lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
RNA exonuclease that acts as a negative regulator of RNA interference (RNAi). Acts by degrading the 3'-overhangs of double-stranded short interfering RNAs (siRNAs). Represses the accumulation of heterochromatic siRNAs leading to negative regulation of the RNAi-mediated heterochromoatin assembly. Also involved in rRNA biogenesis, trimming the 5.8S ribosomal RNA (rRNA) from a slightly longer pre-5.8S RNA in the cytoplasm.
Subcellular Localization:
Cytoplasm.
Sequence:
MNQKTPSTVEEIRIALQELGLSTNGNKEKLKRRWKFREKRLEEKRKQERYQKFSTSNENKTCLRYLLIVDVEATCEEGCGFSFENEIIELPCLLFDLIEKSIIDEFHSYVRPSMNPTLSDYCKSLTGIQQCTVDKAPIFSDVLEELFIFLRKHSNILVPSVDEIEIIEPLKSVPRTQPKNWAWACDGPWDMASFLAKQFKYDKMPIPDWIKGPFVDIRSFYKDVYRVPRTNINGMLEHWGLQFEGSEHRGIDDARNLSRIVKKMCSENVEFECNRWWMEYEKNGWIPNRSYPPYFAS
The following text describes a protein:
Function:
Absolutely required for transposition of IS1.
Sequence:
MRCPEYGSEKVVKTEDNMENKPTDEMWSYVGTKGNEVWIWSVVVELKDGTIKKFLFAGDRSLRTFLKILAKMPEAEEYETDAYRVYEWLPRDRHIVRKYGRVNRNEALHSKLRDKLVAFKRKTKAFFRSFLYLRYALALFSIHHLFR
The following text describes a protein:
Function:
Associates with actin filament appendages that are formed in the inclusion appendages of the parasitophorous vacuole during infection of the host erythrocyte.
Subcellular Localization:
Secreted.
Sequence:
MIVTYGTVGCPVSRGGSPGCGRRIAEELRLAEDARLRLALLGRCIVKGSPAQARGELRAELKAIDATIELRKELDAIDAEWAPKIELSAELRAIDAEWRPAIRLRSAYRAIIGRIELRKELDAIDAEWAPKIELSAELKAIDAEWRPAIRLRSAYRAIIGRWELSKELKAIDAEWRPAIARESLRKELDAIDAEWQHAITFWHISRAIIGSIELSKELKAIDAKWKYVAIYERQKAQRRREERAAKAREELRKELNDIDAKWKSASAIKLRKDLRSTSEGVDHTEFALELRATDKSGNMELVLKLKATDTKNQHDAIVKAIEDGFVGYAAECGAATRELNACGGMSTTSAPSTDLISTVVSAVTTGTGQQQSAGSESQRPTECGGGGTLLSSLFALILPSSNWYCNAVLYGGFLGCLGS
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNTDNIKPTDSSFCRIMKPIYLVSKMAGLWPQSFLRSSPGVTVLDIGYLIVLYAMYFFFILVNTNSKLWDYYMKPFESDILRYGLQTHLVNGLFLGVVIVTINVVQYQKKWDYMELLDNVTKVVEQEFHVRYPIRVVQTFIVIVISSELIYLVVILAGYYYLIDQTLNITTKYLYASYYMMNISLLALINEYIYFTVHIRRLFMIVNRLLKQLLLGDTNESNETVLLDQNRKSKTPTIAYDEIFTVYGRGAGGRKIGDANAGGMMKSKGPPKVTMVAPASAGFNKLSATTVYTTYITQLKIDNQSSMETILKTVNRLSVLHYHLCDAIRLVNRISSLSLMFHFGAMFVFLVFGLFTIYKAFNSGTWAFRIMAIANGAWIAFYLAAILSVITATTAAQTSGRMTGDIVHQIIRKHQNHFSVDVIEKLSTLSLQVTMRDMSFSCGLFNFDWNLFGSILSALAMYLVFLIQFDVAPPVGLNSPNLTIPSIELIDFEV
The following text describes a protein:
Function:
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular Localization:
Nucleus.
Sequence:
MAPRGPAKTRDYDYSNVGKAGRRTGVTLKEGKRDEHGMEEIDGIFSSPEKSPEAYGNNTTIGSDGMSMDEGNGLGPADFLGGTNGGRASFLPPPVARSPMKSGLSGSPRRTPGLRSSASPQRDILSSSPSDGKGLGSAKGETRRDVSPLTNRSINAPSLNHVNGLRNNKGINKTADTTVTVDFSDSDANSQMNGDENANAFEHMRNDYDDITDAGDDTLAEDQQDDSERVNRVDIGISSYTAAGSRKTERSRIAPKTKKLAQTEKTGSQDVTQKSETSEQGNVQKRKRPGRPPKSQKMNNDEDDTVGQRPSKKSKTASQTGQGLKSSGNPMLDKVVENYVNRTGPLKGRSLYILKREIPTDGSATHTRSGRVSVRPLAYWKNERCVYGDGEAAEGHRYPLSTIKEIIRTEELEPEKRKVSKRRSSKKSKSRKGRDDDSDNEDDDYVDPWEKEGGVLHGYVRKWDPDTQAGSIEEEVLDIAYAPSGIETRDVKDSTFRFAKLLSSPFIGSGIVELPPGGVKKPKNSKKMHMVFYVCHGRVQVDISGVQFSAGKGCVFQVPRGNYYSFANTHGKDARLFFTQGCVPVENDQSSPGSASKPAVSTEDESTIQKGRPSGTGKGRPKGKQKAGSGSKAS
The following text describes a protein:
Function:
Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Sequence:
MKQYGAEFFGTFWLVLGGCGSAVLAAGVPELGIGYLGVALAFGLSVLTMAYAIGPISGAHLNPAVSVGLWVGGRFPASQLLPYVVAQVLGGLAAGGVLYLIASGKAGFDLAAGFASNGYGEHSPGGYSLQAALVSEVVLTGMFLLIILGATSKRAPQGFAPIAIGLTLTLIHLISIPVTNTSVNPARSTAVALYVGDWAVSQLWLFWVAPILGAVLGALAYRLIGDKND
The following text describes a protein:
Function:
Putative phospholipase.
Sequence:
MWSCGAAAAAVVAVVVLASPATATVARFVEQTDVQTTYASVFYVESDDSYVVKTENHPWDGDFEKDEAVRIKYTPGYLVAGWDQLHVKSNSAMDDATVAYAAGYGEAQLTAEMIYNYAYNNGYDTFTPNDKLADYLAKNQAFMAASIASNRSDANGYWYHVDLILRQLQGVCDGYNSSDFAKSFPLPCESMLAINLMGDMEDLSDALASSDEWYTEDRFFRATHCSALVKLVGGASSPSDIYISQDTWSSLNSMTRIMKRYDLNFLQAKGADDRIAGSSIVFSSYPGSLYSGDDFYLTSAGMAVIETTIGNSNPELYQYIVPDTVLEWIRNIMANRLASNSQTWYEVYRQFNSGTYNNMNMILDYKQFKPQEALQDELLTIVEQIPGTVTKTDVTGYLRNMTYWGSYNVAFDQNIRELSGANQAEQLYGPWFSYWNTSRALIFAREQKNVSSLEDLKRLMRLNQFKTDPLSVQTATCEYRGWTNCTPAYTAENVIATRGDLNDPNGIYSLSSFGLRNHVATDSKISTFSTYDSNNLNVWAISGPTNGPPPNQPVFNWSTSYYKDTRHRGMPEAFDFDWVNFNWPF
The following text describes a protein:
Function:
This protein negatively controls the transcription initiation of genes such as deoCABD, udp, and cdd encoding catabolizing enzymes and nupC, nupG, and tsx encoding transporting and pore-forming proteins. Binds cytidine and adenosine as effectors.
Sequence:
MKSNKQVTAATMKDVALKAKVSTATVSRALMNPDKVSQSTRSRVEQAALEVGYFPQSMGRNVKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEQGYLVLIGDCAHQNQKEKTFLNLIITKQIDGMVLLSSRLPFDASVEEQRNLPPMVMSNEFAPELELPTVHIDNLTAAFNAMNYLLDLGHKRIGCIAGPEDMPLCHYRLQGYVQALRRSGIVVDPHYIARGDFTFEAGANALKQLLEQPLPPTAVFCHSDVMALGALSWAKRQGLKVPDDLSIIGFDNIALAEFCDPPLTTVAQPRFDIGREAMLLLLDQMQGQNVSSGSRLMDCELIIRGSTRALP
The following text describes a protein:
Function:
Transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MDPASSLISSSAVPFPAAGDGGGQRQVFLFGGGFVGGAPPLVGGAADGRRKRPFQLTAHDELQLQLQLQLDDELCGLDYELHGPQQERTTKRRLTAEQVRELELSFEEEKRKLEPKRKLEPERKSELARRLGIAPRQVAVWFQNRRARWRSKQLEQDFDRLRAAHDDLIAGRDALLADNDRLRSQVITLTEKLQTKESAAAAAEPGEQTVAAQATAYAVLEGDKLCSGSAAAPAAAGTNDSPESYFAGARSPPSSPEDDDRAFFFPPDALLNNWAWVWNDRQY
The following text describes a protein:
Function:
Probable transcription factor that regulates abaxial identity during leaf development. Modulates leaf rolling by regulating the programmed cell death (PCD) of abaxial mesophyll and sclerenchyma cells during leaf development.
Subcellular Localization:
Nucleus.
Sequence:
MAMVRELELMTSWSNSMGRHRYPTRILVDSFGHKCSASDKGVWTSCSIRAPLQGRGSFRRGANIRFGSLPSSAAVATSGGGRGGGGVVVGGGGGDPWRRLDGSTASTELSLSPPPAQAAGGGGGGGGADALPWRHRPSPPSSAVATTSAAAAAALMAPMMLQPLDAGGGASAPPPPIRGIPIYNGPGGFPFLQPSPTAGDVGHHHHHHPKMGFYSSYHHPSTWPSTSPSPLAAPPGAASSPLDPTAAFLSSPHHRMLSAASGRLNGMLSVSDTLRSYGVPGAAAPGVIGGAHHHHHHLHGGQPFVGALASRFMPKLPAKRSMRAPRMRWTSTLHARFVHAVELLGGHERATPKSVLELMDVKDLTLAHVKSHLQMYRTVKSTDKPAASSGPADGGSGDEEFAGGGQAASGGGDSMCLRGGGGGGVAAAAFAEHGRSASEGAASSVGGGGGGDMDQSSAGNTSTTRWSNSSRDPWLSSNSCNMDAHRSVGLSSPIENLEPCRSSSSQVSNHELSSPSLEFTLGRPDWHGADHD
The following text describes a protein:
Function:
Functions as an intracellular molybdate sensor. The ModE-Mo complex acts as a repressor of the modABC operon, which is involved in the transport of molybdate. Binds modA promoter DNA in the absence of molybdate, however molybdate binding confers increased DNA affinity. Binds the promoter of moaA activating its transcription; binding is not enhanced by molybdate. The protein dimer binds the consensus palindrome sequence 5'-TATAT-N7-TAYAT-3' and a variant 5'-TGTGT-N7-TGYGT-3'. Acts as a regulator of the expression of 67 genes, many of which encode molybdoenzymes, acts both directly and indirectly. ModE also binds tungstate.
Subcellular Localization:
Cytoplasm.
Domain:
Deletion of the C-terminus (from residues 122 on) results in constitutive repression of modA. Contains two major domains: the N-terminal domain I forms a winged helix-turn-helix motif and interacts with DNA (Probable). The C-terminal domain II is the olybdate-binding component and contains a tandem repeat of the Mop domain, each of which forms a beta-barrel (Probable). The N-terminal domain plays a major role in the dimerization of the protein whereas the C-terminal domain contributes to the stability of the complex (Probable).
Sequence:
MQAEILLTLKLQQKLFADPRRISLLKHIALSGSISQGAKDAGISYKSAWDAINEMNQLSEHILVERATGGKGGGGAVLTRYGQRLIQLYDLLAQIQQKAFDVLSDDDALPLNSLLAAISRFSLQTSARNQWFGTITARDHDDVQQHVDVLLADGKTRLKVAITAQSGARLGLDEGKEVLILLKAPWVGITQDEAVAQNADNQLPGIISHIERGAEQCEVLMALPDGQTLCATVPVNEATSLQQGQNVTAYFNADSVIIATLC
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MLSQKLWKSQRIELYFLPPQINKTKEYPNSIEFFVPHSNIWIINCVYTNKLQIHNYCRIINGNLDYHQFYVSFLNNLNDLFFTQNDHNVCLYQSQDIFIIYLFILIFCCISPQCLLTSIPNNFKILLQLFDYSNLSTLNHLNFNNLDVFVFTPYTVYLELKLYQIAFHILQYQIDKKTLPQFKHTDSYNNIILQRMSLLLNEFLLLHSIFINLFFLSFNFSNNDYTKKDTQLSITSNSQNQSIKHFRTTQFNQNQQKFFHLTQQKITIVVIILLGPKIWKSHFSIKYSRIFTMIKQDDAESTDIRINIQSEILAIILSYLIKHDLTVSLLYSYKFRFIKTITTHHQMWMKCIQQNEIPCQKLQQVQFSLDQITSNIIHNHIDTTVLRIQLLEYLRLKQNQQTFTIYSKIIINKILSLLLTPNLISYHLSTNSETYTLVLDMDETLIYYDGDKVHQRPFLLTFLKQMSRLYQLILFTAGLESYANRILSQITIKKYFTHLLFRQHTNIYQDFYGKDLRKLGRLLSRTIIIDNTPECFSLQPENGIQIQTWKGEQSDSILLNLIPILKALRFSNKDVRMKLREYKNCPGLIFPK
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Subcellular Localization:
Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MADASVDEVLALKNQFYLGSFQTVINEATNPATTPRTETGKLDRRVLLHRAYICHGRFNLVLSELSAQETSMELRAVRILARYLASMTDQLQQQEAVADAVALAEMIPFDVSPVVYVLLGTVFYHEGQTEEALKLLVRAPKHLECIALAVQVYLKMDRPDLAKKELDLFKSWADDATLAQLIESWVNIAVGGPEKYQEAYYIFEEMANTGTSTCRLLTSKAVAMIQARKFEEADAILLEALNKNPNDPDTLANMVIIATALQKPTSVLNQFMSQLKDVAPHHPLVQEQLLKESLFDRSAMRFSQTA
The following text describes a protein:
Function:
Plays a role in mitochondrial morphogenesis.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MAEENYGVVPRDELQDAALERFMASKVSVIVIEDNQLSGRVASSIQVGNLMHKTAVLASLGCLVGGAMHAPLKTVLLPLGGLGLLCGISYDLGWQDDPMAAYQVLKRPDAPELTSVQLPAHLDDFTVLVRRDDSVRRVLHNTLMLAAGAFLFFRWRRI
The following text describes a protein:
Function:
Could be involved in the unfolded protein response (UPR) pathway.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MDQGTVDSPVTLVIKAPNQKYDDQTINCFLNWTVEKLKKHISNVYPSKPLSKDQRLVYSGRLLQDHLQLRDVLRKQDEYHMVHLVCASRSPPSSPTSDSHFSTTDSSSSTSDSAGPSLSSTPSQEAQANSDGLRHRGNPAATHGLNPAPTGVMQRPEGMPLPMQGGPAAGFPTHPMYMPMQMFWWQQMYARHYYVQYQAAIAASRASSVAPSPSLSAGPATQPVQPNEPAAPMGPNPAPEDRPANPNIQMNAQGGAMLNDDELNRDWLDWMYTVSRAAILLSIVYFYSSFGRFVMVIGAMLLVYLHQAGWFPFRAELQNPRAEEGAQDEADQNQDMQEMERMMDEGIEDDEGDSGEEGPDDPMNPGPHQPGFLSATWSFISTFFTSLIPEGPPQAAN
The following text describes a protein:
Function:
Required for carboxysome formation; the N-terminus interacts with CcmM which itself binds RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS), while the C-terminal 18 residues interact with carboxysome shell protein CcmK2. Required for growth in normal air; Beta-carboxysome assembly initiates when soluble RuBisCO is condensed into a liquid matrix in a pre-carboxysome by the RbcS-like domains of probably both CcmM58 and CcmM35. CcmN interacts with the N-terminus of CcmM58, and then recruits the CcmK2 major shell protein via CcmN's encapsulation peptide. Shell formation requires CcmK proteins and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully encapsulated carboxysomes are formed, they migrate within the cell probably via interactions with the cytoskeleton.
Subcellular Localization:
Carboxysome. Note=This cyanobacterium makes beta-type carboxysomes.
Domain:
The N-terminus interacts with CcmM, while the 18 C-terminal residues (encapsulation peptide) are required for interaction with the hexameric shell proteins (CcmK2) and are predicted to form a helix. The 2 regions are separated by a linker.
Sequence:
MHLPPLEPPISDRYFASGEVTIAADVVIAPGVLLIAEADSRIEIASGVCIGLGSVIHARGGAIIIQAGALLAAGVLIVGQSIVGRQACLGASTTLVNTSIEAGGVTAPGSLLSAETPPTTATVSSSEPAGRSPQSSAIAHPTKVYGKEQFLRMRQSMFPDR
The following text describes a protein:
Function:
Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Subcellular Localization:
Peroxisome membrane; Single-pass membrane protein.
Sequence:
MADPPASSPADEARDPGISEAAHGTSTTQDTKEQEDMKGEAAVATSEPVREELVQSAVSFLSHPKVVASSDVQRRSFLENKGLTMDEIEEAFRRLLLSPPSNSASSDACKPPGAPDPETVTPVAPRHPKSYMEVMEMIQRGERPDDIQDINDEPPNPDQPISKPSMAPKPKPWEKQGQQSSGWDLKVHSSDPSESSSGVRTDSTSQATGSNNSSGHGDLMLTAEPATGEPGGLDKYLDTILDPKSA
The following text describes a protein:
Function:
Small adapter protein that modulate the activity of CLPC (By similarity). Involved in plastid biogenesis in particular when chloroplast protein synthesis capacity is a limiting factor. Probably involved in substrate selection for plastid Clp protease system. Recruitment to ClpC chaperones is facilitated by CLPF thus forming a binary adapter for selective substrate recognition and delivery to plastid Clp protease system (CLPC).
Subcellular Localization:
Plastid, chloroplast stroma.
Sequence:
METAICGRLALAPSSLFNSKSGDKHLVSKGPCVNRSILMTLSTSAALGKGGGVLDKPIIEKTTPGRESEFDLRKSKKIAPPYRVILHNDNFNKREYVVQVLMKVIPGMTVDNAVNIMQEAHINGLAVVIVCAQADAEQHCMQLRGNGLLSSVEPDGGGC
The following text describes a protein:
Function:
Aquaglyceroporin that may modulate the water content and osmolytes during anhydrobiosis.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MRKRRREQEVNEREEEETLISSTAASPPSYSYLSDYQGVSMREPDVALLGNVHSNPMDQMEDQPYIDNEHHQISPPPKKRSLKERLIAVQQMDKAMSFNLVDRIRQRAHITNELYRAVLAEFFCTAFLLFAGCCVNAQYIISKTRYNEWIGVSVGWGLSLFIAVCMGHRISGAHLNPAVSFFQLTQGKISPIRFFLFVIAQNVGAFVGAMFCFLVYYDAINSYDGGDRQVTGNRATAGIFATYPAPYLSMLGGCFDQVLGTAILCIGIGTIVDRRNRVPPFIQPAFIGLLLMLIGMTLGMNCGYAINPARDFGPRLFTLVAGYGWRVFDYRDYKWFWIPIICPMIGAVFGAWIYEAFIGFHMPDDPETTLVIDNPNHSVGSPNTMETSSSSPTRRRFTDDEKSYNNS
The following text describes a protein:
Function:
Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins.
Subcellular Localization:
Nucleus.
Sequence:
MSAAVLSLVERACNTETGVDDARVAAVNDIAQQVSERRLALVDLVVALHGPLTSPEKEAREHGTRLLGEVVARARAALNAGELHTLAEFLAARLRDWPCVGAAAAACCALLQPPDAAAAATAAAGSSAAAELLRDDSALVVMEAAAEMLRTAQSFRQEERGALLQLLLQLAAPGRRWAALAAGRRSGGAAATSAAAAAPVSGAAASGAAGGEGGAAGGGGGGGGGGGAAPPPPPDLLDAFLGAADGEKDPRCLLLAFQAVQALCALHHAPGADAAPLKALADEVVDWASAYFPIAFNPPPPRPGAGSAPAAISRQQLAAALEGALAASPFLAGSALPLMLEKLSSTYRPAKEDALGALRRCCPAYGPDALGPHVAQIWPALRSEVMAPITAAGGAAAAPAPAGGLGGPGGLGGPGGDGEGRLALARAAAGCLTVVVRAAGPGAMDAAALQDAAVTDLLAVVRRAAAAAASAASPAAAAAAAAGALAASAGGSAAGWRADVTVLCGAMLLAAVCAAGPAATERAQPAVLGPLLALLRGSLEPAPAHPDAATAALSTEAADAAAATAGTSGGSSSVQDRWNQTLYGLHVLTSVVAAVAAELAPGPSGNDGGSSGGSSNGIGIGGGGSGAGPWLGPAGAGGIEALAEVRTGLTACLALLQPLLDASSGSSSDGDVAADLAAAAGCYSPVAAAQLRLAAVAAWRALLSLHAAALAAPAATAVAAAARDKLLLPPAELQAAARQMAACALSDGVAAVAADGAGAAVACRMAWGRGMDVGAEAEAALRQLLLLQPQQPLADGTAAEAGAVAPLLVSSLTEAMGRQGPARAAALRLAVQLASAAGGSSISSSNGSSVSSAAATAACGGDGTASFAAALLEALSPLLLRQARDASADDEAWLHDCLSQLSSRVLPALAARPPTDTHRAAAAAAAQRLAAAALGAAADAWAAGGCRGLPFGDAAAAAAAAAAAAVSSSAGAEAPALQRQGGGGDEAAEAAAQLVSGWAGLAQQLAAVCDDRQQLALAMDAAECIATASGSSSGSSSSAAVAAGWVRLPLACGLVAGLRPAVLAPQSTQALADSLLRLLAAAPGAATPPLPEHTACAACVALGAAVNRWQDAAALDGWVAGSFRPALLARLPGSSSSNGSSSSSIRGGAAATHAAAVGWVGRALALRNHAALGDVIQALLGVLAAAATATVAATATAAEAGAPTDMEVEGGVGDGPHAPARSQATAEAASAAAEAFGVLVAEQAASGGVGLPARPAAAVCRVLWQQRTLSLCIQSLSSAVSPQQLRPPTDAAAALLPLPLATAVACLVSAAPRGLCRAESARLTPLLLGSVLRLCAELGPGADADGPAAATATAATATAAAGGPAPQPQPQPQPPGAVAQAAAALSSALGVLGDWLALQATQPAPALGQALQDHVPELVACVCAAAVAVPPPPAHPSLTTSASAAAAAAAAAAAAAAAVAVREEGLRCVLALMDAVPYHLLHPLRAKVLAVIVRALDDDRRSVRQLAVRARRTWSDK
The following text describes a protein:
Function:
Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSEPEDQGVIEYGSEVLRPCGDSESNQAEAQGAQSASSRAGPSSNYSPPIGPEDEEDQEEGQDVGLPGGSAGPSTKKKKKKSKGKALSKNPSEVPADDGSLVEDHTTSEAHKMIIEQIRAQNGDEVADRISALGPKELGKMMDQIRLLEMMDGKSGGTHKNKKDMADHKFWATQPVRRLDEQDSSFEEGEIEPSKSEEEIRKSPLALPDGYEWCTLDLGDESQLRELYELLTVNYVEDDDAMFRFDYTAPFIEWALRPPGFVQDWHAGVRVASGKRRLIAFIAGIPMNLQVRSTRKPCAEINFLCIHKKLRSKRLAPVLIKEITRRCNMQGVFQAIYTAGIFLPTPISRCQYFHRNLNPAKLIATGFSPQPRGVSVARLKRMYDCPAQPQIPGFREIEEKDVDAVAVLLRLYMSRFDLIPVMSDEEVRHNFISGKGTGPVVNGRRNQQVTWTFVVENPTTHLITDLVSFYHLPSTAMKCTPHQTIDAAYLFYYATTAAPSCAHLGQPAQVQEEPSQVAVTEPTEQPNWSAEAPEARQILKKRLISLIGDALTMAQQANFDVFNALTLMDNSLFVKELQFGAGDGYLHYYLYNWKVHQIRGGVPGEPGSEEDAAQATSSGKQLIEAPGVGSGIGVVML
The following text describes a protein:
Function:
Plays a role in mitochondrial DNA base excision repair (BER) pathway induced by oxidative stress. Has apurinic/apyrimidinic (AP) endonuclease activity towards double-stranded DNA (dsDNA) with a preference for C as opposite base. Has 3'-phosphatase activity; removes 3'-phosphate from blunt-end, recessed, and gapped DNA templates and thus, removes 3'-blocks for DNA polymerase activity during BER. Lacks 3'-5' exonuclease activity and does not cleave damaged bases by nucleotide incision repair (NIR).
Subcellular Localization:
Mitochondrion.
Sequence:
MPRHCCCFVFHFLLYMLLINIVKNNIITAFSHRHQALRERKNIFSNSPINYIYYLGANKHIYSKFSSVCEQKKLAHKKIAIKKWGIERNEKKKFTISLNNYNKIQQSKFMSKMVKENKASTKNENKCSINNTQDIRNFMNLKKEEKDEECDEKTKQDNNKENIKNETIVQKKKIDKNNKTKEKIKTKSETNKNTNITYPSIPKSIEKRWADYKKIIEYAKSTNVYLGAHISASGGVQNAPINSFNVSGLAFALFLKNQRKWESPPLTEENIKQFNENCKKYNFDKNLILPHGSYLINLANPDKEKREKSYLSFVDDIKRCEQLNIKLYNFHPGSTVGMCSTEQGIKNISDCINRAHKETSNVIIVLENSAGQKNSIGSKFEHLRDIISQIDDKERIGVCLDTCHTFAAGYDIKSYEKFEEVMNNFHNIVDSKYLKAVHLNDSKSDLGSGLDRHENIGKGKLTLDTFKYIMTSKYFKNIPIVLETPDITNDESVYKYEIEYLYKMCAKEQ
The following text describes a protein:
Function:
Involved in seedling development in the dark. May be involved, when interacting with TSK, in the organization of spindle microtubules and may participate, when interacting with GIP1, in structural links between the nuclear envelope and the cytoskeleton.
Subcellular Localization:
Endoplasmic reticulum lumen. Nucleus envelope. Cytoplasm. Note=In interphase, found in ER bodies and at the nuclear envelope. During mitosis, concentrates in limited areas close to the ends of spindle microtubules ahead of separating chromatids.
Domain:
Contains a N-terminal NAI2 domain (474-759).
Sequence:
MEIYTMKTNFLVLALSLCILLSSFHEVSCQDDGSGLSNLDLIERDYQDSVNALQGKDDEDQSAKIQSENQNNTTVTDKNTISLSLSDESEVGSVSDESVGRSSLLDQIKLEFEAHHNSINQAGSDGVKAESKDDDEELSAHRQKMLEEIEHEFEAASDSLKQLKTDDVNEGNDEEHSAKRQSLLEEIEREFEAATKELEQLKVNDFTGDKDDEEHSAKRKSMLEAIEREFEAAMEGIEALKVSDSTGSGDDEEQSAKRLSMLEEIEREFEAASKGLEQLRASDSTADNNEEEHAAKGQSLLEEIEREFEAATESLKQLQVDDSTEDKEHFTAAKRQSLLEEIEREFEAATKDLKQLNDFTEGSADDEQSAKRNKMLEDIEREFEAATIGLEQLKANDFSEGNNNEEQSAKRKSMLEEIEREFEAAIGGLKQIKVDDSRNLEEESAKRKIILEEMEREFEEAHSGINAKADKEESAKKQSGSAIPEVLGLGQSGGCSCSKQDEDSSIVIPTKYSIEDILSEESAVQGTETSSLTASLTQLVENHRKEKESLLGHRVLTSPSIASSTSESSATSETVETLRAKLNELRGLTARELVTRKDFGQILITAASFEELSSAPISYISRLAKYRNVIKEGLEASERVHIAQVRAKMLKEVATEKQTAVDTHFATAKKLAQEGDALFVKIFAIKKLLAKLEAEKESVDGKFKETVKELSHLLADASEAYEEYHGAVRKAKDEQAAEEFAKEATQSAEIIWVKFLSSL
The following text describes a protein:
Function:
Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule's plus end. Transports cytoplasmic vesicles and particularly phosphatidylinositol 4,5-bisphosphate-containing liposomes along microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
Domain:
The PH domain is required for kif1-mediated transport probably through its binding and docking onto membrane of cargo vesicles.
Sequence:
MNVQVAVRVRPFNSREKERNAELIVQMNNKSTILTRPSALRANPLAAPTADDEKSFSFDYSYWSYDSNDPHFASQSTVYNDLGKEVLKNAWDGFNCSIFAYGQTGSGKSYSMMGYGEEKGIIPLICEELFQRIQSTPSNSNEQTIYKTTVSYMEIYNEKVKDLLNPNNNKTGGLKVRNNPSTGPYVEDLSKLAVKSFSEIDMLMDEGSKARTVASTNMNATSSRSHAVFTIVFTQSKIDKTRGTAIDRVSKISLVDLAGSERANSTGATGVRLKEGANINKSLSTLGKVISALAENSTSKKAVFVPYRDSVLTYLLKETLGGNSKTIMIAAISPADINYEESLSTLRYADSAKKIKTVAVVNEDAQSKLIRELQGEVERLRAMMDQGGQYHANDSKLMNSDYDETVSTLNEKIEQYEKLMAELNKSWEEKLSEAEAIREDRMAALKDMGVAIKVVSSIPHLINLNEDPLMSESLIYYVKEGKTRIGRSDSEIPQDIILNGLNIHKEHCIFENINGKVIISPSNNFMNNNNNKENSSSTTPTSSKSPSKPKSEKEKENNNDDDDGEKKLDRSYIYVNGVEINKPTILTTGNRVILGNNHIFRFNNPEEAIKIARERNQTTGGIVSSTKSPVDQIMDYDFALNELASIQGTLAMSKHINDKQEYKKQMRALYDQIRLQLENDCDPEVKEQREKLALLAFRRWRSKVHRSKLLNKISFIILSLNEANAISSTLNKKINLSLKLYSVFPEPDQISDNIEPEIDWRKTQILIKATDSSTGESTLVTDQDFVDRIYLMRELYQNDGRLDTELPEDPFQFTFTKDSLIGVSHVYLKNTLYLVESNRPVPILDENGNQKGYLNLLVSSSSTDITESERGLYLENPSNNKSLLLGKNLEITIGFEGFSEFIDENKFSDVFIKFNFPNQNGTIVDTFLTEPQPISAFIDQKRIVITSLTESLINLLQTQYVSFEIRGHKKSKQQPKLTSSSSSASTTSSSSKNQPMLENFEFLATLNILESEKNTGTDDQYKPVHILEDPDVYNTHLPSVTFRLKKDKTNRQILFKVIKNESNSIIKECKSARISDIKIFGKRDNPLLSSSATPNTPNTPNNSRIAGIQNTPGTPMTPYSNQTNNQQSSSSQPPLPQQQGTPYNPQSNNPNVISNAPPTPNSNLLKDLSLAANVQTSSSSSSSSLNVLLNNQQQQQQSQQSQQQQQQQSQQSSETSSTTNSITNSASNSSLSLLVNNQTTNSNNSGGNIFEIPVLSCTDDSVLLLWKTNDPSFIFNQKTRKGDKILFKLTFDLLIQGFPDVVSISKDIAIKILSSESMPSATMPDGTSSSSMSNLLDKFKTHFKGESILSEPSIHAGSVFSINLTKSRQQEHQNRIGEMIDAHQENILKLGYAMKMEKLRQELDLREKLTNLKEKTIDSTNTDDVNAANGVAESSNSSTIDVEEIVKKMLLMNSTHQQQQQNFSSPSSTSPTLVNGESSPKSGRSSNTTSSSSGGGGGGGRKRSSTIVEVKVKEVPSSALLKEDETSGYLKKKSAFKEEWKPRWFVFKKPYLYYSHNQKDTHKLKKIDLTNSSVAITQDEVPFGFAIIQLRRVWLLQANSVEDRDKWVQTLDPLRKVTELKDEELRTAKQQIEKSSSQLDQIKSQLQTGQQIVLAKQKEIEELTNTISQLQLEKEINTQQFDGLRDEIQNRDEELEQYKSQQSQKINQLSGQVNKLENVTQEKELTIGSLSSTLNNTNQIIELINEQSKSYKNVAEMEIESLRDETTQLRETSQLLANRLKECRSSIQSAESLLSERDLEITQLKALLTQQEESSGITSLNLKNLQSDQTMKQGQIDILSKTVQQSTATIQNISSQLDSTTKASDSKDEQITSINSAYKDESDRLKDQTTQLNSLTTNLRQQMRSLEQTHLQQKETSASDQKTLLLLLHDMEQGLTRASQTITDQSAQVTVLKKQLEDSKKSNEQLPTVEKQLSLMKDRLIQSENQLIDRECENTILSDKLKLWEEEIKIKDSKLSLLENNVKEVRAEYANGMAFSREFSQHHTDSGSISGKFNRRSKQISAEEQMETLRESSIAHQSHNAFLNSQIQRLETEMRTQEKVYSDTIQRIKKDLQQRNQQNIAFMKHQVGDEIVKKMEDVTASMEILKKKYFVSLVVAAKLQNAMMGNICNVDAYELYEQSVVEHILDQDQWPNWIAQTISTQNKHL
The following text describes a protein:
Function:
Involved in the regulation of D-galactonate metabolism. Represses the expression of the dgoRKADT operon by binding to two closely spaced inverted repeats in the cis-acting element, which overlap with the D-galactonate responsive dgo promoter. Employs a derepression mechanism using D-galactonate as a specific effector molecule.
Domain:
Contains an N-terminal DNA binding region and a C-terminal effector-binding cavity. The C-terminal region also contains a metal binding site. The divalent metal ion is not directly involved in the interaction with DNA, but it plays an important role in interaction with D-galactonate.
Sequence:
MTLNKTDRIVITLGKQIVHGKYVPGSPLPAEAELCEEFATSRNIIREVFRSLMAKRLIEMKRYRGAFVAPRNQWNYLDTDVLQWVLENDYDPRLISAMSEVRNLVEPAIARWAAERATSSDLAQIESALNEMIANNQDREAFNEADIRYHEAVLQSVHNPVLQQLSIAISSLQRAVFERTWMGDEANMPQTLQEHKALFDAIRHQDGDAAEQAALTMIASSTRRLKEIT