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
|
|---|---|---|---|---|---|---|
Q58660
|
PURL_METJA
|
Phosphoribosylformylglycinamidine synthase subunit II
|
Methanocaldococcus
|
MDENDLKYIEKVLGRKPNHIELAMFENLWSEHCAYRTSKKLLRMFAKTVNEKTSKNIVVGIGDDAAVIRLKNDICLAIAMESHNHPSYIDPYNGAATGVGGIVRDVLSMGAKPIALLDPLRFGDIFGKEGDKVRWLIEGVVKGIGDYGNRIGVPTVGGECEFDSSFDYNNLVNVVCVGLVKENEIITGKAKEPGLSLILIGSTGRDGIGGASFASKDLTEESEEERPSVQVGDAFSEKCLIDAVLEAVKTGKVKAMKDLGAAGLSGASSEMCYGGGVGCELYLENVVLREPLTPYEIMVSESQERMLLAVEPGSEEEIIEIFKKYELPASVIGKTIPEKRIIAKYKGEVVVDLPLDLLCEAPLYDREGKEDLKEKEDDKEKIKMPEDLNAVLLKLLESPNICSKEWIYQQYDHEVQIRTVVKPGKDAAVLRINEVYPMGIALTTDCNSRYCKLNPYVGAVNAVAEAVRNLATVGAEPIAMLDNLNFGNPERPERFWQLAECIKGLADAAEFFEIPVVGGNVSLYNETVIEGKEHPINPTPAIFVLGKVEDVEKVPGVLDNKIKEGDILIITNETKDEMGGSEYYKVIHNTEEGRVPRVDLEKEKKIYEEVREVVKEGLVSEAVDCSRGGLAVALAKMAVLNNIGLEVDLTEYNKNNLRDDILLFSETSGRIILAVRDENKDKVLSKLSSAYIIGKVGGSRLKIKINEKDVVNLDVEEMKKRYYEAFPKMMGEL
|
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
|
Q58660
|
B2FQP3
|
ASPN_STRMK
|
Endopeptidase Asp-N
|
Stenotrophomonas maltophilia group
|
MLSRSIGKAAGGLVLGLSVAAAAHAAPLFEPVTVISRASANSEPALGKLLATPSTATVQEVRVDAAATAQPQLEFELLGKRVQAVRSKVEALPDGGSIWYGQFRSPSDRLTAATSSGQDDPGNSLILVRSGDTITGSIRKDGKLYRLRPLGNRHVLVEVDESRMPADHPADYNQLPKIPMADNDHIGIAQASSGTPATIRVLVVATNAAVTAYGGNMQSLVQLAVAESNQGYVNSNVGLTLQLAGYETTNYSESGNFTTDLSRFRGTSDGYMDSIHTSRNTTAADVGVLLINNSAYCGLASGIGSTASTAFAAVYWDCATGYYSFAHEIGHLQSARHDIATDSSTSPYAYGHGYRYEPATGTGWRTIMAYNCTRSCPRLNYWSNPNISYNGIPMGNASTADNQRVLVNTKATIAAFR
|
Metalloprotease, specifically cleaves on the N-terminal side of aspartyl, glutamyl and cysteic acid residues.
|
B2FQP3
|
Q63055
|
ARFRP_RAT
|
ADP-ribosylation factor-related protein 1
|
Rattus
|
MYTLLSGLYKYMFQKDEYCILILGLDNAGKTTFLEQSKTRFNKNYKGMSLSKITTTVGLNIGTVDVGKARLMFWDLGGQEELQSLWDKYYAECHGVIYVIDSTDEERLSESKEAFEKVVSSEALDGVPILVLANKQDVETCLSIPDIKTAFSDCTCKIGRRDCLTQACSALTGKGVREGIEWMVKCVVRNVHRPPRQRDIT
|
Trans-Golgi-associated GTPase that regulates protein sorting. Controls the targeting of ARL1 and its effector to the trans-Golgi. Required for the lipidation of chylomicrons in the intestine and required for VLDL lipidation in the liver.
|
Q63055
|
A8W3A5
|
PSBA_CUSEX
|
Photosystem II Q(B) protein
|
Cuscuta subgen. Monogynella
|
MTAILERRESENLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAIEAPATNG
|
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
|
A8W3A5
|
Q46481
|
LPXA_ALLVD
|
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
|
Allochromatium
|
MRIHPTAIVEDGAQLHDSVTVGPYSIIESGAVIGEGCRIESNVRIFGVTRMGAHNRVCHGATLGSEPQDLSFTPEKARPLIIGDHNHFKECVNISGGIKSEGGTRIGSHNYWMAFSHAGHDCVVGDHNVFANTATLAGHVEIDDHCFLSGQVAVHQFCRIGSYVMIAGVTGVPQDVPPYMLADGHRARLIGLNVVGLRRNGFGQEQRTRIKQVYRLILRSGLRLDDALQRAEDEYPGPETKRIVAFIRASRRGIVSFG
|
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
Q46481
|
A4SVJ1
|
LPXK_POLAQ
|
Lipid A 4'-kinase
|
Polynucleobacter
|
MSFSLFRKAPKFWERRGPTSLLLWPLSWLYGLILRARKLIHDLGIVRTKPTPVPIIIVGNIRVGGTGKTPIVIALAKRLSQLGWKPGIISRGYGSSSQTAPLLVRSDSSPSLVGDEPVLIAKRTDNQFPIWVYPKRQQSIQALLKHSPEVDVIISDDGLQHRGLTRWPAREGGRDIEFVVRDSRGEGNRFLLPAGPLREPATRDRDATLFTGNPSFNEKKTGILDEYFLGRRAFSLGTYLGRPYQLIDHANTQSLEQIAEQFLPKSMTAIAGLGNPQRFFDDLAKQGVTCKQIPLPDHAQYTPEFFAKVKAQCLLITEKDAVKCAEISDERIWVVPMSLHLPENFVEWLQSILQRPDPHRYTL
|
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
|
A4SVJ1
|
Q2GM68
|
MTNA_CHAGB
|
Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein
|
Chaetomium
|
MATLQAIKYSRGKLLVLDQLRLPHEHHYDEVSTAEQAFDCIRSMRVRGAPAIAIVAALAHAVELHNGDCTATTPEDTIAYIESRLDYLKDSRPTAVDLSNAIALLKQAARAATVEGLAHPEAKEAILNAYIAAAETILAKDLDNNTSIGTHGAAWLQQQYHATPSRPLSVLTHCNTGSLATSGHGTALGIIRSLHQQQLLKHAYCTETRPYNQGSRLTAFELVFEGIPATLVTDSMAAALFALHRERMNIGAVVVGADRVVRNGDTANKIGTYALAVLARHHGVKFVVAAPTTSIDLETESGAGIEIEERKPEELTQVTGAVVNADGSVDASRTARVAIADQRIGVWNPAFDVTPHDLIDAIVTERGAVVKGADGRFDFSQVLPERWRW
|
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
|
Q2GM68
|
Q30QJ1
|
LPXA_SULDN
|
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
|
Sulfurimonas
|
MSKISPLAIIEDGAVIGKDVEIGAYCIISSDSTIGDGTKIEQNSCIYGKTTIGKNNHIFSHAVIGSAPQDLKFAGEDVELIIGDNNKIREFTLFNPGTKGGGGKTIIGSHNLFMGYVHIGHDVIIGNHCILANAATLAGHVEMGDYAVIGGMTPIHQFVHIGEYAMVAGASALAQDVPPFCMAEGNRATLRGLNLTGLRRNIEREEIDEIKSAYKELFEAGKPLKDVANEILEHTSSHHVQSLCNFVLKTKRGIPYERKHL
|
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
Q30QJ1
|
B0RB50
|
RL24_CLAMS
|
50S ribosomal protein L24
|
Clavibacter
|
MANIKKGDLVQVITGRTQAKGGDRGKQGRVLSVLVERNRVVVEGVNFVTKHVRVGQTQRGSKTGGIETVEAPIHISNVALVDPESKKPTRVGFRTETVEKDGVSKTVRVRYAKKSGKDL
|
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
|
B0RB50
|
Q1BM55
|
LEUC_BURCA
|
Isopropylmalate isomerase
|
Burkholderia cepacia complex
|
MAQTLYDKLWNTHVVHTEEDGTTLLYIDRQLLHEVTSPQAFEGLKIAQRPVWRISANLAVSDHNVPTTDRSHGIADPVSKLQVDTLDSNCDAFGITQFKMNDVRQGIVHIIGPEQGATLPGMTIVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQTLLQKKSKNMLVKVEGALPRGCTAKDIVLAIIGKIGTAGGTGYAIEFGGSTIRALTMEGRMTVCNMAIEAGARAGMVAVDDTTIDYLKGRPFVPTGAEWDQAVEYWRQFKSDDGAQFDRVVELNAAEIVPQVTWGTSPEMVTSIDGRVPDPEREKDPVKRDAMERALAYMALEPNTPIESIKVDKIFIGSCTNARIEDIRAAAYVVKKLNRRVASNVRLAMVVPGSGLVKAQAEREGLDKVFTDAGFEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAIEGHFVDIRQLG
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
Q1BM55
|
Q5HEG2
|
AGRA_STAAC
|
Accessory gene regulator A
|
Staphylococcus
|
MKIFICEDDPKQRENMVTIIKNYIMIEEKPMEIALATDNPYEVLEQAKNMNDIGCYFLDIQLSTDINGIKLGSEIRKHDPVGNIIFVTSHSELTYLTFVYKVAAMDFIFKDDPAELRTRIIDCLETAHTRLQLLSKDNSVETIELKRGSNSVYVQYDDIMFFESSTKSHRLIAHLDNRQIEFYGNLKELSQLDDRFFRCHNSFVVNRHNIESIDSKERIVYFKNKEHCYASVRNVKKI
|
Required for high-level post-exponential phase expression of a series of secreted proteins.
|
Q5HEG2
|
Q65SE7
|
RECR_MANSM
|
Recombination protein RecR
|
Basfia
|
MQTSPLLENLIESLRCLPGVGPKSAQRMAYHLLQRDRSGGMNLARALTEAMSKIGHCEHCRTFTEEDICSICDNPRRQNSRLLCVVEMPADIQAIEQTGQFSGRYFVLMGHLSPLDGIGPREIGLDLLQRRLQQEQFNEVILATNPTVEGDATANYIAELCNQQNIKVSRIAHGIPVGGELETVDGTTLTHSFLGRRTIG
|
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
|
Q65SE7
|
Q06485
|
ATG33_YEAST
|
Autophagy-related protein 33
|
Saccharomyces
|
MSVCLAITKGIAVSSIGLYSGLLASASLITSTTPLEVLTGSLTPTLTTLKNAATALGAFASTFFCVSFFGAPPSLRHPYLLYGMLVAPLSSFVLGCASNYQSRKYSKVSKESSLFPEDSKLAASELSDSIIDLGEDNHASENTPRDGKPAATTVSKPAEALHTGPPIHTKNLIAATAIAIVGFVQAVIGVYGEGQFI
|
Involved in the selective degradation of mitochondria via autophagy during starvation and at post-log phase.
|
Q06485
|
A0T0W2
|
PSBA_THAPS
|
Photosystem II Q(B) protein
|
Thalassiosira
|
MIATLERREGVSLWERFCAWITSTENRLYIGWFGCLMFPTLLTATSCFIIAFIAAPPVDIDGIREPVAGSLLYGNNIISGAVIPSSNAIGMHFYPIWEAASVDEWLYNGGPYQLIVLHFLLGVASYMGREWELSYRLGMRPWIFVAFSAPVAAASAVFLVYPIGQGSFSDGMPLGISGTFNFMLVFQAEHNILMHPFHMAGVAGVFGGSLFSAMHGSLVTSSLIRETTENESTNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRALHFFLALWPVLGIWLTAMGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRADLGMEVMHERNAHNFPLDLASGDVLPVAFTAPAVNA
|
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
|
A0T0W2
|
Q8BLB0
|
ZFP3_MOUSE
|
Zinc finger protein 3
|
Mus
|
MGTEKKEGLPKEETSEDSKPHGQTVEKLAQEVCHGHEFGEASEEDMSEGHLRESSKEIIEKRYPQERHFASGLLIFKKSSSGEKTSENPRGFNPNPSVLCHGGAERASACAASGHNCLGSIELTKAQGPPVGEKPHTCKECGKAFNQNSHLIQHMRVHSGEKPFECKECGKTFGTNSSLRRHQRIHAGEKPFACTECGKAFIQSSHLIHHHRIHTGERPYKCEECGKAFSQNSALILHQRIHTGEKPYECNECGKTFRVSSQLIQHQRIHTEERYHECSECGKAFKHSSGLIRHQKIHTGEKPYLCNECGKGFGQSSELIRHQRIHTGDKPYECSECGKTFGQNSEIIRHIRIHTGEKPYVCKECGKAFRGNSELLRHERIHTGEKPYECFECGKAFRRTSHLIVHQRIHTGEKPHQCNECARTFWDNSELLLHQKIHIGEKPYECSECEKTFSQHSQLTIHQRIHTGEKPYECQECQKTFSRSSHLLRHQSVHCSE
|
May be involved in transcriptional regulation.
|
Q8BLB0
|
Q3K7L0
|
SYM_PSEPF
|
Methionyl-tRNA synthetase
|
Pseudomonas
|
MSEPRKILVTSALPYANGSIHLGHMLEYIQTDMWVRFQKHRGNQCIYVCADDAHGSAIMLRAEKEGITPEQLIANVQAEHSADFAEFLVDFDNFHSTHAEENRELSSQIYLKLRDAGHIAQRSITQYFDPEKKMFLADRFIKGTCPKCGTEDQYGDNCEKCGATYAPTDLKDPKSAISGATPVLKDSQHFFFKLPDFQEMLQAWTRSGTLQDAVANKIAEWLDAGLQQWDISRDAPYFGFEIPGEPGKYFYVWLDAPIGYMASFKNLCNRTPELDFDAFWGKDSTAELYHFIGKDIVNFHALFWPAMLEGAGFRKPTGINVHGYLTVNGQKMSKSRGTFIKARTYLDHLSPEYLRYYYAAKLGRGVDDLDLNLEDFVQKVNSDLVGKVVNIASRCAGFIQKGNAGLLVDTNAAPELTEAFLAAAPSIADAYEARDFARAMRETMALADRANAWIADKAPWSLNKQEGKQDEVQAVCATAINLFRQLVIFLKPVLPVLAADAEAFLNVAPLTWNDHTTLLANHQLNEFKPLMTRIDPVKVQAMTDASKEDLTASQTDTGAAAPAGNGELAKDPLSPEIDFDTFAAVDLRVALIVKAEHVEGADKLLRLTLDIGDEQRNVFSGIKSAYPDPSKLDGRLTMMIANLKPRKMKFGISEGMVMAAGPGGEEIYLLSPDSGAKPGQRIK
|
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
|
Q3K7L0
|
Q1RAM7
|
UVRC_ECOUT
|
Excinuclease ABC subunit C
|
Escherichia
|
MSDQFDAKAFLKTVTSQPGVYRMYDAGGTVIYVGKAKDLKKRLSSYFRSNLASRKTEALVAQIQQIDVTVTHTETEALLLEHNYIKLYQPRYNVLLRDDKSYPFIFLSGDTHPRLAMHRGAKHAKGEYFGPFPNGYAVRETLALLQKIFPIRQCENSVYRNRSRPCLQYQIGRCLGPCVEGLVSEEEYAQQVEYVRLFLSGKDDQVLTQLISRMETASQNLEFEEAARIRDQIQAVRRVTEKQFVSNTGDDLDVIGVAFDAGMACVHVLFIRQGKVLGSRSYFPKVPGGTELSEVVETFVGQFYLQGSQMRTLPGEILLDFNLSDKTLLADSLSELAGRKINVQTKPRGDRARYLKLARTNAATALTSKLSQQSTVHQRLTALASVLKLPEVKRMECFDISHTMGEQTVASCVVFDANGPLRAEYRRYNITGITPGDDYAAMNQVLRRRYGKAIDDSKIPDVILIDGGKGQLAQAKNVFAELDVSWDKNHPLLLGVAKGADRKAGLETLFFEPEGEGFSLPPDSPALHVIQHIRDESHDHAIGGHRKKRAKVKNTSSLETIEGIGPKRRQMLLKYMGGLQGLRNASVEEIAKVPGISQGLAEKIFWSLKH
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
Q1RAM7
|
B2IUT0
|
PYRG_NOSP7
|
UTP--ammonia ligase
|
Nostoc
|
MTKFIFVTGGVVSSIGKGIVAASLGRLLKSRGYSVSILKLDPYINIDPGTMSPFQHGEVFVTQDGAETDLDLGHYERFTDTSMSRLNCVTTGSIYQAVINKERRGDYNGGTVQVIPHITNEIKERILRVAKSTNPSVVITEIGGTVGDIESLPFLEAIRQFRKEVGRQHVLYMHVTLVPWIASAGEMKTKPTQHSVKELRSIGIQPDILVCRSDRPLPKGLKQKLSGFCDVPEECVITSQDAKSIYEVPLNLEREGMAEQVLNLLQMEQRQPDLTQWQTLVQRLHTPKHELEIAIVGKYVQLSDAYLSVVEALNHAAISTYGKLRLRWVNSEDLENESAETHLGGVDGVVVPGGFGVRGVDGKIAAIKYARDRQIPFLGLCLGMQCSVIEWARNIGGLTDANSAEFDPHTTNPVINLLPGQQEVVDLGGTMRLGLYPCRVLPDTLAFKLYQEDVIYERHRHRYEFNNAYRDLLLKSGYAISGTSPDGQLVEIVELPKHPFFLACQFHPEFQSRPSSPHPLFKGFIQAAIALSLSTSTTPTPLEVS
|
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
|
B2IUT0
|
C3MEN2
|
MRAY_SINFN
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Sinorhizobium
|
MLIWLVELADHFQFFNLFRYITFRTGAALFTSALIVFLFGPAIISSLRIRQGKGQPIRADGPQTHFKKAGTPTMGGLMILAGIVGSALLWADLSSIYVVSTLLVTLGFGAIGFYDDYLKVTKQSDKGFSGKARLGIEFVIAAIAVFFMMQAAQSAGSAGSTFGSSVTFPFFKDLMLNLGYFFVLFGGFVIVGAGNAVNLTDGLDGLAIVPVMIASAAFGLIAYLAGNAVFANYLQIHFVPGTGELAVILGAVIGAGLGFLWFNAPPAAIFMGDTGSLALGGLIGTVAVATKHEIVMVIIGGLFVIETLSVIIQVFWFKRTGRRVFLMAPIHHHFEKKGWTESQVVIRFWIIAVILAMVGLSTLKLR
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
C3MEN2
|
Q1QH78
|
DEF_NITHX
|
Polypeptide deformylase
|
Nitrobacter
|
MAIREIIILPDKQLRLVSRPIETVTPEIRKLADDMFETMYDAPGIGLAGIQIAQPLRIITMDLARRDEEGELTPRPRIFINPEILSASEELSTYEEGCLSIPEYYEEVERPARVRVRFTDLDGKVHEEDAEGIYATCIQHEIDHLNGVLFVDHISKLKRDRVVKKFTKAAKLAAK
|
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
|
Q1QH78
|
A0B738
|
DNAG_METTP
|
DNA primase DnaG
|
Methanothrix
|
MQSVDTTKYIIYADITADGIVERPDVVGAIFGQTEGLLGSDLDLRDLQKTGRLGRIDVQISSSGGKSMGTISIPSSFDKVETAILAAALETIDRVGPCMARIHVTKIEDVRAAKRKYIIDRAKRILVEMFDENLLETEQITEEIKQSVRVEEITYIGKDNLPAGPNVLDSDAILVVEGRADVLNLLKYGIKNAVAVGGTNIPPTITELCSKKIATAFTDGDRGGELIVKELLQVADIDYVARAPEGKCVEELTQKEIIRALRQKIPVEQVMDMYKIKPFTRKKREIVTKRKSLIRERPVSVRTVAQVVPIAHHAEIAPPHEIQTRVHQKEVHEHYEEPEIEGQEPEEWFKHHVEELDGTLTARLFDRNNNPIRDVAVRDLARELKESNGSVHGVIFDGVITQRLLDIAAEKGLDYLIGAKMGSIAKTPVGIKVITSGQ
|
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.
|
A0B738
|
A3PZG1
|
PAFA_MYCSJ
|
Pup-conjugating enzyme
|
unclassified Mycobacterium
|
MQRRIMGIETEFGVTCTFHGHRRLSPDEVARYLFRRVVSWGRSSNVFLRNGARLYLDVGSHPEYATAECDNLIQLVTHDRAGERVLEDLLIDAEQRLADEGIGGDIYLFKNNTDSAGNSYGCHENYLIVRAGEFSRISDVLLPFLVTRQLICGAGKVLQTPKAATFCLSQRAEHIWEGVSSATTRSRPIINTRDEPHADAEKYRRLHVIVGDSNMCESTTMLKVGTASLVLEMIEAGVPFRDFSLDNPIRAIREVSHDLTGRRPVRLAGGRQASALDIQREYYSRAVDYLQTREPNSQIEQVVDLWGRQLDAVESQDFAKVDTEIDWVIKRKLFQRYQDRYNMELSDPKISQLDLAYHDIKRGRGVFDLLQRKGLAARITTDEEIDAAVDTPPQTTRAKLRGEFISAAQEAGRDFTVDWVHLKLNDQAQRTVLCKDPFRSVDERVKRLIASM
|
Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine.
|
A3PZG1
|
A2BSQ0
|
PYRF_PROMS
|
OMP decarboxylase
|
Prochlorococcus
|
MNKRFNSEDKIILAIDGLDLSQAKLLLEKCPHVKWVKVGLELFVREGPRVIEILKGLNKKIFLDLKFHDIPNTMSAACFQVSKLGVDIISIHASAGLKALKDSKKASLEGATSVSVKPPFVVGITVLTSFSLKDFQTDLDRNNSIEENVLRLAKLSFDAGLDGCVCSPWEVKMLRSNYKNNFELITPGIRLNIDSKDDQNRIMTPHEAIDNGASKLVIGRSISKAIDPNMALIEIFKSIDSD
|
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
|
A2BSQ0
|
Q8DHY6
|
SPEA_THEVB
|
Biosynthetic arginine decarboxylase
|
Thermosynechococcus
|
MALTVTKTSNWTIEDSEQLYRIQGWGEPYFGINAAGHVTVSPKGDRGGSLDLYELVQALQQRNISLPLLLRFSDILEDRIERLNACFARAIARYGYQGAYKGVFPIKCNQQRHIIEALVRFGQSHQFGLEAGSKPELLIALAMLNTPGALLICNGYKDRSYIETAILARRLGHTSIIVLEQPEEVAEVIAVSQALGIEPIVGVRAKLSTQGVGRWGTSAGDRAKFGLTVPEILTAVEQLRAAGMLNALQLLHFHIGSQISAISVIKDAIREAGQIYGELVRLGANMQYLDVGGGLGVDYDGSKTNFHASKNYSMQNYASDVVAGIKDACRQRGIPDPTLISESGRAIASHQSVLIFNVLGVSEVPKITPEPATAEEHLIIRNLYDTYQAIDENNYQEAYNDALQFKGEAISLFNFGYLSLPERARAESLFWACCAKILGIARQQEYVPDDLEDLEKIMASIYYINLSVFQSVPDSWAIDQLFPIMPIHRLDEEPTERGILADLTCDSDGKIDQFIDLRDVKSVLELHPFRPGEPYYLGLFLNGAYQEIMGNLHNLFGDTNAVHIRLTPKGYEIEHLVRGDTMQEVLGYVQYQGDALLEKIRCRTEAALAEEQITLAEAQHLLENYERSLRSYTYLSS
|
Catalyzes the biosynthesis of agmatine from arginine.
|
Q8DHY6
|
B0S8M8
|
HPRK_LEPBA
|
HPr(Ser) kinase/phosphorylase
|
Leptospira
|
MPVPGITVETILRDHDDLQLQLVTGEVGLSNRINSAEINRPGLSLTGFFDFFANDRIQILGKGEWAYLNSLSEEKLGEITDKFFEFHLNCIIYTHGNEPQVPFVERAKEKGIPLFKTEIATHRFITLISQILDRALAPRTMRHGVLIEVFGIGTLLTGRSGVGKSETALELIERGHRLVADDMVEIRRLSESYLIGSCSDLLRHHMEIRGLGILNIKDLFGVGSVRDHKLIELIINLKEWEEQTSGDYERTGIEQSMEEILGVSVPYIEIPVKPGRNIPIIVETAAMNQRLRKMGKNSAKEFSNKLNTYIQQSSIETNPIKD
|
Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr).
|
B0S8M8
|
P71335
|
YBEY_HAEIN
|
Endoribonuclease YbeY
|
Haemophilus
|
MGSVLVDLQIATENIEGLPTEEQIVQWATGAVQPEGNEVEMTVRIVDEAESHELNLTYRGKDRPTNVLSFPFECPDEVELPLLGDLVICRQVVEREASEQEKPLMAHWAHMVVHGSLHLLGYDHIEDDEAEEMESLETQIMQGLGFDDPYLAEK
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
P71335
|
Q99220
|
OS9_YEAST
|
Protein OS-9 homolog
|
Saccharomyces
|
MQAKIIYALSAISALIPLGSSLLAPIEDPIVSNKYLISYIDEDDWSDRILQNQSVMNSGYIVNMGDDLECFIQNASTQLNDVLEDSNEHSNSEKTALLTKTLNQGVKTIFDKLNERCIFYQAGFWIYEYCPGIEFVQFHGRVNTKTGEIVNRDESLVYRLGKPKANVEEREFELLYDDVGYYISEIIGSGDICDVTGAERMVEIQYVCGGSNSGPSTIQWVRETKICVYEAQVTIPELCNLELLAKNEDQKNASPILCRMPAKSKIGSNSIDLITKYEPIFLGSGIYFLRPFNTDERDKLMVTDNAMSNWDEITETYYQKFGNAINKMLSLRLVSLPNGHILQPGDSCVWLAEVVDMKDRFQTTLSLNILNSQRAEIFFNKTFTFNEDNGNFLSYKIGDHGESTELGQITHSNKADINTAEIRSDEYLINTDNELFLRISKEIAEVKELLNEIVSPHEMEVIFENMRNQPNNDFELALMNKLKSSLNDDNKVEQINNARMDDDESTSHTTRDIGEAGSQTTGNTESEVTNVAAGVFIEHDEL
|
Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. The recognition of targets is N-glycan specific. Functions in recruiting misfolded protein substrates in conjunction with HRD3 .
|
Q99220
|
Q6CEW9
|
MRD1_YARLI
|
Multiple RNA-binding domain-containing protein 1
|
Yarrowia
|
MSRLIVKNLPPYLDEAGLKKHFSTVKDPKSAGFAPSDITDVKVVRARDGKTRRFGFVGFRSDETAEAAVKYFDTSFINSTKISVAVAMTFTDPNVPLSSRERKRQAAQRAREDAEDDREAKKARYLEKPMTIDDINGLGNASDPRLADYLDAMQVRSNAKTWANNDAGAVANEPQVIQSTASDDEYDEFTGKGDDEIDEDEDEEEESENKKDDDNEEAEEDEEDPVIEDGLAADPGVSDMDWLRQRQTRIKEGEPEEDRENRHTESKSEGKKGKGNAPKAATPVDEEPSEDPTIVSIRKTGRLFLRNLLYTAKEEDFRQLFSQYGELEEVHLPINTKTGQCKGFAHVQFEDPENAIAAYEAQDGKIFQGRLLHILPGKPKKDYNRLDEHDLKNLPLKKQQELKRKAEAAKQQFSWNSLYMNQDAVMESVAKSMGIKKSELIDPDSSDAAVKQALAEATVIGDVKSYFEKMGVDLASFDNKDRDDRVILVKNFPFGTTQPEIAEMFSEYGDLYKVMMPPAGTIAIVIFKHIPDARAAFAKLAFRRFKTSILYLEKGPKNLLPNEKMESDEVEHVKQDKIVTIEDKLSASDVMDTGSNDERPATASTSVFVKNLNFKTTSRVLTDAFKALDGFLVAQVKMKPDSKNKGKFLSMGFGFVEFSSKEAAEIAQKAMDGHVLDGHKLQLKISNRGQDEETTETKKAIDSKILIKNLPFEATKKDVQKLFGAFGSLKTVRVPKKFNSESRGFAFAEYVSAKEAEHAMSALQGTHLLGRRLVLQYAQADASNAEEEIERMQATVSKQAAQRSFADMKLAGEGKRRVDLEGEDEEEF
|
Involved in pre-rRNA processing.
|
Q6CEW9
|
Q8ZR95
|
COPA_SALTY
|
Soluble copper chaperone CopA(Z)
|
Salmonella
|
MSQTIDLTLDGLSCGHCVKRVKESLEQRPDVELADVTVTEAHVTGTASADALIETIKQAGYGATLSHPKAKPLTESSIPSEALAAVPHELPVATADEESQQLLLSGMSCASCVTRVQHALQSVPGVTQARVNLAERTALVMGSASAADLVQAVEKAGYGAEAIEDDIKRRERQQETAIATMKRFRWQAIVALAVGIPVMVWGMIGDNMMVTDDNRSLWLAIGLITLAVMVFAGGHFYRNAWKSLLNGTATMDTLVALGTGVAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPTARVVTEDGEKSVPLADVQPGMLLRLTTGDRVPVDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISAVFVPVVVAIALFSAAIWYFFGPAPQIVYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTLVFDKTGTLTEGKPQVVAIKTFNGVEEAQALRLAAALEQGSSHPLAHAILEKAGDDKLPQVNGFRTLRGLGVSGEAEGHQLLLGNQALLNEQHVATDDMTAEITAQASQGSTPVLLAIDGKAAALLAVRDPLRSDSIAALERLHNAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKADAIKRLQSQGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLRNMKQNLLGAFIYNSIGIPVAAGILWPFTGTLLNPVVAGAAMALSSITVVSNANRLLRFKPKA
|
Probably also encodes a cytoplasmic copper chaperone CopA(Z) that is produced by programmed ribosomal frameshifting (Probable).
|
Q8ZR95
|
Q47HR4
|
LEUC_DECAR
|
Isopropylmalate isomerase
|
Dechloromonas
|
MSKTLYDKLWENHVVHQEADGTALLYIDRHLIHEVTSPQAFEGLKLAGRKPWRVSSIVATPDHNTPTDHWEEGIKDPISRQQVETLDANIREVGALAYFPFKDQRMGILHVVGPENGATLPGMTVVCGDSHTSTHGAFACMAHGIGTSEVEHVLATQCLLQKRSKTMLVAVEGKLGKGVTAKDVALAIIGTIGTAGGTGYAIEFGGSAIRGLSMEGRMTLCNMAIEGGARLGFVAVDDTTINYLKGRPFSPTGETWDRAVAYWRTLHSDAGAQFDRVVTLRAEDIRPQVTWGTSPEMVVSVDAVVPDPAKEADPVKREGMERALQYMGLNPNTPINQIAIDKVFIGSCTNSRIEDLREAASVLKGRHVAANVKLALAVPGSGLVKRQAEAEGLDKVFVAAGFEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQGPGGRTHLVSPAMAAAAAIAGRFADVRDVL
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
Q47HR4
|
Q9UST6
|
SPC24_SCHPO
|
Kinetochore protein spc24
|
Schizosaccharomyces
|
MSDSPIELMRSTLAGFQIAPDVKTISNIQDIRAQIQSFREKELEGSQTKFKVLSRKLEISTQAMESLKQTAESSQHAEEILSREKEKFRIAKLLNITENEIMSLESQLQKMKEQLLQLEERENTSEDICQSEENANMLKLNFYHSLGFDLETAENTGNKRVIIHTENDLQTVQISNKYSPYFYSNYFWDLLDDSKDKK
|
Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
|
Q9UST6
|
Q2NB65
|
BIOB_ERYLH
|
Biotin synthase
|
Erythrobacter
|
MTPIRTNWSRDEIAALFEQPFTELLFQAATVHRAYHPPEQVQLCTLLSIKTGGCPEDCGYCSQSVKADSGVEATKLMDVQRVLQSAAQAKDAGSQRFCMGAAWRNPKDRDMPAIVEIVKGVRDMGLETCMTLGMLTPKQADMLKDAGLDYYNHNVDTGPEYYERVISTRNYQDRLDTLQNVRDAGINVCSGGIVGMGETREDRVGFVHTLATLERHPESVPVNALVPVKGTVLGDMLADTPLAKIDDIEFVRTVAVARITMPLSMVRLSAGRESMSEATQALCFMAGANSIFTGDKLLTAANAGDDKDAALFDKLGLTALQGEEPLRRAKDEAGKAAIPAE
|
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
|
Q2NB65
|
Q64U25
|
SUCC_BACFR
|
Succinyl-CoA synthetase subunit beta
|
Bacteroides
|
MKVHEYQAKEIFSTYGIPVERHALCHTADGAVAAYHRMGVNRVAIKAQVLTGGRGKAGGVKLANNDRDVYQYAQTILEMTIKGYPVTKILLSEAVNIAAEYYISFTIDRNTRSVTLIMSAAGGMDIEEVARQSPEKIIRCSIDPLIGVPDYLAHKFAFSLFEQAEQANRMATIIQDLYKAFIEKDASLAEINPLVLTPVGTLLAIDAKMVFDDNALYRHPDLQKLSEPTEDEKLEAIAKERGFSYVRMDGEIGCMVNGAGLAMTTMDMIKLYGGNPANFLDIGGSSNPVKVIEAMRLLLDDKKVKVVFINIFGGITRCDDVAIGLLQAFEQIQTDIPIIVRLTGTNGNMGRELLRKNNRFQVAQTMEEATKMAIESLKKESI
|
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
|
Q64U25
|
Q1AWA3
|
AROE_RUBXD
|
Shikimate dehydrogenase (NADP(+))
|
Rubrobacter
|
MSVPRIDGETSLVGLIGHPVSHSLSPQMHNASFAALGLNYVYVPLDVPPEELEAGVRGLRALGFRGFNVTMPHKERVCALVDRLDEAARISGAVNTVAVEEDGSLLGMNTDGSGFLLACREAGVEPSGRVALVAGAGGAAAAVAVALLRAGLSELRIANRTPGRALGLRERLGGLGGRVEVFPLSGLAEAAGGADILVNATYLGMRAGDPLPFPEELLRPGVAVCDAVYRPGKSTALVRAARRRGLAAVPGELMLLYQGVEAQRAWTGVDPDVGAMRRALSGEG
|
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).
|
Q1AWA3
|
A5UFM4
|
UXUA_HAEIG
|
D-mannonate hydro-lyase
|
Haemophilus
|
MEQAWRWYGPKDPVSLSDIRQAGATGIVTALHHIPNGEIWRIEEIKKRKTEIENAGLSWSVVESVPVHEEIKTQTGNYQKWINNYKQTLRNLAQCGIDTVCYNFMPVLDWTRTDLAYELPDGSKALRFDHIAFAAFELHILKRPDAEKAYSQEEQVAARTYYDKMSEQDITQLTRNIIAGLPGAEEGYTLDEFQTQLDRYKDISSEKFRTHLAYFLNEIVPVAQEVGIKMAIHPDDPPRPILGLPRIVSTIEDMQWFVETQPLPANGFTMCTGSYGVRSDNDLVKMTEQFADRIYFAHLRSTQREDNPLTFHEAAHLEGDVDMFNMVKALLNEEYRRLNQGETRLIPMRPDHGHQMLDDLRKKTNPGYSAIGRLKGLAEFRGLEMALKKVYFNK
|
Catalyzes the dehydration of D-mannonate.
|
A5UFM4
|
Q88D32
|
YQGF_PSEPK
|
Putative pre-16S rRNA nuclease
|
Pseudomonas
|
MADLRLLLGFDYGSKQIGVAVGQVITGQARELCTLKAQNGVPDWAQVEKLIAEWKPDAIVVGLPLNMDGTPSEMSARAEKFARRLNGRFNLPVHTHDERLTTFEAKGERMARGGQRGSYRDNPVDAIAAALLLQGWLEANT
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q88D32
|
B1VPC1
|
RL9_STRGG
|
50S ribosomal protein L9
|
Streptomyces
|
MKIILTHEVSGLGTAGDVVDVKDGYARNYLVPRGFAIRWTKGGEKDVAQIRRARKIHEIATIEQANEIKAKLEGVKVRLAVRSGDAGRLFGSVTPADVAAAIKAAGGPDVDKRRVELGSPIKTLGGHQVSVRLHPEVAAKLGVEVVAA
|
Binds to the 23S rRNA.
|
B1VPC1
|
B5ZW36
|
RECR_RHILW
|
Recombination protein RecR
|
Rhizobium
|
MAKRVTGPEIEKLIQLLAKVPGLGPRSARRAALHLIKKKDQLLGPLSNAMGEAYDKVKICSRCGNVDTVDPCTVCTDTQRDQSIIIVVEDVSDLWALERAGAMNAAYHVLGGTLSPLDGIGPDDLNIRGLIDRIGEGGIRELIIAVNATVEGQTTAHYITDQLQGLNVKITRLAHGVPVGGELDYLDEGTLAAALRARTVI
|
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
|
B5ZW36
|
B2TTV4
|
DUT_SHIB3
|
dUTP pyrophosphatase
|
Shigella
|
MKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLDDAVELAPGDTTLVPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ
|
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
|
B2TTV4
|
Q6GFE8
|
SSPP_STAAR
|
Staphylopain A
|
Staphylococcus
|
MKRNFPKLIALSLIFSLSITPIANAESNSNIKAKDKRHVQVNVEDKSVPTDVRNLAQKDYLSYVTSLDKIYNKEKASYTLGEPFKIYKFNKKSDGNYYFPVLNTEGNIDYIVTISPKVTKDSSSSSKYTINVSSFLSKALNEYKDQQITILTNSKGYYVVTQNHKAKLVLKTPRLEDKKAKKTESIPTGNNVTQLKQKASVTMPTSQFKSNNYTYNEQYVNKLENFKIRETQGNNGWCAGYTMSALLNATYNTNKYHAEAVMRFLHPNLQGQQFQFTGLTPREMIYFGQTQGRSPQLLNRMTTYNEVDNLTKNNKGIAILGSRVESRNGMHAGHAMAVVGNAKLNNGQEVIIIWNPWDNGFMTQDAKNNVIPVSNGDHYQWYSSIYGY
|
Cysteine protease that plays an important role in the inhibition of host innate immune response. Cleaves host elastins found in connective tissues, pulmonary surfactant protein A in the lungs, and the chemokine receptor CXCR2 on leukocytes. Proteolytic cleavage of surfactant protein A impairs bacterial phagocytosis by neutrophils while CXCR2 degradation blocks neutrophil activation and chemotaxis. Additionally, promotes vascular leakage by activating the plasma kallikerin/kinin system, resulting in hypotension.
|
Q6GFE8
|
P28827
|
PTPRM_HUMAN
|
Receptor-type tyrosine-protein phosphatase mu
|
Homo
|
MRGLGTCLATLAGLLLTAAGETFSGGCLFDEPYSTCGYSQSEGDDFNWEQVNTLTKPTSDPWMPSGSFMLVNASGRPEGQRAHLLLPQLKENDTHCIDFHYFVSSKSNSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTFWPNFYQVIFEVITSGHQGYLAIDEVKVLGHPCTRTPHFLRIQNVEVNAGQFATFQCSAIGRTVAGDRLWLQGIDVRDAPLKEIKVTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGISNYAELVVKEPPVPIAPPQLASVGATYLWIQLNANSINGDGPIVAREVEYCTASGSWNDRQPVDSTSYKIGHLDPDTEYEISVLLTRPGEGGTGSPGPALRTRTKCADPMRGPRKLEVVEVKSRQITIRWEPFGYNVTRCHSYNLTVHYCYQVGGQEQVREEVSWDTENSHPQHTITNLSPYTNVSVKLILMNPEGRKESQELIVQTDEDLPGAVPTESIQGSTFEEKIFLQWREPTQTYGVITLYEITYKAVSSFDPEIDLSNQSGRVSKLGNETHFLFFGLYPGTTYSFTIRASTAKGFGPPATNQFTTKISAPSMPAYELETPLNQTDNTVTVMLKPAHSRGAPVSVYQIVVEEERPRRTKKTTEILKCYPVPIHFQNASLLNSQYYFAAEFPADSLQAAQPFTIGDNKTYNGYWNTPLLPYKSYRIYFQAASRANGETKIDCVQVATKGAATPKPVPEPEKQTDHTVKIAGVIAGILLFVIIFLGVVLVMKKRKLAKKRKETMSSTRQEMTVMVNSMDKSYAEQGTNCDEAFSFMDTHNLNGRSVSSPSSFTMKTNTLSTSVPNSYYPDETHTMASDTSSLVQSHTYKKREPADVPYQTGQLHPAIRVADLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLCGDTSVPASQVRSLYYDMNKLDPQTNSSQIKEEFRTLNMVTPTLRVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLNSG
|
Receptor protein-tyrosine phosphatase that mediates homotypic cell-cell interactions and plays a role in adipogenic differentiation via modulation of p120 catenin/CTNND1 phosphorylation . Promotes CTNND1 dephosphorylation and prevents its cytoplasmic localization where it inhibits SLC2A4 membrane trafficking. In turn, SLC2A4 is directed to the plasma membrane and performs its glucose transporter function .
|
P28827
|
Q6C7C3
|
SPC24_YARLI
|
Probable kinetochore protein SPC24
|
Yarrowia
|
MDPIDLLRDVAKSFSTNEEIASTERVSVDITRLSLFREAKLAEARDKLQDQIRQRDLCQESVAGDSTTSERTQHVHELEREKMRLARAINDLEETLNATQAATSKLNAELELVEKESQQPIESAVENDSSAALQLKLFRTLGVTFDAEKPEKYTKCMIRSNTTSNVATLDLNVKEYSGFFITNYIWDKL
|
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
|
Q6C7C3
|
Q7Y219
|
PMIR2_ARATH
|
Protein PLASTID MOVEMENT IMPAIRED 1-RELATED 2
|
Arabidopsis
|
MSVNDREDSSADLYNGQLLRDIKEVSKALYLTNGPQRPVLSLSPPVRSQSVSRTTEIGLVLSNKKKKSLVPWNWKKPLNAIAHFGQRRFDVCFLLHVHSIEGLPLNLDGTKLVVQWKRKDEVMTTQPSKVLQGTAEFEETLTHRCSVYGSKHGPHRSAKYQVKLFLIYVSPVDAPWLVLGKHWIDLTRILPLSLEEMEGTRSTRKWNTSFKLSGLAESAVLNLSFDYSVVTSSVCDSTSKNVMLRRVGSVPSMDHRSPPLDDGKVVNEVSPSLSLNLSQSIDFLYEKLGEQNPQRSTGTEVELGLETDKQAADSDDSGKGVETFQQERSGLEESNDPNTESSRIEIIDVHEILKDEDESVFEETYFIDQLSVAALKSEPSNLLPKHSVDGTPKSTFSSQVISESSESKSPSAMDDSTEKENFLEVKSSYKAAKISMTSLSLDDITESVANDFLNMLELEECSYVYTSDGEPTSPRESLLREFEKEAFASGNFLLDLNGEAEYVSDIDEKSNDFSFSASSLDVGENKREGKSQLLIDRRKAKVLEDLETETLLRECDFDDNSFDNSLCVCSDGFGSPIELPVDKGLDLLPLGDNIGPSVWTKGGGCIRSMNHLLFRESKEASQLIMQVSVPVVLVSELGSDILEILQIFAASGIEGLCSEVNALIPLEDIMGKTIHEVVDVTKFKRTGQDCSDKSKGVVVQKPPGQLHLCSSNEEFGSSMCPSNVPLEDVTSLAIDEIYILSIEGLKIQCSMSDQDPPSGIAPKPMDQSDALELIRFSLTLDEWLRLDQGMLENKDQDLASNGKGHTLRNKLTLALQVLLRDPSLNNEPIGASMLALIQVERSLDSPNSSLCSLAQEGRNKESFGYDTQLWRITEIGLAGLKIEPGADHPWCTKSQQQSGSRWLLANGTDKTIKCQASESKVIIVSNVQATRKRLDTLWSIISDRHHQEGDLSNSAASVPFTRNLDVIFSNEVTERS
|
Seems not necessary for chloroplast and nuclear photorelocation movements.
|
Q7Y219
|
Q9KTJ7
|
METQ_VIBCH
|
Probable D-methionine-binding lipoprotein MetQ
|
Vibrio
|
MKFSLKSLLTIAAAASTLILAGCGEKAVDNNKVKIGVMAGAEAQVAEVAAKVAKEKYNLDVELVTFTDYVTPNAALDDGSIDANAFQHKPYLDKQIADRGYKLAIVGNTFVYPIAGYSKQIKSVDELQDGARIAVPNDPTNLGRSLLLLQQQGLLKLREDVGLLATVRDIVENPKKLEILELDAAQLPRSLDDVALSIINTTYASSINLTPEKDGIFVENKESPYVNILVAREANVNAENVQNFKKAYQTDEVAKAASEIFQGGAVKGW
|
This protein is a component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system.
|
Q9KTJ7
|
Q589A5
|
NU2C_SILLA
|
NADH-plastoquinone oxidoreductase subunit 2
|
Silene sect. Melandrium
|
MIWHVQNENFILDSTRIFMKAFHLLLFDGSFIFPECILIFGLILLLIIDSTSDQKDIPWLYFISSTSLVMSITTLLFRWREEPMISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMALTEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKKDVRSNEATTKYLLMGGTSSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALIFITVGIGFKLSPAPSHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFACIVLFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGLPPLAGFFGKLYLFWCGWQAGLYLLVLIGLLTSVLSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSKNSIELSMIVCVIASTIPGISMNPIIAIAQDTLF
|
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory 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.
|
Q589A5
|
Q2NEK1
|
RPO5_METST
|
DNA-directed RNA polymerase subunit H
|
Methanosphaera
|
MKADILQHKLVPEHTILSEEEAQKVLDDLNVRLDQIPKILPTDPVVKAIDAKVGDILKITRKSETAGIFVAYRVVRD
|
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q2NEK1
|
A4XKL5
|
NTPPA_CALS8
|
Nucleotide pyrophosphatase
|
Caldicellulosiruptor
|
MKKVVLASSSPRRIELLKQFGIKFDIVPSNVDEIIDPDLPPEKNAMNLAKKKAEEVFRRLGESAKDSLIISADTIVFIEGTILGKPSNEEEAFYMLKKISAKRHTVFTGVCIIDDSCRQILVDFEKSYVYIKQMSDEEILRYIKTGEPFDKAGAYAIQGFGSLIVEKVEGCFYNVVGLPLYKLNTMLQKLGYDLMKGEL
|
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
|
A4XKL5
|
O84771
|
MIAA_CHLTR
|
Isopentenyl-diphosphate:tRNA isopentenyltransferase
|
Chlamydia
|
MFKRTVILLAGPTGSGKTAVSLKLAPLVDGEIISVDSMQVYQGMDIGTAKVSLTDRKEVPHHLIDVCHVQESFNAVDFYYHAVQACQDILSRNKVPILVGGTGFYFHTFLSGPPSGPSPDFVLREQLTLEAQERGISALYQELELLDPVYAATITKHDKNKIIRALEIIRKTGSKVSSYAWQSTVNESKEYHCRRWLLSPDPELLRHNILERCDQMLEEGLLDEVQALLAAGIKGNSSASRAIGYREWIEFLDLGSPPDLFEITKQKFITNTWRYTKKQRTWFKRYSLFRELRPMGMTLDDMAKKIAQDYFLCG
|
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
|
O84771
|
P25047
|
DNRI_STRPE
|
Regulatory protein DnrI
|
Streptomyces
|
MQINMLGPLVAHHNGTSVTPIARKPRQVFSLLALQAGTVVPVPALMDELWGTQPPASALTTLQTYILQVRRGITVALGASHNGPAKDVLRTCYGGYLLDVDPTNTDVYAFERLAEEGKRACERGELDLASARFRQALDLWRGDALVDVHAGMRIGMEVARLEESRLGVLEARMETDLRLGRHAGLLPELSALTARHPMHENLWAQFMIALHRSGRTSQALEAFIKLRKTLVNELGVEPSARLQHLQHAILRADPGIDRNGPEVPAAASVALA
|
May form, with DnrJ a two-component regulatory system for daunorubicin biosynthesis genes.
|
P25047
|
B0BUD7
|
MUKF_ACTPJ
|
Chromosome partition protein MukF
|
Actinobacillus
|
MQNELAQTIPELINWTKEREFSLSLSSDRLAFLLAISIYNNEQTDGELLESDLIDLFRYVSEVFDQSEATLTQRANNAINDLVKQRFLNRFSSEFTEGLAIYRITPLGVGVADYYVRQREFSTLRLSIQLSIVADEIQRASSAAEEGGDERFWRNNVFAPLKYSVAEIFDSIDLSQRMMDENQHQIRERIAELLSQNWHEAILSCEQLLDETSGNLRELQDTLNAAGDKLQAQLLRIQSCLIGRDDLDFVDQLIVNLQNKLDRIISWGQQAIDLWIGYDRHVHKFIRTAIDMDKNRVFGQHLRQSIQDYFNAPWLLYTAKAESLLDLRDDETMLNEAEAVGELPSELEYESLSDVQEQIISVMQAHLAPFRAEGKPIDLGAVLREQLALYPQSRHFDVARIIVDQAVKLGMASLDSQAVYPEWQAINDNGAEVQANVIDQYNK
|
Involved in chromosome condensation, segregation and cell cycle progression. May participate in facilitating chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division. Not required for mini-F plasmid partitioning. Probably acts via its interaction with MukB and MukE. Overexpression results in anucleate cells. It has a calcium binding activity.
|
B0BUD7
|
Q5R931
|
RL10_PONAB
|
Ribosomal protein L10
|
Pongo
|
MGRRPARCYRYCKNKPYPKSRFCRGVPDAKIRIFDLGRKKAKVDEFPLCGHMVSDEYEQLSSEALEAARICANKYMVKSCGKDGFHIRVRLHPFHVIRINKMLSCAGADRLQTGMRGAFGKPQGTVARVHIGQVIMSIRTKLQNKEHVIEALRRAKFKFPGRQKIHISKKWGFTKFNADEFEDMVAEKRLIPDGCGVKYTPNRGPLDKWRALHS
|
Component of the large ribosomal subunit. Plays a role in the formation of actively translating ribosomes. May play a role in the embryonic brain development.
|
Q5R931
|
Q1ACF2
|
RK21_CHAVU
|
50S ribosomal protein L21, chloroplastic
|
Chara
|
MNTNTYAIIQMGGQQLQVQTGRFYDTCDFSILKPDTKIIIYKVTMIHLNSQLVIGKPWLHNAMIKGRILHSYRDNKVTIYRMHSKKKMRRKQGHRQNITRFIVDGIFLDGKNI
|
This protein binds to 23S rRNA.
|
Q1ACF2
|
P42206
|
GUDD_PSEPU
|
Glucarate dehydratase
|
Pseudomonas
|
MEALNQSQAATGAPVITDLKVVPVAGHDSMLLNLSGAHGPLFTRNILILTDSSGHVGVGEVPGGEGIRKTLEDARHLLINQSIGNYQSLLNKVRNAFADRDVGGRGLQTFDLRIAVHAVTAVESALLDLLGQHLQVPVAALLGEGQQRDAVEMLGYLFYVGDRNKTDLGYRSEHEADNEWFRLRNKEALTPESVVALAEAAYDRYGFKDFKLKGGVLRGEDEIAAVTALSERFPDARITLDPNGAWSLKEAVALCRDQHHVLAYAEDPCGAENGYSGREVMAEFRRSTGLRTATNMIATDWRQMGHAIQLQSVDIPLADPHFWTMQGSVRVAQMCNEWGLTWGSHSNNHFDISLAMFTHVAAAAPGNITAIDTHWIWQDGQRLTKEPLQIKGGLVEVPKKPGLGVELDWDALMKAHEVYKSMGLGARDDATAMRYLVSGWEFNNKRPCMVR
|
Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-glucarate (5-kdGluc).
|
P42206
|
A4YAR8
|
MSCL_SHEPC
|
Large-conductance mechanosensitive channel
|
Shewanella
|
MSLIKEFKAFASRGNVIDMAVGIIIGAAFGKIVSSFVADVIMPPIGIILGGVNFSDLSIVLQAAQGDAPSVVIAYGKFIQTVIDFTIIAFAIFMGLKAINTLKRKEEEAPKAPPAPTKEEELLSEIRDLLKAQQEK
|
Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
|
A4YAR8
|
Q9SG12
|
CAMK6_ARATH
|
Calcium/calmodulin-dependent protein kinase CRK6
|
Arabidopsis
|
MGHCYSRNISTVDDDDEIPSATAQLPHRSHQNHHQTSSSSSIPQSPATSEVNPYNISPFQSPLPAGVAPSPARTPGRKFKWPFPPPSPAKPIMAALRRRRGTAPHPRDGPIPEDSEAGGSGGGIGERLDKNFGFAKNFEGKYELGREVGRGHFGHTCWAKAKKGKIKGQTVAVKIISKSKMTSALSIEDVRREVKLLKALSGHSHMVKFYDVFEDSDNVFVVMELCEGGELLDSILARGGRYPEAEAKRILVQILSATAFFHLQGVVHRDLKPENFLFTSKNEDAVLKVIDFGLSDYARFDQRLNDVVGSAYYVAPEVLHRSYSTEADIWSIGVISYILLCGSRPFYGRTESAIFRCVLRANPNFDDLPWPSISPIAKDFVKRLLNKDHRKRMTAAQALAHPWLRDENPGLLLDFSIYKLVKSYIRASPFRRAALKSLSKAIPEEELVFLKAQFMLLEPEDGGLHLHNFTTALTRYATDAMIESRLPDILNMMQPLAHKKLDFEEFCAASVSVYQLEALEEWEQIATVAFEHFESEGSRAISVQELAEEMSLGPNAYPLLKDWIRSLDGKLNFLGYAKFLHGVTVRSSSSRPMR
|
May play a role in signal transduction pathways that involve calcium as a second messenger.
|
Q9SG12
|
Q5PHH8
|
DMSD_SALPA
|
Twin-arginine leader-binding protein DmsD
|
Salmonella
|
MTTFLQRDDFAVTARVLGALFYYSPESHETAPLVQALLNDDWQAQWPLDAEALAPVAVMFKTHSEESLPQAWQRLFIGPYALPSPPWGSVWLDRESVLFGDSTLALRQWMRENGIQFEMQQNEPEDHFGSLLLLAAWLAENGRHHECEQLLAWHLFPWSSRFLDVFIDHAGHPFYQALGQLARLTLAQWQAQLIIPVAVKPLFR
|
Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding-maturation pathway for the substrate protein.
|
Q5PHH8
|
A6KY05
|
G1092_PHOV8
|
Glycosyl hydrolase family 109 protein 2
|
Phocaeicola
|
MKRPNVLNLTCPAIPVVRIGFVGLGNRGILALERYMHLEGIEVKALCDLRKENIERAEHILREFGRPEAENYSEEGMWRKMCECKEIDLIYICTDWLTHTDIAVYALQQGRHVALEVPAAMSVADCWRLVDTAEETRRHCMMLENCCYDAFALTTLNMVQQGVLGEITHAEGAYIHDLRKHYFADEKAGGYHNHWIKLYSQQHTGNPYPTHGLGPVCQWMNIHRGDRMEYLVSMSSRQAGLSAYAGQVFGASSEEAAQSYEMGDVNTTLIHTAKGRTILLQYDVTTPRPYSRHQTVCGTKGFMQKYPVPCLLLDEYGKEPLSGEQFERMMEQYKHPFTAVIGEEARRKNMPNEMNYIMDYRLIHCLRNGLPLDQDVYDAAEWSCITELSERSVRQGSVPVEIPDFTRGNWKER
|
Glycosidase.
|
A6KY05
|
Q9RXZ8
|
RISB_DEIRA
|
6,7-dimethyl-8-ribityllumazine synthase
|
Deinococcus
|
MQRIEATLLAHDLKFALVSTRWNHLIVDRLVEGAELAFVQHGGKTENLDHFLVPGSYEVPLVARRLAETGRYDAVVCLGAVIKGDTDHYDFVAGGAANGILNTSLHTGVPVAFGVLTTDTVEQALNRAGIKAGNKGGEAVLAMIETANLLKQIER
|
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
|
Q9RXZ8
|
A0QL48
|
RPOC_MYCA1
|
Transcriptase subunit beta'
|
Mycobacterium avium complex (MAC)
|
MLDVNFFDELRIGLATAEDIRQWSYGEVKKPETINYRTLKPEKDGLFCEKIFGPTRDWECYCGKYKRVRFKGIICERCGVEVTRAKVRRERMGHIELAAPVTHIWYFKGVPSRLGYLLDLAPKDLEKIIYFAAYVITSVDEEMRHNELSTLEAEMMVERKAVEDQRDADLEARAQKLEADLAELEAEGAKADARRKVRDSGEREMRQIRDRAQRELDRLEDIWNTFTKLAPKQLIVDENLYRELVDRYGEYFTGAMGAESIQKLIENFDIDAEAEQLRDVIRNGKGQKKLRALKRLKVVAAFQQSGNSPMGMVLDAVPVIPPELRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLIDLGAPEIIVNNEKRMLQESVDALFDNGRRGRPVTGPGNRPLKSLSDLLKGKQGRFRQNLLGKRVDYSGRSVIVVGPQLKLHQCGLPKLMALELFKPFVMKRLVDLNHAQNIKSAKRMVERQRPQVWDVLEEVIAEHPVLLNRAPTLHRLGIQAFEPMLVEGKAIQLHPLVCEAFNADFDGDQMAVHLPLSAEAQAEARILMLSSNNILSPASGRPLAMPRLDMVTGLYYLTTEVEGDKGEYRPAAKDTPEVGVYSSPAEAIMAADRGVLSVRAKIKVRLTQLRPPAEIEAELFGANGWQPGDAWMAETTLGRVLFNELLPVGYPFVNKQMHKKVQASIINDLAERYPMIVVAQTVDKLKDAGFYWATRSGVTVSMADVLVPPRKKEILDQYEERAEKVEKQFQRGALNHDERNEALVEIWKEATDEVGQALREHYPADNPIITIVDSGATGNFTQTRTLAGMKGLVTNPKGEFIPRPVKSSFREGLTVLEYFINTHGARKGLADTALRTADSGYLTRRLVDVSQDVIVREHDCETERGIVVELAERQPDGTLIRDPYIETSAYARTLGTDAVDEAGNVIVARGEDLGDPEIDALLAAGITSVKVRSVLTCTTGTGVCATCYGRSMATGKLVDIGEAVGIVAAQSIGEPGTQLTMRTFHQGGVGEDITGGLPRVQELFEARIPRGKAPIADVTGRVRLEDGERFYKITIVPDDGSEEVVYDKLSKRQRLRVFKHEDGSERVLSDGDHVEVGQQLMEGSADPHEVLRVQGPREVQIHLVREVQEVYRAQGVSIHDKHIEVIVRQMLRRVTIIDSGSTEFLPGSLIDRAEFEAENRRVVAEGGEPAAGRPVLMGITKASLATDSWLSAASFQETTRVLTDAAINCRSDKLNGLKENVIIGKLIPAGTGINRYRNIQVQPTEEARAAAYTIPSYEDQYYSPDFGQATGAAVPLDDYGYSDYR
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
A0QL48
|
C5CNB2
|
ATPG_VARPS
|
F-ATPase gamma subunit
|
Variovorax
|
MAAGKEIRGKIKSVENTKKITKAMEMVSVSKMRKAQERMRAARPYSEKIRNIAANLGKANPEYTHAFMKKNEAKAIGFIIVTSDKGLCGGLNTNLLRAVTGKLREAQSAGIAIESVAIGSKGLGFLNRIGARVVAHVTHLGDTPHLDKLIGPVKTLLDAYAEGKLSAVYLCYTKFINTIKQEPLVEQLLPLAADSLQVEAGQHSWDYIYEPDAQSVIDELLVRYVESLVYQAVAENMASEHSARMVAMKAATDNAGNVINELKLVYNKTRQAGITKELSEIVSGAAAAAGV
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
|
C5CNB2
|
Q890Q7
|
RS13_CLOTE
|
30S ribosomal protein S13
|
Clostridium
|
MARIAGIDLPREKRVEVGLTYIFGIGTSSAKKILKETGVNPDIRIKDLSEEEVNLLRDYINQNLKVEGDLRRDVALDIKRLKEIGSYRGIRHRRGLPVRGQKTKTNARTRKGPKKLVVSRKKK
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
Q890Q7
|
Q00790
|
NOSR_PSEST
|
Regulatory protein NosR
|
Pseudomonas
|
MASREIWSLAGTFSTWVKGFFILLILSVCASSLQAKEYAAEQQRLDKFFPGASLSAAEGDYQVRTITKGDEVLGYAFQSIRVTDMPAYSGKPINMQILLDPEGVIVDAYMLEHHEPIVLIGIPEQKVHDFNANYSGIHVDQRVVVGRSSDKSAVTVDAVTGATVTVMVINEIVMRAAHTVAVDLGLVEAGATARPKPALVREDVFQPTSWTELVGNGAIRRMHLTRGQVDDAFKGTEAEGVDVAAAEQRDETFIDLYATHLNPPTIGRNLLGERQYADLMANLKPGEHAFAVLANGEYSFKGSGYVRGGIFDRVQLRQFGDTISFRDLDFIRLSDVYAEGMPEFFEMAIFTAREQYRFDPGSPWNLELLVRRQVGPVESIFTSFEMPYVMPEEYIERVPLTAEELAAIEEANRPLWVNIWYQKSFQVGVILVALALLTVILFLQDKFTQHPNFLKRLRHGYLVFTVVFIGWYALGQLSVVNVLTFVHALVQDFRWELFLTDPVIFILWVFTAASILLWGRGVFCGWLCPFGALQELINEAARKLKIPQYDLPFSVHERLWAIKYIVLLVLFGISLESMMMAEKAAEIEPFKTAITLKFDRQWWFVAYAVFLLVINIFTRKVYCRYVCPLGAGLAITGRFRLFDWLKRRKECGNPCQICANECEVQAIHPDGHINHNECHYCLDCQMTYHNENKCPPLIAKNKRARRDKKAPAAPQLIPVQVVEP
|
Transcriptional activator of the nitrous-oxide reductase gene NosZ.
|
Q00790
|
Q67JV5
|
RL5_SYMTH
|
50S ribosomal protein L5
|
Symbiobacterium
|
MANLKTKYQQEVAPALQKQFNYKNVMMIPRLEKIVINVGLGEAVQNAKALDAAVADIAAIAGQRPVITRAKKSISSFKIRTGMPIGCKVTLRGERMWDFLEKLIYVALPRVRDFRGVSPKSFDGRGNYALGLKEQLLFPEIDYDKVDKIRGMDVIIVTTAKTDEEAKALLKGLGMPFAER
|
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
|
Q67JV5
|
Q9NBX5
|
GAGXE_DROME
|
Nucleic-acid-binding protein from transposon X-element
|
Sophophora
|
MNTLNETAAADESLDTAFLSSPQCAAPQRFQKIKRKSRASPETERKKPKSTIGKQGENPSATEPRYGGNSNRFGLLAHLTADKQVGNEIGDLYDQPSTSHQAAIAAAKRDAASAGTTSSAKRAQSKPPPIVMEGVDDVYLMMQSIENIVDLEKIEARASMSGVLRLYAADANTFRTIVNWLEIEEYEFHCYQLKEDRPYRVCVKGLHHSTLHHQIKDELEKIGHKVLDIHTPLRRNEPGTSKASPVNMFFLNIAAAANNKEILAVKALCHMRVVIEPLRKRNAIVQCHRCQQIGHTAKYCRKAHICVKCAGEHPAKDCTRPRIELCTCYNCGGQHPANYKGCSKLQAFLQRSRPRSGVAGRTEVSDRPTPRGLAGGKEIPSSRGGISYADVARGSIHHKQPMSLTHQQQKQKQQPYDGSPSRQRSRSRTRASRGTLQRSTDASSSIEAILQTLNENINSLRSIQEKQMELMMMMMKQQQQQSHQQGQIINLLTALQARQAP
|
Strongly basic protein that binds directly to retroviral RNA and may be involved in its packaging and in the reverse transcription process.
|
Q9NBX5
|
A6UZI8
|
RL3_PSEA7
|
50S ribosomal protein L3
|
Pseudomonas
|
MTIGVVGRKCGMTRIFTEEGVSIPVTVIEVEPNRVTQFKTEETDGYRAVQVTAGERRASRVTKAQAGHFAKANVAAGRGVWEFRLGEEQYAAGDQITVDLFQAGQMVDVTGESKGKGFAGTIKRWNFRGQDNTHGNSVSHRVPGSIGQCQTPGRVFKGKKMSGHLGAERVTVQSLEIVRVDAERNLLLVKGAVPGATGGDVIVRPAAKARG
|
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
|
A6UZI8
|
P59138
|
RR4_CYABU
|
30S ribosomal protein S4, chloroplastic
|
Cyathophorum
|
MSRYRGPRVRIIRRLGALPGLTNKTPQLKSSSITQSTSNKKISQYRIRLEEKQKLRFHYGITERQLLNYVRIARKAKGSTGEVLLQLLEMRLDNVIFRLGMFPTIPGARQLVNHRHILVNGPIVDIPSYQCKPQDFITIKNQQKSEAIISKNIEFYQKYKIPNHLTYNYLEKKGLVNQILDRESIGLKINELLVVEYYSRQA
|
With S5 and S12 plays an important role in translational accuracy.
|
P59138
|
O02218
|
LID1_CAEEL
|
Lipid droplet protein 1
|
Caenorhabditis
|
MAIATTKTALTTIMNWMTFTDDSKEQLKIVEGRLFQSCEVSYEAKYVPVRFKRGEVYTVTVRPREAENLNGEAIVFIPGLGAGVAMFTANFNSCAKNHAVHSFDPLGFGRSSRSRFSDDNAIAELEMVEVMEDWRKAMGIEKMYIIGHAFGGYLASAYALENPSRVAHLILVDPWGFAEKVETTEKLIKPYAWMSFLGGVAGYFNPFSPMRWMGPYAPAIVKKLRPDLLLRFPGLHDYDIYKYVYYLNLPNPTGETAFMNMTLPVGWAKRPMIKRFNGIDKNVGVSFIYGSKSWIDPGPAIDIQSTRENAYVDIKIVRGAGTHVYADDPAAFNEIVSDVVEGRLSNPSNDFEIEECCHSD
|
Acts coordinately with atgl-1 within the lipolytic cascade to distribute stored energy to tissues during nutritional deprivation.
|
O02218
|
C4K2E2
|
MDH_RICPU
|
Malate dehydrogenase
|
spotted fever group
|
MKQNPKISLIGSGNIGGTLAHLISLRELGDIVLFDVTEGVPQGKALDLMQAGTIAGSDIKIKGTNDYKDIEGSDAIIITAGLPRKPGMSRDDLISINTGIMKTVAANVKKYAPDAFVIVITNPLDVMVYVMLKESGLPHNKVIGMAGVLDSSRFNLFLAEEFKVSVSNVNSMVLGGHGDAMVPLARYSTISGVPIPDLIKMGLSSNENIEKIIDRTRNGGGEIVALLKTGSAYYAPAASAIEMLESYLKDKRQILTCAAHLQGEYGVHDLYVGVPIMIGKEGVLKVIELQLTAEEKALFDKSVEGVKKLIETIKEMIKSYY
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
C4K2E2
|
Q49WT0
|
HPS2_STAS1
|
D-arabino-3-hexulose-6-phosphate formaldehyde lyase 2
|
Staphylococcus
|
MELQLAIDLLNKEDAAELANKVKDHVDIVEIGTPIVINEGLPAVQHLNDNVDGVKVLADLKIMDAADYEVSQAVKFGADIVTILGVAEDASIKAAVDEAHKHGKQLLVDMIAVQDLEKRAKDLDDLGADYIAVHTGYDLQAEGQSPLESLRKVKSVISNSKVAVAGGIKPDTIKDIVAENPDLIIVGGGIANADDPVEAAKQCRDIVDAHTKA
|
Catalyzes the condensation of ribulose 5-phosphate with formaldehyde to form 3-hexulose 6-phosphate.
|
Q49WT0
|
P15754
|
LEP4_KLEPN
|
N-methyltransferase
|
Klebsiella
|
MVENIALLPEFAAQYPFLWGSFLFLSGLAFGSFFNVVIHRLPLMMEQAEGINLCFPASFCPQCREPIAWRDNIPLLGFLFLKGRSRCCGQPISPRYPLMELATGALFVLAGYLMAPGVPLLGGLILLSLLLILAAIDAQTQLLPDGLTLPLMWAGLLFNLSATYVPLAEAVVGAMAGYLSLWSVYWVFRLLSGKEALGYGDFKLLAALGAWLGWQALPQTLLLASPAA
|
Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
|
P15754
|
Q9XNM1
|
CYB_DICTO
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Dicrostonyx
|
MTIIRKKHPLIKIINHSFIDLPAPSNISSWWNFGSLLGLCLIIQILTGLFLAMHYTSDTATAFSSVTHICRDVNYGWLIRYVHANGASMFFICLFLHVGRGIYYGSYNMIETWNMGIILLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFIMPFIITALVLVHLLFLHETGSNNPSGLNSDADKIPFHPYYTIKDFLGALLLLMALMILVLFFPDILGDPDNYTPANPLNTPPHIKPGWYFLFVYAILRSIPNKLGGVLALILSILVLALMTFLHTSKQRGLTFRPITQTMYWILVSDLLILTWIGGQPVEYPFIIIGKVASIAYFTIIVILMPIAGMIENNILDLD
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q9XNM1
|
A4YK73
|
ACSA_BRASO
|
Acyl-activating enzyme
|
unclassified Bradyrhizobium
|
MSEKIYDVPAEWAKRAFVDDAKYQEMYASSIRDPNGFWAEQAKRVDWIHAPTKIENVSYAPGNISIKWFEDGVLNAAYNCIDRHLATRADQTAIIWEGDDPADSKHITYRQLHDEVCKMANILRNRNVKKGDRVTIYLPMIPEAAYAMLACARIGAIHSVVFAGFSPDSLAQRIKDCDSKVVITADEGLRGGRKVPLKANVDAALNKVDNVDWVVVVKRTGGKIEMNPTRDLWYHEAAEMVTTECPVEHMNAEDALFILYTSGSTGQPKGVLHTTGGYLVYASMTHQYVFDYHEGDVYWCTADVGWVTGHSYILYGPLANGAVTLMFEGVPNYPDNSRFWNVIDKHKVNIFYTAPTAIRALMQGGDGPVTKTSRESLRLLGSVGEPINPEAWEWYHRVVGDNRCPIVDTWWQTETGGILITPLPGATRLKPGSATRPFFGVVPEIVDADGNTLEGATEGNLCLTRSWPGQMRTVYGDHARFEMTYFSTYKGKYFTGDGCRRDADGYYWITGRVDDVINVSGHRMGTAEVESALVAHPKVSEAAVVGYPHDIKGQGIYAYVTLMAGETPSEELRKELVGWVRKEIGPIASPDQIQFSQGLPKTRSGKIMRRILRKIAEDEPGALGDTSTLADPAVVDDLVQHRQNRKEKQA
|
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
|
A4YK73
|
A8GKD1
|
G6PI_SERP5
|
Phosphohexose isomerase
|
Serratia
|
MKNINPSQTAAWQALQQHFEQMKDVQISDLFAQDKERFSKFSATFNDQMLVDYSKNRISAETLEKLQALAKETDLQSAIKSMFAGEKINRTEDRAVLHVALRNRSNTPIIVDGKDVMPEVNAVLAKMKQFCDRVIGGDWKGYTGKAITDVVNIGIGGSDLGPYMATEALRPYKNHLNMHFVSNVDGTHIAETLQPLNPETTLFLVASKTFTTQETMTNAHSARDWFLSTAGDQKHVAKHFAALSTNGKAVGGFGIDTANMFEFWDWVGGRYSLWSAIGLSIALSLGFDNFEQLLSGAHAMDQHFAQTPAEKNLPVLLALIGIWYNNFFGAETEAILPYDQYMHRFAAYFQQGNMESNGKYVDRNGNPVDYQTGPIIWGEPGTNGQHAFYQLIHQGTKLVPCDFIAPAISHNPLSDHHAKLLSNFFAQTEALAFGKSLEVVEAEFAAQGKTPEEVKHVAPFKVFEGNRPTNSILLREITPFSLGSLIALYEHKIFTQGAILNIFTFDQWGVELGKQLANRILPELAGDEAVSSHDSSTNALINRFKEWR
|
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
|
A8GKD1
|
Q4QNC1
|
TRMN6_HAEI8
|
tRNA m6A37 methyltransferase
|
Haemophilus
|
MSGFTFKQFHINQDSCAMKVGTDGILLGAWADVKHCKNILDMGSGTGLLTLMLAQRTEENCQIQAVELDPIAAKQAQENINNSVWKNRIQLTQADIQHFLQTTEQTFDLIVANPPYFEQGIACKNEERELARYTKQSHLNWLEWAATRLSENGKISFVLPYDAGKTLTKSTALFCIKQTNVITKIGKTPQRMLLTFAKQPEVLMQDQLVIYDADNQYTEAFIELTKDFYLKF
|
Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
|
Q4QNC1
|
B3PV77
|
NDK_RHIE6
|
Nucleoside-2-P kinase
|
Rhizobium
|
MAIERTFSMIKPDATKRNLTGAITKMLEDAGLRVVASKRVWMSRREAEGFYAVHKDRPFFGELVEGMTSGPTVVQVLEGEGAILKNREIMGATNPANADEGTIRKVHALSIGENSVHGSDAPETAAQEIKYWFSDTEIVG
|
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.
|
B3PV77
|
Q39J12
|
CH602_BURL3
|
Chaperonin-60 2
|
Burkholderia cepacia complex
|
MAAKDVVFGDSARSKMVEGVNILANAVKVTLGPKGRNVVLERSFGGPTVTKDGVSVAKEIELKDKLQNMGAQMVKEVASKTSDNAGDGTTTATVLAQSIVREGMKYVASGMNPMDLKRGIDKAVAAAVEELKKISKPCTTNKEIAQVGSISANSDTSIGDRIAEAMDKVGKEGVITVEDGKSLADELDVVEGMQFDRGYLSPYFINNPEKQVAVLDNPFVLLHDKKVSNIRDLLPVLEQVAKAGRPLLIIAEDIEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLEDIAILTGGQVIAEETGLTLEKATLAELGQAKRIEVGKENTTIIDGAGEAVNIEARVKQVRAQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGIVAGGGVALIRARTAIAALTGANADQNAGIKIVLRAMEEPLRQIVTNGGEEASVVVAAVAAGTGNYGYNAATGEYVDMVEAGVVDPTKVTRTALQNAASVAGLLLTTDAAVAELPKEDAPMPGGMPGGMGGMGMDM
|
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.
|
Q39J12
|
Q4D3B7
|
DRE21_TRYCC
|
Fe-S cluster assembly protein DRE2 homolog 1
|
Schizotrypanum
|
MSSTTTQAFSLKTRQAVDEDALLTEEDRVVKEATKGEDCTTRRRACKNCTCGRAELERKMLAEGKKVEMPQMPAGGCGNCAKGDAFRCATCPFLGQPAFDNTSDGKVKLNLTDDI
|
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
|
Q4D3B7
|
Q1QN16
|
RS8_NITHX
|
30S ribosomal protein S8
|
Nitrobacter
|
MSTHDPISDLITRIRNAQMRNKSKVSTPGSRMRANVLEVLKSEGYIRGYASVEHSSGRSELEIELKYFDGEPVIREIERISRPGRRVYASVKNLPRVKNGLGISVLSTPKGIMADHEARDANVGGEVLFTVF
|
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.
|
Q1QN16
|
O58497
|
Y763_PYRHO
|
Putative transcriptional regulatory protein PH0763
|
Pyrococcus
|
MKTFLTEQQIKVLVLRAKGLKQSEIAKILKTTRANVSILEKRALEKIEKAKNTLLLWEQINSKVNVNVKAGEDIFSVPEKLFKKADEAGVKVPYSTAEIIAFLVEHAPIENRLAKRDFVIFLDSKNRLRISDCLINLDEIEKK
|
Putative transcriptional regulator.
|
O58497
|
Q9Z810
|
Y542_CHLPN
|
Probable metal transport system ATP-binding protein CPn_0542/CP_0210/CPj0542/CpB0563
|
Chlamydia
|
MTIRILAEGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSAGKQTHSMIGWVPQHFSYDPCFPISVKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLHHTTNYFNKVFYMNKTLTSLADTSTLTDQFCCHPYKNQEFSCSPH
|
Part of an ATP-driven transport system CPn0541/CPn0542/CPn0543 for a metal. Probably responsible for energy coupling to the transport system.
|
Q9Z810
|
Q8PKY6
|
DER_XANAC
|
GTP-binding protein EngA
|
Xanthomonas
|
MLPLVALVGRPNVGKSTIFNALTRTRDALVHDQPGVTRDRNYGVCRLDEQQPFIVVDTGGIAGDEEGLAGATARQARAAAGEADLVLFVVDGREGASSLDDEILAWLRKLARPTVLVINKIDGTDEETVRSEFARYGFSDVVALSAAHRQGIDELLDEVGARLPEEGAGELLDNDPARVRIAFVGRPNVGKSTLVNRLLGEERMIASEVPGTTRDSIAVDLERDGRQYRLIDTAGLRRRGKVEEAVEKFSAFKTLQAIEQCQVAVLMLDATEGVTDQDATILGAILDAGRALVVAINKWDGQSDYQRAQAEDLLSRKLGFVNWAEAVRISALHGSGMRELFQAIHRAHASATHEFSTSEVNQALEIAYETNPPPSIRGHVSKLRYVHPGGANPPTFIVHGTRLKVLPESYKRYLENFFRKRFKLVGTPVRFIFREGANPYEGKKNPLSDRQVARKRRLMRHVKGK
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
Q8PKY6
|
C0MGX4
|
RECU_STRS7
|
Recombination protein U homolog
|
Streptococcus
|
MVNYPHNPICQKVTPLQKQQKHRQVDFANRGMSFEAAINATNAYYLAKGIAVIHKKPTPIQIVKVDYPRRSRAKIVEAYFKQASTTDYSGIYKGHYIDFEAKETRQKTAMPMKNFHAHQIEHMAAVLKQKGICFVLLHFATLKETYYLPAKALIDFYQIDRGNKSMPLDYIRKNGFEVKLGAFPQVPYLDIIEQKFLGGDYN
|
Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation.
|
C0MGX4
|
Q01NW3
|
PNP_SOLUE
|
Polynucleotide phosphorylase
|
Candidatus Solibacter
|
MHHIVEVDLGDRKITLETGKMAKQANGAVVVRSGDAVVLVTACMADQPKPSAGFFPLTVDYREYTYAAGKIPGGFIKREGRLSEKEVLTCRLIDRPIRPLFPEGFMNETQIIAMVLSADPEQDPNSLAIVGTAAALAISDIPFQYVMAGVRVGMRDGQYTANPTYTEGRASKLNIVVAGTEEGIVMVEAGAQEVSEAEVLGAIEFGHECCKKIAAGIRQLMKLCGKTKREFVSPVLDETIYAEVEKQARVDLTDALNTEKHEKLASYALVASVKKRTIEALPDEQKEQGAKCFDALKERIFRDDMLKKHRRPDGREFDQIRQITIETGVLPRVHGSTLFTRGETQALVTVTLGTKDDEQRIELLEPGEASKRFMLHYNFPPFSVGEVGFMRGAGRREIGHGALAERALTALIPGEDKFPYTMRVVSDTLESNGSSSMAAICGGSLALMQAGVPMTAHVGGVAMGLVMEGKDYAILTDIAGAEDHYGDMDFKVAGTRDGITGMQMDIKVPNITTAIMKEALEQARRGRLFILDKMYEAMPQANTAISQYAPRIYTLHIPTDKIRDVIGPGGKVIRGIIEQTGVKIDVEDDGTIHVASADEASANKAIQIISDLTATAEIGKTYLGKVVRLVDFGAFVEIFPGTDGLLHISEIAENRIKDVRDELKEGDQILVKCLALEGNKIKLSRKAVLKEQREKMKQGKE
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
Q01NW3
|
Q567V6
|
EIF3K_DANRE
|
eIF-3 p25
|
Danio
|
MATTFEQMRANVGKLLRGIDRYNPENLATLERYVDTQARENAYDLEANLAVLKLYQFNLAYFQTTVTAQILLKALTNLPHTDFTLCKCMIDQTHQEERPIRQILYLGNLLETCHFQSFWASLEENRDLIDGITGFEESVRKFICHVVGITYQNIEYRLLAEMLGDPLDTQVKVWMNKYGWTENEDGQIFIHNQEESVKPKNIVEKIDFESVSSIMATSQ
|
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
|
Q567V6
|
A0A0R4IMY7
|
TRPM2_DANRE
|
Transient receptor potential cation channel subfamily M member 2
|
Danio
|
MDEAALEPTLVQTLAVSTAKGGRYLSLSPSFQRCSLASWIKENIKKKECCFYVEDGREGICKCGYPKVQHCDEAIKPEDYMGEQWDKHRHVRETPTDAFGDISFGGLGQKTGKYVRVSSDTSCENLYQLMTEQWKLRSPNLLISVTGGAKNFYIKTHLKDKFRRGLIKVAQTTGAWILTGGTHAGVMKHVGMAVRDYTLSSGSMEGQIVVIGVAPWGVIHNRSTLIHPEGRFPAYYSLDEQGQGRLSCLDINHTHFLLVDDGTQGHYGVEIELRARLEKLISKLSLGNRESGVTIPVVCVVLDGGPGTLNTIYNSMLNHTPCVVLEGSGRLADVIAHVASVPVSKVTMALINRLLKRFFMQEYKNFTELQIIEWTKKIQDILRMPHLLTVFRIDEDKNYDVDVAILQALLKASRSDEHAGRHCWERQLELAVAWNRVDIAESEIFTEESQWTSSDLHPAMFSALVGDKPEFVRLLLENGVCVREFLEREETLCELYSHLPSCFFLRKLAKRVQGGKMRRGQEPLPGSRKVCLSHVSEEVRHLLGSFTQPLYIASRYKPTKDDVRLKVPSKGALDLPCSGEEWSADTVWDPGRDLFLWAVVQNNRELAEIGWEQCRDCIAAALAASKILRKLAQESGEDDSEEATEMLELANHYEKQAIGVFSECHSWDAQRAQKLLIRISPSWGRSTCLWLALEAHDKSFIAHSGVQALLTQIWCGELSVDNPHWKVLLCMIFFPLIYTGFLTFRRDEDIQRQAERTEQQKLAMESVFAGQSDGKIKRHLRGFSQKSELKPLNCSSRLMSFLKSPQVKFYWNIASYFGFLWLFAVVLMIDFQTSPSWRELLLYVWLTSLVCEEIRQLYHDFDGSGFRRKAKMYIKDLWNILDVLSIVLFIAGLICRLQASDTVFYIGKVILCIDFIIFCLRLMAIFSISRTLGPKIIIVRRMMLDLFFFMFLLSIWVVAYGVAKQGILIENEERLNWIIRGAVYEPYITIFGNFPTNIDNTLFDISSCSVNASDPLKPKCPMLNADNTPVFPEWLTIMMLCVYLLFANILLLNLLIAIFNYTFQEVQDNTDTIWKFQRYELIKEYHSRPALPPPFILLSHLILFIRGVFLRDLPQRHKNFRQELEQTEEEELLSWEAYMKDNYLASTRQDESQSVEHRIHDTAEKVGAMSELLEREQEMVSATMAKRLARLEEQVSESAKALRWIIDALKSQGCKSKVQPPLMRSKSSDRDDGDSSGQETDDEEAPHMFARQLQYPDSTVRRFPVPEEKVSWEVNFSPYQPPVYNQQDSSESDTSALDKHRNPGGRTGIRGKGALNTLGPNHILHPIFTRWRDAEHKVLEFLAVWEDAEKRWALLGGPAQPDEPLAQVLERILGKKLNEKTKTLLKAGEEVYKGYVDDSRNTDNAWVETSIITLHCDKNTPLMADLNHMVESSLSSHQPLQWREVSSDACRCSYQREALRQIAHHHNTYF
|
Nonselective, voltage-independent cation channel that mediates Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels. Functions as ligand-gated ion channel. Binding of ADP-ribose to the cytoplasmic N-terminal region causes a conformation change; the channel is primed but still requires Ca(2+) binding to trigger channel opening.
|
A0A0R4IMY7
|
O83225
|
RS3_TREPA
|
30S ribosomal protein S3
|
Treponema
|
MGQKVSPIGLRLGINKVWSSRWYAGPREYAALLHEDLRIRSMIRSFPECKNADIAEVEIVRHPQRVTVVMHTARPGVVIGAKGVNIEKIGAEVQKRLNKKVQIKVKEIKRMELNAYLVAQNVARQLTARVSFRKCLRQACAGTMKSGAQGVKIRVSGRLGGAEMSRTEEIKEGRTPLHTLRADIDYGFAEAHTTYGSIGVKVWLYSGMMYGNECRKDVGSLLRRSRRESGQKSDELVRDERTHAERG
|
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
|
O83225
|
Q160Y9
|
ZNUC_ROSDO
|
Zinc import ATP-binding protein ZnuC
|
Roseobacter
|
MSLVDVDGLSLRYGARTVLSRVSLSIAPGEIVTIVGPNGSGKTSLLRAIIGAVKPFQGRVTRGAGVTLGYVPQKLHIDETLPMTVARFLRLPGGASEAEIDQALAQAGVRDLSGSQLAQLSGGQFQRVMLARALIGKPDLLLLDEATQGLDQRGSASFYQQIEQVRRDTGCAVLMISHELHVVMSASDRVICLNGHVCCEGTPAVVASAPEYRALFGTGTGGALALYRHEHDHEHDHHDGCAHGQATEDRTEAAE
|
Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system.
|
Q160Y9
|
Q97U28
|
KDGA_SACS2
|
2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase
|
Saccharolobus
|
MGRQGNLEELWCLRMPEIITPIITPFTKDNRIDKEKLKIHAENLIRKGIDKLFVNGTTGLGPSLSPEEKLENLKAVYDVTNKIIFQVGGLNLDDAIRLAKLSKDFDIVGIASYAPYYYPRMSEKHLVKYFKTLCEVSPHPVYLYNYPTATGKDIDAKVAKEIGCFTGVKDTIENIIHTLDYKRLNPNMLVYSGSDMLIATVASTGLDGNVAAGSNYLPEVTVTIKKLAMERKIDEALKLQFLHDEVIEASRIFGSLSSNYVLTKYFQGYDLGYPRPPIFPLDDEEERQLIKKVEGIRAKLVELKILKE
|
Involved in the degradation of glucose and galactose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze the reversible cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-deoxygalactonate (KDGal).
|
Q97U28
|
Q5U2R0
|
MAT2B_RAT
|
Methionine adenosyltransferase II beta
|
Rattus
|
MVGREKELSIHFVPGCCQLVEEEVNIPSRRVLITGATGLLGRAVYKEFQQSNWHAVGCGFRRARPKFEQVNLLDSEAVHHLIHDFQPHVIVHCAAERRPDVVESQPDAASQLNVGASGNLAKEAAAIGAFLIYISSDYVFDGTNPPYTEEDIPSPLNLYGKTKLDGEKAVLENNLGAAVLRIPVLYGEVEKLEESAVTVMFDKVQFSNKSANMDHWQQRFPTHVKDVASVCRQLAEKRMLDPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVIGAQRPKNAQLDCSKLETLGIGQRTPFRIGIKESLWPFLIDKRWRQTVFH
|
Regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates MAT2A catalytic activity by changing its kinetic properties, increasing its affinity for L-methionine. Can bind NADP (in vitro).
|
Q5U2R0
|
Q9FYC1
|
CHX4_ARATH
|
Protein CATION/H+ EXCHANGER 4
|
Arabidopsis
|
MEFNGDRIPYLRDTWRDANMICGILPINPSSSGLWPSPKLPDPQANIEFWNYMFPHVQIIFLIVTILWQFFHFFLRRLGMIRFTSHMLTGILLSKSFLKENTPARKFLSTEDYKETLFGLVGACSYMMFWFLMGVKMDLSLIRSTGRKAVAIGLSSVLLSITVCALIFFLILRDVGTKKGEPVMSFFEIIFIYLIQCLSSFPVIGNLLFELRLQNSELGRLAMSSAVISDFSTSILSAVLVFLKELKDDKSRLGSVFIGDVIVGNRPMKRAGTVVLFVCFAIYIFRPLMFFIIKRTPSGRPVKKFYIYAIIILVFGSAILADWCKQSIFIGPFILGLAVPHGPPLGSAILQKFESVVFGTFLPFFVATSAEEIDTSILQSWIDLKSIVILVSVSFIVKFALTTLPAFLYGMPAKDCIALSLIMSFKGIFEFGAYGYAYQRGTIRPVTFTVLSLYILLNSAVIPPLLKRIYDPSRMYAGYEKRNMLHMKPNSELRILSCIYKTDDIRPMINLLEATCPSRENPVATYVLHLMELVGQANPVLISHRLQTRKSENMSYNSENVVVSFEQFHNDFFGSVFVSTYTALSVPKMMHGDICMLALNNTTSLIILPFHQTWSADGSAIVSDSLMIRQLNKSVLDLSPCSVGIFVYRSSNGRRTIKETAANFSSYQVCMLFLGGKDDREALSLAKRMARDSRITITVVSLISSEQRANQATDWDRMLDLELLRDVKSNVLAGADIVFSEEVVNDANQTSQLLKSIANEYDLFIVGREKGRKSVFTEGLEEWSEFEELGIIGDLLTSQDLNCQASVLVIQQQQQMI
|
May operate as a cation/H(+) antiporter.
|
Q9FYC1
|
C6E4P8
|
RS17_GEOSM
|
30S ribosomal protein S17
|
unclassified Geobacter
|
MSERGNRKTQVGVVVSDKMDKTAVVKVDRLVKHPVYNKYIKRSAKYKAHDMDNAAKIGDRVIIVETRPLSKDKRWKIRQIIESKA
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
C6E4P8
|
Q6FDH0
|
ASPD_ACIAD
|
L-aspartate dehydrogenase
|
Acinetobacter
|
MKQLMMIGFGAMASEVYAHLPQDLELKWIVVPERSVESVKQKVDRHIQVISDINQCDGAPDYVIEVAGQAAVKEHAKNVLAHGWNIGLISVGTLADSEFFTELQQTAEQNGAHLHLLAGAIAGIDGIAAAKEGGLEKVTYKGCKSPNSWRGSYAEQLIDLDQVHTVTMFYRGTAREAAQKFPANANVAATIALAGVGMDNTIVELTVDPDTTQNKHTIVAEGRFGQMTIEMVGVPLASNPKTSTLAALSVIRACRNSVEAIQI
|
Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
|
Q6FDH0
|
Q9V196
|
RL13_PYRAB
|
50S ribosomal protein L13
|
Pyrococcus
|
MRIINAEGLILGRLASRVAKMLLEGEEVVIVNAEKAVITGNREVIFSKYKQRTGLRTLTNPRRGPFYPKRSDEIVRRTIRGMLPWKTDRGRKAFKRLKVYVGIPKEFKDKQLETIVEAHVSRLSRPKYVTVGEVAKFLGGKF
|
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
|
Q9V196
|
A8G7R9
|
IBPB_SERP5
|
16 kDa heat shock protein B
|
Serratia
|
MRNYDLSPLLRQWIGFDKLASSMGGQEPQGFPPYNIEKSDDNHYRISLALAGFKQSELDIEVEGPRLTVRGKPTPSEKQVEYLHQGLVCKEFALTFTLAEHLQVSEAQFENGLLHIDLVRQVPEALQPQRIAIGTTPGLEAK
|
Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent.
|
A8G7R9
|
Q03HT1
|
DAPEL_PEDPA
|
N-acetyldiaminopimelate deacetylase
|
Pediococcus
|
MTIEPLNLVRIRRQFHESPELALKEFQTHALLLSVIRSLPQNLLEIKTIPELPTALLVRVAGSHPHRTIGYRADIDALPVNEKTGLDFASKTPGIMHACGHDIHMTVALGILEYFANHQPQDNLIFFFQPAEESHSGSVRAFNANIFTNQFRPNEFYGLHSTPTLPAGVIGCRMGTLFAGTTEVNLKLTGKGGHAAYPQDANDMVVAQAYLITQLQTIVARNVNPIEGGVLTLGKVSAGNVRNVIADQAVIEGTIRGLTQKMILLIQQRVQQICEGTAQAFNCQVEVKMNQGGYLPVENDPTLTHELIQFMQSDSAIKFKKTPPAMTGEDFGFLLSKFPGTMFWLGVGATSSLHSATFNPDERAIQLGIDAVIKFLQNRMSKGA
|
Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate.
|
Q03HT1
|
Q7UPT7
|
DEOC_RHOBA
|
Phosphodeoxyriboaldolase
|
Rhodopirellula
|
MADYQYHDVSKMIDHSLLPPTLTEADLDSGIDLAIAYEVASVCILPYYLKRCAAKLAGTGVKASTTIGFPHGGHTTAIKKAEAEQAIQDGCEELDFVVNISQVLSGGWDYVQNEIGEVTELTHAAGQKIKVIFENCYLQDEHKIRLCEICTELKVDWVKTSTGYGTGGATMDDLRLMRQHSGENVQVKAAGGVRDLATLLEVRALGASRCGASRTAEMLGEARKQLGMPAIEITATGSSGY
|
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
|
Q7UPT7
|
A2RLF5
|
RF2_LACLM
|
Peptide chain release factor 2
|
Lactococcus cremoris subsp. cremoris
|
MELSEIRNLLEGYSEKINGFRDSLDLDRLEEEIALLENDMAQPEFWNDQAAAQKVIDESNALKAKYDNYQAMNTMLEEAQTMLEMLQEEADEDMQVELEEMTTALGQKIESYELEIMLNQPYDHMNAVLEIHPGSGGTESQDWGSMLMRMYTRWGEAHGFKVEILDYQDGDVAGLKSVAIRFVGRNAYGFLRGEKGVHRLVRISPFDSANRRHTSFTSVDVMPELDDSIEVEVRDADVKMDTFRSGGAGGQNVNKVSTGVRLTHVPTGIVVQSTMDRTQYGNRDKAMAMLKSKLYQLEMDKKQAEVDELRGDQSEISWGSQIRSYVFMPYQLVKDTRTGYETGQISNVMDGEIDGFINAYLRWNL
|
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
|
A2RLF5
|
P09469
|
VATA_DAUCA
|
Vacuolar proton pump subunit alpha
|
Daucus sect. Daucus
|
MPSVYGDRLTTFEDSEKESEYGYVRKVSGPVVVADGMGGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKTIAKRSGDVYIPRGVSVPALDKDTLWEFQPKKIGEGDLLTGGDLYATVFENSLMQHHVALPPDAMGKITYVAPAGQYSLKDTVLELEFQGVKKQFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAEVLMDFPQLTMTLPDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEKFDSDFIDIRTKAREVLQREDDLNEIVQLVGKDALAETDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGMDGQKISYTLIKHRLGDLFYRLVSQKFEDPAEGEDVLVGKFKKLHDDLTSGFRNLEDETR
|
Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
|
P09469
|
A7MBP4
|
IFT46_DANRE
|
Intraflagellar transport protein 46 homolog
|
Danio
|
MASVAYICSLPVNTSRDQVSLATVHRLVFMERSERQKIQLTTNQPYDESFEVNAEEAASVHTPSPRQIVSRRTGRQKQSTMSGYAGEKLEEDTKRKKEPPPGPRGANKNDEEEDEDDDDDDDDDDSDDTESDEEEEEPGSAPEGAYDPADYEHLPVTGEIKELFQYITRYTPQTIELDHKLKPFIPDFIPAVGDIDAFLKVPRPDGKPDNLGLLVLDEPCTKQSDPTVLSLWLSENSKQHNVTEVKVKSIENPEKNPKAIDNWIESISELHRSKPPATVHYTRPMPDIDSLMQEWPSEFEELLGKVNLPTADIDCDLAEYVDMICGILDIPVYKNRIHSLHVLFTLYSEFKNSQHFKSATDGQKSDTPPASRSATAEIERLTLD
|
Forms part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. Plays a role in early embryonic development.
|
A7MBP4
|
Q6CJZ2
|
IPI1_KLULA
|
Pre-rRNA-processing protein IPI1
|
Kluyveromyces
|
MAKKTVRQQDFMKRKLKVGKPKQKPSNVTDTSFQMKRISLPSQTKISSGSNGKSAGNGTGVLDLNQEVIKRVSLLRHHSDVTRKETVLYFESMISRIIHLPSMNNLMQSSIPLMCDSSKQVRDELANLLDTIGKHDANVLKLQIRAITLYLNNAMTHIIAPIQRDSGMFVQVVLKYCADELVRHAWIKMLKGFFQVLGWTIVTQGNNKAKGKSISMGITSSSVLSMNKNKKHKNENLKAMLQFIRAGVLGAAAIGHEDRNPEQGNGANSVSPLLQQRYVPYMIPEFPQPYAYLKLFTRQFAKGELTSTGAETSSTDSGNMTLEELETLSCEDTHTRRMVFNQHFYPSIQRQLPALIKDGGECGRTAHSFSSTLEEILQITV
|
Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA.
|
Q6CJZ2
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.