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2.75k
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5.51k
AlphaFoldDB
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Q6R6M4
U17L2_HUMAN
Ubiquitin-specific-processing protease 17-like protein 2
Homo
MEDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSSEARVDLCDDLAPVARQLAPRKKLPLSSRRPAAVGAGLQNMGNTCYENASLQCLTYTPPLANYMLSREHSQTCQRPKCCMLCTMQAHITWALHSPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKLAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHDGHYFSYVKAQEGQWYKMDDAKVTACSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDERLVERATQESTLDHWKFPQEQNKTKPEFNVRKVEGTLPPNVLVIHQSKYKCGMKNHHPEQQSSLLNLSSTTRTDQESVNTGTLASLQGRTRRSKGKNKHSKRALLVCQ
Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Regulates cell proliferation by deubiquitinating and inhibiting RCE1 thereby controlling the small GTPases NRAS and HRAS localization and activation. In parallel, mediates deubiquitination of CDC25A, preventing CDC25A degradation by the proteasome during the G1/S and G2/M phases promoting cell-cycle progression. Also regulates cell proliferation and apoptosis through deubiquitination of SUDS3 a regulator of histone deacetylation. Through activation of the Rho family GTPases RAC1A, CDC42 and RHOA, regulates cell migration. Through the cleavage of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains of the cytoplasmic innate immune receptors DDX58 and IFIH1 stimulates the cellular response to viral infection.
Q6R6M4
Q01726
MSHR_HUMAN
null
Homo
MAVQGSQRRLLGSLNSTPTAIPQLGLAANQTGARCLEVSISDGLFLSLGLVSLVENALVVATIAKNRNLHSPMYCFICCLALSDLLVSGSNVLETAVILLLEAGALVARAAVLQQLDNVIDVITCSSMLSSLCFLGAIAVDRYISIFYALRYHSIVTLPRARRAVAAIWVASVVFSTLFIAYYDHVAVLLCLVVFFLAMLVLMAVLYVHMLARACQHAQGIARLHKRQRPVHQGFGLKGAVTLTILLGIFFLCWGPFFLHLTLIVLCPEHPTCGCIFKNFNLFLALIICNAIIDPLIYAFHSQELRRTLKEVLTCSW
Receptor for MSH (alpha, beta and gamma) and ACTH . The activity of this receptor is mediated by G proteins which activate adenylate cyclase . Mediates melanogenesis, the production of eumelanin (black/brown) and phaeomelanin (red/yellow), via regulation of cAMP signaling in melanocytes .
Q01726
A2BY12
MIAB_PROM5
tRNA-i(6)A37 methylthiotransferase
Prochlorococcus
MLTKTIQEEKKTPKDESIGSYWITTFGCQMNKADSERMAGTLEKMGYSRAIDELKADLVLYNTCTIRDSAQQKVYSFLGRQIKRKHSLPKLKLVVAGCLAQQEGESLLRRVPELDLIMGPQHVNNLENLLERVDSGNQVVATEETFISEDITNARRDSTICGWVNIIYGCNERCSYCVVPSVRGKEQSRYPKAIKSEIQTLAQNNYKEITLLGQNIDAYGRDLPVTTKEGRKENTLTDLLYFIHDVDGIRRIRFSTSHPKYFSKRLIKACYELDKVCEHFHIPFQSGNDEILRLMARGYTIDKYKKIIENIRSLMPNASITADAIVAFPGETEKQYQDTLRLISDVGFDQVMTAAYSPRPNTPAAIWNNQIAEEVKKERLKEINELVEATSRKRNQRYLNNTESVLIEGLNPKNSMQMMGRTRTNRLTFVEIPENIEFNYSFGDELNVKITEARSFSLSGQIYK
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
A2BY12
A0KKI5
RSMF_AERHH
rRNA (cytosine-C(5)-)-methyltransferase RsmF
Aeromonas
MHDNTYLPDHFLRHIAAIMPAHLSMDEFVASCRRPLRRSIRVNTLKISVAAFVARMQPLGWQLDPVPWCDTGFWLSREDESVPLGNTAEHLSGLFYIQEASSMLPVTALFACEQTRRDGMLLDAAAAPGSKTTQIAALMNNQGMLVANEYSSSRLKVLSANLQRCGVTNVGMTHFDAKVFGQWLPETFDAILLDAPCSGEGSVRKDEDALRNWSIESIDEIAAVQQGLLESAFHALKPGGVLVYSTCTLSLQENQAVCQSLLDKFGAAFSFDSLADLFPAAEQACTPEGYLHVWPQIFDSEGFFVARLRKHYSVPNTMFKPGKLGKFPFLPLPAKESEPMLREIEAAFGVVPQGNLFGRSEEIWLFPQRFEQVQGKLRFDRIGLKLAETFKKGYRLTHEWALAYGDGASKGFVELGIADAREFMMGRDVWPEQAAGTGEVIVRYQGHTLGMGKWVGSRVKNALPRELVRDNNLFV
Specifically methylates the cytosine at position 1407 (m5C1407) of 16S rRNA.
A0KKI5
A0PYX5
DEOC_CLONN
Phosphodeoxyriboaldolase
Clostridium
MNLNKYIDHTLLKPQATEEDIKKICKEAKEYNFASVCVNTCYTSLVSKELEGTDVTTCVVVGFPLGATTTETKAFEAKQAIEQGAGEVDMVINVGALKSKKYDYVKKDIEAVVEAAKGKALVKVILENCLLEKEEIVKACELSKEAGADFVKTSTGFSTGGAKVEDVKLMRETVGPDMGVKASGAVRTKEDAEAVIAAGANRIGASSSIAIVEGTKSENAGY
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
A0PYX5
B9KFM1
PNP_CAMLR
Polynucleotide phosphorylase
Campylobacter
MRHKININNHIEIFDTDKVAKQAAGAVLMQEKNAVVLATVAREEKMVEEDFLPLTVQYIEKAYAAGKIPGGYVKRETKPGDSETLSARIIDRSLRPLFPKGYAYPTQIVVMVLSADPEVDLQVMSLNAASVALYLSDIPIKAPVCGVRIGRINNEFVLNPSNSELKNSTLDLYVAGVKDELLMIEMRALSNKKDNQHCMNELSEDDTLKALDFASSAILRGSNEYEKAFAAYRKNSKLEFKIESDNIQIIDYIKNTYITKLKIAINQMAKSERASEILQIAKEIESESMAIENEWKFEDIEKALHVCKRELVRNQIINENKRADGRGLKDVRKIDIETNILPSAHGSCLFTRGQTQALVVATLGNDNDAQMSDMLTEKNPICEKFMVNYNFPGFSVGEASPIKAPGRRELGHGNLAKRALYPSVDADYIHTIRLVSEILESNGSSSMATVCGGALALRAAGVKSEKLVAGVAMGLVFEEEKYAILTDIMGLEDHDGDMDFKVAGSHDGITALQMDIKLGGIEQKVLQEALYQAKEARGYILNLMQEACEKIIVNEAILPKVEIFNVDPNKIPDIIGQGGKTIKDIIEKFEVNIDLDRDKGEVKIAGIDHNLISQSKEYILNLLHSKGSNKRRDKKEMPKFDIGEEFLGRVQKVVEFGVFVELKEGVDGLLHNSKIKEKLEVGHEIKVKVAEIKNGKVSLDLA
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
B9KFM1
B7IHU7
RL4_THEAB
50S ribosomal protein L4
Thermosipho
MAKVSLFNSKGENIGPIDLKDEVFAIEPNFDVIWRYVDMQLTNARAGTASTKTRGEVSGGGRKPWIQKHTGRARQGSIRAPHWRHGGVAHGPKPRVYFKRLNKKMKRLALKSALSLRLKEGNLIVVDEIKFKRPKTKDLREVLKNLGLENQKVLVVLPKKVEEYVNVKISGRNIPGVKVIIADNPGVDRTNIDGLNVYDILNHDKLVLLQGTVQKIEEVLG
Forms part of the polypeptide exit tunnel.
B7IHU7
P10463
CAYP1_CANLF
Thyroid protein p24
Canis
MDAVDATVEKLRAQCLSRGALGIQGLARFFRRLDRDRSRSLDSRELQRGLAELGLVLDTAEAEGVCRRWDRDGSGTLDLEEFLRALRPPMSQAREAVIAAAFAKLDRSGDGVVTVDDLRGVYSGRTHPKVQSGEWTEEEVLRRFLDNFDSSEKDGQVTLAEFQDYYSGVSASMDTDEEFVAMMTSAWQL
Calcium-binding protein. May play a role in cellular signaling events (Potential).
P10463
Q977Z9
RFCS_THEVO
Clamp loader small subunit
Thermoplasma
MIEIWTEKYRPKSLSEIYGEDENIQKLKSFVEKKELPHLLFAGSVGTGKTSTAIALAIELFGESWKENFIEMNASNENGIDVIRNKIKDIARIRPSNPLGFKILFLDEADQLTAEAQAALRRTMEMYSETTRFVFACNYSSKIIPPIQSRTVVMRFRPVQDEFIKKKLNEIAKNEGFTIDDESMEAMVEVSGGDMRKAINVLQAVYTSGEISPKKIYEIIGYASPESVNKLISRAINGLFDEARQIVDKMMIEDGLSGIDIVKSVHSIVRASVVPPKQKIEIIKALADAEFRIVEGSNDRIQLDALIARIADIGSKIN
Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA.
Q977Z9
A5W9R5
RL9_PSEP1
50S ribosomal protein L9
Pseudomonas
MELILLEKVANLGNLGDKVKVKAGYGRNFLLPFGKATVANAANLAAFEERRAELEKAAADKKASAESRAAQLAELEVTITATAGDEGKLFGSIGTHDIADALTASGVEVAKAEVRLPNGTIRQVGEYDVAVHLHSDVEATVRVVVVAA
Binds to the 23S rRNA.
A5W9R5
B5ECF3
PURA_CITBB
IMP--aspartate ligase
Citrifermentans
MANVVVIGAQWGDEGKGKVVDIYTEFADNVVRYQGGNNAGHTLVVGDEKVILHLIPSGILHEGKRCVIGNGVVLDPEVFIMEITKLKANGYLKDDKMLLLSEALHIIMPYHKRIDIAREKKSGSKKIGTTGRGIGPAYEDKIGRRGIRLMDLLDEKAFTRKVKEVLEEKNLILTQLLGDQPFTFEEIYEEYMKYAETLRKYAADTSLILHQETKAGKSLLFEGAQGTLLDVDHGTYPYVTSSSTCSGGACTGSGVSPREIHEVIGISKAYATRVGSGPFPTELEDETGEQLRQAGREFGSTTGRPRRTGWYDALVARYAVRVNGLSGIAITKLDVLSGQETVKVCTAYNYKGQVLTEVPASLEIMEQCTPIYEELPGWNDDITGAKSMAELPKNARDYVARIEKLSGAPVVLVSVGPRRDETIVLRNPFELN
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
B5ECF3
C6DFY7
IF3_PECCP
Translation initiation factor IF-3
Pectobacterium
MKGGKRVQPARPNRINREIRAHEVRLTGVEGEQLGIVSLNEALEKAEEAGVDLVEISPNAEPPVCRIMDYGKFLYEKSKATKEQKKKQKVIQVKEIKFRPGTDDGDYQVKLRNLIRFLEDGDKAKITLRFRGREMAHQQIGIEVLNRVRDDLSELAVVESFPTKIEGRQMIMVLAPKKKQ
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
C6DFY7
A6V1P7
ALGL_PSEA7
Poly(beta-D-mannuronate) lyase
Pseudomonas
MKTSHLIRITLPGALAAALLASQVSQAADLVPPPGYYAAVGERKGSAGSCPSVPPPYTGSLVFTSKYEGSDSARATLNAKAEKAFRSQIKDITDMERGATKLVTQYMRSGRDGDLVCALNWMSAWARAGALQSDDFNHTGKSMRKWALGSLSGAYMRLKFSSSRPLSAHAGQSREIEDWFARLGTQVVRDWSNLPLKKINNHSYWAAWSVMSTAVVTNRRDLFDWAVSEFKVAANQVDEQGFLPNELKRRQRALAYHNYALPPLAMIAAFAQVNGVDLRQENHGALQRLAERVMNGVDDEETFEEKTGEDQDMTDLKVDNKYAWLEPYCALYRCAPKMLEAKKDREPFNSFRLGGEVTRVFSREGGS
Catalyzes the depolymerization of alginate by cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues via a beta-elimination mechanism. May serve to degrade mislocalized alginate that is trapped in the periplasmic space.
A6V1P7
Q8TJS1
IXTPA_METAC
Nucleoside-triphosphate pyrophosphatase
Methanosarcina
MHKIVFVTGNKGKFAEIRDILKTFGIEVIQEKNGYPELQEDELEPIAAHGAQYVANKLNMPVMVDDSGIFINALNGFPGPYSRFVEDKLGNLKVLKMMEGEEDRTAYFKTVIGYCEPGKEPLVFPGVVEGKIAYEERGTGGFGYDPIFEYQGLTFGELGDTEKNKVSHRRRAVDEFLEWFTSKA
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Q8TJS1
Q62885
U119A_RAT
Retinal protein 4
Rattus
MKVKKGGGGTGPGAEPVPGASNRSVEPTREPGAEAESGSESEPEPGPGPRLGPLQGKQPIGPEDVLGLQRITGDYLCSPEENIYKIDFVRFKIRDMDSGTVLFEIKKPPVSERLPINRRDLDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIERHYFRNQLLKSFDFHFGFCIPSSKNTCEHIYDFPPLSEELISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSGTP
Involved in synaptic functions in photoreceptor cells, the signal transduction in immune cells as a Src family kinase activator, endosome recycling, the uptake of bacteria and endocytosis, protein trafficking in sensory neurons and as lipid-binding chaperone with specificity for a diverse subset of myristoylated proteins. Specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated GNAT1 and is required for G-protein localization and trafficking in sensory neurons. Probably plays a role in trafficking proteins in photoreceptor cells. Plays important roles in mediating Src family kinase signals for the completion of cytokinesis via RAB11A.
Q62885
P29745
PEPT_ECOLI
Tripeptide aminopeptidase
Escherichia
MDKLLERFLNYVSLDTQSKAGVRQVPSTEGQWKLLHLLKEQLEEMGLINVTLSEKGTLMATLPANVPGDIPAIGFISHVDTSPDCSGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIMTALAVLQQKKIPHGDIRVAFTPDEEVGKGAKHFDVDAFDARWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNALSLAARIHAEVPADESPEMTEGYEGFYHLASMKGTVERADMHYIIRDFDRKQFEARKRKMMEIAKKVGKGLHPDCYIELVIEDSYYNMREKVVEHPHILDIAQQAMRDCDIEPELKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVQVIVRIAELTAQRK
Cleaves the N-terminal amino acid of tripeptides.
P29745
Q6D178
RLMD_PECAS
23S rRNA(m5U1939)-methyltransferase
Pectobacterium
MAQFYSPNRRVTTRKAVPAKNLTVTVASLDPFGQGVARHEGKTVFVTGVLPGEQAEVQLTEEKRQFSHAKLKRLLTPSPQRVEPPCPHFTRCGGCQQQHAEITLQQSSKTAALMRMMTRETGIELSAASLIAGTPYAYRRRARLALYFQAKEQRLLMGYRQSNSHDLVDIKACPVLRPELEALLQPLRDCLSQLSAVKRLGHVELVQAENGPLLVLRHLDPLHPADEQALRDFAQRQGVSVYLAPDAESLTCLHGEEPVYHVAGLTLAFSPRDFIQVNDAVNQQMVAQALAWLDVQSQDRILDLFCGMGNFTLPLAQRAASVVGVEGVTALVEKGRENARRNALSNVTFFHQNLEDDVTQQPWAAQGFDKILLDPARAGAAGVMEQITRLAPKRVVYVSCNATTLARDSKVLLAAGYRLANVAMLDMFPHTGHLESMALFLHDTGMRKAQ
Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Q6D178
P46170
DFB12_BOVIN
BNDB-12
Bos
GPLSCGRNGGVCIPIRCPVPMRQIGTCFGRPVKCCRSW
Has bactericidal activity. Active against E.coli ML35 and S.aureus 502A.
P46170
Q7PND3
UFC1_ANOGA
Ufm1-conjugating enzyme 1
Anopheles
MVDDGTRKALSGIPLLKTKAGPRDKELWVQRLKEEYQALIKYVQNNKASDMDWFRLESNKEGTKWFGKCWYMYNLHKYEFDVEFDIPITYPTTSPEIALPELDGKTAKMYRGGKICLTDHFKPLWARNVPKFGIAHAMALGLAPWLAVEVPDLIEKGVISYQEKGSS
E2-like enzyme which forms an intermediate with UFM1 via a thioester linkage.
Q7PND3
Q8E5C3
RF1_STRA3
Peptide chain release factor 1
Streptococcus
MNIYDQLQAVEDRYEELGELLSDPDVVSDTKRFMELSREEANTRETVTAYREYKQVIQNISDAEEMIKDASGDAELEEMAKEELKESKAAKEEYEERLKILLLPKDPNDDKNIILEIRGAAGGDEAALFAGDLLTMYQKYAETQGWRFEVMESSVNGVGGIKEVVAMVSGQSVYSKLKYESGAHRVQRVPVTESQGRVHTSTATVLVMPEVEEVEYEIDQKDLRVDIYHASGAGGQNVNKVATAVRMVHIPTGIKVEMQEERTQQKNRDKAMKIIRARVADHFAQIAQDEQDAERKSTVGTGDRSERIRTYNFPQNRVTDHRIGLTLQKLDTILSGKMDEVIDALVMYDQTQKLEALNK
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Q8E5C3
Q3J436
GLO2_CERS4
Glyoxalase II
Cereibacter
MPLELVTVPCLSDNYAFLVHDAGTGETSVVDVPEAGPILKALEERGWHLSQILLTHHHSDHVAGVEELRAATGARVAGAAADAHRLPPLDLELAEGDLVRVGASEGRVIEVPGHTVGHIAFHFPDSSLAFTGDSLMAMGCGRLFEGTAEAMWQSLRKLSALPPETMICSGHEYAASNARFAATLEPDSPMLIFRVGSIAAARKEGRPTVPSHLSDEIATNPFLRAGEASLKAAVGMVDAEDAEVFAEIRRRKDKF
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Q3J436
B8NG97
NAGS_ASPFN
N-acetylglutamate synthase
Aspergillus subgen. Circumdati
MSSRALTWPRTAKSSLLKQQTSSFVGQPKLGTPNCRSFSSTADRPINQSAEFSSSSKSYDRLGRRAKEKLLDREFFLSLLNSASTKREAKSYLARLKAQHPPKAQTEPTTGHSKGTVTQSLPSGVNLGSFYGASRSVYDSPVFRHDSTPLPPPSELPEERLHLALIKIRTPQLLDDTIINGVAKTLSQLSRLGMACCVVVDPGTAGNANTLRRVAAEQAERISIAVDAQPDSKSAHLDSVLSLSPMFPELPTVLSRKALLNPLRDGQIVVVAPIAYTEDVPKAVTISANDAILALTKELAGLAMRPDPDEDPWLTAQKIAKLQKEVSLDRVILLDPLGGIPSFRGPQTSHVFINMEQEFDDIKNELLHVQSSEACTATTPKGGNTFVEDPLERHLDNLQLSQNVLAMLPSASSGIITSPLEVSNSARTPQANPSDVSAVGTRRQRNPLIHNLLTDKPLLSSSLPMSRREAMNRRRGSINTPSSHTTFVKRGMPLTMIPNPRVEVWTAQNRPRLSLDDPSIDLPRLVQLIEDSFNRKLDVQDYLNRVNDRLAGLIIAGEYEGGAILTWELPPGVEDDGSPASEARMVPYLDKFAVLKRSQGAGGVADIVFNAMVRSCFPNGVCWRSRKDNPVNKWYFERSTGTWKLSDTNWTMFWTTPGLTENSQRFSDYEQVCRSIQPSWADDTGVVD
N-acetylglutamate synthase involved in arginine biosynthesis.
B8NG97
B7V3N3
HIS6_PSEA8
ImGP synthase subunit HisF
Pseudomonas
MALAKRIIPCLDVDNGRVVKGVKFENIRDAGDPVEIARRYDEQGADEITFLDITASVDGRDTTLHTVERMASQVFIPLTVGGGVRSVQDIRNLLNAGADKVSINTAAVFNPEFVGEAADRFGSQCIVVAIDAKKVSAPGEAPRWEIFTHGGRKPTGLDAVLWAKKMEDLGAGEILLTSMDQDGVKSGYDLGVTRAISEAVNVPVIASGGVGNLEHLAAGILEGKADAVLAASIFHFGEYTVPEAKAYLASRGIVVR
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.
B7V3N3
Q7TYX4
QCRA_MYCBO
Ubiquinol--cytochrome c reductase iron-sulfur subunit
Mycobacterium tuberculosis complex
MSRADDDAVGVPPTCGGRSDEEERRIVPGPNPQDGAKDGAKATAVPREPDEAALAAMSNQELLALGGKLDGVRIAYKEPRWPVEGTKAEKRAERSVAVWLLLGGVFGLALLLIFLFWPWEFKAADGESDFIYSLTTPLYGLTFGLSILSIAIGAVLYQKRFIPEEISIQERHDGASREIDRKTVVANLTDAFEGSTIRRRKLIGLSFGVGMGAFGLGTLVAFAGGLIKNPWKPVVPTAEGKKAVLWTSGWTPRYQGETIYLARATGTEDGPPFIKMRPEDIDAGGMETVFPWRESDGDGTTVESHHKLQEIAMGIRNPVMLIRIKPSDLGRVVKRKGQESFNFGEFFAFTKVCSHLGCPSSLYEQQSYRILCPCHQSQFDALHFAKPIFGPAARALAQLPITIDTDGYLVANGDFVEPVGPAFWERTTT
Iron-sulfur subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis.
Q7TYX4
Q6N5U5
QUEF_RHOPA
PreQ(0) reductase
Rhodopseudomonas
MSKTPRKSAPSPSLQLGQAVEWPDRPEAAKLDRVPNPQKDTNFLARFTAPEFTSLCPVTGQPDFAHLVIDYVPGPWLLESKSLKLYLASFRNHGAFHEDCTVAIGKRIATEIKPKWLRIGGYWYPRGGIPIDVFWQTGKLPKDVWVPDQGVQPYRGRG
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Q6N5U5
Q0W720
SYI_METAR
Isoleucyl-tRNA synthetase
Methanocella
MIQEEKEQYSSKSLEAGVDELWRASDAYALTRKKRLGSKRFFFVDGPPYTTGRIHLGTAWNKIIKDSVLRYRSMNGYDLIDRPGWDMHGLPIEVKVESILGFKTKKDIEEFGVARFTEECKKFAIGNMHEMTSQFKKLGVWMNWDDPYMTLKNEYIEAAWWTIKQAHEKHLLERGLRNVNWCPRCETAIADSEVEYADRKDDSIYVKFPLKNEEGFLVIWTTTPWTIPANMAVAANKDFTYAMVYALPAAVLEEAAMQAGLDHTTLVEHHSDGRPKPMRYSDKVAKMKEAIGEEKVKELYEKHGEKLIIARDLVDGVLKMGRYADYQVLKTMTGEELKGTEYVHPLADLIPCQKETEHKVYLADFVVGENTGMVHIAPGHGFDDFELGLKEGIRAYCPVKANGHYDDSVGAYAGMEIREANPKIMEDLRQRNLLLGATTIEHRYGHCWRCKTPIIFLTTDQWFIAVSKMKEDMLAEVKRVNWYPDWAGSARFYDWVNGARDWCVSRQRYWGIPIPIWKCEKCGSLDVIGTKEELERKVGREVPDLHRPFVDEVRLECECGGSMRRVEDIFDVWFDSAVASWATLHFPGRKDLMDWWPADFIVEGHDQTRGWFYSQLGAGMVGFGKAPYNGVCMHGFTLDETGKKMSKSLGNVVAPEDVVEKLGADTLRLYVLSQNAPWEDLSFSWEECGNINRAINIFWNVYRFPLPYMVLDKFDPAKVTLESVKGSLRVEDRWILSKLQAVIKDVDTYMATYELHRATRSIISFILEDLSRWYVQLARERTWVEADDPDKLAAYRVLYDTLVTTVKLIAPFTPYIAERMYQNLVRNVSAEAPVSVHMCDWPVVDSSLLDEQLNRDMDIARKIVEASSNARQKAKRKLRWPVQKIVVAAENPDVVTAVKDLSGVIGEQTNSKEVVVLAPGEANTELGVEVVPNPKLIGPIFKAVAGKVTAALKEADGRAVKKAIEEEKKYIVEIPEGSFDILLDMVSFRDVIPESLAMADFPGGKVYVDVTLSKELEAEGYTRELIRRIQDMRKEMNLNVEDRIKVEVYVGDEKVLDLVKSMKDYAAGEVRADTLDLKTEKPAAGFVKDWDVEGIPMTIGLEKI
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
Q0W720
P09567
GLUC_TORMA
Glucagon
Torpedo
HSEGTFTSDYSKYLDNRRAKDFVQWLMNT
Promotes hydrolysis of glycogen and lipids, and raises the blood sugar level.
P09567
Q3YVY1
TDH_SHISS
L-threonine 3-dehydrogenase
Shigella
MKALSKLKAEEGIWMTDVPVPELGHNDLLIKIRKTAICGTDVHIYNWDEWSQKTIPVPMVVGHEYVGEVVGIGQEVKGFKIGDRVSGEGHITCGHCRNCRGGRTHLCRNTIGVGVNRPGCFAEYLVIPAFNAFKIPDNISDDLASIFDPFGNAVHTALSFDLVGEDVLVSGAGPIGIMAAAVAKHVGARNVVITDVNEYRLELARKMGITRAVNVAKENLNDVMAELGMAEGFDIGLEMSGAPPAFRTMLDTMNHGGRIAMLGIPPSDMSIDWTKVIFKGLFIKGIYGREMFETWYKMAALIQSGLDLSPIITHRFSIDDFQKGFDAMRSGQSGKVILSWD
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
Q3YVY1
A5VEV8
ATPF_RHIWR
F-type ATPase subunit b
Rhizorhabdus
MSVNASTLVADNLADAASLEGLPENVSAGHAAAGTEEHHVDPTALGMTATAWVSLAMVIVILLLLWKKVPSVIGASLDKKIASIRANLDEAAALRADAEKLKAEYEAKAKAAAKEAEEMLAHARSEAEAIVSQARVDATALIERRGKMAEDKIAAAERGAVAEVRAKAASAAAAAAGALIAERNNAKADKALIDGAIDALGNARF
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
A5VEV8
Q10585
SPD1_SCHPO
Protein p14
Schizosaccharomyces
MHSSKRVMTTKTHVEQPESSMRPQLPESIQGSLMDVGMRVRKSISTGYKSKQTTFPAYNPPLYNTVSENIALKNTAFSYEPNGTKRPFEQAIPNYNWANPPQDFEEPEWLKPFDVVMEGTNERL
Regulates the ribonucleotide reductase activity through its mediation of the nuclear localization of suc22, the small subunit of the ribonucleotide reductase. Delays the progression of the G1-S phase transition, thereby ensuring the G1 phase is complete. Interacts with both p34 and the p34-p56 complex, although no direct inhibitory effect on the bound proteins has been demonstrated. The action of p14 may happen coincidentally with the cdc10 function or may happen downstream of this.
Q10585
C6BYG5
MURC_MARSD
UDP-N-acetylmuramoyl-L-alanine synthetase
Maridesulfovibrio
MRSRVGNIHMIGIGGSGMSGIAEVLINMGFTVTGSDLAAGAPVKRLLKMGAQVFIGHGADNVNDADVVVKSTAISDDNPELVKARELGIPIIPRAEMLAELMRLRTGIAVAGTHGKTTTTSLLATIFTEAELDPTVIIGGRLNTFGSNARLGDGQFLIAEADESDGSFLCLAPIITVVTNVDKDHLDFYGGQEAIDESFRKFMNSIPFYGMNVVCGDDPGVQRLLPSIKRPCMTYGLNKGNRLRGEILSCEVRSLFKVYLDEKLLGEVSLAQPGKHNVLNALGAIGVSLEAGLDPKVILSGLSNFMGVGRRFEKKGESKGILVVDDYGHHPAEIQATIETAKSCFPQRRLVVAFQPHRFTRTEALFGEFCKTFEKADELLLTEIYPASEDPIPGVNGMSLAQGIRQVSDTKVRFYPDFEMMQNELPNILKPGDLFITQGAGSIYTVGEKFLKYLEEDGEKVLKPEEITAL
Cell wall formation.
C6BYG5
Q0AZ31
COAD_SYNWW
Pantetheine-phosphate adenylyltransferase
Syntrophomonas
MKLAVYPGSFDPVTNGHIDILEKSSKIFDEIIVAVIHNVTKKALFSLDERVKLIEESTRHLNNVRVDAFSGLLANYLADKQACAIIRGLRTVTDFEYEMHMAMMNKKLIPNIDTMFFMSDSQYTFISSSAVKEAALLGGDVGSLVPAVVKAGLEEKMLNDG
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Q0AZ31
P19039
EF1A_APIME
Elongation factor 1-alpha
Apis
MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGIGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDMTDPPYSEARFEEIKKEVSSYIKKIGYNTASVAFVPISGWHGDNMLEPSPKTPWYKGWKVERKDGNADGKTLIEALDAILPPSRPTDKALRLPLQDVYKIGGIGTVPVGRVETGILKPGMLVTFAPAALTTEVKSVEMHHEALTEALPGDNVGFNVKNISVKELRRGYVAGDSKNQPPRGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEENPKSIKSGDAAIVMLQPTKPMCVEAFQEFPPLGRFAVRDMRQTVAVGVIKSVTFKDTQGKVTKAAEKAQKKK
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
P19039
Q5A6N1
LONM_CANAL
Lon protease homolog, mitochondrial
Candida
MIKASKCNKPRALFLVRVSIPRTFIRNATSAVPTTIKLNDLASLPPITKSLPTNLPFLMPDTLQSLLRFDSEKEKQPSTDKSNDKDKPSRKEKGKDKEKENEEKKDINMDEKYEINEETDTKPTIDPNNPVSSKSNISSSSGGDNNNNNNNNNNNNDSDGKNDDGSPKDKEFLSPSDSGLHPPFLAIAMKDRPFLPGATRHLHVSDPEVIKCVNHMINSNIKSPYFVLFHVRDTNSEDAALDVIKDRDFVHEVGTLCQIIKTTGSEILVYPHYRVKLVDISTPNSRSESIEKEQDNSQTSYLKKFEVSYAVTQQLKDEPYDEQSITINAWTRRIKELYEKLAPKYDQPENKEEIMSNPSMLADFIASKVHAKPEQIQEILESSNVETKLELSLQLLQVEADADEMRQTALKNIRERTEKAYAQSLIKEYTKELLKAAGIGENSKVHKFDERIKHLKMPEEAMKAYKTEKERLGTQSDMEQNVVERYLDWLTQIPFGVYTKDSFNVKKAREILDRDHYGLKDVKDRILEFISVGKISGNVDGKILCLAGPPGTGKTSIAKSIAEALNRKYTRIAVGGVQDVHDVKGHRRTYVASIPGRIVTALTQAKTSNPLMLIDEIDKLDTTSHGGAARAFLEILDPEQNNSFVDNFIEVKVDLSKVLFVCTANYLGSIPGPLRDRMEIIEVNGYTKNDKIEITKRHLIPAAAKKVGLDEGRVVIPDETISRLIDKYCRESGLRHIKSLINRIFSKASRKIVEELEETDVDSHNKDTVEGTLVAKESEKVISDKAKIDTENSPIEYIQSNTEVKAETTTESQQEQEKEKEKDEEIKKLDLPADLKIEVKPETLKDFVGPEIYIKDRLYETLNPGVATGLAYNTSGDGDALYIESILTDSISSDLGNAGLHVTGSLKDVMKESASIAYSFAKQFMVRQFPDNRFFEAAHIHVHCPGGAIPKDGPSAGIAFTSSLVSLALNKSLPNDTAMTGEITLTGKVLAIGGLREKSLGAKRAGYTKIIFPKDCEYQLDEIPDEVKEGLTYIPVEWYSEVFEHLFQGISKEEGNSVWKEEFAKLEDKKKSKKTNTK
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Q5A6N1
Q5HWH4
PANC_CAMJR
Pantoate-activating enzyme
Campylobacter
MEVITSIKEAKQTVKNWKSHNLSIGYVPTMGFLHDGHLSLVKNAKTQDKVIVSIFVNPMQFGPNEDFSSYPRDLERDIKMCQDNGVDMVFIPDAAQMYLKNFSTYVDMNTITDKLCGAKRLGHFRGVCTVLAKFFNILNPDIVYMGQKDAQQCVVVRHMVDDLNFDLKIQICPIIREEDGLAKSSRNVYLSEEERKASLAISQSIFLAEKLVQEGEKDTSKIIQAMKDILEKEKLIKIDYIELVDFNTMENIKNIADNVLGAVAAFVGKTRLIDNFLVQGLK
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Q5HWH4
A4FNI7
SECA_SACEN
Protein translocase subunit SecA
Saccharopolyspora
MVLSRLLRAGEGKLLKRLRRIAAHINELEDDVLALSDAELRAKTDEFKRRHTDGESLDELLPEAFAVAREGARRTLGQRHFDVQLMGGAALHLGQIAEMKTGEGKTLTCVLPAYLNAIAGRGVHVVTVNDYLAKRDADWMGRVHRFLGLEVGAIMADMTPEQRRHAYAADITYGTNNEFGFDYLRDNMAWSLADCVQRGHFFSIVDEVDSILIDEARTPLIISGPADQSSRWYQEFARLAPMLKKDQHYEVDERKRTVGVTEDGVTIIEDQLGIENLYEAANTPLVGYLNNALKAKELYKRDKDYIVRNGEVVIVDEFTGRILHGRRYNEGMHQAIEAKEGVEIKAENQTLATITLQNYFRLYEKLAGMTGTAETEAAEFNGTYKLGVVPIPTNRPMARADQPDLVYKSEVAKFEAVAEDIEEKHRKGQPVLVGTTSVERSEYLAKLLVKKGVPHNVLNAKYHQSEAAIIAEAGRKGAVTVATNMAGRGTDIVLGGNVDHLADAELRKRGLDPVDNREEYEAQWPAVVEKIKEQVEAEAEEVRELGGLYVLGTERHESRRIDNQLRGRSGRQGDPGESRFYLSLGDELMRRFNAAMVETVMTRLKVPDDVPIEHKMVTRAIRSAQTQVEQQNMEIRKNVLKYDEVMNQQRSVIYDERRRVLEGEDLQEQVRHMIRDVVTEYVNAATADGYAEDWDFEKLWSALKTLYPVSVSWEALVDSDEDLSKERLLEEVLADAEAAYAKREAEVDGKVGPGAMRELERRVVLSVLDRKWREHLYEMDYLKEGIGLRAMAQRDPLVEYRREGFDMFHAMLDALKEESVGFLFNVQVEAAEPEPAPEQPSVPVSVSRSAEPTPDLQAAAEAAAAQSQVRRAKPTSAGPALSQLPGSTTQAPSALRGKGLDAPEKQRLNYSGPTEQGGVQTTSESAGEQGNGTSTRRERRAAARAEAKKNKRR
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.
A4FNI7
P92481
COX3_EQUAS
Cytochrome c oxidase polypeptide III
Equus
MTHQTHAYHMVNPSPWPLTGALSALLMTSGLAMWFHFNSTLLLALGLLTNILTMYQWWRDIIRESTFQGHHTSIVQKGLRYGMILFIISEVFFFSGFFWAFYHSSLAPTPELGGCWPPTGIHPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKNMLQGLFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGFHGLHVIIGSTFLIVCFLRQLKFHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
P92481
Q40302
CALM_MACPY
Calmodulin
Macrocystis
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIIEAFKVFDKDGNGFISAAELRHIMTNLGEKLTDEEVDEMIREADIDGDGQINYEEFVKMMMAK
Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Q40302
Q0K4N8
FLHD_CUPNH
Flagellar transcriptional regulator FlhD
Cupriavidus
MESSEVLQEIREVNLAYLLLAQRLVRENQVEAMFRLGVSKEIADILAKLTSAQLVKLAASNMVLCRFRFDDHALLSTLTHTAKSHDMQQIHAAILLARQPVESLN
Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways.
Q0K4N8
P44872
FTSX_HAEIN
Cell division protein FtsX
Haemophilus
MSRSTDASVFVQTAYTLRAVWADLWQRKFGTLLTILVIAVSLTIPTVSYLMWKNLHLATTQFYPESELTIYLHKNLSEENANLVVEKIRQQKGVESLNYVSRQESLKEFKSWSGFGEELEILDDNPLPAVVIVKPTSEFNVSEKRDELRTNLNKIKGVQEVRLDNDWMEKLTALSWLIAHVAIFCTVLMTIAVFLVIGNSIRSDVYSSRSSIDVMKLLGATDQFILRPYLYTGMIYALLGGLVAAIFSSFIISYFTSAVKYVTDIFAVQFSLNGLGVGEFVFLLVCCLIMGYVGAWIAATRHIAMMERKE
Part of the ABC transporter FtsEX involved in cellular division.
P44872
A7GUU4
LGT_BACCN
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Bacillus cereus group
MLLGSVPQLDRVAIHLGPFPVYWYGIIIGTGVLLGLWLATREGERLGIPKDTFVDLVLFAVPIAIICARAYYVAFEWEYYMQNPIQIINTRQGGLAIHGGLIGAVMTGIIYAKVKRISFWKLADIAAPSILLGQAIGRWGNFMNQEAHGGEVTRQFLEGLHLPDFIVNQMYIDGVYYHPTFLYESLWSFAGVILLLLLRKANLRRGELFFTYLIWYSIGRFFVEELRTDSLMLGPLRIAQVMSIGLIVISIIFIIVRRKTGQADKRYLEK
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
A7GUU4
Q39QR8
PURT_GEOMG
Phosphoribosylglycinamide formyltransferase 2
Geobacter
MIGTPLKKSATRVMLLGSGELGKEVVLEAQRLGVEVIAVDRYADAPAMQVAHRAHVVNMLDRVELGRIVARERPHLIVPEIEAIDTPYLLELEQEGYTVIPTARAANLTMNREGIRRLAAEELGLPTAAYRFAASIESFRAAVKDIGLPCVVKPIMSSSGKGQSVVKSMEEIDGAWTYAMEGGRGASDTVIVEEFIPFDYEITLLTVRHAGGTTFCPPIGHVQIKGDYHESWQPMAMTPAALAESQRQAKAVTDALGGSGIFGVELFIKGDRVWFSEVSPRPHDTGMVTMISQNLSEFELHVRAILGLPVPEVANLAPAASHVVLASEAAEEVTFSGLDAALSVPETKLRLFGKPDTRPGRRMGVALSFGADTDEARNRAEQAAHAVKIVTL
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
Q39QR8
Q8ZWK4
SYT_PYRAE
Threonyl-tRNA synthetase
Pyrobaculum
MRVLYIHAERFNWEPRDPALDIRDEPTSGNANNALVVFTSVERGDVPDENFLRAVASDIIDVAKKVKASAIVIYPYAHLSSDLARPYTAREVLNKLFEVVKSQFNGEVLKAPFGYYKAFEIKCLGHPLSELSRSFKPEEGRADRRAEERRDYYVIITPNGEEHDPAKFNYANYGDLKALVEKEVFRKELGGGEPKYLEYLRKFGFEWEPMSDAGHMRYAPEATVMMELVEDYSYIVAKSLGIPVFKIRGTNMFKLSEKAIESHARLFGERLYIVESDTDLILRYAACFQQFAMAKDWVISYKHLPFGMLEIADSYRHEQPGETVLLFRLRRFYMPDLHIFTKDLKEAMEVTYKLHEVIFREIGKLGRTYVSLYNVTEGFYKNHRDYLVELARREGKPILVRVLPGQKYYWVLNVEFHIVDELGRPREIATFQIDVGNAQRFGIKYVDENNQIKYPVIIHTAILGSVERYLYAVFDTMAKMEKEGKVPRLPTWLSPVQVRVIPVSKENLKYAISIADVLEAEGIRVDIDDREETLSKKIRDAETSWIPYIVVVGSKEEAEGVIAVRERGGGQYKIRLEELVKKLKDETRGYPQRPLYLPRLLSQRPSRF
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Q8ZWK4
Q2YL69
NIKE_BRUA2
Nickel import ATP-binding protein NikE
Brucella
MSLISADNIVKIYQSHSLVGASARKTMLHDISISIGQGETVALLGRSGCGKSTLARLLVGLERPTSGEVRFRGVPLTKLDRSGMKAFRREVQLIFQDSPGAVNARSSVRAIIGEPLRHLTSLDETRREERIQELLRLVELPPEIADRLPAQVSGGQLQRICIARALAVNPKLIILDEAVSNLDIHLQASALALLTKLQQEGGIAYLFVTHDLRLVQKFAARCLVMDEGQIVEEIKTADLDSMRHPASRLLREAVLPPLPVRAVETN
Part of the ABC transporter complex NikABCDE involved in nickel import. Responsible for energy coupling to the transport system.
Q2YL69
Q6GKB4
PTXBC_STAAR
PTS system MurNAc-GlcNAc-specific EIIC component
Staphylococcus
MTKEQQLAERIIAAVGGMDNIDSVMNCMTRVRIKVLDENKVDDQELRHIDGVMGVIHDERIQVVVGPGTVNKVANHMAELSGVKLGDPIPHNHNDSEKMDYKSYAADKAKANKEAHKAKQKNGKLNKVLKSIANIFIPLIPAFIGAGLIGGIAAVLSNLMVAGYISGAWITQLITVFNVIKDGMLAYLAIFTGINAAKEFGATPGLGGVIGGTTLLTGIAGKNILMNVFTGEPLQPGQGGIIGVIFAVWILSIVEKRLHKIVPNAIDIIVTPTIALLIVGLLTIFIFMPLAGFVSDSLVSVVNGIISIGGVFSGFIIGASFLPLVMLGLHHIFTPIHIEMINQSGATYLLPIAAMAGAGQVGAALALWVRCKRNTTLRNTLKGALPVGFLGIGEPLIYGVTLPLGRPFLTACIGGGIGGAVIGGIGHIGAKAIGPSGVSLLPLISDNMYLGYIAGLLAAYAGGFVCTYLFGTTKAMRQTDLLGD
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in the uptake and phosphorylation of MurNAc-GlcNAc, the principle peptidoglycan turnover product of S.aureus, yielding cytoplasmic MurNAc 6P-GlcNAc.
Q6GKB4
C0Z7W5
ACCD_BREBN
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Brevibacillus
MLKDLFGKKRKFATVPSETLARVPASTDISKEAGTKEKEVPEGLMNKCPHCGTIHYSKDLEKNLRVCKGCQFHYSMSAPERLQALLDDGVLREEFDANLITANPLGFPGYLEKLEQDMANTNLNEAIITGEGFLGGNRIVIGVMDSRFRMASMGSVVGEKITRAIEQAIERRLPFILFSASGGARMQEGVLSLMQMAKTSAALSRLDRERLLFVSVMTNPTYGGVSASFSSLGDYNIAEPGAMIGFAGRRVIEQTIRQELPKDFQTAEFLLKNGQLDMVVHRKDMRNTLSKLVEMHTSREGVETWQASSPLKSH
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
C0Z7W5
B1VAD1
RS5_PHYAS
30S ribosomal protein S5
16SrXII (Stolbur group)
MKTIKKEFVKKTSPYEEKVVKIKRITKVVKGGRRFRFSALVVVGNKKDQIGFATAKAQEIVDAIKKAVEKAKKQLIRIPIVGTTIPHDTIGHFGASKFLLRPASKGTGIVAGGAAARTVLELVGISDVLTKTFGSRTSINVIRAVMDGLKNLRTKEEVAKLRGLTLAKNEQ
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
B1VAD1
B9IT45
RNPA_BACCQ
Protein C5
Bacillus cereus group
MKKKHRIKKNDEFQTVFQKGKSTANRQFVVYQLDKEEQPNFRIGLSVSKKIGNAVVRNRIKRMIRQSITELKDEIDSGKDFVIIARKPCAEMTYEEVKKSLIHVFKRSGMKRIKK
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
B9IT45
Q17V60
NADK_HELAH
ATP-dependent NAD kinase
Helicobacter
MKDSHQTIGVFVRPTHHQNPLFSELTQAKEWVLRLLEDEGFESFMADDNGLKDERLIEKAYAFLCLGGDGTILGALRMMHSYNKPCFGVRMGNLGYLTAIELNELKDFLQNLKHNKIKLEEHLALEGRIEEISFYAINEIVITRKEALGILDIEACVSHTPFNTYKGDGLIIATPLGSTAYNLSAHGPIVHALNQSYVLTPLCDFSLTQRPLVLGAEFCLSFCANKDALVIIDGQATYDLKANQKLYIQKSPTTTKLLQKNSRDYFKVLKEKLLWGESSSKKN
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Q17V60
Q9N589
MTMR1_CAEEL
Phosphatidylinositol-3-phosphate phosphatase
Caenorhabditis
MDDRGNNSGEVGEFASSSMIQESIDLKLLAAESLIWTEKNVTYFGPLGKFPGKIVITRYRMVFLVGDGGKMYEQWKLDIPLGQVSRIEKVGRKTTSVAKRGDDNYGFTIYCKDYRVYRFTCNPASSDRKNVCDSLNRYAFPLSHNLPMFASVHAAETPRLMKDGWKIYSAEKEYERLGIPNSRLWKEVDINKDYKFSETYPRTFVIPTVSWEEGKPFVKKLGEFRSKERIPVLSWINQTTLASISRCSQPMTGISGKRSAEDERHLTNIMNANANCRELLILDARPAVNAKLNKAKGGGYEENYVNAPLTFLNIHNIHVVRDSLKRLLAALIPRVDEKGYYKALDESKWLNHVQSILEGAVKAVFNVDTEKQSVLIHCSDGWDRTAQLTSLAMIQLDSYYRTIEGFIVLIEKEWCSFGHKFGERIGHGDDNYSDGERSPVFVQFCDCLWQIMRQFPWAFEFTQELLICMLDELYACRYGTFLYNSEKIRLKDKKCDETTISFWSYVLENKKKFRNPMFKHGKSNKVINVNPSLCGLHVWIDYYARSNPYVVTPNHEDVQQPGAQFVDEKKQLLDEIMALDDAAQKLTA
Dephosphorylates phosphatidylinositol 3-phosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Negatively regulates accumulation of PI3P on intracellular vesicles . Negatively regulates phagocytosis of apoptotic cells probably by limiting the recruitment and/or the activation of ced-5, ced-2 and ced-12 complex . In addition, may positively regulate phagosome maturation by promoting recycling of apoptotic receptor ced-1 back to the plasma membrane . Essential for embryonic and larval development . May promote migration of distal tip cells .
Q9N589
P37001
PAGP_ECOLI
Lipid A acylation protein
Escherichia
MNVSKYVAIFSFVFIQLISVGKVFANADEWMTTFRENIAQTWQQPEHYDLYIPAITWHARFAYDKEKTDRYNERPWGGGFGLSRWDEKGNWHGLYAMAFKDSWNKWEPIAGYGWESTWRPLADENFHLGLGFTAGVTARDNWNYIPLPVLLPLASVGYGPVTFQMTYIPGTYNNGNVYFAWMRFQF
Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. Phosphatidylglycerol (PtdGro), phosphatidylethanolamine (PtdEtn), phosphatidylserine (PtdSer) and phosphatidic acid (Ptd-OH) are all effective acyl donors.
P37001
Q6VNS1
NTRK3_MOUSE
TrkC tyrosine kinase
Mus
MDVSLCPAKCSFWRIFLLGSVWLDYVGSVLACPANCVCSKTEINCRRPDDGNLFPLLEGQDSGNSNGNASINITDISRNITSIHIENWRGLHTLNAVDMELYTGLQKLTIKNSGLRNIQPRAFAKNPHLRYINLSSNRLTTLSWQLFQTLSLRELRLEQNFFNCSCDIRWMQLWQEQGEARLDSQSLYCISADGSQLPLFRMNISQCDLPEISVSHVNLTVREGDNAVITCNGSGSPLPDVDWIVTGLQSINTHQTNLNWTNVHAINLTLVNVTSEDNGFTLTCIAENVVGMSNASVALTVYYPPRVVSLVEPEVRLEHCIEFVVRGNPTPTLHWLYNGQPLRESKIIHMDYYQEGEVSEGCLLFNKPTHYNNGNYTLIAKNALGTANQTINGHFLKEPFPESTDFFDFESDASPTPPITVTHKPEEDTFGVSIAVGLAAFACVLLVVLFIMINKYGRRSKFGMKGPVAVISGEEDSASPLHHINHGITTPSSLDAGPDTVVIGMTRIPVIENPQYFRQGHNCHKPDTYVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKILHALGKATPIYLDILG
Receptor tyrosine kinase involved in nervous system and probably heart development. Upon binding of its ligand NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different signaling pathways, including the phosphatidylinositol 3-kinase/AKT and the MAPK pathways, that control cell survival and differentiation.
Q6VNS1
Q6DFJ3
FUD1B_XENLA
FUN14 domain-containing protein 1B
Xenopus
MSKKSTNIFTCSGAQHKWIQVVNIDGNIFSIYVCFFVCFFFYLEPSSDDESYEVLDLTEYARRHHWWNRLFGRNSGPLTEKYSVATQIVIGGVSGWCAGFLFQKVGKLAATAVGGGFLLLQIASHGGYIQIDWKRVEKDVNKAKRKIKKEANKTPEINTVIEKSTDFFKKNIVVSGGFVGGFLIGLAS
Acts as an activator of hypoxia-induced mitophagy, an important mechanism for mitochondrial quality control.
Q6DFJ3
Q9LFT5
EPFL1_ARATH
MEPFL1
Arabidopsis
MFAIYKSTLLLLPLILILLITPQVSSFLQPIQPPISPQVALIEDKARLGSTPPSCHNRCNNCHPCMAIQVPTLPTRSRFTRVNPFSGGFVRPPSSLTTVLDQYSNYKPMGWKCHCNGHFYNP
Controls stomatal patterning.
Q9LFT5
Q4L4Y3
ADDA_STAHJ
ATP-dependent helicase/nuclease AddA
Staphylococcus
MNNIPIKPKDAQWTDAQWKSIYANGQDVLVAAAAGSGKTAVLVERIIQKIIRDEIDVDKLLVVTFTNLSAREMKHRVDQRIQQASIEDPRNEHLKNQRIKIHQAQISTLHSFCLKIIQQHYDVIDLDPNFRTISDVENVLLLEQSIDEVLEKHYDTPDIEFLTLVEQLSSDRNDDNFRDLLKRFYNFSIANPSPFEWLDSLVEIYTDDNKHKLYLDELERLSKIYIKAAYHTLLEAENNFLNCIEAEKHLDVIKLEKFKCEKMIEGNVINFEEIINYTSEKLPTITKKLKDTNEDEGISSQFLTNAKDFFDDYKKLLSEVKNKYLMRSYEDLKVDMKRLAPRIQYLVQIVKDIINGFAEKKRSRNVLDFSDYEHFALQILTDQEGNASPIAKEYRSQFEEILVDEYQDTNQVQEAIISKIKRGDESNGNLFMVGDVKQSIYKFRQADPTLFMDKYHRFTKDGDQSGLRIDLSKNFRSRKEVLATTNYLFDHMMDEEVGEIEYDADARLYFGATKYSDKSMPLELHALIQDKSSDNDLEKSEQEARYIAEQVKYIIEHKQVYDMKSETYRQATFKDIVILERGLKNARNLQQVFKDYNIPFHVNSKEGYFEQTEVRLVLSFLRTVDNPLQDIYLVGLMRSVIYQFTEDELANIRVQSMNDDYFYQSILHYMKDQEANPLLVEKLEHFMDDINMYQEYSQSHPVYQLIDKFYNDHYVIQYFSGLIGGKGRRANLYGLFNKAVEFENSSFRGLYQFIRFIDELIERNKDFGEENVIGPNDNVVRMMTVHSSKGLEFPYVIYSELSKNFNKGDLRKPLILNQKYGLGIDYFDLEQNVTYPSLSSVVIKSITEKELISEEMRLMYVALTRAKEQLILIGTIDKEEALEKLERLPISGNQIALHKRLSADRPFDLIYSILAKYQSTSLLPEYRFEKSIDNLDESLRPTVDIKIAQFEELSIEDSESEQESRNISDLEVEGSHDDTLKQQINDQLSFKYPYLKDTEKPSKQSVSELKRQLETEESGTSYERVRQYRIGVSTYERPKFLRENKKRKANEIGTLMHTVMQHLPFKETRMTETELNDYINELIEKHIIEEDAKKDIQFEAVMNFIRSDLYMTITQADKVYRELPFVVNQARVDEMPESDEDVSIIQGMIDLIFLKDDQYYFVDYKTDAFNKRRGMTDEEVGIQLRDKYKIQMKYYKNTLETILNSKVYGYLYFFQFGQMSIEEDV
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddA nuclease domain is required for chi fragment generation; this subunit has the helicase and 3' -> 5' nuclease activities.
Q4L4Y3
B3EP74
OBG_CHLPB
GTP-binding protein Obg
Chlorobium
MKFVDSAKIYVKGGNGGNGCMSFRREKYVPKGGPDGGDGGRGGHVYLRADGQMSTLLDFRYKKHYEAQRGVHGQGSKKNGKMGKDTVIPVPCGTVVRNAADGSLIADLTEEGEELLVAEGGKGGKGNPHFASSTRQAPRYAEPGGVGMALEIELELKLMADVGLVGFPNAGKSTLISSVSAARPKIADYPFTTLVPNLGIVQYREYSSFVMADIPGIIEGAAEGKGLGLQFLKHIERTKVLAVLIAADSEDIEAEYASLKREMERFGSGLLEKPRVVLITKMDIAPEDFSVPSFSDDAPVLMISSVTGEGIDVLKDELWSRVKSEG
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
B3EP74
B7JW76
TIG_RIPO1
PPIase
Rippkaea orientalis
MKVTQEKLPDSQIGLEIEISAEASKKAYETKVNTLARTANIPGFRKGKVPRQILLQRIGTEYIKATTLQELIEDSLKAAIKQESLESIGDFELKSKFDELVQQFKPGEPLTFSAAIDVPPTVTLGDYQSLSVKAEETVYNPEKLENWFKERQEQQATLVPVEDRKAEMGDVAIVDYEGYFAPEEGEETERKPIPGVQGQDFRVDLTEGRFIQGMVEGIVGMQPEETQEITVTFPSDYPREDLAGQVAIFKITVKELKAKELPELDDDFAEEVSEFATIAELRESLEKQFTEEAQEATKKSIHDAMITQLLEICPVDLPNTLIEDEVTQVLTQTAMQMEQMGIDIRQLFVKENIPKLRENARPDAISRLKQSLILQEIAKVESITPEASLVEERINKIKEQLSERDVDFDKLEQMVTEELTMEAILNWLQEKATVELVPEGTLKPAEDQEAESQEE
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.
B7JW76
P50304
METK_ASCIM
Methionine adenosyltransferase
Ascobolus
MSIPVNPNSFKGSFLFTSESVGEGHPDKIADQVSDAVLDACLAEDPLSKVACETATKTGMIMVFGEITTKAHLDYQKIIRNAVKDIGYDDSAKGFDYKTCNVLVAIEQQSPDIAQGLHYEKALEELGAGDQGIMFGYATDETPELLPLTLLLAHQLNANMAKARRDGSLPWLRPDTKTQVTIEYEHDGGAVVPKKVKTVVVSAQHSEDITTEELRKEILEKIIKTTIPAKYLDEDTVFHIQPSGLFIIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYSKVDRSAAYLARWIAKSLVTAGLVRRCLVQLSYAIGVAEPLSIFVEDYGTSAEGRTSDQLVEIIRKNFDMRPGVIVQELDLAKPIYFQTAKNGHFTNQEFAWEKPKKLNL
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
P50304
Q4UTP4
ISPD_XANC8
MEP cytidylyltransferase
Xanthomonas
MTGSVWAIVPAAGRGTRFGGAVPKQYLHAAGQPLMAYTLAALAAHPAVAGIVVAIAPDDADWPGWTAVHAKPVLTCVGGATRAASVLAGLLALPDGVRADDFVLVHDAARPNLALADLDRLLEIGRGDPVGAILAAPVRDTLKRAGDDGGIDGTEPRERLWRALTPQLFRRHQLIRGLTEASAAGVDVTDEAMAIERLGLRPLLVEGAEDNFKVTTPADLARFEFELANRDRGGASREAERSAMPSAATSVFSGARSAASGSEEV
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Q4UTP4
Q7U4K1
NDHN_PARMW
NAD(P)H dehydrogenase I subunit N
Parasynechococcus marenigrum
MPLLLTGRTFRRDLEAHGCLAVHAPLEGGAETRLLRRLRGAGYRTRLWSARGLGDPEVFLTQKHGIRPPHLGHQSVGRGAAVGEVQEVVPQLGDLLDGDAQVALWLLEGQVLSQSELRSLCDLCSREPRLRIIVEMGGARSLRWQPMSGLLAS
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
Q7U4K1
A8MEB3
SYS_ALKOO
Seryl-tRNA(Ser/Sec) synthetase
Alkaliphilus
MLDIKRIRNNLDEIKAAMARRGEKDFDLDAVVALDEKRRELLQQVELMKNEQNTVSKEVPKLKKEGKDATEVMARMKELSGKIKELDGQVKEVEDQLEYTLLRIPNVPHPDVPQGETDDDNIEVRKWSEPTHFDFEPKAHWDIATDLGIIDFEAASKITGARFALYKGVGARLERALINFMLDLHIEEHGYTEVLPPFMVNRSSMTGTGQLPKFEEDAFKLPQKDYFLVPTAEVPVTNMHRDEIIEGANLPLSYVAYTPCFRSEAGSAGRDTRGLIRQHQFNKVELVKFVKPEDSYAELEKLTNNAEKVLQLLEIPYRIVRICTGDLGFTAAFKYDIEVWMPSYNRYVEISSCSNFEDFQARRANIRYRPEEKGKVEFLHTLNGSGLAVGRTVAAILENCQDDEGNVKIPEALIPYMRGIKVITK
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
A8MEB3
A4SUY2
IF11_POLAQ
Translation initiation factor IF-1 1
Polynucleobacter
MSKDDVIQMAGEVVENLPNAMFRVKLENGHVFLGHISGKMRMHYIRILPGDKVTVEMTPYDLTRARIIFRAK
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.
A4SUY2
B3EWD3
HBA_PERCR
Hemoglobin subunit alpha
Peromyscus
VLSAEDKANVKAVWSKLGGHGAEYGAEALGRMFESHPTTKTYPFHFDVSHGSAQVKGHGKKVADALATAASHLDDLPGALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHHPAEFTPAAHASLDKFLASVSTVLTSKYR
Involved in oxygen transport from the lung to the various peripheral tissues.
B3EWD3
Q4FLM2
RS19_PELUB
30S ribosomal protein S19
Candidatus Pelagibacter
MARSVWKGPFVEESLIKKVEKQKLDPKKMPIKTWSRKSTIIPEFIGVSFLIYNGKKFIPVTISEDMVGHKLGEFSPTRTFFGHTPAEKKGKPAEKKK
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Q4FLM2
Q6G091
DAPA_BARQU
4-hydroxy-tetrahydrodipicolinate synthase
Bartonella
MLKGAVTALITPFDDNGAIDEKAFCNFVEWQITQGINGVSPVGTTGESPTLSHEERKQVVELCVEQVAKRVPVVAGAGSNSTSEAVELAQHAEKAGADAILVVTPYYNKPNQKGLYTHFSSIAKAISIPVIIYNIPGRSVIDMAVETMRDLCQDFKNIIGVKDATSKIGRVSEQREKCGKDFIQLSGDDCIALGFNAHGGVGCISVSSNVAPKLCAELHAACFRGDYETALKLNDLLMPLNRAVFIEPSPAGIKYAAAKLGLCGSLVRSPIVPLAETTKKIIDAALHHAGLLKE
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Q6G091
Q72DU2
RIMM_DESVH
Ribosome maturation factor RimM
Desulfovibrio
MEASRFIEIGLLTRPHGLKGEVCVDYYADSPFLLEGTVYLKAGRAAPRPVKVQSMRMHKGRPLVIFEGVNDRTAAELLRGHVMLVPEDTLPELDEDEVYLFELEGISVVIDESGEHLGVIERIDTDAYQEIWVIRTPQGKEVLFPAAAPFVLDIDLDSRTARIAPPPGLLDIYLSD
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.
Q72DU2
Q6D1I3
PROB_PECAS
Gamma-glutamyl kinase
Pectobacterium
MSGSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHAAGHRIVIVTSGAIAAGREHLGYPELPATIATKQLLAAVGQSRLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTMRALLDNNIVPVINENDAVATAEIKVGDNDNLSALAAILADADKLLLLTDQAGLFTADPRNNPDAELIREVTGINDALRSIAGDSVSGLGTGGMSTKLQAADVACRAGIDVVIAAGSKPGVIGDVIADISVGTRFHALDTPLESRKHWIFGAPPAGEITVDDGALSAILERGSSLLPKGIRTVEGNFSRGEVIRVRSLAGRDVAHAVTRYNSDALRLIAGHHSQQIAEILGYEYGPVAIHRDDMIIN
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Q6D1I3
Q93ZT6
IF4G1_ARATH
Eukaryotic translation initiation factor isoform 4G-1
Arabidopsis
MQQGDQTVLSLRPGGGRGNRLFGSSSSSSSLSFGSLSSSDLPLLRPHGGAPASSFPFKGGDSRFDGRERVKYTREQLLELKETTQLSDEILRVQRETAAELFGEEGTWARGESVVSNLVPVQSASRFSEPDSRDWRSRSTQPPPSGEERSWDNLREAKDSRYVEASQYNRQDQPNSQFSRANISSNQGGGPAPVLVKAEVPWSARRGNLSENDRVLKTVKGILNKLTPEKYDLLKGQLIESGITSADILKGVITLIFDKAVLEPTFCPMYAKLCSDINDQLPTFPPAEPGDKEITFKRVLLNICQEAFEGASQLREELRQMSAPDQEAERNDKEKLLKLKTLGNIRLIGELLKQKMVPEKIVHHIVQELLGADEKVCPAEENVEAICHFFKTIGKQLDGNVKSKRINDVYFKRLQALSKNPQLELRLRFMVQNIIDMRSNGWVPRREEMKARTITEIHTEAEKNLGLRPGATANMRRGMVSSGGPVSPGPVYPGGRPGAGGLMPGMPGTRRMPGMPGVDNDNWEVPRTRSMSRRDGPGPLHSPAVSKSASMNTRLLPQGSSGIMSGKTSALLQGSGSVSRPVTVSAERPAQSVAPLTVPVPVEKPQPSGPKLSEEVLQRKTKSLLEEYFNVRLLGEALQCVEELGLPSYHPEFVKEAISLSLEKSPPVVEPIATLLEYLLSKKVVAPKDLETGFLLYGAMLDDIGIDLPKAPNNFGEIVGKLILAGGVDFKLVREIIGKMEDDRFQKMVVDAAVRIVESSEQGKSLLASQAADIEACRNL
Plays a role in the accumulation of some potyvirus during viral infection.
Q93ZT6
Q2P4A6
EFTS_XANOM
Elongation factor Ts
Xanthomonas
MEITASLVKELRERTGAGMMECKKALVENAGDIDAAAEWLRKSGLAKADKKADRVAAEGRIATAQAGGKAVLVEVNSETDFVAKDENFLAFTEVVANAALNSDAADAEALKSVKLDSGETIEERRAAVIAKVGENLQVRRLVRIDSANNVAAYVHGGRIGVLVELKGGDIELARGIAMHIAAMNPPHVKASDVPAEFVAKEKEIELAKMSEKDKAKPADILEKIISGKISKIVNEVTLYGQPYVLNTDQTVEQAVKAAGAEVIRFQRLAVGEGIEKVVEDYAAEVMKQAGLA
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.
Q2P4A6
B0TLZ8
RS8_SHEHH
30S ribosomal protein S8
Shewanella
MSMQDPIADMLTRIRNGQAAKHVSVKMPSAKLKIAIAQMLKEEGYITDYAVADEAKPELEITLKYFQGQPVVETIQRVSRPGLRIYKGKNELPKVMGGLGVAIVSTSKGLMTDRTARQNGMGGEVICYVA
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
B0TLZ8
A7ZCD9
SURE_CAMC1
Nucleoside 5'-monophosphate phosphohydrolase
Campylobacter
MKEILITNDDGFEATGLLALKEALSELDGVNVTIVAPSSEKSACAHSLTLTRPLRFIKLDDNFFKLDDATPSDCVYLALHALYNKKPDLVISGINHGANLGEDITYSGTCGAAMEGVLQGIRSIAFSQFYENNSLNELGFELAKEVVKFITPKVLNDEISLNPREFLNVNIPATTSKNFKGYAVVPAGRRTYATHATLNRNPRGIEYYWLGNAALEYEKGEPSDISKVNEGFATITPIKLNMTSYESLESLKGKFDAK
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
A7ZCD9
A7FFS0
PXPA_YERP3
5-oxoprolinase (ATP-hydrolyzing) subunit A
Yersinia
MKIDLNADLGEGCANDQALLQLVSSANIACGFHAGDAQTMRQSVRWALEYGVAIGAHPSFPDRENFGRTAMQLPPETVYAQVVYQLGALAAIVQVEGGVMQHVKPHGMLYNQAAVDPLLADAIAQAVKAVDPSLRLVGLAGSELIRAGTRVGLVTRQEVFADRHYQPDGTLVPRSQPDALIESDELALSQTLAMVQQHQVQACDGSWVQVQADTVCVHGDGVQALAFARCLRDRFQQEGISVIAQ
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
A7FFS0
Q10493
MU106_SCHPO
Meiotically up-regulated gene 106 protein
Schizosaccharomyces
MSIKVEWIKFTRLKKCATLLVQLSLLRYRYMVLAYNHKFDCIVVTIYCGCLFWFSNGALFTEGKARDRGRWAKATMKKNYGVKLKIFLFTILLAFETNTFTPYTSTFSHFARGCL
Has a role in meiosis.
Q10493
B0CAV7
RL9_ACAM1
50S ribosomal protein L9
Acaryochloris
MGKRVQLVLNEDVRKLGYSGDLVEVAPGYARNYLIPKGIAYRATPGVLKQIEHRKAEELKRLEGIKDEAAKQKVALQTIGTFRIEQKAGEEDMLFGRVTSPDVAELIANISGFEIDKRGIDIPDIRKLGTYSVDIKLHPEVIATVKVEVVPE
Binds to the 23S rRNA.
B0CAV7
Q2RGV7
HIS1_MOOTA
ATP phosphoribosyltransferase
Moorella
MVTNLLTLALPKGKLGQDALQLLQAAGLPVEGVATEARQLTFTFPAPGIRYLICRPTDVPTYVEYGAADLGIVGKDTLAEAGADVFELVDLGFGYCRFVVAAPRERWEEAGRSLENLLAGSRRVATKFPRVAASFFQERGLPVEIIKLHGNIELAPRAGLADLIVDIVSTGRTLKENDLVEVAPIFSSTARLIANRVSYRINYRRLTSVVEALKRAAGQGGEKIATTN
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Q2RGV7
A5VT38
HSLV_BRUO2
ATP-dependent protease subunit HslV
Brucella
MIEHNPTTIYGTTIVTVRKDGKVVIAGDGQVSLGNTVMKGNARKVRRIGKGNVIAGFAGATADAFTLLERLEAKLEQYPDQLMRASVELAKDWRTDRYLRKLEAMMLVADSKATLALTGTGDVLEPEQGVMAIGSGGNYALAAARALIETDKSAEEIARKAMNIAADICIYTNHNIIVESLDAQ
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
A5VT38
Q1LNF5
RRF_CUPMC
Ribosome-releasing factor
Cupriavidus
MTVADTKKSVEQKMQKSIEAFKADLAKVRTGRAHTGLLDHVQVDYYGSMVPISQVAAVSLADARTISVQPWEKKMVQAVEKAIRDGDLGLNPATMGDVIRVPMPPLTEERRRELTKVVKGEAEGAKVAVRNLRRDANEQFKKLVKDKAISEDDERRGQDEVQKLTDKFVAEIDKLVAEKEKEIMTV
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
Q1LNF5
Q03I82
ECFA1_STRTD
Energy-coupling factor transporter ATP-binding protein EcfA1
Streptococcus
MIEIKNLKFKYNQDQTSYTLNDVSFHVKRGEWLSIVGHNGSGKSTTARLIGGLLVADSGQIIVDGQELTEETVWDIRDKIGMVFQNPDNQFVGATVEDDVAFGLENKGLPYKEMVSRVQEALSFVGMMDFKDREPARLSGGQKQRVAIAGIIAMRPSILILDEATSMLDPEGRQELIQSIEDIRQQYGMTVLSITHDLDEVAMSNRVLVLKQGKVESISSPRELFSRGSELVDLGLDIPFSALLTQKLKNQGLIDCEGYLTEKELVEQLWEYLSKM
ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Q03I82
P30886
BMP7_XENLA
Osteogenic protein 1
Xenopus
MNALTVKRRLPVLLFLFHISLSSISSNTILENDFHSSFVQRRLKGHERREIQKEILTILGLQHRPRPYLPEKKKSAPLFMMDLYNAVNIEEMHAEDVSYSNKPISLNEAFSLATDQENGFLAHADTVMSFANLVDNDNELHKNSYRQKFKFDLTDIPLGDELTAAEFRIYKDYVQNNETYQVTIYQVLKKQADKDPYLFQVDSRTIWGTEKGWLTFDITATGNHWVMNPHYNLGLQLSVESMDMQNVNPRLVGLVGKNGPQDKQPFMVAFFKTSDIHLRSVRSTSNKHWNQERAKTYKEQDNLPPANITDGIMPPGKRRFLKQACKKHELFVSFRDLGWQDWIIAPEGYAAYYCDGECAFPLNSFMNATNHAIVQTLVHFINPETVPKPCCAPTQLNGISVLYFDDSANVILKKYKNMVVQACGCH
Growth factor of the TGF-beta superfamily that plays important role in various biological processes, including embryogenesis, hematopoiesis, neurogenesis and skeletal morphogenesis. Initiates the canonical BMP signaling cascade by associating with type I receptor ACVR1 and type II receptor ACVR2A. Once all three components are bound together in a complex at the cell surface, ACVR2A phosphorylates and activates ACVR1. In turn, ACVR1 propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes.
P30886
Q0P4H6
LBX1_XENTR
Ladybird homeobox protein homolog 1
Silurana
MTSKDEAKSSSVEERRRHALDLLPPPANSNKPLTPFSIEDILNKPSVRRSYTICGTAHLLSTAEKPPAAGLPLSSRALLSQTSPLCALEELASKTFKGLEVSVLQAAEGRDGMTIFGQRQTPKKRRKSRTAFTNHQIYELEKRFLYQKYLSPADRDQIAQQLGLTNAQVITWFQNRRAKLKRDLEEMKADVESVKKMSPSTVEAVLTISELEEETNSVRDDSRSRSPQLGLSGHMPLSPSSPLTEQHTSKECSEDEEDVEIDVDD
Transcription factor that controls hypaxial muscle development by down-regulating myod1 and cdkn1b/p27, thereby allowing myoblasts to proliferate before the onset of terminal differentiation.
Q0P4H6
Q87RU8
NRDR_VIBPA
Transcriptional repressor NrdR
Vibrio
MHCPFCSENDTKVIDSRLVADGHQVRRRRQCLACSERFTTFETAELVMPKVIKSNGNREPFDEDKMVGGIQRALEKRPVSADSIELAISMIKSQLRATGEREVPSQMIGNLVMDQLKELDKVAYIRFASVYRSFEDIREFGEEIARLED
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
Q87RU8
Q8YPK5
TRUA_NOSS1
tRNA-uridine isomerase I
Nostoc
MLDSHQPKQTQRVALVVQYLGTHFHGWQRQKQHRTVQEEIETAIAKILGHHVTLHGAGRTDSGVHAAAQVAHFDATGLIPAHKWASVINSYLPKDILIKASAAVGDRWHARFSAAYRRYRYTIYTEDRPNLFVTPFSWHYYYAPLDESLMQAALKPLMGKHHLAAFHRAGSKRSHSWVEVQAVECHRSGPFIHIEIQADGFLYGMVRLLVGMLVQVGSGQRTLANFTELWKEQRREEVKHAAPSQGLCLLRVGYPDFPFTPDVWYDTMPKLVFSQESLVNSH
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Q8YPK5
A5IXM0
RL1_MYCAP
50S ribosomal protein L1
Mycoplasmopsis
MSAKGGKKIQNARSSFDKNIAYDLAEAVEIVKRTSYAKFDASVDLVFKLNLDVRKADQQLRGSVLLPNGTGKSISVLVVTNNVEKQKLATAAGADQVVDGQTLEQKIKEDIFDFDVMVADPAMMPLLGKYGKKLGPKGLMPNPKTGTVTPTPEKAVEELKKGKANYRTDKAGVVHTLVGKVSMDTEKLVENIKTVISLIKRLKPSAVKGTYIQNIVLSATMGPGVKVKIEK
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
A5IXM0
Q256K7
RS20_CHLFF
30S ribosomal protein S20
Chlamydia
MAPKKTTKKGGPKKRPSAEKRILTAQKRNLINQSFKSKAKTMMKKFEAALKAGDQTSISSGLQLVYSVADKAVKRGVFKSNKAARIKARATLRANAKV
Binds directly to 16S ribosomal RNA.
Q256K7
B8NTZ8
LNAE_ASPFN
Lna diastereomeric piperazines biosynthesis cluster protein E
Aspergillus subgen. Circumdati
MTRVTMDQDTENKVLVIKNMDSGYLVAGEQVTLEDVSYDATEPLAEDELMVQLLYATYDLFKRDLASSSADATELRGRKPVETMSIAQVIKSNNKQFQEGDMVIGRLPVQQYVLIKADDATELKLLENPCEFDDIRLFLSVLGVPGLLAFSSLYEIGRPKKGETILIAGASDEIGQLVGQMARLEGLKVFGSVESDEKLDFLITELGFDGGFNYAKESPYEALPRLVPNGIDIYYDNLSWMSRLNIGGLDTHFDLLGSRHLNAAFSSMRRYGRIMFYGTIAEQTVLDPIIGMFLHNTVLKRLTIRGFGLSDPSFGKKWGKLHMERMQQWVKEEKLKIPTFEITGMDNAAKAFVEAFYSSENTHTHTILAVT
NADP-dependent oxidoreductase; part of the lna gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine . The lna and lnb biosynthetic pathways appear to be part of a signaling network that controls the formation of sclerotia, a resilient overwintering structure . One primary function of the non-canonical nonribosomal peptide synthetases lnaA and lnbA consists in the reduction of L-tyrosine . The presence in the clusters of tailoring enzymes such as the oxidoreductases lnaB, lnbB, lnaE or lnbE, as well as of the cytochrome P450 monooxygenases lnaC, lnaD, or lnbC, might explain formation of various diastereomeric piperazines .
B8NTZ8
Q7NKL3
QUEG_GLOVI
Queuosine biosynthesis protein QueG
Gloeobacter
MAPTAAQIKSRARALGFHKVGIARADALDGEAAERLGGWLAAGYAGEMRWMHDPRRRDIQQVLPGVRSVICVALSYNTAQGEPAPGQARISRYALGRDYHKVLGKPLKELARWIEASDPGCRAVAYVDTGPVQEKAWAEAAGLGWIGKNACLITLEYGSWVFLGEILTTLDLEANDPHPNYCGTCTRCLSACPTAALVEPAVVDARKCLAYHTIENRAPELPEAIAEHQHGWVVGCDLCQTCCPFNLRAERWGRYSEVADFAPRDPWNEITLDQLADLSDAEFERWSEGSAIRRVKASGLRRNARSALGASGDSLAQAH
Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Q7NKL3
Q4A5L2
RL21_MYCS5
50S ribosomal protein L21
Mycoplasmopsis
MFAIIETGGKQILVKEGDSIYVEKLEGQEKSEVKFDKVLAVNDVFGKPYVTGAVVHGTIEKQGKAKKIVVYRHNPKSTHKRKLGHRQPYTLVKITKIKGK
This protein binds to 23S rRNA in the presence of protein L20.
Q4A5L2
C5BGI4
MUTS_EDWI9
DNA mismatch repair protein MutS
Edwardsiella
MTTTDNLDAHTPMMQQYLRLKAQHPDILLFYRMGDFYELFYDDARRASQLLDISLTKRGASAGEPIPMAGVPYHAVENYLAKLVQLGESVAICEQIGDPAASKGPVERKVVRIVTPGTVSDEALLSERQDNLLAAIWQSPNGFGYATLDISSGRFRAAEPQDADSMAAELQRTNPAELLYPEEFTSMALIEQRRGLRRRPMWEFELETARQQLNLQFGTRDLSGFGVEQAPQALRAAGCLLQYAKDTQRTMLPHIRAITMERQQDGIIMDAATRRNLELTQNLAGGQENTLAAVLDASVTAMGSRMLKRWLHMPIRDRQALQRRQDAIEALLPLIDDLQPLLRQVGDLERILARLALRSARPRDLARMRVAFQQLPTLQTLLGERGSEALAPLARQAGRFDALCELLERALVETPPVLVRDGGVIASGYHAELDEWRALADGASDYLDRLEVREREKLGLDTLKVGFNAVHGYYIQVSRGQSHLVPIHYVRRQTLKNAERYIIPELKEYEDKVLTSKGKALALEKQLYDELFDLLLPHLAALQQSATALAELDVLSGLAERADRYGYVRPQLSERTGINIDEGRHPVVEQVLREPFIANPLTLSGARRMLVITGPNMGGKSTYMRQAALIVLMAHIGSFVPAQRAVIGPVDRIFTRVGAADDLASGRSTFMVEMTETANILHNATEHSLVLMDEIGRGTSTYDGLSLAWACAESLASRIKAMTLFATHYFELTTLPEKLEGVYNVHLDALEHGETIAFMHSVQDGAASKSYGLAVAALAGVPREVIKRARQKLRELETLSQHGNQSQADGAQLPLLVEAEPSAALEALTAIDPDVLTPRQALDWLYRLKGML
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
C5BGI4
Q1QIV7
RL25_NITHX
General stress protein CTC
Nitrobacter
MATVRELKATARPKSGKGAARAERRAGRVPGVIYGNNQPPQPISVEEPELRQRILAGRFLTTVFDISLEGKKHRVIPRDFHLDPVKDFPIHVDFLRLGEGATIRVSIPIRLLKADVAPGVKRGGTVNLVIHAIDVECAADDIPQFIEADVGGLEMSHSLHLSDVELPPGVKPLAREDMTLVTIVPPSGYAEEVKAAAAAAAAGTAAPAAGAAPAAGAAAAGAKAPAGGGDKKK
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
Q1QIV7
C4ZPV7
DAPB_ECOBW
4-hydroxy-tetrahydrodipicolinate reductase
Escherichia
MHDANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGELAGAGKTGVTVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVIGTTGFDEAGKQAIRDAAADIAIVFAANFSVGVNVMLKLLEKAAKVMGDYTDIEIIEAHHRHKVDAPSGTALAMGEAIAHALDKDLKDCAVYSREGHTGERVPGTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSRMTFANGAVRSALWLSGKESGLFDMRDVLDLNNL
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
C4ZPV7
Q21NW8
RPPH_SACD2
(Di)nucleoside polyphosphate hydrolase
Saccharophagus
MIDADGFRPNVGIILTDDQGRLLWARRVGGQDAWQFPQGGIKHNESPENALYRELEEEVGLCKADVEVLGVTQGWLRYRLPRRLVRDKEPKCVGQKQKWYLLRLVSNDSAIRLDASSPAEFDTWNWVSYWYPLGKVVAFKRDVYRRALKELSPVYNQYFLSTLGEGRALC
Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage.
Q21NW8
Q0KED0
DTD_CUPNH
Gly-tRNA(Ala) deacylase
Cupriavidus
MIALIQRVAQARVTVEGRTTGEIGAGLLALVCAERGDTEAQAERLLAKMLSYRVFSDAAGKMNLPVQNMDGNGNAGGLLVVSQFTLAADTNSGTRPSFTPAASPEDGRRLYEHFVAQARAAHPQVQTGEFGAMMQVSLVNDGPVTFWLRVPPA
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.
Q0KED0
B5YAR3
DNAK_DICT6
Heat shock protein 70
Dictyoglomus
MAKIVGIDLGTTNSLIAYLEGGRPTIIPNAEGSRLTPSVVAFTKDGQLLVGEPAKRQAIVNAERTIKSIKRHMGTNYKVKIDDKEYTPQEISAMILRKLKKDAEAYLGEPIEKAVITVPAYFSDAQRQATKDAGAIAGLEVVRIINEPTAAALAYGLDKEGHQKILVFDLGGGTFDVSILEIGEGVFEVIATAGNNRLGGDDFDERIVNWLVEMFMEEHGINLKEDRTALQRLFEAAEKAKIELSSKLQTEINLPFIAMKGNTPLHISVTLTRAKFEELTYDLVEKTKEPTERALKDAGLSPSQIDKIILVGGATRMPCIQEWIKKHFGKEPQRNVNPDEAVALGAAIQAGVIGGEIRDIVLVDVTPLSLGIETLGGVFTKIIERNTPIPVSKSQIFTTAADYQTSVEIHVLQGERALAKDNISLGRFILDGIPPAPRGVPQIEVTFDIDVNGIVHVSARDKATGREQRITISNAIRLSEEEIKRMTEEAKRFEEEDRKRREEIETKNQAEHLIYTARKTLKDYGDKVSKDLVQRVEDKIKNLEELIKPERINVEQVKKGMEELTQALGEIGQFMYQSASAAGNPGQGQTNENPGGKTIDGDYKVN
Acts as a chaperone.
B5YAR3
Q2K8V9
LIPA_RHIEC
Sulfur insertion protein LipA
Rhizobium
MVTILDTINPDAKRVRHPEKAHRPDTEVMRKPDWIRVKAPTSKGYAETRAIVKEHKLVTVCEEAGCPNIGECWDKKHATFMIMGEICTRACAFCNVATGKPNALDMDEPENVAKAVREMGLSHVVITSVDRDDLEDGGAEHFEKVIWAIRSASPATTIEILTPDFLKKPGALERVVAAKPDVFNHNMETVAGNYLTVRPGARYFHSIRLLQRVKELDPTMFTKSGIMVGLGEERNEVLQLMDDLRTADVDFLTIGQYLQPTRKHHKVESFVTPEEFKSYETVAYSKGFLMVASSPLTRSSHHAGDDFARLRAAREKKLLMAAE
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Q2K8V9
A2T391
CHLN_ANGEV
Light-independent protochlorophyllide reductase subunit N
Angiopteris
MNTFEILTFECETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNALGVMIFAEPRYAMAELEEGDISAQLNDHEELKRLCLHIKKDRNPSVIVWIGTCTTEIIKMDLEGIAPKVETEIGIPIVVARANGLDYAFTQGEDTVLAAITHRCPEYKSWVDEEDGTEKKVLSVYSERNRDETFKSPNHPPLVLFGSVPSTVASQLDSELKRQSIRVSGWLPAQRYTELPSLGEEVYVCGVNPFLSRTATTLMRRRKCKLIGAPFPIGPDGTRAWIEKICSVFGIKPQGLEERETQIWNNLKDYLDLLRGKSVFFMGDNLLEVSLARFLIRCGMIVYEIGIPYMDKRYQAAELSLLQDTCKKMHIPMPRIVEKPDNYNQIQRMRELQPDLAITGMAHANPLEARGINTKWSVEFTFAQIHGFTNAKDVLELVTRPLRRNNSLEHLGWTNLLQPTII
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
A2T391
B0SH84
RF1_LEPBA
Peptide chain release factor 1
Leptospira
MIDRLKKIQEKYLRIEDELAKATASDTLKNLSKERSRLTPVYTKADEYLKITKDCQDAKSLLESENDPDMHSMLKSEIEEGEKKLEELAKELEIMLLPPDPNSGKSILVEIRAGTGGEESGLFCADLFRMYNKYADKKGLRVEIIDMSQTGIGGYKEIVFSLDDDKAYDLFKFESGTHRVQRIPETESGGRIHTSAVTVAILPEAEEKEVEIKESDLRIDVYRSSGAGGQHVNTTDSAVRITHIPTGIVVASQEERSQIKNRDKAMRVLRARIADQAAETAKLSADALKKAQVGSGDRSERIRTYNFPQGRCTDHRIGFTSHNLPAIMEGDLDELIDALIQEDRSKRLAEAKA
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
B0SH84
B1MMH9
RL9_MYCA9
50S ribosomal protein L9
Mycobacteroides abscessus
MKLILTTEVEHLGTAGDAVEVKDGYGRNYLLPRGLAIVATRGAERQANDIRRAREAKEIRGVEHANEIKQAIEGLGAVKLTVKTAGEGKLFGSVTAADVVGAIKAAGGPNLDKRTVTLPKAHIKQIGSYVLDVHLHAGVATKVTVDVVAEG
Binds to the 23S rRNA.
B1MMH9
Q9I2C3
PQQB_PSEAE
Pyrroloquinoline quinone biosynthesis protein B
Pseudomonas
MHIRILGSAAGGGFPQWNCNCRNCRGVRDGSVAAQPRTQSSIALSDDGERWILCNASPDIRAQIAAFPALQPARRPRDTAIGAIVLLDSQIDHTTGLLSLREGCPHEVWCTQMVHQDLSEGFPLFPMLSHWNGGLRHRPIALDGEPFAIPACPRLRFTAIPLRSSAPPYSPHRGDPHPGDNIGLFVEDLDSAGALFYAPGLGEVDEALLEWMRRADCLLVDGTLWRDDEMLVCEVGDKLGRQMGHLAQSGPGGMLEVLAKVPAARKVLIHINNTNPILDTASAERAELDASGIEVAWDGMHIQL
May be involved in the transport of PQQ or its precursor to the periplasm.
Q9I2C3
Q5QW15
RLMM_IDILO
23S rRNA 2'-O-ribose methyltransferase RlmM
Idiomarina
MSEIVNGRGSGIVLLCRAGFEGDCAAEIQDKTAELGVYGYCQTQPEQAYVTYHCQHEEAEHIARKLTLKDLVFAREMFALLGPVKVAGIEDRASEVIKVLKPHQETFGLAGELRVGTPDTNEANQLSKFCRKFSVPLRQALRKEELLSNKPLAKRPMLHVLFVNPAHALVGYSYSYNQTLHNGGIVRLRMSKEAPSRSTLKLDEAFQVFVPENEHEKRVHSGMKAVDLGAAPGGWTYQLVRRGMMVQAVDNGPMAESLMETGQVKHIQEDGFKFRPKRKNVTWLVCDMVEKPARVGELMTSWLLEGDCEEAIFNLKLPMRQRYAAVKGYLDQIKEQLQTEGTKPFEIQAKHLYHDREEITVHLRWLPRS
Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
Q5QW15
Q10YY1
RRP3_TRIEI
Ycf65-like protein
Trichodesmium
MSKFILKVVWLDDNVALAVDQVVGNGTSPLTCYFFWPRNDAWEQLKKELEGKHWISEADRVALLNKATEIISYWQEEGRRRPFLEAQAKFPEIVFTGTN
Probably a ribosomal protein or a ribosome-associated protein.
Q10YY1