PharMolix/UniProtQA huggingface dataset:
Protein: Y2929_MYCTU
Sequence: MIELSYAPDVAGRRSNWPKGSGVNTWTAIRWTFAEDSPYVGTGLERMASDTHGGGGGRPVTPPPPGMHHLGCSRGVLLISSQRDAGHKTCDPAAGGTLTSVLT
What are the official names of this protein?
Uncharacterized protein Rv2929.
Protein: GLMU_BRADU
Sequence: MTARSSLTIVLAAGEGTRMRSHLPKVLHPVAHQTLLAHVLTAAPKGTGTSLAVVIGPDHQAVADEARRIRPDAVTFVQAERLGTAHAVLAAREAIARGVDDLLIAFGDTPLISAETFARLRAPLANGAALAALGFRAADPAGYGRFIVEGDRLVAIREQADASADERKIDLCNAGVMAIDGRRALAILDKIGNANSKGEYYLTDAVEIVREQGWESVVIETSEDEVRGINTKAQLAEAESVMQARLRKAAMEAGVTLIAPETVYLSADTVFGKDVTIEPFVVIGPGVSIADGTVIHSFSHIVETTLGRNVSIGPYARLRPGTSLGDGARIGNFVETKAATLEAGVKVNHLSYIGDATVGANSNIGAGTITCNYDGFKKHKTIIGQGAFVGTNSSLVAPVKIGNGAYIGSGSVITRDVPDDAMALERNQQTIREGGAARYREMKTRGKKPEK
What is the function of this protein?
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc).  The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
What are the official names of this protein?
Bifunctional protein GlmU.
What is the protein family that this protein belongs to?
In the C-terminal section; belongs to the transferase hexapeptide repeat family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: YTH1_EMENI
Sequence: MAVDVGHVASQLVSTDRTREPGFDRFSFVPFLRKSYGFGLVTDVPVCKAYSEGHCPLGPACPDRHPTPSRVTTSTTTASGLAPSTTHGSLVCKHFLKGLCKKGMKCEYLHEYNLRRMPECQSFSRSGYCPNGDDCLYQHVREQARLPPCEHYDQGFCPLGPLCAKRHVRRRLCPYYVAGFCPEGPNCANAHPRWSENLPKPTIRVEKTEEELEHERNLIREEQEREREREREWRNERGRGGFGMRGRYRGRGRG
What is the function of this protein?
Component of the cleavage factor I (CF I) involved in pre-mRNA 3'-end processing.
What are the official names of this protein?
mRNA 3'-end-processing protein yth1.
What is the protein family that this protein belongs to?
Belongs to the CPSF4/YTH1 family.
What are the subcellular locations of this protein?
Nucleus.
Protein: SWC4_CANGA
Sequence: MSSSDIFDVLNIKQKSSSPNAASPSVPASGKSSKPQLTGMQRELYNLLGENEAPVVVQSMNRFKEKLASNAKPTPWSLANFKANEYLTLQHWVKGSRELIGEEPQESEFKKYDVHLTIPEFTEDEYNSFIPTSNAEENEKQNIGEKVEANGDSTDVNMTEEDTNDKVKESVPQDENKSTSDNKKNNEKWEYNEVKYLFDLCKKYDLRWFVIQDRYDYENSNRTLEDLKSKFYEVSKCYFKAKKPDDPMLQSLNYSKDKETQRKKYLERLLARSAAEIAEEEALIIESRKFEMAAKKTLAERETLLRLLDSPQSDISVAQYLTSNGMSQLYNSLLADKSRKRKIDSAVPENPWMKQQHQFAQQRQQMQQLQQKKLEKHDASATPGPATTVTATETSTNVTSAGSIPSGLQSPKKTKRQKLELQTALKRKSESEYAEQLLKIFNMDERKSLGVIAHGEKLSPGVFLRSAKITTFKPAIQNKIISTAQELGIPARPVMPTFEVVTEYEALLKKIATLLDIKKQIDKIEAGKQITK
What is the function of this protein?
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling.  Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A.  The NuA4 complex is also involved in DNA repair (By similarity).
What are the official names of this protein?
SWR1-complex protein 4.
What is the protein family that this protein belongs to?
Belongs to the SWC4 family.
What are the subcellular locations of this protein?
Nucleus.
Protein: ATAT_TETTS
Sequence: MEFNFIINKLVQLDQQGLGVYIPRASRSKVSSQQEQQLGQVLNTMGERSAIAQGLKQVITNYDKVQGTDQRVYIVAEGRTCQGFLKVGQKNLFYRDMMGNIKEIKPLCVLDFYVHESCQRQGYGKLLFEYMIQCEQTSPEKLAYDRPSPKLIAFLKKHYNLVKYIAQNNNFVVFDQYFRSDASSQNKQNQNTRSYSQPYSDYSSQIPTNYPQQQQQQSNSKSYPYKQENNIDLMQHSSSRNNKEFLNAGRAILSKEEIYKKDNLSQQNIENTLNNINNSQYSTKSQQQQQYQKDYQLDKYENNWGADKNIKKPPFPGQDRQLDKIQQKIQQTERELDVVNQQIIKQRQNLSQDPLTQNHRAQNVYNTNQFGTSPWAQTGFNYYSTSSSNYGNHYTYYKK
What is the function of this protein?
Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules.  Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity.  Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer.  Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules.  Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released.
What are the official names of this protein?
Alpha-tubulin N-acetyltransferase, Alpha-TAT, TAT, Acetyltransferase mec-17 homolog.
What is the protein family that this protein belongs to?
Belongs to the acetyltransferase ATAT1 family.
Protein: PDXT_BACAA
Sequence: MVKIGVLGLQGAVREHVKSVEASGAEAVVVKRIEQLEEIDGLILPGGESTTMRRLIDKYDFMEPLRTFAKSGKPMFGTCAGMILLAKTLIGYDEAHIGAMDITVERNAFGRQKDSFEAALSIKGVGEDFVGVFIRAPYVVDVADDVEVLSTHGDRMVAVKQGPFLAASFHPELTDDHRVTAYFVEMVKEAKMKKVV
What is the function of this protein?
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate.  The resulting ammonia molecule is channeled to the active site of PdxS.
What are the official names of this protein?
Pyridoxal 5'-phosphate synthase subunit PdxT, Pdx2, Pyridoxal 5'-phosphate synthase glutaminase subunit.
What is the protein family that this protein belongs to?
Belongs to the glutaminase PdxT/SNO family.
Protein: UPPP_TROWT
Sequence: MVLEAVLLGIVQGITEFLPISSTAHMYILAKLLNLHVPGRFFLSSVQLGTSFALILYFFKDVKGIISETSRSIYSFIQFGIRQKQGKRNEYTRLGLLLVTGTIPVVLLGFLLVRFVPDGFFSAARNLFTMGVALIVFGLLLGFADALFRRKKGNIFQITFIESVLIGAAQVFAIIPGVSRSGITITTARFLNFDRQLAVRFSFLLSLPVTFIGGMYGLVAGPDTDYYSLGYSLIGAIVSFVVGLLVVSALLRIISKTTFVLFVYYRVLFGLFLVIVSFF
What is the function of this protein?
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP).  Confers resistance to bacitracin.
What are the official names of this protein?
Undecaprenyl-diphosphatase, Bacitracin resistance protein, Undecaprenyl pyrophosphate phosphatase.
What is the protein family that this protein belongs to?
Belongs to the UppP family.
What are the subcellular locations of this protein?
Cell membrane; Multi-pass membrane protein.
Protein: RISB_HAEIE
Sequence: MKVLEGSVAAPNAKVAVAIARFNSFINESLLEGAIDALKRIGQVKDENITIVRTPGAYELPLVARRLAESKKFDAIVALGTVIRGGTAHFEYVAGEASSGLGKVAMDAEIPVAFGVLTTENIEQAIERAGTKAGNKGAEAALTALEMVNLIQQIDAA
What is the function of this protein?
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.
What are the official names of this protein?
6,7-dimethyl-8-ribityllumazine synthase, DMRL synthase, LS, Lumazine synthase.
What is the protein family that this protein belongs to?
Belongs to the DMRL synthase family.
Protein: DNAJ_METPB
Sequence: MSKRDYYEVLGVAKTASESELKVAFRKLAMVHHPDRNPGDKEAEIKFKEVNEAYQCLSDGEKRAAYDRFGHAAFSQGGAGGPGFGNEFGDFMSDIFENFFGDGRGAPGGGRGRGGAPGRERGADLRYNLEISLEEAFSGKTETIRIPTSIACEACSGTGAKAGSKPRTCSTCGGYGRVRAAQGFFAIERTCPNCHGRGEVVDDPCTACSGAGRVNRERTLSINVPAGVDDGLRIRLAGEGESGLRGGPSGDLYVFLSIKPHPFFQRDGADLFCRVPISMVTAALSGEITVPVIDGSQTQVRIPAGTQTAKQFRIKGKGMPVLRSREVGDLYIQVSVETPQNLTKRQRELLQEFDQSASDENHPESAGFFSKVRDFFVSGATRA
What is the function of this protein?
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion.  Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex.  GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle.  Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.  Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
What are the official names of this protein?
Chaperone protein DnaJ.
What is the protein family that this protein belongs to?
Belongs to the DnaJ family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: DADD_METTP
Sequence: MLIRSASIIRNGSLLKNIDILIEGNRISEVGRDLRPNDDEIIDARNMLAVPGLVNSHTHLAMTLLRGYADDMELIPWLQEKIWPLEARLKPSDVRAGVKLGCLELIRFGVTCYNDMYYFMDETAAATREMGIRGVLSGVLFDMRPEFINDVEPFIKKWRDDDLIKPAVGPHAVYTCSEETLLRAKDIAERYDVKIHIHLSETRDEVDTFVNQRHMSPVEYLENLGFLSERVVAAHCVWLTPRDIRILAERHVNVAHCPISNLKLASGIAPVATLIEHGVNVCLGTDGASSNNNLDIFEEMKVAAVVQKCSVGRSAILPADAVWRMATENAYKAFSLDMGIRRGALADLALINMRRPWFIPVTSMISHLVYSMSGEASYTICNGRVLMRDGVIEGEAKILDEAQRCYERLISEE
What is the function of this protein?
Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs.  Can also deaminate adenosine.  The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated.  Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions.  May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
What are the official names of this protein?
5'-deoxyadenosine deaminase, 5'-dA deaminase, 5'-methylthioadenosine deaminase, MTA deaminase, Adenosine deaminase, S-adenosylhomocysteine deaminase, SAH deaminase.
What is the protein family that this protein belongs to?
Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.
Protein: PP268_ARATH
Sequence: MISSVRNCGTIQRFCTTSISLLQKPVEENIVRISNQVMVKFDPNSHLRSLINAGNLRAARQVFDKMPHGDIVSWTSIIKRYVTANNSDEALILFSAMRVVDHAVSPDTSVLSVVLKACGQSSNIAYGESLHAYAVKTSLLSSVYVGSSLLDMYKRVGKIDKSCRVFSEMPFRNAVTWTAIITGLVHAGRYKEGLTYFSEMSRSEELSDTYTFAIALKACAGLRQVKYGKAIHTHVIVRGFVTTLCVANSLATMYTECGEMQDGLCLFENMSERDVVSWTSLIVAYKRIGQEVKAVETFIKMRNSQVPPNEQTFASMFSACASLSRLVWGEQLHCNVLSLGLNDSLSVSNSMMKMYSTCGNLVSASVLFQGMRCRDIISWSTIIGGYCQAGFGEEGFKYFSWMRQSGTKPTDFALASLLSVSGNMAVIEGGRQVHALALCFGLEQNSTVRSSLINMYSKCGSIKEASMIFGETDRDDIVSLTAMINGYAEHGKSKEAIDLFEKSLKVGFRPDSVTFISVLTACTHSGQLDLGFHYFNMMQETYNMRPAKEHYGCMVDLLCRAGRLSDAEKMINEMSWKKDDVVWTTLLIACKAKGDIERGRRAAERILELDPTCATALVTLANIYSSTGNLEEAANVRKNMKAKGVIKEPGWSSIKIKDCVSAFVSGDRFHPQSEDIYNILELAVSGAEAHRFDCTLKRAFGVNLYS
What are the official names of this protein?
Putative pentatricopeptide repeat-containing protein At3g47840.
What is the protein family that this protein belongs to?
Belongs to the PPR family. PCMP-E subfamily.
Protein: NOP16_SCHPO
Sequence: MANPRQRNKQRSGKPRLTRRNANKKAKAKIYGNFVIQQNWDKHATLRQNYARLGLLATPNYVTGGVEKLYPDPKRENEDRELTSEELDELKKSLPPGQAIVRRDDDGNIIEIIHGEAKTLDDVLDKEISIAPAKTEVVRQLEEEAVKKAARQSNKMLPLSAFEHAYIQRLINKYGTEDFESMAKDVKLNSKLFNGSKLKNLYIRMKATK
What is the function of this protein?
Involved in the biogenesis of the 60S ribosomal subunit.
What are the official names of this protein?
Nucleolar protein 16.
What is the protein family that this protein belongs to?
Belongs to the NOP16 family.
What are the subcellular locations of this protein?
Nucleus, nucleolus.
Protein: ATNL_EMENI
Sequence: MALPSSVESLLSTVWDFITINRLLTGAGIYFLLLNAKGLPGVWHYRLFKGLFIELVWKRSTTPAPLLDSQGRPRLYSYFVTECSNPVIECDYNLHKSNSTFFSDLDINRTQLMMTHFKHVLSTASMPRKTKTANGNGDDQKRKRPLMMAMGGVSCLFHREIKPLQRYEVWSRVLAWDEKWVYVVSYFVKKGSLSRDGNFKGDLDLDPKVNAKVVLASCMARYVFKEGRITVKPERVLQECGLFPLAEEAVAGEKAEKASVDSWGKEQFEEARQKGLVTAGKFSGLEVLPLMTGFGESGVLGRYNDF
What is the function of this protein?
Part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584).  The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol (PubMed:27310134).  The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584).  The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps (PubMed:27310134, PubMed:26563584).  First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ (PubMed:27310134, PubMed:26563584).  the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains (PubMed:27310134).  The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr (PubMed:26563584).  Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134).  After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide (PubMed:26563584).  Further reduction would generate aspercryptins (PubMed:27310134, PubMed:26563584).  The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version (PubMed:27310134).  AtnB seems to be involved in the selectivity for Ile versus Val by the third module (PubMed:26563584).  Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively (PubMed:27310134).
What are the official names of this protein?
Probable thioesterase atnL, Aspercryptin biosynthesis cluster protein L.
What is the protein family that this protein belongs to?
Belongs to the lcsJ thioesterase family.
Protein: TSAD_LACP3
Sequence: MAARELILAFESSCDETSVAVVENGDTILSNIIATQIKSHQRFGGVVPEVASRHHVEQITLVTDAALKEAGVTYDDLTAVAVTYGPGLVGALLIGVTAAKTIAYAHHLPLIPVNHMAGHIYAARFVKPLAYPLLALAVSGGHTELVYMRSAGEFEIIGDTRDDAAGEAYDKVGRILGIPYPAGKEVDRLAHLGQDTFHFPRAMDKEDNLDFSFSGLKSAVINTVHHAHQLGQELSREDLAASFQAAVVDVLVHKTQKALHQYPVKQLIVAGGVAANQGLKEAMNETLAVNFPDVDVIVPPLRLTGDNGAMIGAAAHIEWAKQHLASESLNADPGLSFTHAS
What is the function of this protein?
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.  Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB.  TsaD likely plays a direct catalytic role in this reaction.
What are the official names of this protein?
tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD, tRNA threonylcarbamoyladenosine biosynthesis protein TsaD.
What is the protein family that this protein belongs to?
Belongs to the KAE1 / TsaD family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: DRAG_RHORU
Sequence: MTGPSVHDRALGAFLGLAVGDALGATVEFMTKGEIAQQYGIHRKMTGGGWLRLKPGQITDDTEMSLALGRSLAAKGTLDVADICEEFALWLKSRPVDVGNTCRRGIRRYMHEGTTTAPYSEGDAGNGAAMRCLPAALATLGHPADLEPWVLAQARITHNHPLSDAACLTLGRMVHHLIGGRGMKACREEANRLVHQHRDFHFEPYKGQSSAYIVDTMQTVLHYYFVTDTFKSCLIQTVNQGGDADTTGALAGMLAGATYGVDDIPSGWLSKLDMKVEREIRRQVDALLALAGLD
What is the function of this protein?
Involved in the regulation of nitrogen fixation activity by the reversible ADP-ribosylation of one subunit of the homodimeric dinitrogenase reductase component of the nitrogenase enzyme complex.  The ADP-ribosyltransferase (DraT) transfers the ADP-ribose group from NAD to dinitrogenase reductase.  The ADP-ribose group is removed through the action of the ADP-ribosylglycohydrolase (DraG, this entry).
What are the official names of this protein?
ADP-ribosyl-[dinitrogen reductase] glycohydrolase, ADP-ribosylglycohydrolase, Dinitrogenase reductase-activating glycohydrolase, Mono-ADP-ribosylhydrolase.
What is the protein family that this protein belongs to?
Belongs to the ADP-ribosylglycohydrolase family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: ARF4_MOUSE
Sequence: MGLTISSLFSRLFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIQEGAAVLQKMLLEDELQDAVLLLFANKQDLPNAMAISEMTDKLGLQSLRNRTWYVQATCATQGTGLYEGLDWLSNELSKR
What is the function of this protein?
GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase.  Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
What are the official names of this protein?
ADP-ribosylation factor 4.
What is the protein family that this protein belongs to?
Belongs to the small GTPase superfamily. Arf family.
What are the subcellular locations of this protein?
Golgi apparatus. Membrane; Lipid-anchor.
Protein: D9_FOWPN
Sequence: MFDISREQQNMLEKNKDCVITFETNRERITIENTNIKDILSDRRIHIFALCITSDNIPIIGIRRTSFMYQSVISKRRSFSEILAVDINHLKYMYNNEIKEICIRSIVPFTYSGFNNFEELVLLGGRVKNKESIYQCLSRELSEESDGILTIKTFGNKILKLTIEDKILRRTFYGYCIVCFIDQLYSEIIKPLYNIEIKELGSLFDRSSNEKYEYLHFIYNTLLTYKYGGVL
What is the function of this protein?
Decapping enzyme required for the removal of the 5'-end m7GpppN cap tethered to viral and host mRNAs to allow their decay in cells.  May therefore accelerate viral and cellular mRNA turnover to eliminate competing host mRNAs and allow stage-specific synthesis of viral proteins.  Acceleration of the turnover of cellular transcripts may even promote the shutoff of host protein synthesis.  Does not cleave unmethylated RNAs or RNAs shorter than 24 nucleotides (By similarity).
What are the official names of this protein?
Putative Nudix hydrolase FPV054.
What is the protein family that this protein belongs to?
Belongs to the Nudix hydrolase family.
Protein: RMR2_ARATH
Sequence: MNRALVLLLYVCTVSCLASSKVILMRNNITLSFDDIEANFAPSVKGTGEIGVVYVAEPLDACQNLMNKPEQSSNETSPFVLIVRGGCSFEEKVRKAQRAGFKAAIIYDNEDRGTLIAMAGNSGGIRIHAVFVTKETGEVLKEYAGFPDTKVWLIPSFENSAWSIMAVSFISLLAMSAVLATCFFVRRHRIRRRTSRSSRVREFHGMSRRLVKAMPSLIFSSFHEDNTTAFTCAICLEDYTVGDKLRLLPCCHKFHAACVDSWLTSWRTFCPVCKRDARTSTGEPPASESTPLLSSAASSFTSSSLHSSVRSSALLIGPSLGSLPTSISFSPAYASSSYIRQSFQSSSNRRSPPISVSRSSVDLRQQAASPSPSPSQRSYISHMASPQSLGYPTISPFNTRYMSPYRPSPSNASPAMAGSSNYPLNPLRYSESAGTFSPYASANSLPDC
What is the function of this protein?
Involved in the trafficking of vacuolar proteins.  May function as a sorting receptor for protein trafficking to the protein storage vacuole (PSV) (By similarity).
What are the official names of this protein?
Receptor homology region, transmembrane domain- and RING domain-containing protein 2, AtRMR2, ReMembR-H2 protein JR702.
What are the subcellular locations of this protein?
Protein storage vacuole membrane. Golgi apparatus membrane; Single-pass type I membrane protein. Note=Traffics through the Golgi apparatus before reaching the vacuolar compartment.
Protein: MRAY_BORPE
Sequence: MRAIGVFEYITLRAVLACATALLIGLVAGPRVIRRLTEMKIGQAVRAYGPESHLVKTGTPTMGGALILIAIAISTLLWADWTNRFVWVVLLVTFGFGWIGWMDDYRKVVYRDPEGMPARQKFFWQATIGLVAAVYLAFAVSAPANTELWPLFKAWVGSGFTMPLPTRADLIVPFFKSVSYPLGVLGFVALTWAVIVGTSNAVNLTDGLDGLAIMPTVMVGSALGIFAYVVGRVDYSKYLLFPYIPGAAELMVLCAAIGGAGLAFLWFNAYPAQVFMGDVGALALGGALGTIAVIVRQEIVLFIMGGVFVVETLSVMVQVTWFKYTKRKYGQGRRIFRMAPLHHHFEVGGWKETQVVVRFWIITMMLVLVGLSTLKLR
What is the function of this protein?
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.
What are the official names of this protein?
Phospho-N-acetylmuramoyl-pentapeptide-transferase, UDP-MurNAc-pentapeptide phosphotransferase.
What is the protein family that this protein belongs to?
Belongs to the glycosyltransferase 4 family. MraY subfamily.
What are the subcellular locations of this protein?
Cell inner membrane; Multi-pass membrane protein.
Protein: EFTU_CHICK
Sequence: GPLRVRTSKMALPAALLRAAALRCRLPLASVGRRHLAAEAFVRDRPHVNVGTIGHVDHGKTTLTAAITKVLSESGGARFQRYEDIDKAPEERARGITINAAHVEYSTARRHYAHTDCPGHADYVKNMITGTAPLDGCILVVAATDGQMPQTREHLLLARQVGVRHVVVYVNKADAVSDAELLPLVELELRELLAEMGYDAERTPVVVGSALCALQDRDPTLGRDSVLQLLEAIDTHIPLPHRDVQRPFLLPIEGVHSIPGRGTVVTGTVERGAVSKGDECELRGYGRVLKAVVTGLETFHKSLPRAEAGDNVGALLRGLRREDVRRGMVMGQPGALRDHRKLQAQVYVLSAQ
What is the function of this protein?
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
What are the official names of this protein?
Elongation factor Tu, mitochondrial, EF-Tu.
What is the protein family that this protein belongs to?
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
What are the subcellular locations of this protein?
Mitochondrion.
Protein: RS16_LACCB
Sequence: MAVKIRLKRMGSKRKPFYRIVVADSRSPRDGRFIEAVGYYNPLTNPVDLKLNEEDILNWLQKGAQPSDTVRNLLGSKGIMQKYHEARFAKK
What are the official names of this protein?
30S ribosomal protein S16.
What is the protein family that this protein belongs to?
Belongs to the bacterial ribosomal protein bS16 family.
Protein: COTH2_RHIO9
Sequence: MKLSLTIVSSSFLVAIAHAASVQFNLIAPSATDVKVSVNGQQVALTASDPNVPYFTGSAEVGGTEESFERSLAGITNSTFNDFYNRPVTYANLPQLPWPIENDPQWTRKGKKAEIFDDNYIPSVFFHGDDSQVQDLVKNVPKDKVTGTLTFIGSNYVHSFANVSFGIHGAGKKHNNAKQSWKWTLSGTDTMGNRNHFKLRHMEEDPTQIRERLYADILHAMGTYANETTMVRLFINGQGFGTFNMLDDITEFSYINAMFYGGNPPATLGPLFDGASGADFIYHPGNLDGYSSWKPNKDNANGEGYEAFDPLCKAWNETDYTDNTAIANFEKMFDTEHFLRFMVIEYLTAHWDGYWMGQTNDGAYRDPSDNNKWYFLDQDFDATFGVNLDVPENKDFISVSYKDFPSRYPAGVMANGLLQNADKKAKFEQYLTETVRVLFNNVTLTNRVLAIHNFLSPDLEWDRSIVQQSPGTNFGWTFEQTSQNLWQGVSAPNNNGGGAEWGLVEYIAAKSQAMAKEFNITIVSEPVGPPAANGTATSTNDGGNTHTAAGESKPASSSESSGSKIASQSVSGASRSAVSTVLLGVTALVATAIF
What is the function of this protein?
Promotes invasion of host epithelial cells by adhering to receptors on the host cell surface to facilitate endocytosis of the pathogen into host cells (PubMed:24355926).  Binds HSPA5/BiP protein on the cell surface of host epithelial cells (PubMed:24355926).
What are the official names of this protein?
Invasin CotH2, Spore coat protein homolog 2.
What are the subcellular locations of this protein?
Cell membrane; Lipid-anchor, GPI-anchor.
Protein: NLP3_ARATH
Sequence: MVGPFKKILHAHNQRFPPSSSSSLDPVVDDSSRKQTRIILSYLLHLSLSLHITYSLCLLHFFFGSSNPFSPMEESNNSAVVDFPDNFMDQLLWEECWEEEATQHDQALSSPSGLKERVACAMGHLQEVMGERELLIQLWVPVETRSGRVLSTEEQPYSINTFSQSQSLALYRDASAGYSFAAEVGSEQLVGLPGRVFLRRMPEWTPDVRFFRKEEYPRIGYARRYQVRATLALPLFQGTSGNCVAVMEMVTTHRNLEYASQLSTICHALEAFDLRTSQTSIVPASLKVTSSSSSSSRTEVASILQGICSSHGLPLAVTWGHQDSSSCLSALISASYAADHGSRCFLAACSEHHLLGGEGIAGRAFATKKQCFATDVAIFSKWSYPLSHYAKMFDLHAALAVPILTRGNRTVQFVLELFFPRDCLDIQTHSLTLASQLKLRFQSSPHLMVDDNQIAEEVRDAATPPLTQEDPKGKQVSFSFSSASSLENRKRKTKAEKDITLDTLRQHFAGSLKDAAKNIGVCPTTLKRICRQNGISRWPSRKIKKVGHSLRKLQVVMDSVEGVQGSLHLASFYSSFPQLQSSSSSSFPFINPTQTVHVPPKSPPSSSGSQSSSGSSTCCSSEEQQLGGFQKPALSHPQLLTLSSMHEDQRPVRVTSSLPPLPSATTPRKAKDGMKVKAMFGDSMLRMSLLPHSRLTDLRREIAKRFGMDDVLRSNFSLKYLDDDQEWVLLTCDADLEECIQVYKSSSLKETIRILVHHPLSRPSFGS
What is the function of this protein?
Probable transcription factor.
What are the official names of this protein?
Protein NLP3, AtNLP3, NIN-like protein 3, Nodule inception protein-like protein 3.
What are the subcellular locations of this protein?
Nucleus.