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
|
|---|---|---|---|---|---|---|
A6Q522
|
TRUB_NITSB
|
tRNA-uridine isomerase
|
unclassified Nitratiruptor
|
MNRLFVAYKPPFVSSNAFLHKIKKRYRVKKAGFSGTLDPFACGTLIIAFGAYTKLFRFLQKYPKRYRTTIWLGASSPSLDIEKIESIQDVPPLDERTIKDIINSFVGEFTYIPPLFSAKKVGGKRAYHFAARGKQIDLKPVTSTIEEISFVHYRHPFITFEATVSEGTYIRSLAEAIAKKLGFPGTLSYLERLAEGKFVYENENPLDPVQYLRTKQNFVKKSKEAIFHGAKLTIDDLAYKEDGEYHILFDDFFAIIRVEKKKVRYLLNQIPRKYQ
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
A6Q522
|
Q17WI2
|
RUVC_HELAH
|
Holliday junction resolvase RuvC
|
Helicobacter
|
MHILGIDPGSRKCGYAIISYASNKLSLITAGFINITTTHLQEQILDLIEALDCLLDRYEVHEVAIEDIFFGYNPKSVIKLAQFRGALSLKILERVGNFSEYTPLQVKKALTGNGKAAKEQVAFMVKRLLHITSEIKPLDISDAIAVAIMHAQRLKLY
|
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
|
Q17WI2
|
C6DKK4
|
RBFA_PECCP
|
Ribosome-binding factor A
|
Pectobacterium
|
MAKEFSRTQRVAQEMQKEIAIIIQREVKDPRIGMATVSGVEVSRDLAYAKVFVTFLNDNEPEQVKTALKALQDASGFIRTLVGKAMRLRVVPALTFSYDNSLVEGMRMSNLVTNVVRNDTERRSVTGEDQED
|
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.
|
C6DKK4
|
Q49WT7
|
HPS1_STAS1
|
D-arabino-3-hexulose-6-phosphate formaldehyde lyase 1
|
Staphylococcus
|
MELQLAIDLLNKEEATILANKVKDYINIVEIGTPIVINEGLPAVQHLNDNIDGVKVLADLKIMDAADYEVSQAVKFGADIVTILGVAEDASIKAAVDEAHKHGKQLLVDMIAVQDLEKRAKDLDDLGADYIAVHTGYDLQAEGQSPLESLRKVKSVISNSKVAVAGGIKPDTIKDIVAENPDLIIVGGGIANADDPVEAAKQCRAAIEGK
|
Catalyzes the condensation of ribulose 5-phosphate with formaldehyde to form 3-hexulose 6-phosphate.
|
Q49WT7
|
A7MH63
|
PDXB_CROS8
|
Erythronate-4-phosphate dehydrogenase
|
Cronobacter
|
MKILVDENMPYARELFSRLGEVQAVPGRPIPQAALDDADALMVRSVTQVNRDLLAGKNIRFVGTATAGTDHVDEDYLREAGVGFSAAPGCNAIAVVEYVFSALLMLAERDGFALTDRTVGIVGVGNVGSRLQARLEALGVRTLLCDPPRADRGDSGDFRTLDELVREADILTFHTPLFKEGPYKTLHLADEALIARLKPGAILINACRGPVVDNAALLARLEAGQPLSVVLDVWEPEPALNVELLKRVDIGTAHIAGYTLEGKARGTTQVFEAYSQFLGTPQQVALATLLPPPEFGRITLQGPLDQPTLKRLVHLVYDVRRDDAPLRRVAGMPGEFDKLRKNYQERREWSSLYVQCDDEAAAALLQKLGFNATHHPIR
|
Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
|
A7MH63
|
Q60BS0
|
RL19_METCA
|
50S ribosomal protein L19
|
Methylococcus
|
MNIVQQLESEWMSGKTIPAFGPGDTVVVQVKVKEGNRERLQAFEGVVIAKRNRGYNSAFTVRKVSHGEGVERVFQTYSPQVEEIQVKRRGDVRRAKLYYLRDRAGKAARIKEKI
|
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
|
Q60BS0
|
Q9TV43
|
CCR5_CHLSB
|
C-C chemokine receptor type 5
|
Chlorocebus
|
MDYQVSSPTYDIDYYTSEPCQKIKVKQIAARLLPPLYSLVFIFGFVGNILVVLILINCKRLKSMTDIYLLNLAISDLLFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAIVHAVFALKARTVTFGVVTSVITWVVAVFASLPRIIFTRSQREGLHYTCSSHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNDKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQDAPERASSVYTRSTGEQETSVGL
|
Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor.
|
Q9TV43
|
P32458
|
CDC11_YEAST
|
Cell division control protein 11
|
Saccharomyces
|
MSGIIDASSALRKRKHLKRGITFTVMIVGQSGSGRSTFINTLCGQQVVDTSTTILLPTDTSTEIDLQLREETVELEDDEGVKIQLNIIDTPGFGDSLDNSPSFEIISDYIRHQYDEILLEESRVRRNPRFKDGRVHCCLYLINPTGHGLKEIDVEFIRQLGSLVNIIPVISKSDSLTRDELKLNKKLIMEDIDRWNLPIYNFPFDEDEISDEDYETNMYLRTLLPFAIIGSNEVYEMGGDVGTIRGRKYPWGILDVEDSSISDFVILRNALLISHLHDLKNYTHEILYERYRTEALSGESVAAESIRPNLTKLNGSSSSSTTTRRNTNPFKQSNNINNDVLNPASDMHGQSTGENNETYMTREEQIRLEEERLKAFEERVQQELLLKRQELLQREKELREIEARLEKEAKIKQEE
|
Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 minutes before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.
|
P32458
|
C5J8E3
|
SAUVE_PHYSA
|
Sauvatide
|
Phyllomedusa
|
MDILKKSLFLILFLGLVSISFCDGEKRQDDDEANESEEKKEIHEVEKRLRPAILVRTKGKGK
|
Induces contraction of smooth muscle in isolated rat urinary bladder with an EC(50) value of 2.2nM.
|
C5J8E3
|
Q93P60
|
AMGDS_ACHLA
|
UDP-glucose:1,2-diacylglycerol 3-alpha-D-glucosyltransferase
|
Acholeplasma
|
MRIGIFSEAYLPLISGVVTSVVNLKEGLEALGHEVYVITPIPSKDKFENDPSVIRIPGWVIPRKSLKGFRLVLFVKRYVRKMRKLKLDVVHIHTEFSMGKLGLAVAKKERIPSVYTLHTSYQDYTHYVSKLLTRFAPNAAKKLAGKINNQYTKNCHMTIVPTKKIYDKMIRLKHDGEFTIIPSGINLKPFYKSSYTSEQVQALKDKLGIRNDEFVAILVARIAKEKSIGDLVEAFVEFYKSYPNSRFIIIGDGPDKPVLDKLIDSKKASKYINTLGFVKNAEVGLYYQIADVFLNASTTETQGLTYVEALAASLPIIVRYDDVFDAFVEDGKNGIFFNKNEELVKHLIHIRQNPEILGTLSKNAEISTKPYAKEVYAKSCETLYLDLIDKNNKKLNKK
|
Glucosyltransferase involved in the biosynthesis of the non-bilayer-prone membrane lipid alpha-monoglucosyldiacylglycerol. This is a major component for maintaining a certain anionic lipid surface charge density, for balancing the bilayer to non-bilayer phase equilibria and for keeping a constant lipid bilayer spontaneous curvature (curvature packing stress). Catalyzes the transfer of a glucosyl residue from UDP-Glc to diacylglycerol (DAG) acceptor to form the corresponding alpha-glucosyl-DAG (1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol). It can only use UDP-Glc as sugar donor and DAG is the preferred substrate.
|
Q93P60
|
A7Z6M3
|
GCSPA_BACVZ
|
Glycine dehydrogenase (aminomethyl-transferring) subunit 1
|
Bacillus amyloliquefaciens group
|
MKHRYLPATEQDKKEMLKAIGAETIDELFADIPENVRFQKDYQIKKAKSETELTRELTKLAAKNKDAVTYASFLGAGVYDHYQPVIVDHVISRSEFYTAYTPYQPEISQGELQAIFEFQTMICELTGMDIANSSMYDGGTALAEAAMLASGHTKKKKIVISAAVHPESRDVLKTYAKGQYIEVVEVPAKNGVTDLEALEHAVCDETAAVIVQYPNFFGQIEPLKDIEPLAHKGNSQLIVSSNPLALGILTPPGAYGADIVVGDAQPFGIPAAFGGPHCGYFAVTKKLMRKVPGRLVGQTEDENGRRGFVLTLQAREQHIRRDKATSNICSNQALNALAASAAMTALGKNGVKDMARQNILKADYARRQAEKAGLHVAFDGPIFNEFAVRLNLPVKEANRRLLQDGIIGGYDLGLAYPELNQHMLIAVTELRTKEKIDSLIARLGDQHE
|
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.
|
A7Z6M3
|
F4J117
|
LSF1_ARATH
|
Protein LIKE SEX4 1
|
Arabidopsis
|
MAFLQQISGLGALERSCPSIMIGSSFRSGNGRVFDGRGIAYLGSREKFGFNRRRRVVLRVVAMSSSSTPFKMNLNEYMVTLEKPLGIRFALSADGKIFVHAIKKGSNAEKARIIMVGDTLKKASDSSGGTLVEIKDFGDTKKMLVEKTGSFSLVLERPFSPFPIQYLLHLSDLDLLYNRGRVSFVTWNKNLLSSNLRASSQGSGNSGYAAFSSKFFTPQGWKLLNRQSNSFQSGTKKNILSPPISPLVSVFSEDVPGDGEWGYGNFPLEEYIKALDRSKGELSYNHALGMRYSKITEQIYVGSCIQTEEDVENLSEAGITAILNFQGGTEAQNWGIDSQSINDACQKSEVLMINYPIKDADSFDLRKKLPLCVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVTGLHACKPDRPAIAWATWDLIAMVDDGKHDGTPTHSVTFVWNGHEGEEVLLVGDFTGNWKEPIKATHKGGPRFETEVRLTQGKYYYKYIINGDWRHSATSPTERDDRGNTNNIIVVGDVANVRPTIQQPRKDANIIKVIERVLTESERFRLAKAARCIAFSVCPIRLCPKS
|
Starch granule-associated phosphoglucan phosphatase involved in the control of starch accumulation. Participates in the regulation of the initial steps of starch degradation at the granule surface. May release a different set of phosphate groups from those removed by DSP4.
|
F4J117
|
Q28RG1
|
FABH_JANSC
|
3-oxoacyl-[acyl-carrier-protein] synthase III
|
unclassified Jannaschia
|
MIIRAVPVGIGHYLPERVVPNAEFEAMEGLETSDEWIRARSGIERRHFAAEGETTSQMAVTAARKALDHAALNPDDIDAVIVATSTPDLTFPSVATMVQAGLGMTGGFAFDVQAVCAGFVYALANANALIVSGQANRVLVIGAETFSRIMDWTDRTTCVLFGDGAGALILEGRDSAGTPQDRGILSTDLHSDGTHRELLYVDGGVSSTGTTGVLKMQGKEVFRHAIEKLTKTADTGLAKAGVTVGDVDWVVPHQANIRIISGTVKKFGLPMDKVIVTVQDHGNTSAASIPLAMSVGVGDGRIQPGHLLVTEAIGGGLAWGAVVMRW
|
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
|
Q28RG1
|
Q32RG4
|
CYB6_ZYGCR
|
Cytochrome b6
|
Zygnema
|
MGKVYDWFEERLEIQSIADDITSKYVPPHVNIFYCLGGITLTCFIIQVATGFAMTFYYRPTVTEAFASVQYIMTDVNFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVILGVLTVSFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVVGSPIVELLRGSVSVGQTTLTRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL
|
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.
|
Q32RG4
|
B2A158
|
CLPP_NATTJ
|
Endopeptidase Clp
|
Natranaerobius
|
MNLIPMVIEQTNRGERSYDIYSRLLKDRIIFIGTGINDDIANSVIAQMLFLESEDPDKDIHLYINSPGGHVHAGLAIYDTMQYIRSDVSTICVGMAASMGAVLLAAGNEGKRFCLPNSRIMLHQPMGGAQGQAADVEIHAREIMKTKERLNQILAHHTGQPVEQISKDTDRDFFMSSEEAQKYGVIDDVLKRPPENS
|
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
|
B2A158
|
Q5T1S8
|
NCMAP_HUMAN
|
Myelin protein of 11 kDa
|
Homo
|
MTTATPLGDTTFFSLNMTTRGEDFLYKSSGAIVAAVVVVVIIIFTVVLILLKMYNRKMRTRRELEPKGPKPTAPSAVGPNSNGSQHPATVTFSPVDVQVETR
|
Plays a role in myelin formation.
|
Q5T1S8
|
P71590
|
FHAA_MYCTU
|
FHA domain-containing protein FhaA
|
Mycobacterium tuberculosis complex
|
MGSQKRLVQRVERKLEQTVGDAFARIFGGSIVPQEVEALLRREAADGIQSLQGNRLLAPNEYIITLGVHDFEKLGADPELKSTGFARDLADYIQEQGWQTYGDVVVRFEQSSNLHTGQFRARGTVNPDVETHPPVIDCARPQSNHAFGAEPGVAPMSDNSSYRGGQGQGRPDEYYDDRYARPQEDPRGGPDPQGGSDPRGGYPPETGGYPPQPGYPRPRHPDQGDYPEQIGYPDQGGYPEQRGYPEQRGYPDQRGYQDQGRGYPDQGQGGYPPPYEQRPPVSPGPAAGYGAPGYDQGYRQSGGYGPSPGGGQPGYGGYGEYGRGPARHEEGSYVPSGPPGPPEQRPAYPDQGGYDQGYQQGATTYGRQDYGGGADYTRYTESPRVPGYAPQGGGYAEPAGRDYDYGQSGAPDYGQPAPGGYSGYGQGGYGSAGTSVTLQLDDGSGRTYQLREGSNIIGRGQDAQFRLPDTGVSRRHLEIRWDGQVALLADLNSTNGTTVNNAPVQEWQLADGDVIRLGHSEIIVRMH
|
Regulates cell growth and peptidoglycan synthesis by binding to MviN. May inhibit the late stages of peptidoglycan synthesis.
|
P71590
|
B4SP02
|
BPT_STRM5
|
Aspartate/glutamate leucyltransferase
|
Stenotrophomonas maltophilia group
|
MAIHGDRDDELRLFQTGEHPCGYWSDRVARDLVLDPHDRRLGGLYPLALSWGFRRSGDLVYRPHCAHCQACVAVRIPVARFAPDRSQRRCAARNEDLEVRITAATARDDLFALYHRYLTHRHANGGMDDHGPHEFEQFLIGSWSHTRFMEMRLPGHDGQPSQLLGVAVTDVTEHGLSAVYTFFDPDHAARGLGTFAILQQIEWARREGLPHVYLGYWIRGHQKMDYKRRYRPLEAYDGRRWHDFDDELDGR
|
Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
|
B4SP02
|
Q5ZVR4
|
RLMH_LEGPH
|
rRNA (pseudouridine-N3-)-methyltransferase RlmH
|
Legionella
|
MLKITIITLGNKMPDWVNSGVNEYAKRFHDGIQIKLIEIPLLRRNKSSDLARILEKESALTKDALPANARLIALDMLGKSFSSEELALRLTQLQQISSHLCFIIGGPEGLSNEILTLCDERWSLSKLTLPHPLVRIILLESLYRAWSIINNHPYHK
|
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
|
Q5ZVR4
|
Q7YS71
|
IL4_BUBBU
|
Lymphocyte stimulatory factor 1
|
Bubalus
|
MGLTYQLIPVLVCLLVCTSHLVHGHKCDITLAEIIKTLNILTTRKNSCMELPVADVFAAPKNTTEKETFCRVGIELRRIYRSHTCLNKFLGGLDRNLNSLVSKTCSVNEAKTGTSTLKDLLERLKTIMKEKYSKC
|
Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4.
|
Q7YS71
|
A4WU31
|
NUOD_CERS5
|
NDH-1 subunit D
|
Cereibacter
|
MDTKFDDVLTGEQKLRNFNINFGPQHPAAHGVLRLVLELDGEVVERCDPHIGLLHRGTEKLMETRTYLQNLPYFDRLDYVAPMNQEHAWCLAIERLTGVQVPRRASLIRVLYSEIGRVLNHLLNVTTQAMDVGALTPPLWGFEEREKLMVFYERASGARLHAAYFRPGGVHQDLTPRLIEDIEEWAEHFPKVLDDLDGLLTENRIFKQRNVDIGVVTEKDILDWGFSGVMVRGSGLAWDLRRSQPYECYDEFDFQIPVGKNGDCYDRYLCRMEEMRQSTRIIQQCLAKLRVEKGDVLARGKITPPPRAEMKTSMEALIHHFKLYTEGFHVPAGEVYAAVEAPKGEFGVYLVADGTNRPYRAKIRAPGFLHLQAIDYIAKGHLLADVSAIIGTLDVVFGEIDR
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
|
A4WU31
|
Q2LQ97
|
RS19_SYNAS
|
30S ribosomal protein S19
|
Syntrophus
|
MARSIKKGPFVDEKLFDKVQKAVASGNKSVIKTWSRRSTITPDLIGHTFAVHNGKKFIPVFVTENMVGHKLGEFAPTRIFFSHAGDRKSKVRK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
Q2LQ97
|
Q9BMX0
|
ERF1_DICDI
|
Eukaryotic peptide chain release factor subunit 1
|
Dictyostelium
|
MSAVDDQQNADKQVEQWKIKKLIKNLEAARGNGTSMISLIIRPGDQIAKVNKMLAEEYGTASNIKSRVNRLSVLGAITSAQQRLKLYTKVPDNGLVIYCGTMVTDEGKEKPVRIDIEPFKPINTSLYLCDNKFHTAPLGELLESDEKFGFIVVDGNGALFGLLCGSTRTVLHKITVDLPKKHGRGGQSALRFARLRMEKRHNYVRKVSELATQFYVTNDKPNVSGLILAGSADFKTELGTSDMFDQRLREKIIKIVDVSYGGDNGFNQAIELSGEVLSSVKFIQEKKLISQFFEEIAQDTGKYCFGIADTLKALDLGAAHTLIVWESLETIRYLLRLPTGEEKVIFLNKDQNKDASVFKDKESGLDYEIVEEMPIVEWFANNYKNFGASLEFVTNKSQEGSQFCKGFGGLGGLLRYQVDFAQLNDFDNPDENEYDDSDSDF
|
Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
|
Q9BMX0
|
C5DXG0
|
YFH7_ZYGRC
|
ATP-dependent kinase YFH7
|
Zygosaccharomyces
|
MLGCFFFFFIQYKVQVEIFVFKVHYLREDTPFPKMVVDVDALANEAIGLLDQCKDDNYRVCILIVGPPGSGKSTVAQDLSRQINHRFDEYRLQGNQKSAHGGTRSRASDVALASDVPEITTPLSEELAFNGGILPKYVEDVNFQPVKRRLENGDLQILGRGGLPNAFTISNDVEPDEESSFAQIVPMDGFHLSRQCLSSFQNPQEAHKRRGSPPTFDSNNFAQLCKTLAQTCTIKPGSCDAKSCFEFMAKTYDPHFPCIKIPGFDHSLKDPTPDQFCLNGHTRIVILEGLYLLYDKENWQRVHEILQNTGSLLVWYIDIEDHVIEERVAKRHFNSGLADSVEQGRLKFQGNDLLNARLIRKNLVQSGKVVTLRND
|
ATP-dependent kinase that could be involved in endoplasmic reticulum membrane assembly.
|
C5DXG0
|
A3CLY3
|
SYA_STRSV
|
Alanyl-tRNA synthetase
|
Streptococcus
|
MKQMSSAQVRQMWLDFWATKGHAVEPSVSLVPVNDPTLLWINSGVATLKKYFDGTIIPENPRITNAQKAIRTNDIENVGKTARHHTMFEMLGNFSIGDYFRDEAIEWAYELLTSPEWFDFPKDKLYMTYYPDDKDSYNRWIAMGVEPSHLIPIEDNFWEIGAGPSGPDTEIFFDRGEAFDPENIGVRLLEEDIENDRYIEIWNIVLSQFNADPAVPRSEYKELPHKNIDTGAGLERLVAVIQGAKTNFETDLFMPIIREVEKLSGKVYDQDGDNMSFKVIADHIRSLSFAIGDGALPGNEGRGYVLRRLLRRASMHGQKLGINEPFLYKLVPTVGKIMESYYPEVLEKQEFIEKIIKSEEESFARTLHSGQHFAETIVADLKAKGQTVISGQDAFKLYDTYGFPLELTEEIAEEADMTVDRAGFEAAMKEQQDRARASVVKGGSMGMQNETLQAITVESAFNYEKEELTAELLAIVADDAAVESVETGTAALIFAETPFYAEMGGQVADHGQIFDGAGNLVAQVTDVQKAPNGQPLHTVEVLAPLALGQSYKLEIDHSRRHRVMKNHTATHLLHAALHNVLGNHATQAGSLNEVEFLRFDFTHFQAVTAEELRAIEQEVNEKIWEALAIETVETDIDTAKEMGAMALFGEKYGKEVRVVTIGDYSVELCGGTHVGNTSEIGIFKIVKEEGIGSGTRRILAVTSKEAFEAYREEEEALKAIAATLKAPQIKEVPHKVEALQEQLRQLQKENAELKEKAAAAASGEVFKDVQEANGHSFIASQVSVSDAGALRTFADTWKQKDYSDVLVLVAAIGDKVNVLAASKTKDVHAGNLIKELAPIVDGRGGGKPDMAMAGGSKQSAIPDLLAAVAEKL
|
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
|
A3CLY3
|
Q3A944
|
ATPA_CARHZ
|
F-ATPase subunit alpha
|
Carboxydothermus
|
MNLRPEEIGSIIKQQIENYQVQVEVSSVGTVIQVGDGIARVYGLEDCMASELLEFPGGVLGMALNLEEDNVGCVILGPYTHIKEGDTVKRTGRVVSVPVGEALIGRVVNPLGQPLDGKGPIVTDKFRPVERIAPGVITRKSVHEPLQTGIKAIDSMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKNTDVICIYVAIGQKASTVAKVVQTLKDHGAMDYTIVVSATASDPAPLLYLAPYAGCAMGEEFMEQGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEYGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIYLESDLFYAGVRPAVNVGLSVSRVGGAAQIKAMKQVAGSLRLDLAQYRELAAFAQFGSDLDKATLARLTRGERLVELLKQDQYKPMPVEEQVMAIFAAVNGYLDDLPVEKVRPFEAEFLKFMRANYPQIGEEIRTKGVLTDELTSRLKSAIEEFKKTFA
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
Q3A944
|
A1CGN9
|
MTNA_ASPCL
|
Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein
|
Aspergillus subgen. Fumigati
|
MTLEAIRYSTGKLVIIDQLQLPYVEKYIEVPTSKDAWHAIKKMRVRGAPAIAIVAALALASELHTLMAHDKLSNRAEEVRLFIQEKLDYLVSSRPTAVNLSDAARKLAAHVSDHAEMPNSTGRAVAEAFIQAAEEMLAKDLKDNTNIGKYGAEWIIRNALAGGRSKATILTHCNTGSLATSGYGTALGVIRALASKNALAYAYCTETRPYNQGSRLTAYELVHENLPATLVTDSMVAALLAKAEAAVDAIVVGADRVAANGDTANKIGTYALAVLAKFHGVKFLVAAPLTTIDRSTKSGADIVIEERPASEVTTIKGAVETESSCDRIKLETVRIAAEGIHVWNPAFDVTPSALIDAIITERGVVERGTDGRYNFDGIFEDHSAF
|
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
|
A1CGN9
|
B1J812
|
URED_PSEPW
|
Urease accessory protein UreD
|
Pseudomonas
|
MLLAERVEQSEHDAGWSAHLQLRFVEGGGVTRLGARRHFGPLLVQRPFYPEGAPCHVYVLHPPGGIVAGDRLELDIHLEPGSHALLTMPGASKFYRSIGPTARLTQRFHLQAGSTLEWLPQDSIFFSGARASLDSRFTLEPGARLLAWETLCLGRPVMGERFDQGALDSRLSIELPDDPGLHERLRISGGQLEKLGGHPLLATFCASPADPSVLEKVRHLLDELKTPAGATLLGSLLVIRLLDHDNQHLQHTLQRLWHVLRPAVLGLPACPPRIWAT
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
B1J812
|
P42039
|
RLA2_DAVTA
|
Minor allergen Cla h 5
|
Cladosporium
|
MKYLAAFLLLGLAGNSSPSAEDIKTVLSSVGIDADEERLSSLLKELEGKDINELISSGSEKLASVPSGGAGAASAGGAAAAGGAAEAAPEAERAEEEKEESDDDMGFGLFD
|
Plays an important role in the elongation step of protein synthesis.
|
P42039
|
Q5ZLT0
|
XPO7_CHICK
|
Exportin-7
|
Gallus
|
MADHVQSLAQLENLCKQLYETTDTATRLQAEKALVEFTNSPDCLSKCQLLLERGSSSYSQLLAATCLTKLVSRTNNPLPLEQRIDIRNYVLNYLATRPKLATFVTQALIQLYARITKLGWFDCQKDEYVFRNVITDVTRFLQDSVEHCIIGVTILSQLTNEINQADTTHPLTKHRKIASSFRDSSLFDIFTLSCNLLKQASGKNLNLNDESQHGLLMQLLKLTHNCLNFDFIGTSTDESSDDLCTVQIPTSWRSAFLDSSTLQLFFDLYHSIPPSFSPLVLSCLVQIASVRRSLFNNAERAKFLSHLVDGVKRILENPQSLSDPNNYHEFCRLLARLKSNYQLGELVKVENYPEVIRLIANFTVTSLQHWEFAPNSVHYLLSLWQRLAASVPYVKATEPHMLETYTPEVTKAYITSRLESVHIILRDGLEDPLDDTGLVQQQLDQLSTIGRCEYEKTCALLVQLFDQSAQSYQELLQSATASPMDVAVQEGRLTWLVYIIGAVIGGRVSFASTDEQDAMDGELVCRVLQLMNLTDSRLAQAGNEKLELAMLSFFEQFRKIYIGDQVQKSSKLYRRLSEVLGLNDETMVLSVFIGKIITNLKYWGRCEPITSKTLQLLNDLSIGYSSVRKLVKLSAVQFMLNNHTSEHFSFLGINNQSNLTDMRCRTTFYTALGRLLMVDLGEDEDQYEQFMLPLTAAFETVAQMFSTNTFNEQEAKRTLVGLVRDLRGIAFAFNAKTSFMMLFEWIYPSYMPILQRAIELWYHDPACTTPVLKLMAELVHNRSQRLQFDVSSPNGILLFRETSKMITTYGNRILTLGEVPKDQVYALKLKGISICFSMLKAALSGSYVNFGVFRLYGDDALDNALQTFIKLLLSIPHSDLLDYPKLSQSYYSLLEVLTQDHMNFIASLEPHVIMYILSSISEGLTALDTMVCTGCCSCLDHIVTYLFKQLSRSTKKRTTPLTQESDRFLHIMQQHPEMIQQMLSTVLNIIIFEDCRNQWSMSRPLLGLILLNEKYFSDLRNSIVNSQPPEKQQAMHLCFENLMEGIERNLLTKNRDRFTQNLSAFRREVNDSMKNSPYGVNSNDMMS
|
Mediates the nuclear export of proteins (cargos) with broad substrate specificity.
|
Q5ZLT0
|
Q25297
|
KM11B_LEIIN
|
Kinetoplastid membrane protein 11B
|
Leishmania
|
MATTYEEFSAKLDRLGEEFNRKMQEQNAKFFADKPDESTLSPEMKEHYEKFERMIKEHTEKFNKKMHEHSEHFKQKFAELLEQQKAAQYPSK
|
May be involved in the regulation of the cytoskeleton through interaction with the subpellicular microtubules. May be involved in parasite mobility and attachment to the surface of the host cell. Behaves as a strong immunogen during infection.
|
Q25297
|
Q8U4A4
|
VATD_PYRFU
|
V-ATPase subunit D
|
Pyrococcus
|
MPEILKVKPTRMELLKLKRRVKLAERGHKLLKEKQDALIMEFFTIYDEALSMRRELIKKIGEAFEALRLAQVEVGSVRLKEIAIGVNPNKEIEVRSRNIMGVRVPLIEVPELKRKPSERGYAFISTSSAVDVAAEKFEEVLELAIRLAEVEESLKRLGKEIEKTKRRVNALEYIIIPRMKNTIKFIEQHLDEMERENFFRLKRIKALLEARESM
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
Q8U4A4
|
A9NFP5
|
NADD_ACHLI
|
Nicotinate mononucleotide adenylyltransferase
|
Acholeplasma
|
MVLVYGGSFNPPTIAHEAIIHKLHEEFKPKKILIVPTGNYFSWKTDLIDFEHRFKMVELMTQHLDYVEISRLENTKAFLGSYHTLNELSKRYDDLYFVVGADHIKTLDQWKDYKKLIENYKFILLTRNNYTFDDDLLSKLGLKYEKMMFQSDISSSEIRKNLNQNLDKLNLNVKTYILENKLYEEVKV
|
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
|
A9NFP5
|
Q0I5G9
|
NAPA_HAES1
|
Periplasmic nitrate reductase
|
Histophilus
|
MNLSRRDFMKANAALAAASVAGLIIPVKNVNAADTSITWDKAVCRFCGTGCAVLVGTKDGRVVASQGDPDAEVNRGLNCIKGYFLPKIMYGKDRLTHPMLRMKNGQYDKEGEFTPVTWDFAFKTMAEKFKSALKAKGPNGVGMFTSGQSTIFEGVAKSKLFKAGLLSNNIDPNARHCMASAAVAFVRTFGIDEPMGCYDDIEHADAFVLWGSNMAEMHPILWSRISDRRLANPDTVSVNVLSTFEHRSFELADLGILLKPQSDLAILNYIANYLIENNAINREFIEKHTKFKRGETDIGYGLRPQDPREQIAKNVKTAGKMYDSSFEEFKKLVAPYTLEKAHEISGVPKEQLEKLAKLYADPNKKVVSYWTMGINQHTRGVWANHLIYNIHLLTGKISLPGCGPFSLTGQPSACGTAREVGTFIHRLPADLVVTKPEHRKIAEKIWKLPEGLISDKLGFHAVAQSRALKDGKMQVLWQMCNNNMQAGPNINEETYPGWRNPDNFIVVSDPYPTVSALSADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDLWQLVEFSKYFTTDEVWPAEILAKNPAYQGKTLYEVLYLNGQVNQYSNDELKGRLNDEAYHFGFYIQKGLFEEYASFGRGHGHDLADFDTYHKARGLRWPVVDGKETLWRYREGYDPYVKAGEGVSFYGQADKRAVILAVPYEPPAEVPDREYDLWLTTGRILEHWHTGSMTRRVPELHRSFPNNLVWMNPNDAKKRGLKHGDKIKVISRRGEITSYIDTRGRNKCPEGLIYTTFFDAGQLANKLILDATDPISKETDFKKCAVKVVKA
|
Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.
|
Q0I5G9
|
B7JC10
|
ACP_ACIF2
|
Acyl carrier protein
|
Acidithiobacillus
|
MDNVADRVKKVVVEQLGVNEDEVTNEASFVDDLGADSLDTVELVMALEEEFDCEIPDEEAEKIATVQQAIDYVSAHIPAKDA
|
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
|
B7JC10
|
Q18297
|
TRPA1_CAEEL
|
Transient receptor potential cation channel subfamily A member 1 homolog
|
Caenorhabditis
|
MSKKSLGLDVRLELEGLISNDDTIRSEKDGRQASIFRVAELDARTEADNLRSIIHQSAREGNVNALQEALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTPLHIASKYIYGYSDICSIIDEDQADSARKYNTATKKIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADVDAEDDNKMTPLLLACVHGSQEIIQELIKANSNVTKRDQRLNTVFHIVALRGEPEYLEMMMDHDPVEAIKALNLFNNEKKTPLRMAVEGNHPETLKKILQMEKKNSCKWMDREKELIHFAAEKGFLEVLKALVEAGGNKNELNEVKAVPLHVAAQMNQLEVVSYLIEEEKDNIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPVFIGAKFNALSSVEYILDHLRKKNKETERSALKSPTRNTLRIVSEDVRRTMVNMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEETALHRAAIGGQTGAVRQLLEWDIRLLLMKDEMGNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRLVAKGAQIESSSDTKTVLHTAAFYGNESIVRYFIAEGVTIDRRDEEGKTAFDIACENDHKDVARAFLETDQWKNLMIPCDVIPLDKHRNPVNMKRRTPFRTLLTKFPELASFVMDNCIEKSKEETDSTQSVAYNFEFLDDTYMMRCVSDDGTGEQLIGCKSAYDEDFKLEKDAQSYASNYDRVYKYHPLKLMADAEKLHLLNHPLSKALLKYKWNRLGRPMYYFALFMYLVFIVSLTQYVRHTKAPYNVWNEESYYDSEYFDENETCPQINTTKPDVVWKIIIQTLAVCQILVECFQLFQRKFAYLVNWENWIDCFIYSTALITVYDFSECSATSGVRQNWQWILAALCIFFGWINLLFMIRKMPRFGIFVVMFVDIVKTFFRFFPVFVLFIIAFSSSFYVILQNRPEFSTIFMSPLKTTVMMIGEFEFTGIFHGDETTHAEKMFGPAHTAVACALFFFFCIIMTILLMNLLVGLAVDDIKGVQEKAELKRLAMQVDLVLQIEASLHFFIQRTKKYATCRYATFPYGKLHKTGFAGWWSNFRRRFGLSVSTDPEIDEMYEREAEFTSEMTQKLQNQAAKLKNIQENIDVMYEKQVRLEAIIAKLATGLNINIELEEKDN
|
Receptor-activated non-selective cation channel involved in the nose-touch response and foraging behavior. Contributes to the neural responses of sensory neurons to touch, particularly after repeated mechanical stimulation. Has no apparent role in thermosensory or chemosensory behaviors.
|
Q18297
|
Q1ISQ0
|
CH60_KORVE
|
Chaperonin-60
|
Candidatus Koribacter
|
MAKQIVHGEESRQSILRGVNVLADAVKVTLGPKGRNVVIDKKFGSPLITKDGVTVAKEIELKDTLENMGAQMVKEVASKTSDIAGDGTTTATVLAQAIYREGVKNVAAGSNPMALKRGIDKAVTAVCGYNDAEGNRIPGALDKFSKPVTGEMIAQVGTISANNDETIGKIIAEAMKKVGKDGVITVEESKTMETQLEVVEGMQFDRGYLSPYFVTDPERMEAVLENPYILIHEKKVSSMKDLLPLLEQIAKGGRPLVIIAEDVEGEALATLVVNKLRGTLNVAAVKAPGFGDRRKAMLQDIAILTGGKAITEDLGIKLENVHMDDLGSAKKVTIDKDNTTIVEGKGKSSDIEGRVKEIRSQVEKTTSDYDREKLQERLAKLVGGVAVIKVGAATETEMKEKKARVEDAMHATRAAVEEGIVPGGGVALIRCVEAVDALKLTGDEGIGANIIKRALEEPLRQIVGNAGEEGAIVVGKIRDHKDPHYGYNAQTSEYVDLVKAGVIDPTKVTRTALQNAGSIAGLMLTTEALISEIPEEKKSEPAGGHGGGMGGMY
|
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
|
Q1ISQ0
|
Q68XM0
|
DAPB_RICTY
|
4-hydroxy-tetrahydrodipicolinate reductase
|
typhus group
|
MINIGLSGATGKMGKTIIEIIDQFKDCQISEKFNSTNNLNDLDNLCKNSDVIIDFSTPEVLEKLINYALKHNTKLVIGTTGLKKQHFKLLEKAAKTLPILYSANMSIGANLLNYLAKESTKILDDYDVEILEMHHRNKKDAPSGTALMLASTIAGIKELNITFNRGNRIKSKKEIGISSLRGGNVHGIHEIFFLDNDEIITLKHEALNKNSFAVGAIKSAIWLQDKPSALYSMQDIYKV
|
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
|
Q68XM0
|
O66630
|
DAPAT_AQUAE
|
LL-diaminopimelate aminotransferase
|
Aquifex
|
MFEFSDRLKVLPPYLFAELDRKKQEKIEQGVDVIDLGVGDPDMPTPKPIVEAAKKALENPENHKYPSYVGKYEFRKAVADWYKRRFDVDLDPNTEVITLIGSKEGIAHFPLAFVNPGDIVLCPDPAYPVYRIGAIFAGGTPYTVPLKEENNFLPDLDSIPEDVAKKAKIIWINYPNNPTSAPPTLEFYKKLVDWAKEYNVIIASDNAYSEIYTGQEKPPSILQVPGAKDVAIEFHSLSKTYNMTGWRIGMAVGNKELVAGLGKVKTNVDSGQFGAVQDAGIVALNLPEEEVEKIRDVYRERKKIMTEALEKIGLEIYRSDYTFYLWIKVPEGYTSAEFVGRLIDEAGIVCTPGNGFGEYGEGYFRISLTVPTERLLEAAERIKNLKL
|
Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
|
O66630
|
A2BN27
|
PSB2_HYPBU
|
Proteasome core protein PsmB 2
|
Hyperthermus
|
MLHHPGTGQLRALKGTTTVGIVFRDFVVLAADRRATAGYFVAHKRTKKIIKITDYMAMTTAGLVADAQMLAEWLANHTHYYEIVNKRRMSIHAAAQYLSIILHSAKFYPYIVQLLLGGYDTQPRLYNIDWFGSVTEEKYVATGSGSPTAIGVIEDQYSPNLSMEEAVELAKRAVASSIRRDTFTGNGVDVVVIGKDFYREYSFELKDILKTK
|
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
|
A2BN27
|
Q8SVM5
|
PMM_ENCCU
|
Phosphomannomutase
|
Encephalitozoon
|
MARDEKTIFLFDVDGTLSESRAKMPEKMGKMLESLRRKVRIGFVGGSDLAKQKEQVGDNILEIFDYGFPENGVSFYKNGTLESQEKIIDVLGEEFYKEFANFVLRYLSDIDLPIKRGNFIEYRNSMINISPIGRNCSREERMKFFELDKKEKFREKMVTAMRDRFKDSCLVFSIGGQISIDCFPKGWDKTYCLRHIKKEGVENVYFFGDMTMEGGNDYEIYNHKDVHGISVGNPDDTYRKVDQALKKIGLGGLEEN
|
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
|
Q8SVM5
|
Q5E6W1
|
PROB_ALIF1
|
Gamma-glutamyl kinase
|
Aliivibrio
|
MNTQSQTIVVKLGTSVLTGGTLKLDRAHMVELVRQCVQLKKAGHQVIVVTSGAIAAGREHLNYPELPKTMANKQLLAAVGQSCLIQAWQSLFGIYGVDVGQMLLTRADLDDRERYLNARDMLQALLKNNIVPIVNENDAVATNEIKVGDNDNLSALVGILAGADKLLLLTDQSGLFTADPRKDPKAELIKEVHTIDETLRKIAGGSGTTLGTGGMATKLQAADVARRAGIEVIIAAGSAENVITDVVNSKPQGTKFLPVECALESRKRWILAGPPSKGSIVIDEGAVNAVQQKGSSLLSKGITEVSGHFVRGGVAKIVNTKGELIARGISRYSSDDLSKILGKHSQDIYAVLGYEYGPVAIHRDDLVLI
|
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
|
Q5E6W1
|
B7LNS2
|
TYPH_ESCF3
|
TdRPase
|
Escherichia
|
MFLAQEIIRKKRDGHALSDEEIRFFINGIRDNTISEGQIAALAMTIFFHDMTMPERVSLTMAMRDSGTVLDWKSLHLNGPIVDKHSTGGVGDVTSLMLGPMVAACGGYIPMISGRGLGHTGGTLDKLESIPGFDIFPDDNRFREIIKDVGVAIIGQTSSLAPADKRFYATRDITATVDSIPLITASILAKKLAEGLDALVMDVKVGSGAFMPTYELSEALAEAIVGVANGAGVRTTALLTDMNQVLASSAGNAVEVREAVQFLTGEYRNPRLFDVTMALCVEMLTSGKLAKDDAEARAKLQAVLDNGKAAEVFGRMVAAQKGPTDFVENYAKYLPTAMLTKAVYADTEGFVSEMDTRALGMAVVAMGGGRRQASDTIDYSVGFTDMARLGDQVDGQRPLAVIHAKDENSWQEAAKAVKAAIKLADKAPESTPTVYRRISE
|
The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis.
|
B7LNS2
|
A3QFC8
|
NDK_SHELP
|
Nucleoside-2-P kinase
|
Shewanella
|
MAIERTFSIIKPDAVAKNHIGAIYNRFETAGLKIIASKMVHLSKEQAEGFYAEHSERPFFGALVEFMTSGPIMVQVLEGENAVLANREIMGATNPAEAARGTLRADFADSIDENAVHGSDAVASAEREIAYFFSAEELCPRTR
|
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
|
A3QFC8
|
Q03200
|
LIRP1_ORYSJ
|
Light-regulated protein, chloroplastic
|
Oryza sativa
|
MQTAASSVVGLSAVLPAAVKGRSLQIQAPRRVALRVRAAAAAVAVEAAEVDYSSNISVFPMEACDLIGGEACNVQMYPEAKLSSSAAVAVSRAAAEEVDRDYLSYDEPTTVFPEEACDDLGGEFCKAT
|
Thylakoid-determinant subunit of high molecular weight LFNRs-containing protein complexes.
|
Q03200
|
A7N655
|
PYRC_VIBC1
|
Dihydroorotase
|
Vibrio
|
MTTLTITRPDDWHVHLRDGEVLKDTVRDISRYNGRALIMPNTVPPVTNTEMALAYRDRILAEQHGEQFEPLMALYLTDNTTPDEIRKAKATGKIVAAKLYPAGATTNSDSGVTDAKNIYHVFEAMEEVGMLLLVHGEVTHNHVDIFDREKEFLDTVLAPIVNDFPNLKIVLEHITTSDAANFVNNASDNVAATITAHHLLFNRNHMLVGGIKPHFYCLPILKRNTHQQALIEAATSGSKKFFLGTDSAPHAKGAKESACGCAGSYTAHAALELYAEVFENEGKLENLEAFASLNGPDFYGIARNTDTVTLEKASWDVPETMPFGSDIVVPIRANEKIEWEVK
|
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
|
A7N655
|
P34814
|
PYG_AGLNE
|
Phycobilisome rod-core linker polypeptide cpcG
|
Aglaothamnion
|
MSIPILNYSLSTQNQRVNGFEGLPGDELPKIYTTDNLPTSIEMDEIIWAAYRQIFSEHQMLSSCMDRFLESQLRFNQIKVKDFIKGLVLSSAFRNLNYDCNNNYRFVEMCIQRVLGRDIYNEREKLAFAIIIASQGIETFVDFLLNSDEYIENFGDNTVPYQRRRIIAQRSKGEIPFNLKTPRLDYNFLYKKNMPQLLWSGPVRQFRPQEQKPKAGDPALFLNMVLDVSPSYLISS
|
Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
|
P34814
|
Q87L92
|
CYSH_VIBPA
|
PAdoPS reductase
|
Vibrio
|
MLDSVASKPELAELLTLTKTEQILRLAQINVELEPLSAQERVKWALENLDGEFAVSSSFGIQAAVMLHLVTQEKPDIPIILTDTGYLFAETYRFIDELTEKLNLNLKVYRAEQSAQWQEARYGKLWEQGVEGIEKYNKINKVEPMRRALKELNVGTWFSGLRREQSKSRAGLPILSIQNGVFKFLPVIDWTNKDVHYYLEQHGLTYHPLWEEGYLSVGDTHTTRKWEPGMSEEETRFFGLKRECGLHEDDGNEQDGSGI
|
Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.
|
Q87L92
|
O76878
|
RIPL_DROME
|
Rab-interacting lysosomal protein-like
|
Sophophora
|
MPGFHLNEMGEMVLDAIDDIGVVDVYDLASDIGKEYERIMDRFGTDAVSGLMPKIINTLELLEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQWRSETNELVDLVSSLQDENKRLVKQTQDLQSSSAQSSGLGASLTESIISMTNHELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQNDPNRPRYTTRELKELISERDELLTTIDTLNEQLAELKPPSQAKGKRQRHFSSSDDSDEDDDGHVADNDDDDDEEEAAAEANELEPPAAGETPPGHDAPVQGPLPYEPDDAPWKKSSESGIRKFFRKLFSDPSDGSNTFPKRSLATLSKMALSATPGSVSASAAAK
|
May have a role in lysosome distribution by interacting with Arl8.
|
O76878
|
Q9CPY7
|
AMPL_MOUSE
|
Prolyl aminopeptidase
|
Mus
|
MYLLPLPAAARVALRRLGVRGLWDRGLSTADMTKGLVLGIYAKDKDDDLPQFTSAGESFNKLVSGKLREMLNISGPPLKAGKTRTFYGLHQDFPSVVVVGLGKRSAGVDDQENWHEGKENIRAAVAAGCRQVQDLELPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKKKVAVSAKLHGSGDLEAWEKGVLFASGQNLARHLMESPANEMTPTRFAEIIEKNLKSASSKTKVHIRPKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYMGSPNATEAPLVFVGKGITFDSGGISIKASANMDLMRADMGGAATICSAIVSAAKLNLPINIIGLAPLCENMPSGKANKPGDVVRARNGKTIQVDNTDAEGRLILADALCYAHTFNPKVIINAATLTGAMDVALGSGATGVFTNSSWLWNKLFEASVETGDRVWRMPLFEHYTRQVIDCQLADVNNLGKYRSAGACTAAAFLREFVTHTKWAHLDIAGVMTNKDEIPYLRKGMSGRPTRTLIEFLLRFSKDSS
|
Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status.
|
Q9CPY7
|
Q1LR89
|
YBEY_CUPMC
|
Endoribonuclease YbeY
|
Cupriavidus
|
MVALLAEHTDTRQQAGLLVRPDNSDALSVAVTATPIVTTTGTPATPPALELDVQHGDGVSKRNGLPSRKQIEKWVKSALYADAALTVRFVDETEGRTLNRSYRGKDYATNVLTFAYAENDDDPVAGDIVLCCPVVESEAKAQKKSLEAHYAHLIVHGVLHAQGYEHDDDTEAEEMEAIETETLQALGFEDPYKPIRE
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
Q1LR89
|
C0R2X3
|
COXX_WOLWR
|
Heme O synthase
|
unclassified Wolbachia
|
MYTSVLLNVESTILDFWRLLKPRIMYLVVFTAVAGMVTAPGSMHPFLALISLICVALGSGSAGAINMWYDRDIDLLMERTKNRPIPSGRVSAESALEFGITLGILSVFIMAIAVNYISAALLAVSILFYVFIYTIWLKRRTPQNIVIGGAAGAFPPMIGWAAVTNSVSWESFILFLVIFMWTPPHFWALSLNKSEDYAKASIPMFNIVYGPEKTRKYILIYSVLLVLTSLLPALFLKKALLYLSMAIFAGCIFIWYAISILRFKNHNSQKQMFSYSISYLFSLFASIIFCSIDLF
|
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.
|
C0R2X3
|
Q8BTR5
|
DUS28_MOUSE
|
Dual specificity phosphatase 28
|
Mus
|
MGTSEAAPPPFARVAPALFIGNARAAGATELLVRAGITLCVNVSRQQPGPRAPGVAELRVPVFDDPAEDLLTHLEPTCAAMEAAVRDGGSCLVYCKNGRSRSAAVCTAYLMRHRGHSLDRAFQMVKSARPVAEPNLGFWAQLQKYEQTLQAQAILPREPIDPE
|
Has phosphatase activity with the synthetic substrate 6,8-difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site.
|
Q8BTR5
|
Q9XSZ6
|
FCERG_PIG
|
IgE Fc receptor subunit gamma
|
Sus
|
MIPAVVLLLLLLVEQAAALGEPQLCYILDAILFLYGIVLTLLYCRLKLQVRKAAIDSYEKSDGVYTGLSTRNQETYETLKHEKPPQ
|
Adapter protein containing an immunoreceptor tyrosine-based activation motif (ITAM) that transduces activation signals from various immunoreceptors. As a component of the high-affinity immunoglobulin E (IgE) receptor, mediates allergic inflammatory signaling in mast cells. As a constitutive component of interleukin-3 receptor complex, selectively mediates interleukin 4/IL4 production b basophils priming T-cells toward effector T-helper 2 subset. Associates with pattern recognition receptors CLEC4D and CLEC4E to form a functional signaling complex in myeloid cells. Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of ITAM, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes. May function cooperatively with other activating receptors. Functionally linked to integrin beta-2/ITGB2-mediated neutrophil activation. Also involved in integrin alpha-2/ITGA2-mediated platelet activation.
|
Q9XSZ6
|
A9MJ94
|
5DNU_SALAR
|
Nucleoside 5'-monophosphate phosphohydrolase
|
Salmonella
|
MKQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAAIKNRKFGGQLNAEHIALLAMYHDTSEVLTGDLPTPVKYFNSQIAQEYKAIEKIAQQKLVDMAPDELRDIFAPLIDENAWSEEEQAIVKQADALCAYLKCLEELSAGNNEFKLAKTRLEKTLALRRSQEMDYFMAVFVPSFHLSLDEISQDSPL
|
Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates.
|
A9MJ94
|
A0A0K2G9F6
|
UBACT_NITMO
|
Prokaryotic ubiquitin-like protein UBact
|
Nitrospira
|
MNMRYTLMPERREGPVDPMPQSPSPSDEGGGPRRPETGSPDKDNLLKRMRKVDPKQAERYRQRTGE
|
May function as a protein modifier covalently attached to lysine residues of substrate proteins. This may serve to target the modified proteins for degradation by proteasomes.
|
A0A0K2G9F6
|
Q5PLH2
|
EPMA_SALPA
|
EF-P-lysine lysyltransferase
|
Salmonella
|
MSETATWQPSASIPNLLKRAAIMTEIRRFFADRGVLEVETPCMSQATVTDIHLFPFETRFVGPGHSQGMNLYLMTSPEYHMKRLLAAGCGPVFQLCRSFRNEEMGRHHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCQPAESLSYQQAFQRHLEIDPLSADKTQLREAAAKLDLSNIADTEEDRDTLLQLLFTMGVEPHIGKEKPTFIYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQQPIDQNLLDALAAGLPDCSGVALGVDRLVMLALGAESLADVIAFTVDRA
|
With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34'.
|
Q5PLH2
|
O60678
|
ANM3_HUMAN
|
Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3
|
Homo
|
MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSAEETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEYLKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAREDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLNKLEDTITLIKGKIEEVHLPVEKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYPDICTISLVAVSDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIKHIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTVFLLEKPFSVKAGEALKGKVTVHKNKKDPRSLTVTLTLNNSTQTYGLQ
|
Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases (Probable). May regulate retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal dehydrogenase activity .
|
O60678
|
Q6GDF3
|
SECA2_STAAR
|
Protein translocase subunit SecA 2
|
Staphylococcus
|
MKHKLDVTINELRLKSIRKIVKRINTWSDEVKSYSDDVLKQKTLEFKERIASGVDTLDTLLPEAYAVAREASWRVLGMYPKEVQLIGAIVLHEGNIAEMQTGEGKTLTATMPLYLNALSGKGTYLITTNDYLAKRDFEEMQPLYEWLGLTASLGFVDIVDYEYQKGEKRNIYEHDIIYTTNGRLGFDYLIDNLADSAEGKFLPQLNYGIIDEVDSIILDAAQTPLVISGAPRLQSNLFHIVKEFVDTLIEDVHFKMKKTKKEIWLLNQGIEAAQSYFNVEDLYSEQAMVLVRNINLALRAQYLFESNVDYFVYNGDIVLIDRITGRMLPGTKLQAGLHQAIEAKEGMEVSTDKSVMATITFQNLFKLFESFSGMTATGKLGESEFFDLYSKIVVQVPTDKAIQRIDEPDKVFRSVDEKNIAMIHDIVELHETGRPVLLITRTAEAAEYFSKVFFQMDIPNNLLIAQNVAKEAQMIAEAGQIGSMTVATSMAGRGTDIKLGEGVEALGGLAVIIHEHMENSRVDRQLRGRSGRQGDPGSSCIYISLDDYLVKRWSDSNLAENNQLYSLDAQRLSQSSLFNRKVKQIVVKAQRISEEQGVKAREMANEFEKSISIQRDLVYEERNRVLEIDDAENRDFKVLAKDVFEMFVNEEKVLTKSRVVEYIYQNLSFQFNKDVACVNFKDKQAVVTFLLEQFEKQIALNRKNMQSAYYYNIFVQKVFLKAIDSCWLEQVDYLQQLKANVNQRQNGQRNAIFEYHRVALDSFEVMTRNIKKRMVKNICQSMITFDKEGMPVIHFP
|
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
|
Q6GDF3
|
Q96HU8
|
DIRA2_HUMAN
|
Distinct subgroup of the Ras family member 2
|
Homo
|
MPEQSNDYRVAVFGAGGVGKSSLVLRFVKGTFRESYIPTVEDTYRQVISCDKSICTLQITDTTGSHQFPAMQRLSISKGHAFILVYSITSRQSLEELKPIYEQICEIKGDVESIPIMLVGNKCDESPSREVQSSEAEALARTWKCAFMETSAKLNHNVKELFQELLNLEKRRTVSLQIDGKKSKQQKRKEKLKGKCVIM
|
Displays low GTPase activity and exists predominantly in the GTP-bound form.
|
Q96HU8
|
Q9SQ80
|
G2OX1_PEA
|
Protein SLENDER
|
Pisum
|
MVLLSKPTSEQYTYVRNNMPITFSSSIPLVDLSKPDAKTLIVKACEDFGFFKVINHGIPLDAISQLESEAFKFFSLPQTEKEKAGPANPFGYGNKRIGLNGDIGWIEYLLLTTNQDHNFSLYGEDIDKFRGLLKDYKCAMRNMACEILDLMAEGLKIQPKNVFSKLVMDKQSDCLFRVNHYPACPELAINGENLIGFGEHTDPQIISILRSNNTSGFQISLRDGSWISVPPDHSSFFINVGDSLQVMTNGRFKSVRHRVLANGIDPRLSMIYFCGPPLSEKIAPLPSLMKGKESLYKEFTWFEYKSSTYGSRLADNRLGNYERIAAT
|
Catalyzes the 2-beta-hydroxylation of several biologically active gibberellins, leading to the homeostatic regulation of their endogenous level. Catabolism of gibberellins (GAs) plays a central role in plant development. Converts GA9/GA20 to GA51/GA29 and GA4/GA1 to GA34/GA8.
|
Q9SQ80
|
P45626
|
GLNA2_RHIML
|
Glutamine synthetase II
|
Sinorhizobium
|
MTKYKLEYIWLDATRPYQTLRGKTQIKEFDAFPTLEQLPLWGFDGSSTLQAEGRTSDCVLKPVTVYPDPVRTNGALVMCEVMMPDAETPHASNTRATVLDDEGAWFGFEQEYFFYKNGRPLGFPEQGYPAPQGPYYTGVGYKNVGDVARQIVEEHLDICLAAGINHEGINAEVAKGQWEFQIFGKGSKKAADEVCVARYLLVRLTEKYGIDVEFHCKPLGDTDWNGSGMHANFSTAYLREVGGQDYFEALMAAFEKNLHDHINVYGPDNHLRLTGKHETAPWDKFSYGVADRGASIRVPHSFVNNAYPGYLEDRRANSQGDPYQMLLSS
|
Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
|
P45626
|
Q31VE6
|
NIKE_SHIBS
|
Nickel import ATP-binding protein NikE
|
Shigella
|
MTLLNVSGLSHHYAHGGFSGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNISWRGESLAKLNRAQRKAFRRDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDETVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQAVGDKLTFSSDAGRVLQNAVLPAFPVRRRATEKV
|
Part of the ABC transporter complex NikABCDE involved in nickel import. Responsible for energy coupling to the transport system.
|
Q31VE6
|
O18924
|
PPARG_MACMU
|
Nuclear receptor subfamily 1 group C member 3
|
Macaca
|
MGETLGDSPIDPESDSFTDTLSANISQEITMVDTEMPFWPTNFGISSVDLSVMDDHSHSFDIKPFTTVDFSSISAPHYEDIPFTRTDPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY
|
Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of ARNTL/BMAL1 in the blood vessels.
|
O18924
|
Q99Z28
|
PYRDA_STRP1
|
Putative dihydroorotate dehydrogenase A (fumarate)
|
Streptococcus
|
MVSTATQIGHFSFDNCLMNAAGVYCMTKEELMEVEKSQAASFVTKTGTLEVRPGNPEPRYADTRLGSINSMGLPNNGFRYYLDFVSDLAKTGQHKPHFLSVVGLSPTETETILKAIMASDYEGLVELNLSCPNVPGKPQIAYDFETTDQLLENIFTYYTKPLGIKLPPYFDIVHFDQAAAIFNKYPLSFVNCVNSIGNGLVIKDEQVLIKPKNGFGGIGGDYIKPTALANVHAFYKRLKPSIHIIGTGGVKTGRDAFEHILCGASMVQIGTALHQEGPAIFERVTKELKTIMVEKGYQSLDDFRGNLRYKD
|
Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor.
|
Q99Z28
|
A8GW65
|
ACPS_RICB8
|
4'-phosphopantetheinyl transferase AcpS
|
belli group
|
MIIGVGTDIVQIPRIEKIIKLYPEIFPKRILNTEELKKFALLKKESHVTFLAKRFAAKEAISKAFGVGIGRGINFKDITLLNDELGKPIVKIDSLYTQKLPPFNIHLSLSDDYPICVAFVVVEKIIL
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
|
A8GW65
|
Q91XM9
|
DLG2_MOUSE
|
Postsynaptic density protein PSD-93
|
Mus
|
MFFACYCALRTNVKKYRYQDEDGPHDHSLPRLTHEVRGPELVHVSEKNLSQIENVHGYVLQSHISPLKASPAPIIVNTDTLDTIPYVNGTEIEYEFEEITLERGNSGLGFSIAGGTDNPHIGDDPGIFITKIIPGGAAAEDGRLRVNDCILRVNEVDVSEVSHSKAVEALKEAGSIVRLYVRRRRPILETVVEIKLFKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIDGGAAQKDGRLQVGDRLLMVNNYSLEEVTHEEAVAILKNTSDVVYLKVGKPTTIYMTDPYGPPDITHSYSPPMENHLLSGNNGTLEYKTSLPPISPGRYSPIPKHMLGEDDYTRPPEPVYSTVNKLCDKPASPRHYSPVECDKSFLLSTPYPHYHLGLLPDSDMTSHSQHSTATRQPSVTLQRAISLEGEPRKVVLHKGSTGLGFNIVGGEDGEGIFVSFILAGGPADLSGELQRGDQILSVNGIDLRGASHEQAAAALKGAGQTVTIIAQYQPEDYARFEAKIHDLREQMMNHSMSSGSGSLRTNQKRSLYVRAMFDYDKSKDSGLPSQGLSFKYGDILHVINASDDEWWQARRVTLDGDSEEMGVIPSKRRVERKERARLKTVKFNAKPGVIDSKGDIPGLGDDGYGTKTLRGQEDLILSYEPVTRQEINYTRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVISREQMEKDIQEHKFIEAGQYNDNLYGTSVQSVRFVAERGKHCILDVSGNAIKRLQVAQLYPIAIFIKPKSLEPLMEMNKRLTEEQAKKTYDRAIKLEQEFGEYFTAIVQGDTLEDIYNQCKLVIEEQSGPFIWIPSKEKL
|
Required for perception of chronic pain through NMDA receptor signaling. Regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord. Interacts with the cytoplasmic tail of NMDA receptor subunits as well as inward rectifying potassium channels. Involved in regulation of synaptic stability at cholinergic synapses. Part of the postsynaptic protein scaffold of excitatory synapses.
|
Q91XM9
|
P93198
|
2SS_JUGRE
|
2S albumin seed storage protein large subunit
|
Juglans
|
AALLVALLFVANAAAFRTTITTMEIDEDIDNPRRRGEGCREQIQRQQNLNHCQYYLRQQSRSGGYDEDNQRQHFRQCCQQLSQMDEQCQCEGLRQVVRRQQQQQGLRGEEMEEMVQSARDLPNECGISSQRCEIRRSWF
|
Seed storage protein.
|
P93198
|
P46017
|
FRAH_NOSS1
|
Protein FraH
|
Nostoc
|
MIVCPNCNHPNPDGAVQCEACYTPLPATSNCPNCGATVQSDAAFCGQCGFNLHSVAAPAATVATIAPDVPVEVPPLANPDPLLELLQPNALGLDPVANENPPAPAPLPPTAVAAPPDATPVVVEVTPAPPPPEPVVVEASIPTPPPEPVAPPEPVPAVEPAPAPETVVAAPPSPARTQLQQITARLVHVQSDQEIELPPSLSVVHIGKPNDRIPPDVDVSGFANSEIVSRVHADIRLEGDAHYIEDVGSSNGTYINNLPLLPGNRHRLRPGDRISLGKGDLVTFLFKLA
|
Putative heterocyst to vegetative cell connection.
|
P46017
|
Q58HT5
|
AWAT1_HUMAN
|
Long-chain-alcohol O-fatty-acyltransferase 1
|
Homo
|
MAHSKQPSHFQSLMLLQWPLSYLAIFWILQPLFVYLLFTSLWPLPVLYFAWLFLDWKTPERGGRRSAWVRNWCVWTHIRDYFPITILKTKDLSPEHNYLMGVHPHGLLTFGAFCNFCTEATGFSKTFPGITPHLATLSWFFKIPFVREYLMAKGVCSVSQPAINYLLSHGTGNLVGIVVGGVGEALQSVPNTTTLILQKRKGFVRTALQHGAHLVPTFTFGETEVYDQVLFHKDSRMYKFQSCFRRIFGFYCCVFYGQSFCQGSTGLLPYSRPIVTVVGEPLPLPQIEKPSQEMVDKYHALYMDALHKLFDQHKTHYGCSETQKLFFL
|
Acyltransferase that catalyzes the formation of ester bonds between fatty alcohols and fatty acyl-CoAs to form wax monoesters . Shows a strong preference for decyl alcohol (C10), with less activity towards C16 and C18 alcohols . Shows a strong preference for saturated acyl-CoAs .
|
Q58HT5
|
Q7VMD0
|
NDK_HAEDU
|
Nucleoside-2-P kinase
|
Haemophilus
|
MLQQTLCLIKPDATQRNLIGKIISYLENAGLKIKAIKKLQLTQAQAEKFYLEHQDKPFFASLVGFMISAPIVAIVLEGENAIAHYRELMGATNPEQREAGTIRALYAISNQENSVHGSDSETSAKREIDYFFSKEEIC
|
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
|
Q7VMD0
|
Q3AHX1
|
RPIA_SYNSC
|
Phosphoriboisomerase A
|
unclassified Synechococcus
|
MADLQTQMKQAVADAAVEQIKDGMVLGLGSGSTAALMIQGLGAKLASGELKDIVGVTTSFQGEVLAAELNIPLLSLNAVSRIDLAIDGADEVDPGFQLIKGGGACHVQEKLVAARADRFVVVVDSTKLVDRLNLGFLLPVEVLPGAWRQVKQQLEALGGSAELRMAQRKAGPVVTDQGNLVLDAKLDGGISDPVALEQTINNIPGVLENGLFVNITDEVLVGEITDGVAGVRSLQKRLS
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
Q3AHX1
|
Q5PCK6
|
PXPA_SALPA
|
5-oxoprolinase (ATP-hydrolyzing) subunit A
|
Salmonella
|
MNIDLNADLGEGCASDSELLTLVSSANIASGFHAGDAQTMLTCVREALKNGVAIGAHPSFPDRDNFGRTAMVLPPETVYAQTLYQIGALGAIVQAQGGVMRHVKPHGMLYNQAAKDPRLAQAIAKAVHDYDPSLILVGLAGSELIRAGERCRLVTRQEVFADRGYQADGSLVPRMQPGALIHDEEQALAQTLDMVQAGRVKSVTGVWTTVTAQTVCIHGDGEYALAFARRLRAAFNARNIHVIA
|
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
|
Q5PCK6
|
Q5QW09
|
SYDP_IDILO
|
Protein Syd
|
Idiomarina
|
MKTLEESIDALMTRYKENVPVRYTEYVEEWNSPIYGTVIDENTVEWTPCRQPEALNFDDLESALEMSFHQSIKTLFGRWYAGDLALDYQGHTISLLQTQSAEDGERLLENITGHILMKRRLKQPETVFIGLGSEDDGLLVTIDNQSGAVGLEWVGKEQHDVLSDSLAAWLDNCQPQVETDKNS
|
Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function.
|
Q5QW09
|
F4HWY6
|
MYO11_ARATH
|
Myosin XI E
|
Arabidopsis
|
MRNSGTPVNIIVGSHVWIEDSDVAWIDGLVEKINGQDVEVQATNGKKITAKLSKIYPKDMEAPAGGVDDMTKLSYLHEPGVLQNLKIRYELNEIYTYTGNILIAINPFQRLPHIYDAHMMQQYKGAPFGELSPHVFAVADVAYRAMINEGKSNSILVSGESGAGKTETTKMLMRYLAYLGGRAVTEGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKQGRISGAAVRTYLLERSRVCQISDPERNYHCFYLLCAAPQEELEKYKLGHPKTFHYLNQSKCFELVGISDAHDYIATRRAMDIVGMSEKEQEAIFRVVAAILHLGNVEFTKGKEVDSSVPKDDKSKFHLNTVAELLMCDVKALEDALCKRVMVTPEEVIKRSLDPQSALISRDGLAKTIYSRLFDWLVEKINVSIGQDATSRSLIGVLDIYGFESFKTNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEAIDWSYIEFVDNQDVLDLIEKKPGGIVALLDEACMFPKSTHETFANKLYQTFKTHKRFIKPKLSRTDFAVAHYAGEVQYQSDLFLDKNKDYVIPEHQDLLGASKCPFVVGLFPPLPEETSKSSKFSSIGSRFKLQLQQLMETLNSTEPHYIRCVKPNNLLKPAVFENVNIMQQLRCGGVLEAIRISCAGYPTRKPFFEFINRFGLLYPRALEGNYEEKAAAQKILDNIGLKGYQVGKTKVFLRAGQMAELDARRTMVLSAAAKKIQRRIRTHQAQRRFILLRKATISLQALCRGRLSSKIFDNLRRQAAAVKIQKNARRLHSRKSYKNLHVAALVVQTGLRAMAAHKQFRFRKQTKAATTIQAQFRCHRATLYFKKLKKGVILSQTRWRGKLARRELRQLKMASRETGALKEAKDMLEKKVEELTYRAQLEKRSRVDLEEEKNQEIKKLQSSLEEMRKKVDETNGLLVKEREAAKKAIEEAPPVVTETQVLVEDTQKIEALTEEVEGLKANLEQEKQRADDATRKFDEAQESSEDRKKKLEDTEKKAQQLQESVTRLEEKCNNLESENKVLRQQAVSIAPNKFLSGRSRSILQRGSESGHLSVDARPSLDLHSHSINRRDLSEVDDKPQKSLNEKQQENQELLIRCIVQHLGFQGKRPVTACIIYKCLLQWRSFEVERTSVFDRIIQTIGQAIETQDNNNILAYWLSNASTLLLLLQRTLKASGAAGMAPQRRRSSSATLFGRMTQSFRGTPQGVNLAMINGGVDTLRQVEAKYPALLFKQQLTAYVEKIYGMIRDNLKKEISPLLGLCIQAPRTSRASLVKGASRSVGNTAAQQALIAHWQGIVKSLTNFLNNLKSNHVPPFLVRKVFTQIFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELEHWCYNATDEYAGSSWDELKHIRQAIGFLVIHQKPKKTLDEISHELCPVLSIQQLYRISTMYWDDKYGTHSVSPDVIANMRVLMTEDSNNAVSNSFLLDDDSSIPFSVDDLSKSMERIEIGDVEPPPLIRENSGFSFLLPCSD
|
Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in trafficking of Golgi stacks, mitochondria and peroxisomes.
|
F4HWY6
|
Q4UMI6
|
RICKA_RICFE
|
Actin polymerization protein rickA
|
spotted fever group
|
MAKEIDINKLLAQENNALNTILSQVNELCEQNKKLQGLIEIQNETKELEKEHNRSLPWFKRLVKTVSNVKYIFVKSEEQLTNEAIKYNNKILKDIDNKIYNIAEKSAPLKQELQEEIEKNFKDLTKKDLSKEQRERLSEVYFSYKSKPERFSALNMTNPLQFIKAEELEKQYNSLNATKQNIQNLISENSNIKELKEIQKQVAEIREEIPYTFFEKLNNIWQNVKNVFVNNSEQVLAKNKESNTRAIRKIDEQLYKTKHKFEELIENKERNINDIIAKLPDNEELQKIVSNLANHMTSKKEPILTTSSIAKPLENNVTPPPPLTKNNIPPPPPPPPLSKNNILPPPPPPMPTMAPAQTETLSKPVGVTTTVKKLENQPRPSIDTSDLMREIAGPKNLRKVEKTDVKTQDSRDLLLQSIRGEHKLRKVEFDPNTGKPVAHSHSKPAQNVSKPNGVASILARRVAMEMSDSSSSSGSESDSGNWSDASVNSNKPKALKTRGERDAKTTTHAQKILSNRSSQKPSFVRS
|
Recruits and activates the Arp2/3 complex, which in turn leads to actin polymerization, promoting Rickettsia motility during infection.
|
Q4UMI6
|
Q96CN9
|
GCC1_HUMAN
|
Golgi coiled-coil protein 1
|
Homo
|
MEKFGMNFGGGPSKKDLLETIETQKKQLLQYQARLKDVVRAYKSLLKEKEALEASIKVLSVSHEADVGLAGVQLPGLTFPDSVDDRCSTHSEDSTGTATSLDTAASLTSTKGEFGVEDDRPARGPPPPKSEEASWSESGVSSSSGDGPFAGGEVDKRLHQLKTQLATLTSSLATVTQEKSRMEASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKATALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLHRQELERCQLDFRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALASGLPGRRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTFFLYAEQLARKEVEITSLRKQKHRLEVEVHQLQDRLLEEGERHREEVAALQSHIEKNIRDQSREGANLEYLKNIIYRFLTLPDSLGRQQTLTAILTILHFSPEEKQVIMRLPTSASWWPSGKR
|
Probably involved in maintaining Golgi structure.
|
Q96CN9
|
Q4URG5
|
DSBB_XANC8
|
Disulfide oxidoreductase
|
Xanthomonas
|
MNPFRWGFRAQFLLGFLACAGLLAYAIYVQLHLGLEPCPLCIFQRIAFATLALLFLLGALHGPRGAGGRKAYGVLAFIAAGVGMGIAARHVWVQIRPKDMMSSCGPPLSFLSETMGPFEVFRTVLTGTGDCGNIDWRFLGLSMPMWSMVWFVGLALWALYAGFKHRGPRKLF
|
Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
|
Q4URG5
|
Q5PAJ5
|
IF2_ANAMM
|
Translation initiation factor IF-2
|
Anaplasma
|
MLMSDVEKFGGDCGSSGGSGRPTLKLGTRASTLAKTPTSTGGRTFMTVEVRSRKRKASGASPAEGVGYGTSPYTSDDNRQGQISRSATCSLTAREQLSRINAIHTADSISAQKEAAKKLRDEEEVEVAPPEGESVIDEPDSVKEPAAAADAVADVATPVLGDIAPGAAGTRPGRGGHDDKGKRYSYQGAGGKIKEKEGGGGVKKAAASRASSKHIKLDIENALSGTEERYVLMASSRRRGGSKSDRRISRDVVIPDEIEVKALAAAMAEKVGDVLRVLSHMGVEARQNTAIGSDVASEVAERFSHRPKVVSKIQMERELSDISDSGLALEPRPPVVTVMGHVDHGKTSLLDVLRKSNVAEKEFRGITQHIGAYQIDVDGKKITFLDTPGHEAFSDMRARGTNVTDIVVLVVAADDGVMPQTVESINHVKTAGVSMVVAVNKIDRSDANVDKITNDLLQHGVVPEKLGGDVMIVPVSAKTGENLDKLKSSILLLAEMLELRAPVEGRAQGVVIESKIERNCGVVATVIVQRGTLRKGNVVVAGDGSYGKVRNMFDDSDNSVEEALPSMPVRVLGLDKVPKAGDVFLVMPSEKHARDLLEHRAGINLSRGRDSGRNDSVFTGPLFSMDRPEGVNMILKADVAGSLEAISRSVAQIEHEEVKFNILHKDIGDVTKSDILLAEAASAVVLAFNVKVDAQARDLVRQKDVDIRHHRVIYDLIDDVKGVVCGKLKPIIREVQVGLLVVREVFSSGKGGTVIGCYVSEGAVSRGALVKIYRNDAVTCEGKVKVLRRFKDDVKEVGHGLECGVLVEGAKDVAVGDVIKVLEVVEHARVVE
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
Q5PAJ5
|
C1DJD3
|
HIS6_AZOVD
|
ImGP synthase subunit HisF
|
Azotobacter
|
MALAKRIIPCLDVDNGRVVKGVRFENIRDAGDPVEIAQRYDEQGADEITFLDITASHEGRDTTLHTVERMASQVFIPLTVGGGVRTVQDIRNLLNAGADKVSINTAAVFNPEFVGEAAGRFGSQCIVVAIDAKKVSGPGEAPRWEIFTHGGRKPTGLDAVAWAKKMEDYGAGEILLTSMDQDGMKSGFDLGVTRAISEAVGIPVIASGGVGNLEHLAAGILEGKADAVLAASIFHFGEYTVPEAKAYLAGRGIVVR
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
|
C1DJD3
|
Q252V9
|
RS3_CHLFF
|
30S ribosomal protein S3
|
Chlamydia
|
MGQKGCPIGFRTGVTKKWRSLWYGNKQEFGKFLIEDVKIREHLRKKPSCQGAAGFVVRRMSGKIEVTIQTARPGLVIGKKGAEVDLLKEELRKLTGKEVWVEIAEIKRPELNAKLVADNIARQIERRVSFRRAMKKAMQSVMEAGAIGVKIQVSGRLAGAEIARSEWYKNGRVPLHTLRADIDYATASAETTYGIIGVKVWINLGEKTSTANASAGSAVSTAQ
|
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
|
Q252V9
|
P97347
|
RPTN_MOUSE
|
Repetin
|
Mus
|
MPQLLNSILNVSKVFQDYAEYHGVGASLSKKELKQLLLTEFGDILRRPNDPETVETILEHLDRDRNGYVDFHEYLLLVFQLVQACHHKLDSKFYGSRTSSQKEHDQEGTRSHKFSESTGRQHRQRYEGERRNSHHNQSEGQHQNVQHDQSQRQDKDSERHDTDPHCGQSETFHGDSHYGHSERQDTDYSSDQSESDNESSSSSQRLGYKSSHEQPKGQGYVFALSQSKNPEQAFHYGQSKTSGQQSSHGQSGRFRKDSYSSQTSQQESDSYEQYGSQHQKSGNSQTERQGQNSQYGQTNKKGHSSYHEQTEGQGQSFHYGQKGRKDQSFQQGQKGRKDQSPHLGQKGRQDQSPHRGQKGRQDQSPHQGQKGRQDQSPHRGQKGRQDQSPHQGQKGRQDQSPHLGQKGRQDQSPHQGQKGRQDQSPHQGQKGRQDQSSHQGQKGRQDQSSHQGQKGRQDQSSHQGQKGRQDQSSHQGQREGQDQNSQWHRTDSQGQSFHYGQTGGHSLSSHQGQTDSQGQNSNWHRTDSQGQSFHYGQTGGQGLSSHQGQTDSQGQNSNWHRTDSQGQSFHFDQAGREVQGSHHGQTDRQSQNSNWHRTDSQGQSFHFDQAGKEVQGSHQGQTDSQGQSSHWHQTDRQGQSSQQGHKDRQGQNTHQGQKGRQDLSPHQGQKGRQDQSPHLGQKGRHDQSPHQGQKGRHDQSPHQGQKGRQDLSSHQGQKGRQDQSPHLGQKGRHDQSPHRGQKGRQDQSPHQGQKGRQDQSSHQGQREGQDQNSHWHRTDRQGQSFHYGQTGGQGLSSHQGQTDSQGQNSQWHRTDSQGQSFHFDQAGREGQSSHHGQTDRQSQSSHCGQSEIGKTENQGQNRHSLGTDRTRRDSYVEQSGRSVKLSQQNSREEVRQTQSQRSHDRREQQIQQQTWKPKEDNQHKLLAQVQQEPYSYEEYDWQSQSSEQDHCGEEEYQDWDRHSVEDQENLYEMQNWQTHEEEQSHQTSDRQTHVDEQNQQRQHRQTHEENHDHQHGRHHEDEHNHRRQDHHQQRERQTHEEKEKYQGGQDQSRSFPNREKSHMSEDDQCEGPQGRRFHPTHGGGKSQRREKSGNHPTKPANYSSPLYDYVQEQAAYQY
|
Involved in the cornified cell envelope formation. Multifunctional epidermal matrix protein.
|
P97347
|
E0SIS1
|
RHSIB_DICD3
|
Immunity protein RhsIB
|
Dickeya
|
MNIENAYDQLNAWINTSNGSYIDIGGERYSFSRLKTITKDELSNFESDNNLKLPNDYKSFLINVGCVNIFVGEKTAGIEIIPPTDIRNFSKSVFYNFGDDLYPRLLLTTSIPKLGYFGGFWMESESKENYGIFYPDIPPELWIEECDFIKFDDWLIKLVKYKSRKI
|
Immunity component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. Specifically inhibits its cognate toxin RhsB. Cell contact is necessary for growth inhibition.
|
E0SIS1
|
Q3KLI3
|
RL6_CHLTA
|
50S ribosomal protein L6
|
Chlamydia
|
MSRKARDPIVLPQGVEVSIQNDEISVKGPKGSLTQVLAKEVEIAVKGNEVFVTPAAHVVDRPGRIQGLYWALIANMVKGVHTGFEKRLEMIGVGFRAAVQGSLLDLSIGVSHPTKMPIPTGLEVSVEKNTLISIKGINKQLVGEFATCVRAKRPPEPYKGKGIRYENEYVRRKAGKAAKTGKK
|
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
|
Q3KLI3
|
Q2RIU8
|
IDI2_MOOTA
|
Type 2 isopentenyl diphosphate isomerase
|
Moorella
|
MNEREYIGRGRRKLEHLRFFQEDSKGSNGLEDVHLVHQALPELNWSDIDLTCRWLGKTLAAPFIINALTGGPPETLAINAALARVARRTGIALAVGSQRAGLENKEWRESFTIVRRENANGLILANIGAGNSPADAGEAVAMIAADGLQVHLNAAQELIMPEGDRAFRGWLENIRGMVNTLGVPVIAKEVGFGLSRETALQLYQAGVRIMDVGGRGGTNFAAIEERRRGRSVAALAGWGLSTAVSILEIRELGLPVEVVATGGIRSALDAARALALGAKIVGAAGYFLKILLEQGEDALTEEILQWQEDLKRICLLTGCTTPAELATKPVVITGQTRAWLEGRQRH
|
Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
|
Q2RIU8
|
B2FMH7
|
AROE_STRMK
|
Shikimate dehydrogenase (NADP(+))
|
Stenotrophomonas maltophilia group
|
MTDRYAVFGHPVAHSKSPQIHATFGRQEGIAVDYRAIDLAPEAFLAGLEAFAADGGVGANVTSPHKEAAFSVCTTLTARARRAGSVNTLLRKGDRWHGDTTDGIGLVRDLTDRHGLDLRGRRMLLIGAGGSARSVAPALLDAGITELVVVNRTPERADELIDAMGEPGRAISRYWEDLRDLGDFELIVNATSAGRDRDIEFKLPLSLVNSMTTAVDLNYGEAAIAFLAWARAAECRNTVDGLGMLVEQAAESFLQWHGVRPQTDEVYQSLRQGSAVLAGED
|
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
|
B2FMH7
|
Q1BT81
|
LIPB_BURCA
|
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
|
Burkholderia cepacia complex
|
MSVSPVSIVSTPVAVSASPAGAPDQPVQPVTVRWRGREAYEASFDAMRAFTDTRTADTGDEIWVVEHPPVYTLGQAGDPAHLLVADSGVPLVKVDRGGQITYHGPGQIVVYLLLDLRRRKLMVRALVTKIEEAVIETLAAYNLASVRKAGAPGIYVASGVHEGAKIAALGLKIRNGCSYHGLSLNVKMDLRPFLAINPCGYAGLETVDMASLEVAADWNDVAHTLVGRLIANLDGASAAADKPHALEQSND
|
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.
|
Q1BT81
|
Q9LYT5
|
PME35_ARATH
|
Pectin methylesterase 35
|
Arabidopsis
|
MATTSFSLPNHKFGIKLMLFLVLNLLSLQTSVFAHSSNSKFTKISRHPNSDSSSRTKPSTSSNKGFLSSVQLSLDHALFARSLAFNLTLSHRTSQTLMLDPVNDCLELLDDTLDMLYRIVVIKRKDHVNDDVHTWLSAALTNQETCKQSLSEKSSFNKEGIAIDSFARNLTGLLTNSLDMFVSDKQKSSSSSNLTGGRKLLSDHDFPTWVSSSDRKLLEASVEELRPHAVVAADGSGTHMSVAEALASLEKGSGRSVIHLTAGTYKENLNIPSKQKNVMLVGDGKGKTVIVGSRSNRGGWNTYQSATVAAMGDGFIARDITFVNSAGPNSEQAVALRVGSDRSVVYRCSIDGYQDSLYTLSKRQFYRETDITGTVDFIFGNSAVVFQSCNLVSRKGSSDQNYVTAQGRSDPNQNTGISIHNCRITGSTKTYLGRPWKQYSRTVVMQSFIDGSIHPSGWSPWSSNFALKTLYYGEFGNSGPGSSVSGRVSWAGYHPALTLTEAQGFTVSGFIDGNSWLPSTGVVFDSGLL
|
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
|
Q9LYT5
|
Q6C1W9
|
TRM10_YARLI
|
tRNA(m1G9)-methyltransferase
|
Yarrowia
|
MVDVTEPVAPVEAVKETAGASSATPEVDRTSEPHPKNPQNVPAPYNTKTAVIPEGMSKNEWKKAQKKAIWESKKDEIAAVKKEKKKAARKRKQLAISRGEIPAPIPQDERPPQTQLPISIVLDCGFDEMMTQKEKVSLSAQVGRCYSANRKADARFDLTVNSFNKGLKDRFNNEMNKVHELWTNIKFVEDDYTVPEDETAKSKLVYLSSDSDNVINELEDGKTYIIGGIVDKGRYKNLCQDKASKQGLQTGRLPIADFIKLSGRKVLTTNHVFEILLKWTELKDWKAAFEAVLPMRKLDPANYGRAHRRARKKARLAEGAEGNDEEDDEDDDDEEEEEEESVSAEPEVVETKAEVETDTETKAETEAETKA
|
S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
|
Q6C1W9
|
Q4FQD6
|
DTD_PSYA2
|
Gly-tRNA(Ala) deacylase
|
Psychrobacter
|
MRALIQRVKHASVSVDGHDVGAIEHGVLAYIGLGHDDNLQSAQRMVDKILTYRIFENDDDPAKYGKLDKNVQQVDGGLLLVSQFTLMAKTDKGRRPDFGGAMAPDAAQDLFAQLIAYAKTQHVDVATGQFGADMQVLSVNDGPLNFLLEVP
|
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.
|
Q4FQD6
|
B4SUV1
|
TUSD_SALNS
|
tRNA 2-thiouridine synthesizing protein D
|
Salmonella
|
MRYAIMVTGAAYGTQQASSALQFAHALLNEGHELASVFFYREGVYNANLLTSPASDEYDLVRAWQKLNTQHGVALNICVAAALRRGIIDETEAGRLGLPSANLQPGFTLSGLGALAEASLTCDRVVQF
|
Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Accepts sulfur from TusA and transfers it in turn to TusE.
|
B4SUV1
|
Q7U4S9
|
NRDR_PARMW
|
Transcriptional repressor NrdR
|
Parasynechococcus marenigrum
|
MQCPSYQNTDSRVLESRAADGGRSVRRRRECLNCEFRFTTYERVETVPITVIKRNGNREIFSRSKLLHGLNRACEKTGLDASRLETLVEELELKLQQRSGREVSSAEIGELVLVELKQMSEVAYIRFASVYRQFQGIDDFVSTLETMNRKAGPGHLAAVG
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
|
Q7U4S9
|
Q75AV6
|
RTC1_ASHGO
|
Restriction of telomere capping protein 1
|
Eremothecium
|
MGARRESGLHSFLNRKTPPTADMQQGSGGTRPQPFSRFTYGSKSAQSSGGMGGQVACSPKGRGSQRSLLSSNFPFMESVFEDRTAAPQRTPTPRDERSEYFGEAEGSSGLRSSLQCNRELASLDKINDAQARMVVVAGKSHLGLYKFDEAYRMQQVHDYMTPGSLGGGTKFSSSMRRNMRKISTISDVKAGFHHHKNYIAICGTSTSVSIYDINRASAKDSPLITTLSEHSRSINSVDFNMGQTHLLISGGQDGCIKVWDLRSHSYKVNRSDLNFNSGSDSVRDVKWMPTYDFASLGADTSLCSSGRSNKFASVHDSGLLLTFDMRQPNQVERKINAHSGPGLCMHWHPHMDYIISGGRDGKCALWYVGDKVNSMVSVPQGHNSATSYSINTAPITTGYLETVINTSHPVSKLKFRPKYVHNMLNSLIATSSMGEDSDVTIYSLARKHIPQNILTTAAPSLGFVWWNEDIVFNIDKQSVISAWDIRYEPTLLDNLPKGIVKWRDMDGSGLVFVAQEKGTYSMDNGGVTDSVGKGAANRMSNTTLNSTNNMGRDQEVFTYSFQQQYKHQDQEAADRESDHDKELEKERETEVDQHYHYLREQEREHHQEYQEWEHEPFGRHDDHQGNPQTDFYSHAYSDRPMLSKALSTYSSKIASPILSYYGAQTLSHHTSIVSNSPSISGAALEYPGGIESPIMITLDLPQVFGSVRASRLADRKTSKNKGNAPAVRESAVDIFKYLVRELELCHVQERNDPKSISVDDRSKSLDDTELKIQLMENIGLSEHNTWATLIRSTTSMDTNDPAGSHTQGHSKLVDMVKLQGSNILSPDNSDMEDDLGDKLDEMGTARLQENVNHLVGLIFLSTHNAETYASVNDLQNFKIWMLIRDSLLNDLKEAADGSTGRRDASGGAANSDKNGIYTTTSTVNHARQDSITSNFSSFEPSDISRSDGEEKLNLGRLSEQNLKATNQNTTAKLDDTRKLASSSSLNSSEPLLLLEGGNQAKEQSIGLSDLKTCLKERYTASNESVLDIEEESSATVAYSSKQANTECSSSIPIRKTEARTSFIDTIMTNLRSPGLSHLDVDNDAIFGKGKTSTSLGSGASKRSSMHSTDSYHKRPYSSPITYSKITTAAQKAKLGLADHDGLPNRGSISFLANIDAAHADKLLLGKLGLASSPDDGKLLPPWDTGRLIQQLYRYSVETGNIILTVCIILLFQTMYKVTSTRIVKSTLAEFITILHRYEMFEISAHLLKNCPWDDILGAGSGQSTVRLFCENCGKLIVNEHSKTILSKRHQAGESNMTNFGYWYCDSCRKPNSLCVYCEQPMKKLALSFLNCGHGGHFECLQQWFLDEGMSECPSGCSGVLL
|
May be involved in a process influencing telomere capping.
|
Q75AV6
|
C6DB84
|
Y1077_PECCP
|
Nucleoid-associated protein PC1_1077
|
Pectobacterium
|
MFGKGGIGNLMKQAQQMQEKMQQMQEEVANLEVTGESGAGLVKITINGAHNCRRVEIDPSLMEDDKEMLEDLIAAAFNDAARRIAETQKEKMAAVSSGMQLPPGFKMPF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
C6DB84
|
A6VR57
|
RS20_ACTSZ
|
30S ribosomal protein S20
|
Actinobacillus
|
MANIKSAKKRAVQSEKRRQHNASQRSMMRTYIKKVYAAVAAGEKSAAQAAFLEMQKVVDRMASKGLIHANKAANHKSKLSAQIKKLA
|
Binds directly to 16S ribosomal RNA.
|
A6VR57
|
Q6G3A4
|
SYP_BARHE
|
Prolyl-tRNA synthetase
|
Bartonella
|
MRLSQYFLPLLKENPKEAEIISHRLMLRAGMIRQQTSGIYSWLPLGKKVLDKICKIIREEQERAGAIEILMPTIQSADLWRESDRYDDYGLEMLRIKDRQKRDLLYGPTNEEMVTDIFRSYIRSYKDLPLNLYHIQWKFRDEIRPRFGVMRSREFLMKDAYSFDLDYEGSKISYNRMFVAYLRTFSCLGLKAIPMRADTGPIGGKLSHEFIILAETGESAIFCDKHFLELTVPDSSIDFSDKAILANIVKQWTSFYAATEEMHDEEEWAKISDNNRLSARGIEVGHIFHFGTKYSAPMGAKVMGQDGKEHLVSMGSYGIGPSRLVAAVIEASHDENGIIWPKSIAPFDFGIINMKPDDEKCTHACETLYKGLRYAGFDPLLDDRNERPGSKFATMDLIGLPTQIIVGPKSVAQNEVEIKDRKTGIKKSLTVENVLNQFSVI
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
|
Q6G3A4
|
O33431
|
RPOC_PORCN
|
Transcriptase subunit beta'
|
Porphyromonas
|
VLRYRGIVCDRCGVEVTEKKVRRERMGHIALEVPVAHIWFFRSIPNKIAYLLGIPSKKLDAIIYYERYAVIQPGTVEGLAAGDLLTEEEYLDILDSLPEGNQDLEDDAPEKFIAKIGAEAIYDLLCRVDLDKLSYELRAKASKDSSQQRKKEALKRLQVVESFRASEGYSRPEWMVMKVIPVIPPELHTLVPLDGGRFATSDLNELCRRVIIRNNRLRRLIEQRAPQVILRNEKRMLQEAVDSFFDNSSKAGAVKSDSNRPLKSLTDSLKGKQGRFRQNLLGKRVDYSGRSVIVVGPEPKMHECGLPKYMAAELYKPFVIRKLLERGIVKTVKSARRIVDKKGPEVWDILEHVIKGHPVLLNRAPTLHRLGIQAFQPKLIEGKAIQLHPLACTAFNADFDGDQMAVHLPLSNEAILEAQMLMLASHNILNPANGAPITVPSQDMVLGLYYITKLRKDAKGAGLVFYGREEATIAYNDGKVAIHAPIKVMVDDVDADGNPIRHLVETSVGRLMFNECVPQGVGYINSILGKKALRDIIGHVIKECGIAKTAKFLDDIKDLGYQMAFKGGLSFNLSDVLIPKEKDTLIQEGFAEVDEIMSNYNMGFITNNERYNQIIDTWTHVNTCLSGILMKQLSEDNEGFNSIFMMMDSGARGSKDQINQLSGIRGLMAKPQKSGTEGRTLLENPILSNFKEGLSVLEYFISTHGARKGLSDTALKTAECGYLTRRLVDVSQDVIVTEEDCGTLRGLVTEEIKEGDVVIASLYERILGRVSVHDVIHPNTGEVIVKAGEEINEKAATIIQDSPITNVEIRSVLTCESKKGVCAKCYGRNLSQGHMVHIGEVVGVVAAQSIGEPGTQLTLRTFHTGGIASNIGSEKYVKAKYDGILEIDELRTVDAKDEEGNAYQVVVGRLAEMRVIDENTRMTLITHHIPYGSKLYFKPGDKVKKDDNIFESDPFNAVIIAEETGKLKFEDVVENVTYKVEYDSNVSAGHKEHIIIESKDKNLSPSVSILNSKGDILRTYNLPVGAHFVKSNGDSVKTGDVLVKIPRSTLKGGDITGGLPRVTELFEARNPTNPAIVAEIDGEVSLGRVRRGNREVTITSKLGEERKYLIPLSKQLLIQENDYVRAGMPLSDGAITPADILAIKGPNAVQDYIVNGVQD
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
O33431
|
Q65ZT0
|
OTCC_BORGP
|
Ornithine carbamoyltransferase, catabolic
|
Borreliella
|
MYNLRNRSFLNLLDFTSKDIRYLLDLSIDLKKSKYAGIEVQKLKGKNMAIIFEKDSTRTRCAFEIAAYDQGANITYLGSRGNQIGVKESMMDTARVLGRMYDAIGFRGFSQQTVECLANYSNVPVYNGLTDTAHPTQILADLMPIEEHKGSLKGVKIVFCGDGRGNVANSLLKGCAIMGLDFRIFAPKELFPDSNLTLKAKSLALDSGGKITITDSKEEAVKCADVVYTDVWVSMGENNWEDRINLLRFYQVNKEIMDMAKDSAIFMHCLPAFHDLNTVVGKDIFDKYGINGIEVTEEIFESKNSVVFDIAENRVHTIKAIVVATLG
|
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
|
Q65ZT0
|
B4T688
|
PAT_SALNS
|
Putrescine--2-oxoglutaric acid transaminase
|
Salmonella
|
MNRLPSSASALACSAHALNLIEKRTLNHEEMKALNREVIDYFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGSLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRRPFMPLLPGFRHVPFGNIDAMSMAFSEGKKTGDEIAAVILEPIQGEGGVILPPQGYLTEVRKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVMPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLPAQAEQKGDTLLDGFRQLAREYPNLVHDARGKGMLMAIEFVDNETGYRFASEMFRQRVLVAGTLNNAKTIRIEPPLTLTIELCEQVLKSARNALAAMQVSVEEV
|
Catalyzes the aminotransferase reaction from putrescine to 2-oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal. Also functions as a cadaverine transaminase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate.
|
B4T688
|
A4J102
|
RL7_DESRM
|
50S ribosomal protein L7/L12
|
Desulforamulus
|
MSKVAEVLEIVKGLTVLELAELVKAFEEEFGVSAAAPVAVAAAPAAGAAAAEEEKTEFDVILTSAGDKKINVIKVVREITGLGLKEAKELVDGAPKPVKEKIAKEEAESIKAKLTEAGATVDVK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
A4J102
|
Subsets and Splits
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