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
|
|---|---|---|---|---|---|---|
A6LP60
|
DAPH_THEM4
|
Tetrahydrodipicolinate N-acetyltransferase
|
Thermosipho
|
MNTQEIINLIANSKKRTIAKAYVSGNLKNIKLENVEFVGNELFGVLFGDLKDIENTINKNDIKNYKIEILAKNSAIPLADIKKYNARIEPGAIIRDMVEIGDGAVIMMGAVINIGAVIGEKTMIDMNTVIGGRAIIGKNCHIGAGSVIAGVIEPPSAKPVMIKDNVMVGANAVILEGVEIGEHSVIAAGAVVIEDIPPYSVVAGVPAKVIKKVDKKTESKTQIIDSLRNLK
|
Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate.
|
A6LP60
|
Q2MGI2
|
RF2_STRPN
|
Peptide chain release factor 2
|
Streptococcus
|
MDISVIRQKIDANREKLASFRGSLDLEGLEEEIAILENKMTEPDFWNDNIAAQKTSQELNELKNTYNTFHKMEELQDEVEILLDFLAEDESVHDELVAQLAELDKIMTSYEMTLLLSEPYDHNNAILEIHPGSGGTEAQDWGDMLLRMYTRYGNAKGFKVEVLDYQAGDEAGIKSVTLSFEGPNAYGLLKSEMGVHRLVRISPFDSAKRRHTSFTSVEVMPELDDTIEVEIREDDIKMDTFRSGGAGGQNVNKVSTGVRLTHIPTGIVVQSTVDRTQYGNRDRAMKMLQAKLYQMEQDKKAAEVDSLKGEKKEITWGSQIRSYVFTPYTMVKDHRTSFEVAQVDKVMDGDLDGFIDAYLKWRIS
|
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
|
Q2MGI2
|
C3MIE4
|
BETA_SINFN
|
Betaine aldehyde dehydrogenase
|
Sinorhizobium
|
MQADYIIIGSGSAGSALAHRLSEDSRNSVIVLEFGGTDIGPFIQMPAALAWPMSMNRYNWGYLSEPEPHLNNRRITAPRGKVIGGSSSINGMVYVRGHAEDFDRWEQLGAKGWAYADVLPYFKRMEHSHGGEDGWRGTDGPLHVQRGPVKNPLFHAFVEAGKQAGFEMTDDYNGSKQEGFGLMEQTTWRGRRWSAASAYLKPALKRPNVQLIRCFARKIVIENGRATGVEIERGGRIEVVKANREVIVSASSFNSPKLLMLSGIGPAAHLKDLGIDVKVDRPGVGQNLQDHMEFYFQQISTKPVSLYSWLPWFWQGVAGAQWLFFKSGLGISNQFEACAFLRSAPGVKQPDIQYHFLPVAIRYDGKAAANTHGFQVHVGYNLSKSRGSVTLRASDPKADPVIRFNYMSHPEDWEKFRHCVRLTREIFGQKAFDQYRGPEIQPGERVQTDEEIDAFLREHLESAYHPCGTCKMGSKDDPMAVVDPETRVIGVDGLRVADSSIFPHVTYGNLNAPSIMTGEKAADHILGKQPLARSNQEPWINPRWAISDR
|
Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate.
|
C3MIE4
|
P27675
|
GLNQ_GEOSE
|
Glutamine transport ATP-binding protein GlnQ
|
Geobacillus
|
MIYFHQVNKYYGDFHVLKDINLTIHQGEVVVIIGPSGSGKSTLVRCINRLETISSGELIVDNVKVNDKHIDINQLRRNIGMVFQHFNLYPHMTVLQNITLAPMKVLRIPEKEAKETAMYYLEKVGIPDKANAYPSELSGGQQQRVAIARGLAMKPKIMLFDEPTSALDPETIGEVLDVMKQLAKEGMTMVVVTHEMGFAREVADRIVFMDQGRILEEAPPEEFFSNPKEERAKVFLSRILNH
|
Part of the binding-protein-dependent transport system for glutamine. Probably responsible for energy coupling to the transport system.
|
P27675
|
B4ECP3
|
DAPE_BURCJ
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Burkholderia cepacia complex
|
MSATLALTEQLIARASVTPDDQHCQQIMTERLAALGFECETIASHGVTNLWAVKRGTDGRDGKLLAFAGHTDVVPTGPLEQWTSPPFIPAHRDGKLYGRGAADMKTSLAAFVVASEEFVAAHPDHRGAIAFLITSDEEGPATDGTVKVVELLQARGERLDYCIVGEPTSTTELGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDAGNEYFPPTTWQVSNLHAGTGATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDKHGLEYTLKWSVSGLPFLTPRGELSGALEHAIRTETGITTELSTTGGTSDGRFIARICPQVIEFGPPNGSIHKIDEHIEVRFVDPLKNVYRRVLEQLIA
|
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
|
B4ECP3
|
P48101
|
CHLI_CYAPA
|
Mg-protoporphyrin IX chelatase
|
Cyanophora
|
MKNNNRPIFPFTAIVGQEEMKLALLLNIVDPKIGGVMIMGDRGTGKSTTIRALADLLPEIDIVANDPFNSHPTDIELMSDNVRQLKENGEEISLIQKKVPMIDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAQANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMHAEIRTVKDPTLRVQIVEERSEFDRSPEDFLQEYKLQQEVLRQRIINAQQQLNNVQLNYEIKVKISQVCSELDVDGLRGDIVTNRAAKALAAFEGRDEVTVDDVLRIITLCLRHRLRKDPLEEIDSGQKVEKVFQRIFSNL
|
Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
|
P48101
|
Q82SJ7
|
PDXJ_NITEU
|
Pyridoxine 5'-phosphate synthase
|
Nitrosomonas
|
MIALGVNIDHVATVRQARGTTYPSPVEAALVAEVAGADAITLHLREDRRHIQENDVVILRDRLKTRMNLESAVTEEMIAFACRIKPHDICLVPERREELTTEGGLDVIRHFQQVSVACKRLAEAGIRVSLFVDAQAGQIDAAVEAGAPVIELHTGRYADAATPEMQQVELETIRTMAAYAFGRGLQVNAGHGLHYENTVQIAAIPELSELNIGHAIVARALFVGFAEAVREMKALLQQARA
|
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
|
Q82SJ7
|
Q1PFB9
|
AGC17_ARATH
|
AGC serine/threonine-protein kinase subfamily 1 member 7
|
Arabidopsis
|
MLTKPGKKLDSSESTHHTTSSNYPPLDIVHQTPQPRKEMQQKPLFDPKKMDNLIKPEPAGFTNHHRPNPSPKIPSSPGSNMTESQSNLNTKPNNNNSNNNSNMSSRSNSIESTSSNPSKPHTGGDIRWDAVNTLTSKGVQLGISDFRLLKRLGYGDIGSVYLVELRGTITYFAMKVMDKASLASRNKLLRAQTEREILSQLDHPFLPTLYSHFETDKFYCLVMEFCGGGNLYSLRQKQPNKCFTEDAARFFASEVLLALEYLHMLGIVYRDLKPENVLVRDDGHIMLSDFDLSLRCSVSPTLVKSSSVHAAGGGSGSSRPVGLIDEDAAVQGCIQPSTFFPRILQSSKKNRKAKSDFGLFVNGSMPELMAEPTNVKSMSFVGTHEYLAPEIIRGEGHGSAVDWWTFGIFIYELLYGATPFKGQGNRATLHNVIGQALRFPEVPHVSSAARDLIKGLLVKEPQKRIAYKRGATEIKQHPFFEGVNWALIRSATPPHVPEPVDFSCYASKDKESMAAVDGGGKKNNNGAGGGCSTGGGDNKPNGDCNDPDYIDFEYF
|
Functions redudantly with AGC1-5 as signaling component in the pollen tube. Required for polarized growth of pollen tubes.
|
Q1PFB9
|
Q0W1X7
|
RL24_METAR
|
50S ribosomal protein L24
|
Methanocella
|
MCEVCVMVTSSQPRKQRKFRYEAPQHVRSNFINARLSEELSKKYGRTARVIVGDTVKVMRGDAAGTEGKVREIDVKREKVVVEGVSVARADGKEEARPIHPSNLMITKLVLDDPKRVASLERK
|
Located at the polypeptide exit tunnel on the outside of the subunit.
|
Q0W1X7
|
Q07GW8
|
HTPG_RHOP5
|
High temperature protein G
|
Rhodopseudomonas
|
MTTTDTAPQTQPFQAEVAELLNLMVHSVYSETEIFLRELISNGSDALDKLRYEAISKPDLMEAGGTPKIQIVPKKAPDTLSVIDNGIGMDRQELIDNLGTIAKSGTKSFLTKLTEAKDGSNLIGQFGVGFYAAFMVADRIVVTSRRAGSTEAWTWTSSGGAGFEIAPASAEEAERIVRGTEIVLHLKPEAAKYLEAYQIERIVSAYSDNIQFPIELVPEEGEARQINSASALWQRSKSELAAEDYKQAYKSIANAFDDPAMTLHYRAEGRYSYAVMLFAPSTKPFDLFEPQRKGHVKLYVRRVFITDDADLLPAYLRFIRGVIDSEDLPLNLSREMLQNNPQLVQIRKAVTGKVIGELESLGEKDPENFAKIWDAFGPVIKEGIWEDYERREKLLALSRFTTTKGDNRTLKNYVEDLRDNQTEIYYLVGDSLERLKSNPKLESAAARGIEVLLLTDPVDAFWTSAPLDFGGKPLKSLSQGDVNFDLIPTTDEAKDEQPKPETDEALVIATIKDALGERVSDVRASQRLTASASCLIAGGQGPDRALERMLAQQNRGGASKPILEINLRHPLVAAIGRPGNADAADLSLLLLEQAQILDGELPEDPAGFAGRINRLVLRAL
|
Molecular chaperone. Has ATPase activity.
|
Q07GW8
|
Q7LZQ4
|
PA2A_GLOUS
|
Phosphatidylcholine 2-acylhydrolase
|
Gloydius
|
SLIQFETLIMKVAKKSGMFWYSNYGCYCGWGGQGRPQDATDRCCFVHDCCYGKVTGCDPKMDVYSFSEENGDIVCGGDDPCKKEICECDRAAAICFRDNLNTYNDKKYWAFGAKNCPQEESEPC
|
Snake venom phospholipase A2 (PLA2) that inhibits ADP-induced platelet aggregation. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
Q7LZQ4
|
Q8RDQ0
|
MRAY_FUSNN
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Fusobacterium
|
MLYFLAEHLAKLEFLKSIYLRAFLGFVISFCIVLFAGRPFIKYLKIKKFGEEIRDDGPSSHFSKKGTPTMGGVLIIAAVLLTSIFINDLTNSLILLVLLSTIMFAAIGFIDDYRKFTVSKKGLAGKKKLLFQGAIGLIIWAYIYFIGLTGRPMVDLSLINPISAYPYYIGAIGLFFLIQIVLMGTSNAVNITDGLDGLAIMPMIICSTILGVIAYFTGHTELSSHLHLFYTVGSGELSVFLSAVTGAGLGFLWYNCYPAQIFMGDTGSLTLGGILGVIAIILKQELMLPIMGFIFVLEALSVILQVGSFKLRGKRIFKMAPIHHHFELMGIPESKVTMRFWIGTLIFGIIALGAIKMRGIL
|
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.
|
Q8RDQ0
|
Q8GEH7
|
METN_ERWPE
|
Methionine import ATP-binding protein MetN
|
Erwinia
|
MVFYTIGPQTPQIDKGQIYGIIGYSGAGKSTLIRLLNGLEKPGSGSVTIAGQDIAQASVEALRQARLKISMVFQHFNLLWSRTVSENIAFSLQISGTSKSVIQDRVQELIALVGLVGKEQAYPSQLSGGQKQRVGIARALANNPNVLLCDEATSALDPQTTDAILELLLDINRKLWLTIVLITHEMHVVRKICHRVAVMEEGRIVEEGEVLSLFTHPQQPITRQFVKQTSGYISANVPFNPQLVNIDNGKVLKLTFVGQSTQQPVIGELTLKYGLAFNMLHGIMTQTTNGTFGEIWLQVPASQSQLPRILADLHAYEISTEVVTNV
|
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
|
Q8GEH7
|
P52736
|
ZN133_HUMAN
|
Zinc finger protein 150
|
Homo
|
MAFRDVAVDFTQDEWRLLSPAQRTLYREVMLENYSNLVSLGISFSKPELITQLEQGKETWREEKKCSPATCPADPEPELYLDPFCPPGFSSQKFPMQHVLCNHPPWIFTCLCAEGNIQPGDPGPGDQEKQQQASEGRPWSDQAEGPEGEGAMPLFGRTKKRTLGAFSRPPQRQPVSSRNGLRGVELEASPAQSGNPEETDKLLKRIEVLGFGTVNCGECGLSFSKMTNLLSHQRIHSGEKPYVCGVCEKGFSLKKSLARHQKAHSGEKPIVCRECGRGFNRKSTLIIHERTHSGEKPYMCSECGRGFSQKSNLIIHQRTHSGEKPYVCRECGKGFSQKSAVVRHQRTHLEEKTIVCSDCGLGFSDRSNLISHQRTHSGEKPYACKECGRCFRQRTTLVNHQRTHSKEKPYVCGVCGHSFSQNSTLISHRRTHTGEKPYVCGVCGRGFSLKSHLNRHQNIHSGEKPIVCKDCGRGFSQQSNLIRHQRTHSGEKPMVCGECGRGFSQKSNLVAHQRTHSGERPYVCRECGRGFSHQAGLIRHKRKHSREKPYMCRQCGLGFGNKSALITHKRAHSEEKPCVCRECGQGFLQKSHLTLHQMTHTGEKPYVCKTCGRGFSLKSHLSRHRKTTSVHHRLPVQPDPEPCAGQPSDSLYSL
|
May be involved in transcriptional regulation as a repressor.
|
P52736
|
B9M174
|
MURB_GEODF
|
UDP-N-acetylmuramate dehydrogenase
|
Geotalea
|
MTVDTLARLCTAVRGKVLVNEPLAGHTSLKVGGPADYFAIPADLADLEELIKVVRSLSLPYFIIGGGFNVLVGDGGFRGVAISLKELNGMESPSRGRIRAEAGATNQQLVNYATGKELTGLEFLSCIPGTIGGALSVNAGAHGQSTMEQVETLITMRDGRIFENEGRKRNFGYRYLELEPGEIVVAAVFSLSEGKAEAIGEKLESYRRHRLESQKIGYPNAGSFFKNPEGQQAWRLIDEAGFRGFQVGGAQVSEIHTNFLVNRGGASAADFITLAGMIKQKVLERSGILLQEEVRILDEYEQK
|
Cell wall formation.
|
B9M174
|
Q8CCS2
|
NALF1_MOUSE
|
Transmembrane protein FAM155A
|
Mus
|
MTRGAWMCRQYDDGLKIWLAAPRENEKPFIDSERAQKWRLSLASLLFFTVLLSDHLWFCAEAKLTRTRDKEHHQQQQQQQQQQQQQQQQQQQQQQRQQQRQRQQQRQRQQEPSWPALLASMGESSPAAQAHRLLSASSSPTLPPSPGGGGGSKGNRGKNNRSRALFLGNSAKPVWRLETCYPQGASSGQCFTVESADAVCARNWSRGAAAGEEQSSRGSRPTPLWNLSDFYLSFCNSYTLWELFSGLSSPSTLNCSLDVVLTEGGEMTTCRQCIEAYQDYDHHAQEKYEEFESVLHKYLQSDEYSVKSCPEDCKIVYKAWLCSQYFEVTQFNCRKTIPCKQYCLEVQTRCPFILPDNDEVIYGGLSSFICTGLYETFLTNDEPECCDIRSEEQTAPRPKGTVDRRDSCPRTSLTVSSATRLCPGRLKLCVLVLILLHTVLTASAAQNSTGLGLGGLPTLEDNSTRED
|
Auxillary component of the NALCN sodium channel complex, a channel that regulates the resting membrane potential and controls neuronal excitability.
|
Q8CCS2
|
Q9F466
|
HYDRA_PAEAU
|
Hydantoin racemase
|
Paenarthrobacter
|
MRILVINPNSSSALTESVADAAQQVVATGTIISAINPSRGPAVIEGSFDEALATFHLIEEVERAERENPPDAYVIACFGDPGLDAVKELTDRPVVGVAEAAIHMSSFVAATFSIVSILPRVRKHLHELVRQAGATNRLASIKLPNLGVMAFHEDEHAALETLKQAAKEAVQEDGAESIVLGCAGMVGFARQLSDELGVPVIDPVEAACRVAESLVALGYQTSKANSYQKPTEKQYL
|
Involved in the asymmetric conversion of racemic 5-substituted hydantoins to the corresponding L-amino acids. Catalyzes the racemization via enolization of D- and L-5-monosubstituted hydantoins. It shows preference for hydantoins with arylalkyl side chains such as 5-benzyl-hydantoin (BH) and 5-(3-indolymethylene)-hydantoin (IMH).
|
Q9F466
|
B8HPZ1
|
PRMA_CYAP4
|
Ribosomal protein L11 methyltransferase
|
unclassified Cyanothece
|
MVSSWWEIQVVGDAALEEGISWRLQSFGCQGTASQKQNHDCHMTGYLPQKQVNHLDLAALSLWLAQDAIALGFLPPTTRWKLINEEDWATSWQQYWHPQEVGDRLLIYPAWLDLPEHCERLLLRLDPGVAFGTGTHPTTQLCLEALEMHLDQTFGPVEQVTVADIGCGTGILSIAALRLGAKQAFAVDLDPLAVESADRSRDLNEIPPEQMIVQQGSVEQVPHPVQGIVCNILAETIIDLIPTLATISQPHTWAAFSGILVTQAKSVVDALEQQGWQVGSLWQRQDWCCINAHRL
|
Methylates ribosomal protein L11.
|
B8HPZ1
|
P0AG78
|
SUBI_ECOLI
|
Sulfate starvation-induced protein 2
|
Escherichia
|
MNKWGVGLTFLLAATSVMAKDIQLLNVSYDPTRELYEQYNKAFSAHWKQQTGDNVVIRQSHGGSGKQATSVINGIEADVVTLALAYDVDAIAERGRIDKEWIKRLPDNSAPYTSTIVFLVRKGNPKQIHDWNDLIKPGVSVITPNPKSSGGARWNYLAAWGYALHHNNNDQAKAQDFVRALYKNVEVLDSGARGSTNTFVERGIGDVLIAWENEALLAANELGKDKFEIVTPSESILAEPTVSVVDKVVEKKGTKEVAEAYLKYLYSPEGQEIAAKNYYRPRDAEVAKKYENAFPKLKLFTIDEEFGGWTKAQKEHFANGGTFDQISKR
|
This protein specifically binds sulfate and is involved in its transmembrane transport.
|
P0AG78
|
Q9P3U4
|
HEL1_SCHPO
|
RING-type E3 ubiquitin transferase dbl4
|
Schizosaccharomyces
|
MSDLLDDEFYEEEFENDLLDASEFEDEFDEDAEIDDDGFTVERKRRRAHSVSYRVVSVRDLRASLNEKINQLTSIIDLTREQVLGLYRYFKWNRERLLERYIDAPEESLQKAGVGLSGSKQREVVHHEGTCEICYDEGCLPFFSAECDHEFCLACYRQYLDSRISEGESVIQCPEESCTQIVSIQSITKVLDEKSLDRYHRLLDRSFVDDNDHLRWCPAPDCEFAIECHVTQASLSSVVPTVTCNCGKQFCFGCGHDNHQPTICPLVKIWLQKCQDDSETANWIHANTKECPKCSTTIEKNGGCNHMTCKKCKYEFCWVCLGPWTEHGNNWYTCNRYEEKSSTSARDSQSKSRASLERYLHYYNRFANHEQSAKLDHELYEHTHKRMTQMQVDSNLSWVEVQFLKNAVDILFQCRQTLKWTYAFAYYLARNNQTEIFEDNQRDLELAVENLSELCERPCQDCSLSVFKQRVLDKTVYVRSRRDVLLDDTARGLAEGRWEYVVDV
|
Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation.
|
Q9P3U4
|
Q03637
|
COLQ_TORMA
|
AChE Q subunit
|
Torpedo
|
MLGILLQKATATLASGLNSSRAGMFPIALGLLLQLFFDHALAESTFLDKAFSLQAALLPMEHKKRSVNKCCLLTPPPPPMFPPPFFTETNILQEVDLNNLPLEIKPTEPSCKITCIIGPPGPSGPQGPQGIQGIMGPKGEIGEIGRPGRKGRPGVRGPRGMPGSPCSPGPIGPRGEKGDIGLTGLPGARGPMGPKGLTGQKGEKGIIGEKGQQGIKGEMGVMGLPGMLGQKGEMGPKGVSGAPGHRGPVGRPGKRGKTGLKGDIGPPGIMGPSGPPGPSGLPVMSGSGHLMVGPKGERGLPGPVGRCDCNLPQTVVNPSYNKFPTLINPPQVPAIFVVDSEDELEKLNTENALAFRKDQKSLYYRDTVGWLPIQIAPIQQMRQNPTGFCGDEIVQVENGEECDDGNRIVTDSCINCKQAYCGDGYLQSGLEECDGKDFGYHTCKSYLPGSYGELKCTSYCYIDSTGCRYFT
|
Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.
|
Q03637
|
A9MSA2
|
RLMM_SALAR
|
23S rRNA 2'-O-ribose methyltransferase RlmM
|
Salmonella
|
MNKVVLLCRPGFEKECAAEITDKAGKRELFGFARVKENTGYVIYECYQPEDGEKLISELPFSSLIFARQWFVVGELLQHLPPEDRITPIVGMLQGVVEKGGELRVEVADTNESKELMKFCRKFTVPLRAALRDAGVLTHYETPKRPVVHVFFIAPGCCYTGYSLAHNHSPFYMGIPRLKFPSDAPSRSTLKLEEALHVFIPEDEWDERLANGMYAVDLGACPGGWTYQLVKRNMWVYSVDNGPMAQSLMDTGQVTWLREDGFRYRPNRNNISWMVCDMVEKPAKVTALMAQWLVNGWCRETIFNLKLPMKKRYEEVSHNLAYLQAQLDEHGVNAQIQARQLYHDREEVTVHVRRLWAAVGGRRDER
|
Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
|
A9MSA2
|
Q4FP17
|
LEU3_PELUB
|
Beta-IPM dehydrogenase
|
Candidatus Pelagibacter
|
MIKIKKRKILLLPGDGIGPEVIQEVKKVILWLNSNKSLDFEIDEDLAGGCSYDKHGTPITDEVFYKALESEFVMLGAVGGPKWDNLEFSKKPERALLKLRKELKLFANLRPAICFEQLVDASTLKPEIVSGLDIMIVRELTGGIYFGEPRGIKPIENGERKGINTHSYTTSEIVRVAKVAFDLARKRSNRVTSCEKSNVMEAGQLWKEEVQELHDKEYKDVELSHMLADNCAMQLLKNPKQFDVIVTDNLFGDMLSDQASMLTGSLGLLPSASLGAKNKDGEMRAMYEPIHGSAPDIAGKEIANPIASILSFAMALRYSLDLDSEADALEKAVQDVLNDGLRTKDILSQGKKEVSTSAMGDAIISKLQ
|
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
|
Q4FP17
|
Q3SGF7
|
RSMA_THIDA
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Thiobacillus
|
MHTPRKRFGQNFLIDDGIVHAIVNAIHPQAGETVVEIGPGLGALTRPLLERLPHLHAVELDRDIIARLRRAWPPERLTLHAGDALKFDFGSLGDDLRIVGNLPYNISTPLLFHLLEFAPRIRDMHFMLQKEVVERMVASPATADYGRLSIMLQRRFHMEWLLDVPPTAFDPPPKVESAVVRLIPKSTAEVPSVDEALFARVVAAAFAQRRKTLRNTLSALMRPEDFVALGIDPGLRAEALHVADYEAITAYLATR
|
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
|
Q3SGF7
|
P0DPT2
|
CA1B_CONCT
|
C1.2
|
Pionoconus
|
SDGRNEAANDEASDVIELALKGCCSNPVCHLEHPNACGRRR
|
Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks rat neuronal nAChR alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=128.9 nM) and alpha-7/CHRNA7 (IC(50)=1511 nM) . In vivo, intramuscular injection into zebrafish does not produce any effect on the locomotion of zebrafish .
|
P0DPT2
|
Q7NTU0
|
LOLD_CHRVO
|
Lipoprotein-releasing system ATP-binding protein LolD
|
Chromobacterium
|
MNKVLSCRSLGKRYQEGKLALDVLSGVDLEVGKGEHLAIVGASGSGKSTLLHLLGGLDTPTAGTVEVLGRDLSKLSETERGKLRNESMGFVYQFHHLLPEFTALENVMMPLLIRRMDKGEAARRAAEMLERVGLGKRLEHKPGELSGGERQRAAIARALVTQPACLLADEPTGNLDAHTASQVFELMLELNRTLGTSLIIVTHDLELAGRTQRVLRLNEGRLAVSDTVSA
|
Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
|
Q7NTU0
|
Q00016
|
IFR_CICAR
|
NADPH:isoflavone oxidoreductase
|
Cicer
|
MASQNRILVLGPTGAIGRHVVWASIKAGNPTYALIRKTPGDINKPSLVAAANPESKEELLQSFKAAGVILLEGDMNDHEALVKAIKQVDTVICTFGRLLILDQVKIIKAIKEAGNVKRFFPSEFGLDVDRHDAVDPVRPVFDEKASIRRVVEAEGVPYTYLCCHAFTGYFLRNLAQFDATEPPRDKVIILGDGNVKGAYVTEADVGTYTIRAANDPRTLNKAVHIRLPHNYLTSNEVVSLWEKKIGKTLEKSYISEEKVLKDINVSTFPHNYLLALYHSQQIKGDAVYEIDPAKDAEAYDLYPDVKYTTADEYLDQFV
|
Reduces achiral isoflavones to chiral isoflavanones during the biosynthesis of chiral pterocarpan phytoalexins.
|
Q00016
|
Q8R7Y5
|
ECFA2_CALS4
|
Energy-coupling factor transporter ATP-binding protein EcfA2
|
Caldanaerobacter
|
MPIKVENVSFIYNEGTPYATVALKDINFSIDDEEFVGIIGHTGSGKSTLIQQLNGLLKPSKGKIYINGIDITDKKVSLKDIRKQVGLVFQYPEYQLFEETVFKDIAFGPSNLGLSEEEVKERVYEAMEIVGISKELADKSPFELSGGQKRRVAIAGILAMRPKILILDEPTAGLDPKGKQEILNKIKEIHDKYKMITILVSHNMEDIARIADKIIVMNRGKIELIGTPREVFREAERLEKIGLSVPQITSLARELRKRGVPIPPDVLTIEEAKEHILRYLRGTKNV
|
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.
|
Q8R7Y5
|
Q32K50
|
KEFF_SHIDS
|
Quinone oxidoreductase KefF
|
Shigella
|
MILIIYAHPYPHHSHANKRMLEQARTLDGVEIRSLYQLYPDFNIDIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVLSHGWAYGHGGTAPRGKHLLWAVTTGGGESHFEIGAHPGFDVLSQPLQATAIYCGLNWLPPFAMHCTFICDDETLEGQARHYKQRLLEWQEAHHG
|
Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC.
|
Q32K50
|
Q5U2U6
|
CDIP1_RAT
|
LITAF-like protein
|
Rattus
|
MSNEPPPPYPGGPTAPLLEEKSGAPHTPGRTSPAVMQPPPGMPLPSADIAPPPYEPPGHPVPQPGFVPPHMNADGTYMPAGFYPPPGPHPPMGYYPPGPYPPGSYPGPGGHTATVLVPSGAATTVTVLQGEIFEGAPVQTVCPHCQQAITTKISYEIGLMNFVLGFFCCFMGCDLGCCLIPCLINDFKDVTHTCPSCKAYICTYKRLC
|
Acts as an important p53/TP53-apoptotic effector. Regulates TNF-alpha-mediated apoptosis in a p53/TP53-dependent manner.
|
Q5U2U6
|
Q6K508
|
GLUD1_ORYSJ
|
Glutelin type-D 1 basic chain
|
Oryza sativa
|
MATTTSLLSSCLCALLLAPLFSQGVDAWESRQGASRQCRFDRLQAFEPLRKVRSEAGDTEYFDERNEQFRCAGVFVIRRVIEPQGLVVPRYSNTPALAYIIQGKGYVGLTFPGCPATHQQQFQLFEQRQSDQAHKFRDEHQKIHEFRQGDVVALPASVAHWFYNGGDTPAVVVYVYDIKSFANQLEPRQKEFLLAGNNQRGQQIFEHSIFQHSGQNIFSGFNTEVLSEALGINTEASKRLQSQNDQRGDIIRVKHGLQLLKPTLTQRQEEHRQYQQVQYREGQYNGLDENFCTIKARVNIENPSRADYYNPRAGRITLLNNQKFPILNLIGMGAARVNLYQNALLSPFWNINAHSVVYIIQGSVRVQVANNQGRSVFNGVLHQGQLLIIPQNHAVIKKAEHNGCQYVAIKTISDPTVSWVAGKNSILRALPVDVIANAYRISRDEARRLKNNRADEIGPFTPRFPQKSQRGYQFLTEGLSLIGM
|
Seed storage protein.
|
Q6K508
|
Q5F3W2
|
INSI2_CHICK
|
Insulin-induced gene 2 protein
|
Gallus
|
MAENDAKPTLPKKSGPYISSVTSHGMNLVIRGIVLFFIGVFLALVLNLLQIQRNVTLFPPDVITSIFSSAWWVPPCCGTASAVIGLLYPCMDRHLGEPHKFKREWSSVMRCVAVFVGINHASAKVDFANNIQLSLTLAALSIGLWWTFDRSRSGFGLGVGIAFLATLVSQLLVYNGVYQYTSPDFLYVRSWLPCIFFAGGITMGNIGRQLAMYECKVIAEKSHED
|
Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR. Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs). Binds oxysterol, including 22-hydroxycholesterol, 24-hydroxycholesterol, 25-hydroxycholesterol and 27-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum. In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBPs to the Golgi. Sterol deprivation reduces oxysterol-binding, disrupting the interaction between INSIG2 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBPs. Also regulates cholesterol synthesis by regulating degradation of HMGCR.
|
Q5F3W2
|
Q3IMX0
|
RL19E_NATPD
|
50S ribosomal protein L19e
|
Natronomonas
|
MTDLKAQKRLAADILDVGENRVRFDPDAQAEIADAITREDIRELIEDGTIEAKTAKGNSRGRARKRQQKRAYGHKKGHGSRKGRSGGRQNEKEDWQSRIRAQRRELRELRDAGDISREQYRELYDMASGGEFDSVADLNRYIDDKHGEQ
|
Binds to the 23S rRNA.
|
Q3IMX0
|
Q48RI5
|
PEPX_STRPM
|
X-prolyl-dipeptidyl aminopeptidase
|
Streptococcus
|
MRYNQFSYIPTSLERAAEELKELGFDLDLQKTAKANLESFLRKIFFHYPDSDYPLSHLIAKNDMDALSFFQSEQELSKEVFDLLALQVLGFIPGVDFTEADAFLDKLAFPIHFDETEIIKHIHHLLATRCKSGMTLIDDLVSQGMLTMDNDYHFFNGKSLATFDTSQLIREVVYVEAPLDTDQDGQFDLIKVNIIRPQSQKPLPTLMTPSPYHQGINEVANDKKLYRMEKELVVKKRRQITVEDRDFIPLETQPCKLPIGQNLESFSYINSYSLNDYFLARGFANIYVSGVGTAGSTGFMTSGDYAQIESFKAVIDWLNGRATAYTSHSKTHQVRADWANGLVCTTGKSYLGTMSTGLATTGVDGLAMIIAESAISSWYNYYRENGLVCSPGGYPGEDLDVLTELTYSRNLLAGDYLRHNDHYQELLNQQSQALDRQSGDYNQFWHDRNYLKNAHQIKCDVVYSHGLQDWNVKPRQVYEIFNALPSTINKHLFLHQGEHVYMHNWQSIDFRESMNALLCQKLLGLANDFSLPEMIWQDNTCPQNWQERKVFGTSTIKELDLGQELLLIDNHYGEDEFKAYGKDFRASKAALFKGKANQALIDILLEEDLPINGEIVLQLKVKSSENKGLLSAQILDYGKKKRLGDLPIALTQSSIDNGQNFSREPLKELPFREDSYRVISKGFMNLQNRNNLSSIETIPNNKWMTVRLPLQPTIYHLEKGDTLRVILYTTDFEHTVRDNSNYALTIDLSQSQLIVPIASN
|
Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
|
Q48RI5
|
Q9FNF8
|
P4KG3_ARATH
|
Phosphatidylinositol 4-kinase gamma 3
|
Arabidopsis
|
MSVASVALSPALEELVNFPGIIGRFGFNLDDPILVFLTIAGSVIPKRVMESDSIASVKLRIQSIKGFFVKKQKLLYDGREVSRNDSQIRDYGLADGKLLHLVIRLSDLQAISVRTVDGKEFELVVERSRNVGYVKQQIASKEKELGIPRDHELTLDGEELDDQRLITDLCQNGDNVIHLLISKSAKVRAKPVGKDFEVFIEDVNHKHNVDGRRGKNISSEAKPKEFFVEPFIVNPEIKLPILLKELISSTLEGLEKGNGPIRSSDGSGGAYFMQDPSGHKYVSVFKPIDEEPMAVNNPHGQPVSVDGEGLKKGTQVGEGAIREVAAYILDYPMTGPRTFPHDQTGFAGVPPTTMVKCLHKDFNHPNGYSFSPENTKIGSLQMFVSNVGSCEDMGYRVFPVDQVHKISVLDIRLANADRHAGNILVSRDGKDGQMVLTPIDHGYCFPNKFEDCTFEWLYWPQAKEPYSSETLEYIKSLDPEKDIELLRFHGWEIPPSCTRVLRISTMLLKKGSAKGLTPFTIGSIMCRETLKEESVIEQIIHDAEAIVPTETTEDEFISTVSAIMDNRLDQYAWN
|
The phosphorylation of phosphatidylinositol (PI) to PI4P is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3).
|
Q9FNF8
|
P04570
|
SCP2_BRALA
|
Sarcoplasmic calcium-binding proteins II, V, VI, and VII
|
Branchiostoma
|
GLNDFQKQKIKFTFDFFLDMNHDGSIQDNDFEDMMTRYKEVNKGSLSDADYKSMQASLEDEWRDLKGRADINKDDVVSWEEYLAMWEKTIATCKSVADLPAWCQNRIPFLFKGMDVSGDGIVDLEEFQNYCKNFQLQCADVPAVYNVITDGGKVTFDLNRYKELYYRLLTSPAADAGNTLMGQKP
|
Like parvalbumins, SCPs seem to be more abundant in fast contracting muscles, but no functional relationship can be established from this distribution.
|
P04570
|
Q317B9
|
PURA_OLEA2
|
IMP--aspartate ligase
|
Oleidesulfovibrio
|
MSNVVIMGAQWGDEGKGKIVDLLSREIDVIVRFQGGNNAGHTVIVGDKSYILHLIPSGILHEGKTCLIGNGVVLDPVVFWKEVEALAERGIDVGPQRLMISRKAHVIMPYHKALDVAREDFKNKESRIGTTGRGIGPCYEDKMSRIGVRAGDLADPALLRSKIEAALVEKNALFTALYGREAMSVDAVFDEVMAVGGRLVPYLTDVSSVIEDAWANDSGVMFEGAQGTHLDIDHGTYPFVTSSNTVAGNAAAGSGIPASRLDRVVAIVKAYTTRVGAGPFPTELDDEAGNHMQSVGHEFGATTGRKRRCGWLDCALLRESVRLNGPTDIALTKLDVMSGLKELKICVAYEYNGQRLQHPPQEQNGLAHVTPVYETMPGWDDDITAAKTWEDLPEAARNYICRIEELLGVPVSMISVGPERDQTLNRK
|
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.
|
Q317B9
|
Q21360
|
MAK1_CAEEL
|
MAP kinase-activated protein kinase mak-1
|
Caenorhabditis
|
MMFEYEEDEDPMEQQKHEEFKHHSTDHSGSPQENPFRFSYDTGKRAASMFVTPSSEDLIAYGTKHLLDSPTAVQRSLVLNATTSLNIDCDLSSDDDLSPTTQRKICFCASQNPAETQEQGLRPAKSTLAISFPCHQHQITEDYTISAEIIGIGESGKVMACYQKVTGEKFALKVLRDSQKARREVELHWLTNAHENVVSILDIYENTFDNVKCLLMVVEFLEGGDLLSQFESQGSIPYTEKKVGEIIRQIGNAVMYLHDMNIAHRDIKLENILCSGTGDNCVYKLGDYGFAKRPERNVLMESPCCTPFYAPPEVLGRERYDKSCDMWSLGVAMYILLCGYPPFYSMKGVALSPGMRSRIANAYYAFPHEEWDCVSKDTKDDIRCLLRTNPSDRLTIHELMATPLVTGEPIVPGKHITTAIAIPGADESECGGGVFDDGFIVEEEETPDTVAEILPVPKSVRFLRDGVKAPRLHSIQEEVGRAMEIMRMGTDQVYIKNPTASCNNLFERRRAVHLSIPRVYC
|
Serine/threonine-protein kinase which may play a role in body wall muscle contraction. May phosphorylate unc-22/twitchin.
|
Q21360
|
Q74ZL5
|
H2B1_ASHGO
|
Histone H2B.1
|
Eremothecium
|
MSSKASKAPASKAPAEKKPAAKKTSSSVDASKKRTKTRKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIASEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA
|
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
Q74ZL5
|
Q9P0K7
|
RAI14_HUMAN
|
Retinoic acid-induced protein 14
|
Homo
|
MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHDQVSKISSERSGTPKKRKAPPPPISPTQLSDVSSPRSITSTPLSGKESVFFAEPPFKAEISSIRENKDRLSDSTTGADSLLDISSEADQQDLLSLLQAKVASLTLHNKELQDKLQAKSPKEAEADLSFDSYHSTQTDLGPSLGKPGETSPPDSKSSPSVLIHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEVISVYRMHLLYAVQGQMDEDVQKVLKQILTMCKNQSQKK
|
Plays a role in actin regulation at the ectoplasmic specialization, a type of cell junction specific to testis. Important for establishment of sperm polarity and normal spermatid adhesion. May also promote integrity of Sertoli cell tight junctions at the blood-testis barrier.
|
Q9P0K7
|
Q817W6
|
TGT_BACCR
|
tRNA-guanine transglycosylase
|
Bacillus cereus group
|
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEYEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF
|
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
|
Q817W6
|
B2JG21
|
RL9_PARP8
|
50S ribosomal protein L9
|
Paraburkholderia
|
MQIILLEKVLNVGNLGDIVKVKDGYARNFLIPNKKARRATKEAIAEFEVRRAELEKVAAEKLSAAQAQGEKLSGMTVQIAQKAGVDGRLFGSVTNADIAAALGKQGFEVEKAQVRLPEGPLKMVGDHPVHVSLHTDVTVDVTVSVLGEHV
|
Binds to the 23S rRNA.
|
B2JG21
|
P35362
|
OPSD_SPHSP
|
Rhodopsin
|
unclassified Sphodromantis
|
MSLINEPSYSAYSWGGQGGYGNQTVVDKVLPEMLHLIDPHWYQFPPMNPLWHGLLGFVIGCLGFVSVVGNGMVIYIFSTTKGLRTPSNLLVVNLAFSDFLMMLSMSPPMVINCYYETWVLGPFMCELYALLGSLFGCGSIWTMVMIALDRYNVIVKGLAAKPMTNKTAMLRILGIWAMSIAWTVFPLFGWNRYVPEGNMTACGTDYLNKEWVSRSYILVYSVFVYFLPLATIIYSYWFIVQAVSAHEKQMREQAKKMNVASLRSAENANTSAECKLAKVALMTISLWFFAWTPYLVTDFSGIFEWGKISPLATIWCSLFAKANAVYNPIVYGISHPKYRAALNKKFPSLACASEPDDTASQASGATTVSDEKSASA
|
Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
|
P35362
|
A4FYN1
|
FLPA_METM5
|
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase
|
Methanococcus
|
MEKIKVKEIFNNVYSVDFGDGLKRIATKSLIPGKRVYGEKLVYSDNIEYRVWNPNKSKLGAAIINGLKKMPIKKGTKVLYLGASAGTTPSHVADIAENSLVYALEFAPRIMREFIDSCNERKNLIPVLGDANRPQDYSNIVEKVDVIFEDVAQPNQAEILVKNAKWFLKENGYAMISIKARSVDVTKNPREIFAEQKKILIEGGFEIVDEVNIEPFEKDHMMMVGIWKGN
|
Involved in pre-rRNA and tRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA.
|
A4FYN1
|
P01523
|
CM3A_CONGE
|
Myotoxin I
|
Gastridium
|
MMSKLGVLLTICLLLFPLTALPMDGDEPANRPVERMQDNISSEQYPLFEKRRDCCTPPKKCKDRQCKPQRCCAGR
|
Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin potently blocks rat Nav1.4/SCN4A (IC(50)= 19-110 nM) . It also moderately blocks rNav1.1/SCN1A (Kd=260 nM), rNav1.2/SCN2A (IC(50)=2.7-17.8 uM), and mNav1.6/SCN8A (IC(50)=680 nM) . The inhibition is reversible. In vivo, induces paralysis to an isolated skeletal muscle preparation from frog (cutaneous pectoralis) within a few minutes .
|
P01523
|
Q65HX2
|
SCPB_BACLD
|
Segregation and condensation protein B
|
Bacillus
|
MTLDIVNWKAIVEALLYAAGDEGLTKKQLLSVLEVDEAELLDIMLDVKETYEKEDRGIELVEYADTYMLSTKKEFAVYLKKLIEAPSKGLSQAALEVLAIVSYKQPITRAEVEEIRGVKSERILQSLVAKALLCEVGRADGPGRAILYGTTETFLEQFGLKTLEELPPLPENVEEDGVQEEADLFFENFNQTFEDLK
|
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves.
|
Q65HX2
|
Q8ZPZ1
|
RLUE_SALTY
|
rRNA-uridine isomerase E
|
Salmonella
|
MRQLISSENTMQKTSFRNHYVKRFSSRQASKSRKENQPKRVVLFNKPYDVLPQFTDEAGRRTLKDFIPVQGVYAAGRLDRDSEGLLVLTNDGALQARLTQPGKRTGKIYYVQVEGIPDNAALQALRTGVTLNDGPTLPAGIEIVAEPDWLWPRTPPIRERKNIPTSWLKVTLYEGRNRQVRRMTAHVGHPTLRLIRYSMGDYTLNGLDNGQWREIAQEKDR
|
Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA.
|
Q8ZPZ1
|
B3EGT4
|
MIAB_CHLL2
|
tRNA-i(6)A37 methylthiotransferase
|
Chlorobium
|
MPRDRRKFYIHTFGCQMNQADSGIIAALLEQDGYQQASSEEEAGIIMLNTCAVRENAVERIAHYLQHVKGFKRKCPELLVGLTGCIPQYRREELFTVFPVIDFLAGPDTYRVLPVLIAEAGKGRAARLDFNPFETYDGVTQARTQSLTAFVPIMRGCNNMCAFCVVPFTRGRERSHPFGSVLDEVRALAESGCREITLLGQNVNSYHDSQSGADFSRLLDAVSREAPETRIRFTTSHPKDMSHSLVETMASRPNICNHLHLPVQSGSTRMLARMNRGHDIEDYRNKIELLRERIPGISLSTDLIAGFCGESDADHCQTLELMREVRFDSAFMFYYSVRPGTLAARTMPDDVPEEVKKQRLQEIIDLQNGISAELLRLAIGSVVEVLVESESRRSSDQLMGRTGGNRVVVFDRGIHQPGDMVRVMITGSTSATLIGRAAENQH
|
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
|
B3EGT4
|
D4CZZ6
|
NSCR_TRIVH
|
Neosartiricin B biosynthesis protein R
|
Trichophyton
|
MEKRGPKRRQEAAHLSCELCRERKVKCDKLDPCTNCSSAGVICVPVRRPRLPRGAHAQRLRRISPEDPEAPIQIDIASPADAGTIADDDLKERIRRLEALVDSMRSSNHVSKQLIKNFQTNKDQEAQDTIESTLNRIDEDSLLIKGPRVHPSDGGLRILGLSGSSSPETGWASIIEDREVSMQLCQVYLLNVDPVIKILHRPSLEKWMLEGQRYLGLPEGHAAVESLGAAICYVAATSLTETQSWARFHTTKSSIVARARRACETTLEKSSPLLSPDVTTLQAFVLYLVARRSEDPSRAVWTLMAFAVRIAKALDLPRGIDDNFFGQQMRKRLWLAICLLDFQTSLSQPSEPLITVAEATSLFSPPRHINDSDFDPTTSHDIPDREGLTDTTFSLVSHHVQAAGRLLNFEPSVKDDGSRQQHVQNFEQRTLRLLLYCDPESTPYAWFTWHRIQCFVSGARLSAIRPLIHQHGGHPIPILDANEGTSILSLALNILEKVQLVHTDPRGEGFRWFVTVPWQPLAIAISECYICQDRSLVQRAWPIVEAAFQQHEATVSGSSKAISITLERLMCRVRGKLLPSLELSRPGEDLALVTEAPISTSPQKVDPLVFSLDSPLLIAGQEQLLDADQSWAAWEEVIASLHYDETGRADMFLS
|
Transcription factor that specifically regulates the neosartoricin B biosynthesis gene cluster .
|
D4CZZ6
|
P0DUH8
|
SCX6_CENTE
|
Beta-toxin Ct6
|
Centruroides
|
MKTFVLALCLVLIGMVYAKDGYLVSKHTGCKLGCSPKIGDRYCHIECTSMNHKGDEGYCYWLACYCKGMPENAEVYPLPNKSCGK
|
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.
|
P0DUH8
|
Q8W8V0
|
RR7_PSINU
|
30S ribosomal protein S7, chloroplastic
|
Psilotum
|
MSRQSETKKRTAKSDPIYRNRSVSMFINHILKDGEKSLAHKILYRAMKQIKRKTKKNPLSVLRQAVYRVTPNVAVKSRRVGGSNYQVPVEVKPARGKALAIRWIVGASRNRSGRSMASKSSYELIDAARNTGSAIRKKEETHKMAEANKAFAHLR
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit.
|
Q8W8V0
|
P57867
|
DAPB_PASMU
|
4-hydroxy-tetrahydrodipicolinate reductase
|
Pasteurella
|
MTLRVAIVGAGGRMGRQLIQAVSETEGVVLGAAFERQGSSLLGADAGELANVGHLGVQITDDLASQQDQFDLLIDFTRPEGTLAHLAFCVAQHKNMVIGTTGFDDDGKAKIQQAADSIGIVFASNFSVGVNLVFKLLEKAAKVMGDYCDIEIIEAHHRHKVDAPSGTALSMGEHIAKTLGRDLKTHGVFTRDGITGERKRDEIGFATIRASDVVGEHSVWFADIGERVEIAHKATSRMTFAKGAVRAAKWLAQKEKGLFDMTDVLDLNQL
|
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
|
P57867
|
Q2GL53
|
RS3_ANAPZ
|
30S ribosomal protein S3
|
phagocytophilum group
|
MGQKSNPIGLRLKIVGTWDSLWYANRDYATKLHEDLLLRSFVKKTFHHAAVSKVVIARKVDAVIINIHSARPGVIIGKKGVDIDRIKQKIAKMVNHEVELHIVEVKKPDLKAVLIAENIAQQLEKRVSFRRAMKRGVQNCLKMGAKGVKVSCAGRLGGAEIARTEWYKEGSVPLHTFRANIDYSCVEAKTIYGIVGVKVWVYVGDSRAVVE
|
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
|
Q2GL53
|
A7FIG9
|
PTH_YERP3
|
Peptidyl-tRNA hydrolase
|
Yersinia
|
MSSIKLIVGLANPGAEYAQTRHNAGAWYVDLLAERHNQSLKEESKFFGYTARLNLAGQDIRLLVPATFMNLSGKAVAAMASFYRILPEEILVAHDELDILPGMAKLKLGGGNGGHNGLKDIQNKLGNNPNFYRLRIGIGHPGDKSKVTGFVLGKPPASEQTLIDNAIDESIRCTEVLLNEGMTKAMNRLHAFKASA
|
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
|
A7FIG9
|
O51551
|
CHED_BORBU
|
Probable chemoreceptor glutamine deamidase CheD
|
Borreliella
|
MLNHFNFKLKRDVTIIVPGEAFVSNKRVISTILGSCVAVVLCDESNNLIGMNHYVLVKSDLDISPDQRGRYGIYAIPMLINAMLENGASKSNLKAKLFGGTNFMAKGSVKVGLENSEFAVNTLNKYRIPILAKDFDQSKSRKIFAFPENFKVIVEYPDGTKVF
|
Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
|
O51551
|
Q1BGJ2
|
RHAM_BURCA
|
Type-3 mutarotase
|
Burkholderia cepacia complex
|
METIAFRMHLHPGKRDEYRRRHDAIWPELADALRAAGISDYWIFLDDDTHHLFAVLKRPADHRIAQLAETDVMRRWWAYMADLMATGPDGRPVEKALEPMFHLE
|
Involved in the anomeric conversion of L-rhamnose.
|
Q1BGJ2
|
Q8PV99
|
ASPD_METMA
|
L-aspartate dehydrogenase
|
Methanosarcina
|
MLKIGIIGCGFIGGQICRAIDSGEIDAELYALCDSSESKAFGLAKSLNTCKPAYMKIEELISSVDLVVESASQNAVRFIVPQALKAGCSVMVLSVGALADKELRETLFGLAKKHNCKLYFPSGAVVGIDGINSAHAAGISSVTLTTRKPPSGLMGAPYVVEHGIELEKLEKETILFEGTASEAVKAFPANVNVAATISLAGIGFERTMVRVIADPSLSRNIHEINVEGEFGKFCTKVENLPSPENPKTSYLAALSAISTLKKILNPVQIGT
|
Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
|
Q8PV99
|
B6ES34
|
GCSH_ALISL
|
Glycine cleavage system H protein
|
Aliivibrio
|
MEKDLKFTASHEWVRENGDGTVTVGISNHAQGLLGDVVFVDLPDVDDEVTAGENFSLVESVKAASDIYAPISGVIVEINEELEDSPELVNEEPYEGGWIARIKLSDDGDLENLIPGDQYLESIEEE
|
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.
|
B6ES34
|
Q74LQ3
|
PHNC_LACJO
|
Phosphonates import ATP-binding protein PhnC
|
Lactobacillus
|
MIQLKNVSKIYDNGTVGLKDINLNIDKGEFIVVVGLSGAGKSTLLRSINRLQDVSEGDIIIDGKSITSAKGKDLREIRRDIGMIFQSFNLVKRSSVLRNVLTGRVGYYPTWKTTFNLFTKEDKQKAYEALQRVDLADKVYTRADQLSGGQQQRVAIARVLTQNPKIILADEPTASLDPQTSRRVMHDLKMLNEEYGMTVVANLHSVELAKEFGDRVIGVRAGQIVYDGKMSETSQAVFDDIYNGGNGKKGEEDA
|
Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
|
Q74LQ3
|
Q01718
|
ACTHR_HUMAN
|
Melanocortin receptor 2
|
Homo
|
MKHIINSYENINNTARNNSDCPRVVLPEEIFFTISIVGVLENLIVLLAVFKNKNLQAPMYFFICSLAISDMLGSLYKILENILIILRNMGYLKPRGSFETTADDIIDSLFVLSLLGSIFSLSVIAADRYITIFHALRYHSIVTMRRTVVVLTVIWTFCTGTGITMVIFSHHVPTVITFTSLFPLMLVFILCLYVHMFLLARSHTRKISTLPRANMKGAITLTILLGVFIFCWAPFVLHVLLMTFCPSNPYCACYMSLFQVNGMLIMCNAVIDPFIYAFRSPELRDAFKKMIFCSRYW
|
Receptor for corticotropin (ACTH). This receptor is mediated by G proteins (G(s)) which activate adenylate cyclase (cAMP).
|
Q01718
|
Q8NGG4
|
OR8H1_HUMAN
|
Olfactory receptor OR11-180
|
Homo
|
MGRRNNTNVPDFILTGLSDSEEVQMALFILFLLIYLITMLGNVGMILIIRLDLQLHTPMYFFLTHLSFIDLSYSTVITPKTLANLLTSNYISFMGCFAQMFFFVFLGAAECFLLSSMAYDRYVAICSPLRYPVIMSKRLCCALVTGPYVISFINSFVNVVWMSRLHFCDSNVVRHFFCDTSPILALSCMDTYDIEIMIHILAGSTLMVSLITISASYVSILSTILKINSTSGKQKALSTCASHLLGVTIFYGTMIFTYLKPRKSYSLGRDQVASVFYTIVIPMLNPLIYSLRNKEVKNALIRVMQRRQDSR
|
Odorant receptor.
|
Q8NGG4
|
Q4QMD8
|
MLTC_HAEI8
|
Murein lyase C
|
Haemophilus
|
MKKYLLLALLPFLYACSNSSNQGINYDEAFAKDTQGLDILTGQFSHNIDRIWGVNELLVASRKDYVKYTDSFYTRSHVSFDEGNIVIETQQDLNRLHNAIVHTLLMGADAKGIDLFTSGDVPISSRPFLLGQVVDHQGQQIANQVIASNFATYLIQNKLQTRRLQNGHTVQFVSVPMIANHVEVRARKYLPLIRKAAQRYGIDESLILGIMQTESSFNPYAISYANAIGLMQVVPHTAGRDVFAMKGKGGQPSTRYLYDPANNIDAGVSYLWILQNQYLDGITNPTSKRFAMISAYNSGAGAVLRVFDNDKDTAIYKINQMYPEQVYRILTTVHPSSQARNYLLKVDKAQKKFRVRR
|
Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division.
|
Q4QMD8
|
Q1QUF2
|
RSMC_CHRSD
|
rRNA (guanine-N(2)-)-methyltransferase RsmC
|
Chromohalobacter
|
MSAETPPCQLLERQSEAYRDWLWVAPPHDAWLHTVGGSVWSADATICQAWRARGRPVHADLAPTLTAPVPGAVLFWPKTHALGEWWLLALCAALPEGTPLQVVGEHQGGVKRVLKSLAALGLGCRKVDSARRCTLYATRTARLALSPEAAWTRFEAAGLTLESHPGVFGHGKLDDGTRQLLEVLPTALGDPAGQRVLDVGCGDGILGAWLGVRGAQVAAVDLDAFAVAATRRTFQANGVAGEAWQSDVFGDVSGSYDAIVSNPPFHQQRAIDYGPAERLIREAPARLVPGGRLVLVANAFLPYPRWLEDAFGEFTVLADDRRFRVYQAVKTRR
|
Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
|
Q1QUF2
|
Q6DH87
|
FUND1_DANRE
|
FUN14 domain-containing protein 1
|
Danio
|
MADRGEDAESEDELYEVVNITDYARRHQWWSRVFGNSTGPIAEKYSVASQIMMGGVSGWCAGYLFQRVGKLVATAVGGGFLLLQIANHSGYVQVDWRKVEKDVNKAKKHLKKNAKKAAPELNTFIEDSTEFVKRNIVISGGFVGGFLLGLAS
|
Acts as an activator of hypoxia-induced mitophagy, an important mechanism for mitochondrial quality control.
|
Q6DH87
|
Q5HTK3
|
DNAJ_CAMJR
|
Chaperone protein DnaJ
|
Campylobacter
|
MEISYYEILEITQNADKETIKKAYRKMALKYHPDRNQGDKEAEDKFKLVNEAYEVLSNDEKRAIYDRYGKDALKGGGFGSSSSGFGGFEDLGDIFSSFFGEGFGSSRRRKSSNDEKIPSDFIVNLKLSFKEAVFGCKKNIDFTYKCSCKTCNGTGAKDGKLQTCPKCQGRGQVGVSQGFITFAQTCPDCQGIGEKASEKCSDCKGLGYNESKNSVELNIPEGVDTGMKLRVNAKGNILKNGTRGDMYVKIIAAEDDTFIRDDDDIYIEFPVFFTQAILGESIKVPTIRGEATLNLPKGAKDGQRFVLEKEGVKDVHSSRIGNQIVQISIKFPTSLNDEQKELLEKLSESFGIKDGMHQEQKGLFEKIANWFKS
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
|
Q5HTK3
|
Q8XVV4
|
MNMA_RALSO
|
tRNA-specific 2-thiouridylase MnmA
|
Ralstonia
|
MSGKRVVVGMSGGVDSSVTAWLLKQQGYEVIGLFMKNWEDDDDSEYCSTRQDWIDVVSVADLIGVDVEAVNFAAEYKDRVFADFLREYSAGRTPNPDVLCNAEIKFKAFLDHAMALGADTIATGHYARVREAGGRFELLKAFDHTKDQSYFLHRLNQAQLSRTLFPLGEMPKTRVREIAAEIGLPNARKKDSTGICFIGERPFRDFLNRYLPTKPGPIRTPDGKTIGQHIGLAFYTLGQRKGIGIGGSRDGNGDAWYVARKDMAANTLYVAQGHDHPWLLAHTVHADDLSWVAGHPPAEGTQLAAKTRYRQADAPCAVTRATGDALTLTFQQAQWAVTPGQSAVLYDGDICLGGGIIASTEAASLEQAVA
|
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
|
Q8XVV4
|
B2GBC9
|
UVRC_LIMF3
|
Excinuclease ABC subunit C
|
Limosilactobacillus
|
MASEYLEHKLALLPDQPGCYLMKNANAQIIYVGKAKNLKNRVRSYFKSSHTGKVAAMVEEVADFETIVTSSNKESFLLEITLIQKHQPYYNIKLKRGTGYPYIKITNERDPIIKITGQVKKDGAYYFGPYPNVYAAEETVHFIQKVFPLRRCHGYQGRPCLYYHLGQCLGCCFKEVPEEEYAVQTKRIKSFLNGNTAQVKKQLTARMERAAGQLEFERAAEIRDQLHYIEVTVEKQKIISNDKTPRDLFNFYLDKGWLSIQVFFIRQARLMKREKRLFPVVDTAEEEMTSFILQFYNRRNKLLPKEILLPEGLPNQEIEEILGVPVRTPQRGEKRDLLDMAKENAILSLNEKFRLLEMDRQKTTGAMKEITDELGLPTGHVIEAFDHSHIQGADPVSAMVVFVNGEPAKKLYRKYKLTTVVDHADEAASTREVIFRRYSRLLKEEKPMPDMIMMDGGPIQMEAAKDVLENQLGLNIPVIGMVKNDKHQTADLLYGDDAHHVNLDPRSQGFYLVQRIQDEVHRFAITYHRKVHTKHSLSSRLDEIHGVGPRTRNKLLKAFGSINKIAVAPVEEIRALGINQTTAQLIKVSLQGQAEVKKGSSHD
|
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.
|
B2GBC9
|
Q68XS9
|
NDK_RICTY
|
Nucleoside-2-P kinase
|
typhus group
|
MTIQYTFSMIKPDVIKRNKIGQVNTYLENAGLKIVAQKMKFLTKYEAECFYDEHRARPFFNSLVEYITSGAVVLQVLKGEDAITLNRIIMGATNPAEAKEGTIRKDLGESIEANSIHGSDSENSAKREIKFFFSKSEIIE
|
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
|
Q68XS9
|
B7MIL6
|
HSCA_ECO45
|
Hsc66
|
Escherichia
|
MALLQISEPGLSAAPHQRRLAAGIDLGTTNSLVATVRSGQAETLADHEGRHLLPSVVHYQQQGHSVGYDARTNAALDTANTISSVKRLMGRSLADIQQRYPHLPYQFQASENGLPMIETAAGLLNPVRVSADILKALAARATEALAGELDGVVITVPAYFDDAQRQGTKDAARLAGLHVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSRGVFEVLATGGDSALGGDDFDHLLADYIREQAGIPDRSDNRVQRELLDAAIAAKIALSDADSVTVNVAGWQGEISREQFNELIAPLVKRTLLACRRALKDAGVEADEVLEVVMVGGSTRVPLVRERVGEFFGRPPLTSIDPDKVVAIGAAIQADILVGNKPDSEMLLLDVIPLSLGLETMGGLVEKVIPRNTTIPVARAQDFTTFKDGQTAMSIHVMQGERELVQDCRSLARFALRGIPALPAGGAHIRVTFQVDADGLLSVTAMEKSTGVEASIQVKPSYGLTDSEIASMIKDSMSYAEQDVKARMLAEQKVEAARVLESLHGALAADAALLSAAERQVIDDAAAHLSEVAQGDDVDAIEQAIKNVDKQTQDFAARRMDQSVRRALKGHSVDEV
|
Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU.
|
B7MIL6
|
Q5HPP5
|
MUTS_STAEQ
|
DNA mismatch repair protein MutS
|
Staphylococcus
|
MANITPMMQQYLKIKSEYDDCLLFFRLGDFYEMFFDDAKEASRVLEITLTKRDAKKENPIPMCGVPYHSADNYIETLINKGYKVAICEQMEDPKQTKGMVRREVVRIITPGTVMDQNGMDEKKNNYILSFIENEEFGLCYCDVSTGELKVTHFKDTATLLNEITTINPNEIVIKQALSEELKRQINMITETITVREDISDEDYDMNQLTHQLMHDTTQLLLDYIHHTQKRDLSHIEEVIEYAAVDYMKMDYYAKRNLELTESIRLKSKKGTLLWLMDETKTPMGARRLKQWIDRPLINKQQINDRLNIVEEFMDRFIERDTLRNHLNQVYDIERLVGRVSYGNVNARDLIQLKHSISEIPHIKALLNELGAQTTTQFKELEPLDDLLQILEESLVEEPPISIKDGGLFKNGFNAQLDEYLEASKNGKTWLAELQAKERERTGIKSLKISFNKVFGYFIEITRANLNNFQPEAFGYNRKQTLSNAERFITDELKEKEDIILGAEDKAVELEYELFVKLREHIKTYTERLQKQAKIISELDCLQSFAEIAQKYNYVKPTFSDDKVLHLENSRHPVVERVMDYNDYVPNDCHLDDETFIYLITGPNMSGKSTYMRQVAIISIMAQMGAYVPCDSATLPIFDQIFTRIGAADDLVSGKSTFMVEMLEAQKALTYATENSLIIFDEIGRGTSTYDGLALAQAMIEYVAQTSHAKTLFSTHYHELTSLDQMLKCLKNVHVAANEYQGELIFLHKVKDGAVDDSYGIQVAKLADLPNEVIDRAQVILNAFEQKPSYQLSHENTDNQQTVPSYNDFGRTEEEQSVIETHTSNHNYEQATFDLFDGYNQQSEVECQIRELNLSNMTPLEALIKLNELQSQLK
|
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
|
Q5HPP5
|
Q8X610
|
METAS_ECO57
|
Homoserine transsuccinylase
|
Escherichia
|
MPIRVPDELPAVNFLREENVFVMTTSRASGQEIRPLKVLILNLMPKKIETENQFLRLLSNSPLQVDIQLLRIDSRESRNTPAEHLNNFYCNFEDIQEQNFDGLIVTGAPLGLVEFNDVAYWPQIKQVLEWSKDHVTSTLFVCWAVQAALNILYGIPKQTRTDKLSGVYEHHILHPHALLTRGFDDSFLAPHSRYADFPAALIRDYTDLEILAETEEGDAYLFASKDKRIAFVTGHPEYDAQTLAQEYFRDVEAGLDPEVPYNYFPHNDPQNKPRASWRSHGNLLFTNWLNYYVYQITPYDLRHMNPTLD
|
Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
|
Q8X610
|
Q3MBA3
|
LEU1_TRIV2
|
Alpha-isopropylmalate synthase
|
Trichormus
|
MTTKPERIIIFDTTLRDGEQCPGATLNIDEKLAIAKQLARLGVDIIEAGFAFASPGDFEAVHKIAQTVGTENGPVICSLARARHDDIKAAAEAIKPAAKGRIHTFIATSDIHLQYKLKKTRPEVIAIAEEMVAYAKSFTDDVEFSPEDAGRSDPEFLYQVLERAIAAGATTINIPDTVGYTTPSEFGAIIKGIKENVPNIDQAIISVHGHNDLGLAVANFLEAVKNGARQLECTINGIGERAGNAALEELVMAMHVRRQYFNPFLGRHPDSEEPLTNIDTKQIYKTSRLVSNLTGMLVQPNKAIVGANAFAHESGIHQDGVLKNKLTYEIMDAQLIGLTDNQIVLGKHSGRNAFRTRLKELGFELSETELNKAFVKFKEVADKKKEISDWDLEAIVNDEIQQAPDLFRVELVQVSCGSNARPTATVTLRTPDGEELTDAAIGTGPVDAVYKAINRVVNVPNQLIEFSVQSVTAGIDAIGEVTIRLRYESRVFSGHAANTDIIVASAQAYVNALNRLYASLQTQDKQTEVTA
|
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
|
Q3MBA3
|
Q6NRH7
|
CIPC_XENLA
|
CLOCK-interacting circadian protein
|
Xenopus
|
MEKNQKCATEQERFKARSGHGDGQRAEPRKTQTTTESDKDSGYSDVASECLSSVEQTDTEEGPTTSRWNVALKPSGKTPSQPQSLVVLKNLLVDQGSGPEPNASSWAVHPSIQLLQTSPQIVFFPPTVSSSKPSTCRKDTKYLPILKSYTKIAPHPSHRVSNISLPCARKRGPDERPHNQTKRQCSKGHSGSRKGMDAATLLDTGVQQGPVDQNVKESSVSAKNKELDMQLTTQNINSNEKGSRVASLDTQQNLLSAGQQNKSQRFQNTLDILHRSGLLSIAMKTKELARHNQATQSQLEKLQEQVQLYATAMSSNNPHDWQRLQDSLAEVVKGDTEDLSVREMDL
|
Transcriptional repressor which acts as a negative-feedback regulator of CLOCK-ARNTL/BMAL1 transcriptional activity in the circadian-clock mechanism. The physiogical relevance of these observations is unsure.
|
Q6NRH7
|
Q22038
|
RHO1_CAEEL
|
Ras-like GTP-binding protein rhoA
|
Caenorhabditis
|
MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTKDGIREVFEKATQAALQQKKKKKSKCMIL
|
Required for ventral migration of epidermal cells during ventral enclosure in the embryo and for cell elongation . Also required for ventral migration of P cells during larval development . Involved in asymmetric spindle positioning during anaphase and establishment of cell polarity during embryo development . In adults, involved in regulation of multiple processes including locomotion, pharyngeal pumping, fecundity, ovulation, defecation and body morphology . In body wall muscles, regulates organization of myosin thick filaments downstream of unc-89 . Association with the oxidase bli-3 promotes ROS production and this interaction may be modulated by memo-1, in order to control the oxidative stress response and longevity .
|
Q22038
|
B7H2Y1
|
PQQD_ACIB3
|
Pyrroloquinoline quinone biosynthesis protein D
|
Acinetobacter calcoaceticus/baumannii complex
|
MNKEQFDVNLVPTWRQGYRFQFEPAQNGFVILYPEGMIKLNESAGAIGQYIDGTNNVSAIIAQLKQQFGDIPEIDNDVIDYMLVAQQQHWIDLV
|
Functions as a PqqA binding protein and presents PqqA to PqqE, in the pyrroloquinoline quinone (PQQ) biosynthetic pathway.
|
B7H2Y1
|
Q03VG1
|
RNY_LEUMM
|
Ribonuclease Y
|
Leuconostoc
|
MVVTIISVFFAIVIGLGIGYYVRKSQDAHKVISAEQMATNILEQANNEAKSLKRAAEVDAKDLAQTYRNQVNDSYNDRQKHLQQQEQRLEDRINNLDKKDAALNQRDASLIQKENQVQTRLDDADKKEVLAQKLLTTQQDKLEEIAQLSPDEAKKQILSETKASLTRQRAALIKEAEEEATSEAEKRARNIIVQAIQRSSADSVADVTVSVVNLPSEDMKGRIIGREGRNIRTLESLTGIDLIIDDTPESVVLSGFDPVRREIAKMALDALVADGRINPSRIEEMVEKSRRQMDETIREKGEQAVFELGLRGMHPDLIKMIGRMNYRTSYGQNVLQHSIEVAKLAGMMAAELKMDVALAKRAGLIHDIGKAVDAEVEGSHVELGVRLAEKFNEKPIVINAIASHHGDVAAISPIAELVAAADAISAARPGARSESLENYVQRLKDLEAIANNNQEVHTAYAIQAGREVRVIVEPTKVTDLQAKVLAHDIKSDVEEKLEYPGHIKVTVIRETRAIDYAH
|
Endoribonuclease that initiates mRNA decay.
|
Q03VG1
|
O81787
|
PTF2_ARATH
|
TFIIB-related protein PTF2
|
Arabidopsis
|
MRCKRCNGSNFERDEDTGNSYCGGCGTLREYDNYEAQLGGIRGPQGTYIRVGTIGRGSVLDYKDKKIYEANNLIEETTERLNLGNKTEVIKSMISKLTDGEFGQGEWFPILIGACCYAVVREEGKGVLSMEEVAYEVGCDLHQLGPMIKRVVDHLDLELREFDLVGLFTKTVTNSPRLTDVDRDKKEKIIKQGTFLMNCALKWFLSTGRRPMPLVVAVLAFVVQVNGVKVKIDDLAKDASVSLTTCKTRYKELSEKLVKVAEEVGLPWAKDVTVKNVLKHSGTLFALMEAKSMKKRKQGTGKELVRTDGFCVEDLVMDCLSKESMYCYDDDARQDTMSRYFDVEGERQLSLCNYDDNISENQLSTKYNEFEDRVCGGTLAKRSQGSSQSMWQRRSVFGMVSTENWWKGKSELSKRLLLKDLLEKDVGLEALPPSYIKGCVAVERRREKIKAAKLRINAIQHPSDNVSEGALSLELEHSKKKRKKGSEIDWEDLVIQTLVLHNVNEEEIEKGHYKTLLDLHVFNSGEV
|
Plant-specific TFIIB-related protein that plays important roles in pollen germination and embryogenesis, possibly by regulating gene expression through interaction with TBP2 and the subunits of RNA polymerases. Binds double-stranded DNA in vitro.
|
O81787
|
Q46WM4
|
TATB_CUPPJ
|
Sec-independent protein translocase protein TatB
|
Cupriavidus
|
MIDLGISKLALIGAVALIVIGPERLPRVARTVGALVGRAQRYINDVKAEVSREVELEELRKMRTEFEDAARDVERTIHKEVSEQTQALNEALGGIEPSAESGGGVSDFVPSWHSAHKAHNGRKSWRVKQGARPLWFKRQNNVRVWVQSGAARVKRHRPAAGRARSFFE
|
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.
|
Q46WM4
|
Q6GIV9
|
UPPP_STAAR
|
Undecaprenyl pyrophosphate phosphatase
|
Staphylococcus
|
MFIIELIKGIILGIVEGLTEFAPVSSTGHMILVDDMWLKSSEFLGSQSAFTFKIVIQLGSVFAAAWVFRERFLEILHIGKHKHVEGDNNQQRRSKPRRLNLLHVLVGMVPAGILGLLFDDFIEEHLFSVPTVMIGLFVGAIYMIIADKYSAKVKNPQTVDQISYFQAFVIGISQAVAMWPGFSRSGSTISTGVLMKLNHKAASDFTFIMAVPIMLAASGLSLLKHYQDIQIADIPFYILGFLAAFTVGLIAIKTFLHLINKIKLIPFAIYRIVLVIFIAILYFGFGIGKGI
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
Q6GIV9
|
Q0AMK3
|
RNH2_MARMM
|
Ribonuclease HII
|
Maricaulis
|
MSVTIPQKDNQSLNKAGMGNTVRIAGVDEAGRGPLSGPVVAAAVILDPTRPITGLGDSKALSERRRRELFRLIRANAWVGIGIAEPAEIDRLNILHATMAAMRRAVARLPVRPTLVLVDGNRLPPGLPCPAEAIIKGDAKEACIGAASIIAKTVRDDLMEQAARRFPGYGFEGHKGYPSAAHKAALETSGACPIHRRSYAPVRAALESRFSTNANRCG
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
Q0AMK3
|
P53816
|
PLAT3_HUMAN
|
Renal carcinoma antigen NY-REN-65
|
Homo
|
MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKHDDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDVIIAASVAGMGLAAMSLIGVMFSRNKRQKQ
|
(Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm . May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection . Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome . May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery . The lipid-modifying enzyme activity is required for this process .
|
P53816
|
P09113
|
SOMA_THUTH
|
Growth hormone
|
Thunnus
|
MDRVFLLLSVLSLGVSSQPITDSQRLFSIAVSRVQHLHLLAQRLFSDFESSLQTEEQRQLNKIFLQDFCNSDYIISPIDKHETQRSSVLKLLSISYRLVESWEFPSRSLSGGSAPRNQISPKLSELKTGIHLLIRANQDGDEMFADSSALQLAPYGNYYQSLGADESLRRSYELLACFKKDMHKVETYLTVAKCRLSPEANCTL
|
Growth hormone plays an important role in growth control and is involved in the regulation of several anabolic processes. Implicated as an osmoregulatory substance important for seawater adaptation.
|
P09113
|
B2GB73
|
RSMH_LIMF3
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Limosilactobacillus
|
MAEFNHVTVLLHEAVAGLAIQPAGVYVDATLGGGGHSGEILKQLTSGHLYSFDQDETAIHYNQANLGPAIEEGKLTLMQTNFRNLKQALADQGVTAIDGIVYDLGVSSPQFDDAKRGFSYQHDAPLDMRMNQDQPLSAYQVVNEWSYQELVRILYRYGEEKFAKQIARAIERARQKQPIQTTMELANIVKEAIPAAARRHGGHPAKKSFQAIRIAVNDELGALEDSLEQALALLKVGGRISVITFQSLEDRLVKTMFKEATSLPDLPPGLPVIPADAQPDFKLINKKPVLPTEDELKVNHRAHSAKLRVIERLK
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
B2GB73
|
Q5R678
|
IDH3A_PONAB
|
NAD(+)-specific ICDH subunit alpha
|
Pongo
|
MAGPAWISKVSRLLGAFHNPKQVTRGFTGGVQTVTLIPGDGIGPEISAAVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPSEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAENCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAARIEAACFATIKDGKSLTKDLGGNAKCSDFTEEICRRVKDLD
|
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.
|
Q5R678
|
Q20EW3
|
PSBF_OLTVI
|
PSII reaction center subunit VI
|
Oltmannsiellopsis
|
MANQKTYTYPIFTVRWLAIHALAVPTVFFLGSITAMQFIER
|
This b-type cytochrome is tightly associated with the reaction center 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.
|
Q20EW3
|
Q9CYH5
|
GFOD2_MOUSE
|
Glucose-fructose oxidoreductase domain-containing protein 2
|
Mus
|
MKLLPGVGVFGTGSSARVLVPLLRAEGFTVEALWGKTEEEAKQLAEEMNITFYTSRTDDVLLHQDVDLVCINIPPPLTRQISVKALGIGKNVVCEKAATSMDAFRMVTASRYYPQLMSLVGNVLRFLPAFVRMKQLIAEHYVGAVMICDARIYSGSLLSPSYGWICDELMGGGGLHTMGTYIVDLLTHLTGQKAEKVHGLLKTFVRQNATIRGIRHVTSDDFCFFQMLMGGGVCSTVTLNFNMPGAFVHEVMVVGSAGRLVARGADLYGQKNSAAQEELLVRDSLAVGAGLPEQGPQDVPLLYLKGMVYMVQALRQSFQGQGDRRTWDRTPVSMAASFEDGLYMQSVVDAIKRSSRSGEWETVEMLAEEPDANQNLSETLQRNNL
|
Promotes matrix assembly.
|
Q9CYH5
|
Q9KPB6
|
ACPS_VIBCH
|
4'-phosphopantetheinyl transferase AcpS
|
Vibrio
|
MIVGLGTDIAEIERVEKALARSGENFARRILTDSELEQFHASKQQGRFLAKRFAAKEAASKALGTGIAQGVTFHDFTISHDKLGKPLLILSGQAAELASQLQVENIHLSISDERHYAMATVILERR
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
|
Q9KPB6
|
P30722
|
DNAK_DIALT
|
Heat shock protein 70
|
Diacronema
|
MAKVVGIDLGTTNSVVAVMEGGKPTVITNSEGGTTTPSVVAYAKNGDLLVGQIAKRQAVINSENTFYSVKRFIGRPSKEVSDELRQTPYKIEDSEGKIRLKCPNLNKNFAAEEISAQVLRKLVNDANKYLGEKVEKAVITVPAYFNDSQRQATKDAGKIAGLEVLRIINEPTAASLAYGLDKKDNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTRLGGDDFDEKIVKWLLNEFEKEEKFSLKGDSQALQRLTEAAEKAKIELSSLSQTEINLPFITANENGAKHIEKTLTGEKFESLCSDLFDRCRIPVENALKDAKLKPNQIDEVVLVGGSTRIPAVKKLVKDILGKEPNETVNPDEVVAIGAAIQAGVLSGEVKDILLLDVTPLSLGVETLGGVTTKIIPRNTTVPTKKSEIFSTAVDNQPNVEIHVLQGEREFARDNKSLGTFRLDGILPAPRGIPQIEVTFDIDANGILSVTAQDKGTSKQQSITISGASTLPKEEVEKMVKEAEQNAAADKEKGENIRVKNEADLYCYQAEKQISELPEALVNENQSLIKESKETVEMLKENIKKEDYDKIKENLKKLQEKLMEIGQKAYAKKEPLKDEDSNKAGSQDDFIDADFTESK
|
Acts as a chaperone.
|
P30722
|
Q9H4B0
|
OSGL1_HUMAN
|
tRNA threonylcarbamoyladenosine biosynthesis protein OSGEPL1
|
Homo
|
MLILTKTAGVFFKPSKRKVYEFLRSFNFHPGTLFLHKIVLGIETSCDDTAAAVVDETGNVLGEAIHSQTEVHLKTGGIVPPAAQQLHRENIQRIVQEALSASGVSPSDLSAIATTIKPGLALSLGVGLSFSLQLVGQLKKPFIPIHHMEAHALTIRLTNKVEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLIKHPECSTMSGGKAIEHLAKQGNRFHFDIKPPLHHAKNCDFSFTGLQHVTDKIIMKKEKEEGIEKGQILSSAADIAATVQHTMACHLVKRTHRAILFCKQRDLLPQNNAVLVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRAGLGILHDIEGIRYEPKCPLGVDISKEVGEASIKVPQLKMEI
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance.
|
Q9H4B0
|
P29302
|
PSAD_NICSY
|
Photosystem I 20 kDa subunit
|
Nicotiana
|
MAMATQASLFTPALSAPKSSAPWKQSLASFSPKQLKSTVSAPRPIRAMAEEAATKEAEAPVGFTPPQLDPNTPSPIFGGSTGGLLRKAQVEEFYVITWESPKEQIFEMPTGGAAIMREGANLLKLARKEQCLALGTRLRSKYKINYRFYRVFPNGEVQYLHPKDGVYPEKVNAGRQGVGQNFRSIGKNKSPIEVKFTGKQVYDL
|
PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein.
|
P29302
|
O70591
|
PFD2_MOUSE
|
Prefoldin subunit 2
|
Mus
|
MADSSGRVGKSGGSGAGKGAVSAEQVIAGFNRLRQEQRGLASKAAELEMELNEHSLVIDTLKEVDETRKCYRMVGGVLVERTVKEVLPALEGNKEQIQKIIETLSQQLQAKGKELNEFREKHNIRLMGEDEKPAAKENSEGAGAKASSAGVLVS
|
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
|
O70591
|
P08824
|
RUBA_RICCO
|
CPN-60 alpha
|
Ricinus
|
RTALQSGIDKLADAVGLTLGPRGRNVVLDEFGSPKVVNEGVTIARAIELPDPMENAGAALIREVASKTNDSAGDGTTTASVLAREIIKLGLLSVTSGANPVSIKRGIDKTVQGLIEELEKKARPVKGRDDIKAVASISAGNDELIGTMIADAIDKVGPDGVLSIESSSSFETTVEVEEGMEIDRGYISPQFVTNPEKLICEFENARVLVTDQKITAIKDIIPLLEKTTQLRAPLLIIAEDVTGEALATLVVNKMRGILNVAAIKAPGFGERRKALLQDIAILTGAEFQASDLGLLVENTSVEQLGIARKVTITKDSTTLIADAASKDELQARIAQLKRELAETDSVYDSEKLAERIAKLSGGVAVIKVGAATETELEDRKLRIEDAKNATFAAIEEGIVPGGGAALVHLSTVVPAINGEDKDADERLGADILQKALVAPASLIAQNAGIEGEVVVEKVKAREWEIGYNAMTDKYENLVEAGVIDPAKVTRCALQN
|
This protein binds RuBisCO small and large subunits and is implicated in the assembly of the enzyme oligomer.
|
P08824
|
A8AUL5
|
G6PI_STRGC
|
Phosphohexose isomerase
|
Streptococcus
|
MPHIKFDYSKVLDKFVAPHEVEYMQSQVTAADELIRKGTGAGSDFLGWLDLPENYDREEFDRILKAAEQIKSDSDVLVVIGIGGSYLGAKAAIDFLNHHFANLQTKEERKAPQILYAGNSISSTYLADLVEYVADKDFSVNVISKSGTTTEPAIAFRVFKELLVKKYGQEEANKRIYATTDRQKGAVKVEADANGWETFVVPDDIGGRFSVLTAVGLLPIAASGADIKALMEGANAARKDYTSDKLSENEAYQYAAVRNILYRKGYATEILVNYEPSLQYFSEWWKQLAGESEGKDQKGIYPTSANFSTDLHSLGQFIQEGTRIMFETVVRVDKPRKNVIIPTLEEDLDGLGYLQGKDVDFVNKKATDGVLLAHTDGDVPNMYVTLPEQDAFTLGYTIYFFELAIALSGYLNAINPFDQPGVEAYKRNMFALLGKPGFEELSKELNARL
|
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
|
A8AUL5
|
Q2NU30
|
LPOB_SODGM
|
Penicillin-binding protein activator LpoB
|
Sodalis
|
MKKRALIVLAALVLASCTSRKPASPPAPIEPVPPPVTVSVQPPPPATSEPVPMPPKIKTIDWQASLSPLVQQMLAVEGINDGSVLLVNTMKNTTNGSVQTGKATAALTRLITDAGGKFQVVGANQLNAARQMLGLSADDSLESRSKAVGLARYLNAQYVLYSAAAGDVKQPTLDLQLMLVQTGEIIWSGNGVAQD
|
Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b).
|
Q2NU30
|
B2V1V3
|
RNPA_CLOBA
|
Protein C5
|
Clostridium
|
MIYRLKKNIEFIIVYRRGKSFANKTLVLYVLKNKRNKDKDGIAYSKVGISVSKKVGNSVVRSKCKRLLSESFRLNYNNILKGYDCVFVARNPMRDSDYFETEKAMKNLIKKAGLYYDEENGIKSN
|
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
|
B2V1V3
|
F4IHY7
|
PTA12_ARATH
|
Protein HEMERA
|
Arabidopsis
|
MASISTTTWLYRGQVCTDSGKSSNCIVQRRVKCGFPLKTLHAGITSRDRSLRHCIKCKKEDGDGDVSEGSKKSEEGFEYVTVERHPYHSYMDSTSGKLEPASGARASIPGEDYWPEGTSSRVRAARAPQPAGESSSFPSYGKNPGSRRKKNRKATEENVTVETNDEVSDSEDSSEEEENDSSDGFVTYKNEFEREEEETGFELDKKLGRPHPFIDPTKKKQIEKTLTSDESWWNWRKPEKEQWSRWQRRRPDVETVFLKAMAETGQVKLYGEEPTLTETSLYRARRHLFKEERLQAERERLAKEGPMAFYSEWVKAWKRDTSREAVQKHFEETGEDENTQLIEMFSHQTDREYRIMMGTDIRIKRDPLAMRMREDQIKQIWGGDPVYPTINYIQDPNAVMDFRGPDFHEPTPNMLSYLKENGKVISREMHEALLTKEKTEQLEVPDMDDAMAQAVDIGENDDDEDDADVEKDDEKVPRNWSVLKETPELRTAKPKPKKEGRMSLDEAVDDAENLTDFLMDFEEETDP
|
Involved in plastid gene expression . Required in the nucleus for the initiation of photomorphogenesis mediated by phytochromes (PHYs) (e.g. PHYA and PHYB) by mediating PHYs localization to photobodies, especially in response to red and far-red light, and implicating phytochrome nuclear bodies as sites of proteolysis for PHYs and PIFs proteins (e.g. PIF1 and PIF3). Acts downstream of PHYs and upstream of DET1 .
|
F4IHY7
|
P45738
|
RBL_HELAN
|
Ribulose bisphosphate carboxylase large chain
|
Helianthus
|
MSPQTETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYGLEPVPGEDNQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYVKTFDGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGNCEDMMKRAVFARELGVPIVMHDYLTGGFTANTSLSQYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHSGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLATEGNEIIREATKWSPELAAACEVWKEIKFEFQAMDTLDTDKDKDKKR
|
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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
|
P45738
|
Q57M77
|
UBIG_SALCH
|
3-demethylubiquinone 3-O-methyltransferase
|
Salmonella
|
MNTEKPSVAHNVDHNEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYITERSGGLFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALESGIEVEYMQETVEEHAAKHAQQYDVVTCMEMLEHVPDPQSVVHACAQLVKPGGEVFFSTLNRNGKSWLMAVVGAEYILRMVPKGTHDVKKFIKPAELLSWVDETVLKEQHITGLHYNPITNTFKLGPGVDVNYMLHTRAKKA
|
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
|
Q57M77
|
F1QMB9
|
CCNK_DANRE
|
Cyclin-K
|
Danio
|
MKDGKENSNATFGSFTTNLDHTKPCWYWDKKDLAHTPSQSDLDPATEARYRREGARFIFDVGTRLGLHYDTLATGITYFHRFYMFHSFKQFPRYVTGACCLFLAGKVEETPKKCKDIIKTARSLLNDVQFAQFGDDPKEEVMVLERILLQTIKFDLQVEHPYQFLLRYAKQLKGDKNKVQKLVQMAWTFVNDSLCTMLSLQWEPEIIAVAVMYLAGRLCKFDIQEWTSKQSSRRWWEQFVQDVPVELLEDICHQILDLYSQGKQPIPQQPPMQDKEKPPPPPAAPPGQSGAQNPPAQPPSKKNSPQASPPAKIKRQHVSPKDEPKAPAEQVGSKIPRLESPMPPLPVSQPPERKTPSAIPAPPAEAEPAAASELDPAQGPAPPLPHGAPPPLPHRPPPTEFGGPCSDFLSSVKHKRRYLDDDRNL
|
Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A).
|
F1QMB9
|
Q8G5Q9
|
CLPP2_BIFLO
|
Endopeptidase Clp 2
|
Bifidobacterium
|
MSNTFATLPVMAGDDVPAGPVDPIFNRLLKDRIIWMGEEVKDDMANRICAQLLMLAAEDPKKDIWLYINSPGGSITAGMAIYDTMQLIEPDVATVGLGMCASMGQFLLSSGTKGKRYLTSHARVLMHQPSGGIGGTATDVRINAELIMDMKKTMSELTAEQTGHTLEEIYRDNEYDHWFTAQEALDYGFVDKLVTTPDTIGNNQQGE
|
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
|
Q8G5Q9
|
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