lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol. Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways. Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids. Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism. BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting.
Subcellular Localization:
Late endosome membrane; Single-pass type II membrane protein. Lysosome membrane; Single-pass type II membrane protein. Mitochondrion membrane; Single-pass type II membrane protein.
Sequence:
MFWAGFSNNTIRIGDFEFSYIERGSEKTTQSTIVLIHGFSSSKDVWCQMSHGLPRSYHLIALDLPGHGKTTRKHHDNFSIPSQVSKLHQFLHAVGVNKRKFHLAGISMGGHIVGVYAAQHPARVASVIMMCPAGIQAPEHSEFITDVVLNGEKNYLIPDTPEDFQKMLNKVLHREVTIPYFIAKLFADVRRPCKDFYQKVLEDIVHPDHRFLLHHVLDDIHVPSLVLWGVDDKIIHVSSVHVMKEKMKNCQVQLIERCGHAIFLERPWKTAKLVNEFLSSLH
The following text describes a protein:
Function:
Constitutively open nonselective divalent cation-conducting channels which mediate the influx of Ca(2+), Mg(2+), Mn(2+), Ba(2+), and Ni(2+) into the cytoplasm, leading to membrane depolarization. Impermeable to zinc ions. In addition, forms heteromultimeric ion channels with TRPM3 which are permeable for calcium and zinc ions. Plays an essential role for the depolarizing photoresponse of retinal ON bipolar cells. In the dark, tonic release of glutamate activates the G-protein coupled receptor for glutamate (GRM6), its activation induces the release of G(o) and the beta-gamma G protein dimer. Both subunits can interact and inactivate the TRPM1 channel. A light onset, induces decrease in glutamate release and deactivation of GRM6 leading to channel opening and membrane depolarization. May play a role in metastasis suppression.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell projection, axon. Note=In ON-bipolar cells is intracellular and located predominantly in the ER, and not at the plasma membrane or Golgi apparatus.
Sequence:
MGSMRKMSSSFKRGSIKSSTSGSQKGQKAWIEKTFCKRECIFVIPSTKDPNRCCCGQLTNQHIPPLPSGAPSTTGEDTKQADTQSGKWSVSKHTQSYPTDSYGILEFQGGGYSNKAMYIRVSYDTKPDSLLHLMVKDWQLELPKLLISVHGGLQSFEMQPKLKQVFGKGLIKAAMTTGAWIFTGGVSTGVVSHVGDALKDHSSKSRGRLCAIGIAPWGMVENKEDLIGKDVTRVYQTMSNPLSKLSVLNNSHTHFILADNGTLGKYGAEVKLRRQLEKHISLQKINTRLGQGVPVVGLVVEGGPNVVSIVLEYLKEDPPVPVVVCDGSGRASDILSFAHKYCDEGGVINESLRDQLLVTIQKTFNYSKSQSYQLFAIIMECMKKKELVTVFRMGSEGQQDVEMAILTALLKGTNASAPDQLSLALAWNRVDIARSQIFVFGPHWPPLGSLAPPVDTKATEKEKKPPTATTKGRGKGKGKKKGKVKEEVEEETDPRKLELLNWVNALEQAMLDALVLDRVDFVKLLIENGVNMQHFLTIPRLEELYNTRLGPPNTLHLLVRDVKKSNLPPDYHISLIDIGLVLEYLMGGAYRCNYTRKSFRTLYNNLFGPKRPKALKLLGMEDDEPPAKGKKKKKKKKEEEIDIDVDDPAVSRFQYPFHELMVWAVLMKRQKMAVFLWQRGEECMAKALVACKLYKAMAHESSESELVDDISQDLDNNSKDFGQLAVELLDQSYKHDEQVAMKLLTYELKNWSNSTCLKLAVAAKHRDFIAHTCSQMLLTDMWMGRLRMRKNPGLKVIMGILIPPTILFLEFRTYDDFSYQTSKENEDGKEKEEENVDANADAGSRKGDEENEHKKQRSIPIGTKICEFYNAPIVKFWFYTISYLGYLLLFNYVILVRMDGWPSPQEWIVISYIVSLALEKIREILMSEPGKLSQKIKVWLQEYWNITDLVAISMFMVGAILRLQSQPYMGYGRVIYCVDIILWYIRVLDIFGVNKYLGPYVMMIGKMMIDMLYFVVIMLVVLMSFGVARQAILHPEEKPSWKLARNIFYMPYWMIYGEVFADQIDLYAMEINPPCGENLYDEEGKRLPPCIPGAWLTPALMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIMTFHDRPVLPPPMIILSHIYIIIMRLSGRCRKKREGDQEERDRGLKLFLSDEELKKLHEFEEQCVQEHFREKEDEQQSSSDERIRVTSERVENMSMRLEEINERENFMKTSLQTVDLRLSQLEELSGRMVSALENLAGIDRSDLIQARSRASSECEATYLLRQSSINSADGYSLYRYHFNGEELLFEEPALSTSPGTAFRKKTYSFRVKDEDAKSHLDQPSNLHHTPGPSPPATPGRSRLALEGPLSTELRPGSDPGISAGEFDPRADFKSTEAAPSLNAAGVTGTQLTVESTDSHPLRESKLVRYYPGDPNTYKTMKSRSFVYTEGRKLVRGLSNWSAEYSSIMDQAWNATEWRCQVQRITRSRSTDIPYIVSEAASQDELEDEHRGSLLDPQISRSALTVSDRPEKENLLSVKPHQTLGFPCLRSRSLHGRPRSAEPAPSKLDRAGHASSTSNLAVMSVVPEGQNTQQEKRSAETEC
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 (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MSIISPQDVKKLREETNAGFGDCKKALSVAGGDFELAKKKLREMGIASAEKRLDRDAKEGRVFSYSNNIYAGLLLVSCETDFVALNHNFVNFGNSLIKELVESGIDSLTTSQELELKNLAATIKENIQVKKIFITKIQSNEFVKIYLHGEQSKIGVLVKLKVNDFSKTEDKIFKNFAMDLALHVAAFAPVYLRNDDVCPNYIKEQEEIFTKQLESSGKPESIIKGIVAGKIKKHLAEISLLEQSFVKNDKITVKEMLEEISKAISSKVEMVEFKYLRIG
The following text describes a protein:
Function:
Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12.
Subcellular Localization:
Bacterial microcompartment.
Sequence:
MVSELELKEIIGKVLKEMAVEGKTEGQAVTETKKTSESHIEDGIIDDITKEDLREIVELKNATNKEEFLKYKRKTPARLGISRAGSRYTTHTMLRLRADHAAAQDAVLSSVNEDFLKANNLFIVKSRCEDKDQYITRPDLGRRLDEESVKTLKEKCVQNPTVQVFVADGLSSTAIEANIEDCLPALLNGLKSYGISVGTPFFAKLARVGLADDVSEVLGAEVTCVLIGERPGLATAESMSAYITYKGYVGIPEAKRTVVSNIHVKGTPAAEAGAHIAHIIKKVLDAKASGQDLKL
The following text describes a protein:
Function:
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MLKPARNKEKDPEGRMPLAEHLRELRNRLAKALLAIVVVTVVAAFFYQWIINALTDPILQSIGCEKSFAELAQSEAGSEPCAQITINGLLGPFTLALKVSLTAGVVLASPVWLYQLWAFVAPGLHRNEKKYAYAFVATGAPLFLAGAYFAYAVLPTSAKVLIEFTPNDVDNLLPLDELLDLVTRMVVVFGLSFELPLLLVMLNFTGVLTGKRMLGWWRAMIMGITLFAAIATPSTDPLTMIMLAGPIWVLYFAAVVVSLLNDRRKARLEALEPDDDEASDLDLTPEDIGEVEPVTTARALPEQATKDRVNGYDDVT
The following text describes a protein:
Function:
Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin.
Miscellaneous:
MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
Sequence:
MGNIITDTIIITSDKCDIVDNDNVERIQVWLSKNILRKFQINENEPLQLIILKRFKRILLICPSHDISQHVMDASRALEMENFNFSYSLQDGQRNLTKQYLKVPESEKMFLISPPASPPPEFDFSKCEDAPQRHIQSHIQQDQQQRLEASQLLPNNPDKNNNGTFTLLKSKVGAITIDRCPTNDGNGQMQLADHVKTAFPPKSIFDTDDDD
The following text describes a protein:
Function:
Probable ATP-dependent RNA helicase which may be involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MSYNSSNSGSGRYDDNRSGNSSYSSTSRGGSSYGNRSGSDRDYNRDGGSYNRDSSRDYNSSSGSGSGNGSSSYNKYPSSSSSSSSSSSTSSYGPSKGKDFQDSWGSSSTGTTNGYNGSSNGYNSSSNGYNSSNSSSSYGASNNGYNNSSGSSSSGSSGSSNGGSYNNSGSSNSNGYSKPTSNYSYSNGYTGPTTNYSSYSNGYSTPPTSTSTSSSSTTTTTTTTPSTSYNGGSTSYGYSTSGSSNGYGGYSQPPIPSYDPSSVSSYGAVTPASSSYNASVPGSSYGNSTYRSSGYGNQSYATTNSYGSSSYGSSGFYGNAKANTGSFGSALSPISWDLSKLPRFEKNFYLEHPDVSKFTQEEIEKFRASFQMTVKGREVPPPIMQFTQAPFPGYLMKEIIGAGFPNPTPIQSQAWPIALKGRDIIGLAKTGSGKTLAFLLPSIVHINAQPVLREDDGPIVLVLAPTRELALQIQEETNKFGGTSQISNTCVYGGASKHTQVAALKKGVEIVIATPGRLIDILESGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIISQIRPDRQTLMFSATWPKEVQALAHDFLTDHIQVHIGSTEITANHNVRQIVEVCQDFEKKERMLSFLGSVGRDEKVIVFAETRKGVDDLQRVLQFSGFKSIGIHGNKSQPERDFVLSQFKNGMVPIMIATDVASRGLDIKDIKYVVNYDFPNTIEVYIHRIGRTARAGASGVSYSLLTTDNARLANELIKVLTEAKQKIPIELSNLSVTPSTSSNTKKFSPYPTYSKRY
The following text describes a protein:
Function:
RNA-binding protein involved in post-transcriptional regulation through transcript degradation.
Subcellular Localization:
Cytoplasm, P-body. Cytoplasm, cytosol.
Sequence:
MDAPGGTALPSRPSNFESSNAELRPTDGLLDTPSHGFSGRSPSRNGNSPRKSLDDGSLGLENKFSELDVAFMDPEFASEMTQVEKWFQVLTIPERTAALYTLLQRISPSEAKMLSFAFFRRSSFDSSHAGSVVANMVAASSSSLPSGNTGPTSALSPSSAVPLSAKIKNEKTTPGLGARGSTEHSNTAPPTPSYFAQDRDTPMHTRFTRVLAQSSLESPIGAAQTTPSRRSVQDISEPGSGHSVGGSSRLFPSSHLSGNGNASLQTPRSRIRDAYDRGDPMSAPAGYVRNEGSLSHRWPNELCSPPPPPPELMLPSFLPHRRAHSDAHRSLQWGRPMGGRHWLDRPPPPHPASEEPHRTYHYRPTSPCFPPEYGRMSGPPVTPLSQRTGLLAEGASGGSHSPAPFQSHSASQLKFDGDRHFSRHPSGLWANNWPPSLSSQSHEYPYSQSPATYRVNSLPSDAKNNLGQGRYDRSPRFLSAYDTEYSTSEDATTPLSSHNRDLPYLNDTPRSMRTSFSKVRRASAHAKYDSNTSMELPQDIPSWLRSLRLHKYTDNLKDVSWQELIELTDEDLQRKGISALGARRKLLKSFQHIATILENMNSEKQKSGEMKASSDSMEPVKMAELESSQKTSPPFTTLLDSKSTDSQSSAGPEEHPLKHTVEEPIATSKALDSETSDSVSPSS
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MSGMHGASREALAAARERLDALTDSTSVDAGSLADELAAVTALLHREVSLRRVLTDPAQSGEAKAELAQRLLGTQVSGTAVDLVAGTVRSRWSQSRDLVDALEQLANIADLTAAQKRGRLDNVEDELFRFGRIISSNTELRAALTSRSATTAAKSELLAGLLGSRAERTTERLVTRLVTAPRGRSLESGLESLSKLAADRRDRMVAVVTSAVPLSDTQKQRLGAALAKVYGRPMHLNLDVDPEVLGGIRVQVGDEVINGSIADRLEDAGRRLAS
The following text describes a protein:
Function:
Required for cytokinesis and embryo elongation. May regulate myosin II complex formation and/or the association of myosin with actin. May be involved in the organization of mlc-4 and nmy-2 into bundles.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton. Note=Forms a filamentous structure during 2-fold embryonic stage which may co-localize with actin and whose formation may be regulated by mlc-4.
Sequence:
MDDLADCREVFAYFDSKGDERISVQQVGDVLRALGQNPTEAEIHKCVGSFDREARLSFEDFVPIFQSVSKNREKHTVEEFVEGLSHFDKEGNGMINVAELRHLLTTLGERLSDEDVDQLLSGHNDSHGNVNISDFVRAVMNS
The following text describes a protein:
Function:
Transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MMMPWNGNLLLPPYGGGGWSHSPSMAAVYNDGPGGGAMGAFLKQEGGTGRKRRLSEEQIESLEKCFQEETKLQPERKMRLAGELGLHPRQVAVWFQNRRARWKSKQVEHLYHSLKHQFHLVSKEKQKLHEEVLKLRAELRERERERGMTAREESGVVELSTVGGEESASACVGNATTTNYEDNGDEDDDTLMKCDCHPFSTINCRYGAGCSDDNNYLIPCLDDDGRPSQPNYYYNWDVGPGCIKSL
The following text describes a protein:
Function:
Directs RNA polymerase II nuclear import.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MATVIRLKRRVDEDPLNAFVLNCKRQRVDGATAGEEDPNANGAAAGTSTILKFAGTFTKAEGIASHIQNIHKDQAKDALSRVHRPNITSRNRLATKQTAQNSRFKIVNCTRSITNVEPSEPSDNNALPLTTTIVDVEREVARLGEGTGAAAAAAAAEVPPQQHSSLPALSGVTPDIVHSAMGNGTAALPEDQMPYFYENGVHYVYDLYVADASQNVTHIPYYTDNLDDLSVMVCDDPLYACHRGLDSDDSSDADSEDSNAENDWRNDYPDEDEDGLADGASVGEDDMVRAVEDLDLDGERELSSDEDYVRYDENEEDGFAYPRHDGVLYTDEEDDSDSEAEGINREDVRRYGTAYARYKARILREEKRDQAAGSSSSSSSTEDLNLYD
The following text describes a protein:
Function:
Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation.
Subcellular Localization:
Nucleus.
Sequence:
MKAVSPVRPSGRKAPSGCGGGELALRCLAEHGHGLGGSAAAAAAAAAARCKAAEAAADEPALCLQCDMNDCYSRLRRLVPTIPPNKKVSKVEILQHVIDYILDLQLALETHPALLRQPPPPAPPHHPAGTCPAAPPRTPLTALNTDPAGAVNKQGDSILCR
The following text describes a protein:
Function:
Involved in meiotic recombination. Facilitate crossovers between homologs during meiosis.
Miscellaneous:
MISCELLANEOUS: Two distinct classes of crossovers have been demonstrated in budding yeast. Class I is MSH4/MSH5 dependent and exhibits crossover interference. Class II is MUS81/MMS4 dependent and exhibits no interference.
Sequence:
MSESNLSSFISTNYFNLRSAANSSNSISKPSTKKSIRNQKSPTNISSWALKKKTLQIAETTWENNEKDSTHSHYLMTGSMASRTATSLSRYSTNASLLGPSIDCVLCCIYEVPRDISTRIGLCIINCNTGQMYLSDFMDSQIYIRVVHKLQIYQPTEILIPSSSLAPTVSKLATMIKFNVAETVKIEEGSRKCFNSQDGLAAITKYLMDDTKKDLKIEEIIDKTFALCAASAAISYMEEIISKSSRNLNAFRKLRIQFEGTENTMLIDSKTVRGLELVENKLDKNGISLWKFLDTTSTKMGQRSLRNSILQPLTDRGSIEMRLEALEELKANDDLLQKLRLEMKSLPDLDKLFSRLLCINHSAIKPDQRINYVLLLKETLQSVKSLKDALNDQLIQSRLISETKKIFNNDAIMEIEKLINSCINEDCVWASSAIQLLNQRSYAVKSDSNGLLDVSRQIYKEVKEEFFREVEDLTAKNKINLDHNYDSARGFYLRIKRQEFTDDVATLPDVFISRTIKKNYIECTTLNIIKKNARLKEVMEEILLLSEETVDELLDKIATHISELFMIAEAVAILDLVCSFTYNLKENNYTIPIFTNNLLIRDSRHPLLEKVLKNFVPNTISSTKHSSSLQIITGCNMSGKSVYLKQVALICIMAQMGSGIPALYGSFPVFKRLHARVCNDSMELTSSNFGFEMKEMAYFLDDINTETLLILDELGRGSSIADGFCVSLAVTEHLLRTEATVFLSTHFQDIPKIMSKKPAVSHLHMDAVLLNDNSVKMNYQLTQKSVAIENSGIRVVKKIFNPDIIAEAYNIHSLLKIAKARTENEDSNGVVDQKTINQMKRIHNLVAILKECAGNEKEPLTLGKLKEINSDFIENFEE
The following text describes a protein:
Function:
GTPase that plays an essential role in the late steps of ribosome biogenesis.
Sequence:
MKKGVPVVSIVGRPNVGKSVLFNRIVGEEKAIVADEPGVTRDPLVHLCEHEGKYFYLVDSAGWGLTDDLSELIQEKIQEVINISDLILFVVDGRSELTALDHEFVDILRKSGKRVILVVNKMEGRIDREEYLAPFTALGLGEPFPISALHKQNLYELLDLIISLIPAPEEVSSEDKSIKLAFVGRPNSGKSSLLNALIGRDRSIVSEIPGTTRDAVDLIWDFNGKKYIIVDTPGLRRPAKVEEGLEELSVQKTLQTIRRIDIAIMVIDLSVGIREQEKRILHYIEDKGKSCLIVFNKTDLIPSLKERREFEKIVPQILQPFDYFPFIFTSAIRNYNVKKILPWVDKLFELRNMRIPTSQINRAIGEALSKTNFSKKGKILKIYYATQVDVAPPTIVFFVNEPEIMNKNVVKYFEKFLRNYFGWVGTPIKIEVRKRE
The following text describes a protein:
Function:
Serine protease inhibitor which exhibits antifibrinolytic, antielastolytic and antimicrobial activities. Displays antimicrobial activity against bacteria and fungi. Likely functions in the innate immune response to microbial infection and possibly in the venom, as an antifibrinolytic agent. The recombinant form inhibits trypsin (IC(50)=80.02 nM, Ki=127.25 nM), chymotrypsin (IC(50)=393.78 nM, Ki=432.59 nM), the microbial serine proteases subtilisin A (IC(50)=379.20 nM, Ki=492.77 nM) and proteinase K (IC(50)=189.43 nM, Ki=271.76 nM), plasmin (IC(50)=457.98 nM, Ki=502.91 nM), human elastase (IC(50)=347.81 nM, Ki=469.90 nM) and porcine elastase (IC(50)=94.70 nM, Ki=125.62 nM). Does not inhibit thrombin. Binds to human plasmin and inhibits the plasmin-mediated degradation of fibrin to fibrin degradation products, indicating its role as an anti-fibrinolytic agent. Also binds to bacterial and fungal surfaces. Exhibits antimicrobial activity against the Gram-positive bacteria B.thuringiensis (MIC=4.21 uM) and P.larvae (MIC=11.13 uM), the Gram-negative bacteria E.coli (MIC=6.50 uM) and the multidrug-resistant A.baumannii (MIC=5 ug/ml, MBC=10 ug/ml), as well as against the fungus B.bassiana (IC(50)=2.57 uM). The synthetic peptide also exhibits antimicrobial activity against the Gram-positive bacterium P.larvae (MIC=41.12 uM), the Gram-negative bacterium P.aeruginosa (MIC=65.75 uM), and the fungus B.bassiana (IC(50)=44.27 uM) (Ref.2). Is also able to prevent A.baumannii biofilm formation and eliminate established A.baumannii biofilms. In vitro, does not induce an inflammatory response and has no cytotoxic activity against mammalian cells (Ref.2, PubMed:39224503).
Subcellular Localization:
Secreted.
Sequence:
MRFQVYILHLCFFILVVLTYLSQGQSYTTTTTTSTTEQPTFLQKIHETFKKVKENAKIHNLYIFDPPTWIYTTTTEKPVESTENFDITNRQLITVPVRCPPNYDFIKGRCREKIP
The following text describes a protein:
Function:
Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Activates SPO14/PLD1 (phospholipase D1) by stimulating phosphoinositide synthesis via the STT4 PtdIns 4-kinase. Modulates ArfGAP function through effects on SPO14 activity. Inhibits phosphatidylcholine degradation by PLB1 (phospholipase B1). May also regulate post-Golgi membrane-trafficking events and have a role resistance to oxidative stress. Inhibits fatty acid synthase activity in response to heme depletion and oleic acid starvation, preventing saturated fatty acid (SFA) accumulation.
Miscellaneous:
MISCELLANEOUS: Present with 9600 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Microsome. Endosome.
Sequence:
MSFDRQLTEDQEVVLKQIWTHLFHLWQVPVDGTHIFPNNSLHSSSTPAKKKKSSWFSKLQSSDHTQDSSEAAEAAHLYEKGKIHKALANLDPQTTKKQFWHDIKNETPDATILKFIRARKWNADKTIAMLGHDLYWRKDTINKIINGGERAVYENNETGVIKNLELQKATIQGYDNDMRPVILVRPRLHHSSDQTEQELEKFSLLVIEQSKLFFKENYPASTTILFDLNGFSMSNMDYAPVKFLITCFEAHYPESLGHLLIHKAPWIFNPIWNIIKNWLDPVVASKIVFTKNIDELHKFIQPQYIPRYLGGENDNDLDHYTPPDGSLDVHLKDTETRAMIEKEREELVEQFLTVTAQWIEHQPLNDPAYIQLQEKRVQLSTALCENYSKLDPYIRSRSVYDYNGSLKV
The following text describes a protein:
Function:
Component of the mitochondrial outer import machinery (MIM) complex that mediates transport of proteins into mitochondrial compartments. Promotes the insertion of tom70 into the outer mitochondrial membrane. Promotes the insertion of atg43 into the outer mitochondrial membrane. The MIM complex cooperates with the receptor tom70 in binding of precursor proteins and promotes their insertion and assembly into the outer membrane (By similarity). Involved in import of the subset of proteins with multiple alpha-helical transmembrane segments (By similarity). Required for the assembly of the TOM (translocase of outer membrane) receptor complex, which is responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins (By similarity).
Subcellular Localization:
Mitochondrion outer membrane.
Sequence:
MEKNTVTVPKTLFSQVIHIFKYAAINLGLPFLNGVMLGFGEIFAHAFIHSLGWAPGHTRIYSIQRHQYIQA
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MAERANLVFQNKEIDGTAMKRLISRLIDHFGMGYTSHILDQIKTLGFHQATTTSISLGIEDLLTIPSKGWLVQDAEQQSFLLEKHYYYGAVHAVEKLRQSVEIWYATSEYLKHEMNSNFRITDPSNPVYLMSFSGARGNASQVHQLVGMRGLMADPQGQMIDLPIQSNLREGLSLTEYIISCYGARKGVVDTAVRTADAGYLTRRLVEVVQHIIVRRRDCGTIQAISVSPQNGMTEKLFVQTLIGRVLANDIYIGSRCIATRNQDIGIGLVNRFITTFRAQPFRAQPIYIRTPFTCRSTSWICQLCYGRSSTHGDLVELGEAVGVIAGQSIGEPGTQLTLRTFHTGGVFTGGTADLVRSPSNGKIQFNGDLVHPTRTRHGQPAFLCYIDLHITIQSQDILHSVTIPSKSLILVQNDQYVESEQVIAEIRAGTSALHFKEKVQKHIYSESDGEMHWSTDVYHAPEYQYGNLRRLPKTSHLWILSVSMCRSSIASFSLHKDQDQMNTYSFSVDGRYIFGLSMADDEVRHRLLDTFGKKDREILDYSTPDRIMSNGHWNFVYPSILQNNFDLLAKKRRNRFAIPLQYHQEQEKEPISCFGISIEIPFMGVLRRNTIVAYFDDPRYKKDKKGSGIVKFRYRTLEDEYRTREKDSENEYGSPENEYRTREEECKTLEDEYRTREEEYETLEDEYGIPENEYETLEDEYGILEDEYRTREEESEDEYGSPENKYRPREDKYGTLEEDSEDEHGTLEEDSEEDSEDEYGNPEEDSVLKKGVLIEHRGTKEFSLKYQKEVDRFFFILQELHILPRSSSLKVLDNSIIGVDTQLTKNTRSRLGGLVRVKRKKSHTELKIFSGDIHFPEEADKILGGSLIPLEREKKDSKESKKRENWVYVQWKKILKSKEKYFVLVRPAVAYEMNEGRNLATLFPQDLLQEEGNLQLRLVNFISHENSKLTQRIYHTNSQFVRTCLVLNWEQEEKEEARASLVEIRANGLIRDFLRIGLIKSTISYTRKRYDSRSAGLILHNRLDRTNTNSFYSKAKIQSLSQHQEAIGTLLNRNKEYQSLMVLSASNCSRIGFFKNSKNPNGVKESNPRIPIPKFWGLFRNFSGLLGTIAPSISNFSSSYYLLTYNQILLKKHLLLDNLKQNFKVLQGLKHSLINENQRTSNFDSNIMLDPFQLNWHFLPHDSWEETSAKIHLGQFICENVCLFKSHIKKSGQIFIVNIDSFVIRAAKPYLATTGATVHGHYGEILYKGDRLVTFIYEKARSSDITQGLPKVEQIFEARSIDSLSPNLERRIEDWNERIPRILGGPWGFLIGAELTIAQSRISLVNKIQKVYRSQGVQIHNRHIEIIIRQVTSKVRVSEDGMSNVFSPGELIGLLRAERAGRALDESIYYRAILLGITRVSLNTQSFISEASFQETARVLAKAALRGRIDWLKGLKENVVLGGIIPVGTGFQKFVHRYPQNKNLYFEIQKKKLFASEMRDILFLHTELVSSDSDVTNNFYETSESPFTPFI
The following text describes a protein:
Function:
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MYSSMSRLEKLVAVEEKLVEMSKEFLKEEKSRLHSLESFVETAEQQLQMSVNKSMSLVHHPVGAYLLVKRLSSDWLQHVKSVYQPLTDFVNRYNSEYHGQLPSAEDAEWSAHAILRLQEVYQLDIRNIISGQMELGLSTNNVPGSMEQNALRLKREDIFAIAKGAYRNNDYRNAVKWLNESIQLMEAEEVTENRENLEESEDAGDTSGALRYKGNVKKENLKFSALQYLGYSLYKQGDLEDALAIYKKASSLDPKHDEVRDSIKLLQRKIRSANMFGNVNNDEHPRPWASASNAKMIKYMALCRHELKPRPDVQARLKCRYQSNGNPYLLLGPVKTEVLSRKKPEITLFYDVITDEEAQTIKNRSLPKMFRSRIGNSFSEVESHIRISQQAWLHDKDDEVVSRVSKRIGLLTGLNTTPTSTELLQVLNYGLGGQYEPHHDYMTAEEKMWGTILGNRMATFLMYLSDVTAGGATVFPVANVTVPVVKNAGLLFMDLLRSGRGDVNSLHAGCPVVIGSKWIANKWIHEGGNEFRRKCGLSPNE
The following text describes a protein:
Function:
May control cellular differentiation.
Subcellular Localization:
Nucleus.
Sequence:
MQPKRMSHNLTVGEKAGSPFNVILNAANNTNSDNSSNNSDNENDDNQNNNNNNNNNNNNNNEEEEEEDDDDDDDSQQNRHNISIPFTINKNSINNNNNLINNINNNINNMNNNMNNNNNNNNMNNNINNNGNSNISNNNTPKVEKKKTKGKWTSEEDQILIKAVNLHNQKNWKKIAEHFPDRTDVQCHHRYQKVLHPNLVKGAWTKDEDDKVIELVKTYGPKKWSDIALHLKGRMGKQCRERWHNHLNPNIKKEAWSDEEDQIIRDQHAIHGNKWAEIAKFLPGRTDNAIKNHWNSSMKRVSNNNVHLKSHAIEHSLSSQDNQDSPKSIITSSSPIPTTTTTTTTTSTTLITPPPPPLLPPPPSINKKEKKIKQPKKRNASEIEQTLSQPHINQHESSPIVFENISNGNNKIDIPAAQYLMTNGISCINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNINNNNNINNNNNNNNNINNNNNNNNNNNNNNNNNNHSNVSANTNNNNNTINNNVSLQPPSQLNSNIAQLPSTPKNLAHVNIANKLNSPGELMANIVTPIKFFQTATVSMNSSSKNYNNENTNNNNNNNNNHHHHHHNNNNNNNKRPRLDFSSATPTKNNESFSADLCSQFPDILFSPIQNKNNKESFLDNSGLSPLRSPLHTNFFETPMKNYEYLDFNSPKIPNTISPLKNFNSPFNKINNHSNYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNHNPNHNSHNHNNHNNNHNHNHNEFAQPQPPQGNYQQSPYKNNSTTASSTLSTPSYSNNSSISSSSCSSSSSNSASKATKVIQLSSSGIDKNSLLTINAKLNNNHHKNYLDSSSSSSSSSSSSSSSSSSSSSSSSSSSSAASSSSTPNNQSDLATVPFTPDDNVFNNNNNNNPPTPGKTKFKSRFSPNSKPYSYPQEYDNYGQSSSTPQNINNTYNSICLGTNNNNNSNSSASNSFENNEENNNENDNNGSSSGGDKVPQMDSSFMALKLLKDNPNKSLFSKARKILGLGNISSSSLSPSSFVQQISNSASASSTPTSSSSTPLSSPTTTTSSVAAAIINKISSTPKYFSNQNQNQNNNNNNNNNNISNNSNLSAFSTPGGNDHVPNFESNSFLAQSPFQDILNSQKLDQLHQLTQTNQLSKSKVLLRNHKNSNQTESNSRSTIESINSNGSNNGNNSGSSNSGSNSDKNNGKPISFRLMESSKPIEGL
The following text describes a protein:
Function:
Seems to have a role in zinc absorption and may function as an intracellular zinc transport protein.
Sequence:
MPKCPKCDKEVYFAERVTSLGKDWHRPCLKCEKCGKTLTSGGHAEHEGKPYCNHPCYSAMFGPKGFGRGGAESHTFK
The following text describes a protein:
Function:
Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis.
Subcellular Localization:
Nucleus.
Sequence:
MDNDQENANSEEYPSFLRSLDDESFITHIQDLNKQHSQKNRQDYPFEHVSTPKKMASFNSAISSDPFDDGLDEEIINHVNKIDDKKALSGDEDDNNKETVGKLHEFGDYATYFHSKRLKQQKQDEEYVKWDKKRRKLQNVEYEPKQIFKGCSIFVNGHTNPSITEIHRLVILHGGQFVSYMVNKSSVTHIVCDRLTPRKSIQFKNCRVVKAQWIVDSVAQQTLLDWTLYRSISEVAYDQRRLDFAKQSTIEESKEINGECENNKEEDLDGEINSSLFGEDNADFLDKSQELETFFEKREGLVQEPEEDLPVVTDEPPQSGKGIHKVNNKYVLDARHPDFLPNFFANSRLHHLSVWKADLRLKFLRRIVKERLHQPASHFQNPFIDPGEKKVIMHIDFDCFFATASCLKRPDLDSSKHPIAVSHGGKTSDIASCNYVARKYGVKNGMWLMQATKLCPDLILLPYEFESYEKFSSEFYNYLLTSKFFDSIFPVSIDEVLVDATSYCHSGVSDSVSLVNELATRIRKDVFKLTNCPVSVGASTNVLLAKLALRKAKPNGQFYLFDDIEKFLESIYIKDLPGFGRGILEKLNSEIQSSNPQIKDVVTISKQRLVQLLGEKTGTKLFEYARGMDETSIEIDTNNPEAVLGRKSVSVDVNFGIRFDTVEELDDFLMRLSRELYQRLVSLGICGSSLTLKLAKRAEGASINPPKFLGMGRCDFVNKSSKLGVPTNDWGIIGNEVKVLYRMVNIPVKELRGISITISKLVDAEGVKSNKQMRLPFKKAESNALSVRDLKQLQKMSDSKDNKSQKLIFSKQSPEKRHVNKVLISHEFADFKSLDWEVFHVLPDEIKSELKVELRRRGMLSEKSTPTKGKTYLQQLLPTQAGNAPKYIRVTESPQRRKSPRKSRSETSSPIKVTKQEPVYEESQSYDTSVLNELPSSIKESVIRDVEYKEKIKKFDLVSMRDKLAQKLENKKVPVNEVTSDWLKSQEKLNKTPLFLNEQLKDNELSVKLDDWVKSSLLQGGPHEEDMDYFALFVQTMLQRDQFNRVLLLLRRLKERLKYHKTLINCQVFNEEEYLVYEESFEDWYKQLDNKVQPLVDCYSKEKKIQVGYIGVV
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Miscellaneous:
MISCELLANEOUS: Present with 2250 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1.
Sequence:
MKGSPISQFSKTSINALTRPWKKYRDGELFYGLSKVGNKRVPLTTKQGNKTMYKGTRASGIGRHTKFGGYVINWKKVRTYVTPDMVNFELKPYVNANVPPLKHEFKGFSGGPLDPRLQLLKIKEYIVNGRVQSEGATDTSCYKERG