lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Required for autophagy.
Subcellular Localization:
Cytoplasm.
Sequence:
MRKAIQKRMEAKKYVWEGAIPLQIHLHESQVTTLPPPPPALILAPRIGYLPLLVPLIKPHFSSTLPPGVDTIWFEYRGLPLKCQNQPPNGGFFCCRYIPTGVLFDLLCAEPERPWNITVHFRGYPGNVLIPCDGEDSVKWSFINSLKEAAYIINGNCKNVMNMSQSDQLELWHSVMNDRVPCDILDDENRKLHTLASPGWENLLFKVIWRPTYGSRLSLNLQQLRMSIQVCVHQNLNKALEKQILLDRSRQLEFFIGWDNADINFPHTFVQCRVPVRLYVWSISEDFDDWEDLSQVDSWEKISYINRPIEIHKEGKCFTLHDAMKSLLPEFFSDESLSDSKLARVDFEDAQKIPSEDVSSNKVVEDQGQNAYEHREACCISSSAEIKLIRIQGIEPKLEIPFSWLVNNLLNPDHFLHICVCVKVPQ
The following text describes a protein:
Function:
Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.
Subcellular Localization:
Nucleus.
Sequence:
MDPSLLRERELFKKRALSTPVVEKRSASSESSSSSSKKKKTKVEHGGSSGSKQNSDHSNGSFNLKALSGSSGYKFGVLAKIVNYMKTRHQRGDTHPLTLDEILDETQHLDIGLKQKQWLMTEALVNNPKIEVIDGKYAFKPKYNVRDKKALLRLLDQHDQRGLGGILLEDIEEALPNSQKAVKALGDQILFVSRPDKKKILFFNDKSCQFSVDEEFQKLWRSVTVDSMDEEKIEEYLKRQGISSMQESGPKRVAPIQRRKKPASQKKRRFKTHNEHLAGVLKDYSDITSGK
The following text describes a protein:
Function:
Binds to a number of sites in the transcriptional regulatory region of ftz. Isoform alpha is required to repress genes that promote the R7 cell fate. Probable repressor of the transcription of the segmentation genes ftz, eve, h, odd, run, and en. May bind to the region 5'-AGGG[CT]GG-3'. Degradation of ttk is directed by binding of sinah or sina, via the adapter molecule phyl which binds to the BTB domain of ttk.
Subcellular Localization:
Nucleus.
Sequence:
MKMASQRFCLRWNNHQSNLLSVFDQLLHAETFTDVTLAVEGQHLKAHKMVLSACSPYFNTLFVSHPEKHPIVILKDVPYSDMKSLLDFMYRGEVSVDQERLTAFLRVAESLRIKGLTEVNDDKPSPAAAAAGAGATGSESTATTPQLQRIQPYLVPQRNRSQAGGLLASAANAGNTPTLPVQPSLLSSALMPKRKRGRPRKLSGSSNGTGNDYDDFDRENMMNDSSDLGNGKMCNESYSGNDDGSDDNQPNAGHTDDLNESRDSLPSKRSKNSKDHRVVSHHEDNSTSVTPTKATPELSQRLFGSSSTTISATAPGGSSTGPSETISLLEISDERESAPVHLPTILGLKIRAINTTTPAQQGSPQTPTKSKPKIRQATGSNNSNSLLKQQLRGGAKDPEVPPATRITGAVTPNAALNAEEQSKEMPKKNQDEVNACIGLHSLANAAEQQAAQVASTGNLHHQLLLHMAANNSMLNTTDYYQQQQQESPSSAGQFMDDDLELLSLNDQQDKSDEPDHEMVTLADENAGLPGYQGNEAEATPAQEDSPAAETATAPPPAPRSGKKGAKRPIQRRRVRRKAQSTLDDQAEHLTEMSVRGLDLFRYASVVEGVYRCTECAKENMQKTFKNKYSFQRHAFLYHEGKHRKVFPCPVCSKEFSRPDKMKNHLKMTHENFTPPKDIGAFSPLKYLISAAAAGDMHATIYQQQQDHYHRQLAEQLEQQNASFDSRDSSLILPDVKMEHAEDQDAEQEAELSDGGYDASNPAAAAAAMLSLQQDVIIKDEIQISPSPSPTPPASCAVAEGKSLALASTAQTAT
The following text describes a protein:
Function:
As part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, maintains misfolded and hydrophobic patches-containing proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated and sorted to the proteasome. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome.
Subcellular Localization:
Cytoplasm, cytosol. Nucleus.
Sequence:
MQLTVKALQGRECSLQVSEDELVSTLKHVVSEKLNVPVRQQRLLFKGKALADGKRLSDYSIGPNSKLNLVVKPLEKVLLEESAAACRLTEAPLPRPPAWQLIAKVLARHFSAADASRVLDQLQRDYERSLSRLTLDDIERLASRFLHPEVTEAVEKGFSK
The following text describes a protein:
Function:
RNA-binding protein that suppresses transcription of some RNAs. Together with Wdr82, part of a transcription termination checkpoint that promotes transcription termination of RNAs and their subsequent degradation by the nuclear exosome. Promotes transcription termination of aberrant RNAs, transcripts from genes containing a transposon inserted at their very 5' end or RNAs from heat-shock-inducible repetitive element. Binds RNA preferentially at a sequence that resembles a cryptic 5'-splice site.
Subcellular Localization:
Nucleus. Chromosome. Note=Localizes to polytene chromosomes.
Sequence:
MSVALADEPLIDLEEDLEDGEIDDDEEDEQQSSKIQVQKKTFVGDDDVQFVGVEAKNQNDDEDVVYVGPSTDAVCLQNSNSTKSKKPRPLEDDHASSIELAIANALKKKGIEPPMPRMRSSNQDTSDQSLEGSGEGLATANPLLQSTRSSRRRKRKKEREREQKKDKEQQNRSRRDENDVSVVPGGVEDMDEYEMMNVRGGSPPPGGAAPPLSSCGQRFSGADWDMDDGSAATGAAGLGAGGGGGYNSHSSYDSYSDEETNGPGLMNQRRRTRRDNEKEHQRGVNNRKRRDRDRLEGGLAGSGSKRNRRDSGEGGGGGQEKMGGSNRVEPRKLELCKFYLMDCCAKRDKCSYMHKEFPCKYYYLGMDCYAGDDCLFYHGEPLSEQLRNVLLKHMETAPKEILGDFKRISRDIAIVQMTRRHEQLCDQLNRENTWNSIGCGLMGKRQDHQMQQQQQQLQHQQLQQQQEQQQTQQQAAADGGGCIPSLLDMVINPPLSENKRKSRWTEKMGAKAAAGAAGSSERDSTSPDAKPLPPHLDLANLSHVLSAENMAKLNKLGITNLEQMLQVPFGQLTEAGLTLVEIGEIQRKAEDAKPQTQAELESSTPPSKRETEANNSNSKSNGLIMVDYTQYLKDAHVSFSGNDPLDDDRDDDEQLIIDDGNDSTAEEDQQPKKAKAPPAATHESSTEEAPLPSVFDLPSFMNNMLGQGSSARQLLPASATSPNQENAHLPGGDQSTHKSAPIGGGTSTNVLGRILFGDKQSDPEARAAFYRDIIRNPFKAHSGDGDVDSSNENSNSNSHSLTPTPTPEPGSQSPKPEDHDQDMPELPVIAPALPPTTPSLYVRRSMYDFDPVKEQEHGRQELLTEEKEQYQRDTDMRLPFEPMKHYMPATEIDAAIFSHTPIRWQLHEVTIEESSYAQIRASALHKEQRELRDPRMRRILGLPETPDNSGPLGSVPIMGPSSFSVDNIARCATTIASPDLETAVRDSTPSSPPPSVVNLPSMSVPPPSMRVPPPNIQVEKPTVRTDPRRDPRRAVLQAPTKGASTANTTAPNASGGSKQISEIRSLLQVSNWYNNLGTNNKIMVNQQLALVFTELKKFHQLPNDAPKIFDVSFIVNNTTLQQIFAKLFIFVDDNGEVVQIPEEPNGNGAALGGGGDSGGGVGGGGGGGGVVLPNLSQPPPNLSQMLRLPPPNIRMLRMSGMMMQMGNVGPPFNQPPPRGGLMGMPPNGNGLNQGVGNLGGLGQLGINQGGGPVPNGNPFNPFGGNNGGGAGVMNNMNSMGNMGMGFNNFNNNGGRGGHFPGGGSGGNGNGNNRNQRGGNHRNRNI
The following text describes a protein:
Function:
Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Subcellular Localization:
Nucleus.
Sequence:
MAEVLADELYKDRVRIFQEYLEHEPSDNNVVVYREAIMRMLNTGKRRLIVNLDELRDYNKELADGILYKPMEYCDAFNEALETVVSTMMDPIVHVELQGKKFYIGYSGSFGEFHVTPRTIRANHLNKMISLEGIVTRCSLVRPKVIKSVHYCEATKRHHIKQYADATMNGGLSFQSTVYPTQDENGNPLSIEFGYSTFQDHQTISLQEMPERAPPGQLPRSIDIVLDDDLVDTVKPGDRVHIVGQYRSMGAKNTNNTSATFRTLLLANNVVLLGTKSSLSGDTGAIMITDADVRNINRLAKKKNIFELLSTSLAPSIYGYEYIKQAILLLLLGGTEKNLENGTHIRGDINILLVGDPSTAKSQMLRFVLNIAPLAIATTGRGSSGVGLTAAVTTDKETGERRLEAGAMVLADRGVAGIHTSLNARCSVLAAANPIYGQYDTRKDPTRNIALPDSMLSRFDLLFVVTDDVDDVKDRALSEHVLRMHRYTPPGVEEGVPVRDTIGNVLSVGVNSAAGVGATGADEPEKETPVWETFSSLLHANARTKKKEILNIAFVRKYIQYAKTRIRPVLSQPAADFIVSTYSALRNDELQGNQRRTSPLTARTLETLIRLSTAHAKARLSLSVDVKDARAAEKILRYALFREIVKPESKRKKQRLEAQSASSSEDEEEAVTQRDSSYRGSQTSTATTQSTRKTRSQTAATPIAGSISAQAPSSVDVAMSEANDSLAATEGATVSSAEKTTQNSWPSTHLSLETTTKDSNTTESQERVSTTSQANAELDHLPRDKMTVFTARLAELTRTELFAEECASLDDLIPAMNRASDVQFTREETISALREMDSQNKIMFSDNVIYRI
The following text describes a protein:
Function:
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Subcellular Localization:
Cytoplasm.
Sequence:
MRVIASSIRKGNVIEQDGKLYVVVSAENIHPGKGTPVSQIEMRRISDGVKISERYKTTDQVEKATIEERNFTFLYEDGDGYHFMNPETYDQVQVSKDVVGDAAAYLQPDMTVKLSTHDVNVVSLALPQRVTLEVVETEPVTKGQTASSSYKPAVLSNGIRTTVPPHIAVGTRIVVMTEDGSYSERAKD
The following text describes a protein:
Function:
Required for normal mitochondrial ribosome function and mitochondrial translation. May play a role in ribosome biogenesis by preventing premature association of the 28S and 39S ribosomal subunits. Interacts with mitochondrial ribosomal protein uL14m (MRPL14), probably blocking formation of intersubunit bridge B8, preventing association of the 28S and 39S ribosomal subunits. Addition to isolated mitochondrial ribosomal subunits partially inhibits translation, probably by interfering with the association of the 28S and 39S ribosomal subunits and the formation of functional ribosomes. May also participate in the assembly and/or regulation of the stability of the large subunit of the mitochondrial ribosome. May function as a ribosomal silencing factor.
Subcellular Localization:
Mitochondrion.
Sequence:
MLTRVFRLVHDRRLSVPVLRCFHHEFSKPPQQAAKGQEIEGNPEKTLVAGVQDKYKIFRDEEATEIFDVEEARHQEQQLPEPDLELDHYYGLNLKRGVRGVFDVEDLVELLRKENVDDIFVCYVPENLKYVDHLVVCSGRSYRHMLSTAEFVRRMFKIKRGKGDILPRIEGDKSRDWMAMDLGNIALHIFSPSAREEYDLESLWAIGSEFDRESQKPTNPYGDIFMAQTPLSFVDKSKLKT
The following text describes a protein:
Function:
May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MGSKYPRSLRCCLPLWALELQTAFSLLFCFFIPHDTAQVDHRFMASYQVLRNLTLMAALGFGFLSSSFRRHSWSSVAFNLFMLALGVQGTILLDHFLGQVLQWNKINNLSSIQIATMSTLPVLISAGAVLGKVNLVQLTVMVLMEAMAFGAIRFADEKVFKMTEHIIMMHGHVFGAYFGLTVAWWLSRSLPRRVGENAQTEKVQMATSSSLFAMLGTLFLWIFWPAINSALLEGTKKRNAVFNTYYALAVSAVTATSMSALSHPQGKINMVHIHNAVLAGGVAVGAPGCLISSPWISMVLGLIAGLISIWGAKCPRACLNHMLQNSSGIHYTFGLPGLLGALTYYCLQIVTEPKSSDLWIITQTVTHIGALSFAVAMGMVTGLLTGCLLSVRVWRAPHAAKYFDDQTFWEFPHLAVGF
The following text describes a protein:
Function:
Ceramide-binding protein that may transfer ceramides from the endoplasmic reticulum membrane to the cis-Golgi network membrane, and is thereby required for the biosynthesis of complex sphingolipids.
Subcellular Localization:
Golgi apparatus, cis-Golgi network membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Cytoplasm. Nucleus. Note=Localizes to the interface between the cis-Golgi network and endoplasmic reticulum exit sites.
Sequence:
MNWLKSTLSAVAGTQEPIYGPEAIQPVSQQQTEDAPYTELTKHDLRWRAYQYTNVETQTYYAMADNGTLVMVQIIYSNIAGIHTTAQFNCKIFNTSGDGTPHIWFSDPLYNHMFDESMSSFAADNISLSLNEEGNAYTLKSAVNEGCLVDLTFNRAAPGFAIGKDGTTYFGTDPQNPWGSMRHMFWPRCNVTGTITTKEKVHDMTGRGMFSQALQGMKPHHAASRWNFINFQTPSFSAIMMEFTTPPSYGSTVVNVGGIAKDGEIIYAGTTNSATHTEASQDETSDWPEPKSIKWVWEGKTKDGKTVTAEVDGPLGPKLDRIDVMAEVPGFIKTIAGSVAGARPYIFQYSPQQKLSLKLKVGDEEFTEEGSMFSEATFIS
The following text describes a protein:
Function:
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Subcellular Localization:
Cytoplasm.
Sequence:
MKKQRVVVKIGSSSLADSHGGISTEQLSDHVAALARLKEDGHEVVLITSGAVAAGFSALGYPSRPVTIKGKQAAAAVGQSLLMQAYTEEFRKYGIVTAQLLLTRSDFSRKEQYSNAYATLGELLNRSALPIINENDSISLEELTFGDNDMLSALVSGLVSADMLMIFTDVNGLYDKNPQKNADAKKYYFLPEVTEEISSLAGDAGSKLGTGGMKSKIDAAKTALSLGVSVFIGTGRGQEKFVNVLKGKGDGTYVGNAPQKEMKMNKQWIALHSLVSGQIEVDAGAATAIIQHGKSLLPAGVTNVSRFFQVGEVVEVVTQQGRVIGKGQCTYSAEELIDVKGMQSQDIQVRGERHSYEVIHRDHWVSL
The following text describes a protein:
Function:
Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Subcellular Localization:
Cytoplasm.
Domain:
The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme.
Sequence:
MANPPHGGVLKDLLARDAPRHDELEMEAEKLPAIVLTERQLCDLELIMNGGFSPLEGFMNQKDYDSVCENVRLADGNLFSMPITLDVSQAVIDEGKLKPGSRVTLRDFRDDRNLAILTIDDIYRPDKAKEAKLVFGGDEEHPAIKYLYNKVQEFYVGGKIEAINKLNHYDYVALRYTPAELRVHFDKLGWNRVVAFQTRNPMHRAHRELTVRAARARQANVLIHPVVGLTKPGDIDHFTRVRAYQALLPRYPNGMAVLGLLGLAMRMGGPREAIWHAIIRKNHGATHFIVGRDHAGPGKNSKGQEFYGPYDAQHAVEKYREELGIEVVEFQQVTYLPDTDEYKPKDEVPPGVKTLDISGTELRNRLRTGAPIPEWFSYPEVVKILRESSPPRHTQGFTIFLTGYMNSGKDAIARALQVTLNQQGGRSVSLLLGDTVRHELSSELGFSREDRHTNIQRIAFVAGELTRAGAAVIASPIAPYEESRNAARDAVTQAGGNFFLVHVATPLEYCEKTDKRGIYAKARRGEIKGFTGVDDPYETPSKADLTVDVSKQTVRSIVHEIILMLETEGFFDRS
The following text describes a protein:
Function:
May play metabolic roles in sperm maturation or fertilization (By similarity). Phospholipid transfer protein that preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position. Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline (PE) between membranes.
Subcellular Localization:
Cell projection, cilium, flagellum. Cytoplasm. Membrane. Note=In testis was predominantly detected at the flagella of elongated spermatids, with a strong signal also found at the tail of epididymal sperm (By similarity). Mainly cytosolic.
Sequence:
MEKLAASTEPQGPRPVLGRESVQVPDDQDFRSFRSECEAEVGWNLTYSRAGVSVWVQAVEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACLKYPEWKQKHLPHFKPWLHPEQSPLPSLALSELSVQHADSLENIDESAVAESREERMGGAGGEGSDDDTSLT
The following text describes a protein:
Function:
Required for anaerobic carnitine reduction. May bring reductant to CaiA.
Sequence:
MNKFSSVWVFSDTPSRLPELMSGAQAVGEKVNAFVLNEADSATACHLGADHVWLLSGKPEDRMIEDYAAAMAETIRQHSEGGAVLLPNTRRGKLLAAKLGYRLSAAVSNDASDVSLQDGKAAVKHMVYGGLAIGAETIASPFAVITLSSGTFDAQQPDASRSGEMHTVQWQAPATAVTRTATQARQSNSVDLDKARLVVSVGRGIGSKENISLAEALCQTIGAELACSRPVAENEKWMEHERYVGISNLMLKPELYLAVGISGQIQHMVGANGAQTIFAINKDKNAPIFQYADFGIVGDALKILPALTAALAR
The following text describes a protein:
Function:
G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLEIGNYGYNGIDEFTSRAKDAGICVANSHAIPTDADDDDYDNVVRSLDKFAAARVVVCFCEGFTVQALINATNRLRVAGKYVFFGSDGWSDRQDVVKNQEKASVGSLSIRFHANYDHDFDRYYFGLDPFTNLRNPWFKEFWEVRFNCSLSIGPGSARYNRTCTGKEQLREGHKQDTKVEFVKKSIYTMAHGLHNMHRDLCPNTSGVCPAMVPVNGSIFLQYLMNVTFDWGNETVFFHENGDPPGRYDLMNYQKLPGTQHFDYVQVGSWINGEMRMTGDVQWNRAQVNPPISICSLPCEKGKVKSIHSETMKCCWNCVECKENQVVLDEYTCMDCERGWWPNENLTGCDRIPEEYIRWSDSQSIAAMTIACLGFLATLAAMVIFIRHNDTPVVKSSTRELSYIILLRHDLLGPGHQDNRIARILAGSKKKIITKKPRFMSATAQVVITWLLISVEAAIIGAMVVLEPPDYMFAYPALDRVKLICNTTTLGIIAPLGFDFFLIAMCTVYAVKTRNVPENFNEAKFIGFTMYTTLVIWAAFVPIYFGSKHKVITLCLCISFSAEVALVLLFLPRVYIIIFRPDKNNRSAFTTSKDVRCHIGYMNSAVTGPGGSSAAAAAAAATSAVSRNSSHSTSEFSLESPRNHSGDTVLKPPPTRSKSLNLLERFRASKQDRIAASVAQHIRAVRAAEALDRRTRLRHSAEPLFGPNKIPATRTSSDSPPGAQERKRLVGMLQHAYGADGQRLPQTAGAVGPRQEASCQTTDDLVEMWLPCLRRRIVRSETLMSTLTPEEDEDPGGALAPGLRHRKLCRHVPAAVGADDDVSDVVFRGGSSQGALPPPLRYGRPGSERSAFKSDESLIEGASSIVEESASSGSEDAAVYKNIIISLGSPDTVRVRQTPASPVMVPRDVRDDTLPAPVTPSPWAEVSAQLLLRSYNDQEPFGK
The following text describes a protein:
Function:
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease.
Sequence:
MVLLKDVEFVCLDCETTGLDVKKDRVIEFAAIRFTFDEIIDSVEFLIHPERAVSAESQKIHKISDAMLRDKPKFGEVFSRIKGFFKERDHIVGHHVGFDLQVLSQESERLGETLLPKHHYVIDTLRLAKGYGDSPNNSLEALARHFNVPHQGNHRAMKDVEMNVKVFKHLTKRFRTLSQVTHILSKPIKMKYMPLGKYKGRLFTDIPLEYLLWASKMDFDQDLLFSIRSEIKSRKKGTGFAQANNPFLGL
The following text describes a protein:
Function:
Probably part of an ABC transporter complex. Probably responsible for energy coupling to the transport system (By similarity).
Sequence:
MGDLSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVELTPDFAETNRPPETVHLQAGEVLFEQSTMGDLIYVVSEGEFEIVHELADGGEELVKVAGPGDYFGEIGVLFHLPRSATVRARSDATAVGYTVQAFRERLGVGGLRDLIEHRALAND
The following text describes a protein:
Function:
Core component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases. The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage. Within the MRN complex, MRE11 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. MRE11 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR. It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation, which is required for single-strand invasion and recombination.
Subcellular Localization:
Chromosome. Nucleus.
Sequence:
MSAPNRVPDSQPSSETGDEPPLSIVEPDLENCFRILIATDNHIGYAEKDPVRGQDSINTFREILELARDHDVDFILLAGDLFHENRPSRTCMHQTIALLREFTLGDKPIEFELLSDPMDGSTPGFSFPAVNYEDPNINIAIPVFSIHGNHDDPQGTGPEGALCALDVLSVSGVLNYFGKSDLVADESAADNPEKGIQIRPVLLRKGTTHVALYGCGNIRDQRMYQELRANKVKMFMPTGGNVPDSDWFNILLVHQNRVRHGPQNYVPENMFDDSMRLVIWGHEHDCRITPESVADKSYFITQPGSSVATSLAPGEAIPKHVGLLSIQGSQFQLEEIPLKTVRPFELDEVVLSYAAEQGAVDLNDRDSITSFLREQVEALILQAKKNWKEKNNGSTKNMMLPLIRLKVETTDAKEMVNPVRFGQEYVNRVANPRDILQYYRKKKNERKVKNNPDMPDIDHDEWEEDPESLTADERLSKLRMATLVKQYLQAQSLDVLVENGMEDAVMRFVDKDDKDAIKDFVADTLRMVGRKMKEKEVKEDDVDLAMAEAKVKEYNRYADSNPVPPQSVKGKNKQRDSDVDSMAASDDDMDLDEMPTQQRAPVRRTTAKQSVRSAKGKGKQPLFDDASEEEEEEEDEEEEEEEPAPTKSRGRAAAASTKKAPAKKAPARTPAKSTTKAPARRVPTASQRSTGRGVTQSQLTFSRSGAGKASAVPIELSSDED
The following text describes a protein:
Function:
Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Subcellular Localization:
Cytoplasm.
Sequence:
MTKYHSYSHADGSHLQPCQYQQQIPYLKQQQMQQVQQQQIQQQQIQQQQMQQQQQMQMQQQQMLIQQQQQQQQQQQQQQPKKQKTNILNIYKEGKQKIMMSLYNIYRNFPTEPPSFSSSPIWMMGRCYEINNNNSNNYNNNSNNGYIANNSSSSNSGLKSSLFQSLFNSKDSNNSNNNNNNNNNNNNSNNNIINYNNTNSFSTLNNNIIQSNFLDDVRSLIWFSYRKDFPPIENTTITTDIGWGCMLRTGQMILARALLKHVIQIM
The following text describes a protein:
Function:
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.
Sequence:
MAAETFLFTSESRNEGHPDKLCDQVSDAVLDVCLAQDPEGKVACETCTKTNMVMVFGEITTKASVDYEKIVRDTCRNIGFVSDDIGLDADRCKVLVNIEQQSPDIAQGVHGHFTKHPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEVRKNGTCA
The following text describes a protein:
Function:
Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome.
Sequence:
MSVNQSRAERTQGQLRKPSRSGSSGQQRGSIGSGALGKGGSSAPSPISSSASSAAPSSISPSLSTNRSIKKSGNGHGGQSRIIPASTTSEASGAAPSTTAHRAVQNGAQAPQPSPGFSDASVPSGAKLIDMPTPRNASRGIPKSPYSQSATGASSSSTTSAPPKGDTSRTFPLQFGSINPGIVNGLQIPARTSSAPPNLDEQKCDQARIESFGAAPTLPVASIPKQQQQQQARKDVSGAQQSNSVEAHPLPQSKRDVSIPVPSASVTSMPKSSVLPIPGMPPMPMPMPFQPHQPQIPPQLGGPSPQMQSPGLAANSLQMTMTLPVGNVPQVAQQIYVPGIQSHFVQQQAMMHQGQGLGFAPPISHQLSQQLGNMGMGISSQFPQQHMGKFSGPRKTIVKITHPETHEVLRLDKRMDSSKDGVSSGQRSLSNVIPQAQPIPTYSAAHQMNYYAPMQQNSYSPSPLIFTTTTVPLTSGQVPLSSQAPKYSYPVSQSGQNLSFMKSSMANAVPGGKPALSMPEAVNLEGLPVSTSLPYAVQINVKGLQSEIVGASSGTPPVVISMPLTEAEPVKSVKTVADATVSCHKNNETSPDGPAQQLKSGSEPLLTLPVLDKSSAAAPPVLSSQRMLSEASSTPESRTGDSGSVQSGSDIRKREPLRRSDSLKDNQKKQNRKDLRNSQQEHQLDVSSPEGAKLSSPKPTKSSYAGELIYQEGCTNTENTEAVLASDLATPSAWSCNKAENMILSEVGATEPFKGEIMPAASGLSGSILEKEASQGTSLFHADSFGSAPDGVSIKEDVPSEVTTSLSPMMDGTNSRSLCTSSCLVNEVLDVMRDEMLDVTKHEKSEVSDASLQDSSDNNVHQPSTTKKSYKLFDPVMLLKQDDGGGNDGKVKFSDYHEADNKQFSSFVVGTKEGESRIANEENKTIDASLDPADSGTAPSNDIRSANDDKDKVDIFTTKCEIKYSEDIGLTDSGVIETAPVPSPSLSEVTQKSESEVVGLHSGLVSATSLRQKEKPSLETLKPKITTTRKKKRKEILSKADAAGTSDLYNAYTGPEEMHETVSNPESIDNSMTDTKSAHVDFTNKEVAASEEDGQNKAELDDWEDAADISTPKLKTSEHGHSADGHDYDGDEATTQKKYSRDFLMTLSQQFTELPVGFEIGSDISDALMSTPLGKSPCPSPGRIIDRPSGASRVDRRMVGNLDDEKWTKSPSFGLGRDRLDIGHGAAIVSLRPGQGVSHGVLRNPRGQASNQFGGILSGPTQSVASQGGMPRDADRWQRARGLMPSPQTPLQVMHKAERKYEVGKAVDQEEGKQRQLKAILNKLTPQNFEKFCAQVKEVNIDSAATLTGVISQIFDKALMEPTFCEMYANFCFHLSGALPDFNEDNERITFKRLLLNKCQEEFERGEREQAEANKVEEEGEIKQSEEEREKKRLRARRRMLGNIRLIGELYKKKMLTERIMHECIKKLLGQYQNPDEEDVEALCKLMSTIGEMIDHPKAKEHMDAYFDMMTNLSTNQKLSSRVRFMLRDAIDLRKNKWQQRRKVEGPKKIEEVHRDAAQERQAQSSRLARGPVISNFPRRGQVVDYGSRGSTPLTSPNSQQVGSLRGLPTQARGYGTQDVRLDDRHHFETRTVSLPLPQRSTDDDSITLGPQGGLARGMSTRGHPSISISNVLASESPAVGEHRRLTSGPNGTSYMADRFSGTAHDQVKPHDRTSYYGSRDFKISDHTSDRSVMSILPAGRTHGTSDSSLTSASEIRTLPEEVLREKSILAIREFYSAKDENEVALCIKELNAPSFYPSVISLWVTDSFERKDAERDHLTELIINLCKSRDSLLNQVQLLQGFESVLSSLEDSMNDAPRAAEFLGRIFAKFVMEDMVTLREIGRLLCEGGEEPGRLRETGIAADVLSNIFETIRSEKGGTILNEIRASSNLPLEDFQPHPKQSKMDAFL
The following text describes a protein:
Function:
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.
Subcellular Localization:
Mitochondrion.
Sequence:
MSGSRSALSVVRLAACAKPCTLGSTSSVLTRPFSHSAQLCSPAKPSIKAIGELRKLVPGTSMLKAKEALLASRPASSPDTDSIALALEWLEADRKKSGAKKADKVASRTAREGVVAVSILSDGLPSSIEMQGELKDEAKRAGIGATSAAAGAIVEINCETDFVAKNEVFAQLVKDVVHTVALFPGLSAQSGAKRGLVEVPVDQLLAFPLLPSSREATGTSVSAKTVGSAIIDVVSRLGEKISIARAAAIVAPSVPSPDATRRSESGTARGGSIVELASAFAHGGSAGFAAAKDVSNPGYVLTSGKVASLVMTRFASDKLPDALQAGSIQSNIRALTRSLARQVAGLETNCIDSAATCPVDGQVSSALYKQPFMMLLPAAAPSLESNAQPVRQVLSTWASHNNLDSNGNNVVEVVDMHRWELGETIAPPDDAGPGFADEVRKAAGLA
The following text describes a protein:
Function:
Involved in response to both electrophiles and reactive chlorine species (RCS). Represses the transcription of the nemRA-gloA operon by binding to the NemR box. May sense electrophiles, primarily quinones and glyoxals, as redox signals and regulate the redox state by modulating the expression of nemA and gloA. Also uses the oxidation status of HOCl-sensitive cysteine residues to respond to bleach and related RCS. Involved in response to methylglyoxal.
Sequence:
MNKHTEHDTREHLLATGEQLCLQRGFTGMGLSELLKTAEVPKGSFYHYFRSKEAFGVAMLERHYAAYHQRLTELLQSGEGNYRDRILAYYQQTLNQFCQHGTISGCLTVKLSAEVCDLSEDMRSAMDKGARGVIALLSQALENGRENHCLTFCGEPLQQAQVLYALWLGANLQAKISRSFEPLENALAHVKNIIATPAV
The following text describes a protein:
Function:
Exhibits phosphatidylinositol-phosphate phosphatase activity. Has a preference for phosphatidylinositol 5-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate)) in vitro. May be involved in membrane trafficking by dephosphorylating phosphatidylinositides.
Miscellaneous:
MISCELLANEOUS: Dictyostelium phosphatidylinositol phosphates (PIPs) are unusual, with the lipid chain joined to the sn-1-position of the glycerol backbone by an ether, rather than ester linkage. The composition of the inositol phospholipids in Dictyostelium is strikingly biased, over 95% of the PI, PIP and PIP2 pools contain the C34:1e structure, with an ether-linked C16:0 chain (palmityl or hexadecyl) in the sn-1 position and an ester-linked C18:1 chain (11-octadecenoyl) in the sn-2 position.
Subcellular Localization:
Membrane; Single-pass membrane protein. Golgi apparatus membrane.
Sequence:
MNENEGIIIENINNDSGSTYLMNILGILIPIKIVVTIYLFSKARLPVGFARYFGRLYHFMTNPIRLGLQIAGLRGPFISQLDDNVYLGAMPMGSDVTLLFYKYKINSIVNLCDEYQGPTQHYTQYGMQQLYVPVVDHFEPDVEIIEKSIQFILKQIELGNRVYIHCKAGRGRSGAIAICWIAYSRRVSLEVAQKILLEKRKIVRKQLYKQKNVNQYYSSYCLNSNINSTTSI