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
|
---|---|---|---|---|---|---|
A6VM61
|
LUXS_ACTSZ
|
Autoinducer-2 production protein LuxS
|
Actinobacillus
|
MPLLDSFKVDHTKMQAPAVRIAKTMTTPKGDLITVFDLRFCVPNKEIMSPKGIHTLEHLFAGFMRAHLNSDEVEIIDISPMGCRTGFYMSLIGAPSERRVADAWLAAMHDILNVQDQSKIPELNIYQCGTYTEHSLSDAHATAQHVITRGIGINKNEELLLDESLLTE
|
Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
|
A6VM61
|
Q3AW00
|
RSMH_SYNS9
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
unclassified Synechococcus
|
MPPFSHVPVLADAVVAGAEHLPHHNGVLIDATLGGGGHSALLLERFPGLRLIGLDQDPTARAAAAERLAAFADRVEILATNFASYTPPAPVLMVLADLGVSSPQLDVAERGFSFRLDGPLDMRMNPGSDGETAAELIDRLEENALADLIYGYGEERLSRRIARRIKADLAAQGPYEGTAALAYAVAGCYPPKARRGRIHPATRTFQALRIAVNDELAVLDRLLQQAPDWLETGGVMGVISFHSLEDRRVKTAFLQDERLERITRKPTVATDDEQNRNPRSRSAKWRLARRVNGC
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
Q3AW00
|
A8H0M9
|
E4PD_SHEPA
|
D-erythrose-4-phosphate dehydrogenase
|
Shewanella
|
MIRVAINGYGRIGRSILRALYESAKRDRIQIVAINELAKPEAMLHLTQYDTTHGRFHTQVKLDNQHMIIGDDAIKLLHEPDPAKLPWKEMDIDIVFEATGVINDRLECEAHIQAGAKQVLISHPSSSDVDATIVFGVNQDLLKAEHTVVSNASCTTNCIVPVIDVLDRHFEVKSGAITTIHSAMNDQQVIDAYHDDLRRTRAAGQSIIPVDTKLARGIERILPHMKDKFEAISVRVPTINVTAIDLSVTLNKRVDIETVNQVLKQATEGSFSGVVGFTNEPLVSCDFNHDPRSSIVDGTQTRVSDGHLVKLLLWCDNEWGFANRMLDTSLEMIKAKSRT
|
Catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate to 4-phosphoerythronate.
|
A8H0M9
|
B1YS63
|
FABZ_BURA4
|
Beta-hydroxyacyl-ACP dehydratase
|
Burkholderia cepacia complex
|
MSTEKINLDIHKILTLLPHRYPILLVDRVLELEPHKGIKALKNVSINEPFFQGHFPKRPVMPGVLILEALAQAAALLTFAEEQPKDPENTLYYFVGIDGARFKRVVEPGDQLILNVTFERYIRGIWKFKAVAEVDGKVAAEAELMCTVKTADAAP
|
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
|
B1YS63
|
Q8TZV1
|
ALBA_PYRFU
|
DNA/RNA-binding protein Alba
|
Pyrococcus
|
MAEEHVVYIGKKPVMNYVLAVITQFNEGAKEVSIKARGRAISRAVDVAEIVRNRFLKDTVDIKEIKIGTEELPTADGRTTNTSTIEIVLERKV
|
Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.
|
Q8TZV1
|
C4L3Z5
|
ISPH_EXISA
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
|
unclassified Exiguobacterium
|
MKVKKISPRGYCYGVVDAMKLANEAVANPDLPRPIHILGMIVHNRHVTQAFEDLGVKTVDGEDRMQALETIDRGTVVFTAHGISPLVRKRAIEKGLTIVDASCPDVLVTHDLIREKTAEGYDVIYIGKHGHPEPEGAIGVAPDHVHLIQYEHEIDQLPSRLFERKILVTNQTTMSQWDVSALIETIQARYPHVEVHNEICNATQVRQEAVAEQAGDCELLIVVGDPKSNNSNRLAQVSKEIAGTNAYRIGDLSELDLNWLEGVETVAVTSGASTPTPITKKVIDFLSQYDPDDLSTHDKTPFLELRSILPKVKALRK
|
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
|
C4L3Z5
|
Q9PP85
|
SYM_CAMJE
|
Methionyl-tRNA synthetase
|
Campylobacter
|
MRYITTPIYYVNDVPHLGHAYTTIIADTLARFYRLQGHETRFLTGTDEHGQKIEEAAKLRNSTPQEYADKISFEFKKLWDEFEITYDIYARTTDTRHIEFIKAMFLKMWQKGDIYKDEYEGHYCISCESFFTQSQLINDCSCPDCGKQTRILKEESYFFKLSKYQDKILQWYEEKDPILPKNKKNELINFVQNGLKDLSITRTSFDWGIKLPQEINDDKHIIYVWLDALFIYVSSLDFQNKGENAKFWPAHVHLVGKDILRFHAIYWPAFLMSVDLPLPKFIGAHGWWTKEGEKMSKSKGNVVKPKEVVDAYGSEAFRYFLLREVPFGNDGDFSENMLINRINAELSNEFGNLLNRIIGMSTKYSQGNISKEGVLKFYNAELNQAKEHLNLAVEFLENLQCNRYLEELFKALSVANLAISKYEPWSLIKENKHEQANALVALCANILAKTSLLLSPTLPKSSQKVALALNFEISSANYTKMILDNELLDFKANPCEALFPKVEKALLKQEIKEEPKKEESPKIKIDDFAKIEIKVAKVLDCQNIEGSEKLLKFQLELDDKEIRQVLSGIAKYYKASDLIGKQVCVISNLKKAKIFGHESDGMILSAKSGDKLVLIAPEQLVQNGSLVG
|
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
|
Q9PP85
|
P55946
|
MT_ARIAR
|
Metallothionein
|
Arianta
|
SGKGKGDLCTAACKNEPCQCGSKCQCGEGCACASCKTCNCTSDGCKCGKECTGAASCKCNSSCSCK
|
The metallothioneins are involved in the cellular sequestration of toxic metal ions and regulation of essential trace elements.
|
P55946
|
Q2RMS3
|
RIMP_RHORT
|
Ribosome maturation factor RimP
|
Rhodospirillum
|
MALWGWRGVGRRPTFFVFASLAPIGRDFLRRNGDDARMMGHLEKLLAPTLDAMGYEVVRVTLLGSQNPTLQVMAERLDGVAMTVSDCETISRALGALLDVEDPIAGRYSLEISSPGIDRPLTRPKDYARFAGHEARIETDRLIEGHRRMKGLLLGIDEDRTVRLRLIEGKAAEDGTLPEVEIPFGAIVKAKLLLTDALIAKALKDAEALADEGEAAGGAVEGGVA
|
Required for maturation of 30S ribosomal subunits.
|
Q2RMS3
|
A5FX03
|
TIG_ACICJ
|
PPIase
|
Acidiphilium
|
MQVTETLTEGLKRGFTVVVPGSDLSEKREKRLAELSKTMQMPGFRPGKVPLSMVRKRFGDAVAAEVMEASVNEATERMINDRSLRPAVQPKVEVVRAEPDSDLEFTVELEVLPEVTIPDLKAISLTRPKAPVTEAEIDEAIARFAEQRAETEVVTEDRPAATGDILTVDFLGKRDGVPFEGGAGTDTDIELGGSGFIPGFAEQMEGMKAGETKVITVTFPEQYHAAELAGKEATFDITAKALKRRVAPVIDDAFAEANGFENLAEFRKFFADRLEQSRAGASRLKVKRALLDKLAEQADFPAPASLVDAEFAEIWRQVEAEKQAGRLDEEDAGKDEETLRADYRAIAERRVRLGLLVAEIGRTNNVQITEQDMRRAMIAEMQQFPGQEKMIMEFYQKNPRALDRLRGPIFEDKVVDYALELATVTDEEVSAEALFADTDD
|
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
|
A5FX03
|
A7GN87
|
RECU_BACCN
|
Recombination protein U homolog
|
Bacillus cereus group
|
MTIRYPNGKRYNQALQPQKTKMKKHTYGNRGMSLEEELNETNQYYLSHNIACVHKKPTPLQIVKVDYPARSAAVVREAYFKQPSTTDYNGVYKGKYIDFEAKETKNKTNFPLQNFHLHQIEHMKQVIAHDGIAFVIIKFTLYNEIYLLDAKHVISFWNRKDTGGRKSITKQEIEEHGSLLSCGYHPRIDYISILDMVYFS
|
Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation.
|
A7GN87
|
Q83LM0
|
RLMI_SHIFL
|
rRNA (cytosine-C(5)-)-methyltransferase RlmI
|
Shigella
|
MSVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPSESIDIAFFSRRLQQAQKWRDWLAQKDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALITALQTLYPECAIYDRSDVAVRKKEGMELTHGLLTGELPPALLPIEEHGMNLLVDIHHGHKTAYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALMGGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGYKDINMLAIQLLNEGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM
|
Specifically methylates the cytosine at position 1962 (m5C1962) of 23S rRNA.
|
Q83LM0
|
B4NEU3
|
MTNB_DROWI
|
Probable methylthioribulose-1-phosphate dehydratase
|
Sophophora
|
MSLSIFKDLPDEHPRHLIPSLCRQFYHMGWVTGTGGGMSIKLNNEIYIAPSGVQKERMQPEDLFVQDISGKDLQLPPEIKGLTKSQCTPLFMLAYRHRKAGAVIHTHSQHAVMATLLWPGKTFQCTHLEMIKGVYDEADKRYLRYDEKLVVPIIENTPFERDLADSMYAAMMEYPGCSAILVRRHGVYVWGQTWEKAKAMSECYDYLFQLAVEMKKNGLDPEKFEPNC
|
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
|
B4NEU3
|
Q8PH20
|
HPPA_XANAC
|
Pyrophosphate-energized inorganic pyrophosphatase
|
Xanthomonas
|
MLEHYGLWLALGCAVLAIVYGIVSARWVVAQPSGNARMQEIAAAIQEGARAYLNRQYLTISVAGAVLFVLVGLFLSWYTAIGFALGAVLSGLAGYIGMNVSVRANVRTAEAARHGIGKAMDVAFRGGAITGMLVVGLGLLGVAGYFAVLQGMGLPLEQNLHALVGLAFGSSLISIFARLGGGIFTKGADVGADLVGKVEAGIPEDDPRNPAVIADNVGDNVGDCAGMAADLFETYAVTVIATMLLGSLTLADTGSHAVLYPLVLGGVSIIASIVGAAFVKVKDGGSIMGALYKGVIVSGVLAALAYWPITQSLMRDNIHGATALYACALIGLVLTGLIVWITEYYTGTQYTPVQHVASASTTGHGTNIIAGLGISMKSTALPVIAVCAAIWGAFHFGGLYGIAIAATAMLSMAGMIVALDAYGPITDNAGGIAEMAELPPEVRNITDPLDAVGNTTKAVTKGYAIGSAALAALVLFADYTHNLQAANPDQVYAFDLSDHTVIIGLLIGGLIPYLFGAMAMEAVGRAAGAVVEEVRRQFRELPGIMAGTAKPQYDRAVDMLTRSAIGEMIVPSLLPVVVPIIVGLLLGPRALGGLLIGTIVTGLFLAISMTTGGGAWDNAKKYIEDGHFGGKGSEAHKAAITGDTVGDPYKDTAGPAINPLIKIINIVALLLVPLL
|
Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force.
|
Q8PH20
|
Q4FFP2
|
PSBD_NUPAD
|
Photosystem Q(A) protein
|
Nuphar
|
MTIALGRFTKEENDLFDIMDDWLRRDRFVFVGWSGLLLFPCAYFALGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSLAHSLLLLWGPEAQGDFTRWCQLGGLWTFVALHGAFGLIGFMLRQFELARSVQLRPYNAIAFSAPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSALGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENLIFPEEVLPRGNAL
|
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. D2 is needed for assembly of a stable PSII complex.
|
Q4FFP2
|
B0B7W5
|
GRPE_CHLT2
|
HSP-70 cofactor
|
Chlamydia
|
MTETPNTSSEEIQTSEPSPDNELQVLQQENANLKAELQEQNDRYLMALAEAENSRKRLQKERTEMMQYAVENALMDFLPPIESMEKALGFASQTSEEVKNWAIGFQMILQQFKQIFEEKGVVEYSSKGELFNPYLHEAVEIEETTTIPEGTILEEFTKGYKIGDRPIRVAKVKVAKLPAKGNSDSNEEKE
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
|
B0B7W5
|
O84874
|
GLGB_CHLTR
|
Glycogen branching enzyme
|
Chlamydia
|
MDPFFLNTQHVELLVSGKQSSPQDLLGIVSESLNQDRIVLFRPGAETVFVELRGKIQQAESHHSGIFSLPVMKGISPQDYRVYHQNGLLAHDPYAFPLLWGEIDSFLFHEGTHQRIYERMGAIPCEIDGVPGVRFIVWAPHAQRVSVIGDFNGWHGLVNPLHKVSDQGVWELFVPGLTAGACYKWEMVTESGQVLIKSDPYGKFFGPPPWSVSVVIDDSYEWTDSEWLEERIKKTEGPMNIYEVHVGSWRWQEGQPLNYKELADQLALYCKQMHYTHVELLPVTEHPLNESWGYQTTGYYAPTSRYGSFEDLQYFIDTMHQHGIGVILDWVPGHFPIDSFAMSGFDGTPLYEYTRNPSPLHPHWHTYTFDYAKPEVCNFLLGSVLFWIDKMHVDGIRVDAVSSMLYLDYGRYAGEWVPNRYGGRENLDAIRFLQQFNTVIHEKYPGVLTFAEESTTFPKITVSVEEGGLGFDYKWNMGWMHDTLHYFEKDFPYRPYHQSDLTFPQWYAFSERFLLPFSHDEVVHGKRSLIGKMPGDAWRQFAQLRLLLGYQICQPGKKLLFMGGEFGQGREWSPGRELDWELLDISYHQGVHLCSQELNALYVQSPQLWQADHLPSSFRWVDFSDVRNGVVAYLRFADADAKKALLCVHHFGVGYFPHYLLPILPLESCDLLMNTDDTRFGGSGKGFREPEILTPEIARQEREAAGLIEADDESGPDCWGLDIELPPSATLIFSVTLQ
|
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
|
O84874
|
Q8TCE6
|
DEN10_HUMAN
|
Protein FAM45A
|
Homo
|
MAAAEVADTQLMLGVGLIEKDTNGEVLWVWCYPSTTATLRNLLLRKCCLTDENKLLHPFVFGQYRRTWFYITTIEVPDSSILKKVTHFSIVLTAKDFNPEKYAAFTRILCRMYLKHGSPVKMMESYIAVLTKGICQSEENGSFLSKDFDARKAYLAGSIKDIVSQFGMETVILHTALMLKKRIVVYHPKIEAVQEFTRTLPALVWHRQDWTILHSYVHLNADELEALQMCTGYVAGFVDLEVSNRPDLYDVFVNLAESEITIAPLAKEAMAMGKLHKEMGQLIVQSAEDPEKSESHVIQDIALKTREIFTNLAPFSEVSADGEKRVLNLEALKQKRFPPATENFLYHLAAAEQMLKI
|
Guanine nucleotide exchange factor (GEF) regulating homeostasis of late endocytic pathway, including endosomal positioning, maturation and secretion, possibly through activating Rab proteins such as RAB27A and RAB27B. Seems to promote the exchange of GDP to GTP, converting inactive GDP-bound RAB27A and RAB27B into their active GTP-bound form.
|
Q8TCE6
|
B3QYJ4
|
RECR_CHLT3
|
Recombination protein RecR
|
Chloroherpeton
|
MRYTSHAVETLIDEFAKLPGIGRKTAQRLTMFILHEEKEKVESLAQALLDLKNKVSYCSLCQNVTDKEIDPCNICTSVKRDKRVVCVVEAPNDVLAFEKTNQYNGLYHVLHGVISPLDGVGPDDLKVKELIHRLSETDPETSIKEVILAINPTVEGETTVLYLSKLLKPLGVKVTRIARGIPIGTELEYIDDATLTRALEGRSEL
|
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.
|
B3QYJ4
|
B0R6G2
|
PYRG_HALS3
|
UTP--ammonia ligase
|
Halobacterium
|
MPTETEYDPSLGSKFVFVTGGVMSGLGKGITAASLGRLLSNAGFDVTAVKIDPYLNVDAGTMNPYQHGEVYVLDDGGEVDLDLGNYERFLDEDMTSDHNVTTGKVYQDVIERERSGDYLGKTVQIIPHVTDDIKRRVREAAEGSDVCLVEVGGTVGDIEGMPFLEALRQFSHEQDDEDILFTHVTLVPYSKNGEQKTKPTQHSVKELRSIGLQPDILVGRCEDRLDPDVREKIALFCDVPMDAVFSNPDVEDIYHVPLTVEEEGLDQYVMEQFDMVEDALPAAQRSTEWRDLVTRERTGEVDIALVGKYALEDAYMSIHEALKHASLEAGVEVNVLWVDSEKMHDHHERRIADADGIVVAGGFGSRGTAGKIDAIQHAREHDVPFLGLCLGFQLAVVEYARNVLGMTGAHSAEIDEDTEYPVIDLLPEQYDLEDLGGTMRLGAHETAIEPGTLAHDLYGATSCTERHRHRYEVNPEYIDDLTADGLTFSGEAGNRMEIVEHDDHPFFFGTQFHPEYRSRPTRASPPFVGLLDAVLERADVAPAGSDADVEVTN
|
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.
|
B0R6G2
|
Q503L4
|
IAH1_DANRE
|
Isoamyl acetate-hydrolyzing esterase 1 homolog
|
Danio
|
MSALKRVIWPQIILFGDSITQFAFQANGWGSELCHKLERKCDVINRGLSGYNTRWAKIVLPRIVPVSDAPISAVTVFFGANDCALEDKNPTQHVPLQEFSENLKDIVRFLVSKGVSNDNIIFITPPPLLEADWEKECLLKGSPLNRLNSVAGQYAQACVQAAGESGVDVLDLWTLMQKDGQDFSVYLSDGLHLSDKGNQFVAEHLWTLLERRVSDLPFILPYWGDVDPKCPESSLLCD
|
Probable lipase.
|
Q503L4
|
Q12GX4
|
EFG1_POLSJ
|
Elongation factor G 1
|
unclassified Polaromonas
|
MSRATPIQNYRNIGISAHIDAGKTTTTERILFYTGVNHKIGEVHDGAATMDWMEQEQERGITITSAATTCFWKGMDTSLPEHRINIIDTPGHVDFTIEVERSMRVLDGACMVYCAVGGVQPQSETVWRQANKYKVPRLAFVNKMDRTGANFFKVVEQMKLRLKASPVPMVIPIGAEENFTGVVDLLKMKAIIWDEASQGMKFTYSEIPAELVELAKEWREKMVEAAAESSEELMNKYLEEGDLTEAEIKLGIRTRTIASEIQPMYCGSAFKNKGVQRMLDAVIEFMPSPIDIPPVKGMDEDEAPVTRKADDEEKFSALAFKLMTDPFVGQLTFVRVYSGVLKKGDSVYNPIKGKKERIGRIVQMHANNREEVSEIRAGDIAACVGLKDVTTGETLCDPDAIVMLERMVFPEPVITQAVEPKTKADQEKMGIALQRLAQEDPSFRVKTDEESGQTLIAGMGELHLEIIVDRMKREFGVEANVGKPQVAYRETIRKTVEDAEGKFVRQSGGKGQYGHVVLKIEPNEAGKGIEFVDAIKGGVVPREYIPAVEKGINEAVTSGVLAGYPVVDVKVTLHFGSYHDVDSNELAFKMAAIFGFKEGCRKASPVILEPMMAVEVETPEDYAGNVMGDLSSRRGMVQGMEDMVGGGKAIKAEVPLSEMFGYSTTLRSMSQGRATYSMEFKHYSEAPRNVSEAIMASRAK
|
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
|
Q12GX4
|
Q9MUJ7
|
PSAA_ARAAA
|
PsaA
|
Araucaria
|
VERDPIKTSFEKWAKPGHFSKTLSKGPNTTTWIWNLHADAHDFDSHTDDLEEISRKVFSAHFGQLAIILIWLSGMYFHGARFSNYEAWLSDPTHIKPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQLWRASGITSELQLYCTAIGGLIFAGLMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQVHVSLPINQLLDAGVDPKEIPLPHEFILNRDLLAQLYPSFAKGLTPFFTLNWSEYSDFLTFRGGLNPVTGGLWLTDTVHHHLAIAILFLIAGHMYRTNWSIGHSLKEILEAHKGPFTGEGHKGLYEILTTSWHAQLALNLAMLGSLTIVVAHHMYSMPPYPYLAIDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTQYNNLLDRVLRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPIFAQWIQNTHASAPSLTAPDATASTSLTWGGGDLVAVGNKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNAISVVIFHFSWKMQSDVWGSISDQGVVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLLFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPAIQPRALSIVQGRAVGVAH
|
PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
|
Q9MUJ7
|
Q5FFZ7
|
LIPB_EHRRG
|
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
|
Ehrlichia
|
MEWKIESLPVPYDKAMCFMQQRVEGIANKTQDELVWLLEHFPLYTAGTSARSEELLTDSLFPVYSTGRGGKYTYHGPGQRIAYVMMDLKARDKCNVRLYVETLGEWIVKTLKHFSIRSYFNPNLIGVWVNHNGSEKKIAAFGIRIRKWITYHGVSINVFTDLSHYSGIIPCGIKEYGITSLKTLGVNILYEEFDVVLKKEFNKVFCNC
|
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.
|
Q5FFZ7
|
B5FFR4
|
METE_ALIFM
|
Methionine synthase, vitamin-B12 independent isozyme
|
Aliivibrio
|
MTTESKTKTVTHILGYPRVGAQRELKFAQEKYWRGEIEQKELLAVGSELRQRHWKDQSASGLDFVTAGDFAWYDHVLTTSLLLGHVPARHNNGFPDLDTLFKVGRGQSQNSCGCGEAASDMTKWFNTNYHYIVPEFSKNDKFNVSWSQLFDEIAEAQKQGHNVKPVLLGPLSYLWLGKEVNDEEVEQGFDRLSLLPRLLTAYQAIFSKLSALGVEWVQIDEPILALELPKAWADSFKLAYQVIQSDVKLLLTTYFDGVEHHLDKITKLAVNGLHIDVSAAPDQLDAIVSALPKEWVLSVGAVNGRNVWRADLERLHERLQPVKEALGDKLWIASSCSLLHSPVDLEQETELSKETLQWFAFAKQKLREVTLLADALDGNQNAILACHQYSQPLRERESAEHINKPAVQQRLAAITPALAERAEAYSVRAQHQAEKLGLPLLPTTTIGSFPQTSDIRQQRSAYRTGKLNEQDYVTAMKGHIADAVERQERLDLDVLVHGEAERNDMVEYFAENLNGFQATRFGWVQSYGSRCVKPAIVVADIEREAPITVSWTQYAQSLTTKQMKGMLTGPVTILGWTFPREDITRKEIAQQLALVLRDEVSDLQQAGINIIQIDEPAIREGLPIKKSDQKAYLDWAVEAFKISAASAKSETQIHTHMCYSEFNEIIESVAALDADVITIETSRSNMELLKAFEDFNYPNEIGPGVYDIHSPNIPSQEWIVDLIETAAARVPVERLWVNPDCGLKTRNWKETEAALENMVKAAKALRKKWQSNAA
|
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
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B5FFR4
|
Q66C72
|
SYM_YERPS
|
Methionyl-tRNA synthetase
|
Yersinia
|
MAQVAKKILVTCALPYANGSIHLGHMLEHIQADIWVRFQRMRGNQVHFICADDAHGTPIMLKAQQMGIEPEQMIAEMSQEHQQDFAGFAISYDNYHSTHSDENRELSSLIYGRLKANGYIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKAPEQYGDNCEVCGATYSPTELIDPKSAVSGATPVMRESEHFFFDLPAFSDMLQAWTRSGALQEQVANKMQEWFDSGLQQWDITRDAPYFGFEVPDAPGKYFYVWLDAPIGYMGAFKNLCDKRGDLDFDEFWGKDAKTDLYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVHGYVTVNGAKMSKSRGTFIKAGTYLKYLDADCLRYYYAAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRFAGQLADQLADPVLYKTFTDAATSIADAYNNRESGKAIREIMALADVANRYVDEQAPWVVAKQEGHDADLHAICSMGINLFRVLMTYLKPVLPSLTERTEAFLNTELTWDSIEQPLLGHSITAFKALFNRIDLDKVNEMVASSKEDMAPATRVTGPLADDPIQETISFDDFAKVDMRIALIQQAEFVEGSDKLLKLTLELGGETRQIFSGIRSAYPDPKALEGRMTVMVANLAPRKMRFGVSEGMVMTAGPGGSDIFLLSPDSGAQPGMQVK
|
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
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Q66C72
|
Q9A0A6
|
Y865_STRP1
|
DegV domain-containing protein SPy_0865/M5005_Spy0672
|
Streptococcus
|
MKLAVITDSTATLPTDLKQDKAIFSLDIPVIIDDETYFEGRNLSIDDFYQKMADSQNLPKTSQPSLSELDNLLGLLSSKGYTHVIGLFLAGGISGFWQNIQFLAEEHPEIEMAFPDSKITSAPLGSMVKNVLDWSRQGMTFQAILNKLQEQIDGTTAFIMVDDLNHLVKGGRLSNGSALLGNLLSIKPILRFDEEGKIVVYEKVRTEKKAMKRLVEILNDLIADGQYNVFIIHSKAQDKADYLKRLLQDSGYQYDIEEVHFGAVIATHLGEGAIAFGVTPRL
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May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
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Q9A0A6
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Q8N3J3
|
HROB_HUMAN
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Homologous recombination OB-fold protein
|
Homo
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MACSLQKLFAVEEEFEDEDFLSAVEDAENRFTGSLPVNAGRLRPVSSRPQETVQAQSSRLLLLHPTAPSEALGLPDLDLCLPASSTPSADSRPSCIGAAPLRPVSTSSSWIGNQRRVTVTEVLRETARPQSSALHPLLTFESQQQQVGGFEGPEQDEFDKVLASMELEEPGMELECGVSSEAIPILPAQQREGSVLAKKARVVDLSGSCQKGPVPAIHKAGIMSAQDESLDPVIQCRTPRPPLRPGAVGHLPVPTALTVPTQQLHWEVCPQRSPVQALQPLQAARGTIQSSPQNRFPCQPFQSPSSWLSGKAHLPRPRTPNSSCSTPSRTSSGLFPRIPLQPQAPVSSIGSPVGTPKGPQGALQTPIVTNHLVQLVTAASRTPQQPTHPSTRAKTRRFPGPAGILPHQQSGRSLEDIMVSAPQTPTHGALAKFQTEIVASSQASVEEDFGRGPWLTMKSTLGLDERDPSCFLCTYSIVMVLRKQAALKQLPRNKVPNMAVMIKSLTRSTMDASVVFKDPTGEMQGTVHRLLLETCQNELKPGSVLLLKQIGVFSPSLRNHYLNVTPNNLVHIYSPDSGDGSFLKPSQPFPKDSGSFQHDVAAKPEEGFRTAQNLEAEASPEEELPEADDLDGLLSELPEDFFCGTSS
|
DNA-binding protein involved in homologous recombination that acts by recruiting the MCM8-MCM9 helicase complex to sites of DNA damage to promote DNA repair synthesis.
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Q8N3J3
|
Q49162
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ACDE1_METMA
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ACDS complex carbon monoxide dehydrogenase subunit epsilon 1
|
Methanosarcina
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MVDTTKNTKLFTSYGVTTSKAVNPDMVAKMISKAKRPLFVVGTGVLRPEVLDRAVKIAQKANIPIAATGSSLKGFLDKGVDAKYINLHQLGFYLTDPAWPGLDGKGNYDTIIVLEFKKYYINQVLSGTKNFSNVKAISIGRDYIQNATMSFGNISREDHYAALDELIDNL
|
Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.
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Q49162
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Q24QI7
|
HISZ_DESHY
|
ATP phosphoribosyltransferase regulatory subunit
|
Desulfitobacterium
|
MPRSSLGLRIPEGMHDLLPDELALQEQAETSALDLFKAWAYQKVATPTLEYGACIQPVEEEGDSFFKLFDRQGHVLVLRPELTTSIARMVSTRMRGTAFPLRLCYAADVFRYSKSHKQEFRQVGVELIGSASSAADAEVVALAIEALRKIGGMDFQINLGHMGIFTGIMAELGVPQEFQLHYQEKLARKDFVGIERLVKDYGFETRVQDVLLKLPHLHGKEDMLDQVLEWSRRPSLLEAVNALRQVYRYLKDFGVQDYVSLDLGILRGFSYYTGAVFEGYVPGVGFPVVEGGRYDALYGDFGEDAPATGFAINLKAIIEQMVCSNAERPEVLVYGSDVSKVIAEARKLRQTGKRVEMCLESLTQEQAMESAECKGIKEVVCAR
|
Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
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Q24QI7
|
A1WW09
|
DTD_HALHL
|
Gly-tRNA(Ala) deacylase
|
Halorhodospira
|
MITVIQRTGSARVRVGGEVVGEIERGLVALVCAVHGDGSAQAQRLAERVLGYRVFPDAEGRMNGSALDLGCGVLAVPQFTLAADTRKGMRPSFGPAADPQTGQALFETFLEALRERATGPVASGVFGADMQVELVNDGPVTFWLEAPPRPAGPV
|
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. 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 and helps enforce protein L-homochirality.
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A1WW09
|
B5FUG6
|
GCSP_SALDC
|
Glycine dehydrogenase (aminomethyl-transferring)
|
Salmonella
|
MTQTLSQLENRGAFIERHIGPDAAQQQEMLNAVGAESLNALTGQIVPKDIQLATPPQVGEAATEYAALAELKAIAGRNKRFTSYIGMGYTAVQLPPVILRNMLENPGWYTAYTPYQPEVSQGRLEALLNFQQVTLDLTGLDMASASLLDEATAAAEAMAMAKRVSKLKNANRFFVASDVHPQTLDVVRTRAETFGFDVIVDDAAKALDHQDVFGVLLQQVGSTGEIHDYSALISELKARKVIVSVAADFMALVLLTAPGKQGADIVFGSAQRFGVPMGYGGPHAAFFAAKDEFKRSMPGRIIGVSKDAAGNTALRMAMQTREQHIRREKANSNICTSQVLLANIASLYAVYHGPVGLKRIANRIHRLTDILAAGLQQKGLKLRHAHYFDTLCVEVADKAAVLARAEAAEINLRSDIHNAVGITLDETTTRENVAQLFNVLLGGSHGLNIETLDKDVALDSRSIQQSMLRDDAILTHPVFNRYHSETEMMRYMHSLERKDLALNQAMIPLGSCTMKLNAAAEMIPITWPEFAELHPFCPPEQAEGYHQMISQLSDWLVKLTGYDAVCMQPNSGAQGEYAGLLAIRHYHESRNEGHRDICLIPASAHGTNPASAHMAGMQVVVVACDKNGNIDLDDLRAKAEQHAANLSCIMVTYPSTHGVYEETIREVCEVVHQFGGQVYLDGANMNAQVGITSPGFIGADVSHLNLHKTFCIPHGGGGPGMGPIGVKAHLAPFVPGHSVVQIEGMLTRQGAVSAAPFGSASILPISWMYIRMMGAEGLKQASQVAILNANYIASRLKDAYPVLYTGRDGRVAHECILDIRPLKEETGISELDIAKRLIDYGFHAPTMSFPVAGTLMVEPTESEGKAELDRFIDAMLAIRAEIDQVKAGVWPLEDNPLVNAPHIQSELVAEWAHPYSREVAVFPAGVADKYWPTVKRLDDVYGDRNLFCSCVPISDYQ
|
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
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B5FUG6
|
Q9LXD9
|
PME51_ARATH
|
Pectin methylesterase 51
|
Arabidopsis
|
MSSILILLFSLFLFSSPSSSSRHHHHHNSGDTSPVNPSSSLAAQIRLACNATRYPDQCVSSLSEQGRVPPDPKPIQIIHSAISFSFQNLKTAQSKIKSIVDSSVGNLNRTNAANTCLQLLTYSEHRTQSTDQALTRGKIKDARAWMSAALVYQYDSWSALKYVNDTSQVGETMSFLDGLIHVTSNALSMMVSYDNFGDNVASWTYPATERDGFWEKTGPGLGLDPSTGLNLGFPSGLKEDVTVCKDGKCGYKTVQDAVNAAPEDNGMRKFVIKISEGVYEENVIVPFEKKNVVFIGDGMGKTVITGSLNAGMPGITTYNTATVGVVGDGFMARDLTFQNTAGPDAHQAVAFRSDSDFSLIENCEFLGNQDTLYAHGLRQFYKNCRIQGNVDFIFGNSAAVFQDCEILIAPRQINPEKGEKNAVTAQGRIDPSQSTGFVFLNCLINGTEEYMKLFKANPKVHKNFLGRPWKDYSRTVFIGCNLEALITPDGWLPWSGDFALKTLYYGESKNTGPGSDRSQRVSWSSQIPDEHVHVYSVANFIQADEWASMSA
|
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
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Q9LXD9
|
Q5KWS2
|
APT_GEOKA
|
Adenine phosphoribosyltransferase
|
Geobacillus thermoleovorans group
|
MDLKQYITIVPDFPKPGIMFKDITTLMDNGPAYKYATDQIVQYAREKQIEIVVGPEARGFIIGCPVAYALGVGFAPVRKEGKLPREVVRVEYGLEYGTDVLTMHKDAIKPGQRVLITDDLLATGGTMRATIDLVEQLGGVVAGLAFLIELTELGGRKKLEGYDILTLMQF
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
Q5KWS2
|
Q09485
|
RAPSN_CAEEL
|
43 kDa receptor-associated protein of the synapse homolog
|
Caenorhabditis
|
MGQRQAKQHMQAGVKLYHQRHYAQAINKWRQSLNRLNNAEDRFITLGYLAQALCDQGEYEGMLSYALSQMQLATDQNDSAMKCEAFLNLAKAYERLADFTKALQYGKASLEHPSMDPRTPGYAHLTIALAHLGMSQFQQCLESFESAMNVANETSDRLLELQICVGLGSLFTLLRDITKALIFLRNALAIVQSVTVDDVHAKYRCLILYHLSVALRMKGSLVDAKEACDEASQLAVEMGNRAIHARCMCSLADIYRELGESEAKETITKSWARYEDAYRVMRGANDKMGEVLVLSSMAKSASESRSHYTGQCECQAIQLNKKCIEIANQIGCKHVVLKCHLRLAELYSQLNDDDSEETARRAASRLTQEMQLFCNFCGQRYGLKDESLQALRCSHIFHEKCLHTYLLQRTDQTCPKCRCRAVLSDNISIRSSIASTIDVQSPSTSFAPPGGVATPLVSAAAELGDITPQATLTRRSQQDKILRGAEKDIDRVDRSLARLKSQQSAAANACSAVAVPSPEVPSTTASCASEPILTASTTSQSHTHSNANHKPPPPPRKPCCSQAALPPSSIVALPPAMPLAEDGPLVITHTPTVTDV
|
Postsynaptic protein required for clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction.
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Q09485
|
Q6G5C8
|
EFTS_BARHE
|
Elongation factor Ts
|
Bartonella
|
MSITAAQVKELRELSGAGMMDCKAALAETNGDMEAAVDWLRKKGIAKADKKAGRTAAEGLIGVVSQDLSAVLVEINSETDFVARNDVFQDIVRNVATAALGTEGSIDAVCASFYPGSEKTVEATIKDAIATIGENMTFRRSAKLSVEDGVVATYIHNSVAEGLGKLGVLVAIETTGNKKAAAAFGRQVAMHIAATNPLALTAEDVDSSAIEREKAIFSEQARQSGKPENIIEKMVEGRMRKFFEEVVLLSQAFVMNPDITVDAALKDAEKSIGAPAKITAFIRFALGEGVEKEESDFAAEVAAAAKG
|
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
|
Q6G5C8
|
P84022
|
SMAD3_HUMAN
|
SMAD family member 3
|
Homo
|
MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS
|
Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
|
P84022
|
Q3K5V9
|
COQ7_PSEPF
|
2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase
|
Pseudomonas
|
MTTQRHYSPIDRLLLQADAAMRTLLPFSGQPYRPSPAIVQPDVQMSDEDIRHVAGLMRINHTGEVCAQALYQGQALTAKLPQVREAMEHAAEEEIDHLVWCEQRIHQLGSHTSVLNPLFYGMSFGIGAVAGLISDKVSLGFVAATEHQVCKHLNEHLEQLPAEDEKSRAILEQMRIDEEHHAESALEAGGFRFPAPVKFGMSLLAKVMTKSTYRI
|
Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol during ubiquinone biosynthesis.
|
Q3K5V9
|
B1M4N1
|
RNPH_METRJ
|
tRNA nucleotidyltransferase
|
Methylobacterium
|
MRPSKRAADELRPVSLERAVSRYAEGSCLVSFGNTRVLCTASLEERAPPWLRGSGKGWVTAEYAMLPRATHERTRREVGSGKPSGRTQEIQRLIGRSLRAVTNLPAMGERQITIDCDVIQADGGTRTAAITGAWVALHDCFAWMRTRSIISVDPLRDHVAAVSCGLYKGTPVLDLDYAEDSAAETDANFVLTGRGGIVEVQGTAEMEPFTQEQLLELLGLARAGTERLVALQKEAIA
|
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
|
B1M4N1
|
Q8MA04
|
MATK_CHAGL
|
Intron maturase
|
Chaetosphaeridium
|
MERNKNYYINVFHKQAENDLNFNKFYFYFFQETFYCLAYKQVSYKFLQNNVFIKKKKKFSFFNLKRTIRSMRNQNYKESFFFIEQKKLSKKLLFSKLFYELLQEILKCILEISFKIKKNPKISSYSTMSSIHGPFISFEENLIYFPVAIQSYLPNRVHPELIVRILRSYNLDVNLFHFLRNIVHNGLYILSPPFLLNFGFRSLSTIFFNIYAYEIDLGFLSFLKLQKDLPQKYQTELDIFSSSRKITFYFKNYSDFNNLKKIDQIERKYNNIIDYGPIYYLRYSNILLISLNLIKKNANFFQLIYIRFFHLRFHFLFAKNLVKKISFNQDQIFFLGFLVFFFYTKIQIRIKLKKCLVNFIKLEKKICINVPIKLLIIFLSKNGFCDISGNSKSKLSWSVLQDIEIIEKFRRLWLTISGYYSGSSNKYCLKIVLYILRYSCAKTLACKHKMSLKKIWKKYTLNLSVTLKFQTGKKKFLSFSHFKDFHKDEKSWQLNLKETNSIVYTFWN
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
Q8MA04
|
B0B9I2
|
RECF_CHLT2
|
DNA replication and repair protein RecF
|
Chlamydia
|
MRVLSLFLKDFRNYTDLRLELGPEMNSIFGLNAQGKTNLLEALYILSLGRSFRTSRLTDAIRFGASHFFIEAVFSHKEVFHTLSIQVDKKGKKILFDGAPITKLSELVGLFPVILFSIKDIAIIEGSPSERRRFLDLLLAQASDKYTEHISLYHKALDQRNASIKAQNQKAISAWNSPLIAYGSLVAFLRNECTKKLNTIFQTLWDNTLKETLSLRYESSLITEESPTLNDIASNYYEQLRIANTKDLDLGYTMVGPHRDELLLTINDLPVAKFSSEGQKHSLLAVLRFAECVYLQEEFCIHPLLCMDDIHACLDQQRLDQLLQLSNSLGQVVTTSTICPDHRSTTSCIFHVTQAQVSLVAPQSL
|
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
|
B0B9I2
|
Q9BUH8
|
BEGIN_HUMAN
|
Brain-enriched guanylate kinase-associated protein
|
Homo
|
MEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQCSQTYGRVHKVSELPSDFQERVSLHMEKHGCSLPSPLCHPAYADSVPTCVIAKVLEKPDPASLSSRLSDASARDLAFCDGVEKPGPRPPYKGDIYCSDTALYCPEERRRDRRPSVDAPVTDVGFLRAQNSTDSAAEEEEEAEAAAFPAGFQHEAFPSYAGSLPTSSSYSSFSATSEEKEHAQASTLTASQQAIYLNSRDELFDRKPPATTYEGSPRFAKATAAVAAPLEAEVAPGFGRTMSPYPAETFRFPASPGPQQALMPPNLWSLRAKPGTARLPGEDMRGQWRPLSVEDIGAYSYPVSAAGRASPCSFSERYYGGAGGSPGKKADGRASPLYASYKADSFSEGDDLSQGHLAEPCFLRAGGDLSLSPGRSADPLPGYAPSEGGDGDRLGVQLCGTASSPEPEQGSRDSLEPSSMEASPEMHPAARLSPQQAFPRTGGSGLSRKDSLTKAQLYGTLLN
|
May sustain the structure of the postsynaptic density (PSD).
|
Q9BUH8
|
P18779
|
TERB_ALCSP
|
Tellurium resistance protein TerB
|
Alcaligenes
|
MRMSFFDKVKGALTSGREELTRQVGRYKNKKFMQGTVAVCARIAVASDGVSSEEKQKMIGFLRSSEELKVFDTAEVIEFFNKLVTSFDFDLEIGKGETMKYILALKDQPEAAQLALRVGICR
|
Not yet known.
|
P18779
|
Q32RS9
|
PSBC_STAPU
|
Protein CP-43
|
Staurastrum
|
MKTLYSLRRFYHVETLFNGNLAVSGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGIGPGGEVVDTFPYFVSGVLHLISSAVLGFGGVYHALIGPETLEESFPFFGYVWKDKNKMTTILGIHLIILGLGAFLLVFKAVWFGGVYDTWAPGGGDVRKITNLTLNPGVIFGYLLKSPFGGEGWIVSVDNMEDIIGGHVWLGAICIFGGIWHILTKPFAWARRAFIWSGEAYLSYSLAAISMMGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEIIFGGETMRFWDLRAPWLEPLRGPNGLDLAKLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLSTSHFVLGFFFFIAHLWHAGRARAAAAGFEKGIDRETEPVFFMNPLN
|
One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
|
Q32RS9
|
C4K2G3
|
RL18_RICPU
|
50S ribosomal protein L18
|
spotted fever group
|
MRSAKLKFEKRRSRIRHKISKTSHSVRLSIFKSGRHIYAQIIDDSKSITIAAASTLDEKIKKLKKSHCNIENAIKVGEEIAKKADSAGIQDVVFDRGGYKYHGVVKALADAAREKIKF
|
This is one 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.
|
C4K2G3
|
Q9UBN7
|
HDAC6_HUMAN
|
Tubulin-lysine deacetylase HDAC6
|
Homo
|
MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH
|
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) . Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events . Histone deacetylases act via the formation of large multiprotein complexes . In addition to histones, deacetylates other proteins: plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin . Required for cilia disassembly; via deacetylation of alpha-tubulin . Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy . Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer . In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome . Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy .
|
Q9UBN7
|
A0A0E0RXA9
|
FSL3_GIBZE
|
Fusarielin biosynthesis cluster protein 3
|
Fusarium
|
MSVTRLSEPLQNILLQDLRNFYDRASRIATLSVSAIAAIKSAWTRGSPFAAATALYPTNEEGKYVIQAEGIRMEFTNYGGAVTNLWLNNSRGEEVDIVLGLDHARDYEDYPKNPYLNGAIGRYAGFMRGGRFDMDGESYQVATNAHNGSSTFNGGDRGWGRSILDIGSHTENSITFVLFDRSWNGFPGTAASCLTHTVTPYEWRVAFGVTPTKKPGPINMSQQAFFNLDGFKKKNLTGSVPVSDKTVRDHKLHLPLSGLRFETDALGLSTGDILGNPRGSEYDFWSASRRIGDVLEKPYMGICDRCQKRQYHNHNPSGAYDTIFQLGRSQPWNKEDVPAAILSSPESGISMKLYSDQEALHVHTWSQKEFPLKLKKGQGQGMVPQHGGISFEMQDWPDGLNHPEWRRESKTIWGMDGLYTAFSSYRFSVDKTEP
|
Epimerase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells . The initial compound in the pathway is produced by the reducing polyketide synthase FSL1. FSL1 lacks an active enoyl reductase (ER) domain and biosynthesis of fusarielins relies on the trans-acting enoyl reductase FSL5, before it is released through hydrolysis catalyzed by the thioesterase FSL2 . Fusarielins F, G, and H have a C11=C12 cis double bond and is fully reduced between C10 and C11 and between C12 and C13. FSL3 can be involved in the formation of the C11=C12 cis double bond by moving a hypothetical C10=C11 or C12=C13 trans double bond to form prefusarielin . Prefusarielin is oxygenated at C15 and C16 by the cytochrome P450 monooxygenase FSL4, resulting in fusarielin F, which subsequently is epoxidized into fusarielin G by the same enzyme . The final step in the pathway is a reduction of the carboxylic acid moiety to yield fusarielin H via a still undetermined mechanism .
|
A0A0E0RXA9
|
P43236
|
CATK_RABIT
|
Protein OC-2
|
Oryctolagus
|
MWGLKVLLLPVVSFALHPEEILDTQWELWKKTYSKQYNSKVDEISRRLIWEKNLKHISIHNLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLKVPPSRSHSNDTLYIPDWEGRTPDSIDYRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENYGCGGGYMTNAFQYVQRNRGIDSEDAYPYVGQDESCMYNPTGKAAKCRGYREIPEGNEKALKRAVARVGPVSVAIDASLTSFQFYSKGVYYDENCSSDNVNHAVLAVGYGIQKGNKHWIIKNSWGESWGNKGYILMARNKNNACGIANLASFPKM
|
Thiol protease involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen.
|
P43236
|
Q97EK1
|
IF1_CLOAB
|
Translation initiation factor IF-1
|
Clostridium
|
MSKEDVIEMQGTVLESLPNAMFEVELESGQKILAHISGKLRMNFIRILPGDKVTVELSPYDLTRGRITWRAK
|
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.
|
Q97EK1
|
P65212
|
KDPC_MYCBO
|
Potassium-translocating ATPase C chain
|
Mycobacterium tuberculosis complex
|
MRRQLLPALTMLLVFTVITGIVYPLAVTGVGQLFFGDQANGALLERDGQVIGSAHIGQQFTAAKYFHPRPSSAGDGYDAAASSGSNLGPTNEKLLAAVAERVTAYRKENNLPADTLVPVDAVTGSGSGLDPAISVVNAKLQAPRVAQARNISIRQVERLIEDHTDARGLGFLGERAVNVLRLNLALDRL
|
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
|
P65212
|
A7I4X5
|
RS7_METB6
|
30S ribosomal protein S7
|
Methanoregula
|
MAEAEVKAQPEGDAAPQSKALLFNKWDVSEVKVTDPSLVRYVNLTPQIIPHSCGKFSRQEFNKANMMIVERLINRLMQTENNTGKKQLAIGIVRDAFELINKKTKRNPIEVLVEAIGNTGPREETVRLKYGGINVPKSVDTAPLRRVDSAIGFIAEAVWKSSRKSKKPASAILADELIAASKGDAKCYSVGKKEEKERIAKSAR
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center.
|
A7I4X5
|
Q1MA52
|
LEUD_RHIL3
|
Isopropylmalate isomerase
|
Rhizobium
|
MDKFVKLTGVAAPLPVVNVDTDMIIPKDYLKTIKRTGLGTGLFAEARYNEDGSENPDFVLNKPAYRDAKILVAGDNFGCGSSREHAPWALLDFGIRCVISTSFADIFYNNCFKNGILPIKVSQEDLDKLMDDASRGSNAILTVDLENLEITGPDGGLIKFDLDEFKRHCLLNGLDDIGLTLEKGKAIDSFEKKNAASHPWAA
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
Q1MA52
|
Q5QP82
|
DCA10_HUMAN
|
WD repeat-containing protein 32
|
Homo
|
MFPFGPHSPGGDGSAGAGAEEPTPHEGQAAATGPPSPLHPGADATHPPPPARSPRRPGAPSLSPAPRSGELGLPGAPESSTASAPGEPSPPSPPCRRPGPDCRAKSRGRHGLGAGLGGPGARLFGWLKERSLGRGLFVDPARDNFRTMTSLYGSIHPADSVYLSTRTHGAVFNLEYSPDGSVLTVACEQTEVLLFDPISSKHIKTLSEAHEDCVNNIRFLDNRLFATCSDDTTIALWDLRKLNTKVCTLHGHTSWVKNIEYDTNTRLLVTSGFDGNVIIWDTNRYTEDGCPHKKFFHTRFLMRMRLTPDCSKMLISTSSGYLLILHDLDLTKSLEVGSYPILRARRTTSSSDLTTSSSSSGPRVSGSPCHHSDSNSSEKHMSRASQREGVSPRNSLEVVTPEVLGESDHGNCITSLQLHPKGWATLLRCSSNSDDEECTCVYEFQEGAPVRPVSPRCSLRLTHYIEEANVGRGYIKELCFSPDGRMISSPHGYGIRLLGFDKQCSELVDCLPKEASPLRVIRSLYSHNDVVLTTKFSPTHCQIASGCLSGRVSLYQPKF
|
May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.
|
Q5QP82
|
Q1LUK1
|
MIC13_DANRE
|
MICOS complex subunit MIC13
|
Danio
|
MAAKIFPVVKFATKVTIAGGALYVAYDSGLLGGSNEGSVALARAKSAIPPAVDEWMKYFGFELPATPKIEFSPLDAWNSGVQKSIHALSVAPSTVGDYTKQGLQYVKDLSK
|
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Constituent of mature MICOS complex, it is required for the formation of cristae junction (CJ) and maintenance of cristae morphology. Required for the incorporation of MIC10 into the MICOS complex.
|
Q1LUK1
|
Q5PGH0
|
MSBA_SALPA
|
Lipid A export ATP-binding/permease protein MsbA
|
Salmonella
|
MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMILRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILVVLAPIVSIAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDEGKRVIDRATGDLEFRNVTFTYPGREVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGHILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLMIAHRLSTIEQADEIVVVEDGIIVERGTHSELLAQHGVYAQLHKMQFGQ
|
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.
|
Q5PGH0
|
O97398
|
CTR_PHACE
|
Chymotrypsin
|
Phaedon
|
MKVALVVLALFGVSLAASIDNIEIPPSKNIYVEPINQPEVDPSLEIVNGQEVVPHSIPYQIFLVASAGETSWTCGGSLITKRYVLTAAHCIQGAKSVHVTLGAHNLAKHEASKVTVNGRSWVIHEKYDSTNIDNDIGVIQLERNLTLTRSIQLARLPSLRDVGINLEGRTATVSGWGLTNGIFQTTTDVLRANNTIISNKECNDVFKIVQPTEVCLSIAGGRSACSGDSGGPLVIDNVQHGIVSYGSSYCRSTPSVFTRVSSYLNWLQTHSEWRAQ
|
Serine protease with chymotryptic and collagenolytic activities.
|
O97398
|
Q5L0P0
|
RNH2_GEOKA
|
Ribonuclease HII
|
Geobacillus thermoleovorans group
|
MKRYTVKDIEALLPKLGADDPRWEMLRQDERKSVQALLARFERQKARRHAIEQRWEELMRYERELYAAGVRRIAGIDEAGRGPLAGPVVAAAVILPKDAYLPGLDDSKRLTPEKREALFAQIEACAVAIGIGIVSAAEIDERNIYEATRQAMAKAVNALSPPPEHLLVDAMAVPCPLPQQRLIKGDANSASIAAASVIAKVTRDRWMKELDRRYPQYGFARHMGYGTPEHFEAIRRYGVTPEHRRSFAPVREVLKASEQL
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
Q5L0P0
|
B4TQ44
|
END8_SALSV
|
Endonuclease VIII
|
Salmonella
|
MPEGPEIRRAADNLEAAIKGKPLTDVWFAFAQLKPYESQLTGQIVTRIETRGKALLTHFSNGLTLYSHNQLYGVWRVIDTGEIPQTTRILRVRLQTADKTILLYSASDIEMLTADQLTTHPFLQRVGPDVLDARLTPEEVKARLLSPRFRNRQFSGLLLDQAFLAGLGNYLRVEILWQVGLTGQHKAKDLNEAQLNALSHALLDIPRLSYTTRGQADENKHHGALFRFKVFHRDGEACERCGGIIEKTTLSSRPFYWCPHCQK
|
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
|
B4TQ44
|
B4S4S7
|
RBFA_PROA2
|
Ribosome-binding factor A
|
Prosthecochloris
|
MSIRTGKVSSLLQKELSSIFEKELPRSGPLLTIVEVKVTADLGIARVYVSLIGSEKERGLLMEHLQNETKYIRKLLSSRIRHQFRRIPELEFYEDEQYDKARRIEELLKEALNRPGEEQTES
|
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
|
B4S4S7
|
O69267
|
GRPE_LYSSH
|
HSP-70 cofactor
|
Lysinibacillus
|
MIMRRIQVTETTENKDLVQGDVQAETATEEVERSEVQEEIELSVEEQYEANVAELQAKLDDDEENRHLRLRADFDNMRRRQQLDGEAAEKYRAQSLLSDLLPVLDNFERALQVETTSEETASIIKGIEMVYRSLLEATVFEGLQVIKAEGEQFDPNIHQAVMQEQDSEKETGVVLRELQKGYILKDRVLRPTMVSVNE
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
|
O69267
|
Q93ZV7
|
LA1_ARATH
|
La protein 1
|
Arabidopsis
|
MSIPCLTEETAKTVLRQVEFYFSDSNLPIDDFLKKTVTESEDGLVSLALICSFSKMRGYLKLGDSKGDDIPEDTIKAVADTLRTSSALKISDDGKKVGRSTELLKLEDLIEQLNARTVAASPFSYDVKREDVESFFSQYGKVNSVRMPRHVAESRIFSGVALVEFPTEEDAQNVMKQNLVFAGQELELKPKKEFDNEREKDEVKFANYQPQKGSANQKNGSDHKNNSAYEPDYPKGLIISFTLKRSAEEGTTEQKSSEEPTDKTMEESETKPADTPDADKENTGEVQAEGAEDEDDEKEEKGALATHKDNKDVVLREDLKAVFGKFGDVKFVDFKMGSETGYLRFDEPEASQKARAAAVLANEGGLAVKNFIAVLEPVIGEAEKEYWTLLRSKDRFDKGGRGGRGGRRGGRFGRKRGSDSPGGRWNKSQKVEA
|
Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation.
|
Q93ZV7
|
P15922
|
PEHX_DICCH
|
Exo-poly-alpha-D-galacturonosidase
|
Dickeya
|
MKVITFSRRSALASIVATCLMSTPALAATAQAPQKLQIPTLSYDDHSVMLVWDTPEDTSNITDYQIYQNGQLIGLASQNNDKNSPAKPYISAFYKSDAANFHHRIVLQNAKVDGLKAGTDYQFTVRTVYADGTTSNDSNTVTTTTTAVPKVINITQYGAKGDGTTLNTSAIQKAIDACPTGCRIDVPAGVFKTGALWLKSDMTLNLLQGATLLGSDNAADYPDAYKIYSYVSQVRPASLLNAIDKNSSAVGTFKNIRIVGKGIIDGNGWKRSADAKDELGNTLPQYVKSDNSKVSKDGILAKNQVAAAVATGMDTKTAYSQRRSSLVTLRGVQNAYIADVTIRNPANHGIMFLESENVVENSVIHQTFNANNGDGVEFGNSQNIMVFNSVFDTGDDSINFAAGMGQDAQKQEPSQNAWLFNNFFRHGHGAVVLGSHTGAGIVDVLAENNVITQNDVGLRAKSAPAIGGGAHGIVFRNSAMKNLAKQAVIVTLSYADNNGTIDYTPAKVPARFYDFTVKNVTVQDSTGSNPAIEITGDSSKDIWHSQFIFSNMKLSGVSPTSISDLSDSQFNNLTFSNLRSGSSPWKFGTVKNVTVDGKTVTP
|
Contributes significantly to bacterial utilization of polygalacturonate and the induction of pectate lyase in the presence of extracellular pectic polymers.
|
P15922
|
B3N666
|
IHOG_DROER
|
Interference hedgehog
|
Sophophora
|
MTLLTSSLLLFSLLTSRLEAIPVLEKSPAHPAHSAHPAHPSHPSPGVRILRAPESLVAPLGDEVVLECETSLQPERFEWSHRSSRSQGAGFKYLRTGTAKANVSQEAAISRLRVLVREDTLGEYRCVGWFGPLVVTSTIARLELASTSLVGAQESESPLQWRVAAGNSVLWSCGQQVQSNPSASWSYYRNGVEIKPEFIGTNGNLILSNVSSESSGSYSCQATNPASGERIQLPGLLQLQVTPEQRSLSKSPHLLKGQPSSQEITIREGSSLLLLCPGVGSPPPTVVWSSPDVVGAVKNKRSKVFGHALEISDTRVQDAGTYICFQDNGVRPALEHYIKVHVEQPPQIVRPPWADLTNEGDRLKLECEATGVPSPEIYWLLNGHSSIDDTEAELSNNFLILHSVLKRHAGYVQCFARNRLGEHSAGTLLQVNPKQIQEPRESGGTHRPKPNQGSKQKQMYPPSPPNVTRLSDESVMLRWMVPRNDGLPIVIFKVQYRMVGKRKNWQTTNDNIPYGKPKWNSELGKSFTASVTDLKPQHTYRFRILAVYSNNDNKESNTSAKFYLQPGAALDPMPVPELLEIEEYSETAVVLHWSLASDADEHLITGYYAYYRPSSSAGEYFKATIEGAHARSFKIAPLETATMYEFKLQSFSAVSASEFSALKQGRTQRPKTSTTEEPTLQMGDRDTTTPSHNETFNMSPMLTGTLGGGAVLTLLLISICLCVCRRRSSRSRGNNPNKPRMAELRDDFVPLGNCSPTKQRQRTRHIHITLNPLAQQQQGMEEKNDTDQDAPYYQRPSSYDYDPGLRRMSSSSLRRSQRTLERAGGSNGSNNGNNNNLNQSTETGPVENPGKPGRVLMKRPRLSSRSENLSSGSLNSVGV
|
Mediates response to the active Hedgehog (Hh) protein signal in embryos, functioning upstream or at the level of patched (ptc).
|
B3N666
|
B0XW47
|
AMPP3_ASPFC
|
Prolidase
|
Aspergillus subgen. Fumigati
|
MMAAVDAILAGKYPAKAHARRVAESLQSYRNGCPGIVYLEAQKTRLIEDNDEPAPFRQRRPFFYLSGCPLPDSCLVYDLSEDQLTLFIPPVDPEDVIWSGLPMSTEEAQNQYDVDRVLVTTELNSTLASIVSSHGGKAIAFTIADQVSESTQFHGFSEVNHSVLKGVIEQSRVVKDEYEVALLRKANDISAKAHIAAIKASQTAVNEREIEGAFIATCIANGAREQSYHPIVACGENGATLHYGKNDDTLIDPVTNQKKRNVLIDAGGEYRTYCADITRVIPVGGKFTAETRQIYDIVLQMQTECIAMLKEGVQWEDVHAHAHRVAIRGLLKLGILRGAEDEIFEKRVSVAFFPHGLGHYLGMDTHDTGGNPNYADKDTMFRYLRVRGRLPAGSVITVEPGVYFCRFIIEPYIKSPESNKYIDTNVLDRYWRVGGVRIEDNVLVTKDGYDNLTTAPKAVDELERLAAS
|
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
|
B0XW47
|
B5XNB5
|
RS4_KLEP3
|
30S ribosomal protein S4
|
Klebsiella
|
MARYLGPKLKLSRREGTDLFLKSGVRAIDTKCKIEQAPGQHGARKPRLSDYGVQLREKQKVRRMYGVLERQFRNYYKEAARLKGNTGENLLALLEGRLDNVVYRMGFGATRAEARQLVSHKAIMVNGRVVNIASYQVKANDVVSIREKAKKQSRVKAALELAEQREKPTWLEVDAGKMEGTFKRQPERSDLSADINEHLIVELYSK
|
With S5 and S12 plays an important role in translational accuracy.
|
B5XNB5
|
B3A0M2
|
SLS4_TRYBB
|
Sphingomyelin synthase
|
Trypanosoma
|
MISYPFFSLSPPGLVPPPMAVPPVEMYSGSFWNRMRKPLPLRTQVIRFTVVFVIVSFILAVALQITHERMPDPKVTKPLPDLGFELLTKVPGMYVLADCCIGFLNILSVFTAFKLYLLHRHCVGSGEPELPCNIPGVSRFFLSVWLCKENCRIELRNIHTIAWIRFITSYALLLLFRSAVIVMTSLPAPDDLCQDPPKIENPVKNVILTVLTAGGGSIHCGDLMYSGHTVILTLHLMFHWIYGAMVHWSFRPVVTVVAIFGYYCIVASRFHYTDDVLVAIYLTIATFIAVGHNADGAPWQLQLFIRWWPCCGANSREVTEDSQPVMVAFKSEELDEMNGVLEGRQKKHGGVGDGESLMFKCGAYV
|
Bidirectional lipid cholinephosphotransferase capable of converting inositol phosphorylceramide (IPC) to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target.
|
B3A0M2
|
B1I5R2
|
COBQ_DESAP
|
Cobyric acid synthase
|
Candidatus Desulforudis
|
MTARVLMVQGTSSSAGKSLIVAGLCRLYARRGFRVAPFKSQNMALNSYATPDGREIGRAQALQAEAAGVPPHVDMNPILLKPTGEAGSQVVLLGRPLGVYKPANYYALKEKLWPLAAAALDRLRADADLVFAEGAGSPAEINLRPHDIANMEVALYAGASVLLVGDIERGGVFASLLGTMELLAERERELVAGFVVNKFRGDEELLRPGLALIGARTGRPVLGVLPYLHDLHLDEEDSVGLSGRGKAPAPGDLAVAVIRLPRISNYTDFLPLETENGVALCYVDRPQELDGAHAVILPGSKETLADLAWLRRRGLDRALRDFAARGKPLLGICGGFQMLGRTIREGGQTVAGLGLLPVRTRFASEKRTVQVRGVTAEGVWGIPGGLSVRGYEIHRGFSEVCGGRPCFLLGGQGTGLAPEGCAAEEGYVAGTYLHGCFDSDTYRTQWIAAVRRLAGLPARPSEQPGFAARRQRDLDRIADLLAERIGVERLDGILGL
|
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
|
B1I5R2
|
B7LQN3
|
SYY_ESCF3
|
Tyrosyl-tRNA synthetase
|
Escherichia
|
MASSNLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTADSLHLGHLVPLLCLKRFQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEETVQEWVDKIRKQVAPFLDFDCGENSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNREDQGISFTEFSYNLLQGYDFACLNKLYGVSLQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTEGGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIEEINALEEEDKNSGKAPRAQYVLAEQVTRLVHGEEGLQAAKRITECLFSGSLSALSEADFEQLAQDGVPMVEMEKGADLMQALVDSELQPSRGQARKTIASNAVTINGEKQSDPEYFFKEEDRLFGRFTLLRRGKKNYCLICWK
|
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
|
B7LQN3
|
B2JJK2
|
ATPD_PARP8
|
F-type ATPase subunit delta
|
Paraburkholderia
|
MAELATIARPYAEALFGVAEAGDIAAWSTLVQELAQVARLPDVLSIASSPKVSRAQISDLLLAAVKSPLKDNAQAKNLVQMLVDNHRLPLLPEIATQFEELKNAREGAADALIVSAFPLEGAQLDGLVASLERKFKRKLKPTVQVDSSLIGGVRVTVGDEVLDTSVRARLASMQTALTA
|
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.
|
B2JJK2
|
Q9ERD9
|
I23O1_RAT
|
Indoleamine-pyrrole 2,3-dioxygenase
|
Rattus
|
MPHSQISPAEGSRRILEEYHIDEDVGFALPHPLEELPDTYRPWILVARNLPKLIENGKLREEVEKLPTLRTEELRGHRLQRLAHLALGYITMAYVWNRGDDDIRKVLPRNLAVPYCELSEKLGLPPILSYADCVLANWKKKDPNGPMTYENMDILFSFPGGDCDKGFFLVSLMVEIAASPAIKAIPTVSSAVEHQDPKALEKALCSIAASLEKAKEIFKRMRDFVDPDTFFHVLRIYLSGWKGNPKLPEGLLYEGVWDTPKKFSGGSAGQSSIFQSLDVLLGIKHDVGEGSAAEFLQEMREYMPPAHRNFLSSLESAPPVREFVILRRNEDLKEAYNECVNGLVSLRMFHLSIVDTYIVKPSKQKPMGGHKSEEPSNTENRGTGGTDVMNFLRSVKDTTKKALLSWP
|
Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. Involved in the peripheral immune tolerance, contributing to maintain homeostasis by preventing autoimmunity or immunopathology that would result from uncontrolled and overreacting immune responses. Tryptophan shortage inhibits T lymphocytes division and accumulation of tryptophan catabolites induces T-cell apoptosis and differentiation of regulatory T-cells. Acts as a suppressor of anti-tumor immunity. Limits the growth of intracellular pathogens by depriving tryptophan. Protects the fetus from maternal immune rejection.
|
Q9ERD9
|
Q75VB5
|
MATK_QUECE
|
Intron maturase
|
Quercus
|
MEEFQGYLELDRFRQHDFLYPFIFREYSYALAHGHGLNRYMLLENIGYDNKSSLLIVKRLITTMYQQNYLIISANDSKQNPFFGYNKNLHSKILSEGFAIIVEIPFYLRLISSLEGAEIVRFYNLRSIHSIFPFLEEKFPHLNYSADILIPYPAHLEILVQTLRYRVKDASYLHLLRFFLHEYSNCNSLIITNKSISIFSKSNPRFFLFLYNSYLCEYESIFLFLRNQSSHLRLTSSGVLFERLCLYRKIEHFAEVFANDFPVIPCFLKDPFMHYVRYQGKSILASKDTPLLMNKWKSYLVNLWQCHFDVWSHAASIRINQLSKHSLDFLSYFSSVRRNPAVVRNQMLENSFLLNNAPNKLDTIVPIIPLIGSLAKAKFCNAVGHPISKLTRADLSDFEIINRFLHICRNLSHYYSGSSKKKNMYRIKYILRLSCVKTLARKHKSTARAFLKRVDSEFFQEFFTEEGGFISLIFPRASFALRRLYSGRVWYLDIIFINGLSNHE
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
Q75VB5
|
A4XI81
|
DTD_CALS8
|
Gly-tRNA(Ala) deacylase
|
Caldicellulosiruptor
|
MRAVVQRVKRASVAVDGNAVGEIDKGLCILLGVANDDTEEDANYLCEKIVNLRIFEDETSKFNLSLKDIDGEVLVVSNFTVMGDARKGRRPNFMFAADKEKAERLYNYFVERLKGLAKKVECGIFQAHMEVEIVNDGPVTILLDSKKVF
|
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. 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 and helps enforce protein L-homochirality.
|
A4XI81
|
A6WX66
|
SECB_BRUA4
|
Protein-export protein SecB
|
Brucella
|
MSDKAAGEVKNGNGATAEPSLNILAQYVKDLSFESPGAPLSLRPREKAPSININVNVNANPLSETDFDVVLTLEAKAVDGKDVLFNTELVYGGVFRIQGIPQEHMLPLLFIECPRLLFPFARQIIADATRNGGYPPLMIDPIDFAQMFQQRMAEEQAKSAVKS
|
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.
|
A6WX66
|
Q2NIC5
|
CDC6_METST
|
ORC1-type DNA replication protein
|
Methanosphaera
|
MNNIFKTINNKDSIFLTKKYLDHRFIPETLPHRDEKIKSIAQYWVESLDKITPPDITIYGKTGTGKTAVTLYAKKQLEEVAAEQNLNIRVEYIRCTDYNTEYQILARLCQQLGKPVPYRGWTKAEVVNAFRNLFKKNILGEDLILIVILDEVDVILKNDGDNILYTLTRTDNVAITSISNYIDFKQFIKPKVKSSLRDREIVFPPYNAQQLIDILKERSKVSFSEGAISEGVIALCSALAAKEEGDARYALDLLKTSGEIADEKESSVIEESFVKEAKDRIEHSKIIDVVVTLPIQQQKVLESITYLTKKREEITSGRLYEVYQDLAKNDKVSYRRIFDFINELEMLGLISTNTISRGRGKGRTNIITLQCDIELIDKALIYKD
|
Involved in regulation of DNA replication.
|
Q2NIC5
|
O09112
|
DUS8_MOUSE
|
Neuronal tyrosine threonine phosphatase 1
|
Mus
|
MAGDRLPRKVMDAKKLASLLRGGPGGPLVIDSRSFVEYNSCHVLSSVNICCSKLVKRRLQQGKVTIAELIQPATRSQVDATEPQDVVVYDQSTRDASVLAADSFLSILLSKLDGCFDSVAILTGGFATFSSCFPGLCEGKPATLPSMSLSQPCLPVPSVGLTRILPHLYLGSQKDVLNKDLMTQNGISYVLNASNSCPKPDFICESRFMRIPINDNYCEKLLPWLDKSIEFIDKAKLSSCQVIVHCLAGISRSATIAIAYIMKTMGMSSDDAYRFVKDRRPSISPNFNFLGQLLEYERSLKLLAALQTDGPHLGTPEPLMGPAAGIPLPRLPPSTSESAATGSEAATAAREGSPSAGGDAPIPSTAPATSALQQGLRGLHLSSDRLQDTNRLKRSFSLDIKSAYAPSRRPDFPGPPDPGEAPKLCKLDSPSGGTLGLPSPSPDSPDSVPECRPRPRRRRPPASSPARSPAHGLGLNFGDTARQTPRHGLSALSAPGLPGPGQPAGPGGWVPPLDSPGTPSPDGPWCFSPEGAQGPGAVFSAFGRVSAGAPGPGNSSSSGGGGGGGGGGGGGGGGGGSSSSNSSSSSSSSSSSSSSSSSSSDLRRRDVRTGWPEEPAADAQFKRRSCQMEFEEGMVEGRARGEELAALGKQTSFSGSVEVIEVS
|
Has phosphatase activity with synthetic phosphatase substrates and negatively regulates mitogen-activated protein kinase activity, presumably by catalysing their dephosphorylation . Expected to display protein phosphatase activity toward phosphotyrosine, phosphoserine and phosphothreonine residues (Probable).
|
O09112
|
Q99PT1
|
GDIR1_MOUSE
|
Rho-GDI alpha
|
Mus
|
MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVAVSADPNVPNVIVTRLTLVCSTAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVSGMKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPMEEAPKGMLARGSYNIKSRFTDDDKTDHLSWEWNLTIKKEWKD
|
Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1.
|
Q99PT1
|
P91124
|
RIC19_CAEEL
|
ICA1 homolog
|
Caenorhabditis
|
MAAQFYERNTSGMNADRFMTRLTDESTVNTMQRHYWTARQFIRTKLGKKEDEHLEASDNELDTCLNLYRSVHGTSFQLLNNVDNYANFLLDETLVQNVLGKYLKEKGKIDKTEAVGRILIAVGRSLLFSSHRLNAARIGVSTFYNKLSVFVERAIGDCSQTIEAVQMCRTEYRGSLLWMKKTSEELDPEVDGSMEKFREAQTTVKSNKERLDRLKTDTLQKVDLLSASRSNLLSYVLTHYQNELYEYYSKTSRAFETLAENINCYNNYDFEILSHLATGTKPERERKSEKEESAKTSQPRGNEEELKNLLFGRESPQFGEEEVQDESRSQCDSPLIEDVDDERRKTGDLLDLESAASIAFPIGPLATLFDTSSFVPPILPPPKPNAVSDDILSLFDGNKANSSGKEASATTMDWQSLIDGFDRENEDNLL
|
May be involved in neurotransmitter secretion . In association with the GTPase activator protein tbc-8 activates rab-2 during dense core vesicle maturation in cholinergic motoneurons .
|
P91124
|
Q5M7E0
|
F210A_XENLA
|
Protein FAM210A
|
Xenopus
|
MHLLRTLLLRSNTSNISLLTKCSFRASPLHKWPISLRSGSQISLLPTEQKKWLHSQPKQQDTATKTPVHDLPSGIQHQSEETSPSARSSISTDPSSIAEEDPLQDQSIGLLKRFKKTFRQHGKVLIPVHLVTSSIWFGSFYYAAMQGVNVVPFLEYIGLPDGIVNILKNSQGGNALTAYAMYKIATPARYTVTLGGTSVSVKYLRKYGYLSTPPLVKDYFQDRMEETKELFTEKMEETRDIISGKMEETKDRISEKLQETKDRVAFRKKKNEDME
|
May play a role in the structure and strength of both muscle and bone.
|
Q5M7E0
|
Q48AB7
|
CYOE_COLP3
|
Heme O synthase
|
Colwellia
|
MPSVINTGHHHFSISNIFANWRAYYDITKPKVVALLVLTALVGMSLSVPGALPWQRLIPAMLGIGLLSSAAAAINHIVDEKIDTVMGRTHNRPLPAGKISVTNAIVFATSIALLGFIILYALVNPLTAFLTLAGLVGYSFVYTMYLKRATPQNITIGGLAGAIPPLLGWTAMTNEVVPNALLLVLIIFTWTPPHFWALAIHRKNDYAKVNIPMLPVTHGVSFTKTQILLYTVLLFVVCLLPYLVGMSNWLYLIGACSLNLIFFGYAWQLKFNAKEGTAMATFKFSIIHLMLLFIILLLDHYWLPMG
|
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
|
Q48AB7
|
Q08185
|
RBS5_MESCR
|
Ribulose bisphosphate carboxylase small subunit, chloroplastic 5
|
Mesembryanthemum subgen. Cryophytum
|
MASSLMSNAATTMAAATTTAQANMVAPFNGLKSISAFPVTRKNNDITSVASNGGRVQCMVWPPLGMKKFETLSYLPPLSEESLLKEVQYLLNNGWVPCLEFEPTHGFVYREHGNTPGYYDGRYWTMWKLPMFGCTDPSQVVAELEEAKKAYPEAFIRIIGFDNVRQVQCVSFIAYKPASYGA
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.
|
Q08185
|
B3PMI7
|
RS15_META1
|
30S ribosomal protein S15
|
Metamycoplasma
|
MVSKQKIEELVKKFGRNAKDTGHLPVQIAILTEKIESLKKHFEANKKDLHSMRGFIAKVNHRKALLSHLKSSNYELYLETIKALNIRK
|
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
|
B3PMI7
|
P0DD98
|
RL10_STRP3
|
50S ribosomal protein L10
|
Streptococcus
|
MSEAIIAKKAEQVELIAEKMKAAASIVVVDSRGLTVDQDTVLRRSLRESGVEFKVIKNSILTRAAEKAGLDELKDVFVGPSAVAFSNEDVIAPAKVINDFTKTADALEIKGGAIEGAVSSKEEIQALATLPNREGMLSMLLSVLQAPVRNVAYAVKAVAENKEGAA
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
P0DD98
|
A9KNS9
|
END4_LACP7
|
Endonuclease IV
|
Lachnospiraceae
|
MLKIGSHVGMSGKEAFFGSAKEAHSYDANTFMVYTGAPQNTRRKDISDLRLEEGFEFMKQHGISDIVIHAPYIINLGNSVNLDTYSLAVDFLAKEMERTKAFRSKYLVLHPGAHVGAGVDAGIKQIVQGLNEVLTRDTDLYIALETMAGKGSEIGRNFEELARIYDGVKYNDRLRVCFDTCHTNDAGYDVVNDFDGVIEQFDKLIGKEQIAVFHINDSKNDRGASKDRHENIGFGTLGFDAISYIVHHSDFIEVPKILETPYVSLPNEKEKSLPPYRYEIEMLRNSVFDPQILEKIQNNR
|
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
|
A9KNS9
|
P56579
|
PTHC_ECOLI
|
Glucitol/sorbitol permease IIC component
|
Escherichia
|
MIETITHGAEWFIGLFQKGGEVFTGMVTGILPLLISLLVIMNALINFIGQHRIERFAQRCAGNPVSRYLLLPCIGTFVFCNPMTLSLGRFMPEKYKPSYYAAASYSCHSMNGLFPHINPGELFVYLGIASGLTTLNLPLGPLAVSYLLVGLVTNFFRGWVTDLTTAIFEKKMGIQLEQKVHLAGATS
|
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The enzyme II complex composed of SrlA, SrlB and SrlE is involved in glucitol/sorbitol transport. It can also use D-mannitol.
|
P56579
|
A1B9F0
|
TRMFO_PARDP
|
Folate-dependent tRNA(M-5-U54)-methyltransferase
|
Paracoccus
|
MEPIHIIGAGLAGSEAAWQIARAGVPVVLHEMRPQVATFAHRTGDCAEMVCSNSFRSDDDRMNAVGQLHWEMRAAGGLIMAMADRHRLPAGGALAVDRDAFSQAVTQALQAEPLVSFQPGEISDLPSEGHWIVATGPLTSEALGRSIRSLTGEGSLAFFDAIAPIVHAESIDMSICWRQSRYDKGETEEERTAYINCPMTREDYEGFIDALLAADKTEFHEGETAGYFDGCLPIEVMAERGRETLRHGPMKPVGLTNAHNPAEKPYAVVQLRRDNALGTLYNIVGFQTKMKYGAQVDVFRRIPGLQDASFARLGGIHRNTFLNSPRLIDDRLRLRARPHLRFAGQVTGVEGYVESAAMGLLAGRMAAAEALGRDLPPPPATTSMGALVSHITGGADAKTFQPMNVNFGLYPPLDAMRGGRKGRKDRYPAYTDRAKADFQQWVAGES
|
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
|
A1B9F0
|
A8AKQ2
|
DPO4_CITK8
|
DNA polymerase IV
|
Citrobacter
|
MRKIIHVDMDCFYAAVEMRDNPALRDIPIAIGGSRERRGVISTANYPARKFGVRSAMPTGMALKLCPHLTLLPGRFEAYKEASQHIREIFSRYTSRIEPLSLDEAYLDVTDSTYCHGSATLIAQEIRQTIFNELQLTASAGIAPVKFLAKIASDLNKPNGQYVITPADVPEFLKTLPLGKIPGVGKVSAARLETMGLRTCEDVQKYDLAMLLKRFGKFGRVLWERSQGIDERDVNNERLRKSIGVERTLAEDIHEWAECEAIIERLYPELERRLAKVKPDLLIARQGVKLKFNDFQLTTQEHVWPRLSKDDLITTARKTWNERRGGRGVRLVGLHVTLLDPQLERQLLLGL
|
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
|
A8AKQ2
|
A5VYR4
|
QUEA_PSEP1
|
Queuosine biosynthesis protein QueA
|
Pseudomonas
|
MRVADFSFELPDSLIARHPLAERHGSRLLVLDGPTGALAHRQFPDLLDYLRPGDLMVFNNTRVIPARLFGQKASGGKLEVLVERVLDSHRVLAHVRASKAPKVGAVILIDGGGEAEMVARHDTLFELRFTEEVLPLLDRVGHMPLPPYIDRPDEGADRERYQTVYAQRAGAVAAPTAGLHFDEALLEKIADKGVERAFVTLHVGAGTFQPVRVDKIEDHHMHKEWLEVGQDVVDAIEACRARGGRVIAVGTTSVRSLESAARDGVLKAFSGDTDIFIYPGRPFHVVDALVTNFHLPESTLLMLVSAFAGYPETMAAYAAAVEHGYRFFSYGDAMFITRNPAPRGPEDQA
|
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
|
A5VYR4
|
P52632
|
STA5B_RAT
|
Signal transducer and activator of transcription 5B
|
Rattus
|
MAMWIQAQQLQGDALHQMQALYGQHFPIEVRHYLSQWIESQAWDSIDLDNPQENIKATQLLEGLVQELQKKAEHQVGEDGFLLKIKLGHYATQLQNTYDRCPMELVRCIRHILYNEQRLVREANNGSSPAGSLADAMSQKHLQINQTFEELRLITQDTESELKKLQQTQEYFIIQYQESLRIQAQFAQLAQLNPQERMSRETALQQKQVSLETWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRLEHLCQQLPIPGPVEEMLAEVNATITDIISALSTSTFIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKNENTRNDYSGEILNNCCVMEYHQATGTLSAHFRNMSLKRIKRSDRRGAESVTEEKFTILFDSQFSVGGNELVFQVKTLSLPVVVIVHGSQDNNATATVLWDNAFREPGRVPFAVPDKVLWPQLCEALNMKFKAEVQSNRGLTKENLVFLAQKLFNSSSNHLEDYNSMSVSWSQFNRENLPGRNYTFWQWFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSQERMFWNLMPFTTRDFSIRSLADRLGDLNYLIYVFPDRPKDEVYSKYYTPVPCERATAKAADGYVKPQIKQVVPEFVNASTDAGSGATYMDQAPSPVVCPQAHYNMYPQNPDSVLDTDGDFDLEDTMDVARRVEELLGRPMDSQWIPHAQS
|
Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Binds to the GAS element and activates PRL-induced transcription. Positively regulates hematopoietic/erythroid differentiation.
|
P52632
|
A6V0A6
|
RLMH_PSEA7
|
rRNA (pseudouridine-N3-)-methyltransferase RlmH
|
Pseudomonas
|
MRLRLIAVGSRMPRWVEEGWQEYVKRLPAELSLELVEIPLNTRGKNADVARLIRQEGEAMLARVQPGERVVTLEVEGRPWSTEQLARELDRWRLDARTVNLMVGGPEGLAPEVCARSEQRWSLSPLTLPHPLVRILVGEQIYRAWTVLSGHPYHK
|
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
|
A6V0A6
|
Q8CIH9
|
PUR1_MOUSE
|
Glutamine phosphoribosylpyrophosphate amidotransferase
|
Mus
|
MELEELGIREECGVFGCIASGDWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSAVPKFRVHKGMGLVNHVFTEDNLKKLYDSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAYTPPQEKDDAPDWVARIKNLMKEAPAAYSLVIMHRDFIYAVRDPYGNRPLCIGRLMPVSDVNDKEKKSSETEGWVVSSESCSFLSIGARYCHEVKPGEIVEISRHGIRTLDIIPRSNGDPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVEADLVSTVPESATPAALGYATKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDCLAEYLGANSVVYLSVEGLVSSVQQEIKFKKQKVKKHDIAIQENGNGLEYFEKTGHCTACLTGQYPVELEW
|
Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
|
Q8CIH9
|
A8W3C2
|
RR14_CUSEX
|
30S ribosomal protein S14, plastid
|
Cuscuta subgen. Monogynella
|
MARKSLIQRNKKRQKLELKYHWIRGSSKKEIHRVPLLSDKWEIYVKLQSSPRNSAPTRLHRRCFLTGRPRANYRDFGLSGHILREMVQACLLPGATRSSW
|
Binds 16S rRNA, required for the assembly of 30S particles.
|
A8W3C2
|
A1S6D3
|
AROA_SHEAM
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Shewanella
|
MDQLRLEPVSRVNGVVNIPGSKSISNRALLLATLASGETTLVNLLDSDDIRHMLNALKSLGVNFTLSDDKTVCTLNGLGGPIQTDKAFELFLGNAGTAMRPLCAALTLGTGEFTLTGEPRMEERPIGDLVDALRQLGADIRYLKNDGFPPLTINATGLAGGVVEIDGSLSSQFLTALLMVAPLAKGAVTIAVKGELVSKPYIDITLDLMAKFGVTVVNDNYQRFEIASGQHYVSPGKVLVEGDASSASYFLAAGAIGGGEVKVTGVGRLAVQGDVKFADALAAMGADIEWGEDYIIARGSKLHGIDMDMNHIPDAAMTIATAALFAEGTTRMSNIYNWRIKETDRLAAMATELRKVGAKVEEGHDYIQITPPVKPVHAEIDTYNDHRMAMCFSLLAFADCGVTINDPGCTSKTFPDYFNRFANLAKPD
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
A1S6D3
|
Q0ASI7
|
ENGB_MARMM
|
Probable GTP-binding protein EngB
|
Maricaulis
|
MGAVALDHLPEPDRLEVAFAGRSNVGKSSLINALTNQKGLARASGEPGRTRELNFFNVEGGDLRIVDLPGYGYAKAPKPVVEKWTRLTKAFLRGRVNLKRVYLLIDSRHGLKDVDLKIMDVFDEAAVSYQVVLTKTDKIKPPAVKRLIGETGEKIARRPAAFPRVIATSSAKQDGVDQLRAEIVALLPDMG
|
Necessary for normal cell division and for the maintenance of normal septation.
|
Q0ASI7
|
P48550
|
KCNJ6_RAT
|
Potassium channel, inwardly rectifying subfamily J member 6
|
Rattus
|
MTMAKLTESMTNVLEGDSMDQDVESPVAIHQPKLPKQARDDLPRHISRDRTKRKIQRYVRKDGKCNVHHGNVRETYRYLTDIFTTLVDLKWRFNLLIFVMVYTVTWLFFGMIWWLIAYIRGDMDHIEDPSWTPCVTNLNGFVSAFLFSIETETTIGYGYRVITDKCPEGIILLLIQSVLGSIVNAFMVGCMFVKISQPKKRAETLVFSTHAVISMRDGKLCLMFRVGDLRNSHIVEASIRAKLIKSKQTSEGEFIPLNQTDINVGYYTGDDRLFLVSPLIISHEINQQSPFWEISKAQLPKEELEIVVILEGMVEATGMTCQARSSYVTSEILWGYRFTPVLTLEDGFYEVDYNSFHETHETSTPSLSAKELAELANRAELPLSWSVSSKLNQHAELETEEEEKNPEELTERNGDVANLENESKV
|
This potassium channel is controlled by G proteins. It may be involved in the regulation of insulin secretion by glucose and/or neurotransmitters. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium or cesium.
|
P48550
|
Q54K00
|
AATR2_DICDI
|
Aromatic amino acid aminotransferase DDB_G0287711
|
Dictyostelium
|
MTEKSNIIKDYTYFLSKRGKLKEASPIRSLFQYSSLPGMISLGGGLPNASTFPFKSINIELKDGSKLEIEGSDLEEAFQYSPTPGLPRLQKALKDLQIRQHNLCPPDEAGKEWNLIISNGSQESLANAFEVLIDDNDSIITENPTYSGTLSILKPLSLNICGIETDRYGMIPEKLQRLLSEWDHSKFKFPRVIYLIPCGQNPSGTTMNHQRKLDIYSICSKYNLLIIEDDPYYYLQFESSENADDDDGASCSSLNLGKSLLSMDVDGRVLRFDSLSKILSSGLRIGFVTGNKQLLEKINFHQQSTTLHSSGLSQAVVLSLLNKWGVEKWNQHISFIQRFYLEKRNQMIDSIDKHLKGLVEFNIPSAGMFIWFKLPVEDSKTLIFKNAVEKKILLVPGISFSTDSTKPSQFVRASYSTASKEQIDEAIKRFADLLNEELKK
|
Has aromatic amino acid transaminase activity.
|
Q54K00
|
A8F3G2
|
RIMM_PSELT
|
Ribosome maturation factor RimM
|
Pseudothermotoga
|
MSDYVVIGKITKTHGLFGSVKVLPLTNALEVFQKLENVFIKNDAQSNTHRLQIEEIRKAGKGFLIKFSGIDDEERARKIVGLSLAVRVTDLPKPKSPNEYYYYELLNVEVLDQSGNFIGRVEDIIQTGSNEVAVVKNGSFEMLIPVIHDYIIKFEKRKRLVVKVPEWI
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An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
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A8F3G2
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Q7VPP1
|
ATPG_HAEDU
|
F-ATPase gamma subunit
|
Haemophilus
|
MAGAKEIRTKIASVRNTQKITKAMEMVATSKMRKTQERMAAGRPYSETIRKVISHIAKGSIGYKHPFLIERDVKKVGYLVISTDRGLCGGLNINLFKTTLNEFKAWKDKDVSVELGLVGSKGVSFYQSIGLKVRAHITGLGDSPEMERIVGAVNEMINAYRNGEVDMVCIAYNRFENTMSQKTVIAQLLPLPKLENDELETKCSWDYLYEPNPQVLLDSLLIRYLETQVYQAVVDNLASEQAARMVAMKAATDNAGALIDELQLVYNKARQASITNELNEIVAGAAAI
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Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
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Q7VPP1
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Q9UL52
|
TM11E_HUMAN
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Transmembrane protease serine 11E catalytic chain
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Homo
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MMYRPDVVRARKRVCWEPWVIGLVIFISLIVLAVCIGLTVHYVRYNQKKTYNYYSTLSFTTDKLYAEFGREASNNFTEMSQRLESMVKNAFYKSPLREEFVKSQVIKFSQQKHGVLAHMLLICRFHSTEDPETVDKIVQLVLHEKLQDAVGPPKVDPHSVKIKKINKTETDSYLNHCCGTRRSKTLGQSLRIVGGTEVEEGEWPWQASLQWDGSHRCGATLINATWLVSAAHCFTTYKNPARWTASFGVTIKPSKMKRGLRRIIVHEKYKHPSHDYDISLAELSSPVPYTNAVHRVCLPDASYEFQPGDVMFVTGFGALKNDGYSQNHLRQAQVTLIDATTCNEPQAYNDAITPRMLCAGSLEGKTDACQGDSGGPLVSSDARDIWYLAGIVSWGDECAKPNKPGVYTRVTALRDWITSKTGI
|
Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position.
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Q9UL52
|
Q5WWN7
|
PROA_LEGPL
|
Glutamyl-gamma-semialdehyde dehydrogenase
|
Legionella
|
MNTDIANQLRAAKKATTDLNLIQSDTRTIILETLAANLEKHIENIIQENQKDLSLMLEQDPRYDRLLLNKERILSLANDVRKVASLPNPLGVSLLEKSMPNGLSIKKITVPLGVIAVIYESRPNVTIDIFSLCFKSGNVCILKGGKEAHFTNSYLLLLIKNTLKNFNINTDIVCLLPPERALMTQLLNATGLVDLCIPRGSQNLINFVRDNAKIPVIETGAGIVHTYFDKSGDLGKGKKIINNAKTRRVSVCNALDTLIIHADRLKDLPELVETLSQKHVIIYADQDAYHVLDKNYPEQLLIKAKPQDFGHEFLDYKLAIKTVPNIKAAIGHIQQFSSHHSEAIIAEDESAIDQFLIEVDAAAVYANASTAFTDGGEFGLGAEIGISTQKVHARGPMGLEALTSYKWVIRGTGQIRD
|
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.
|
Q5WWN7
|
A0A1D8PDZ1
|
RL34B_CANAL
|
60S ribosomal protein L34-B
|
Candida
|
MAQRVTYRRRNPYNTRSNKIKVVKTPGGKLVAQHVKKAASRVKCGDCGSALAGISTLRPRQYAQVSKTHKTVQRAYGGSRCANCVKERIVRAFLIEEQKIVKRVLKEQQDKEKKAAKKTGKK
|
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
|
A0A1D8PDZ1
|
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