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
|
---|---|---|---|---|---|---|
P02651
|
APOA4_RAT
|
Apolipoprotein A4
|
Rattus
|
MFLKAVVLTVALVAITGTQAEVTSDQVANVMWDYFTQLSNNAKEAVEQLQKTDVTQQLNTLFQDKLGNINTYADDLQNKLVPFAVQLSGHLTKETERVREEIQKELEDLRANMMPHANKVSQMFGDNVQKLQEHLRPYATDLQAQINAQTQDMKRQLTPYIQRMQTTIQDNVENLQSSMVPFANELKEKFNQNMEGLKGQLTPRANELKATIDQNLEDLRSRLAPLAEGVQEKLNHQMEGLAFQMKKNAEELQTKVSTNIDQLQKNLAPLVEDVQSKLKGNTEGLQKSLEDLNKQLDQQVEVFRRAVEPLGDKFNMALVQQMEKFRQQLGSDSGDVESHLSFLEKNLREKVSSFMSTLQKKGSPDQPLALPLPEQVQEQVQEQVQPKPLES
|
May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.
|
P02651
|
A8G797
|
PEBB_PROM2
|
Phycoerythrobilin:ferredoxin oxidoreductase
|
Prochlorococcus
|
MLIKDTIFYRPDWRWHIFLKYLTNNLSKYNCLEKIIPSEYSYKDSTYGSKKSKKNVNLCTWGVTHKKRIQFARAVCINSPKYSVLNFLIIPNTIYNVPFFGVDFVSLPNIYLLVLDFQPSLKIQNQYNNQLLEKLIKLKNHCHSSLPLAEEMSVDVARFFSPGAIWSKLPKEERSDFLIANQLYTSFKEYLDLYLEILFESKEVNIDLQKELINGQNNYLNYRRDNDPARPMLSSLFGKEFTESLIKEVLFTT
|
Catalyzes the two-electron reduction of the C2 and C3(1) diene system of 15,16-dihydrobiliverdin.
|
A8G797
|
Q02QU5
|
MNMC_PSEAB
|
FAD-dependent cmnm(5)s(2)U34 oxidoreductase
|
Pseudomonas
|
MSDFQHAQLDWDENGQPLSRAFGDVYFSRHSGLNETRHVFLATNRLAERFAALGDGEVLCIGETGFGTGLNFLCAWQLFEQVAPAGARLEFVSVEKFPLAAADLRRALALWPELAPWSEALLGQYLAVHPGFQRLAFAGGRIGLTLLLGDALECLPQLDARVDAWFLDGFAPAKNPDMWSPALFAELARLSAPQATLGTFTSAGFVRRGLIEAGFAMQRVPGYGQKREMLGGTYQGPPANAGKPWYARPAPHAGRRAALVVGGGLAGCASAASLAARGWQVTLIERHPGLAREASGNPQGVLYLKLSAHGTPLSRLVLSGFGHTRRLLERLRRGHDWDACGVLQLAFDAKEAQRQAQLAAAFPADLLHGLDREQAERLAGVALPAGGLFYPEAGWVHPPALCQALAATPGITLLSGRAVRLRREGDDWCAYAGDECLARAPLAILATAADIRDFPPAAELPLKRIRGQVTRLPATPQSRALRTVVCAEGYVAPPRGDEHTLGASFDFKSEDLAPTLAEHQGNLELLREISPDLLQRLGADDLPLERLEGRAAFRCTSPDYLPLVGPLAERAAFDEAYAVLARDARQVPERACPWLPGLYLNSGHGSRGLISAPLSGELLAAWICGEPLPLPRAVAEACHPNRFLLRDLVRGQRG
|
Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
|
Q02QU5
|
P13678
|
KPC3_DROME
|
dPKC98F
|
Sophophora
|
MFTGKLQIKVCEASGLRPTDFQKRHNLTFGKLADEQLIDPYVSIDVDESHFDRATTRPKTFDPVWNEQFVHDVTNVSNINLTVFHDAALPPDDFVANCIISFEDLMQSETAVQDLWVNLEPQGKIHVIIELKNRTDKAKAEAVVEHTVAVNKEFKERAGFNRRRGAMRRRVHQVNGHKFMATFLRQPTFCSHCREFIWGIGKQGYQCQVCTLVVHKKCHLSVVSKCPGMRDEQPAKVEMVPAGQRFNVNLPHRFVVHSYKRFTFCDHCGSLLYGLIKQGLQCETCGMNVHKRCQKNVANTCGINTKQMAEILSSLGISPDKQQPRRSKYLNQQGGEDNYGASLGADGDGAPGQSFRSCALSVDSLATSTTTMTSGYNSSSCMSLAVTGSGGVGATGETRPGKCSLLDFNFIKVLGKGSFGKVMLAEKKGTDEIYAIKVLKKDAIIQDDDVDCTMTEKRILALAANHPFLTALHSCFQTPDRLFFVMEYVNGGDLMFQIQKARRFEASRAAFYAAEVTLALQFLHTHGVIYRDLKLDNILLDQEGHCKLADFGMCKEGIMNGMLTTTFCGTPDYIAPEILKEQEYGASVDWWALGVLMYEMMAGQPPFEADNEDELFDSIMHDDVLYPVWLSREAVSILKGFLTKNPEQRLGCTGDENEIRKHPFFAKLDWKELEKRNIKPPFRPKMKNPRDANNFDAEFTKEDPVLTPIGNEVVRCINQDEFAGFSFVNPKFGPERKVY
|
PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters.
|
P13678
|
Q1RJJ2
|
YIDD_RICBR
|
Putative membrane protein insertion efficiency factor
|
belli group
|
MTRILLLLLTFYRYFISPLLGGNNCRFYPTCSKYAKEALNTHGGIKGLWLIFKRIIKCQPLCDGGYDPVPLTK
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
Q1RJJ2
|
P12626
|
ANFA_AZOVI
|
Nitrogen fixation protein AnfA
|
Azotobacter
|
MSDQATFEFDTDYFVEEFSHCFTGECRVKMLPILYKISQIITGNADLADALSIVLGVMQQHLKMQRGIVTLYDMRAETIFIHDSFGLTEEEKKRGIYAVGEGITGKVVETGKAIVARRLQEHPDFLGRTRVSRNGKAKAAFFCVPIMRAQKVLGTIAAERVYMNPRLLKQDVELLTMIATMIAPLVELYLIENIERVRLENENRRLKHALKERFKPSNIIGNSKPMQEVYELIHKVASTKATVLILGESGVGKELVANAIHYNSPNAEAALVTSNCAPLPENLAESELFGHEKGSFTGALTMHKGCFEQADGGTIFLDEVGELSPTVQAKLVRVLQNRTFERVGGSKPVKVDVRIIAATNRNLVEMVEQGTFREDLYYRLNVFPITVPPLRERGSDVIALADHFVSAFSRENGKNVKRISTPALNMLMSYHWPGNVRELENVMERAVILSDDDVIHSYNLPPSLQTSKESGTAFGLTLEEKIKAVECEMIVEALKNSSGHIGEAAKELGLARRMLGVRMERYGISYKSFSRYA
|
AnfA is essential for nitrogen fixation under Mo- and V-deficient conditions. It is required for the regulation of nitrogenase 3 transcription. Interacts with sigma-54.
|
P12626
|
Q8ZPZ4
|
MNMA_SALTY
|
tRNA-specific 2-thiouridylase MnmA
|
Salmonella
|
MSESPKKVIVGMSGGVDSSVSAWLLQQQGYQVEGLFMKNWEEDDGEEYCTAAADLADAQAVCDKLGIELHTVNFAAEYWDNVFELFLEEYKAGRTPNPDILCNKEIKFKAFLEFAAEDLGADYIATGHYVRRADVNGKSRLLRGLDGNKDQSYFLYTLGHEQIAQSLFPVGELEKPQVRKIAEDLGLVTAKKKDSTGICFIGERKFRDFLGRYLPAQPGKIITVDGDEIGEHQGLMYHTLGQRKGLGIGGTKDGSEDPWYVVDKDVENNVLIVAQGHEHPRLMSVGLIAQQLHWVDREPFTGTLRCTVKTRYRQTDIPCTINALNDDRIEVIFDEPVAAVTPGQSAVFYSGEVCLGGGIIEQRLPLTV
|
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs.
|
Q8ZPZ4
|
B9E9J2
|
RL4_MACCJ
|
50S ribosomal protein L4
|
Macrococcus
|
MANYDVLKVDGTKAGSIELNDNVFGIEPNQHVLFEAINLQRASMRQGTHAVKNRSAVSGGGRKPWKQKGTGRARQGTIRAPQWRGGGIVFGPTPRSYSYKMPKKMRRLALRSALSAKVQENAFTVLESLTFDAPKTKEFKNMTTTLELPKKVLFVVEAEDVNVALSARNIPGVTVITTTGLNVLDIVHANQVVMTKGAVEKVEEVLG
|
Forms part of the polypeptide exit tunnel.
|
B9E9J2
|
Q93YV6
|
2A5K_ARATH
|
Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' kappa isoform
|
Arabidopsis
|
MFKQFLSKLPRKSSKSDSGELNRSSSGPVSSPVQRSGTSGGGSGPVRSNSGKRMSSAVFPASVVAGIEPLVPFKDVPSSEKLNLFVSKVSLCCVTFDFSDPGKNSIEKDVKRQTLLELLDFVASGSVKFTEPAILAMCRMCAVNLFRVFPPNYRSSSGGENDDDEPMFDPAWPHLQIVYDLLLKFITSPCLDAKVAKKYLDHAFIVRLLDLFDSEDPRERECLKTILHRVYGKFMVHRPFVRKSMSNIFYRFVFETEKHSGIAELLEIFGSIVSGFALPLKEEHKIFLWRVLIPLHKPKSVGNYFQQLSYCITQFIDKEPKLGSVVIKGLLKFWPITNSQKEVMFLGEVEEIVEAMSVMEFQKIMVPLFLRIACCVTSSHFQVSERALFLWNNDQIVNLIGHNRQAILPIMFTALEKNAQNHWNQSVLNLTLNVRKMFCEMDEALFMSCHARFKEDEAKQCSAAEKRKEVWARLENAASMKPITGKTAVLVTPRATSIAC
|
The B regulatory subunit may modulate substrate selectivity and catalytic activity, and may also direct the localization of the catalytic enzyme to a particular subcellular compartment.
|
Q93YV6
|
Q5L5H5
|
IF1_CHLAB
|
Translation initiation factor IF-1
|
Chlamydia
|
MAKKEDTIVLEGRVKELLPGMHFKILLENGMPVTAHLCGKMRMSNIRLLVGDRVTVEMSAYDLTKARVVYRHR
|
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
|
Q5L5H5
|
C6DYJ5
|
SYT_GEOSM
|
Threonyl-tRNA synthetase
|
unclassified Geobacter
|
MNEINVTLPDGSQRPLPAGASIFDLAASIGAGLAKAAIAGKIDGNLVDLNTPLADGARVEIVTEKSPEALEIIRHSTSHLMAQAVKALFPQAKVTIGPAIETGFYYDFDVDHPFTPEDLEKIEEKMRELAKADLKIERRELTSADAIALFKGMGEDYKVELIEDLGADKVSLYSQGDFVDLCRGPHLPKTSYIKAFKLTSIAGAYWRGDEKRAMLQRVYGTAFGDKKELEAYLARIEEAKKRDHRKLGRELDLFSFNDEVGAGLVIWHPKGAMLRTILEDFERKEHLKRGYDIVLGPQILKTELWQRSGHYENYRENMYFTTVDEQSYGVKPMNCLAHMMIYRSQLRSYRDLPLRYFELGTVHRHERAGVLHGLLRVRGFTQDDAHILCTPDQLDAEIKGVIQFVTEVMGIFGFEFEMELSTRPEKSIGSDDAWELATSALLNALKDSGRPYEINEGDGAFYGPKIDIKLRDALDRRWQCATIQCDFTLPERFDLTYVDADGEKKRPVMVHRVILGAIERFIGVLIEHFAGNFPTWLAPVQATIVTVTDNQIPYAQAAFDKLRAAGIRVQKDFRNEKLGFKIREAQLQKIPYMLVVGDKEVESGMLAPRFRDGKNLESMTPEQFITFIENEVKSYK
|
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
|
C6DYJ5
|
B8J9V9
|
RRF_ANAD2
|
Ribosome-releasing factor
|
Anaeromyxobacter
|
MGTIADDILDDLHGRILKTLDQLRTELAAVRTGRASLHLLDNVRVDYYGTPTPLNQVATLSVPEARLIVVKPWEKSMIPPIEKAIRDGNLGLNPMSDKDLVRVPIPALTEERRKEIVKQVKHKGEEHKIAVRNVRREAKELIEVAEKDGDISGDDAEKALEKMQKETDDGVKKIDEIVAAKEKDVLQV
|
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
|
B8J9V9
|
Q2RI73
|
AROC_MOOTA
|
5-enolpyruvylshikimate-3-phosphate phospholyase
|
Moorella
|
MLRYLTAGESHGRGLSVIVEGLPAGVPLTDGDINTWLTRRQGGYGRGGRMAIERDQAEILAGVRGGLTLGSPIALFIANRDWENWQEIMAPGPEARAARVVTRPRPGHADLAGGLKYHQADLRNILERASARETAARVAAGAVAAVLLKELAIELAFHVVRIGPVEVREQVDWEAACRAVESPVYCADPEAGRAMVAAIEEARQQGDTLGGVVEVLARGVPAGLGSHVHWDRRLDGRLAQALMSIPAIKGVEIGAGFRVAALPGSRAHDAIAYRKGQGFYHPTNRAGGLEGGLTNGETLVLRAAMKPIPTLMHPLPSVDLVTKQPATASIERSDVCAVPAAAVVAAAAVAWVLAGAILEQFGGDYLPVIQERLAAYRQYLQEI
|
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
|
Q2RI73
|
O22456
|
SEP3_ARATH
|
Agamous-like MADS-box protein AGL9
|
Arabidopsis
|
MGRGRVELKRIENKINRQVTFAKRRNGLLKKAYELSVLCDAEVALIIFSNRGKLYEFCSSSSMLRTLERYQKCNYGAPEPNVPSREALAVELSSQQEYLKLKERYDALQRTQRNLLGEDLGPLSTKELESLERQLDSSLKQIRALRTQFMLDQLNDLQSKERMLTETNKTLRLRLADGYQMPLQLNPNQEEVDHYGRHHHQQQQHSQAFFQPLECEPILQIGYQGQQDGMGAGPSVNNYMLGWLPYDTNSI
|
Probable transcription factor active in inflorescence development and floral organogenesis. Functions with SEPALLATA1/AGL2 and SEPALLATA2/AGL4 to ensure proper development of petals, stamens and carpels and to prevent the indeterminate growth of the flower meristem. Interacts with APETALA1, AGAMOUS or APETALA3/PISTILLATA to form complexes, that could be involved in genes regulation during floral meristem development . Binds specifically to the CArG box DNA sequence 5'-CC (A/T)6 GG-3' .
|
O22456
|
Q6DW73
|
DGDG2_LOTJA
|
Digalactosyldiacylglycerol synthase 2, chloroplastic
|
Lotus
|
MGKKQHIAIFTTASLPWLTGTAVNPLFRAAYLSKDGERDVTLVIPWLSLKDQALVYPNNITFASPSEHEKYIRQWLEERVGFTSGFSIKFYPGKFSRDKRSILAVGDISEVIPDKEADIAVLEEPEHLTWFHHGKRWKTKFRLVIGIIHTNYLEYVKREKNGQMQAFLLKYLNNWVVGIYCHKVIRLSAATQDYSGSIVCNVHGVNPKFLEIGKKKREQQQNGDQAFTKGAYFIGKMVWSKGYKELLHLFKNHQKELSALEVDLFGSGEDSDEVQKAAKKLEMAVRVHPARDHADALFHDYKLFLNPSTTDVVCTTTAEALAMGKIVVCANHCSNEFFKQFPNCWTFDESKGFVQLILKALAEEPAQLTDAQRHDLSWEAATERFLKAAELDKPFEKKLSRSTSIYMSTSLNLQQTVDDASAYVHHVASGFEISRRMFGAIPGSLKPDEELSKELGLSDSGRK
|
Involved in the synthesis of diacylglycerol galactolipids that are specifically found in thylakoid membranes. Specific for alpha-glycosidic linkages.
|
Q6DW73
|
Q49588
|
PSTB_MYCIT
|
Phosphate-transporting ATPase
|
Mycobacterium avium complex (MAC)
|
MRREQQLPAAVAAPVADGGQLMRAVDLTLGFGPKTVLEQVSLDFPARSVTTLLGPTGSGKTTFLRTLNRMNDKVSGFRHSGDVLLGGRTIFADRDLMEFRRSVGMLFQRPNPFPMSIMDNVVAGVRAHKMAPRKQFKTVAEARLTEVGLWDAVKDRLGDSPFRLSGGQQQLLCLARALAVNPDVLLLDEPTSSLDPTTTEKIEGLIRSLADRLTVIMVTHDLAQAARTGDRTAFFFEGRLVEEGPTKHLFLSPQHEETVRYFAPFRPAQGSDRGSSQTAGVAESQ
|
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
|
Q49588
|
F4HU58
|
TAD1_ARATH
|
tRNA-specific adenosine-37 deaminase TAD1
|
Arabidopsis
|
MEEDWGKTVSEKVISAYMSLPKKGKPQGREVTVLSAFLVSSPSQDPKVIALGTGTKCVSGSLLSPRGDIVNDSHAEVVARRALIRFFYSEIQRMQLTSGKSNEAKRQRIDSETSSILESADSSCPGEVKYKLKSGCLLHLYISQLPCGYASTSSPLYALKKIPSTQVDDSLLVQASDICSSRHSDVPEIGSNSNKGNGSQVADMVQRKPGRGETTLSVSCSDKIARWNVLGVQGALLYQVLQPVYISTITVGQSLHSPDNFSLADHLRRSLYERILPLSDELLTSFRLNKPLFFVAPVPPSEFQHSETAQATLTCGYSLCWNYSGLHEVILGTTGRKQGTSAKGALYPSTQSSICKQRLLELFLKETHGHKRESSKSKKSYRELKNKATEYYLMSKIFKGKYPFNNWLRKPLNCEDFLIN
|
Involved in RNA editing. Catalyzes the specific deamination of adenosine-37 in the cytosolic tRNA-Ala. Generates inosine at the position 3'-adjacent to the anticodon tRNA-Ala.
|
F4HU58
|
Q02953
|
HSF_SCHPO
|
Heat shock transcription factor
|
Schizosaccharomyces
|
MIQTASTISSNGGTNQGMESSSANSPEMNGTQNSMSVGMSGSGSSQNRKITQFSNKLYNMVNDSSTDSLIRWSDRGDSFLVIGHEDFAKLVLPRYFKHNNFSSFVRQLNMYGFHKVPHIQQGVLQSDSPNELLEFANPNFQRDQPELLCLVTRKKAGSQPVEESNTSLDMSTISSELQNIRIQQMNLSNELSRIQVDNAALWQENMENRERQRRHQETIDKILRFLASVYLDGKQKPPSKVMPKSRRLLLEAKYPTVSPTNEPSAHSRPSPQGTTANSSSASISSLHNTTPDGEGKYRSVQNGRALNYVSSFNSDSHSPKDYISQSYTNEPGLKKESADSFNNSIDSYISPNQSPNTDVPSLNRDDTTDPKVVNTGDIINMLDDANSIEGSNMNSLSPLLFDYPNSLYPVNNTSSEQHHNSYRGSVSNSQPSGNLSESTNLQPVQPVDYMSNSNPSYGSYNAEDQLTNFHPGYAMDQKRISKLSDGITKQDQNIQALADILGIPLGDGKIDDAGFSANSPTNLNLPVSSDLDSVLNIPPNEDVFPDSNPVFDEFTNISNLTSPIEASNGNTFGSNPVSLPNQQKSVNPSLMTVSSPRQVRKKRKSSIGA
|
DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. Also required for growth at normal temperatures.
|
Q02953
|
P10176
|
COX8A_HUMAN
|
Cytochrome c oxidase subunit 8-2
|
Homo
|
MSVLTPLLLRGLTGSARRLPVPRAKIHSLPPEGKLGIMELAVGLTSCFVTFLLPAGWILSHLETYRRPE
|
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
|
P10176
|
C6A5J6
|
NADK_THESM
|
ATP-dependent NAD kinase
|
Thermococcus
|
MKFGIVARRDREEALKLAYRVYDFLKVNNYEVYVDEEAYIHFPHFSSEDVLSLKKMDVDMIIAIGGDGTVLRVEHNTSKDIPILAVNMGTLGFLAEIEPAETFFAISRILEGDYFIDERMKIRVFVEDVSIPDALNDVVILTSIPGKVTHLKYYVDGELAEDIRADGLIISTPTGSTAYALSAGGPLVDPRLHAILLVPLAPVALTARPLVVPDCSSIEIEVLTEREIVLTVDGQFYTQLPSNLKIRVEKSPRKTKFVRFSERIYPKYTLKIKKKF
|
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
|
C6A5J6
|
O74499
|
LSM7_SCHPO
|
U6 snRNA-associated Sm-like protein LSm7
|
Schizosaccharomyces
|
MSSLQKRPGPGNSSQPTERPRKESILDLSRYQDQRIQATFTGGRQITGILKGFDQLMNLVLDDVEEQLRNPEDGKLTGAIRKLGLVVVRGTTLVLIAPMDGSEEIPNPFVQAE
|
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Probable component of the spliceosome.
|
O74499
|
A2QLJ9
|
ATG9_ASPNC
|
Autophagy-related protein 9
|
Aspergillus subgen. Circumdati
|
MMTSNILSRFLPPNGSPSVYETIRQHDNHSDASDVEERAGMAFEDEHGDRFSDRELEDALADAGRDDSPGPSEPFLPRSPPTKRDEGGFLKAGSRRRKFSRSGRIHAASPRHKFDDSDDDVPPSLLVEGDQDDDDVLRSKLPPPPRSIDPPNVEPPPRPSPRDDRVHWEAARDRLPLHDTNRRAHHASLWSAGYPNLALVDPKEKALWMWANVENLDNFLKEVYTYFLGNGIWSILLNRVLSLLTFAFVVGFSIFLTNCIDYHKVRGSRTLDDILIQKCTKQMSMSATFLLWLLSFFWIGKAFQYLLDIRRLKHMHDFYHYLLGISDAEIQSISWQEVVSRLMTLRDSNPATAGAVSAKHRKFMGSQSKQRMDAHDIANRLMRKENYLIALINKDILDLTLPIPFLRNRQLFSRTLEWNINLCIMDYVFNEQGQVRTLFLKDTHRRALSEGLRRRFMFAGIMNIFVAPFIVVYFMMHYFFRYFNEYKKNPSQIGSRQYTPLAEWKFREFNELWHLFERRVNMSYPFASRYVDQFPKDKMVQFAGFVAFVSGALASVLALASVVDPELFLGFEITHDRTVLFYLGVFGSIWAVAQGLVPEETNVFDPEYALLEVINFTHYFPGHWKGRLHSDDVRKDFAVLYQMKIVIFLEEILSMIFTPFILWFSLPKCSDRLIDFFREFTVHVDGMGYLCSFAVFDFKKGTNVISQGDTGRRDAARQDLRADYFSTKDGKMLASYYGFLDNYGANPRSGHPSTKRQFHPPPTFPTLGSPSAIEMGNFGDRPAAAGLMGQQSTYGAAPRFGPAGMGDHLSPAPSMLLDPHHQPSASGFRSTHRANPYPRYRASRPPPTISDPIEDEDPPAGKGRSAVKSSPGVGSSGGGIGTSDSNLGESWRMNLVGDEVEEEDEGGENVDTLAGGGGVLGLIQQFQKVNQDNRGRTTVGI
|
Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through atg2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking.
|
A2QLJ9
|
Q10271
|
ARB2_SCHPO
|
Argonaute-binding protein 2
|
Schizosaccharomyces
|
MFRKKKSRVLQRDVNFGNCLEDMNLQITNDFYLRKLNAPNELYEFQVTKDKEYNEKFYFAVLDHVYSWTLQNSLLTRISIPLESSPSEPHSWIYATRNWQTNENGIVIIIQSMSHPLIWSNRNLREGDVRRATVLDVIAKCTEKKLSVVIFSPSALLWDQSINFPRTTRYFTSQGLQITKKSIIKDVETPESYVSIGLNYVMSNSVSTKIHFVGSEYGSYLLNSYLDLNWKKFSGKAGAILLIMNMSINEELHDPDYVSYLIEHARNYLPSHEPCRHLMNSIMTESGIPNFSAGKYIDEFYDYIGDVLLEMIALDTNTSKS
|
A member of the argonaute siRNA chaperone (ARC) complex which is required for histone H3K9 methylation, heterochromatin assembly and siRNA generation. The ARC complex contains mostly double-stranded siRNA. Inhibits the release of the siRNA passenger strand from ago1 together with arb1.
|
Q10271
|
B0BZK7
|
ATP61_ACAM1
|
F-ATPase subunit 6 1
|
Acaryochloris
|
MPLASLEVGQHLYWQIGGLKVHGQVLITSWIVIGILVIVSVLATRKVERIPSGLQNFMEYALEFVRDLTKNQIGEKEYRPWVPFIGTLFLFIFVSNWSGALFPWKLISLPEGELAAPTNDINTTVALALCTSFVYFYAGFRKKGLGYFRKYIEPTPVLLPIAILEDFTKPLSLSFRLFGNILADELVVAVLVLLVPLIVPLPVMLLGLFTSGIQALVFATLAGAYIHESLEGHGEEEEAH
|
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
|
B0BZK7
|
B3EGP4
|
RECA_CHLL2
|
Recombinase A
|
Chlorobium
|
MNMDTNDKEKKNEGIDPAKLKQLNLAVDALEKQFGKGAIMRLGDGSAVMQVQSISTGSMTLDFALGVGGLPRGRVAEIYGPESSGKTTLALHVIAEAQKEGGIAAIVDAEHAFDPSYARKLGVDINALLISQPESGEQALTIVETLVRSGAVDVVVVDSVAALVPQAELEGEMGDSVVGLQARLMSQALRKLTGAISKSSAVCIFINQLRDKIGVMYGSPETTTGGKALKFYASIRLDIRKIAQIKDGDEIVGNRTKVKVVKNKVAPPFKSAEFDILYGEGISAMGELVDLAVEFGVVKKSGSWFSFGQEKLGQGRESAKKALREDHALFQQVYIQVRELMTGTAEIING
|
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
|
B3EGP4
|
B9KJ95
|
LIPB_ANAMF
|
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
|
Anaplasma
|
MSLLGFPVEWRVSDGMVDYKAALDFMTSRVDGILEGRESEMVWLLEHPSVYTAGVSAKDGELLSENKFQVVRTTRGGKYSYHGPGQRVVYVMLHLGRRDKRDVRLYVRNLGLWVVGTLAEFGIDSHFDDDNTGVWVQYSRQAKKIAAFGIAIRRWVTYHGFSVNISTDLGCYSGIVPCGIAGSHVTSLQDLGVTVPFEEFDAVLQQKFDTIFLQ
|
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.
|
B9KJ95
|
Q60CS4
|
RSMG_METCA
|
16S rRNA 7-methylguanosine methyltransferase
|
Methylococcus
|
MLERGLSELGSDAGGDQRERLLRFLELLRKWNRVYSLTAIEDPCEGVRLHLLDSLSIASFLHGRRVLDVGTGPGLPGIPLAIVQPERRFVLLDCNAKKIRFVRQAVIELGLANVVPVQARIESFTDAEGFDCVLARAYASLAEIWTDAAPLLRTGGTVLALKGRRPEAELGDLPAGVAVGIHRLRVPGVEAERHLAELKPTGQDS
|
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
|
Q60CS4
|
O74974
|
UTP25_SCHPO
|
U three protein 25
|
Schizosaccharomyces
|
MAIESDLDGASMDELAGKSYEALLYLMNKNKKRKPEKKDDKEKSSKKVQKKNKVIESLNEMEVEMEDENENENDEQEAIQYYINVESQDADETLHQEAQDSSEDPFHQHFDYDDSEVIKNSIAAYDEGKLCKSIEESKLGVSQSFFPDVTKRLPCSCLSEIKNIDDLGLKQRILDSYKKQKPSGQLTSMQIELAKAMFNYQDVFFTNMSMKSHKLGTSLLALHALNHVFKTRDRVLKNSARISQNPELEFRDQGYTRPKVLILLPTRNSAFEFINLLISYSGTNQVENRKRFDNEFSIEKEVISEKKPEDFRYLFSGNTDDMFRLGVKFTRKTVKLFSQFYNSDIIVASPLGLRLAIGNKGDKKRDLDYLSSIEIAMVDQAHALVMQNWEHIECIFDELNGLPKEAHGCDFSRVRPWYLDQQARYMRQTILFSQYNNLDINSFFSHYMSNIAGKVKFRSLLHGVLNRLGYKVTQTFVRISVDSIIKVPDARFSYFTGSILVQLKKYSQSGILVYIPSYFDFVRVRNYMDEEGINYSAISEYSSVSDMTRARNLFYQGRTNIMLYTERAHHFRRFDFRGVKAVVMYGPPTNPQFYVELVRMPMRTISEGNLDSDAAKCRIMYTKFDSICLEGIVGYQRVSNMCHGKHEVFEFL
|
DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2.
|
O74974
|
Q65JA8
|
HFQ_BACLD
|
RNA-binding protein Hfq
|
Bacillus
|
MKSINIQDQFLNQIRKENTFVTVFLLNGFQLRGQVKGFDNFTVLIESEGKQQLIYKHAISTFAPQKNVQLELE
|
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
|
Q65JA8
|
Q9UUC7
|
CTU2_SCHPO
|
Cytoplasmic tRNA 2-thiolation protein 2
|
Schizosaccharomyces
|
MQNTALDNSADSKCSKCDNKATVLTKSDAVCDSCFVRRIENKIRRQFELVRPNLQGRKSKRAMLAISGGISSMAMLETANYLSKYRDDNYRPMFDELLAVHFQWGTDSAVAKTIEESISKNYPKCPFKVIGEAELLNRTIATDSRGNIEINADNEKFNPEVISSLASRQDLLYRIRDKLLVSYARKANCDTIVFGDSGTTIAARVLELVAEGRGFAIPWYTSVCSKLPNCDTFLLRPLREVLSSDLKSYMNIKGLAFCDSLIEARPNTIHGVTESYFSSLNDTFPSLVSTVVKMSSKLHVPSTEAICTICNLPMQEDAETWLQKTTVEHPDSVEGIKNQNVCYGCSVSLKSLKGTLHIPDIEKEGI
|
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with ctu1 that ligates sulfur from thiocarboxylated urm1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
|
Q9UUC7
|
C0ZAH1
|
HEM3_BREBN
|
Pre-uroporphyrinogen synthase
|
Brevibacillus
|
MGKWKVGTRRSKLALTQTNWVVDKLKGFAPEADFELHEIVTKGDRILDVTLSKVGGKGLFVKEIEQSLFDKETDFAVHSLKDMPAELPDGLVIGAIPKRVDPRDVLLSKDGKTLDELPQGALVGTSSLRRSSQILAYRPDIQIESLRGNIDTRMRKLAEGNFDAIILAAAGLERVNFEGEISQFLPVEISLPAVGQGALAIECRADDEETLALLKQFDDAPTRLAVSAERSFLHKLQGGCQVPIGAYATVGENNEITLTGMVGSPDGKQMFKNTATGQDPLALGIQVAEALLAQGAGDVLAEVLRENEQ
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
C0ZAH1
|
Q58445
|
RPO1N_METJA
|
Mja rpoA1 intein
|
Methanocaldococcus
|
MERYEIPKEIGEIMFGLLSPDYIRQMSVAKIVTPDTYDEDGYPIDGGLMDTRLGVIDPGLVCKTCGGRIGECPGHFGHIELAKPVIHIGFAKTIYKILKAVCPHCGRVAISETKRKEILEKMEKLERDGGNKWEVCEEVYKEASKVTICPHCGEIKYDIKFEKPTTYYRIDGNEEKTLTPSDVREILEKIPDEDCILLGLNPEVARPEWMVLTVLPVPPVTVRPSITLETGERSEDDLTHKLVDIIRINNRLEENIEGGAPNLIIEDLWNLLQYHVNTYFDNEAPGIPPAKHRSGRPLKTLAQRLKGKEGRFRYNLAGKRVNFSSRTVISPDPCLSINEVGVPEVVAKELTVPEKVTKYNIERIRQLLRNGSEKHPGVNYVIRKMIGRDGTEQEYKVKITESNKDFWAENIREGDIVERHLMDGDIVLYNRQPSLHRMSIMAHRVRVLPYRTFRHNLCVCVDGDTTVLLDGKLIKIKDLEDKWKDVKVLTSDDLNPKLTSLSKYWKLNADEYGKKIYKIKTELGREIIATEDHPFYTTNGRKRCGELKVGDEVIIYPNDFPMFEDDNRVIVDEEKIKKVINNIGGTYKNKIINELKDRKLIPLTYNDQKASILARIVGHVMGDGSLIINNKNSRVVFRGDIEDLKTIKEDLKELGYDGEEIKLHEGETEITDYNGKKRIIKGKGYSFEVRKKSLCILLKALGCVGGDKTKKMYGIPNWIKTAPKYIKKEFLSAYFGSELTTPKIRNHGTSFKELSFKIAKIEEIFDEDRFIKDIKEMLKEFGIELKVRVEEGNLRKDGYKTKVYVASIYNHKEFFGRIGYTYANKKETLARYAYEYLLTKEKYLKDRNIKKLENNTKFITFDKFIKEKCLKNGFVKEKIVSIEETKVDYVYDITTISETHNFIANGFLTGNCPPYNADFDGDEMNLHVPQSEEARAEAEALMLVEKHILSPRFGGPIIGAIHDFISGAYLLTSNYFTKDEATLILRSGGIKDELWEPDKVENGVPLYSGKKIFSKALPKGLNLRYKAKICRKCDVCKKEECEYDAYVVIKDGELIKGVIDKNGYGAEAGLILHTIVKEFGPEAGRKFLDSATKMAIRAVMLRGFTTGIDDEDLPEEALKEIEKVLDEAEEKVKEIIEKYERGELELLPGLNLEESREAYISNVLREARDKAGAIAERYLGLDNHAVIMAVTGARGNILNLTQMAACLGQQSVRGKRIFRGYRGRVLPHFEKGDLGARSHGFVRSSYKKGLSPTEFFFHAMGGREGLVDQAVRTAQSGYMQRRLINALQDLKTEFDGTVRDSRGIMIQFKYGEDGIDPMLADRGKAVNIDRIIDKVKMKYNQ
|
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms the clamp head domain.
|
Q58445
|
P61721
|
RISB_CORDI
|
6,7-dimethyl-8-ribityllumazine synthase
|
Corynebacterium
|
MSKEGLPNVSSVAGAGLVVGIVSATWNEKICNQLHAEAIRTAKDCGAKVIETRVIGALELPIVVQKLAQTCDAVVANGCVIKGGTPHFDYVCDSVTEGLTRIALDSGVPVGNGVLTTLNEEQAIDRAGFDGSTENKGAEATIAAMHTALVLRDLP
|
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
|
P61721
|
Q2GB76
|
MURA_NOVAD
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Novosphingobium
|
MDKIIIRGGKRLSGAVPVSGAKNSALTLLPCALLTDEPVTLRNLPRLADIDGFQHLMNQFGVSTSIAGARPEDFGRVMTLQATRLTSTVAPYDLVRKMRASILVLGPMLARAGEATVSLPGGCAIGNRPIDLHLKALEALGAQIELAAGYVRAIAPDGGLPGGRYSFPVVSVGATENALMAAVLAKGKSTLHNAAREPEIVDLCNLLVAMGAQIEGIGTSDLTIHGVDRLHGATYMVMPDRIEAGSYACAAAITGGEVMLNGARIEDMEATVQALRDAGVHVEPRKGGIYVAADGPLKPVTISTAPYPGFATDMQAQLMAMLCLAHGSSVLTETIFENRYMHVPELNRMGARIETKGRTAVVHGVEKLTGAEVMATDLRASMSLVIAGLAAEGETQVHRLYHLDRGYERLEEKLSLLGAEIERVGGD
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
Q2GB76
|
Q8LFU0
|
NFYAA_ARATH
|
Nuclear transcription factor Y subunit A-10
|
Arabidopsis
|
MQTEELLSPPQTPWWNAFGSQPLTTESLSGEASDSFTGVKAVTTEAEQGVVDKQTSTTLFTFSPGGEKSSRDVPKPHVAFAMQSACFEFGFAQPMMYTKHPHVEQYYGVVSAYGSQRSSGRVMIPLKMETEEDGTIYVNSKQYHGIIRRRQSRAKAEKLSRCRKPYMHHSRHLHAMRRPRGSGGRFLNTKTADAAKQSKPSNSQSSEVFHPENETINSSREANESNLSDSAVTSMDYFLSSSAYSPGGMVMPIKWNAAAMDIGCCKLNI
|
Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters.
|
Q8LFU0
|
Q6P0U0
|
NAGA_DANRE
|
Amidohydrolase domain-containing protein 2
|
Danio
|
MPSNKSVSDAPITQFVNCRILKNHKLQWEDLWVREGKILNPEKLFFDEQGFADHRVDCENKIIAPGFIDVQLNGGYGIDFSQASSDIRGGVALVAKKILEHGVTSFCPTLVTSPPHIYHKVIPELRVQDGGPEGAGVLGIHLEGPFISEEKRGAHPPKFLRTFQSGGVADLMETYGQLENVAMVTLAPELTNSAAAIHELSSRGITVSVGHSMADLSQAEEAVQNGATFITHLFNAMLPFHHRDPGIVGLLTSDRIPPGRTVYYGMIADGIHTHPAALRIAHRAHPAGLVLVTDAVTAMGLPPGRHTLGQQQIDIQGLHAYVAGTTTLSGSIATMDMCVRHFREASGCTVEAALEAASLHPAQLLGISHRKGTLEFGADADFIVLDDMLTVRETYIAGQQVWRK
|
Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.
|
Q6P0U0
|
A4Y4X5
|
THII_SHEPC
|
tRNA 4-thiouridine synthase
|
Shewanella
|
MKFIVKLYPEIMMKSKPVRMRFTKMLETNIRNVLKKVDEDAKVQRQWDRIMVMVPKHKPELAQAFGERLACIPGIAHVVQVDEYSFESVDDIYQQALPVYRDQIAGKTFCVRVKRTGDHDFNSIDVERYVGGGLNQFTDAIGVRLKNPDVTVNLEIDRDKLYMVTKRIEGLGGFPMATQEDVLSLISGGFDSGVSSYQFIKKGARTHYCFFNLGGAQHEIGVKQVAYHLWKTYGESHKVKFVSVPFEPVVAEILEKIDNGQMGVVLKRMMMRTAARIAERLGIQALVTGESLGQVSSQTLTNLNVIDRCTELLILRPLIAMDKQDIINESRRIGTEDFAKSMPEYCGVISQKPTVKAVLAKVEAEEKKFSEDLIDQIVAQAVTIDIREIAEQMDTRITETETVIAIETNEVVIDIRAPEEEEHKPLNIEGVEVKRIPFFKLATQFADLDKQKTYLLYCERGVMSKLQALYLIEQGYTNVKVYRP
|
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
|
A4Y4X5
|
Q30YB7
|
OTC_OLEA2
|
Ornithine carbamoyltransferase
|
Oleidesulfovibrio
|
MTKHFTQIRDLGYQAAWDVLRRAKEMKDSRHRSTLLEGKSAIMLFEKASTRTRVSFETAVHQLGGKTIFMTPAESQLGRSEPLRDTARVLSRYNDLMIVRTFGQEKIDELVEYGSIPVINALTDEGHPCQVMSDMLTIYERTPDLEKVRVAWVGDGNNMANSWIEAAIFFKFELFMAFPEGYEPDRNLLALAMQAGAKIFLTHDPAMAVDGAHYVNTDVWASMGQEEEQKKREKAFAGFCVDDALMAKAAPDARFMHCLPAHRGEEVTEDVFESPASIVWDQAENRLHMQKALIEWVMEG
|
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
|
Q30YB7
|
B8J031
|
EFP_DESDA
|
Elongation factor P
|
Desulfovibrio
|
MYSTTDFRKGLKIEVEGIPYEIVDFQHFKPGKGGAMVRTKLRNILTGRMQDITFRSGEKVNKPDLETRDMQFLYRQDDDLIFMDMTTYEQLQMPVSTTDGKEGFLKDGQECRVLLYKGNPLDIDIPVSMVLAVVETEPGAKGDTVSNVTKPAKLETGLVVQVPIFVNEGDRIKVDTRSKEYLGRE
|
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
|
B8J031
|
P80200
|
CGA1_HELPX
|
120 kDa protein
|
Helicobacter
|
MTNETIDQQPQTEAAFNPQQFINNLQVAFLKVDNAVASYDPDQKPIVDKNDRDNRQAFEGISQLREEYSNKAIKNPTKKNQYFSDFINKSNDLINKDNLIDVESSTKSFQKFGDQRYRIFTSWVSHQNDPSKINTRSIRNFMENIIQPPILDDKEKAEFLKSAKQSFAGIIIGNQIRTDQKFMGVFDESLKERQEAEKNGEPTGGDWLDIFLSFIFDKKQSSDVKEAINQEPVPHVQPDIATTTTDIQGLPPEARDLLDERGNFSKFTLGDMEMLDVEGVADIDPNYKFNQLLIHNNALSSVLMGSHNGIEPEKVSLLYGGNGGPGARHDWNATVGYKDQQGNNVATIINVHMKNGSGLVIAGGEKGINNPSFYLYKEDQLTGSQRALSQEEIQNKIDFMEFLAQNNAKLDNLSEKEKEKFRTEIKDFQKDSKAYLDALGNDRIAFVSKKDTKHSALITEFGNGDLSYTLKDYGKKADKALDREKNVTLQGSLKHDGVMFVDYSNFKYTNASKNPNKGVGVTNGVSHLEVGFNKVAIFNLPDLNNLAITSFVRRNLEDKLTTKGLSPQEANKLIKDFLSSNKELVGKTLNFNKAVADAKNTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYAQNLKGIKRELSDKLENVNKNLKDFDKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGINPEWISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVIINQKVTDKVDNLNQAVSVAKATGDFSRVEQALADLKNFSKEQLAQQAQKNESLNARKKSEIYQSVKNGVNGTLVGNGLSQAEATTLSKNFSDIKKELNAKLGNFNNNNNNGLKNEPIYAKVNKKKAGQAASLEEPIYAQVAKKVNAKIDRLNQIASGLGVVGQAAGFPLKRHDKVDDLSKVGLSRNQELAQKIDNLNQAVSEAKAGFFGNLEQTIDKLKDSTKHNPMNLWVESAKKVPASLSAKLDNYATNSHIRINSNIKNGAINEKATGMLTQKNPEWLKLVNDKIVAHNVGSVPLSEYDKIGFNQKNMKDYSDSFKFSTKLNNAVKDTNSGFTQFLTNAFSTASYYCLARENAEHGIKNVNTKGGFQKS
|
May be necessary for the transcription, folding, export, or function of the cytotoxin.
|
P80200
|
D4AZ24
|
ENG1_ARTBC
|
Laminarinase
|
Trichophyton
|
MKPYTTLPGVAVLVSLLTQSAHAAPFPSRADVVHTREQESAARPQPIVYKHERGVSNEIQYLPPDPQGHPTIIPFPTHISYVTFNSRPGAIHPPYPHLDISEASFKAEDSTCWYRGKPCEGVPHIPIVKGFDSIEKRSPAPQRHPPAPTKATAGYQFTNCTSTSNPGPTATSPTSGIPSQPSAPPATMAGQDIFQPIAKDPIPANIKSRDDHPVKANHIENPTGPISTNKFYANFFLGNQTSTTFTHPYTMIWAKGDKNASSFGMAISHVEPSQRATGEPNNKLPGNPVRYYINPVGIKSLVLSASELKESTTMSVAKPQAFSAQAILRPTGGSSESITFPLVQGMGFITAIYNNLQPAIQSAVLFRKVEPAGSPQGGIFKYKITLEDDKNWLLYVIPENGADPKLKLEGNKLISGPTGFKGVIQVAKNPSAEEGEGIYDKSAGSYATDIKISGSVGTDGTGTYKFSFEKAGKGAPLVMYALPHHVESFDDATKNTKKNMKLSTTTKGMATACVGDSWTMVEGNLPLSMDFAPWKPGSSSQVTLSEGAKNAIKAVAGNELSQDMELQTNLNSMYFSGKGLNKFAGAIYTVQELVGDKAAASGPLNSLKESFKRFVDNKQQIPLVYDNVWKGVVSSGTYEKGDTGLDFGNTLYNDHHFHYGYFILTAAILGKLDPAWLDANKAYVNMLVRDSGNSVDNDEHFPFSRAFDWYHGHSWAKGLFESSDGKDQESTSEDTMYAYAIKMWGKTSGDKSMEARGNLMLGILARTLNNYFLMKNDNVNQPKNFIGNKVTGILFENKIDHTTYFGANLEYIQGIHMLPLLPNSAYTRSAEFVKEEWEAMFASGAAAPAEKVTGGWKGVLYANLAIIDPEASWKYFAQPSLDLSSIDGGASRIWYLAYAAGEYSTYIAL
|
Probable endo-1,3(4)-beta-glucanase involved in the cell separation process.
|
D4AZ24
|
C5D2V2
|
PROA_GEOSW
|
Glutamyl-gamma-semialdehyde dehydrogenase
|
unclassified Geobacillus
|
MNELLIKAEQLQQAAKTLALLSTEEKNEALTRIAEALIKQKEWILQENEKDVALGKEQGLSPALIDRLQLTNERIEQIVDGVRQVADLPDPIGEIVEEWTRPNGLRIQTIRVPLGVIGMVYEARPNVTVDAASLCLKTGNAVLLRGSSSALHSNKALVHVMKEALRDSAIPADAIQLLEDTSREAAQQMFRLNGYLDVLIPRGGAGLIRSVIENATVPVLETGVGNCHIFIDESAQKQMAIDIVLNAKLQRPSVCNAVETVLIHQNWPYISELVETLHARGVELRGDSQLASSYSFIQQAAETDWSTEYLAPILAVKLVQNVKEAVDHINRYGTKHSEAIISEQNDNVRFFFQAIDAAVLYHNASTRFTDGEQFGYGAEIGISTQKLHARGPMGLRAITTTKSLVYGTGQIRS
|
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
|
C5D2V2
|
Q93V56
|
IPYR1_ARATH
|
Pyrophosphate phospho-hydrolase 1
|
Arabidopsis
|
MSEETKDNQRLQRPAPRLNERILSSLSRRSVAAHPWHDLEIGPGAPQIFNVVVEITKGSKVKYELDKKTGLIKVDRILYSSVVYPHNYGFVPRTLCEDNDPIDVLVIMQEPVLPGCFLRARAIGLMPMIDQGEKDDKIIAVCVDDPEYKHYTDIKELPPHRLSEIRRFFEDYKKNENKEVAVNDFLPSESAVEAIQYSMDLYAEYILHTLRR
|
Catalyzes the irreversible hydrolysis of pyrophosphate (PPi) to phosphate. The MgPPi(2-) complex binds to the enzyme only after a free Mg(2+) ion has bound (Ref.9). No activity with glycerol-3-phosphate, glucose-6-phosphate, p-nitrophenylphosphate, ADP, NADP(+), NAD(+),NADH, NADPH or phosphoribosyl pyrophosphate as substrates (Ref.9). Controls the equilibrium of gluconeogenic reactions in the heterotrophic growth phase of early seedling establishment. Determinates the rate of cytosolic glycolysis, providing carbon for seed storage lipid accumulation .
|
Q93V56
|
Q2IX94
|
RL9_RHOP2
|
50S ribosomal protein L9
|
Rhodopseudomonas
|
MEVILLERVAKLGQMGELVRVKDGYARNFLLPRGKALRATAANRDKYEHMKADLEARNIAAKAEAAKVAEKIDGHNVIVIRQASETGQLFGSVSVRDIVTSFEAEGVMISRSQILLDAPIKTIGKHAIEVAVHPEVEVGVSVTVARSAEEAERINRGEDISTRREDQDAAAEAIAAAGEFFDPDAVQDDEEQPVEQ
|
Binds to the 23S rRNA.
|
Q2IX94
|
Q54N80
|
FKBP3_DICDI
|
Rotamase
|
Dictyostelium
|
MNKFLIALLVLATLAVSFSQEIGVSILKTDTPKGECKGKTASIGDYISLKYVGKFEDGTVFDSSEIHGGFSFNFTIGERKVIPGLEIGTINICEGEKRSIKIPYQLAYGENGIENAIPPRTDIYFDLEVVSIEGAPAQPFYYQLIPSVGTIIAFSMLAGFIVLVKFIIKRYPDESNSKKPAPGKPKKTKAAKQN
|
PPIases accelerate the folding of proteins by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
|
Q54N80
|
C5DX31
|
GSM1_ZYGRC
|
Glucose starvation modulator protein 1
|
Zygosaccharomyces
|
MTKKLSLELRQTRKPIQTACGFCHEKHLQCDVGRPCQNCRKRNIASFCRDKVKRRRKRKRSDASNFDKDEAATQTLNFNTVNPGEGSSSAMTQDEKNTGTTTATTTRTTTNFRSESKASSSTENISRAMKDPADTIIANSLLDKPTIGDTDDTGWGFGSIWTNDEYMTLNDLTSFASESMPNQLGPIEEQRSPRRTLGEPLARRYDSSQPFQYLNFGSKLHKTDSRPYISLEQPGNVPSIPAFTMNKGSNDEDASPQQKESQQMQLWQQQASQLQQQASQLQQQASQLQQQRTQQNEPVSEWTPFQLRLLIKTPKDLFDKKNLVKPHNYRKAYKDLLECLHKMFLGSYYRRQNGRWRPVSDDEDQMRRRLMRKEQLQHIAKSIGELYMPKFVALTSNMIEEDLLLQELVLQRSLLELENMSKLVNCTPICIWRRSGEICFVSNEFCSLTGFYKREILDQRRFIVEFMDHQSVVSYYDLFHEHLAFGPKDSTRTILNKDQAVYTECNLLLNNGSYLKCACCLTARRDAFNISLLLMGQFLPIFDVQ
|
Transcription factor which regulates nonfermentable carbon utilization.
|
C5DX31
|
P50420
|
CASK_CAPSU
|
Kappa-casein
|
Capricornis
|
MMKSFFLVVTILALTLPFLGAQEQNQEQPICCEKDERFFDDKIAKYIPIQYVLSRYPSYGLNYYQQRPVALINNQFLPYPYYAKPVAVRSPAQTLQWQVLPNTAPAKSCQDQPTTMARHPHPHLSFMAIPPKKDQDKTEIPTINTIASAEPTVHSTPTTEAIVNTVDNPEASSESIVSAPETNTAQVTSTEV
|
Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
|
P50420
|
P87020
|
PRA1_CANAL
|
58 kDa fibrinogen-binding mannoprotein
|
Candida
|
MNYLLFCLFFAFSVAAPVTVTRFVDASPTGYDWRADWVKGFPIDSSCNATQYNQLSTGLQEAQLLAEHARDHTLRFGSKSPFFRKYFGNETASAEVVGHFDNVVGADKSSILFLCDDLDDKCKNDGWAGYWRGSNHSDQTIICDLSFVTRRYLTQLCSSGYTVSKSKTNIFWAGDLLHRFWHLKSIGQLVIEHYADTYEEVLELAQENSTYAVRNSNSLIYYALDVYAYDVTIPGEGCNGDGTSYKKSDFSSFEDSDSGSDSGASSTASSSHQHTDSNPSATTDANSHCHTHADGEVHC
|
Cell surface protein involved in the host-parasite interaction during candidal infection. With MP65, represents a major component of the biofilm matrix. Sequesters zinc from host tissue and mediates leukocyte adhesion and migration. As a surface protein, binds the two human complement regulators CFH and CFHR1, as well as plasminogen PLG, mediates complement evasion and extra-cellular matrix interaction and/or degradation. As a released protein, enhances complement control in direct vicinity of the yeast and thus generates an additional protective layer which controls host complement attack, assisting the fungus in escaping host surveillance. Binds to host fluid-phase C3 and blocks cleavage of C3 to C3a and C3b, leading to inhibition of complement activation. Mediates also human complement control and complement evasion through binding to C4BPA, another human complement inhibitor, as well as through binding to host integrin alpha-M/beta-2. Decreases complement-mediated adhesion, as well as uptake of C.albicans by human macrophages.
|
P87020
|
P24377
|
GVPM1_HALSA
|
Gas vesicle protein GvpM 1
|
Halobacterium
|
MEPTKDETHAIVEFVDVLLRDGAVIQADVIVTVADIPLIGISLRAAIAGMTTMTEYGLFEEWDAAHRQQSEAFTTSPTADRRED
|
Gas vesicles are small, hollow, gas filled protein structures that are found in several microbial planktonic microorganisms. They allow the positioning of the organism at the favorable depth for growth. This protein could be important for the shape determination of the gas vesicle.
|
P24377
|
P0A1K8
|
SPAO_SALEN
|
Surface presentation of antigens protein SpaO
|
Salmonella
|
MSLRVRQIDRREWLLAQTATECQRHGQEATLEYPTRQGMWVRLSDAEKRWSAWIQPGDWLEHVSPALAGAAVSAGAEHLVVPWLAATERPFELPVPHLSCRRLCVENPVPGSALPEGKLLHIMSDRGGLWFEYLPELPAVGGGRPKMLRWPLRFVIGSSDTQRSLLGRIGIGDVLLIRTSRAEVYCYAKKLGHFNRVEGGIIVETLDIQHIEEENNTTETAETLPGLNQLPVKLEFVLYRKNVTLAELEAMGQQQLLSLPTNAELNVEIMANGVLLGNGELVQMNDTLGVEIHEWLSESGNGE
|
Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells.
|
P0A1K8
|
Q3JNY2
|
PHNC_BURP1
|
Phosphonates import ATP-binding protein PhnC
|
pseudomallei group
|
MDAIRIERLSKTFPNGRKGLEDIDLAIAPGEMVALIGASGSGKSTLLRQIASFSSSDARPSRIDIFGRSIQRDGRIARDVRRMRRDIGFVFQQFNLVDRLSVETNVLIGALARVPMWRRLAGRFSRADRALAAQALGEVGIAEHARERAANLSGGQQQRAALARALVQRARIILADEPIASLDPAASRRVMEMLRALNANHRLTVLVSLHQIDVALRFCPRVVALRAGRIVYDGPSAALTRERLHALYGDDAHLPFAVGDEVRPAAREAAGEPARRAPAAFDSAGSPDLPDSQPASPRRMLAASSMR
|
Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
|
Q3JNY2
|
A4SRD4
|
LEPA_AERS4
|
Ribosomal back-translocase LepA
|
Aeromonas
|
MKHIRNFSIIAHIDHGKSTLSDRLIQTCGGLSSREMQAQVLDSMDLERERGITIKAQSVTLNYQAQDGNTYQLNFIDTPGHVDFSYEVSRSLAACEGALLVVDAGQGVEAQTLANCYTAMEMELEVVPVLNKIDLPAAEPERVAEEIEDIVGIDAIDAVRCSAKTGLGVDLVLEEIVARIPAPVGDPDAPLQALIIDSWFDSYLGVVSLVRIKNGSLKKNDKIKVMSTGQVWGVDRIGIFTPKQVDTQGLGCGEVGWVVCGIKDIHGAPVGDTLTQAKNGAEKALAGFKKVKPQVYAGLFPISSDDYESFRDALDKLSLNDASLFFEPESSTALGFGFRCGFLGMLHMEIIQERLEREYDLDLITTAPTVVYEIELNDGSTIHIDSPSAMPPVNNIKEMREPIAECNILLPQEYMGNVITLCIEKRGVQTNMVYHGNQVALTYEIPMAEVVLDFFDRLKSTSRGYASLDYGFKRFETSEMVRLDIMINGERVDALAIITHKENAQYRGRQVVEKMRELIPRQMFDIAIQASIGNQIIARSTVKALRKDVTAKCYGGDVSRKKKLLNKQKEGKKRMKSLGRVDVPQEAFLAILHVGKD
|
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
|
A4SRD4
|
Q0IBC2
|
RECR_SYNS3
|
Recombination protein RecR
|
unclassified Synechococcus
|
MIDQFERLPGIGPRTAQRLALHLLRQPEEQIHSFADALLAARSQVGQCQTCFHLSAEPTCEICRNPERSIGMLCVVADSRDLLALERTREYAGRYHVLGGLISPMDGIGPEMLQISNLVKRVAADEINEVILALTPSVEGDTTSLYLARLLKPFTEVSRIAYGLPVGSELEYADDVTLSRALEGRRAVE
|
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
|
Q0IBC2
|
Q884I3
|
LOLD_PSESM
|
Lipoprotein-releasing system ATP-binding protein LolD
|
Pseudomonas
|
MSDKAVLSCRNLGKSYEEGPESVVVLSGLQLELHPGERVAIVGTSGSGKSTLLNLLGGLDTPSEGSVWLAGEELSALGEKARGLLRNRALGFVYQFHHLLPEFTALENVCMPLLIGRTAIPEARQRATALLERVGLGHRLAHKPSELSGGERQRVAIARALINQPGLVMLDEPTGNLDHHTAQGIQDLMRELSTSSRTAFLIVTHDMSLARQMDRILRLEGGRLVEA
|
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.
|
Q884I3
|
A9B9C4
|
PSBX_PROM4
|
Photosystem II reaction center X protein
|
Prochlorococcus
|
MAFPVLNLLLDVAVSSEAATNSAIGMIGSFLAAAAFIVVPAASFLIWVSQKDALERKR
|
Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.
|
A9B9C4
|
P58097
|
HSLO_CAUVC
|
Heat shock protein 33 homolog
|
Caulobacter
|
MTDIAPDTGVLDDVVSAFQIENLPVRGRVVRLGAAIDEVLTRHDYPEPVANLLGEACALAALVGSSLKFEGRLIVQAQGDGPVRYVVVDYDTSGGLRGYCRFDPEEVAAVSEGFVRPGAKTLLGGGVFIMTLDQGPDMDRYQGVTPIEGETLALCAEQYFAQSEQTPTRVRLAVGQADTGQGATWRAGGILIQVIAGDQARGETQDAWTHVQALFETTGEDELIDPTVSTPTLLWRLFNEDGVRLLDEKPLKAFCRCSEDRIGVVMDSFSAEEVAEMVEPDGKIHVTCEYCSRIYKLDPPGA
|
Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
|
P58097
|
B6JLX1
|
DDL_HELP2
|
D-alanylalanine synthetase
|
Helicobacter
|
MEFCVLFGGASFEHEISIVSAIALKEVLKDRIKHFIFLDENHHFYLIEASNMHSKYFAQIKEKKLPPLILAHNGLLKNSFLGTKIIELPLVINLVHGGDGEDGKLASLLEFYRIAFIGPRIEASVLSYNKYLTKLYAKDLGVKTLDYVLLNEKNRANALDLIKFNFPFIVKPSNAGSSLGVNVVKEEKELVYALDSAFEYSKEVLIEPFIQGVKEYNLAGCKIKTDFCFSYIEEPNKQEFLDFKQKYLDFSRNKAPKANLSNALEEQLKENFKKLYNDLFSGAIIRCDFFVIENEVYLNEINPIPGSLAHYLFDDFKTTLENLAQSLPKTPKIQVKNSYLLQIQKNK
|
Cell wall formation.
|
B6JLX1
|
Q7NK82
|
GPMA1_GLOVI
|
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1
|
Gloeobacter
|
MAHLILIRHGQSLWNAANKFTGWVDVPLSERGRAEATIASCKLRDYRVNVCFTSMLMRAIETAVITLTECDDICGGKIPIIKHEADDENWHGWDNYDGDPAAELPIYPTATLDERYYGDLQGLDKAETTAKYGKEQVQIWRRSYSVRPPGGESLEDTRKRVYPYFTNRILGHIKQGDNVLVAAHGNSLRSIIMILETLSEEEVPKVELATGVPIVYELDKAAHMLSKAVLTN
|
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
|
Q7NK82
|
A2ALI5
|
AJAP1_MOUSE
|
Adherens junction-associated protein 1
|
Mus
|
MWIQQLLGLSSMSIRWPGRSLGSHAWILIAMLQLAVDFPSCDSLGPGPEFRLLSRPQRPQRLWSLRSGPPTRLPTPAWSPRAARAERAHGPIQMQTPRARRAHRPRDQVATLGPKGGLTKPPAATRSSPSLASATASSSIVTAGAAEHQGLLRRGRRHTHDTEFNDFDFRGGRPTTETEFIAWGPTGDEDALESNTFPGGFGPTTVSILQTRKTTVATTTTTTAASTATAMTLQTKGVTESLDPWKRTPVGVSTTEPSTSPSSNGKDIQPPRILGETSGLAVHQIITITVSLIMVIAALITTLVLKNCCAPSGHTRRNSHQRKMNQQEESCQNLTDFTPARVPSSVDIFTAYNETLQCSHECVRASVPVYADETLHSTGEYKSTFNGNRTSSADRHLIPVAFVSEKWFEISC
|
Plays a role in cell adhesion and cell migration.
|
A2ALI5
|
Q2J6V2
|
ILVC_FRACC
|
Ketol-acid reductoisomerase type I
|
Frankia
|
MVEIYYDDDASLDVLADRKVAVIGYGSQGHAHALNLRDSGVDVRVGLPADSRSRARAEEEGLRVLTPAEASAEADIIMLLTPDTTHRTIYAESIAPHLTAGKALAFGHGFNIRYGLIEPPAGVDVFMVAPKGPGHLVRRVFEEGKGVPVLVAVEADASGNALAVALAYAKGIGGTRAGALRTTFTEETETDLFGEQAVLCGGASALVQAGFETLVEAGYTPEVAYFECLHELKLIVDLMYEGGISQMRYSISDTAEYGDVTRGPRVITPAVKAEMRKILDEIRDGAFAREWVAEDDNGRPNFTKLVAEGKQHPIEQVGAKLRPMMSWIA
|
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
|
Q2J6V2
|
P51580
|
TPMT_HUMAN
|
Thiopurine methyltransferase
|
Homo
|
MDGTRTSLDIEEYSDTEVQKNQVLTLEEWQDKWVNGKTAFHQEQGHQLLKKHLDTFLKGKSGLRVFFPLCGKAVEMKWFADRGHSVVGVEISELGIQEFFTEQNLSYSEEPITEIPGTKVFKSSSGNISLYCCSIFDLPRTNIGKFDMIWDRGALVAINPGDRKCYADTMFSLLGKKFQYLLCVLSYDPTKHPGPPFYVPHAEIERLFGKICNIRCLEKVDAFEERHKSWGIDCLFEKLYLLTEK
|
Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine (also called mercaptopurine, 6-MP or its brand name Purinethol) and 6-thioguanine (also called tioguanine or 6-TG) using S-adenosyl-L-methionine as the methyl donor . TPMT activity modulates the cytotoxic effects of thiopurine prodrugs. A natural substrate for this enzyme has yet to be identified.
|
P51580
|
A3CVT7
|
THIC_METMJ
|
Thiamine biosynthesis protein ThiC
|
Methanoculleus
|
MSLIEDARRGVVTEEMRIVAAAEGVTEDFVRRGVAEGHIVIPVSPYRRVKICGIGEGLRTKVNASIGTSTDMVDVDMEVEKVRQAERAGADTLMELSTGGDFLEIRRRVVEATTLSVGSVPLYQAFIEAARKRGAVVHMEPDDLFRITAEQAKLGTNFMAIHTGINYETMKRLQNQGRHGGLVSRGGAFMTAWMLHNEKENPLYSEFDYLLEILKEHEVTLSFGNGMRAGAVHDATDRAQVQELLINAELADKAHEQGVQTIIEGPGHIPVDEIQTNVVLQKRVTNRRPFYMLGPLVTDIAPGYDDRVAAIGAALSSSYGADFICYVTPAEHLALPTPEEVYEGVMSSRIAAHVGDMIKLKKRDADLEMGHARRDLDWERQFAVAMNPERARAIRDERMPADTDGCTMCGDYCALKIVGRHFNF
|
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
|
A3CVT7
|
Q98DG5
|
MSCL2_RHILO
|
Large-conductance mechanosensitive channel 2
|
Mesorhizobium
|
MLKEFQEFISKGNVMDLAVGVIIGAAFGKIVDSLVNDIIMPVIGAIFGGLDFNNYFVGLSSAVNATSLADAKKQGAVFAYGSFITVALNFVILAFIIFLMVKAVNNLRRRLEREKPATPAAPPPADVALLTEIRDLLARR
|
Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
|
Q98DG5
|
Q6EW15
|
RK14_NYMAL
|
50S ribosomal protein L14, chloroplastic
|
Nymphaea
|
MIQPQTLLNVADNSGARKLMCIRIIGASNYRYAHIGDVIVAVIKEAVPNMPLERSEVIRAVIVRTCKELKRDNGMIIRYDDNAAVVIDQEGNPKGTRVFGSIARELRQLNFTKIVSLAPEVL
|
Binds to 23S rRNA.
|
Q6EW15
|
B0R7F9
|
CAPPA_HALS3
|
Phosphoenolpyruvate carboxylase
|
Halobacterium
|
MVDVPRLMSTQHPDNATLPFFTAGDVIEGEDEIQEAYYVYSHLGCDEQMWDFEGKEGDEYAVKKLLSRYDEFFADHQLGTDVRLTVRGPNPDVEGSEAKILLEILESIPRSFDAARRFAGEYGLETTAPIFEVIVPMVTDADQLNAVHEYYERFVTGKADEAVWDGRTVEEWVGEFDPASITVIPLIEEREAMLAADDIVREYATAHDQDAVRVFLARSDPALNYGCLAADLINKVALQRLYEMSEATGVDVHPILGAGSAPFRGNLTPERAAATADAYSEVETFTVQSAFKYDYPVETVRDGVATLRDADLGAPPFPIDEARALAVIDRTADAYADQVDAIAGTVNRLSSYVPDRRARKLHVGLFGYAREVGENALPRAIGYTASLYAVGCPPTLLGAHALTDDDAAFVREAFPAYFDHLADAARYFNPRCTDVLDLDDDTLAAAVERVDVTPNSEHRAATDDAIDALQRGDDDALRSAIRRGARERQFLG
|
Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
|
B0R7F9
|
A4FUD4
|
PEX12_BOVIN
|
Peroxin-12
|
Bos
|
MAEHGAHITTASVVDDQPSIFEVVAQDSLMSAVRPALQHVVKVLAESNPAHFGFFWRWFDEIFTLLDLLLQQHYLSKTSASFSENFYGLKRIVMGDQHKLQRLANAGLPKQQFMKSIMFLVLLPYLKVKLEKLVSSLREEDEYSIHPPSSRWKRFYRAFLAAYPFVNMAWEGWFLVQQLRYILGKAQHHSPLLRLAGVRLGRLTVQDIQALEHKPAEASMMQLPAGSIGEKIKSALKKAVGGVALSLSTGLSVGVFFLQFLEWWYSSENQETIKSLTALPTPPPPVHLDYNSDSPLLPKMKTVCPLCRKNRVNDTVLATSGYVFCYRCVFHYVRSHQACPITGYPTEVQHLIKLYSPEN
|
Required for protein import into peroxisomes.
|
A4FUD4
|
A4YCM2
|
YIDC_SHEPC
|
Membrane protein YidC
|
Shewanella
|
MESQRNILLIGLLFVSFLLWQQWQADKAPKPVATESSLVANVASTHSADVPEADTGVPAAVAASKNLITVKTDQLDVQINPVGGDIVFAALVSHKMEQGKEQPFVLLEQTKDYTYIAQSGLIGRDGIDSSANGRAAFTTSATEFTLAEGQDTLEVPLTYVADNGVTYTKVFVFHRGKFNVDVDYKINNTSAAPLQVQMYGQIKQTIKPSESSMMMPTYRGGAFSTNDVRYEKYNFDDMAKSNLNQATLGGWAAMLQHYFVSAWVPPATDSNTIFSSVSAGGLANIGFRGAVYDIAPGASQEISSQFYVGPKDQAALSAISETLNLVVDYGFLWWLAVPIHWLLMFYQSFVGNWGVAIILITLTVRGLLFPLTKAQYTSMAKMRNLQPKLADLKERFGDDRQKMGQAMMELYKKEKVNPMGGCLPIILQMPIFIALYWVLLESFELRHAPFMLWIHDLSVQDPYYILPLLMGVSMFIMQKMQPIAPTMDPMQVKMMQWMPVIFTVFFLWFPSGLVLYWLVGNIVAIIQQKIIYAGLEKKGLK
|
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
|
A4YCM2
|
C6DF52
|
LOLA_PECCP
|
Outer-membrane lipoprotein carrier protein
|
Pectobacterium
|
MKKWLAISCLIAGMTSTAVYADAAKDLQGRLNKVNSFHANFSQKVTSADGAAVQEGEGELWLKRPNLFNWKTTSPDESTLISDGKTLWFYNPFVEQVTATWLKDATGNTPFILITRNDASDWNKYDVRQKGDDFELTPKSASGNLKQFAINVTTNGTIKQFTATEQDGQRSTYVLKNQQNAAVDAAQFTFTPPKGVTLDDQRQ
|
Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).
|
C6DF52
|
Q9WV23
|
CMAH_CRIGR
|
CMP-NeuAc hydroxylase
|
Cricetulus
|
KQTAETLLSLSPAETANLKEGINFFRNKTTGKEYILYKEKNHLKACKNLCKHQGGLFIKDIEDLDGRSVKCTKHNWKLDVSTMKYINPPGSFCQDELVVEMDGNDGLFLIELNPPNPWDSDPRTPEELAFGEVQITYLTHACMDLKLGDKRMVFDPWLIGPAFARGWWLLHEPPSDWLERLCKADLIYISHMHSDHLSYPTLKQLSQRRPDIPIYVGDTERPVFWNLDQSGVQLTNINVVPFGVWQQVDKNLRFMILMDGVHPEMDTCIIVEYKGHKILNTVDCTRPNGGRLPEKAALMMSDFAGGASGFPMTFSGGKFTEEWKAQFIKAERRKLLNYKAQLVKDLQPRIYCPFAGYFVESHPSDKYIKETNIKNDPIQLNNLIKKNCDVVTWTPRPGATLDLGRMLKDPTDSQGIIEPPEGTKIYKDSWDFGPYLSTLHSAVGDEIFLHSSWIKEYFTWAGFKSYNLVVRMIETDEDFNPFPGGYDYLVDFLDLSFPKERPSREHPYEEIRSRVDVVRYVVKHGLLWDDLYIGFQTRLQRDPDIYHHLFWNHFQIKLPLTPP
|
Sialic acids are components of carbohydrate chains of glycoconjugates and are involved in cell-cell recognition and cell-pathogen interactions. Catalyzes the conversion of CMP-N-acetylneuraminic acid (CMP-Neu5Ac) into its hydroxylated derivative CMP-N-glycolylneuraminic acid (CMP-Neu5Gc), a sialic acid abundantly expressed at the surface of many cells.
|
Q9WV23
|
A1T876
|
PDXT_MYCVP
|
Pyridoxal 5'-phosphate synthase glutaminase subunit
|
Mycolicibacterium
|
MSAPQVGVLALQGDTREHLAALREAGAEARTVRRLDELNSVDALVIPGGESTAMSHLLREFGLLEPLRARLAEGMPAYGSCAGMILLATEIADAGVAGREALPLGGIDMTVRRNAFGRQVDSFEEDVEFEGLDGPVHAVFIRAPWVERVGPDVEVLARAGGHPVAVRQGKMLATAFHPEVTGDRRVHRLFVASLS
|
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
|
A1T876
|
Q2YAA5
|
NUOA_NITMU
|
NUO1
|
Nitrosospira
|
MNASATQATEIWPLVAYFFLVVMLVVGVMALSYIIGERHRSKATDEPFESGIVTVGLARFRLSAKFYLIAVFFVIFDVEAVFLFAWAVAFRELGWPGYIEAIIFISILGAALAYLWRLGALDWGPPRHSAGRFAKDSRSPNHAVVSK
|
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.
|
Q2YAA5
|
C4LC60
|
RNH_TOLAT
|
Ribonuclease H
|
Tolumonas
|
MLKQITLYTDGSCLGNPGPGGYAAVLIYKQHRKELAQGYELTTNNRMELMAAIAGLQSLSEPCQVRLTTDSQYVRQGITQWIHGWKKKGWKTANREPVKNVDLWLLLDSEIQRHDVEWFWVKGHSGHPENERCDELARNAALADSRLIDSGYPS
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
C4LC60
|
Q7V2K6
|
TSAD_PROMP
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Prochlorococcus
|
MHKVLAIETSCDETSVSIVSNSGDIYKIHSNIVASQIEDHSKWGGVVPELAARKHLELLPFVLEQALEESKIRIEKIDVIASTVTPGLVGCLRVGSITARSLCTLYSKPFLGIHHLEGHLSSILFSKNYPKPPFLTLLVSGGHTELIKVGERRKMQRLGRSYDDAAGEAFDKVGRLLGLSYPGGPAIAKIAKKGNASKFNLPKCKISDKEGGFLKYDFSFSGLKTAVLRLVEKINLNGDEIPIPDIAASFERVVAEVLVERTIKCANDYGLDNIVVVGGVAANDTLRKMMISEACKKSIKVHLAPINLCTDNAAMIGAAALYRLKFKAYESSLKLGISGRLPIDQANTLYENKPPF
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
Q7V2K6
|
A9BZY6
|
DAPE_DELAS
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Delftia
|
MSRTLQLTEQLISLPSVTPEDAGCLELLADALQPMGFACERIDSGPDSFRVRNLWARRSGTGADRPVLVFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGASDMKTSIAAFVVALEEFLAETPAPSFDIALLLTSDEEGPSVDGTKVVVELLRERGERLDWCIVGEPTSVERTGDMIKNGRRGTMSGRLTVKGIQGHIAYPQLARNPIHQALPALAELAATRWDEGNAFFPPTSWQISNMHGGTGASNVIPGHVTIDFNFRFCTESTAESLQQRVHAVLDHHGLEYELAWTIGGQPFLTTPGTLVNAVQAAIRAETGLETELSTTGGTSDGRFIAQICSQVVEVGPSNASIHKIDEHIVVADIEPIKNIYRRTLQELQRQQAV
|
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.
|
A9BZY6
|
Q4J8L2
|
PDXT_SULAC
|
Pyridoxal 5'-phosphate synthase glutaminase subunit
|
Sulfolobus
|
MKVGVIAYQGSFEEHAIQLKRAMSKLNLTGEVIAVKKPKDVDLIDGVVIPGGESTTIGIIAEKLGVLDEIKAKINAGLPVLGTCAGAIMLAKDVSDAKVGKKSQPLIGTMDIQVVRNYYGRQRESFETDLDFRVIGGGKARVVFIRAPIIKRTWNDATALISFENGIVMAEQKNMLATTFHPELSESTIVHEYFLSKIKK
|
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
|
Q4J8L2
|
B3H6C3
|
FB311_ARATH
|
F-box protein At4g35733
|
Arabidopsis
|
MSEATVWSDLPGELLDHIANGLFSKVELLRFRSICKTFRSAVDSDKNFLDHLKRNRRRLLSPYSTGKTCSLSPAAFYRVVLSSYPDKGWLIKLQDAYVSSQKQLLSPLSRFSIKSSGKTLDLLEFTVSEIHQSYDVEYLYYNSTRASFNFARVVLAEDFVFIVDNYKKIWLCNSNESDSHWVRIMDEEVKLFSDIVFHKGYMYALDLTGAVWWISLSEFGIFQFGPSSTPMDYCDIDECKDKRFVEYCGDLCIVHRFSRKFRIKRVDIDMTVGFKVYKMDEELVEYVEVKSLGDKAFVMATDSCFSVLAREYYGCLENSIYFTEQNNVKVFKLGDGSITNMVDSSFQSCFQMLIPPLV
|
Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
|
B3H6C3
|
B4R136
|
SNMP1_DROSI
|
Sensory neuron membrane protein 1
|
Sophophora
|
MQVPRVKLLMGSGAMFVFAIIYGWVIFPKILKFMISKQVTLKPGSDVRELWSNTPFPLHFYIYVFNVTNPDEVSEGAKPRLQEVGPFVFDEWKDKYDLEDDVVEDTVSFTMRNTFIFNPKESLPLTGEEEIILPHPIMLPGGISVQREKAAMMELVSKGLSIVFPNAKAFLKAKFMDLFFRGINVDCSSEEFSAKALCTVFYTGEVKQAKQVNQTHFLFSFMGQANHSDSGRFTVCRGVKNNKKLGKVVKFADEPEQDIWPDGECNNFVGTDSTVFAPGLKKEDGLWAFTPDLCRSLGAYYQHKSSYHGMPSMRYTLDLGDIRADEKLHCFCEDPEDLDTCPPKGTMNLAACVGGPLMASMPHFYLGDPKLVADVDGLNPNEKDHAVYIDFELMSGTPFQAAKRLQFNLDMESVEGIEPMKNLPKLILPMFWVEEGVQLNKTYTNLVKYTLFLGLKINSVLRWSLITFSLVGLMFSAYLFYHKSDSLDINSILKDNNKVDDVASTKEPMPPANPKQSSTVHPVQLPNTLIPGTNPATNPATHLKMEHRERY
|
Plays an olfactory role that is not restricted to pheromone sensitivity.
|
B4R136
|
Q88LM7
|
KDSB_PSEPK
|
CMP-2-keto-3-deoxyoctulosonic acid synthase
|
Pseudomonas
|
MSLEFTVVIPARLRSTRLPGKPLLLIAGKPMVQHVWEQARKSGASRVVIATDDTSILEACQAFGAEVMMTRADHESGTDRLAEVAAYLGLPADAIVVNVQGDEPLIPPVIIDQVAANLAAHPEAGIATLAEPIHEPETVFNPNAVKVVSDKNGLALTFSRAPLPWARDTFAKARDVLPEGVPYRRHIGMYAYRVGFLHDFVSWGPCWLEQAEALEQLRALWHGVRIHIEDAIEAPAVGVDTPEDLERVRRLLEA
|
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
|
Q88LM7
|
B4EE50
|
MNMA_BURCJ
|
tRNA-specific 2-thiouridylase MnmA
|
Burkholderia cepacia complex
|
MSKRRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDDDDGEYCSTRQDWIDVVSVADLIGIDVEAVNFAAEYKDRVFAEFLREYSAGRTPNPDVLCNAEIKFKAFLDHAMSLDAEMIATGHYARVRERDGRFELLKAFDHTKDQSYFLHRLNQAQLSKTMFPLGEIPKTKVREIAAQIGLPNAKKKDSTGICFIGERPFRDFLNRYLPTKPGPMKTPDGKVVGEHIGLAFYTFGQRKGIGLGGSKSGSGEPWFVAAKDIASNTLYVVQGHDHPWLLSRELVAGNVSWVAGEPPADGFACGAKTRYRQADAACVFGLAATGAEAAGPAGEARFSLAFDDAQWAVTPGQSAVLYDGEICLGGGIIESAATGQPGQATSTGHAPALAEAR
|
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
|
B4EE50
|
B0TFZ0
|
YQGF_HELMI
|
Putative pre-16S rRNA nuclease
|
Heliomicrobium
|
MRIMGLDVGDKTIGVAVSDLMGWTAQGVATIRRSRLAADLEHLRELVKTYEVERIVCGLPRNMNGTYGPRAEGIRKFGSLVEKKLNIPVDYWDERLTTVAAQKTLIAGDLSRAKRKQVVDKLAAVLILQNYMDAKAHLAAKEQSKETSE
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
B0TFZ0
|
Q125B6
|
ARGB_POLSJ
|
NAG kinase
|
unclassified Polaromonas
|
MTQPTVTADDPDLSHVGPRDKAEILAQALPYIRKFHGKTMVIKYGGNAMTDPALQADFAEDVVLLKLVGMNPVVVHGGGPQIEAALNRLGKKGHFIQGMRVTDEETMEVVEWVLAGQVQQDIVGLINQAGGKAVGLTGRDGGLIRAQKLKMVDKDDPAKEHDIGFVGDIVSIDPSVVKALQDDAFIPVISPIGFGESNESYNINADVVAGKLATVLKAEKLVLLTNTPGVLNKAGELLTDLTAREIDDLFADGTISGGMLPKIEGALDAAKSGVNSVHIIDGRVPHAMLLEILTDQAYGTMIRSH
|
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
|
Q125B6
|
A0M2K0
|
RNY_GRAFK
|
Ribonuclease Y
|
Gramella
|
MEILIIVIAAVVGLALGFAIAKMLEKKQASGTIASAKKEAGSILKEAKAEGESIKKDKILQAKEKFIELKSEHEKVILSRDKKINDAEKRIKDKESHVSNELGKNKKLNKDLEEKVADYDHRLDFLEKKQEDIDKLHNSKVQQLEVISGLSAEDAKAQLIESLKDTAKADAMSIIQDTVEEAKLTAQQEARKIIINTIQRIGTEEAIENCVSVFNLESDDVKGRIIGREGRNIRALEAATGVEIIVDDTPEAIILSCFDSVRREVARLSLHKLVTDGRIHPARIEEVVKKTRKQIEEEIIDIGKRTVIDLGIHGLQPELIKMVGRMKYRSSYGQNLLQHSREVAKLCGVMAAELGLNPKLAKRAGLLHDIGKVPETETEVPHAILGMQWAEKHGEKPEVCNAIGAHHDEIEMNSLLSPIVQVCDAISGARPGARRQVLDSYIQRLKDLEEIAFGFGGVKKAYAIQAGRELRVIVESEKVSDEKASNLSFEISQKIQTDMTYPGQVKITVIRETRAVNVAK
|
Endoribonuclease that initiates mRNA decay.
|
A0M2K0
|
A1KB13
|
RS8_AZOSB
|
30S ribosomal protein S8
|
Azoarcus
|
MSMSDPIADMLTRIRNGQQAQKASVTMPSSKVKVAIAKVLQDEGYIEGFSVREGEGKAVLDVALKYYAGRPVIERIERVSRPGLRVYKGTDDLPRVMNGLGVAIVSTPKGVMTDRAARASHVGGEVICLVA
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
|
A1KB13
|
Q46Z04
|
PLSX_CUPPJ
|
Phosphate-acyl-ACP acyltransferase
|
Cupriavidus
|
MTIKIAIDCMGGDHGVSVTVPAAISFLASHDDAAVVLVGLPDAIQAQLKKLRAQDHPRVSVVPATEVITMDDPVEVALRKKKDSSMRVAVTQVKEGLAGACISAGNTGALMAVSRYVLKTLEGIERPAIATTIPNEQGWGTTVLDLGANADCEPEHLLQFARMAEAMVAVVDHKEHPTVGLLNIGEEVIKGNEVVKRAGELLRASELNFHGNVEGNDIFKGTTDIVVCDGFVGNVALKSTEGLAKMIGGMIKEEFTRSWFTKLLAGIAMPVLSRLAKRLDPARYNGASLLGLRGLVIKSHGSADAHSFEWAIKRGYDAAKNGVIERIARAFADKTSAAGAAPASPETAPTPHPSTRAA
|
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
|
Q46Z04
|
Q23116
|
DEC12_CAEEL
|
Probable 2,4-dienoyl-CoA reductase decr-1.2 [(3E)-enoyl-CoA-producing]
|
Caenorhabditis
|
MACKNPKKFFPIRKSPVLRDGAFKGKLVLVTGGGTGIGKAIATTFAHLRATVVIAARRMEKLEQTARDITKITGGTCEPFQMDIKDPGMVSDAFDKIDMKFGKVPEILVNNAAGNFIMATELLSSNAYGTIIDIVLKGTFNVTTELGKRCIQNKTGASITSITAGYARAGAPFIVPSAVSKAGVETMTKSLATEWSKYGLRFNAVSPGPIPTKGAWGRLNSGEMGDIAEKMKFLNPEGRVGSPEEVANLVAFISSDHMSFLNGAIIDLDGGQQHFNHGSHMGDFLHSWDHKNWEDAENLIRGRTGKEKA
|
Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
|
Q23116
|
Q9K1H0
|
BAMA_NEIMB
|
Outer membrane protein Omp85
|
Neisseria
|
MKLKQIASALMMLGISPLALADFTIQDIRVEGLQRTEPSTVFNYLPVKVGDTYNDTHGSAIIKSLYATGFFDDVRVETADGQLLLTVIERPTIGSLNITGAKMLQNDAIKKNLESFGLAQSQYFNQATLNQAVAGLKEEYLGRGKLNIQITPKVTKLARNRVDIDITIDEGKSAKITDIEFEGNQVYSDRKLMRQMSLTEGGIWTWLTRSNQFNEQKFAQDMEKVTDFYQNNGYFDFRILDTDIQTNEDKTKQTIKITVHEGGRFRWGKVSIEGDTNEVPKAELEKLLTMKPGKWYERQQMTAVLGEIQNRMGSAGYAYSEISVQPLPNAETKTVDFVLHIEPGRKIYVNEIHITGNNKTRDEVVRRELRQMESAPYDTSKLQRSKERVELLGYFDNVQFDAVPLAGTPDKVDLNMSLTERSTGSLDLSAGWVQDTGLVMSAGVSQDNLFGTGKSAALRASRSKTTLNGSLSFTDPYFTADGVSLGYDVYGKAFDPRKASTSIKQYKTTTAGAGIRMSVPVTEYDRVNFGLVAEHLTVNTYNKAPKHYADFIKKYGKTDGTDGSFKGWLYKGTVGWGRNKTDSALWPTRGYLTGVNAEIALPGSKLQYYSATHNQTWFFPLSKTFTLMLGGEVGIAGGYGRTKEIPFFENFYGGGLGSVRGYESGTLGPKVYDEYGEKISYGGNKKANVSAELLFPMPGAKDARTVRLSLFADAGSVWDGKTYDDNSSSATGGRVQNIYGAGNTHKSTFTNELRYSAGGAVTWLSPLGPMKFSYAYPLKKKPEDEIQRFQFQLGTTF
|
Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
|
Q9K1H0
|
Q8ZAM2
|
TATA_YERPE
|
Sec-independent protein translocase protein TatA
|
Yersinia
|
MGSIGWAQLLIIAVIVVLLFGTNKLRTLGSDLGASIKGFKKAMGDDSQTPPTNVDKTSNDADFAKSITEKQQPVAKAEESKSHEKEQG
|
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. TatA could form the protein-conducting channel of the Tat system.
|
Q8ZAM2
|
A1KRT0
|
NUOH_NEIMF
|
NDH-1 subunit H
|
Neisseria
|
MIMQEWFQNLFAATLGLGDLGITVGLVVSVIVKIVIILIPLILTVAYLTYFERKVIGFMQLRVGPNVTGPWGLIQPFADVFKLLFKEVTRPKLSNKALFYIGPIMSLAPSFAAWAVIPFNEEWVLTNINIGLLYILMITSLSVYGVIIAGWASNSKYSFLGAMRASAQSISYEIAMSAALVCVVMVSGSMNFSDIVAAQAKGIAGGSVFSWNWLPLFPIFIVYLISAVAETNRAPFDVAEGESEIVAGHHVEYSGFAFALFFLAEYIFMILIAALTSLMFLGGWLSPFPQSWGFIGTPSAFWMFVKMAAVLYWYLWIRATFPRYRYDQIMRLGWKVLIPIGFAYIVILGVWMISPLNLWK
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
|
A1KRT0
|
A5G7Z5
|
TRMD_GEOUR
|
tRNA [GM37] methyltransferase
|
Geotalea
|
MKFDILTLFPAMFDGPLTESILKRAAEKGLIEVKLHNIRDFAFDRHSVTDDYPYGGGAGMVMKVEPLAACIEHAKVGSPRARVILTTPRGRSFNHAVAEELAREEALIIICGRYEGVDERVRELFVDDEISIGDFVLTGGEMAAMVLVDAVSRFVPGVLGSDESAVNDSFADGLLEYPQYTRPAEFRGLGVPSVLLSGNHQEIAKWRRRQSLGRTAASRPDLLTDAHLSASDREYLEELQRVAGSDG
|
Specifically methylates guanosine-37 in various tRNAs.
|
A5G7Z5
|
Q8JFY9
|
ENDUA_XENLA
|
XendoU-A
|
Xenopus
|
MASNRGQLNHELSKLFNELWDADQNRMKSGKDYRISLQGKAGYVPAGSNQARDSASFPLFQFVDEEKLKSRKTFATFISLLDNYEMDTGVAEVVTPEEIAENNNFLDAILETKVMKMAHDYLVRKNQAKPTRNDFKVQLYNIWFQLYSRAPGSRPDSCGFEHVFVGESKRGQEMMGLHNWVQFYLQEKRKNIDYKGYVARQNKSRPDEDDQVLNLQFNWKEMVKPVGSSFIGVSPEFEFALYTIVFLASQEKMSREVVRLEEYELQIVVNRHGRYIGTAYPVLLSTNNPDLY
|
Poly(U)-specific endoribonuclease involved in the processing of intron-encoded box C/D snoRNAs, such as U16 and U86. Releases products that have 2',3'-cyclic phosphate termini at the 3'-end.
|
Q8JFY9
|
Q9A5V1
|
HISX_CAUVC
|
Histidinol dehydrogenase
|
Caulobacter
|
MRRFLFSDPDFQTAFKAFLDERRGSPADVDAAVAGVLEAVRTQGIEALLDYSRRFDKVDLTAETIRVTAEEIEAGAAETPADVREAIAFAAARIRAYHSRQRPADQAWTDEAGVELGWRWTPLEAVGVYVPGGRAAYPSTVLMNAVPAQVAGVDRIAMVTPPGKLQPAVLAAAKEAGVTEIWRVGGAQAVAALAYGAGPIQPVDKIVGPGNAYVTAAKRRLYGVVGIDALAGPSEIVVVADNKNNPDWIAADLLSQAEHDPAAQSILITDDEAFAAAVEQAIAERLKTLATGEDAAASWRDHGAVIIAPLDESPALVDAIAPEHVEFALDNPERLSDRVRHAGAIFLGRVTPEAIGDYVAGSNHVLPTSRAARFQSGLSIYDFIKRTSIVKCDPASFAVLGPHTVALAKAEGLPAHALSASVRLPSGD
|
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
|
Q9A5V1
|
Q821L7
|
DER_CHLCV
|
GTP-binding protein EngA
|
Chlamydia
|
MLRIAILGRPNVGKSSLFNRMCKRSLAIVNSQEGTTRDRLYGEIRGWSVPVQVIDTGGVDKDSEDHFQKHIYKQALAGANEADILLLVVDIRCGITEQDAELAKMLLPLNKPLILVANKADTFKDEHRIHELYKLGISEILAVSASHDKHIDKLLQRIKTLGNVPEVVEEFSEEEVEEEAVPSMELLSKEPLSDYEEEEIPFSTTSAPDKPLKIALIGRPNVGKSSIINGLLNEERCIIDNVPGTTRDNVDILYSHNDRSYLFIDTAGLRKMKSVKNSIEWISSSRTEKAIARADVCLLVIDAQHHLSSYDKRILSLISKHKKPHIILVNKWDLIEGVRMEHYIRDLRATDVYIGQSRILCISAATKRNLRHIFSSIDELYETVSSKVPTPVVNKTLASTLQKHHPQVINGRRLRIYYAIHKTATPFQFLLFINAKSLLTKHYECYLRNTLKSSFNLYGIPFDLEFKEKTKRTN
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
Q821L7
|
B3EP63
|
EFTU_CHLPB
|
Elongation factor Tu
|
Chlorobium
|
MAKEAYKRDKPHVNIGTIGHVDHGKTTLTAAITSVLAKAGNAEMREFGDIDKAPEERERGITISTAHVEYQTEKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVAGTDGPMPQTREHILLARQVNVPALVVFLNKVDIADPELLELVELELRELLTEYDFPGDDIPIIKGSALKALEGDAEAEKAIMELMDAVDDYIPEPVRDVDKPFLMPVEDVFSISGRGTVGTGRIERGVVKINEEVELVGIKPTKKTVVTGIEMFQKILDQGQAGDNAGLLFRGVGKDEIERGMVVAKPGTITPHTKFKAEVYILKKEEGGRHTPFFNNYRPQFYFRTTDVTGAVTLPEGVEMVMPGDNLSIEVELIVPIAMDENLRFAIREGGRTVGAGTVTQIIE
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
B3EP63
|
Q0KCP3
|
UREG_CUPNH
|
Urease accessory protein UreG
|
Cupriavidus
|
MTQARTKKNPPLRVGVGGPVGSGKTTLLEMLCKAMRDRYDLVAITNDIYTKEDQRLLTVSGALPAERIMGVETGGCPHTAIREDASINLEAVDRMLARFPDADVVFIESGGDNLAATFSPELSDLTIYVIDVAGGEKIPRKGGPGITKSDLLVINKTDLAPYVGASLEVMESDARKMRGARPFVMGSVKSGQGLDEVIRFIERQGMLGV
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
Q0KCP3
|
A1WMW4
|
LEPA_VEREI
|
Ribosomal back-translocase LepA
|
Verminephrobacter
|
MKHIRNFSIIAHIDHGKSTLADRLIERCGGLADRQMQAQVLDSMDLEKERGITIKAQTAALQYQARDGQVYQLNLIDTPGHVDFSYEVSRSLSACEGALLVVDASQGVEAQTVANCYTALELGVEVVPVLNKMDLPNADPDNAKAEIEDVIGIDATDAIPCSAKTGMGIDDILQAIVAKVPAPRGQADGPLRAMIIDSWFDSYVGVVMLVRVVDGRLLKGERIKMMASGAVYNADGLGVFTPANEPRDALAAGQVGYVIAGIKELQAAKVGDTITLEKKLPNNAGPAAQALPGFKEIQPQVFAGLYPTEASAYDSLRDALEKLKLNDASLHYEPEVSQALGFGFRCGFLGLLHMEIVQERLEREFDQDLITTAPSVVYQVVKADGQVLMVENPSKMPDQGRLSEIREPIVTVHLYMPQDYVGPVMTLANQKRGVQMNMAYHGRQVMLTYDMPLGEIVLDFFDKLKSVSRGYASMDYTFKEYRASDVVKVDILLNGDKVDALSIIVHRSQSQHRGRAVVAKMREIISRQMYDVAIQAAIGANIIARETIKALRKNVLAKCYGGDITRKRKLLEKQKAGKKRMKQIGSVEVPQEAFLAILQVQE
|
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
|
A1WMW4
|
B8I2Q5
|
MUTS_RUMCH
|
DNA mismatch repair protein MutS
|
Ruminiclostridium
|
MGTVTPMMQQYLDIKEQYKDCILFFRLGDFYEMFFSDAELASRELEITLTGRDCGLEERAPMCGVPFHAADNYIARLVSKGYKVAICEQVEDPALAKGIVKRDVVKVVTPGTVTDITMLDERKNNYLMSVYKNGNFYGLASVDITTGDFYATRITWGNTRGKLLDEIAKYLPSEIIVNNELNSDNELTSEIKQRFNTYVSTFEETSFEYGNSMDILANHFEKQTLNIQEYDIAVNASGALLKYLESTQKVNLSHIQKFNSYALEEYMILDASSRRNLELTETMREKSKKGSLLWVLDKTMTSMGGRLLRKWIEQPLINHGDISLRLDAVEELKNKFMVRVEARELLKRVYDIERLMGKVVLGSVNCRDLIALKNSMCQIPYIKSLLNGFEAEYIKNCGEQLDCLEDVCNLIEVSIIDEPPVTIKEGGIIKDGYNPEVDKLRMASIQGKDWIAALEASQREKTGIKNLKVGFNRVFGYYIEVTKSYFSLVPEEYIRKQTLSNCERYITPELKEIEDTILGAEEKIIQLEYSLFVEIKEKIAEQLSRIKSTARALAEIDVLASLAEVADREGYCKPEVSLSDKIEIIEGRHPVVEKMTDKSGFVPNDTVLDMEEDRLAIITGPNMAGKSTYMRQTALIVLMAQIGSFVPAATAKIGLVDRIFTRVGASDDLASGQSTFMVEMSEVANILINATKRSLLVLDEIGRGTSTFDGLSIAWAVIEYIVNKEQLGCRTLFATHYHELTELEGKLPGIKNYCITVKEKGEDVIFLRKIIRGGADGSYGIQVAKLAGVPQSVIDRAKEILSNLDDADINRSGKARRIKKQVDGQLDLFAQAAKASADAEILEEIRKIDISRLTPIDSMNILYELQRKMNNRE
|
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.
|
B8I2Q5
|
Q97EW5
|
SYM_CLOAB
|
Methionyl-tRNA synthetase
|
Clostridium
|
MSEKKKFYITTPIYYPSAKLHIGNTYTTVASDALVRFKRLQGYDAFMLTGTDEHGQKIQRIAEDKGITPKAYVDEIVAGIKDLWKMMNISYDKFIRTTDEEHVKAVQKIVKKFYDNGDIYKSAYEGWYCTPCESFWTETQLVDGKCPDCGRPVEKTKEEAYFFKMSKYADRLIKYIEDHPDFIQPESRKNEMLNNFLKPGLQDLCISRSSFDWGIPITFDEKHVIYVWIDALSNYITALGYGSDNDELYNKFWPADLHLVGKDIIRFHTIYWPIMLMALDLPLPKQVFGHGWLLVDGGKMSKSKGNVVDPVVLINEFGTDPVRYYLLHEIPFGSDGLFNNEIFIKKINSDLANDLGNLVSRTAAMIEKYFDGSIQPPVDKEEIDNELIDMAISLPEKLDEDIKKLKIPEALDHIWDLIKRANKYIDETTPWVLAKDENKKARLGTVLYNLVESLRFVATTLTPFLPETGEKIKTQLNIELDTWESLSAFDGTRAGTKVSKGEVIFPRIDVDKKIEELNKLKEEQLKATRKMQPLKPEISIDDVDKLDLRVVKVLECEPVKKSKKLLKLKVELGGEERQVLSGISQFYKPEDLIGKKVVLVANLKPAKLMGQLSQGMILAVATDDDSKLYTLDIPEDIPTGSIVR
|
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
|
Q97EW5
|
C0HL11
|
B1OKD_NIDOK
|
Brevinin-1OKd
|
Nidirana
|
FLGSIIGALAKGLPSLIALIKK
|
Antimicrobial peptide.
|
C0HL11
|
Q8W491
|
U73B3_ARATH
|
Flavonol 3-O-glucosyltransferase UGT73B3
|
Arabidopsis
|
MSSDPHRKLHVVFFPFMAYGHMIPTLDMAKLFSSRGAKSTILTTPLNSKIFQKPIERFKNLNPSFEIDIQIFDFPCVDLGLPEGCENVDFFTSNNNDDRQYLTLKFFKSTRFFKDQLEKLLETTRPDCLIADMFFPWATEAAEKFNVPRLVFHGTGYFSLCSEYCIRVHNPQNIVASRYEPFVIPDLPGNIVITQEQIADRDEESEMGKFMIEVKESDVKSSGVIVNSFYELEPDYADFYKSVVLKRAWHIGPLSVYNRGFEEKAERGKKASINEVECLKWLDSKKPDSVIYISFGSVACFKNEQLFEIAAGLETSGANFIWVVRKNIGIEKEEWLPEGFEERVKGKGMIIRGWAPQVLILDHQATCGFVTHCGWNSLLEGVAAGLPMVTWPVAAEQFYNEKLVTQVLRTGVSVGAKKNVRTTGDFISREKVVKAVREVLVGEEADERRERAKKLAEMAKAAVEGGSSFNDLNSFIEEFTS
|
Possesses quercetin 3-O-glucosyltransferase activity in vitro. Also active in vitro on benzoates and benzoate derivatives. Involved in stress or defense responses.
|
Q8W491
|
Q603L1
|
AROE_METCA
|
Shikimate dehydrogenase (NADP(+))
|
Methylococcus
|
MTQPDRYAVFGHPIEHSQSPRIHALFAAQTGQDLIYTAEDVPPDRFESCVRAFFDGGGRGLNCTIPLKEMAWLLADSRSGRAKRARAVNTLLLRADGSIFGDNTDGIGLLRDLRDNLGLNLAGTKILILGAGGATRGILAPLLAERPDRLVIANRTVATAETLTVEFGDLGPVEGCGFAALAGRRFDLIINATAASLSGELPPLPADILAPGGSCYDLAYAAEPTPFVRWGQEKQAVVSADGIGMLVEQAAEAFLLWRGVRPQTRPVIETLEAERRTAK
|
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
|
Q603L1
|
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