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
|
|---|---|---|---|---|---|---|
Q7TUG0
|
TGT_PROMP
|
tRNA-guanine transglycosylase
|
Prochlorococcus
|
MFEFEIKSNCSNTEARTGIFHTPNGQVNTPRFMPVGTLATVKGISSEQLISTGSEMILSNTFHLHLQPGEKLVKESGGIHKFMNWDKPILTDSGGYQVFSLAKLNNISDKGVEFRNPRDGSHVFLSPEKVMQIQMDLGSDVAMAFDHCPPHTANENDIEDSLERTHSWLQKCVETHQKSNQALFGIVQGGKYPRLREHSAKFTSSFDLPGIAVGGVSVGEAVEEIHSVINNVPKFLPINKPRYLMGIGSLREISLAVAKGFDIFDCVLPTRLGRHGTAFFNDERWNIRNARFKNDFSPIDKTCKCETCKSYSRAYLHHLVRNDEILGLTLISLHNISHLIRFTNAISAAIKDNCFTIDFAPWKRSSIAHHTW
|
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).
|
Q7TUG0
|
A0LJZ7
|
Y2066_SYNFM
|
Nucleotide-binding protein Sfum_2066
|
Syntrophobacter
|
MHVVVVTGLSGSGKSTAIKAFEDLDYFCIDNLPVPMLPEFLALCEKDMPDIHKIALGIDIRERKFLKDYAKIFQDLEESGYRFEIIFLEAATDTLQRRYSQTRRVHPAASSQSLLVDAIHQEREQLRALRSRATRIIDTGTLSVHQLKAMITRTYSMIGDTELLSIQVLSFGFKYGLPFEADMVMDVRFLPNPYFVEALKNLDGRSEEVSSWVLRWTATREFVEEYGALLLKLIPLYIREGKRYLTVAAGCTGGKHRSVVIAERIAGTLRDHNYFVNVFHRDLHLE
|
Displays ATPase and GTPase activities.
|
A0LJZ7
|
A4JCH1
|
SERC_BURVG
|
Phosphohydroxythreonine aminotransferase
|
Burkholderia cepacia complex
|
MRVFNFSAGPAALPEEVLRQAADEMLDWHGSGMSVMEMSHRGKEFMSIHETALADLRELLDVPASHRILFLQGGGIAENAIVPMNLLGWRKSADFVVTGSWSQKSFNEAKKYCTPHLAASGKTADGFTRAPTRAEWQLSDDPAYVHLCTNETIDGVETFEIPDLGDVPLVADVSSHILSRPMDVAKYGVLFGGAQKNIGMAGVTVVIVREDLLDRALSICPSAFEWKTVAENNSLYNTPPTYAIYIAGLVFQWLKRQGGLAAIEARNIEKAKLLYDTIDASGFYLNKVEPAVRSRMNVPFFLADETRNEDFLAGAKARGLLQLKGHKSVGGMRASIYNAVPLEGVKALVEYMKDFERRDA
|
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
|
A4JCH1
|
Q42693
|
RUBB_CHLRE
|
CPN-60 beta-1
|
Chlamydomonas
|
KSGMEKTVQELVKELRKMSSVVQTDKDLANVACVSAGGNTDIGSLISDAMAKVGRTGVVTMEEGKTAEDQLVFVEGMQFERGYTSPYFVTDPERMICEYENCKILLVDKKISTARDIITILESAIRGNYPLLIMAEEVEQEALATLVVNKLRGTLKVVAIKAPGFGERRSSYLEDIAILTGGTVVGDEMGVSLEQATDAVLGTAAKITITKERTTVVGDGSTAADVAARVKQIRNLQMQTDQDYEREKLQERIARLSGGVAIIQVGAQTETELKEKKLRVEDALNATRAAVEEGVVPGGGCTLLRLSEKVDVIKRRMTDPEQQMGADIIKRALCYPIKLIAQNAGVNGSVVMNEVMKNLDRPHYGYNAATDSFENLMETGIIDPSKVVRCSMENAVSVAKTFLLADVVVTELKEIEAGAKPNPVAPGAAGFGGGL
|
This protein binds RuBisCO small and large subunits and is implicated in the assembly of the enzyme oligomer.
|
Q42693
|
P21642
|
PCKGM_CHICK
|
Phosphoenolpyruvate carboxykinase [GTP], mitochondrial
|
Gallus
|
MFWLRGGAQSCRGGETEDRMQRGMWGVGLARRRLSTSLSALPAAARDFVEEAVRLCRPREVLLCDGSEEEGKELLRGLQDDGVLHPLPKYDNCWLARTDPRDVARVESKTVLVTPEQSDAVPPPPPSGGPPQLGNWMSPNAFQAAVQERFPGCMAGRPLYVIPFSMGPPTSPLAKLGVQVTDSPYVVLSMRIMTRVGPAVLQRLDDDFVRCLHSVGRPLPLTEPLVSSWPCDRSPVLVAHIPSERRIVSFGSGYGGNSLLGKKCFALRIASRMAQQQGWLAEHMLILGVTSPSGEKRYMAAAFPSACGKTNLAMMTPSLPGWRIHCVGDDIAWMKFDDEGRLRAINPERGFFGVAPGTSSRTNPNAMATIARNTIFTNVGLRSDGGVYWDGLDEPTEPGVTYTSWLGKPWKHGDPEPCAHPNSRFCAPADQCPIMDPRWDDPEGVPIDAIIFGGRRPRGVPLVVEAFGWRHGVFMGSAMRSEATAAAEHKGGRLMHDPFAMRPFFGYNAGRYLEHWLSTGLRSNARLPRLFHVNWFLRDNEGRFVWPGFGHNARVLAWIFGRIQGRDTARPTPIGWVPKEGDLDLGGLPGVDYSQLFPMEKGFWEEECRQLREYYGENFGADLPRDVMAELEGLEERVRKM
|
Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. Facilitates the recycling of lactate carbon in the liver.
|
P21642
|
Q8RHX4
|
KAMA_FUSNN
|
KAM
|
Fusobacterium
|
MNTVNTRKKFFPNVTDEEWNDWTWQVKNRLESVEDLKKYVDLSEEETEGVVRTLETLRMAITPYYFSLIDLNSDRCPIRKQAIPTIQEIHQSDADLLDPLHEDEDSPVPGLTHRYPDRVLLLITDMCSMYCRHCTRRRFAGSSDDAMPMDRIDKAIEYIAKTPQVRDVLLSGGDALLVSDKKLESIIQKLRAIPHVEIIRIGSRTPVVLPQRITPELCNMLKKYHPIWLNTHFNHPQEVTPEAKKACEMLADAGVPLGNQTVLLRGINDSVPVMKRLVHDLVMMRVRPYYIYQCDLSMGLEHFRTPVSKGIEIIEGLRGHTSGYAVPTFVVDAPGGGGKTPVMPQYVISQSPHRVVLRNFEGVITTYTEPENYTHEPCYDEEKFEKMYEISGVYMLDEGLKMSLEPSHLARHERNKKRAEAEGKK
|
Catalyzes the interconversion of L-alpha-lysine and L-beta-lysine.
|
Q8RHX4
|
A2SGY5
|
LEXA_METPP
|
LexA repressor
|
Methylibium
|
MDDAPKLTARQQQILDLVQTSIERTGSPPTRAEIAAELGFRSANAAEEHLQALARKGVIELVGGTSRGIRLKSDTLRSLNQLRNKQFSLPLPSLSQLMLPLVGRVAAGSPILAQEHIDQSYAIEASMFPRRPDYLLKVRGMSMRDAGILDGDLLAVQKAREAKNGQIVVARLGDEVTVKRFRRVRGTIELLPENPDFEPIVVTPESGEFEIEGLAVGLIRNTLLM
|
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
|
A2SGY5
|
Q491X9
|
SECB_BLOPB
|
Protein-export protein SecB
|
Candidatus Blochmannia
|
MFFVLESNSNNVLFRIQRIYIKDISFEAPNTPGVFQINWNPKIKVDLNSDAKNIHIDMYEVVLCVTVTAKIEDDTAFLCQVKQAGIFNVSGLNKTQMIRCLKVHCPTILFPYASECVSNQVSRGTFPQLNLDPINFDILFIQSLQKKYNDTLKI
|
One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA.
|
Q491X9
|
Q3ZZP6
|
RPOA_DEHMC
|
Transcriptase subunit alpha
|
Dehalococcoides
|
MSDLAIPTISCTESDGKYGRFVVEPLEKGFGTTMGNSLRRILLSYLDGVAITRVRIDGIQHEFCALPKAKEDTLDFLLNLKNIRVESLSGLEGILYLRASGSKVVTAADIEPSNDFEVVNPELYLLTLDSDDAVLNVELEVELGRGYRPPESAENTPIGTIPVDAIFTPIRKVNFTTEPMHVGRETSLERLVLEVWTDGTVEPATAVSRSADILVKQFASLVSHSKVVAEIEASEPVKYTIPEEKYNMPIEQLDLSVRAVNCLRHAGITTVGEVINRGTKELLTLRNFGLKSLTELEDRLKTIGLSLNPEDELFEEAENNKKKNKGIDED
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q3ZZP6
|
Q13P97
|
PHNW2_PARXL
|
AEP transaminase 2
|
Paraburkholderia
|
MIPGNDPILLTPGPLTTSLRTREAMLRDWGSWDAAFNRMTHGVCADLLKIVHGENDYVCVPLQGSGTFAVEAALGTLVPRQGCVLVPNNGAYCARLIRILQRMGIAYIELVLREDEPVSAAAVEDAFNRHSRISHVAHVHLETSAGLLNPLDDIAAVCQRHGKSLIVDAMSSFGALPIDLRRGGIDALISASGKCLEGVPGMGFVIMRRSLLEDSEGRSPSLALDLHDQYVYMRKTTQWRFTPPTHVVAALREALDQFGAEGGQPARGARYARNCAALVGAMKALGFEPFLKPEVQAPVIVTFHAPRDPAWHFAAFYAAVREAGYVLYPGKLTQVETFRVGCIGAIDANELLNAAAAIGHALERLGIRVR
|
Involved in phosphonate degradation.
|
Q13P97
|
Q7MHH4
|
YDJC_VIBVY
|
Carbohydrate deacetylase
|
Vibrio
|
MKVIFNADDFGLTRGVNDGIVHAHLDGVVRSTTMMVGMPAEAHAVELANHLPELKVGLHLRFTAGRPLTEGQNLVGRDGDFTPYGQFWHRRDYDPIAIHNEAVAQVEYFLALGLNLSHIDSHHHAHTHPQFEPVIYDIARTYQVPLRSTGLAGEEEFGCRYHFTDHFYDKRVGHDSLIQHLLTLKEHYDVVEVMCHPAILDTALEACSGYAKQRELELAILTSDELKLSLRKHDIEVTDYSELIFAPLHSCV
|
Probably catalyzes the deacetylation of acetylated carbohydrates an important step in the degradation of oligosaccharides.
|
Q7MHH4
|
Q0G9X9
|
PSBK_DAUCA
|
Photosystem II reaction center protein K
|
Daucus sect. Daucus
|
MLNIFSLICICLNSAFYSSSLFFAKLPEAYAFLNPIVDLMPVIPLFFFLLAFVWQAAVSFR
|
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
|
Q0G9X9
|
P28250
|
ATPB_ANGLY
|
F-ATPase subunit beta
|
Angiopteris
|
MKTNPLVFVVSTAVEKNAGYITQIIGPVLDVAFSPGKLPNIYNSLIVKGQNPAGQEINVTCEVQQLLGNDRVRAVAMSATDGLMRGMKVIDTGAPLSVPVGEVTLGRIFNVLGEPVDNLGPVDAGTTSPIHKSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINQENISESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSASSGRMPSAVGYQPTLATEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHSDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLIETIKGFQMILSGELDSLPEQAFYLVGNIDEATAKAATLQVES
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
P28250
|
D4ARJ9
|
AMPP1_ARTBC
|
Prolidase
|
Trichophyton
|
MTIFRPHLRFLFKPHFLYFQSPIGKSSRPFSTSQILRTALDMPPPPVDTTQRLAKLRELMAQNKVDVYSMQFRYTIKAPLIITVVYSFFFFLLLALKLCLRKTAISQSTLLHVTGVETLIRITAAFISSFTGSAGCAIVSMSKAALSTDGRYFSQAAKQLDANWTLLKRGVEGVPTWEEWTAEQAENGKVVGVDPSLITAGENLQYSPLTSVIVVNCSYVIADARKLSQTLKTTGGSLIGIDQNLIDAVWGDERPARPANQITVQPVERAGKSFEEKVEDLRKELAAKKRSAMVISTLDEIAWLFNLRGSDIPYNPVFFSYAIVTPSVAELYVDESKLSPEARKHLEGKVILKPYDSIFQASKVLAESKASASSGSSGKFLLSNKASWSLSLALGGEQNVVEVRSPITDAKAIKNEVELEGFRKCHIRDGAALIEYFAWLENALIKEGAQLDEVDGADKLFEIRKKYDLFVGNSFDTISSTGANGATIHYKPEKSTCAVIDPEAMYLCDSGGQYLDGTTDTTRTLHFGEPTEFQKKAYALVLKGHISIDNAIFPKGTTGYAIDSFARQHLWKEGLDYLHGTGHGVGSFLYAEVPLSANNVLSNEPGYYEDGNFGIRLENLVICKEVQTAHKFGDKPFLGFESITLVPFCQKLLDASLLTEAERKWVNDYHARVWEKTSPFFEKDELTTAWLKRETQPI
|
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
|
D4ARJ9
|
Q8A9C1
|
DNLJ_BACTN
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Bacteroides
|
MDIKEKIEELRAELHRHNYNYYVLNAPEISDKEFDDKMRELQDLELAHPEYKDENSPTMRVGSDINKNFTQVAHKYPMLSLANTYSEGEVTDFYERVRKALNEDFEICCEMKYDGTSISLTYEDGKLVRAVTRGDGEKGDDVTDNVKTIRSIPLVLHGDNYPSSFEIRGEILMPWEVFEELNREKEAREEPLFANPRNAASGTLKLQNSSIVASRKLDAYLYYLLGDNLPCDGHYENLQEAAKWGFKISDLTRKCQTLEEVFEFINYWDVERKNLPVATDGIVLKVNSLRQQKNLGFTAKSPRWAIAYKFQAERALTRLNMVTYQVGRTGAVTPVANLDAVQLSGTVVKRASLHNADIIEGLDLHIGDMVYVEKGGEIIPKITGVDKDARSFMLGEKVRFITNCPECGSKLIRYEGEAAHYCPNETACPPQIKGKIEHFISRKAMNIDGLGPETVDMFYRLGLIHNTADLYELKADDIKGLDRMGEKSAENIITGIEQSKTVPFERVIFALGIRFVGETVAKKIAKSFGDIDELRQADLEKLISIDEIGEKIARSILLYFSNESNRELVGRLKEAGLQLYRTEEDMSGYTDKLAGQSIVISGVFTHHSRDEYKDLIEKNGGKNVGSISAKTSFILAGDNMGPAKLEKAKKLGVTILSEDEFLKLIS
|
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
|
Q8A9C1
|
P96715
|
YWQC_BACSU
|
Probable capsular polysaccharide biosynthesis protein YwqC
|
Bacillus
|
MGESTSLKEILSTLTKRILLIMIVTAAATAAGGLISFFALTPIYENSTQILVNQSKNERKEVQFNDVQTNLQLINTYNVIIKSPAILDEVIKEMGLSMTSQELNDKITVSSEQDSQVVNISVRDENAETAAHIANTIASVFQDKITSIMNVDNVSILSKAEVSEHPSPVSPKPLLNIAIAFAAGLAGSIGLAFLLEHLDNTIKSEEQLESLLDIPVLGTVSTIANEQKTAKTLQGFQSEKTGSGHFGA
|
Required for YwqD kinase activity. May bring YwqD and its substrates into contact. Probably involved in the regulation of capsular polysaccharide biosynthesis.
|
P96715
|
P68171
|
IDE3_ERYLA
|
Trypsin inhibitor DE-3
|
Erythrina
|
VLLDGNGEVVQNGGTYYLLPQVWAQGGGVQLAKTGEETCPLTVVQSPNELSDGKPIRIESRLRSTFIPDDDEVRIGFAYAPKCAPSPWWTVVEDEQEGLSVKLSEDESTQFDYPFKFEQVSDKLHSYKLLYCEGKHEKCASIGINRDQKGYRRLVVTEDNPLTVVLKKDESS
|
Inhibition of trypsin.
|
P68171
|
Q8NP12
|
ISPG_CORGL
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Corynebacterium
|
MLAPRRKTRQLMVGKVGVGSDHPISVQSMTTTKTHDINGTLQQIAQLTATGCDIVRVACPKTVDAEALPIIAKKSPIPVIADIHFQPKYIFAAIDAGCAAVRVNPGNIKEFDGRVKEVAKAAGDAGIPIRIGVNGGSLDKRILDKYHGKATPEALVESAMWEAGLFEEHGFGDIAISVKHSDPVLMVEAYRQLAEQSDYPLHLGVTEAGPKFMGTIKSSVAFGALLSQGIGDTIRVSLSADPVEEIKVGDQILQSLNLRPRKLEIVSCPSCGRAQVDVYSLAEEVTEALDGMEVPLRVAVMGCVVNGPGEARDADLGVASGNGKGQIFVKGEVIKTVPESQIVETLIEEAMRIAEEMDPEVLAAASASGMKAEVKVTK
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
Q8NP12
|
Q9Z6S3
|
TRMB_CHLPN
|
tRNA(m7G46)-methyltransferase
|
Chlamydia
|
MKPQDLSPPFLWKERRPCIQDGVLYVPRHYFEHQNFSTSYHQEFFQNHTSIACELCSGNGDWVVAQAQKDPQVLWIAVEQRFDRVRKIWSKMINHQIQNLRIVCGTAETFFQYYVPDQFLQRLVVNFPDPWPKMRHRKHRLLQPSFVQEISRSLQDSAVFALATDDKTYLLESIEALQTHLAPRMETPYYIKMTDTYGNSWFENLWRTKGQEIFYTEFIKKAGI
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
Q9Z6S3
|
Q5H7N6
|
CECP2_ASCSU
|
Cecropin-P2
|
Ascaris
|
MIFIYLLVQTAESSWLSKTYKKLENSAKKRISEGIAIAIQGGPRRRRFVVQQDTISPRLEVDERFLPNSVQEQI
|
Has antibacterial activity against several Gram-positive and Gram-negative bacteria. Is weakly active against yeasts. Acts by a nonpore mechanism.
|
Q5H7N6
|
B8D9J4
|
PYRG_BUCA5
|
UTP--ammonia ligase
|
Buchnera
|
MTKNYIFITGGVVSSLGKGIAAASLGAILKARNLNITIIKLDPYINVDPGTISPIQHGEVFVTEDGAETDLDLGHYERFIHTKMTFLNNFTTGGVYSQVLKKERRGDYLGATIQVIPHITNAIKERIILCSENSNIILVEIGGTVGDIESLPFLEAIRQMAVDIGRKNVIYIHLTLVPYIATAGEIKTKPTQHSVKQLLSIGIQPDILICRSEKTVPLHERKKIALFCNVPVDAVISLKDVNSIYKIPKLLKNQKLDDYICNYFKLNVPEADLQEWEEVIYAEKNFNNTIVIGIIGKYIKLPDAYKSVMEALKHAGFKNKIKVDIQLINSQEVENKNFQILKNLNGILIPGGFGDRGIVGKLLSIQYARENHIPYFGICLGMQIAIIEFAQNVVGIKEANSTEFDPQCKYPIIDLIKNRPNNSSKNYNKIENRINLGGTMRLGSQPCKLSANSLSRKLYNQEIIIERHRHRYEVNNLLFKKIEAAGLQVTGRSQKNNVVEIIELSNHPWFLACQFHPEFTSTPRDGHPLFIDFIKSAGKHKKNFI
|
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
|
B8D9J4
|
Q9X1I0
|
GLK_THEMA
|
Glucose kinase
|
Thermotoga
|
MPKLKLIGVDLGGTTFSVGLVSEDGKILKKVTRDTLVENGKEDVIRRIAETILEVSDGEEAPYVGIGSPGSIDRENGIVRFSPNFPDWHNVPLTDELAKRTGKKVFLENDANAFVLGEKWFGAGRGHDHIVALTLGTGIGGGVVTHGYLLTGRDGIGAELGHVVVEPNGPMCNCGTRGCLEAVASATAIRRFLREGYKKYHSSLVYKLAGSPEKADAKHLFDAARQGDRFALMIRDRVVDALARAVAGYIHIFNPEIVIIGGGISRAGEILFGPLREKVVDYIMPSFVGTYEVVASPLVEDAGILGAASIIKERIGG
|
Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ATP as the phosphate donor. Can also phosphorylate 2-deoxyglucose, with lower efficiency. ITP can also serve as a phosphoryl donor.
|
Q9X1I0
|
Q3APT3
|
TRPD_CHLCH
|
Anthranilate phosphoribosyltransferase
|
Chlorobium
|
MESKQLLQKLLAGEHCSKEEMQDCMNSIMDGEFSDSVIAALLALLQKKGVVANELAGAHASLMAHATTVALSTHAVDTCGTGGDHGGTYNISTTASLIACSAGVRVAKHGNRSVTSSCGSADVLEALGFTLELPPEATISLFKKTGFAFLFAPLYHPSMKRVAHIRRELGIRTLFNMLGPLLNPAQVKRQLVGVFSEELSELYADVLLQTGARHALIVHASTEEGVILDEPSLNGTTFVTEIEKGVVRKHTLRPEEFGIAPAPLAALQGGDKEHNARIIQSIADGSASAAQRDAALYSSAMACYVGGKCACLNDGFIVAKEALESGKTQAKLKEIIAYNQALVTEYHVAKS
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q3APT3
|
O23877
|
FENR3_ORYSJ
|
Ferredoxin--NADP reductase, embryo isozyme, chloroplastic
|
Oryza sativa
|
MASALGAQASVAAPIGAGGYGRSSSSKGSNTVNFCNKSWIGTTLAWESKALKSRHMNKIFSMSVQQASKSKVAVKPLELDNAKEPPLNLYKPKEPYTATIVSVERLVGPKAPGETCHIVIDHGGNVPYWEGQSYGVIPPGENPKKPGSPNTVRLYSIASTRYGDSFDGKTASLCVRRAVYYDPETGKEDPTKKGICSNFLCDSKPGDKVQITGPSGKIMLLPEDDPNATHIMIATGTGVAPYRGYLRRMFMEDVPSFKFGGLAWLFLGVANTDSLLYDEEFTNYLQQYPDNFRYDKALSREQKNKNGGKMYVQDKIEEYSDEIFKLLDGGAHIYFCGLKGMMPGIQDTLKRVAEQRGESWEQKLSQLKKNKQWHVEVY
|
May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. Is involved in nitrate assimilation.
|
O23877
|
A7Z4B0
|
CTAA_BACVZ
|
Cytochrome aa3-controlling protein
|
Bacillus amyloliquefaciens group
|
MNKALKALGVLTTFVMLVVLIGGALVTKTGSGLGCGRQWPLCHGRFFPELNAASIIEWSHRLASGVSIVLVLSLAFWAWRKVTPVFRETTFLAIMSIIFLFLQALLGALAVVFGSNALVMALHFGISLISFASVLILTLLIFEADKSDKKLVKPLRIGRKMQFHMIGLSIYTYIVVYTGAYVRHTKSSLACPDVPLCSRLNHGLPSHFQEWVQMGHRTAALLLFVWILVAFAHAVRSYKDQKQILGGWIAALAFVVLQALSGIMVVYSEMATGFALAHSLFIAGLFGVLCYFLLLIARFRYESKQRNI
|
Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
|
A7Z4B0
|
P0DUF5
|
BRXL_BACCH
|
BREX protein BrxL
|
Bacillus cereus group
|
MEDLNIKLNAHFAGKVVRKDLTKKIKEGANVPVYVLEYLLGMYCATDDEKSMNDGVQMVKKILSDNFVRPDEAEKVKSKVKELGKYTVIDKIGVKLNDKKDIYEAEFSNLGLNGVPISSHYVKEFDKLLAGGIWCIVKMEYYFDEESKGTSPFSIESVTPIQMPNMDLEEMFEQRRQFSKEEWIDVLIRSTGMEPTQLEDTVKWHLLERMVPLVENNYNLCELGPRGTGKSHIYKEISPNSILVSGGQTTVANLFYNMSTRKIGLVGMWDTVAFDEVAGITFKDKDGIQIMKDYMASGSFARGREEKNASASMVFVGNINQSVDVLLKTSHLFDPFPEAMAYDSAFFDRMHYYLPGWEIPKMRPEFFTNEYGFITDYLAEFLREMRKRSFSDAIDKYFRLGNNLNQRDVIAVRKTVSGLIKLLYPNGEYIKEDVEEVLRYALIGRRRVKEQLKKIGGMEFYDVNFSYIDNESMNEEFVSVPEQGGGTLIPEGMNKPGHIYTVARGKTGMIGTYKLETEVVSGNGKFEKTGLNSDRDAKESIDTAFRFFKANNKNISGTISTTTKDYLMHIQDIHGVGLTGELSLAAFIALCSGALNKPVQSQMVVLGSISISGTINKVEELANVLQVCFDSGAKKILLPMVSAVDIPTVPPELFAKFQIGFYQSAEDAVFKALGVE
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BREX systems (bacteriophage exclusion) provide immunity against bacteriophage. Part of a type 1 BREX system. This system allows phage adsorption but prevents phage DNA replication, without degradation of the phage DNA. Methylation of bacterial DNA by PglX probably guides self/non-self discrimination. When the brxA-brxB-brxC-pglX and pglZ-brxL operons are transformed into a susceptible B.subtilis strain (BEST7003) they confer resistance to bacteriophages SPbeta, SP16, Zeta, phi3T and SP02 and partial protection to phages SP01 and SP82G (these include lytic and temperate phage). They do not protect against phages phi105, rho10 or rho14. Additionally confers a very slight reduction in efficiency of plasmid transformation.
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P0DUF5
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Q0VQ05
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CYSG_ALCBS
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Sirohydrochlorin ferrochelatase
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Alcanivorax
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MEFLPISWRLQGKVALLAGGGEVALRKGRLLHRSGAILTVVAPQVCDELLDIVVRSGGSCVVRAFESADLDGVALVICATDDRSTNAEIAKQAQQRGLPVNVVDDPSLGDFIFPAIVDRSPVLISISSSGASPVLARKLRAQLESTLPARWGRLADLMARFRQPLKDKLSNIGARRLFWEQTLDSPVVEKVLAGKDSEAEAMLAAAIESADATTLSRGEVYLVGAGPGDPDLLTFRALRLLQKADVVLYDRLVGKGIVDLARRDAELVYVGKARDKHALPQDNINELLVHYAKQGKKVCRLKGGDPFIFGRGGEEIDLIVAEGIDFQVVPGITAASGCASYAGIPLTHRDHAQSVRFVTGHRKDGSVDLDWKHLVSETETVVFYMGLVGLREICSQLIAHGRGGDTPIALVSRGTTNLQEVITGRLDQLPDDIEGREIHAPTLIIVGSVVSLHPKFGWFKP
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Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
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Q0VQ05
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B1MZK4
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MURC_LEUCK
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UDP-N-acetylmuramoyl-L-alanine synthetase
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Leuconostoc
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MTKTYYFIGIKGTGMGPLAQILHDQGNTVLGSDIDSYTYTQAPLEAAGIKILPFSADNVDRYADAIFVRGNAFNDDHVEVQRALTLGVKMISYPDAVQEQIAQTTSIAVAGAHGKTSTTGLLAHVVKNIAPTSYLIGDGTGRGVPNSQFFVVEADEYRRHFKDYAPDYAILTNIDFDHPDYYEDINDVTRAFSDFANHVKKDIFAWGDDPYLRLLQPKADVYYYGTNSEQDDFVATNIRKSTQGSHFDVVFRGQSLGEFSVPLFGQHSILNALSVIAVAYMEKMDLSLIKSFLMTYQGVKRRFSEKQIADITVIDDYAHHPTEIDATLDAARQKYPNKQIIAIFQPHTYSRVIAYKDEFAKSLEAADKVYLANIFGSAREKQGAVTSAEIGAEISKFGGIIEEDNMSLLMPYENAVMVFMGAGDIEKYEFAYEKLLGQLRTDLQ
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Cell wall formation.
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B1MZK4
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B3PEB5
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DCD_CELJU
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Deoxycytidine triphosphate deaminase
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Cellvibrio
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MSIKSDKWMRRMVEQYGMIEPYEPGQVRYDAAGHKIVSYGTSSYGYDVRCADEFKIFTNVHSTVVDPKNFDEKSFVDIKSDVCIIPPNSFALARTVEYFRIPRSILTVCLGKSTYARCGIIVNVTPLEPEWEGHVTLEFSNTTPLPAKIYANEGVAQMLFFESDEICETSYRDRGGKYQGQRGVTLPRT
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Catalyzes the deamination of dCTP to dUTP.
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B3PEB5
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Q8TFM9
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RLA2_FUSCU
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60S acidic ribosomal protein P2
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Fusarium
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MKHLAAYLLLGLGGNTSPSAADVKAVLTSVGIDADEDRLNKLISELEGKDIQQLIAEGSEKLASVPSGGAGGASGGAAAAGGAAEEAKEEEKEEEKEESDEDMGFGLFD
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Plays an important role in the elongation step of protein synthesis.
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Q8TFM9
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Q9UHR5
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S30BP_HUMAN
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Transcriptional regulator protein HCNGP
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Homo
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MAGKKNVLSSLAVYAEDSEPESDGEAGIEAVGSAAEEKGGLVSDAYGEDDFSRLGGDEDGYEEEEDENSRQSEDDDSETEKPEADDPKDNTEAEKRDPQELVASFSERVRNMSPDEIKIPPEPPGRCSNHLQDKIQKLYERKIKEGMDMNYIIQRKKEFRNPSIYEKLIQFCAIDELGTNYPKDMFDPHGWSEDSYYEALAKAQKIEMDKLEKAKKERTKIEFVTGTKKGTTTNATSTTTTTASTAVADAQKRKSKWDSAIPVTTIAQPTILTTTATLPAVVTVTTSASGSKTTVISAVGTIVKKAKQ
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(Microbial infection) Involved in transcriptional repression of HHV-1 genes TK and gC.
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Q9UHR5
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B6YR45
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PURA_AZOPC
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IMP--aspartate ligase
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Candidatus Azobacteroides
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MKVSVLLGLQWGDEGKGKVVDVLTPKYDIVARFQGGPNAGHTLLFADRKYVLCSIPSGVFQGKVNIIGNGVVLDPILFKAETETLTSSCSNLVDKIYISRKAHLILPTHRLLDVAYETQKGNNKIGTTGKGIGPAYTDKVSRNGLRIGDIDYNFEEKYRYAIARHKELLHQMNFQYDLLPLEREWKKSIEVIKRFKRINSDNFINKALIGGRTVLAEGAQGTMLDVDFGSYPFVTSSNTICASACTGLGVAPAKIGDVFGIFKAYCTRVGSGPFPTELSDEIGEKLRNIGNEYGSITKRPRRCGWIDLVALRYAVMINGVTQLIMMKSDVLDTFDTVKACIAYEVNGQKMEDFPFEIGSSVKPIYTELVGWKTNMTKIKSENEFPKAFKDYLLFLEESLGVSIKIVSLGPDREQTIIRE
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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.
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B6YR45
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Q619V5
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GPA5_CAEBR
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Guanine nucleotide-binding protein alpha-5 subunit
|
Caenorhabditis
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MGIALCKPERDAAAKNRQIETQIRIENQANKRKIKMLLLGISDSGKSTIVKQMRVNYCNGFNETEVVNAIFLIRNNIIDAFKHISLLILDSHIIKSDTEKVLLKLFAFESQKIEMMQEVDELRLINSIRVLECISVFFEHYSYHPMIPDNIHYFFPHLERIAISEYMPTVEDLIHMRQTTLGVHEISFDYQTQTIRLIDVGGQKTERRKWIHFFEGVTAVMFVCSLSSFNQATEQEPNNAFAWETSLNKVQNKILVRSTGKAKQRPGMVNRLDESVDLFTSIRENNFLKSSNFMLFLNKIDLLGKKLETIQFVNHFPAYEQWITNDNSVQSVAEFIESMFREGLDADQKIYAHLTQATITTNIEYTFGLCCDVIFNKNIETLSLE
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Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
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Q619V5
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Q2H731
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EIF3C_CHAGB
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Translation initiation factor eIF3, p93 subunit homolog
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Chaetomium
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MSRFFRGGDDSSSESSSDEEELYSTSEEEEEEDQDQEESSEEEDEEESSDEDEGPKKTGLSRFLVDQASSDSEGSDEEGATKVKSAKDKRFDELEATITTIQNRQKIDDWGSIANEFDKLNRQVVKLQDGGKAPKSYIKCIAELEDFLNETLAKQKVTPKNKKLNATNARGLNAVKQRIKKNNKDYQAQIDAFRKDSDDFMESDEEEVPAPKTKVRFQEAAAPEEAAEDEDKGFARVDKRGKAIPFSPESIQKHLRAIVESRGRKNTDRGEQIKIMEELNKVAETPYLKIRVLQTLVSARFDLGSGTTTSMPLDHWKAAERELAALLTLLETHKDHVVIEGAEEWEDDDKTPILGPDDKYIKVPGSVVSYIERLDDELTRSLQSIDPHTSEYIERLTDEASLYNIILQGLLYYETIRKDASLEIPQESLNRIIQRRLDHVYFKPAQVVKILEENAWKQVSSGVDSAITPRGASGDAGKLMYTLCNYLFDNSEGIIRARAMLSQIYFLALHDEYYKARDMMLTSHLQESIANFDVATQILYNRTLVQVGLCAFRRGLVYDAQNTLQDICGSGRQKELLAQGVMMQRYNQVTPEQERLEKQRQLPFHMHINLELLECVYLTCSMLLEIPLLAQIGSSPDIKKRVISKTYRRMLEYHERQIFTGPPENTRDHVMQASKALAAGEWKKATHFIHSIKIWDLMPSSEEIKAMLAKQIQEEGLRTYLFTYAPFYDTLAIETLSTMFELDSVKVSAVVSKMISHEELAAALDQVTKTVIFRKGVELSRLQSLALALSDKASALIETNERTLEVRTQGSANAFSRKDGRQGGQRGGGQRSGRGGARAGGNAQRQAGGTQFTGGALGAAVRG
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Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
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Q2H731
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Q9D554
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SF3A3_MOUSE
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Spliceosome-associated protein 61
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Mus
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METILEQQRRYHEEKERLMDVMAKEMLTKKSTLRDQINSDHRTRAMQDRYMEVSGNLRDLYDDKDGLRKEELNAISGPNEFAEFYNRLKQIKEFHRKHPNEICVPMSVEFEELLKARENPSEEAQNLVEFTDEEGYGRYLDLHDCYLKYINLKASEKLDYITYLSIFDQLFDIPKERKNAEYKRYLEMLLEYLQDYTDRVKPLQDQNELFGKIQTDFEKKWDNGTFPGWPKETSSALTHAGAHLDLSAFSSWEELASLGLDRLKSALLALGLKCGGTLEERAQRLFSTKGKSLESLDTSLFAKNPKSKGTKRDTERNKDIAFLEAQIYEYVEILGEQRQLTHENVQRKQARTGEEREEEEEEQISESESEDEENEIIYNPKNLPLGWDGKPIPYWLYKLHGLNINYNCEICGNYTYRGPKAFQRHFAEWRHAHGMRCLGIPNTAHFANVTQIEDAVSLWAKLKLQKASERWQPDTEEEYEDSSGNVVNKKTYEDLKRQGLL
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Involved in pre-mRNA splicing as a component of the splicing factor SF3A complex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex. Involved in pre-mRNA splicing as a component of pre-catalytic spliceosome 'B' complexes.
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Q9D554
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Q969Y2
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GTPB3_HUMAN
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Mitochondrial GTP-binding protein 1
|
Homo
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MWRGLWTLAAQAARGPRRLCTRRSSGAPAPGSGATIFALSSGQGRCGIAVIRTSGPASGHALRILTAPRDLPLARHASLRLLSDPRSGEPLDRALVLWFPGPQSFTGEDCVEFHVHGGPAVVSGVLQALGSVPGLRPAEAGEFTRRAFANGKLNLTEVEGLADLIHAETEAQRRQALRQLDGELGHLCRGWAETLTKALAHVEAYIDFGEDDNLEEGVLEQADIEVRALQVALGAHLRDARRGQRLRSGVHVVVTGPPNAGKSSLVNLLSRKPVSIVSPEPGTTRDVLETPVDLAGFPVLLSDTAGLREGVGPVEQEGVRRARERLEQADLILAMLDASDLASPSSCNFLATVVASVGAQSPSDSSQRLLLVLNKSDLLSPEGPGPGPDLPPHLLLSCLTGEGLDGLLEALRKELAAVCGDPSTDPPLLTRARHQHHLQGCLDALGHYKQSKDLALAAEALRVARGHLTRLTGGGGTEEILDIIFQDFCVGK
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GTPase involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
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Q969Y2
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B8E240
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EFP_DICTD
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Elongation factor P
|
Dictyoglomus
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MISVNDFYPGLTIELEGEIYIVLEYQHVHMAQGQATVRVKLKNLKTGNVIRKTFKSDEYVPQAFINKREAEYLYKQGDEYYFIDNESFEQYILTEEQLGDAIKYLKEGNTVSVLFYEGNPIGIELPTTVVLEVVETDPGLRGDTVSGGSKPAKLETGLVIQVPLFIQIGDKVVVDTRYAKYVERA
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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.
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B8E240
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A2RVQ5
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AGL16_ARATH
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Agamous-like MADS-box protein AGL16
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Arabidopsis
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MGRGKIAIKRINNSTSRQVTFSKRRNGLLKKAKELAILCDAEVGVIIFSSTGRLYDFSSSSMKSVIERYSDAKGETSSENDPASEIQFWQKEAAILKRQLHNLQENHRQMMGEELSGLSVEALQNLENQLELSLRGVRMKKDQMLIEEIQVLNREGNLVHQENLDLHKKVNLMHQQNMELHEKVSEVEGVKIANKNSLLTNGLDMRDTSNEHVHLQLSQPQHDHETHSKAIQLNYFSFIA
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Probable transcription factor involved in the regulation of flowering time in long-day photoperiod. Participates in the repression of FT expression and floral transition, by interacting closely with the FLC-SVP pathways . Functions in the satellite meristemoid lineage of stomatal development .
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A2RVQ5
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B4UCW3
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MUTL_ANASK
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DNA mismatch repair protein MutL
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unclassified Anaeromyxobacter
|
MPRIHVLPPGLVNQIAAGEVVERPASIVKELVENALDAGATSVGVDVEEGGLALVRVADDGSGMDRDDALLALERHATSKLRDAEGLAAIGTMGFRGEAVPAIASVSRFRLDTSAGEDGAGTRVEIEGGVLGEVAPVARPRGTTVEVRDLFFNTPARRKFMRAASTEAGHVSEAVIRLALARPDVGFTLRSGGRLVLGARAGGGLADRAGQALGREAHRHLLPVDARRGEVRVHGLICSPDHSEATGRALYLFVNGRYVRDRAAAHAVLRAFAGTLPPGRHPAGVLFVELPLHRVDVNVHPQKLEVRFAEGREVFDALFHTVAGALRTAPWLRARPQPGDGVPVGDGGGPAPVPVAGEEAAEVLAWARAARPPEGSGATLVQPAPGAWATGRLAFPVVPAPGAGPEAGPRPEGYFAGLRYVGQHARTYLLCEAPGGTLVVIDQHASHERMLFHRLREAFRARRIPVQPFLLPQVVTLPPAAARALEAGLAELGRLGFDAEPFGGEAFAVKGAPAALAGVDLTALLTDLGSQLAEVERGSAVDDAFHDLLATMACHAAVRANQDVSPEEARALLDGLDAIDFKARCPHGRPVVFELSLADLERRVGRR
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This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
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B4UCW3
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A6V681
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KYNB_PSEA7
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N-formylkynurenine formamidase
|
Pseudomonas
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MTSLRYWDISPALDPSTPTWPGDTPFQQEWAARLDEHCPVNVGRVTLSPHTGAHVDAPLHYRADGLAIGQVPLDVYMGPCRVLHCIGATPLVTPEHLAGQLDDLPPRVLLRTFERVPANWPEGFCAIAPTTVECLAERGVRLIGIDTPSLDPQHSKTLDAHHAVGRHGMAILEGVVLDEVPAGDYELLALPLKFTHLDASPVRAVLRSLPTAE
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Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.
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A6V681
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Q9VP95
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SEMS_DROME
|
Seminase
|
Sophophora
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MKRLLFLFLLAGILINNHALQHNETIDLKKLAKIVLPPAYQTRVIGGRVTTNAKLGGYLVAMRYFNNFICGGTLIHELIVLTAAHCFEDRAEKEAWSVDGGISRLSEKGIRRQVKRFIKSAQFKMVTMNMDVAVVLLNRPMVGKNIGTLSLCSTALTPGQTMDVSGWGMTNPDDEGPGHMLRTVSVPVIEKRICREAYRESVSISDSMFCASVLGKKDACTYDSGGPLVYEKQVCGIVSFGIGCASRRYPGVYTDVHYVKPFIVKGIKALLSRSR
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Seminal fluid protease which is required for cleavage and probably also activation of the metalloprotease Semp1 . Also required for a number of female post-mating responses independent of Semp1 including egg laying and sperm usage .
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Q9VP95
|
P01044
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KNG1_BOVIN
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Kininogen-1 light chain
|
Bos
|
MKLITILFLCSRLLPSLTQESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITEVARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGECTATVAKRGNMKFSVAIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKEVKRAQRQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRISSFSQKCDLYPVKDFVQPPTRLCAGCPKPIPVDSPDLEEPLSHSIAKLNAEHDGAFYFKIDTVKKATVQVVAGLKYSIVFIARETTCSKGSNEELTKSCEINIHGQILHCDANVYVVPWEEKVYPTVNCQPLGQTSLMKRPPGFSPFRSVQVMKTEGSTTVSLPHSAMSPVQDEERDSGKEQGPTHGHGWDHGKQIKLHGLGLGHKHKHDQGHGHHGSHGLGHGHQKQHGLGHGHKHGHGHGKHKNKGKNNGKHYDWRTPYLASSYEDSTTSSAQTQEKTEETTLSSLAQPGVAITFPDFQDSDLIATVMPNTLPPHTESDDDWIPDIQTEPNSLAFKLISDFPETTSPKCPSRPWKPVNGVNPTVEMKESHDFDLVDALL
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The active peptide bradykinin is a potent vasodilatator that is released from HMW-kininogen shows a variety of physiological effects: (A) influence in smooth muscle contraction, (B) induction of hypotension, (C) natriuresis and diuresis, (D) decrease in blood glucose level, (E) it is a mediator of inflammation and causes (E1) increase in vascular permeability, (E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action).
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P01044
|
Q0BPL4
|
GLGC_GRABC
|
ADP-glucose synthase
|
Granulibacter
|
MSGTSSIARSTMAYVLAGGRGSRLLELTDTRAKPAVYFGGKSRIIDFALSNAVNSGIRRIGVATQYKAHSLIRHMQRGWNFFRPERNEGFDILPASQRVSETQWYEGTADAVYQNLDIIAGYEPEYMIILAGDHIYKMDYEIMLHQHVERQADVTVGCIEVPREEATGFGVMQVDDTGRITAFLEKPSDPPGMPGQPDIALASMGIYVFKTKFLFDVLRRDAADPDSKHDFGGDIIPDLVENGTAIAHRFSDSCVRSSKTAEAYWRDVGTLDSYWQANLDLTNVVPTLDLYDSGWPIWTYNEISPPAKFVYDDVGRRGMAVDSLVAGGCIVSGASLSRSLISTGCRVHSFSQLHGTVVLPYADIARSARLRNTVVDRGVRIPEGLVVGEDPELDAKRFRRTEKGICLITQPMIDRLG
|
Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
|
Q0BPL4
|
A3MTQ5
|
TRM1_PYRCJ
|
tRNA(m(2,2)G26)dimethyltransferase
|
Pyrobaculum
|
MDDYVIRREGKAVFYAPNPKKYDIYSAPVFYNPAMEKNRTLSVLLLKVAGAQMGGGLTVCEPLSGTGIRGIRYVIESGVVGKLILNDLSKEAVHVIQKNLSINGVEADVYNEDANVLLHKLRGQCDVVDVDPFGSPAPFLSAAFRALKNEGIVCATATDTAVLVGRYPRKCLRRYGSVIRKSPFYLEMGLRNLVGYVARIAASEDFAIRPLLSYWEGHYFRTCVYAVKSAKDADDMLQRDVGYVEYRRYRKVTRRQSEYTSGPVWIGELGDPSIAFFMAREGQYSDFLKLLEEEYSVSLPWFYKLPEFAVDGKSPTLEEAMAALRRAGVYAARTHMASDGFKAEATYGEVERVLRRVT
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Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
|
A3MTQ5
|
Q21DY7
|
UBIA_SACD2
|
4-HB polyprenyltransferase
|
Saccharophagus
|
MTATRKSTRPSKPLKATLVAYAKLMRLDRPIGIYLVLWPTLWSLWIAADGLPDWDVLVIFVLGVVLMRSAGCVINDFADRKIDGHVRRTANRPLVTGLITPKQAVLFFVALLVIAFILVLFTNPLTIKLSFGGALLAFCYPFMKRYTQLPQIVLGAAFAWSIPMAFAAQTNQLPEAIWVLYTAVVLWTVAYDTFYAMADREDDLKIGVKSTAILFGDQDRIITACLQLMALVAMAMAGERFGLGFSFKVSLLVAGGLFAYQQYLIRNREPNACFRAFLHNNWVGLVVFLGILVDKLITN
|
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
|
Q21DY7
|
Q91WU2
|
S22A7_MOUSE
|
Organic anion transporter 2
|
Mus
|
MGFEELLHKVGGFGPFQLRNLVLLALPRFLLPMHFLLPIFMAAVPAHHCALPDAPANLSHQDLWLKTHLPRETDGSFSSCLRFAYPQALPNVTLGTEVYNSGEPEGEPLTVPCSQGWEYDRSEFSSTIATEWDLVCEQRGLNKVTSTCFFIGVLLGAVVYGYLSDRFGRRRLLLVAYVSTLALGLMSAASVNYIMFVTTRMLTGSALAGFTIIVLPLELEWLDVEHRTVAGVISTTFWTGGVLLLTLVGYLIRSWRWLLLAATLPCVPGIISIWWVPESARWLLTQGRVEEAKKYLSICAKLNGRPISEDSLSQEALNKVITMERVSQRPSYLDLFRTSQLRHVSLCCMMMWFGVNFSYYGLTLDASGLGLTVYQTQLLFGAVEVPSKITVFFLVRLVGRRLTEAGMLLATALTFGISLLVSSDTKSWITALVVIGKAFSEAAFTTAYLFTSELYPTVLRQTGMGFTALIGRLGASLAPLVVLLDGVWLLLPKLAYGGISFLAACTVLLLPETKKAQLPETIQDVERKGRKIDRSGTELA
|
Mediates sodium-independent multispecific organic anion transport. High affinity transport of glutarate and prostaglandin E2 in a sodium-independent manner. Mediates also the uptake of alpha-ketoglutarate, p-aminohippuric acid, methotrexate, ochratoxin A, valproate, allopurinol and bumetanide.
|
Q91WU2
|
P43744
|
DPO3B_HAEIN
|
DNA polymerase III subunit beta
|
Haemophilus
|
MQFSISRENLLKPLQQVCGVLSNRPNIPVLNNVLLQIEDYRLTITGTDLEVELSSQTQLSSSSENGTFTIPAKKFLDICRTLSDDSEITVTFEQDRALVQSGRSRFTLATQPAEEYPNLTDWQSEVDFELPQNTLRRLIEATQFSMANQDARYFLNGMKFETEGNLLRTVATDGHRLAVCTISLEQELQNHSVILPRKGVLELVRLLETNDEPARLQIGTNNLRVHLKNTVFTSKLIDGRFPDYRRVLPRNATKIVEGNWEMLKQAFARASILSNERARSVRLSLKENQLKITASNTEHEEAEEIVDVNYNGEELEVGFNVTYILDVLNALKCNQVRMCLTDAFSSCLIENCEDSSCEYVIMPMRL
|
Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.
|
P43744
|
Q46Y89
|
MSBA_CUPPJ
|
Lipid A export ATP-binding/permease protein MsbA
|
Cupriavidus
|
MSNPAKSEQSAGHDVKVGKRLMGYLRPELRIFIAAILAMAVVAASEGVIPKVVNDLLDKGFGGEYAGKLWHVPAILTGVALIRGVAQFASGYLLSLISNRVLLKMRMQMFDRMLHAPAHFYHRNTAASLINAVIFEVNQVLSILTSVFITLVRDSLTVVALLIYLFYTNWRLTLIVSVILPVIGYLMSKINRRLRRLNRDHQTLTNSAAYVVEEAAGGYKVVKLHGGEAYEMNRFRNMADRLKNYSMRMAVAGGLNQPVTAFLAALALSVIITIAMIQAQGNQTTIGGFTGFVMAMLLLISPLKHLTDINQPLTRGLTAAELIFRLIDEPVEPQDGGVRLERAKGDLVFERVGFRYGEGTRPALEGIDIRVPAGEVVALVGPSGSGKTTLVNLVPRFFDPTDGRILLDGHAIGDIALRELRNQIAFVSQDVVLFNDTVAANVAYGARSEEEIDMARVERALQAAYLTEVVKNLPEGVNTNIGDNGMKLSGGQRQRLAIARAIYKDAPILILDEATSALDSESERQVQAALEALMVGRTTLVIAHRLSTIENADRIVVLDHGRVAEHGTHEELLAANGLYAGLHRIQFATH
|
Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
|
Q46Y89
|
Q31Q60
|
FOLD_SYNE7
|
Methenyltetrahydrofolate cyclohydrolase
|
Synechococcus
|
MAAAILDGRALAAQRRQQLREQVEAIAPAVGRRPGLAVIMVGDNPASAVYVRNKERACEQTGIVSFGKHLPGDSSEAEIRALIEELNQDDRVDGILVQLPLPSHLDAVPLLLAIDPEKDADGLHPLNLGRLLRGEEGLRSCTPAGVMELLAANQIDPAGKKAVVIGRSILVGKPLAMMLLEANATVTIAHSRTPNLPEVCRQADIVVAAVGRPELVGADWIKPGAVVVDVGINRLEDGRLVGDVDYEAASAITSWITPVPGGVGPMTVAMLLHNTVLSYCRRSGQPFLS
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
Q31Q60
|
Q8P244
|
SSRP_STRP8
|
Small protein B
|
Streptococcus
|
MAKGEGHILAQNKKARLDYHIVETVEAGIVLTGTEIKSVRAARIQLKDGFAQIKNGEAWLVNVHIAPFEQGNIWNADPERTRKLLLKKREITHLANELKGTGMTLVPLKVYLKDGFAKVLIGLAKGKHDYDKRETIKRRDQERDIKKQMKHYNAR
|
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
|
Q8P244
|
Q8ZVE0
|
DTDA_PYRAE
|
D-tyrosyl-tRNA(Tyr) deacylase
|
Pyrobaculum
|
MYVLVLSLGDPVSRTFLELHPMPLVETRGDIEVRKYGEIPAVVYKGEPTEFYREDILASLGKYAIFISRHEMSNPRPLFTVHTPGSWPDVSVANPRLASALFRALCKHAYEPFECAFEATHHAPNTSLVSATFIEVGSTEAEWRDKRAVGVLAQALEEALTKEFEGPTPTMAIGDLHYVTISDSVLRGEFDLGHVVPKYINITTNIVENILKKHTISIKKTIIFRKNIKNPIRTEIIELLRAKGIEVTLKG
|
D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
|
Q8ZVE0
|
O85041
|
CSOS2_HALNC
|
Carboxysome shell protein CsoS2B
|
Halothiobacillus
|
MPSQSGMNPADLSGLSGKELARARRAALSKQGKAAVSNKTASVNRSTKQAASSINTNQVRSSVNEVPTDYQMADQLCSTIDHADFGTESNRVRDLCRQRREALSTIGKKAAKTTGKPSGRVRPQQSVVHNDAMIENAGDTNQSSSTSLNNELSEICSIADDMPERFGSQAKTVRDICRARRQALSERGTRAVPPKPQSQGGPGRNGYQIDGYLDTALHGRDAAKRHREMLCQYGRGTAPSCKPTGRVKNSVQSGNAAPKKVETGHTLSGGSVTGTQVDRKSHVTGNEPGTCRAVTGTEYVGTEQFTSFCNTSPKPNATKVNVTTTARGRPVSGTEVSRTEKVTGNESGVCRNVTGTEYMSNEAHFSLCGTAAKPSQADKVMFGATARTHQVVSGSDEFRPSSVTGNESGAKRTITGSQYADEGLARLTINGAPAKVARTHTFAGSDVTGTEIGRSTRVTGDESGSCRSISGTEYLSNEQFQSFCDTKPQRSPFKVGQDRTNKGQSVTGNLVDRSELVTGNEPGSCSRVTGSQYGQSKICGGGVGKVRSMRTLRGTSVSGQQLDHAPKMSGDERGGCMPVTGNEYYGREHFEPFCTSTPEPEAQSTEQSLTCEGQIISGTSVDASDLVTGNEIGEQQLISGDAYVGAQQTGCLPTSPRFNQTGNVQSMGFKNTNQPEQNFAPGEVMPTDFSIQTPARSAQNRITGNDIAPSGRITGPGMLATGLITGTPEFRHAARELVGSPQPMAMAMANRNKAAQAPVVQPEVVATQEKPELVCAPRSDQMDRVSGEGKERCHITGDDWSVNKHITGTAGQWASGRNPSMRGNARVVETSAFANRNVPKPEKPGSKITGSSGNDTQGSLITYSGGARG
|
Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form without cargo protein. CsoS2 is essential for Cb formation and is also capable of targeting foreign proteins to the Cb. The Cb shell assembles with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms pseudohexamers that probably control metabolite flux into and out of the shell.
|
O85041
|
B0JWV0
|
ATPD_MICAN
|
F-type ATPase subunit delta
|
Microcystis
|
MQGSLISSEIAEPYAQALLSVAQSSGQLEAIGGEIKSLLELLENAPDLRAFIGNPVIKEEAKKAVLSQVMGSSANPYLTNFMMLLVDKRRIQFLEPVCQQYLTLARVLTNTVLAEVSSATELNDSQKQIVIDKVKTLTGANVVELKTKVDGSLIGGVVIKVGSQVFDASIRGQLQRLSLSLR
|
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
|
B0JWV0
|
C4L8Y1
|
RLME_TOLAT
|
rRNA (uridine-2'-O-)-methyltransferase
|
Tolumonas
|
MSKKKRTASSTRWLKEHFDDKYVQQAQKQGLRSRAVFKIDEIQQKDKLIKQGMTVVDLGAAPGGWSQFCVEQVGPHGRVIACDILPMDPIAGVDFLQGDFREEAVLSALLGRVGEQKVDIILSDMAPNMSGTPAVDQPRSMYLVELALEMCKQVLAAKGSFVVKVFQGAGFEEYLKEVRSLFSVVKIRKPDSSRSRSREVYIVATGFKL
|
Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
|
C4L8Y1
|
Q9WUF1
|
V1R49_MOUSE
|
Vomeronasal type-1 receptor B2
|
Mus
|
MSKANLLHTDNNMKIILFSEVSVGISANTILFFARLCKLLGENKPKPIDLYIAFLSLTQLMLLITMGLIAVDMFMPWGRWNSTTCQSLIYLHRLLRGLALSATCLLNVLWTITLSSRSSCLTKFKHKSPHHISGAFLFFYVLYMSFSSHVLVSIIVTPNLTSEDFMYVTQSCSLLPMSYSRESRFSTLMAIRETFLISLMALSSGYMVALLWRHKKQAQHLRSTSLSSKASPEQRATRTIMLLTSLFVVLYILERVVFQSRLKFKDCSVFYFVHIIMSHSYATVSPFVFICTEKHIIKFWESIFGRIVNI
|
Putative pheromone receptor implicated in the regulation of social and reproductive behavior.
|
Q9WUF1
|
B8ZUN6
|
Y563_MYCLB
|
Nucleotide-binding protein MLBr00563
|
Mycobacterium
|
MSGNNHPGDASAEIDVVLVTGLSGAGRGTAAKVLEDLGWYVADNLPPQLITWMVDFGLAAGSRITQLAVVMDVRSRGFTGDLDSVRRELATRNIIPRVVFMEASDDMLVRRYEQNRRSHPLQGEQTLAEGIAAERRMLAPVRATADLIIDTSALSVPGLRESIERAFGGDASATTSVTVESFGFKYGLPMDADIVMDVRFLPNPHWVDELRSLTGQHSAVRDYVLGQPGAAEFLRTYRRLLSLVVDGYRREGKRYMTVAIGCTGGKHRSVAIAEALMGLLQSDLQLSVRVLHRDLGRE
|
Displays ATPase and GTPase activities.
|
B8ZUN6
|
P20617
|
ANP8_MYOAE
|
Antifreeze peptide GS-8
|
Myoxocephalus
|
MDGETPAQKAARLAAAAAALAAKTAADAAAKAAAIAAAAA
|
Antifreeze proteins lower the blood freezing point.
|
P20617
|
P41204
|
RL16_MYCPN
|
50S ribosomal protein L16
|
Mycoplasma
|
MLQPKRTKYRKPHNVSYEGKAKGNSYVAFGEYGLVATKGNWIDARAIESARIAISKCLGKTGKMWIRIFPHMSKTKKPLEVRMGSGKGNPEFWVAVVKQGTVMFEVANIPESQMIKALTRAGHKLPVTWKILKREEVSA
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
P41204
|
P31109
|
SNC1_YEAST
|
Synaptobrevin homolog 1
|
Saccharomyces
|
MSSSTPFDPYALSEHDEERPQNVQSKSRTAELQAEIDDTVGIMRDNINKVAERGERLTSIEDKADNLAVSAQGFKRGANRVRKAMWYKDLKMKMCLALVIIILLVVIIVPIAVHFSR
|
SNC1 and SNC2 are vesicle-targeting proteins essential for normal secretory traffic between the Golgi and the plasma membrane. They may also be involved in vesicle fusion.
|
P31109
|
B0BPV2
|
CH10_ACTPJ
|
Chaperonin-10
|
Actinobacillus
|
MTLRPLHDKVILKREEVETRSAGGIVLTGSAATKSTRGKVIAVSTGRLLENGSVQALAVKAGDVVIFNEGYGVKSEKIDGEEVLILSENDILAIVE
|
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
|
B0BPV2
|
Q5FFV2
|
RL5_EHRRG
|
50S ribosomal protein L5
|
Ehrlichia
|
MLKDLYKTQIVPSLQNKLGYSNVMQVPKIVKVCLNMGLGIRGSDSKVMNSCVRDLALIAGQKPVATSVKRSIAGFKIRKGFPIGCKVTLRNNKMYEFLERLIYVVLPREQDFKGLSINQFDGCGNISIGIKEHISFLEVDYDKIDKILGLDINIVTNAVNNKDAKLLLMEFGLPFIN
|
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
|
Q5FFV2
|
P0DB36
|
TRMFO_STRP3
|
Folate-dependent tRNA(M-5-U54)-methyltransferase
|
Streptococcus
|
MSQSTATYINVIGAGLAGSEAAYQIAKRGIPVKLYEMRGVKATPQHKTTNFAELVCSNSFRGDSLTNAVGLLKEEMRRLDSIIMRNGEANRVPAGGAMAVDREGYAKSVTAELENHPLIEVIRDEITEIPNDAITVIATGPLTSDALAEKIHAVNGGDGFYFYDAAAPIIDKSTIDMSKVYLKSRYDKGEAAYLNCPMTKEEFMAFHEALTTAEEAPLNSFEKEKYFEGCMPIEVMAKRGIKTMLYGPMKPVGLEYPDDYTGPRDGEFKTPYAVVQLRQDNAAGSLYNIVGFQTHLKWGEQKRVFQMIPGLENAEFVRYGVMHRNSYMDSPNLLTETFQSRSNPNLLFAGQMTGVEGYVESAASGLVAGINAARLFKREEALIFPQTTAIGSLPHYVTHADSKHFQPMNVNFGIIKELEGPRIRDKKERYEAIASRALADLDTCLASL
|
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
|
P0DB36
|
Q1JGE8
|
UVRB_STRPD
|
Excinuclease ABC subunit B
|
Streptococcus
|
MIDKRDDKPFKLKSKYKPSGDQPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEFFPDNAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATASLLERNDVIVVASVSCIYGLGSPKEYADSAVSLRPGQEISRDTLLNQLVDIQFERNDIDFQRGCFRVRGDVVEVFPASRDEHAFRVEFFGDEIDRICEIESLTGKTIGEVDHLVLFPATHFVTNDEHMEQSIAKIQAELAEQLQLFESEGKLLEAQRLRQRTEYDIEMLREMGYTSGVENYSRHMDGRSPGEPPYTLLDFFPEDFLIMIDESHMTMGQIKGMYNGDQARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGEYEMSQTNTIIEQIIRPTGLLDPEIDVRPSMGQMDDLLGEINQRVARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNVDGHVIMYADKMTDSMQRAIDETARRREIQIAYNKAHGIVPQTIKKDIRGLISISKTSHNDISKEEMDYESMSRGERKEAINALQKQMQEAAELLDFELAAQMRDLILELKLMD
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
|
Q1JGE8
|
A5EVX5
|
PRMA_DICNV
|
Ribosomal protein L11 methyltransferase
|
Dichelobacter
|
MTQRHWLELTLIADNDDDVLLLETALECAGAVAVTYQAANEEEIFEPEIGTTPMWSKTGVTGLFPLDTDPNAVIELLMQALGEDYPIAQHLLPESDWTRAWLEHFQPIAFGNHFWVAASEHVIEEHDAKVLRLDPGLAFGTGTHPSTAMCLHYLVNHAALHGKTVYDYGCGSGILGIAAAMMGAKAVYQTDIDPQALTASYENAQKNQVAEKIFLCEQPDLAPAVDLLVANILLEPLCALRAQFEKHLHAQSVMIFSGLLERQQQKLEQAYQDHYRIERINCRAGWILLRLTSL
|
Methylates ribosomal protein L11.
|
A5EVX5
|
Q62818
|
EI2BB_RAT
|
eIF-2B GDP-GTP exchange factor subunit beta
|
Rattus
|
MPGAAAKGSELSERIESFVETLKRGGGRRTSEDMARETLGLLRRLITDHHWNNAGDLMDLIRREGRRMTAAHPPETTVGNMVRRVLKIIREEYGRLHGRSDESDQQESLHKLLTSGGLSEDFSFHYAPLKSNIIEAINELLVELEGTTENIAAQALEHIHSNEVIMTIGFSRTVEAFLREAAQKRKFHVIAAECAPFCQGHEMAVNLSEAGIETTVMTDAAIFAVMSRVNKVIIGTKTILANGSLRAVAGTHTLALAAKHHSTPLIVCAPMFKLSPQFPSEEDSFHKFVAPEEVLPFTEGDILEKVSVHCPVFDYVPPDLITLFISNIGGNAPSYVYRLMSELYHPDDHVL
|
Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.
|
Q62818
|
Q1E6D3
|
EIF3K_COCIM
|
eIF-3 p25
|
Coccidioides
|
MAAFDKCKTRPAHIDAILNGLDRYNPETTAVFQDYVVQQCEDRTFDCYANLALLKLYQFNPPLLNAETVTNILAKALTVFPSPAFSLSLALLPAYTQPYATSSTQATTANLPMQTADFVEAVQKLTHLSTLLESAQYTAFWSTLNSDDLYADLTADVAGFEELIRIRIAVEVGKAFREIGADVLMGWLDMRGMETLEKFVVDVCGWEVDKSKAEGENGVIVRVPRNKENEARGEVKGEKVGIEMFGRVVRRGFEQPA
|
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
|
Q1E6D3
|
Q7TV05
|
TRPD_PROMM
|
Anthranilate phosphoribosyltransferase
|
Prochlorococcus
|
MPTSVTASSSWSQILEMLLEGQNLPEVEATALMEAWLAEQLTPVQTGAFLAALRAKGVTGNELSGMAQVLRGACPLPCPLPDIPMVDTCGTGGDGADTFNISTAVAFTAAACGANVAKHGNRSASGKVGSADVLEGLGLQLKAPLVSVVEALVEVGVTFLFAPAWHPALVNLAPLRRSLGVRTVFNLLGPLVNPLQPNAQVLGVAKAELLNPMAEALQRLGLQRAVVVHGAGGLDEASLEGANAMRLLENGHLRQASIDSAELGLTRAPLQALQGGDLATNQAILSAVLQGGGTAPQRDVVALNTALVLWAAGLQDDLQAGVSTAKTCLQEGLPWQRLEGLRMALDHQIGE
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q7TV05
|
A0LM17
|
RECR_SYNFM
|
Recombination protein RecR
|
Syntrophobacter
|
MVSSGYPPIMNDLIRRLSKLPGLGEKSATRIAMHLLKMSRTDAESLADAIRELRSRIRTCSRCFHFTDAEECSICADPARDTGEICVVETTADLLAIEQSGAYRGRYHVLQGVLAPLDAVGPDDLRIRELLERIDREGAREVIIATNPSSEGEATAHYLLKLLKDRNVRVSRIAYGIPMGGDLKYTDRFTLERALKGRQAF
|
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.
|
A0LM17
|
B3CNB0
|
MIAA_WOLPP
|
Isopentenyl-diphosphate:tRNA isopentenyltransferase
|
unclassified Wolbachia
|
MKDNIVIITGITASGKSELCDNLIKKHKNISIINCDSKQVYKEIPVITAQPPKQKEFYRLYGYVSARENYSVGLWLEDLKREVNNALKNSRIPIITGGSGLYISSLIKGLSSIPQISQEVRENVNELRKNLSKEEFYKLVLSKDPRIQGKIFINDSHRLSRALEVITETGKTIFVWQENRQPPLFNNFKVYTILPKREDIYRKINSRFIEMVENGAIDEVKNLLSMNPSPHLPAMKAHGVPEIIRYLKGEITLDEAIQIAQTNTRHYAKRQYTWFKNQFPNSQVIDCANKLTEFGIF
|
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
|
B3CNB0
|
B5XJM0
|
G6PI_STRPZ
|
Phosphohexose isomerase
|
Streptococcus
|
MSHITFDYSKVLESFAGQHEIDFLQGQVTEADKLLREGTGPGSDFLGWLDLPENYDKEEFARILTAAEKIKSDSEVLVVIGIGGSYLGAKAAIDFLNHHFANLQTAKERKAPQILYAGNSISSTYLADLVEYVQDKEFSVNVISKSGTTTEPAIAFRVFKELLVKKYGQEEANKRIYATTDKVKGAVKVEADANNWETFVVPDNVGGRFSVLTAVGLLPIAASGADITALMEGANAARKDLSSDKISENIAYQYAAVRNLLYRKGYITEILANYEPSLQYFGEWWKQLAGESEGKDQKGIYPTSANFSTDLHSLGQFIQEGYRNLFETVIRVDNPRKNVIIPELAEDLDGLGYLQGKDVDFVNKKATDGVLLAHTDGGVPNMFVTLPAQDEFTLGYTIYFFELAIAVSGYMNAVNPFDQPGVEAYKRNMFALLGKPGFEALSAELNARL
|
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
|
B5XJM0
|
A4WXK6
|
COWN_CERS5
|
CO weal-nitrogenase
|
Cereibacter
|
MNDHTPDRYVTFLGIDCDAKADRMMEMLSARLASTDSPWVRYFEQKLAEKARMATDNLHFVGSQINSLYSFFEEAEDEEGLDLLWHLEHNCC
|
Is required to sustain N(2)-dependent growth in the presence of low levels of carbon monoxide (CO). Probably acts by protecting the N(2) fixation ability of the nitrogenase complex, which is inactivated in the presence of CO.
|
A4WXK6
|
B2ITQ6
|
NDHN_NOSP7
|
NAD(P)H dehydrogenase I subunit N
|
Nostoc
|
MALITTGNGLIRDLEKFGALGVYVPLEGGYEGRYQRRLRAAGYTTLHITAKGLGDVAAYLTRIHGVRPPHLGKKSTGSGAAVGQVYYLPPILDSHLEQLPPKSKGLVLWIIEGHILSNEELEYLTNLPQLEPRVKVVIERGGDRAFRWTSLEKTLLAS
|
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
|
B2ITQ6
|
A7ZCL5
|
RSMG_CAMC1
|
16S rRNA 7-methylguanosine methyltransferase
|
Campylobacter
|
MKNELCLPAVFDEKVKAYAQIFTKFNKVHSLSNYKDISEQVLDSIKPLEIFDLSAKTAIDVGSGAGFPAIFLALAMPQTKWHLFEPIAKKSSFLSYAKIELGLQNLEVHSQKIELADKFTADLITSRALSKTKELIKICEGFYDENTKFLIYKGSSVMEEISGIDAQIYNEKNRNYIYFNLKNQGEIR
|
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
|
A7ZCL5
|
A1JRX9
|
METAS_YERE8
|
Homoserine transsuccinylase
|
Yersinia
|
MPIRVPDELPAVSFLRNENVFVMTSSRAKTQEIRPLKVLVLNLMPKKIETENQFLRLLSNSPLQIDIQLLRIDSRESKNTPAEHLNNFYCDFEDIQEQNFDGLIVTGAPLGLVDFCDVAYWPQIERIIAWAKDHVTSTLFVCWAVQAALNILYGIPKMTRETKLSGIYQHQTDKPLALLTRGFDETFLAPHSRYADFPVELLQQYTDLDILVSSEEAGAYLFASKDKRVAFVTGHPEYDVDTLAGEYQRDLAAGLNPQIPLNYFPNDDASLPPKASWRSHGHLLFANWLNYYVYQITPFDLRHMNPTLD
|
Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
|
A1JRX9
|
Q8FKI9
|
BETA_ECOL6
|
Betaine aldehyde dehydrogenase
|
Escherichia
|
MQFDYIIIGAGSAGNVLATRLTEDPNTTVLLLEAGGPDYRFDFRTQMPAALAFPLQGKRYNWAYETEPEPFMNNRRMECGRGKGLGGSSLINGMCYIRGNALDLDNWAQEPSLENWSYLDCLPYYRKAETRDVGENDYHGGDGPVSVTTSKPGVNPLFEAMIEAGMQAGYPRTDDLNGYQQEGFGPMDRTVTPHGRRASTARGYLDQAKSRPNLTIRTHAMTDHIIFDGKRAVGVEWLEGDSTIPTRAAANKEVLLCAGAIASPQILQRSGVGNAELLAEFDIPLVHELPGVGENLQDHLEMYLQYECKEPVSLYPALQWWNQPRIGAEWLFGGTGVGASNHFEAGGFIRSREEFAWPNIQYHFLPVAINYNGSNAVKEHGFQCHVGSMRSPSRGHVRIKSRDPHQHPGILFNYMSHEQDWQEFRDAIRITREIMHQPALDQYRGREISPGVECQTDEQLDEFVRNHAETAFHPCGTCKMGYDEMAVVDGEGRVHGLEGLRVVDASIMPQIITGNLNATTIMIGEKIADMIRGKEALPRSTAGYFVANGMPVRAKK
|
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.
|
Q8FKI9
|
P51212
|
PSBA_PORPU
|
Photosystem II Q(B) protein
|
Porphyra
|
MTATLQRRESASLWERFCSWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFVAAPPVDIDGIREPVAGSLLYGNNIISGAVIPSSAAIGIHFYPIWEAASLDEWLYNGGPYQLVVLHFLTGVACYIGREWELSYRLGMRPWISVAFTAPVAAAAAVFLVYPIGQGSFSDGMPLGISGTFNFMLVFQAEHNILMHPFHQLGVAGVFGGSLFSAMHGSLVTSSLIRETSENESANYAYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLGLWPVVGIWLTALSVSTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLASGESLPVALTAPAVNG
|
Photosystem II (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. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
|
P51212
|
A8GL54
|
ILVC_SERP5
|
Ketol-acid reductoisomerase type II
|
Serratia
|
MANYFNTLNLRQQLAQLGKCRFMAREEFADEAGYLKGKKVVIVGCGAQGLNQGLNMRDSGLDVAYALRKEAIDEKRPSWRKATENGFKVGTYEDLIPQADLVVNLTPDKQHTSVVRAVQPLMKDGAALGYSHGFNIVEVGEQVRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVAEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKGIMAPLFQKHMDDIISGAFSGGMMADWAEDDVKLLNWREETGKSAFENAPQFEGKISEQEYFDHGVLMVAMVKAGVELAFETMVDAGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYLFANAAVPLLKEFMTTLQAGDLGKSVAGTSVDNAQLRDVNEAVRNHPIESVGRKLRGYMTDMKRIAVAG
|
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.
|
A8GL54
|
C3L179
|
OTC_CLOB6
|
Ornithine carbamoyltransferase
|
Clostridium
|
MFNLKNRNFLTLMDFTPKEINYFLDLARDLKRAKYTGTEVQRMKGKNIALIFEKASTRTRCAFEVGAKDQGAHVTYLGPTGSHIGKKESAADTARVLGRMYDGIEYRGFGQEIVETLAEYAGVPVWNGLTDEDHPTQILADFLTIREHFNKPLNEIKFAYVGDGANNMANALMIGAVKMGMDFRIVSPKEIPTDAALVAKCKEIAAETGAKVTITDNIEEGVKGCDVLYTDVWVSMGEPDSVWESKIKLLTPYRVDMNMIKMTGNPDAKFMHCLPAFHDEETAVGKEIKEKYGLSEMEVSHELFESKYSIVFDEAENRMHTIKAVMVATLGDQ
|
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
|
C3L179
|
Q6KIF0
|
RL11_MYCMO
|
50S ribosomal protein L11
|
Mesomycoplasma
|
MAKKKEVVRVAKLQFNAGQAKPGPELAGLGIVMPEFTKQFNDATRERSGEPVPVQIIVYKDKSFDFKLFTAPTSFMLKKAAGIKSGSANSKTTIVATIKKSQLEDIAKYKMPDLNTKNLEEAMHTIAGTARNMGILVEGYDDIVKAREEAKLAAKEAASAAAFEAKLESDAAQLLAENKQSAEVEVIKEKDKGNKDE
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
Q6KIF0
|
P36438
|
CYF_BRARR
|
Cytochrome f
|
Brassica
|
MQTRNTFSWIREEITRSISVSLMIYIITWASISSAYPIFAQQNYENPREATGRIVCANCHLASKPVDIEVPQAVLPDTVFEAVVKIPYDMQLKQVLANGKKGALNVGAVLILPEGFELAPPDRISPEMKEKIGNLSFQNYRPNKKNILVIGPVPGQKYSEITFPILAPDPATNKDVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNATAGGIISKILRKEKGGYEITIVDASNERQVIDIIPRGLELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLFFLGSVVLAQIFLVLKKKQFEKVQLSEMNF
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
|
P36438
|
A0RPC8
|
MURA_CAMFF
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Campylobacter
|
MDYLEIKGGKKLFGSVYISGAKNAALPLIAMSILAKNDVVIRNIPQVADIKTLIKLLQNLGAVSKFENLDLVINTTTINSTKATYDIVRKMRASILVLGPLLARFGHCEVSLPGGCAIGARPIDLHLSALEKMGANIEIKDGYVIARAKDGLKGANIIFDKITVTGTENIVMAAALARGTTKILNAAKEPEVVQVCQILNDSGIKIEGIGTNELTIYGGGGELLNLNKICVIPDRIEAGTYLCAAAIAGGEITLKQVEPNHLVSVLGKLSDMGVNFELGDKSIKVISDAKLSPVQIITTEFPGFPTDMQAQFMALACVANGVSTIDERLFENRFMHASELNRMGADIKLNGHIATVSGVSLNGADVMATDLRASSALVLAALVANGTTRVHRIYHLDRGYENLEIKLQSLGADIKRLSE
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
A0RPC8
|
Q3AAK3
|
GLMM_CARHZ
|
Phosphoglucosamine mutase
|
Carboxydothermus
|
MGKLFGTDGVRGVANRDLTPELAYKLGRAAAYVLKKKYNGQGIVVGKDTRISGDMLETALAAGILSVGLNVLRVGVMPTPAIAYLTRELKATAGAVISASHNPMEDNGIKFFSGSGFKLPDEVEEEIEKYVLGEKEIPIRPIGAEIGRVREISDAVLLYKSFAKNTVELPFSGLRVVVDCANGAASYVAPKIYEELGAEVIPIFNTPDGTNINANCGSTHPEALMRAVVEEGAHLGLAHDGDADRVLAVDEKGNLVDGDQIMVIIGKYLKKKGLLKNNRIVVTVMSNLGLKKAFAREGIEVLETKVGDRYVLEEMLKNGAIIGGEQSGHIILLDHNTTGDGIITALQLMQVIVAEGKKLSELAQEMPKFPQVLKNVRVLDKEKIMASEELAKAIARGEKKLGEGRILVRPSGTEPLIRVMAEGADAKLTEEVVDEIIAVIEKL
|
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
|
Q3AAK3
|
B5RQT9
|
RL9_BORRA
|
50S ribosomal protein L9
|
Borrelia
|
MKVILREDFINLGKEGDIVDVKDGFARNYLLPKGFAVFSNKHNIDIFSQKKRAILKRQESRRKMAVELKEKLDKVNLEFIMQSNDSGKLFHSINSSNIADELLKLGFEIERRKIDMHHGALKAFGTYNVIIKLYEGISSVITVEIKREEKKNSLKKSKSVKKEV
|
Binds to the 23S rRNA.
|
B5RQT9
|
P12374
|
COPA_PSEUB
|
Copper resistance protein A
|
Pseudomonas
|
MESRTSRRTFVKGLAAAGVLGGLGLWRSPSWAASGSPALSVLSGTEFDLSIGEMPVNITGRRRTAMAINGGLPGPLLRWKEGDTVTLRVRNRLDAATSIHWHGIILPPNMDGVPGLSFAGIEPGGVYVYQFKVQQNGTYWYHSHSGFQEQVGVYGPLVIEAKEPEPFKYDSEHVVMLTDWTDEDPVSLMRTLKKQSDYYNFHKRTVGDFVNDVADKGWAATVADRKMWAEMKMNPTDLADVSGATYTYLLNGQAPNMNWTGLFRPGEKLRLRFINGSAMTYFDIRIPGLKMTVVASDGQFVNPVEVDELRIAVAETFDVIVEPTAEAYTVFAQSMDRTGYARGTLAVREGLVAQVPPLDPRPLVTMDDMGMGGMDHGSMDGMSGMDSGADDGMQTMSSMGGDSMPAMDHSKMSTMQGMDHGAMSGMDHGAMGGMVMQSHPASENDNPLVDMQAMSPTAKLNDPGLGLRNNGRKVLTYADLKSTFEDPDGREPSRTIELHLTGHMEKFAWSFDGIKFADAQPLILKYGERVRIVLVNDTMMTHPIHLHGMWSDLEDEDGNFRVRKHTIDMPPGSKRSYRVTADALGRWAYHCHLLYHMEMGMFREVRVEE
|
Mediates copper resistance by sequestration of copper in the periplasm along with the copper-binding protein CopC. May have oxidase activity.
|
P12374
|
Q93WE4
|
SINA6_ARATH
|
Seven in absentia homolog 6
|
Arabidopsis
|
MEPRINDLQVESRVHELLDFPVHTNQISSAIYECPNDHIENPKKKPYNCPHSGAKCDVTGDIQRLLLHLRNDHNVEMSDGRSFSHRYVHHDPKHLHHATWMLTLLDCCGRKFCLYFEAFHLRKTPMYMAFMQFMGDEEEAMSFSYSLQVGGNGRKLTWQGVPRSIRDSHKTVRDSQDGLIITRKLALFFSTDNNTTDKELKLKVSGRVWREQPVSI
|
Probable inactive E3 ubiquitin-protein ligase that plays a role in regulation of autophagy. Upon starvation, involved in maintaining ATG6 homeostasis by competitively associating with ATG6, a component of the autophagosome complex . Acts as positive regulator of drought stress response. Functions as positive regulator of abscisic acid-mediated stomatal closure .
|
Q93WE4
|
O75607
|
NPM3_HUMAN
|
Nucleoplasmin-3
|
Homo
|
MAAGTAAALAFLSQESRTRAGGVGGLRVPAPVTMDSFFFGCELSGHTRSFTFKVEEEDDAEHVLALTMLCLTEGAKDECNVVEVVARNHDHQEIAVPVANLKLSCQPMLSLDDFQLQPPVTFRLKSGSGPVRITGRHQIVTMSNDVSEEESEEEEEDSDEEEVELCPILPAKKQGGRP
|
Plays a role in the regulation of diverse cellular processes such as ribosome biogenesis, chromatin remodeling or protein chaperoning . Modulates the histone chaperone function and the RNA-binding activity of nucleolar phosphoprotein B23/NPM . Efficiently mediates chromatin remodeling when included in a pentamer containing NPM3 and NPM .
|
O75607
|
A5IF82
|
KUP3_LEGPC
|
Probable potassium transport system protein kup 3
|
Legionella
|
MPSTRNIETHNDSNPTLRALSLSALGIVYGDIGTSPLYTFKTVILLAGGGTPDVTTIMGSASLIIWTLIIIASVKYICFALRIDNDGEGGILALMSLLSLKLKQKPFIIAVGLMGAALIYGDGTITPAISVLSAVEGLEILSPSLKYYVLPIAITILITLFAIQSKGTATIGKAFGPVMAFWFLTIGILGAREVIQHPFVLAAINPVYGLNFLFSNGATGFFILCGVFLCVTGAEALYADLGHFGTAPIRCAWFGLAFPSLIFNYLGQAALVLEGASTEHNIFYMLCPSDFLLPLIILSTVATIIASQAIITGAFSMTRQAMQLGWLPRLRVTQTSSEGYGQIYIGVVNWLLMLATLGLIIGFGSSEKLAAAYGIAVSATMLCTSVLLFIALHKLWKWNIIKSGLVAGLFMIVDASFFAANLTKFINGGYIPITLAIIIYSMMYIWHKGYKTIAIKQKEKNITVDSFLDSIQKEGVVRVPKTAVFLTSKEQDIPPTLVWHVKKNHVLQDKVIILNINNLSIPWCKPGDQLQIVETGAGIWHAVANYGFMEQPHIPKLLKKLETQGYDINIKDITYYIGHETIFVRNVRHTLSKYIKILFVFMHRNALPMSNYFHLPPESVFEIGRQIEI
|
Transport of potassium into the cell.
|
A5IF82
|
A0B6K6
|
DHQS_METTP
|
3-dehydroquinate synthase II
|
Methanothrix
|
MKEKWLMALASEWDDVKPLITTALESGFDCVVVSRDHIELVRELGSIRIACFGRERGSEDLLIMDTSVPRENQIKSVEKIGRPIGGYVEIRSKEDELFATELGKHVDYLLVVGTDWKVIPLENMIAALQGYDCKIISCVRSSEEAEVALSTLEHGADGVLLDTRDPSEIKRVQAAAERLGMSRIDLKTATVVAVKPVGMGDRVCVDTCSLMRRGEGMLVGSQSRAFFLVQSEAEESPYVAARPFRVNAGAVHAYIRVGDKTRYLSELKSGDEVTIVDKDGMTRSAVVGRVKIERRPMILVEAEVDGERVSTLLQNAETIKLVSHDGTPISVAELKPGDKVLVHVETSARHFGMSIEETIIER
|
Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.
|
A0B6K6
|
P29250
|
LOX2_ORYSJ
|
Lipoxygenase L-2
|
Oryza sativa
|
MLGGIIGGLTGNKNARLKGSLVLMRKNALDINDFGATVIDGISEFLGRGVTCQLVSSSLVDPNNGNRGRVGTEASLEQWLTSLPSLTTGESKFGVTFEWEVEKMGIPGAIIVKNNHAAEFFLKTITLDNVPGHGAVVFVANSWIYPASKYRYNRVFFSNDTSLPSKMPAALKPYRDDELRNLRGDDQQGPYQEHDRVYRYDVYNDLGEPDSGNPRPVLGGSPDRPYPRRGRTGRKPTKTDPTAESRLSLLENIYVPRDERFGHLKMADFLGYSIKALVDGIVPAIRTYVDLTPGEFDSFKDILKLYEGGLKLPSIPALEELRKRFPLQLVKDLIPAGGDYLLKLPMPHVIREDKKAWMTDDEFAREILAGVNPMVIARLTEFPPRSRLDPARYGDQTSTITAAHVERGLEGLTVQQAIDGNLLYVVDHHDHFMPYLLDINSLDDNFIYATRTLLFLRGDGTLAPLAIELSLPHLQDDGLITARSTVYTPAARGGTGAGAVEWWVWQLAKAYVNVNDYCWHQLISHWLNTHAVMEPFVIATNRQLSVAHPVHKLLLPHYRDTMTINALARQTLINGGGIFEMTVFPRKHALAMSSAFYKDWSFADQALPDDLVKRGVAVPDPASPYKVRLLIEDYPYANDGLAVWHAIEQWATEYLAIYYPNDGVLQGDAELQAWWKEVREVGHGDIKDATWWPEMKTVAELVKACATIIWIGSALHAAVNFGQYPYAGYLPNRPSVSRRPMPEPGTKEYDELARDPEKVFVRTITKQMQAIVGISLLEILSKHSSDEVYLGQRDTPEWTSDAKALEAFKRFGARLTEIESRVVAMNKDPHRKNRVGPTNFPYTLLYPNTSDLKGDAAGLSARGIPNSISI
|
Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.
|
P29250
|
Q9U568
|
MT_PERVI
|
Metallothionein
|
Perna
|
MPSPCNCIETQVCICGTGCSGEGCRCGDACKCSSGCGCSGCKVVCKCQPGECACGKQCTGPDTCKCDSSCSCK
|
The metallothioneins are involved in the cellular sequestration of toxic metal ions.
|
Q9U568
|
Q1XDK1
|
EFTU_NEOYE
|
Elongation factor Tu, chloroplastic
|
Neopyropia
|
MARSKFERKKPHVNIGTIGHVDHGKTTLTAAISATLSTLGSTAAKKFDEIDAAPEEKARGITINTAHVEYETDNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPTLVVFLNKEDQVDDEELLELVELEGRELLSQYDFPGDDIPFVAGSALLALEAVTKNPAIKQGEDKWVDKIFSLMEAVDTYIPTPERDVDKTFLMAVEDVFSITGRGTVATGRIERGIIKVGDTIEIVGLRETRTTTITGLEMFQKTLEEGLAGDNIGILLRGVQKKDIERGMVLAKPGTITPHTQFEAEVYILTKEEGGRHTPFFPGYRPQFYVRTTDVTGTINQFTADDGTDAEMVMPGDRIKMTAELINAIAIEQGMRFAIREGGRTVGAGVVSKILK
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
Q1XDK1
|
B8EA75
|
RUVB_SHEB2
|
Holliday junction ATP-dependent DNA helicase RuvB
|
Shewanella
|
MIEADRLIQPQIQAQDESIDRAMRPKMLDEYTGQDDTRAQLKVFIQAAKNRNEALDHMLIYGPPGLGKTTLAMIVANEMGVNIKSTSGPVLEKAGDLAALLTNLESGDVLFIDEIHRLSPVVEEILYPAMEDYQLDIMIGEGPAARSIKLDLPPFTLVGATTRAGALTSPLRARFGIPLRLEFYNIKDLSTIVTRSAQVMELDIDAEGAFEIARRSRGTPRIANRLLRRVRDYAQVKHDGAVTKFVAEHALDLLDVDSEGFDYMDRKLLLAIIDKFMGGPVGLDNLAAAIGEERETIEDVLEPFLIQQGFIQRTPRGRIATARAYQHFELIKPE
|
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
|
B8EA75
|
Q84PW3
|
MDAR5_ORYSJ
|
Monodehydroascorbate reductase 5, chlorplastic
|
Oryza sativa
|
MASTAAAASSQGCISWALRQRGLGGGGARAVPVLPRRRFCVSAAAGAGFDNENREYVIVGGGNAAGYAARTFVEHGMADGRLCIVSKEAYPPYERPALTKGYLFPPDKKPARLPGFHTCVGSGGQRQTAEWYKENGIEVLYEDPVVAFDGKTHTLKTSSGKILKYGSLIISTGCEASRLPAKIGGNLPGVHYIRDVADADSLVSSLGKAKKIVVIGGGYIGMEVAAAACGWNLDTTIIFPEDHIMPRLFTPSLAKKYEELYQQNGVKFIKGALIDKLEAGSDGRVSSAVLEDGSVVEADTVIVGIGARPVIGPFEAVGVNTKVGGIEVDSLFRTSIPGIFAIGDVAAFPLKMYDRMTRVEHVDHARKSAHHCVEALLTSHTKPYDYLPYFYSRVFEYEGSSRKIWWQFYGDNVGETIEVGSFEPKIATFWIDSDSRLKGVFLESGSSEEFSLLPQLAKSQPVVDKAKLKSATSVEDALEIARSSLHSGSSV
|
Catalyzes the conversion of monodehydroascorbate to ascorbate, oxidizing NADH in the process. Ascorbate is a major antioxidant against reactive oxygen species (ROS) and nitric oxide (NO).
|
Q84PW3
|
B7HJF3
|
FOSB_BACC4
|
Fosfomycin resistance protein
|
Bacillus cereus group
|
MLRGINHICFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHISRNEIHQSYTHIAFSVEQEDFKCLIQRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYRDEKPHMTFY
|
Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor.
|
B7HJF3
|
Q9TLU8
|
RR5_CYACA
|
30S ribosomal protein S5, chloroplastic
|
Cyanidium
|
MSRDTSANSSGQQNYTWSERVIQITRVTKVVKGGKKLSFRAIIVIGNNQGSVGVGVGKASDVIGAVKKGVSDCKKQIIEFPLTSSSTISHAVEGRFGAASVILKPSVQGSGVIAGGAMRTVIELSGIKNIVAKQLGTKNHLNNAKATINALSKLNSKSSQLSLMSFSN
|
With S4 and S12 plays an important role in translational accuracy.
|
Q9TLU8
|
A7TP26
|
IRC22_VANPO
|
Increased recombination centers protein 22
|
Vanderwaltozyma
|
MKLLFFIWFAIFSKVFGISEEVAEAADVVSEDLKEDFDVEESPVQQYVNLNVTYSIVERPGLNLTDLFEFVPEETLTLNYNLYNGENSSVSVVGVSGNVYTFPDGYYAANITESSIEPLEVMFNRSAIFQQEVRLVLPEGRYYLEPVLIVEKDEKLMRVAVQPVTVEIAPLPLSIFNPQFLSIIVTLGALVGGAFYYLVYLKASTKETKGKSKTVKVDETWLPDTYKK
|
Is probably involved in a pathway contributing to genomic integrity.
|
A7TP26
|
A7SBN6
|
ZGPAT_NEMVE
|
Zinc finger CCCH-type with G patch domain-containing protein
|
Nematostella
|
MDEDVLKEAIEQYKQQIIQIQTVLESGQIEGRAELAKLKDDLTELIQVTEESLLSLKKSQLLQLLEQQESSHHDSGTPETDTKTSVDYRNSYVNDHTIDDNDDEDNDENIIGTKCRVAFTQEWGVKEHHNAMVFKLESIPLDEETVDQAKVRVLFLNPTHRSMVPCPYFLEGKCKFAGAECRFSHGYLVDVEHLKPFKEPDFSSVKAGQRCLARYSDGVWYNSTIKSIKHESHEFLIHYETYNTDATLPLDDIYPLGPEEVESDSESDSQSDTGDSSSSKAAIEQDDDVIRYAWKPTGALSSLGDWEQHTKGIGSKLMAKMGYIFGKGLGKDGEGRVEPIEVVVLPQGKSLDKCAELREKNKLKEPFKRKKKKLVVASTTSASQGKASDVFDFINHKLGHSKGSLHDLRVSHPGAKPDIRKTRKSADENTNWNIQLFKIHEEISSVKKQLNKQEEALQRHTTRDSRNKTIFTEKRDSVHNRLQELLKKEKKIQEKIHQKDQHRKLTVF
|
Transcription repressor.
|
A7SBN6
|
Q14IC0
|
ENO_FRAT1
|
2-phosphoglycerate dehydratase
|
Francisella
|
MSSQIKQVFARQILDSRGNPTIEVEVVLESGAFGRAAVPSGASTGIREALELRDGNKALFLGKSVYKAVENVNTKIAQAVKGLDALDQRLIDKTMIELDGSENKKNLGANAILGVSLATARAAASHLRKPFYRYLMDVKEYLMPVPMMNVINGGSHADNNVDMQEFMIVPAGFDTFSEALRCGTEVFHILKKVLIADGYSVAGVGDEGGYAPDLPSNEAAIEAILKAVKEAGYEPGKHVFIALDPASSEFYKDGKYELKSENKSLTSEEMIDYYAAWVEKYPIVSIEDGLAEEDWAGWKLLTEKLGNKVQLVGDDLFVTNPSILAKGIEKGIANSILIKLNQIGTLTETFEAMAMAGQAGYTCVVSHRSGETSDTIIADLAVATCSGQIKTGSLSRSDRIAKYNQLLRIEEELGENAIYPGIKAFVFNSDEEVEEVVQEIIVEDSEAEKVVVQVEE
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
Q14IC0
|
B2GI02
|
URED_KOCRD
|
Urease accessory protein UreD
|
Kocuria
|
MDQDRSGAADAGNPDPGRGPAGSAEARNGAAAASSPAEWAGQLRLSVAERNGRSYAARQFHEGALRVLRPHYLDRSGQVTYTVVNPGGAYLGADAYLLDVAVERDASLVLTTQSATKVYRTPQGPATQDMTVRLGPGSCLEHVPDQLIVYRGGSYLQRTRVDMDPAASLLLAEVVTPGWSPSGESFAYDELRLRTEVRVTPPEVPAPAAPDRGAPAAEAQDRPADPCHVPGGPDRAASSGGTGAAPAGERARRLVVDQLRIRPDAHGGMSGVGFMEGFSHTGQLLVADARLDDELYERLCELVDASGTHSGITRAGTGEPYGVRCVCVRSLAHSTSAITALHRAVVDELRQRWRGQSPLRLRKY
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
B2GI02
|
Q5DRD4
|
PCDBI_PANTR
|
Protocadherin beta-17
|
Pan
|
MEPGKGRAQPTRQVLLFFVFLGGSLVYSETWSYSIAEEMEVGTFIANVVKDMGLDVEDLVARGARVIFDDYKPYLRLDPQNGDLLLNEQLDREALCDLTEPCILHFQVLFENPLQFFRAELLVKDINDHTPTFLNNHILLKISEGATLGTLFQIDSAQDLDVGKNGVQNYTISPNPHFHLKLRDGDEGRKYPELVLDQSLDREKESQLSLTLTAVDGGSPPRSGTTLINVVVLDINDNAPEFEKPVYEVHVPESSPLDSLIIKASATDLDAGINGELSYSFSHVSRDVRKTFEIHPISGEVYLKAPLDFEIIQSYIINIQAIDGGSLSGKSSILVRVVDVNDNPPEIAMTSLTSPIPENSSPEMVVAVFSIRDQDAGDNGRMVGSIQDNLPFVLKPTFKNFYALVTEHPLDREVRNEYNITITVTDLGTPRLKTQHNITVLVSDVNDNAPAFTQTSYTLFVRENNSPALHIGSVSATDRDSGTNAQVTYSLLPPQDPHLPLASLVSINTDNGHLFALRSLDYEALQAFEFHVGATDRGSPALSSEALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDVAKHRLVVLVKDNGEPPRSATATLQVLLVDGFSQPYLPLPEAAPSQAQADSLTVYLVVALASVSSLFLFSVFLFVAVRLCRRSRAASVGRCSVPEGPFPGHLLDVSGTGTLSQSYQYEVCLTGGSGANEFKFLKPVIPNLLSRDSDMEKAPPF
|
Potential calcium-dependent cell-adhesion protein.
|
Q5DRD4
|
Subsets and Splits
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