lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers.
Sequence:
MNRLQAMELFVSAVREGSFSAAGRRVGLSPASVSRYIGELEAQLGVQLLNRSTRHLGLTDAGKIFFQRTEQVLHGIEDAEAAALSLQTAPRGTLRVHSRTLFGIRVLSPLIPGFQKLYPELKVELRLSERRPQLREDEFDVDFQIQAAKDPGLMLRRLLRSERILVASPDYVGRMPKLREPEDITRHNCLTYWMGPDDVVWKFMRRNRLREIVVPSSFGSNNGVVLCDLAVAGHGIALLDDYTVAEQLKSGRLVRLLPGFRVTNSTFDEGIYATFLQSSYLPEKIRVFVDYMAENVPRQVKRSAQ
The following text describes a protein:
Function:
Receptor for hyaluronate.
Subcellular Localization:
Membrane; Single-pass type I membrane protein. Note=Colocalizes with TLN1 at the membrane ruffles.
Domain:
The C-terminal domain interacts with the N-terminal domain of RDX.
Sequence:
MRPGTALQAVLLAVLLVGLRAATGRLLSASDLDLRGGQPVCRGGTQRPCYKVIYFHDTSRRLNFEEAKEACRRDGGQLVSIESEDEQKLIEKFIENLLPSDGDFWIGLRRREEKQSNSTACQDLYAWTDGSISQFRNWYVDEPSCGSEVCVVMYHQPSAPAGIGGPYMFQWNDDRCNMKNNFICKYSDEKPAVPSREAEGEETELTTPVLPEETQEEDAKKTFKESREAALNLAYILIPSIPLLLLLVVTTVVCWVWICRKRKREQPDPSTKKQHTIWPSPHQGNSPDLEVYNVIRKQSEADLAETRPDLKNISFRVCSGEATPDDMSCDYDNMAVNPSESGFVTLVSVESGFVTNDIYEFSPDQMGRSKESGWVENEIYGY
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MPRSFLVKKIKADGFQCSGVSAPTYHPLETAYVLPGTRGPPGDNGYVAHCLPPSGYDGEQKPGLELAPAEPAYPAAASEEYSDPESPQSSLSARYFRGEAAVTDSYSMDAFFISDGRSRRRRAGAGGDAAGAGDAGGGGGGGGGGERAGRSGATAGGGHRHACAECGKTYATSSNLSRHKQTHRSLDSQLARKCPTCGKAYVSMPALAMHVLTHNLRHKCGVCGKAFSRPWLLQGHMRSHTGEKPFGCAHCGKAFADRSNLRAHMQTHSAFKHYRCRQCDKSFALKSYLHKHCEAACVKAAEPPPSAGPAS
The following text describes a protein:
Function:
Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
Subcellular Localization:
Cytoplasm.
Sequence:
MVTLMMSGGARRLAPWATWHWQNPIGEVSIELHKPTQMRGRASSLIDLPFRTIAKLLGSDQVTLINTPSIMQKYLGESEKALRQYFAPAEEAVARLGEASPTYVLIFDEIDAIFRERGSGDGSSASLAYDSVVNSLLTLMDGLKEQNNIIVIGMTNQRGLIDKALLRPGRFEVQVEIALPDVTALAFRTGRFSGAEIAGLVRNAASLAIARAEEAGAPLLDHGKLNRVYQQVQQTDFLKSIDASEPAFTTPTHTIARDYLPMGWMRTRKANEQVLHTLQEHIATSTSPEASTSDALRILITGAGGVSLRMHLLGLLFCQGLKFYVFLWHLRLCLDITTGVGKTALAVVTGAELVGLTDLGKVNRIRRAFTSAHAARTAVVLLDDLDTIVEYLHIANQAVFSHALASSLQALLASKPPPSCKLVVLATRTAMPSHSGLLPSTAFDLKNLLRVQSQAATAGWQSERTVLPPWSGGRRYMSNSWQLKVWTWATMKLVLALVVVAGQLAWVYATMIRPRVK
The following text describes a protein:
Function:
Involved in the mineralization and structural organization of enamel. Involved in the extension of enamel during the secretory stage of dental enamel formation.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MLLSCRHGASSPKLDNLVPSGKMKILLVFLGLLCYSAAMPMQMPRMPGFSSKSEEMMRYGHFNFMNAPHMAHLGTLYGNGMQLPQFFPQYQMPMWPQPPPNKKHPQKPSASKQQSKTDPAPESQKPNQPQPKTPTPKQPLNEPSPTPTQPEEETQTPQAFPPFGNGLFPYQQPLWHVPHRIPPGYGRPPTSNEEGGNPYFGFFGYHGFGGRPPYYSEEMFEQDFEKPKEKDPPKTETPATEPSVNTTVPETNSTQPNAPNPRGNDTSPTGTSGQGPNPRSNPTGQNGPAVNVSGQGVPRSQSPWGPRQTIIHENYPNPNIRGFPARRQWRPPGPAMGHRRNGPFYRNQQIQRGPRWNSFTLEGKQAVRPGYPTYRRVYGSTARSNPPNYAGNSANLRRKPEGPNKNPMVTNVAPPGPKHGTVDQNENIQNPREKQVSQKERTVVPTRDPSGPWRNSQDYGINKSNYKLPQPEDNMLVPNFNSIDQRENSYYPRGESKRAPNSDGQTQTQIIPKGIVLEPRRIPYESETNQPELKHSAYQPVYTEGIPSPAKEHFPAGRNTWNQQEISPPFKEDPGRQEEHLPHLSHGSRVHVYYPDYNPYDPRENSPYLRSNTWYERDDSPNTMGQPENPHYPMNTPDPKETIPYNEEDPIDPTGDEHFPGQSRWDMEELSFKEDPTVRHYEGEQYTSNQPKEYLPYSLDNPSKPREDFLYGEFYPWNPEENFPSYNTAPTVSSPVESRGYYANNAVGQEESTMFPSWSSWDPRIQAQGQKEGRPYLNRNFWDQSTNLYKTPTSSPHQKENQPYSNNSPAGLQKNPTWHEGENLNYGMQITRLNSPERDHLAFPDLIPPDYPGGQKESHVFHLSQRGPCCAGGSMWPKNNPLALQDYTQSFGLAPGENPDTSIGYAEDSHIKYARQTVSPTSIVPGQRNSSEKILPGESQNPSPFKDDVSTLRRSTPCSVKSQLSQRGIMPLPEANSLQSKNTPCLTSDLGGDGNNVLEQIFEGNQLNERTVDLTPEQLVFGTPDKEPRPEGIPNEMQGNESERQQQRQSSILQLPCFGSKLANYHTSSIGTPSSLGRQDSFDGDPIMPTETPNSLAGLATGAQFQNINVDPLNEDEHTPFDSLQIGTNPQDQVQDCLLLQA
The following text describes a protein:
Function:
Binds and compacts DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation.
Subcellular Localization:
Cytoplasm. Chromosome.
Sequence:
MGELPIAPIGRIIKNAGAERVSDDARIALAKVLEEMGEEIASEAVKLAKHAGRKTIKAEDIELARKMFK
The following text describes a protein:
Function:
Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Sequence:
MAEANQLFKEFKIQSVSEFFRRNAAMLGYTGKVRSLTTLVHEAVTNSLDACEEAGIPPYVRVEIEELGNEHYKVVVEDNGPGIPEKYITHVFGKMLAGTKAHRNIQSRGQQGIGISGAVMFAQITSGKATRVITSTGNDEIIEAWVKIDVDKNEGKIVKKEKHPNPKGWRGTRIELEVKNVKYMRSKQGVFWYLKLTAIANPHAHIELIEPDGKLIVFPRSSDYIPEPPVEMKPHPKGVLTDDVYRLAKKTRRNTVRRFLIGEFSRISDKKVDELIEYIAALRLIKTVEDKKLQEQYYQKLMEGHVKAVLRAFKGYTKVVKQVAKMMEKPPEKLTWHEAEEIVEAFKYMKFLAPPTHGLRPIGEENIEKGLKGILKPEFVTAVTRPPKVYSGGIPFQVEVGIAYGGEIPAGFDLYRYANRVPLLFDAGSCVTTQAARSIDWKRYKIDDLDRAPLVLMINVVSVHVPYTGTGKQSIASVDEIYNEIRLAIMDAARRLQTYLSGKHRKLAQVKRRKTFEKYVPEIARALSILTGEPEEKIREYFIRFIESKFASAEVEEVAAEEVAENA
The following text describes a protein:
Function:
Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12. Isoform 6 increases water and sodium absorption in the intestine and gall-bladder.
Subcellular Localization:
Cytoplasm, perinuclear region. Apical cell membrane. Cell junction, focal adhesion. Cell projection, lamellipodium. Note=Found at the Z-disk sarcomeres, stress fibers, dense bodies and focal adhesion. In pancreatic acinar cells, localized preferentially to the apical membrane. Colocalized with vinculin and filamentous actin at focal adhesions and lamellipodia of pancreatic cells.
Domain:
The first 2 SH3 domains are required for WASF1-binding. All 3 SH3 domains can bind independently to PTPN12.
Sequence:
MSYYQRPFSPSAYSLPASLNSSIVMQHGTSLDSTDTYPQHAQSLDGTTSSSIPLYRSSEEEKRVTVIKAPHYPGIGPVDESGIPTAIRTTVDRPKDWYKTMFKQIHMVHKPDDDTDMYNTPYTYNAGLYNPPYSAQSHPAAKTQTYRPLSKSHSDNSPNAFKDASSPVPPPHVPPPVPPLRPRDRSSTEKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQHERPASLYQSSIDRSLERPMSSASMASDFRKRRKSEPAVGPPRGLGDQSASRTSPGRVDLPGSSTTLTKSFTSSSPSSPSRAKGGDDSKICPSLCSYSGLNGNPSSELDYCSTYRQHLDVPRDSPRAISFKNGWQMARQNAEIWSSTEETVSPKIKSRSCDDLLNDDCDSFPDPKVKSESMGSLLCEEDSKESCPMAWGSPYVPEVRSNGRSRIRHRSARNAPGFLKMYKKMHRINRKDLMNSEVICSVKSRILQYESEQQHKDLLRAWSQCSTEEVPRDMVPTRISEFEKLIQKSKSMPNLGDDMLSPVTLEPPQNGLCPKRRFSIEYLLEEENQSGPPARGRRGCQSNALVPIHIEVTSDEQPRAHVEFSDSDQDGVVSDHSDYIHLEGSSFCSESDFDHFSFTSSESFYGSSHHHHHHHHHHHRHLISSCKGRCPASYTRFTTMLKHERARHENTEEPRRQEMDPGLSKLAFLVSPVPFRRKKNSAPKKQTEKAKCKASVFEALDSALKDICDQIKAEKKRGSLPDNSILHRLISELLPDVPERNSSLRALRRSPLHQPLHPLPPDGAIHCPPYQNDCGRMPRSASFQDVDTANSSCHHQDRGGALQDRESPRSYSSTLTDMGRSAPRERRGTPEKEKLPAKAVYDFKAQTSKELSFKKGDTVYILRKIDQNWYEGEHHGRVGIFPISYVEKLTPPEKAQPARPPPPAQPGEIGEAIAKYNFNADTNVELSLRKGDRVILLKRVDQNWYEGKIPGTNRQGIFPVSYVEVVKKNTKGAEDYPDPPIPHSYSSDRIHSLSSNKPQRPVFTHENIQGGGEPFQALYNYTPRNEDELELRESDVIDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL
The following text describes a protein:
Function:
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant.
Sequence:
MKVQLIASTILEDPSWAGTDYVGDDETVTSADELAEFAGRNCYLSFDRPNPKTRENVDYLNHILDVGHESVLEHSSATFYIEASRSVLTELERHRHLSFSVVSQRYVDPTELGIHVPPAFTELSGSDADKAKEVLLDVQSFAQEAYEYLVHIFSDAGFPRKKAREAARAVLPNMTNSPMVVTGNHRAWRYVIKNRWHEAADAEIRELAGELLRQLREIAPNTYQDIPTEPYSYGG
The following text describes a protein:
Function:
Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme.
Sequence:
MKRDAEANNSDSPDKYPKCTAEKEGADQEPATISPSSTRLDRQLRLWGNWGQERLKDAGVGICDSSATSTQIAKNLILSGAKSVLMMDTAKVRQSDIGNNFFLEQASLGKTRAEESGKLLEQLTSTFKYHPVYWHDWEFYNEDFWCELEDIDALADWNAFIGVRMVKADEEVTSRFGWGFNVPTFSVQTCGLVASIRLQIRELYVFQTPSDSFVDLRLDCPFPSLSTFANSFEMDKMNHREHAHVPAVAIIVHYLERFKSKHDGKLPQDSTQRAELKEMILAEKRDVDEENFDEAVNLIGNACQPTEVPTHIQELFDDPYCDKAPWFDGSFWLLVKTLREFVKRDPNHQLPLSGAIPDMKSNTKNYVKMESIYRQKASEDLQTFNSILDDVKDSSEPDDDDNDDDNGETETESGFHHYGPEYQLSSEMIETFVKNCAHIRLIRGSKYTNDQPKDLMLKFSKECEPGNQEFTANWFLGFQALSAYRLAKQGEYPGMRKGQEEHDFNSLSEIALKDLIRRGWDKDEKKVPEKLAKVLKEMVRSSGSELPHISSIVGGLVSQEVIKMTTGRYVPMNGICIFDGYRSTTGVLEF
The following text describes a protein:
Function:
Cohesin cofactor dispensable during the meiotic division but playing an important role in DNA repair by homologous recombination (HR) probably by helping SMC5/SMC6 complex. Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair.
Subcellular Localization:
Nucleus.
Sequence:
MRHGLWGFGPGLDGLGAGPPPLALMHSSEGARDPYSGTGVTGSAMMDSSPDAGDLVLDLGISSGVSMPKLRVLGPKVVPDLDSAPGSSMSDAAALLFPDIVPVAKTSTDDADSADSKGSTELEIDFEAIPKKREPKPNKLMNPDEGYKLSWLRVNRQKSGCRKVHSNGHNLSAAPKISSRKRRTPQKVNVEPDAGETTVARDGEALVARDLAGKKSKLSIVGGRMSNFNKAVSEGSGVPGRRLVGRKIKVWWPLDEMFYHGVVQSYDPFRKRHKVLYDDGDTETLNLHKERWEFVEDDLPDEQRWEADLLKPESSPVKSSPVKREYKKGSSKKSHLPRKLMIKQNIERAEASSRVPEVIVPQFGNQNVGRDESSDDESTEDNLYELRVRSNDVQQKYPSSSSSDDSTPEASPPRPWWQK
The following text describes a protein:
Function:
2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of fumigermin that inhibits germination of spores of the inducing S.rapamycinicus, and thus helps the fungus to defend resources in the shared habitat against a bacterial competitor. The partially reducing polyketide synthase fngA alone is sufficient for the production of fumigermin. FgnA catalyzes the condensation of 3 malonyl-CoA units to an acetyl-CoA starter, and 3 methylations to yield fumigermin. It is remarkable that the five cluster genes including fgnA are conserved in distantly related fungi, supporting the assumption of a fumigermin cluster; it is thus possible that originally all five genes were functional, but that the genes encoding tailoring enzymes became inactive from mutations, similar to the case of the fgnA gene in strains A1163 and Af293 (Probable).
Sequence:
MTVNGKDIDSPNAQYVAAGIDMSDLFPAPFPTNVKTVHLETLSLAKLLQRDEDELRRIYENCKDPGFFQLDLTDDEQGVQLLQDAVDCARLMKQLLPNMSVEEKRMYKQHSRVGVYSKGYQVYDVLPNGQPKYNETVNFPMTEMLGYGDSTVDLPDWLSPHRELFQRTMRSGNKIANIVLAALEVGLQVPRGALTDAHRIQDPSDDFLRLLRYPGLQPGQPRDDLCFPAHKDFTSLGILFTWLGGLQLLASASAPGVTSGTMTGPLDIAEDAWRWVQPVPGTAIVNVGNALEILTNKALTSGLHRVVRAPGEQLPFDRYSVLVGTRPANSFPMKPLQSPQISPVLDPAAAEIATMTSGQWGTHNIGSFNNWVKARTERQEVLIIP
The following text describes a protein:
Function:
Required for the correct female sexual development of the soma and germline in hermaphrodite animals, while being fully dispensable in males. Has calcium-dependent proteolytic activity and is involved in the cleavage of tra-2, for which it acts as a potentiator. Capable of calcium-dependent autolysis. Part of the necrosis cell death pathway. Required for necrosis of intestinal cells induced by B.thuringiensis endotoxin Cry6Aa.
Domain:
The calpain catalytic domain is essential for in vivo function to promote female sexual development; The C2 domain associated with the domain III is primarily responsible for calcium binding.
Sequence:
MTRSEKTRHFGNQNYEKLRKICIKKKQPFVDTLFPPTNQSLFLEQRQSSDIVWKRPGELHPDPHLFVEGASPNDVTQGILGNCWFVSACSALTHNFKLLAQVIPDADDQEWSTKHAYAGIFRFRFWRFGKWVEVVIDDLLPTRDGKLLFARSKTPNEFWSALLEKAFAKLYGCYENLVGGHLSDALQDVSGGVAETLHVRKFLKDDPNDTELKLFNDLKTAFDKGALVVAAIAARTKEEIEESLDCGLVKGHAYAVSAVCTIDVTNPNERSFTSFIMGSKRKQNLIRLQNPWGEKEWNGAWSDDSPEWQNVSASQLSTMGVQPANSDSDDGDFWMPWESFVHYFTDISLCQLFNTSVFSFSRSYDEQIVFSEWTTNGKKSGAPDDRAGGCHNFKATFCNNPQYIFDIPSPNCSVMFALIQNDPSEGLKKREPFVTIGMHVMKVENNRQYRVHTAMHPIAISDYASGRSVYLHLQSLPRGRYLLIPTTFAPKEQTLFMLRVYSDEHIHFSPLTKHAPKLGLLKCKSAQSVTRLTIHGVDFNSASTGTHNVYAILKDSRKSFRTKTLSGVKSIQWDEQFLFHKSKNRQQYKIEVWEDRKMARDHLLAQSVIIALIDNENRDTTLQLTDPRGTVIGTVSVTVSAFDDPMYL
The following text describes a protein:
Function:
Not known, does not seem to act on the proton translocating NADH dehydrogenase genes (nuoA-N) which are part of the lrhA operon.
Sequence:
MINANRPIINLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEACSSLMFSNLQGVLTIGASDESADTILPFLLSRISSVYPKLALDVRVKRNAYMVDMVKSQEVDLVVTTNQPHSLDCLNLRTSPTHWYCAAEYVLQRGEPVPLVLLDDPSPFRDMVLETLNAAGIPWRLAYVASTLPAVRAAVKAGLGVTARPVEMMSPDLRVLGAADGLPPLPDTEYLLCRDPNSQNELAMVIFHAMESYQNPWHYNQFSAEGGDDPLMVEGGFE
The following text describes a protein:
Function:
Plays an essential role in the initiation and regulation of chromosomal replication. ATP-DnaA binds to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex once per cell cycle. Binds the DnaA box (a 9 base pair repeat at the origin) and separates the double-stranded (ds)DNA. Forms a right-handed helical filament on oriC DNA; dsDNA binds to the exterior of the filament while single-stranded (ss)DNA is stabiized in the filament's interior. The ATP-DnaA-oriC complex binds and stabilizes one strand of the AT-rich DNA unwinding element (DUE), permitting loading of DNA polymerase. After initiation quickly degrades to an ADP-DnaA complex that is not apt for DNA replication. Binds acidic phospholipids.
Subcellular Localization:
Cytoplasm.
Domain:
Domain I is involved in oligomerization and binding regulators, domain II is flexibile and of varying length in different bacteria, domain III forms the AAA+ region, while domain IV binds dsDNA.
Sequence:
MNLTQIWKATLSALQTQTSRHDYEALLRPATLLSLDNGAAFIGVSSPGQKEGLENRLLMPLRNALARVVGYPVQVQVLIANLNSRTEPSPSLTLSNGSRLMSDPEPVVAETPAPALTPGNGTGERVVQLDLASAMRSGMLNPRYTFSSFIVGSSNRLAHAACLAVADNPGQAYNPLFLYGGVGLGKTHLLHAIGNRVLDRDPEINVLYVSSEKFTNDLINAIRRQQTEEFRMRYRNIDVLLIDDIQFIAGKDATQEEFFHTFNTLHSAAKHIVISSDRPPKAILTLEERLRSRFEWGLIVDVQPPDLETRTAILRAKAEQMSVHVPDEVIDFLAHKIQSNIRELEGSLNRVAAYAELNRAPITIETATAALADLLGNQRRRRISAEAILQIVSEHYGIEVEQLRARNRSRHVVVPRQVAMYLLREETESSLVDIGNLLGGRDHTTVMYGCEKIAEEINSDSRLRSEVMAIRERIQMLRG
The following text describes a protein:
Function:
Involved in regulation of mitochondrial membrane ATP synthase. Necessary for H(+) conduction of ATP synthase. Facilitates energy-driven catalysis of ATP synthesis by blocking a proton leak through an alternative proton exit pathway.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MMLFGKISQQLCGLKKLPWSCDCRNFWGWLNAVFNKVDHERIRDVGPDRAASEWLLRCGAMVRYHGQERWQKDYNNLPTGPLDKYKIQAIDATDSCIMSFGFDHLEGLQHVEKIRLCKCHYIEDNCLERLGKLENLQKSILEMEIISCGNITDKGIMALYHLRNLKYLLLSDLPGVREKENLIQIFKTALPSLELKLDLK
The following text describes a protein:
Function:
Molecular scaffold protein for various multimeric protein complexes. Acts as a module in the assembly of a multicomponent scaffold for the ERK pathway, linking ERK responses to specific agonists. Also involved in response to hypoxia (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MVKISCNKVLSNHSGSVTVVKYNSDGGYCLSGSSDKSIKLYNVSKGSMIHSFEEHGYGIGDLVSTSDNKQLFSCAEKQLYQWDIASGQVIRRFQNAHNDTITSVCVNLDSTLLFSGSSDRLVKAWDLRTKSINPVQILDDAKDTITSIIVNEQTITHNHSHGHGHSHGNNNNNQPHTHTQKEVITSSVDGCIRTYDVRMGTLVTYEDTIPISSVSITKDKKCFIASCTDETVKLIDIDSYETLKEYKGHKNKVYKINSCSNFDDSLIISGSEDNDFYIYELLSGKLLSKLSGHSNIITHVDSHPSKNQFITSSTDCTIRIWDQSE
The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MLCASKIKHDEKSYRNIFSYIFQKIKRKRKQNNYVFTKNIINDVLCIRDSIKKDEIEEEEKKKKIIEEKEGTFLINFVNEKNKIIYDNINDLNKYCIDKFKKYKCDVYISTSSNREYVPYYIYDFFINYPLLKWYITNKTTHKISDNYMNSNRCISSNYHMCRKKKKKYNNFRECKRVYYIQKNIKRYSMNNLFDNKNNICKYLILNKKRLEANNLFNLIKYYNVHKKELFLSSLEHKKLDNINFDSYIKLSLIKNFNVKYLTTVQYVTFPLFLKNYDLLISSFKSSGKTLAYMNCLVHKIIIQINNLRKKTNIKDNYVLGLIICPNVILVEQSYGILKKLIMYHPYNIICYYMHGKKYINIQDEIKNLKKKRPHIIITTPGYLMNFIKYFKNFSQIFFLCDTLIIDEAHFLVDNNYMKNILIIKNILPKSHQTILLTCIVNNFLKNLAYRFLRLHYIHINLINNCIYDHEQLLDPSINQQYQETNKNIIKNIQHITNNINHMNKSKYQLIVQNGFKRLINFNLQLYNELNNKHIYPPNNILFYDNIGKLWYPKEANIFFQNVQSQYNLDNDNITLEEKKKNKNKIIIKKNKIIIKKNNIIIKKNNNNNNNNNNNNVDINDDTQIYDSSKESNYILPFSKKEMKIKKLKLSNSDYNRYHCSHHNKNDNKYIPTHVLLKQEYLIYESNKLSLILFNILHNELITNNNINIVIFMPTVKILQFFYVIYKHYIFKGYIFLLYLKLKKIKWKHPQDIKSYLANHSTYYDKDTVNFTVSSNPYIITNDSTIYQNFNVIHSYDHSVNTNHIIKNDEFTIKRNGEFTIKRNGEVTIKRNGEVTIKKNDDVTIKQNDDVTIKQNDDVTIKQNDDVTIKQNDDVTIKQNDEVTIKQNDNFTNEHMCNYLLNYIQQCTDEYEELKDVSILSLHSKMSLDKKRYTLNCFNGTNLDNEDDEKKKKKKKKKILFATSLLHQGIELNKVNLVIHLGMCKNVDEYILRTNIVTTKYTRGRSLLLLNELEAHYLYILYKNNIPITPINKNYINLVYKNNLLLQHLLNYKYDMGTHEMENINTDIKHKCDKKMNDTNKNIDDQKNIYHENNCSIQIQTFNNYYYKKDENNFFQYNYHNEKDYKNIFFTFNIKHIEWHKYKHLLSSCELMYRSFLGFYCEKNEFLKYEKWQVPSLIKNIIYSFGYLENFYITKCMAARLQIINAPDTFIKFNATSKSVLISSLPTYKSYKSKTNEFKLKKCANQNSTNINTPNINNYNKHNTNYDYLKDDDPLNDFNLLKPNDENQNMQTHPLYFTFHKYVS
The following text describes a protein:
Function:
Amphipathic alpha-helical antimicrobial peptide with potent activity against Gram-positive bacteria, weak activity against Gram-negative bacteria, and moderate activity against fungi. Mainly acts by causing membrane permeabilization, but is unable to forme pore-like openings (Probable). Is also able to penetrate eukaryotic cells (keratinocytes), and kill intracellular S.aureus (both wild-type and MRSA) without injuring host cells. Shows inhibitory effect on biofilm formation of Gram-positive bacteria, but not of Gram-negative bacteria. Shows antiviral activity against herpes simplex virus 1 (HSV-1) by disrupting the viral envelope. Also displays anti-leishmania activity by damaging parasite membrane. Does not show hemolytic activity. Acts synergistically with temporin-L that improves temporin-1Tb activity by preventing its self-association in lipopolysaccharides (LPS). In vitro, promotes cell migration and wound healing.
Subcellular Localization:
Secreted. Target cell membrane. Target cell, target cell cytoplasm. Note=Contact and insertion into membrane begin at the N-terminus.
Sequence:
MFTLKKSLLLLFFLGTINLSLCEEERNAEEERRDEPDERDVQVEKRLLPIVGNLLKSLLGK
The following text describes a protein:
Function:
Cell wall formation.
Subcellular Localization:
Cytoplasm.
Sequence:
MKNIEIFLKENRIPYKKYESLAKYTTLRIGGYADFVVFPDEDSVLKLLEIIRNEGTAYYVIGGGSNLVVHDEGFKGVIINTKQMKRINLEGFTIRTSAGVMLPRLLAFVLKIKLSGIEGLIGIPGTVGGAIKGNAGSFGYEISDCLAEVEIITDKLETKILKKQDITFQYRSSNLVETWLIKSATFSLKEDDGEAFNRMKQFLQRKKQTQPLREYSAGCVFKNPEGQSAGYLIEKAGLKGFRVGDILISHLHANYFINVGKGKANDFLKLMDIVKEKVFKLFSIELVPEIKILEA
The following text describes a protein:
Function:
Mitochondrial GTP/GDP transporter required for GTP uptake and GDP exit from mitochondria. Involved in mitochondrial iron transport and essential for mitochondrial genome maintenance.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MPHTDKKQSGLARLLGSASAGIMEIAVFHPVDTISKRLMSNHTKITSGQELNRVIFRDHFSEPLGKRLFTLFPGLGYAASYKVLQRVYKYGGQPFANEFLNKHYKKDFDNLFGEKTGKAMRSAAAGSLIGIGEIVLLPLDVLKIKRQTNPESFKGRGFIKILRDEGLFNLYRGWGWTAARNAPGSFALFGGNAFAKEYILGLKDYSQATWSQNFISSIVGACSSLIVSAPLDVIKTRIQNRNFDNPESGLRIVKNTLKNEGVTAFFKGLTPKLLTTGPKLVFSFALAQSLIPRFDNLLSK
The following text describes a protein:
Function:
Transcriptional repressor regulating endoreduplication through control of A-type cyclins expression. Does not bind to promoter sequences (in vitro) and may act by interacting with tissue-specific transcription factors. Enhances the endocycle in endoreduplicating cells in seedlings. Required for efficient splicing.
Subcellular Localization:
Nucleus.
Domain:
The C-terminal region (474-908) is responsible for the repressor activity.
Sequence:
MGSNRPKNFRRRGDDGGDEIDGKVATPSSKPTSTLSSSKPKTLSASAPKKKLLSFADDEEEEEDGAPRVTIKPKNGRDRVKSSSRLGVSGSSHRHSSTKERRPASSNVLPQAGSYSKEALLELQKNTRTLPYSRSSANAEPKVVLKGLIKPPQDHEQQSLKDVVKQVSDLDFDEEGEEEQHEDAFADQAAIIRAKKERMRQSRSAPAPDYISLDGGIVNHSAVEGVSDEDADFQGIFVGPRPQKDDKKGVFDFGDENPTAKETTTSSIYEDEDEEDKLWEEEQFKKGIGKRMDEGSHRTVTSNGIGVPLHSKQQTLPQQQPQMYAYHAGTPMPNVSVAPTIGPATSVDTLPMSQQAELAKKALKDNVKKLKESHAKTLSSLTKTDENLTASLMSITALESSLSAAGDKYVFMQKLRDFISVICDFMQNKGSLIEEIEDQMKELNEKHALSILERRIADNNDEMIELGAAVKAAMTVLNKHGSSSSVIAAATGAALAASTSIRQQMNQPVKLDEFGRDENLQKRREVEQRAAARQKRRARFENKRASAMEVDGPSLKIEGESSTDESDTETSAYKETRDSLLQCADKVFSDASEEYSQLSKVKARFERWKRDYSSTYRDAYMSLTVPSIFSPYVRLELLKWDPLHQDVDFFDMKWHGLLFDYGKPEDGDDFAPDDTDANLVPELVEKVAIPILHHQIVRCWDILSTRETRNAVAATSLVTNYVSASSEALAELFAAIRARLVEAIAAISVPTWDPLVLKAVPNTPQVAAYRFGTSVRLMRNICMWKDILALPVLENLALSDLLFGKVLPHVRSIASNIHDAVTRTERIVASLSGVWTGPSVTRTHSRPLQPLVDCTLTLRRILEKRLGSGLDDAETTGLARRLKRILVELHEHDHAREIVRTFNLKEAV
The following text describes a protein:
Function:
Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MSQANLLSPPTHIPPPTALALSQKAPLILSHPPTSSLPWPLSLLFSRETPESWTIHENLFYSALRTGDETSAQAILQRLEARFGDQNERIITLRGIYNEATAQSDADLERVFEGYEKILKEDPTNMSVRKRRVAVLKALGRTQDAITAITVLLQNSPTDVEAWAEASELYASQAAWGQAIYCAEEVLLIMPNAWSAHAHIATLHYLSATSTTPPSLSALSLSLKHFCRAVELNDSYLRGYYGLKMLTSKLLPLLSESATVSSKRGNNQNDDDDIPIPKIETVRKLEEIATSKLGEIVRNASAGKAPGFDQAEVIAARELLDTDGKIER
The following text describes a protein:
Function:
Acts as a decapping enzyme capable of hydrolyzing monomethylated capped RNAs (in vitro). Hydrolyzes monomethylated capped RNA after alpha and beta phosphates to form N(7)-methyl-GDP. Shows low activity towards unmethylated capped RNA.
Sequence:
PVLLILSGMSGFRVKVYRNGSRLEFLPSLVDILQTDDPKGVVSDNEVKVDLCLKNERLLISCNTISKISSDYYRAVNLKRPSFCPFRCLPKNMASEIPQEIKCQGVDVGVALLLESMDHKVLLTRRSQHMRTFPGVWVPPGGHIDKNETLTDAVCRELKEETGVVVKDSSIDVLGLWESTYPPCLEWGLPKRHHIVIYMHCNHSEHSREINKNIKLQIEETDSCIWVSSSEISNTKSDTHKCNDHEIITCSQLVNGGTVEKQMVINHLLADFSKNKTESGNNERISTGTKYALKLWLDKVFSHQYLIY
The following text describes a protein:
Function:
May be involved in protein transport.
Sequence:
MSASGVLSFTQQGWEQVLAKVKRAVVYLDAACAESLHWGCGSTRLLEAVGGPDCHLREFEPDAIGGGAKQPKAVFVLSCLLKGRTVEILRDIICRSHFQYCVVVTTVSHAVHLTANHVPAAAAAEMEGQQPVFEQLEEKLCEWMGNMNYTAEVFHVPLLLAPVAPHFALTPAFASLFPLLPQDVHLLNSARPDKRKLGSLGDVDSTTLTPELLLQIRCLVSGLSSLCEHLGVREECFAVGSLSQVIAADLANYAPAKNRKKTAAGRASVVFVDRTLDLTGAVGHHGDNLVEKIISALPQLPGHTNDVMVNMIALTALHTEEENYNVVAPGCLSQSSDTTAKALWEALLNTKHKEAVMEVRRHLVEAASRENLPIKMSMGRVTPGQLMSYIQLFKNNLKALMNHCGLLQLGLATAQTLKHPQTAKWDNFLAFERLLLQSIGESAMSVVLNQLLPMIKPVTQRTNEDYSPEELLILLIYIYSVTGELTVDKDLCEAEEKVKKALAQVFCEESGLSPLLQKITDWDSSINLTFHKSKIAVDELFTSLRDIAGARSLLKQFKSVYVPGNHTHQASYKPLLKQVVEEIFHPERPDSVDIEHMSSGLTDLLKTGFSMFMKVSRPHPSDYPLLILFVVGGVTVSEVKMVKDLVASLKPGTQVIVLSTRLLKPLNIPELLFATDRLHPDLGF
The following text describes a protein:
Function:
Part of a putrescine export transport system, does not play a role in resistance to antimicrobial peptides. Stimulates K(+)-uptake proteins TrkG and TrkH to import K(+), may act via ATP-binding rather than ATP hydrolysis.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein.
Sequence:
MPLLDIRNLTIEFKTGDEWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVNKDNWRVTADRMRFDDIDLLRLSARERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIVTPRLTGAKNHLYACHFPLNMEKE
The following text describes a protein:
Function:
Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Sequence:
MGRGRHRKGGPAPSHRADADWDALASNESLPVEVPEEDANGNVKVKLPIHLAMWDFGQCDSKRCTGRKLSRLGFLRDLRVHQHFGGVVLSPVGTKCVSREDRNLMRVKGLAVVDCSWSRLPSVPFAALRCGAPRLLPWLVAANPVNYGRPCKLSCVEALVAALYICGEQLTAEALLGKFKWGHGFLSLNKELLDAYAACKTADEVIEVQDEFLASNKGGRSDAPDERYAGSGSDDDLPPLVRNINHLDIEGSDDEESDDEDDDDVDDGEEEEDEEEDGAVVQASHKAQDQERVNKKPVHYDWDQEEETEDAEVDDEVEADDNSKVGQQASTKAKDQSATTKQPHHKSKQKRGGRK