|
Serine hydroxymethyltransferase
|
Shewanella
|
MLKKDMNIADYDPQLFAAIEDETRRQEEHIELIASENYTSPRVLEAQGTQLTNKYAEGYPGKRYYGGCEHVDIVEELAISRAKELFGATYANVQPHSGSQANAAVFMALLQGGDTVLGMSLAHGGHLTHGSHVSFSGKLYNAVQYGIDETTGKIDYAEVERLAVEHKPKMIIAGFSAYSGIVDWGKFREIADKVGAYLFVDMAHVAGLVAAGIYPSPMPHAHVVTTTTHKTLAGPRGGLILSAINDEDIYKKLNSAVFPGGQGGPLMHVIAAKAVAFKEALDPEFTTYQEQVVVNAKAMARTFIERGYDVVSGGTDNHLFLLDLISKDITGKDADAALGNANITVNKNSVPNDPRSPFVTSGLRIGSPAITRRGFGEEESVQLTHWMCDILDDISDLAVSERVKAQVLELCARFPVYG
|
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
|
B0TJY5
|
Q7WFR9
|
MRAY_BORBR
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Bordetella
|
MRAIGVFEYITLRAVLACATALLIGLVAGPRVIRRLTEMKIGQAVRAYGPESHLVKTGTPTMGGALILIAIAISTLLWADWTNRFVWVVLLVTFGFGWIGWMDDYRKVVYRDPEGMPARQKFFWQATIGLVAAVYLAFAVSAPANTELWPLFKAWVGSGFTMPLPTRADLIVPFFKSVSYPLGVLGFVALTWAVIVGTSNAVNLTDGLDGLAIMPTVMVGSALGIFAYVVGRVDYSKYLLFPYIPGAAELMVLCAAIGGAGLAFLWFNAYPAQVFMGDVGALALGGALGTIAVIVRQEIVLFIMGGVFVVETLSVMVQVTWFKYTKRKYGQGRRIFRMAPLHHHFEVGGWKETQVVVRFWIITMMLVLVGLSTLKLR
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
Q7WFR9
|
Q8KF60
|
NIKR_CHLTE
|
Putative nickel-responsive regulator
|
Chlorobaculum
|
MSDLYRFGISLERKLIESFDRHIKAQGYQSRSEALRDLIREELLRKTTAEGGLVAGAIVMTYDHHKRDLVNRLIDIQHDFHDLIISTQHVHLDHENCLEVIAVKGNAPEIEKLSSALKVLVGVKHLDLSLSSAD
|
Transcriptional regulator.
|
Q8KF60
|
B0UF36
|
MCH_METS4
|
Methenyl-H4MPT cyclohydrolase
|
Methylobacterium
|
MSSTTVRPSVNALATPLVEALVADAAKLRLSVSAKSGEARLVDAGAQARGSIEAGRRIAEICLGGLGTVTIAPAGPVAAWPVTVTVHSADPVLACLGSQYAGWSLADEGGSSGFFALGSGPGRAAAAAEHLFEELHYRDHAAQIALVLESASAPPASVVAKVAEAAGVTPDAVTFIYAPTQSLAGATQVVARVLEVALHKAHSVGFDLAKVVDGIGAAPLSPPHPDFIQAMGRTNDAIIYGGRVQLFVEADDAEARGLAEALPSTTSRDHGAPFAEIFARFNGDFYAIDKHLFSPAEVVVTSLLSGTSHRAGRLVPELVERSFA
|
Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
|
B0UF36
|
P19427
|
DERM_BOVIN
|
Tyrosine-rich acidic matrix protein
|
Bos
|
MDLTLLWVLLPLVTVAWGQYGDYGYSYHQYHDYSDDGWVNLNRQGFSYQCPHGQVVVAVRSIFNKKEGSDRQWNYACMPTPQSLGEPTECWWEEINRAGMEWYQTCSNNGLVAGFQSRYFESVLDREWQFYCCRYSKRCPYSCWLTTEYPGHYGEEMDMISYNYDYYMRGATTTFSAVERDRQWKFIMCRMTDYDCEFANV
|
Seems to mediate adhesion by cell surface integrin binding. May serve as a communication link between the dermal fibroblast cell surface and its extracellular matrix environment. Enhances TGFB1 activity. Inhibits cell proliferation. Accelerates collagen fibril formation, and stabilizes collagen fibrils against low-temperature dissociation.
|
P19427
|
Q634C6
|
QUEA_BACCZ
|
Queuosine biosynthesis protein QueA
|
Bacillus cereus group
|
MDINLFDFHLPEELIAQVPLEERETSRLMVLDRETGDIEHKHFTDILSYLHEGDCLVLNETKVMPARLQGVKEDTGAHIEVLLLKQEEGDKWETLVKPAKRVKEGTVISFGEGKLKATCTGTADQGGRQLEFSYDGIFYEILDELGEMPLPPYIKETLEDRDRYQTVYAKEIGSAAAPTAGLHFTEELLEKLKQKGVELAFITLHVGLGTFRPVSADTIEEHHMHAEYYHMSEETAALLNRVKENGGRIITVGTTSTRTLETIATDHDGKLCAASGWTDIFMYPGYEFKAIDGLITNFHLPKSTLIMLVSAFANRDNVLHAYNEAVKEKYRFFSFGDAMFVASHAKMGNK
|
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
|
Q634C6
|
Q4V7N2
|
NSUN2_XENLA
|
tRNA cytosine C(5)-methyltransferase
|
Xenopus
|
MGRKNRRNRQRRTEQRSPAEEERRKAREQAAWEGGYPEIIKENKLFEHYYQELKIVPDGEWDKFMDALREPLPATIRITGYKSHAKEILHCLKEKYFKELPDIEVDGQKIEAPQPLSWYPEELAWHTNLSRKIIRKSPELEKFHQFLVSETESGNISRQEAVSMIPPVLLNVQPHHKILDMCAAPGSKTAQIIEMLHADMNVPFPEGFVIANDVDNKRCYLLVHQAKRLNSPCIMVVNHDASSIPRLLIENNGSREVLYYDRILCDVPCSGDGTMRKNIDVWKKWTTLNSLQLHGLQIRIATRGVEQLAEGGRMVYSTCSLNPVEDEAVIVSLLDKSEGSLELADVASELPGLKWMPGITQWRVMTKEGQWFEKWEDVPTSRHTQIRPTMFPLKDEEKLKSMNLNRCMRILPHHQNTGGFFVAVLIKKAPMPWNKRQPKLQRRPPVSVCDASVAPEIVKAVADISAIADEPAVDAENGETKPCTNQSGSSKTDSVCCPPPSKKMKLFGFKEDPFVFLSEDDPIFEPIQKFYALDPSFPKKNLLTRTQEGKKRQLYMVSKELRNVLLHNSEKMKVINTGIKVLCRNNDGEQYGCAYRLAQEGIYSLYPFINARILTVSVEDIKVLLTQENPFLSKFSKETQKQANNLDMGSIVLKYEPDPQQPETLQCPIVLCGWRGKTSIRSFVFFLHRINLVQWIFI
|
RNA cytosine C(5)-methyltransferase that methylates cytosine to 5-methylcytosine (m5C) in various RNAs, such as tRNAs, mRNAs and some long non-coding RNAs (lncRNAs). Involved in various processes, such as epidermal stem cell differentiation, testis differentiation and maternal to zygotic transition during early development: acts by increasing protein synthesis; cytosine C(5)-methylation promoting tRNA stability and preventing mRNA decay. Methylates cytosine to 5-methylcytosine (m5C) at positions 34 and 48 of intron-containing tRNA(Leu)(CAA) precursors, and at positions 48, 49 and 50 of tRNA(Gly)(GCC) precursors. tRNA methylation is required generation of RNA fragments derived from tRNAs (tRFs). Also mediates C(5)-methylation of mitochondrial tRNAs. Catalyzes cytosine C(5)-methylation of mRNAs, leading to stabilize them and prevent mRNA decay. Cytosine C(5)-methylation of mRNAs also regulates mRNA export. Also mediates cytosine C(5)-methylation of non-coding RNAs, such as vault RNAs (vtRNAs), promoting their processing into regulatory small RNAs. Required for proper spindle assembly and chromosome segregation, independently of its methyltransferase activity.
|
Q4V7N2
|
Q4JT51
|
RS19_CORJK
|
30S ribosomal protein S19
|
Corynebacterium
|
MPRSLKKGPFVDEHLLAKVDAQNEKGNKNVIKTWSRRSTILPDFIGHTFAVHDGRKHVPVFIDDSMVGHKLGEFAPTKTFKGHVKDDKKGRR
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
Q4JT51
|
B1WS50
|
PSBM_CROS5
|
Photosystem II reaction center protein M
|
Crocosphaera subtropica
|
MEVNDLGFIATILFVLVPTVFLLILYIQTREETES
|
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface.
|
B1WS50
|
Q38E83
|
LSM12_TRYB2
|
PBP1-interacting protein LSM12
|
Trypanosoma
|
MPVCNNDSQLIGLGVSVTLADDTTVNGTVYTYNSSEGLLVLFQGFSGSNPNVKIIRTPFIKEVTALRDNEEKLPPQLEAKARLPSMQAARDRSLFKHASSQLRNAKDKRNQLLQTDDQKTPIAALDTLIKLERIYPDIHWDKDAGVIRFNQDVVVKGKPDWTSPAVVIAEGAGDISRSLMERVQKTLSKK
|
Involved in post-transcriptional regulation of gene expression.
|
Q38E83
|
Q8W463
|
RK191_ARATH
|
50S ribosomal protein L19-1, chloroplastic
|
Arabidopsis
|
MAMSFHRLPQALHMIPRNPTQSSKNLGFSSFLSCAPSMDSRISVSRLSLNHPGSKFGFSLDTRVRNEFIVRAEEGNTEAESEEFVAEIADTEGNVEEVVEAKPTRKPRIKLGDVMGILNQKAIEVAEKVRPVPEIRTGDIVEIKLEVPENKRRLSIYKGIVMSRQNAGIHTTIRIRRIIAGIGVEIVFPIYSPNIKEIKVVSHRKVRRARLYYLRDKLPRLSTFK
|
Located at the 30S-50S ribosomal subunit interface and binds directly to 23S ribosomal RNA.
|
Q8W463
|
B5Y8H0
|
MURA_COPPD
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Coprothermobacter
|
MSVLIIDGGIPLKGKVTAQGCKNSALAILAAAALCEDRVYLTNVPDIGDVKTMMSILRSLGYKVTWGSGLTIKPGVIKNYDLTHTGAGSIRGSLLFLGALLGRLGKVVLPMPGGCNIGTRPIDLHLKGLSLMGASLDIQGGNIVGEAPSGLKGAYVYLDFPSVGATENIMIAGALASGETTIENAAQDQQVVELGKFLMACGVKIHGLGTKVIRIKGKKEIGGVTFRISGDSIEAGTYAIAAAATRGSITVDGVDVTFLRPLLFKLQEAGIEVVVTNGHEVTVLPSPRPKGITIKTMPFPGFPTDLQPLMMSLLATAEGRSVITETVYDGRMGHVSELWKMGANIEVEGNTAIITGVEKLTGAPVVANNLRAGAALVVAGLSAEGRSVVYGMEHVMRGYSNIHQKLRALDAKVELVSDEEAVNIA
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
B5Y8H0
|
Q8FMR0
|
MURA_COREF
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Corynebacterium
|
MGGVKDKFLVKGGARLQGSVRVDGAKNSVLKLMAAALLAEGTTTLTNCPEILDVPLMRDVLVGLGCEVEIDGHTVTIHTPAELKSDADFPAVTQFRASVCVLGPLTARCGRAVVSLPGGDAIGSRPLDMHQSGLEQLGATTRTQHGAVVAEADKLVGAEISLDFPSVGATENILMASVMAEGQTTLDNAAREPEIVDLCRMLRSMGADIEGEGSPKITINGVEKLHPTSHEVIGDRIVAGTWAFAAAMTRGDVTVGGIAPRYLHLPLEKLKLAGAQVDTFENGFRVVMNKRPKSTDYQTLPFPGFPTDLQPMAIGLNAIADGVAVVTENVFESRFRFVDEMQRLGADTSVDGHHVVIRGIEELSSTTVWSSDIRAGAGLVIAALCAEGTTEVRDVFHIDRGYPNFVENLQALGADIQRVVA
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
Q8FMR0
|
Q03A55
|
G6PI_LACP3
|
Phosphohexose isomerase
|
Lacticaseibacillus
|
MSYIKFDSSKLDKFVHANELEQMQPLVTAADKELREGTGAGKDFRGFIDLPVNYDKDEFARIKAAAKKVQGNSQVFVAIGIGGSYLGARMAVDFLSQTFRNLDPDLKFPEVYFAGNSISGTYLADLLDIIGDRDFSINVISKSGTTTEPSIAFRVLKAKLIEKYGKDGAKERIYATTDRAKGALKQEADAEGYEEFVVPDDVGGRFSVMSAVGLLPIAVAGGDIDEMMRGLGDGRKAYASADLKENEAYQYAALRNILYRKGYTTELLENYEPTLQYLGEWWKQLMGESEGKDQKGIYPSSANFSTDLHSLGQYIQEGLRNLMETVVWVEEPNRDLTIPEDANNLDGLGYLAGKKMSFVNRKAYEGVVLAHTDGGVPVMTVSIPKQDAYTLGYLIYFFEAAVSISGYLNGINPFNQPGVEAYKKNMFALLGRPGYEDMTKELNARL
|
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
|
Q03A55
|
Q04841
|
3MG_MOUSE
|
N-methylpurine-DNA glycosylase
|
Mus
|
MPARGGSARPGRGALKPVSVTLLPDTEQPPFLGRARRPGNARAGSLVTGYHEVGQMPAPLSRKIGQKKQRLADSEQQQTPKERLLSTPGLRRSIYFSSPEDHSGRLGPEFFDQPAVTLARAFLGQVLVRRLADGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYLIYGMYFCLNVSSQGAGACVLLRALEPLEGLETMRQLRNSLRKSTVGRSLKDRELCSGPSKLCQALAIDKSFDQRDLAQDDAVWLEHGPLESSSPAVVVAAARIGIGHAGEWTQKPLRFYVQGSPWVSVVDRVAEQMDQPQQTACSEGLLIVQK
|
Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
|
Q04841
|
O34739
|
STET_BACSU
|
Serine/threonine exchanger SteT
|
Bacillus
|
MHTEDNGLKKEIGLLFALTLVIGTIIGSGVFMKPGAVLAYSGDSKMALFAWLLGGILTLAGGLTIAEIGTQIPKTGGLYTYLEEVYGEFWGFLCGWVQIIIYGPAIIGALGLYFGSLMANLFGWGSGLSKVIGIIAVLFLCVINIIGTKYGGFVQTLTTIGKLIPIACIIVFGLWKGDQHIFTAVNESISDMNFGAAILATLFAYDGWILLAALGGEMKNPEKLLPRAMTGGLLIVTAIYIFINFALLHILSANEIVTLGENATSTAATMLFGSIGGKLISVGIIVSIFGCLNGKVLSFPRVSFAMAERKQLPFAEKLSHVHPSFRTPWIAISFQIALALIMMLISNPDKLSEISIFMIYIFYVMAFFAVFILRKRAKGEKRAYSVPLYPFMPILAIAGSFFVLGSTLITDTMSCGLSILIGLAGLPVYYGMKKRKAS
|
Exhibits an obligate exchange activity for serine, threonine and aromatic amino acids.
|
O34739
|
Q96HE7
|
ERO1A_HUMAN
|
Oxidoreductin-1-L-alpha
|
Homo
|
MGRGWGFLFGLLGAVWLLSSGHGEEQPPETAAQRCFCQVSGYLDDCTCDVETIDRFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDISQCGRRDCAVKPCQSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGTSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKKEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNIH
|
Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins . Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin.
|
Q96HE7
|
Q65JN4
|
CLPQ_BACLD
|
ATP-dependent protease subunit ClpQ
|
Bacillus
|
MSSFHATTIFAVQHNGKSAMAGDGQVTFGQAVVMKHTARKVRKLFNGKVIAGFAGSVADAFTLFEMFEAKLEEYNGNLQRAAVELAKEWRSDKVLRKLEAMLIVMNADSMLLVSGTGEVIEPDDGILAIGSGGNYALAAGRALKRHAGSQLDAKAIARASLETAGEICVYTNDQIIVEELE
|
Protease subunit of a proteasome-like degradation complex.
|
Q65JN4
|
P06636
|
HBA3_XENLA
|
Hemoglobin alpha-2 chain
|
Xenopus
|
MTLTDSDKAAVVALWGKIAPQANAIGAEALERLFLSYPQTKTYFSHFDLSHGSADLANHGGKVVNALGEAAKHIDDLDAALSTLSDLHAYNLRVDPGNFKLLSHTIQVTLAIHFHKEFDAATQAAWDKFLAEVATVLTSKYR
|
This is a larval (tadpole) alpha-globin.
|
P06636
|
P67860
|
VEGFA_PROFL
|
Vascular permeability factor
|
Protobothrops
|
MNFLLTWIHWGLAALLYFHNAKVLQAAPAQGDGDRQQSEVIPFMTVYERSVCRPIETMVDIFQDYPDEVEYILKPPCVALMRCGGCCNDEALECVPTELYNVTMEIMKLKPYQSQHIHPMSFQQHSKCECRPKKETRIIQEKKSKREKGKGQKRKRKRGRYKPQNFHCEPCSERRKHLYKQDPLTCKCSCKFTDSRCKSKQLELNERTCRCEKPRR
|
Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels.
|
P67860
|
B7V8A6
|
NADD_PSEA8
|
Nicotinate mononucleotide adenylyltransferase
|
Pseudomonas
|
MGKRIGLFGGTFDPVHIGHMRSAVEMAEQFALDELRLLPNARPPHRETPQVSAAQRLAMVERAVAGVERLTVDPRELQRDKPSYTIDTLESVRAELAADDQLFMLIGWDAFCGLPTWHRWEALLDHCHIVVLQRPDADSEPPESLRDLLAARSVADPQALKGPGGQITFVWQTPLAVSATQIRALLGAGRSVRFLVPDAVLNYIEAHHLYRAPH
|
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
|
B7V8A6
|
P69821
|
ULAC_ECO57
|
Ascorbate-specific phosphotransferase enzyme IIA component
|
Escherichia
|
MKLRDSLAENKSIRLQAEAETWQEAVKIGVDLLVAADVVEPRYYQAILDGVEQFGPYFVIAPGLAMPHGRPEEGVKKTGFSLVTLKKPLEFNHDDNDPVDILITMAAVDANTHQEVGIMQIVNLFEDEENFDRLRACRTEQEVLDLIDRTNAAA
|
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport.
|
P69821
|
A4Y9G1
|
LIPB_SHEPC
|
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
|
Shewanella
|
MPLQDTTLHIRHLGKQDYESVWHAMQHYTDTRNSESPDELWIVEHPPVFTQGQAGKSEHILNAGDIPVIQVDRGGQVTYHGPGQLVVYPLIDIKRSKIGVRQLVTHIEQSIINMLAKYDIQAYAKADAPGVYVNERKIASLGLRIRRGCSFHGLALNVDMDLAPFRRINPCGYAGLEMVQSKALGGPQTVTEAGEQLTITFSQLLGYQHLVHHQGLAAS
|
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
|
A4Y9G1
|
B0C1D7
|
RS19_ACAM1
|
30S ribosomal protein S19
|
Acaryochloris
|
MSRSLKKGPFVADHLLTKVENLNEKGEKQVIKTWSRASTIIPQMIGHTIAVHNGRQHVPVYVSEQMVGHKLGEFAPTRTFKSHSKGDKKARM
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
B0C1D7
|
Q1ISB3
|
RS17_KORVE
|
30S ribosomal protein S17
|
Candidatus Koribacter
|
MAETTNTPETSHRKELIGLVVSTKMQKTIVVQVERQKSHAMYGRVISRRKRFYAHDEEQTAHIGDYVRIEETRPLSKLKRWKLAEVLRRSALAPEVQEAAS
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
Q1ISB3
|
Q06221
|
TH11_TRYBB
|
Glucose transporter 1B/1C/1D/1F/2B
|
Trypanosoma
|
MTERRDNVSHAPDAIEGPNDGAHAEDTSPGFFSLENLGVAQVQVVGGTLNGYVIGYVAVYLLLYLTATECKFTTEGACGGRKIYGCKWSGTTCKFENPKCSEGSDPSDSCKNEVAYTSVYSGIFACAMIVGSMVGSIIAGKCITTFGLKKSFIIVSITCTIACVVVQVAIEYNNYYALCTGRVLIGLGVGILCSVFPMYVNENAHPKLCKMDGVLFQVFTTLGIMLAAMLGLILDKTGASKEEANMAGRLHVFSAVPLGLSVAMFLVGMFLRESTATFAQDDDGKADGGMDPNEYGWGQMLWPLFMGAVTAGTLQLTGINAVMNYAPKITENLGMDPSLGNFLVMAWNFVTSLVAIPLASRFTMRQMFITCSFVASCMCLFLCGIPVFPGVAGKEVKNGVATTGIALFIAAFEFGVGSCFFVLAQDLFPPSFRPKGGSFVVMMQFIFNILINLLYPITTEAISGGATGNQDKGQAVAFILFGLIGLICSVLQFFYLYPYDANQDHENDHGGEPVEQKTYPVEASPRN
|
Facilitative glucose transporter.
|
Q06221
|
Q8TRL1
|
RAD50_METAC
|
DNA double-strand break repair Rad50 ATPase
|
Methanosarcina
|
MKLKNLYIENIRSYRKLDFTFEDGVTVISGVNGSGKSSLLEACFMGLFGSKILSKDFVLADMIFKGAETAKINLGFEHLGKEYLIEQAFRYSSKSENASSSKCVLYADGENIIDQATRTYEEVRTLLNMDEEAYRNCAYIRQGEIDVLINAKPKDRQRMIDDLLQLGKLEEYRERTGYAKTAVRRLERDTKNSLVGVKAEIEGIESTEPVKALNGLKQKAKETDGSLKELNEKKDYAAARKGELDLRIAEYRERLQEIEVLKEAIRKTQEDKAGCFKEKEAFSGEVQGQRRILLELGEENTGLRDDCGFGDLEIEALLLHQEKEESSAREKVNAVSKDLALLLKEGETGSQALCELEKEKTQAERTLLECRTSIGAANKEIEGYRENIRKLEEESKGLREKAGFKAASGAADEIALLIKEFEEKESLLRDRKNEASTKLGLSLKEKETCDLNLVELEKELQNAGAAVRKGSTEIEALEKELRENSKAVLDIQEQKSEVLAELKGLGFAADQLENLEDFSELLLENKSRLHGKEKELEATLRELENNIRKNRELFAAGKCPTCGQELKGSEIACTAEECEDKKEKLASELADIKVQHAELEKKITRLKDAKKLEKRISDYDIEIEKLQEKAKASGKLIETHRARIEEDALKLESLDKRKQELETSGRQLLSDIKTLQVQEAEARKAHIEGEKTLIEVKTLDRKLAENTAEIESLNGKIRTSLALIENYGERLGELNDKLKALAEKENLSKEKLKALELALEAAQKKENEAKKAHSESEKLLGQAKKLQANLLSMENIKHKISELEAAIRNLAEKVGFLDREILERSERIRQLGEKLEGNRLSELQQKRAQFEQAQAKITENIREKTEEKDSLLKEIGMLENSLKRLRELRKELKALENRQLYLEAVYSNAEELENTYIRVRADMRARNIGALSVLLNEMFAFMYTNNAYSHIELDPEYNLTVYRKDGTPLEPKLLSGGERAIFNLVLRCAIYRLLALGFGGDKADGLPPMILDEPTVFLDRGHIRQLLKLIDMMRSIGVGQIIVVSHDDSLIDSADHVFQVEKDPLTNMSSITRL
|
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.
|
Q8TRL1
|
Q2RSB3
|
PNTAB_RHORT
|
dII
|
Rhodospirillum
|
MEDKNILVEGFNQLSQQALELSQHAQALALQASHAVLPAAAATEGASEFWWLMTVFVLACFIGFYVVWSVTPALHSPLMGVTNAISSVIVVGALIATGPEAFSASKVLGFFAILLASVNIFGGFIVTQRMLAMFKKKQK
|
The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
|
Q2RSB3
|
O28440
|
ASPD_ARCFU
|
L-aspartate dehydrogenase
|
Archaeoglobus
|
MLVGLIGYGAIGKFLAEWLERNGFEIAAILDVRGEHEKMVRGIDEFLQREMDVAVEAASQQAVKDYAEKILKAGIDLIVLSTGAFADRDFLSRVREVCRKTGRRVYIASGAIGGLDAIFSASELIEEIVLTTRKNWRQFGRKGVIFEGSASEAAQKFPKNLNVAATLSIASGKDVKVRLVADEVEENIHEILVRGEFGEMEIRVRNRPMRENPKTSYLAALSVTRILRNLKEGLVV
|
Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
|
O28440
|
Q39E99
|
HEM6_BURL3
|
Oxygen-dependent coproporphyrinogen-III oxidase
|
Burkholderia cepacia complex
|
MTDSTYDVARVRTYLQDLQTRIADALGALDGTPLATDAWQRGPAERLRGGGCTRILEGGRVFERAGIGFSDVAGDALPPSASAARPQLAGRGFEALGVSLVLHPRNPYCPTVHMNVRMLIATKPGEEPVFWFGGGMDLTPVYGFEDDARHFHQTCKDALDPFGVELYPRFKKWCDEYFFLKHRNEMRGIGGIFFDDFSEPGFERSFDMMQSVGDAFLQAYLPIVERRAELPYGERERDFQAYRRGRYVEFNLVFDRGTLFGLQSGGRTESILMSMPPVANWRYNWQPEPGSPEARLYSDFIVPRDWI
|
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.
|
Q39E99
|
Q9TDL4
|
CYB_CEPHE
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Cephalorhynchus
|
MTNIRKTHPLMKILNNAFIDLPTPSNISSWWNFGSLLGLCLIMQILTGLFLAMHYTPDTSTAFSSVAHICRDVNYGWFIRYLHANGASMFFICLYAHIGRGLYYGSYMFQETWNIGVLLLLTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALTAVHLLFLHETGSNNPTGIPSNMDMIPFHPYYTIKDILGALFLILILLALTLFAPDLLGDPDNYTPANPLNTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILILIFIPMLQTSKQRSMMFRPFSQLLFWTLIADLLTLTWIGGQPVEHPYIIVGQLASILYFFLILVLMPTVSLIENKLLKW
|
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.
|
Q9TDL4
|
Q5B8A1
|
PKFF_EMENI
|
Dehydrogenase pkfF
|
Aspergillus subgen. Nidulantes
|
MRHTALLPLVSSFIVPALAQIPGQTTVNATVNQGRFGNATYDYVIVGGGTSGLAIAARLAEDPSLSVAVIEAGGYYELDGTVASIIPGLAAGANVGTDATEYSTVDWNFQAQPLTSANDRSLRYNRGKTLGGSSARHYMVYQRGTRGSYDQWAELTGDESWGWDSVFPYFQRSVNVTPANMTGRFPNTTVTYDPSGFNKAGGPLHVTWPNYGSPWSTWIEQGLEAIGILPDTDFNTGTLNGSSWAPITINPLSQKRDSSETSFLQQSLKTTNLTVYLHTMALKIGFDGTTASSVDVRSPVGRFTLSARREIIVSAGALQSPQLLMVSGIGPRETLERHGIPVVKELAGVGQKMWEHPFFGITHQVNLVTATELAINQQALLQALNQYKSQQGPLTSAGFGVLGWEKLPNSTLSDSTNEALATFPSDWPTIEYLSIDGYLNGWHSAADQATGNGQQWGTIAVALVAPLSRGNVTISSSDMDDPPVFDLGFLTHPADREIAVAAMRRIRQAFAAISEITIGDEVVPGADVSTDEELLDFIRESIVPVYHVAGTCAMGREDDPEAVVDPQARVIGVNNLRVVDASIFPTLPPGHPQSTCYMVAEKIADLIKKGN
|
Dehydrogenase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone . The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA . Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E . The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
|
Q5B8A1
|
P48356
|
LEPR_MOUSE
|
OB receptor
|
Mus
|
MMCQKFYVVLLHWEFLYVIAALNLAYPISPWKFKLFCGPPNTTDDSFLSPAGAPNNASALKGASEAIVEAKFNSSGIYVPELSKTVFHCCFGNEQGQNCSALTDNTEGKTLASVVKASVFRQLGVNWDIECWMKGDLTLFICHMEPLPKNPFKNYDSKVHLLYDLPEVIDDSPLPPLKDSFQTVQCNCSLRGCECHVPVPRAKLNYALLMYLEITSAGVSFQSPLMSLQPMLVVKPDPPLGLHMEVTDDGNLKISWDSQTMAPFPLQYQVKYLENSTIVREAAEIVSATSLLVDSVLPGSSYEVQVRSKRLDGSGVWSDWSSPQVFTTQDVVYFPPKILTSVGSNASFHCIYKNENQIISSKQIVWWRNLAEKIPEIQYSIVSDRVSKVTFSNLKATRPRGKFTYDAVYCCNEQACHHRYAELYVIDVNINISCETDGYLTKMTCRWSPSTIQSLVGSTVQLRYHRRSLYCPDSPSIHPTSEPKNCVLQRDGFYECVFQPIFLLSGYTMWIRINHSLGSLDSPPTCVLPDSVVKPLPPSNVKAEITVNTGLLKVSWEKPVFPENNLQFQIRYGLSGKEIQWKTHEVFDAKSKSASLLVSDLCAVYVVQVRCRRLDGLGYWSNWSSPAYTLVMDVKVPMRGPEFWRKMDGDVTKKERNVTLLWKPLTKNDSLCSVRRYVVKHRTAHNGTWSEDVGNRTNLTFLWTEPAHTVTVLAVNSLGASLVNFNLTFSWPMSKVSAVESLSAYPLSSSCVILSWTLSPDDYSLLYLVIEWKILNEDDGMKWLRIPSNVKKFYIHDNFIPIEKYQFSLYPVFMEGVGKPKIINGFTKDAIDKQQNDAGLYVIVPIIISSCVLLLGTLLISHQRMKKLFWDDVPNPKNCSWAQGLNFQKPETFEHLFTKHAESVIFGPLLLEPEPISEEISVDTAWKNKDEMVPAAMVSLLLTTPDPESSSICISDQCNSANFSGSQSTQVTCEDECQRQPSVKYATLVSNDKLVETDEEQGFIHSPVSNCISSNHSPLRQSFSSSSWETEAQTFFLLSDQQPTMISPQLSFSGLDELLELEGSFPEENHREKSVCYLGVTSVNRRESGVLLTGEAGILCTFPAQCLFSDIRILQERCSHFVENNLSLGTSGENFVPYMPQFQTCSTHSHKIMENKMCDLTV
|
Antagonizes Isoform A and isoform B-mediated LEP binding and endocytosis.
|
P48356
|
A8W3B2
|
ATPI_CUSEX
|
F-ATPase subunit IV
|
Cuscuta subgen. Monogynella
|
MDVLSCSINTLKGLYDISGVEVGQHFYWQIGDFLVHGQVLITSWVVIAILLGSATVAVRNPQTIPTGGQNFFEYVLEFIRDVSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGALLPWKILQLPHGELAAPTNDINTTVALALLTSAAYFYAGILKKGLGYFEKYIKPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIGESMEGHL
|
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
|
A8W3B2
|
A0PMB5
|
RS11_MYCUA
|
30S ribosomal protein S11
|
Mycobacterium
|
MPPKKASGTGPKKGQKTRRREKKNVPHGAAHIKSTFNNTIVTITDPQGNVIAWASSGHVGFKGSRKSTPFAAQLAAENAARKAQEHGVRKVDVFVKGPGSGRETAIRSLQAAGLEVGAISDVTPQPHNGVRPPKRRRV
|
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.
|
A0PMB5
|
Q8N300
|
SVBP_HUMAN
|
Coiled coil domain-containing protein 23
|
Homo
|
MDPPARKEKTKVKESVSRVEKAKQKSAQQELKQRQRAEIYALNRVMTELEQQQFDEFCKQMQPPGE
|
Enhances the tyrosine carboxypeptidase activity of VASH1 and VASH2, thereby promoting the removal of the C-terminal tyrosine residue of alpha-tubulin . This activity is critical for spindle function and accurate chromosome segregation during mitosis since microtuble detyronisation regulates mitotic spindle length and postioning . Also required to enhance the solubility and secretion of VASH1 and VASH2 . Plays a role in axon and excitatory synapse formation .
|
Q8N300
|
B9JUW1
|
AMPA_AGRVS
|
Leucyl aminopeptidase
|
Agrobacterium
|
MSMKLEISFAPSALIEAGLVLSLKEAEATLPAGAATVDPSGIFAKAAATAKFKAKAMSVLDILAPTGSQADRLIVIGAGKAADLVDHDWLRLGGVAAANLKGSEAVTVFLDADGLTITAEGVRDFAIGMLLRAYSFDDYKTKKKDDDDKAPSAVQITLVTAVADAAERLFAAEGRAVVDGVLLARNLVNLPANVLGPVEFADRAKALEALGVEVEILTETEMASLGMGALLGVAQGSVRPPRLAVMQWKGGAPEGQPIAFIGKGVVFDTGGISIKPAGGMEDMKGDMGGAAAVIGLMHTLAARKAKVNAIGILGLVENMPDGNAQRPGDIVTSMSGQTIEVINTDAEGRLVLCDALWYCNDRFKPAFMINLATLTGAILVALANLHAGLFSNDDTLAENLLKAGLSTNERLWRMPLGKDYDKLIDSKFADMKNTGGRYGGSITAAQFLKRFVGDTPWAHLDIAGTAMASPKDEINQSWASGFGVRLLDQLVRDAYEA
|
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
|
B9JUW1
|
Q8Z534
|
MENH_SALTI
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
|
Salmonella
|
MMLHAQHMPGQPGTPSLVFLHGFSGDCREWQPVGEQFHGCSRLNIDLPGHGGSAAIPVGGFADVIRLLRATLISYNILKFWLVGYSLGDRVQMIASCQGIPGLCGLVVEGGHPGLQNEQARAERRLSDGRWAERFRHEPLTEVFHDWYQQPVFASLTAQQRQALTALRSQNNGETLAAMLEATSLAVQPDLREVLNALAFPFYYLCGERDSKFRALAQEVAATCHVIRNAGHNAHRENPAGVVDSLAQILRL
|
Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).
|
Q8Z534
|
Q9FJH8
|
NRT24_ARATH
|
High affinity nitrate transporter 2.4
|
Arabidopsis
|
MADGFGEPGSSMHGVTGREQSYAFSVESPAVPSDSSAKFSLPVDTEHKAKVFKLLSFEAPHMRTFHLAWISFFTCFISTFAAAPLVPIIRDNLNLTRQDVGNAGVASVSGSIFSRLVMGAVCDLLGPRYGCAFLVMLSAPTVFSMSFVGGAGGYITVRFMIGFCLATFVSCQYWMSTMFNGQIIGLVNGTAAGWGNMGGGVTQLLMPMVYEIIRRLGSTSFTAWRMAFFVPGWMHIIMGILVLTLGQDLPDGNRSTLEKKGAVTKDKFSKVLWYAITNYRTWVFVLLYGYSMGVELTTDNVIAEYFFDRFHLKLHTAGIIAASFGMANFFARPIGGWASDIAARRFGMRGRLWTLWIIQTLGGFFCLWLGRATTLPTAVVFMILFSLGAQAACGATFAIIPFISRRSLGIISGLTGAGGNFGSGLTQLVFFSTSTFSTEQGLTWMGVMIMACTLPVTLVHFPQWGSMFLPSTEDEVKSTEEYYYMKEWTETEKRKGMHEGSLKFAVNSRSERGRRVASAPSPPPEHV
|
Involved in high-affinity nitrate transport. Might be involved in the transfer of nitrate from stored pools to cytoplasm.
|
Q9FJH8
|
B7MIY2
|
NUDC_ECO45
|
NADH pyrophosphatase
|
Escherichia
|
MDRIIEKLDHGWWVVSHEQKLWLPKGELPYGEAANFDLVGQRALQIGEWQGEPVWLVQLQRRHDMGSVRQVIDLDVGLFQLAGRGVQLAEFYRSHKYCGYCGHEMYPSKTEWAMLCSHCRERYYPQIAPCIIVAIRRDDSILLAQHTRHRNGVHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPQSLMTAFMAEYDSGEIVIDPKELLEAHWYRYDDLPLLPPPGTVARRLIEDTVAMCRAEYE
|
mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.
|
B7MIY2
|
Q2JQT6
|
NUSB_SYNJA
|
Antitermination factor NusB
|
unclassified Synechococcus
|
MQPRRVARELALLGVNQLPATAAKLSEKQLEDLLLAAIRALQEETHETLSTAAAEIQRSDRLLHESDPLLLAASDAKEEGGARSLTVRLQQAQRHLQRLETALKEANAGDTVQGELLELAHQAQVALSNAGQALEHLEQRLYSVRRILDEVVQLSQKAVNRLGVALSMPELLHIAQAQEVRAYALQLLTALRTHKEAIDARLQGVLVGWQLKRVGRIERDILRLAVVEMEILRSSPDKVAINEAVELAKKYGDPEAAAFVNGVLRRLVDSRMEAPFGRNPSPAGDLRS
|
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
|
Q2JQT6
|
Q6NCG4
|
ACCA_RHOPA
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
|
Rhodopseudomonas
|
MSGPMRSYLDFEKPVAELDSKIDELRTLAASGSDIHEEIEKIEEKAQQALQDLYAALTPWQKTQVARHPQRPHCVDYIEGLIAEFTPLAGDRKFGDDEALVGGFGRFRGEAVCVIGQEKGSTTETRLRHNFGMARPEGYRKAVRLMEMADRFDLPVLSLVDTAGAYPGIGAEERGQAEAIARSTDACLQLGVPNVALVIGEGGSGGAIAIATANKVLMLEHAVYSVISPEAASSILWRDGTKAQEAANSMKITAQDLLKFGVIDQILAEPKGGAHRDPEAMIATAGDAIAAAFAELKGQGRDAIRAKRRQKFLDIGRKLA
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
|
Q6NCG4
|
Q2JPH1
|
MINE_SYNJB
|
Cell division topological specificity factor
|
unclassified Synechococcus
|
MLLDFLDQLFSRHSGNSRQQAKQRLKLILAHDRADLTPAALESMRLEILGVVSRYVELDSEGMQFHLATEGGTTALIANLPIRRVKPLETGLSRSEGEKA
|
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
|
Q2JPH1
|
B1MB62
|
GCSH_MYCA9
|
Glycine cleavage system H protein
|
Mycobacteroides abscessus
|
MTEIPADLHYTEEHEWVRRTGDTTVRIGITDYAQSQLGDVVFVQLPDVGSELTAGSTFGEVESTKSVSDLFAPITAKVIAANGDLDSDPQLVNSDPYGEGWLVDLEAASAADLDAALNDLLDASGYGDATD
|
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
|
B1MB62
|
Subsets and Splits
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