lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in both the arginine and lysine biosynthetic pathways.
Subcellular Localization:
Cytoplasm.
Sequence:
MRFQAHRGLKLIRGEGQYVWDSEGRRYLDAHTGHGAAFLGHRPRKVVDAIKEQLDKLMVASTTFSTDAMEDCLSSLGKILPSKLNNVYFQNSGAEAVELALKLAFKATGRRGLLSFKNGFHGRTLGALSVTWNREYREGLPLLRAEFGEFNDISSADLINDETAAVILEPVQGEGGIEPSRRDFLVELRRACDEAGAVLIFDEVQCGFGRTGATWAHQSRGVEPDILIAGKSIASGFPISLVAAKDWVIEGLRAGFHGSTHGGNPLACAALKASIELFIEENVPEAARKMGKSLASMISEYAELKGEGLMLGVRVKQPGRAIRSLQASGVLALKAGEDMVRLLPPYCITEEDCSFLSGRLRRVLSEQSS
The following text describes a protein:
Function:
May play a role in sperm motility, especially in the regulation of flagellar function.
Sequence:
MKRWQVCQDLRSNTFEEAALTEHYEILTTLGQGTFGDVKLANHLVTQTKVAIKILPQNRKNPLVQPEIEIMKSLDHPHIIKLLHIIDTTRNIFIVLEHAVGGELMNRIEEFGYLAEVECHRLFKQLVYALQYCHEKGIVHRDLKPENILLDHRGNVKLTDFGLGTKIIMGQKLVTFCGTLPYCAPELFEDRGYDGRATDVWSLGVVLYFMATGCLPFNGYSYEAIKQKIIAGKYPRSFSLSPELWEVIAKLLTVNPGERPTVHDIARFKWLKPDNEASPASLGENIESHPDPSIMVLMGVMGYNPGEIRESLREKKFDQVMATYLMLKQQSAWENKTTKKPDPRLCDRMLRSTEPTIKNQTAVRRASSVPTHSTFSLPNESESLEKGKRTTMSHSMPPTRNCFNEETTPLHSICPQLVQKAHYRRSIWGETEISDTSEESSTGESLEHPSLKIHTLQTSMGVSKAGSTYSKSKGSSQCVSSHHTSVEEDQCEGTNISREINPPLSPVSPQENLMGQLHIVTTAGSMDIMNTQVTSPPFSRKEAKGEGPAIQQRESRPSSPNTLQGHLHGRHQTAPQAPFQRRVWRTLRNGLIRGLRTLCCCLPIEKRVHPTNNRDLAVSQKSQGGSHGIRAFRGTVLPEK
The following text describes a protein:
Function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MSLSLLLRGAVRCNAANLVKSARITPLKSYSTLVANVQRKAVVQPLAVAKIVAPVVREISVSAPRMASAGSSHTLLWTVERIVSAGLLAVIPAAFIAPSQVLDALMAISVVIHTHWGVEAMVVDYMRPSVVGNVLPKVAHIALIIISVATLGGLFYFIQNDVGLANGIKRFWAIKGKDAEKA
The following text describes a protein:
Function:
Major spermidine uptake transporter that is also used by salivary gland-secreted histatin 5 (Hst 5) to enter into candidal cells. A major component of host nonimmune defense systems is salivary histatins, a family of small (3-4 kDa), histidine-rich, cationic proteins secreted by major salivary glands in humans and higher primates. Hst 5 is the most potent of the 12 histatin family members and has fungicidal activity against blastoconidial and filamentous forms of Candida albicans. Hst 5 cojugates to spermidine to be uptaken by DUR3.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MADSYVPLPQSAGYAVVVGLGFVFAFGMMLTTYILRRYNKEVMTAEEFATAGRSVKTGLIAACIVSSWTWSATLNGSTSQVYNNGVCGSIFYAMGATVQITLFACLAIKARERAPAAHTYLEIVKGRYGTTTHFVYIFWGIVTNILVTSMLLSGGSATVNDLTGMNIVAAILLLPLGVVIYTLFGGIKATFLTDYAHTVVLIVIIFIFAFTTWATSSKLGSPQAVWEIVTKLAESNPREGNAGGSYFTMHSRSGGMFFVINIIGNFGTVFLDNGYFNKAFAANPSSTYKGYIFGSLAWCAIPALCSLTMGFAALALEHTEYWPLGRPMTAAEVASGLVLPNAASALLGKAGAVLALLMVFMAVTSAMSAELIAVSTIATYDIYRTYINPNASGKKLIWVSHLSTVIFAYTMAGFAIGLYYAKVSMGYLYEMMGVIIGGAVLSSALTILSKRQNWHAATFSPIISTALAIMAWLVCTKKKFGSVTYLKTFEDDAMLTGNCVALLTPFIIVPILTFIFKPQNFDWKLLDQRITRVDEEEELAEALGGTVSSDPERLHPIKSQISVIASQLVEGEREQYQKEKEILNKSFKICCIVCCTLAICLVVLFPMPLYGTKYIFSKKFFTGWVVVFIIWLFYSAFQVIIFPIWESRTDLYHTFRGIYWDLTGQTYKLKAWQNEHPEEMHAVRSQLQAQLSRTAVTHEIVDGKAFGDGYVTPANIDDALEEKKG
The following text describes a protein:
Function:
The complex LTO1:YAE1 may function as a target specific adapter that probably recruits apo-RPLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MFRDTEFPLSSGTFTMPQSESTPHNDDFDDVFGSEPGSPTLDGRDMRDGDMFGVGNTEISDIPRLKEKHETEGYRDGVTKGKSESVQKGFDEGYGLGAVLGLRIGKIIGILEGISGAVSVSASKSEGEEWTKEKSRVEELSNNAKNELKTEKVFAREWWGEDGIWKFEVPGEKEGKDVVFPDVAAAHPLLKKWEGIVEEEIQKWSLDMDLMEGNEEDVVLVGQHVKADAVEQRIGAAKTDLNW
The following text describes a protein:
Function:
Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MGKSYVIIARIALLLNLIIAAVSHEAKDFDDSILYKIDFEVPDLDVQPSLGNQLRTFYTPDKEKYDCLIPTLEHQKEEEKSDKPELSPITLLQPIFSALTCTYRIEAYWSYEICHGHHVRQYHEEREGKNVKFQEYYLGKWTDEKMEILTKAWQADIKAGVKPKYKSLKIDNTRYPYFEMEYSDGTMCDIINAPRTTMVRYVCYPHGKNDIYSFKETSSCNYEAIILSSALCPIRALHAEETKELSIQCFNSESKPHRPLSMLRSELKEWVESEADLLVFKEKATENLWPKTDGDLVTLNYGGDMEKVLLEHFRNGDLKVDGDFQQLLLSIAASETGPTPITDLTPLKDFISGKNCLTGGNGWWKYEFCYGRHVRQFHKDKTSEVELFLGYFSEEAHRAWSNANPDKGARRSGFTTSI
The following text describes a protein:
Function:
Bacterial hemolysin that causes cytolysis by forming heptameric pores in target host membranes.
Subcellular Localization:
Secreted. Host cell membrane; Multi-pass membrane protein. Note=In the hemolytic biotype El Tor the 80 kDa hemolysin precursor is secreted as monomer. After binding to target membranes the protein assembles into a heptameric prepore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation.
Domain:
May bind to glycans on target cells via the C-terminal beta-prism domain.
Sequence:
MPKLNRCAIAIFTILSAISSPTLLANINEPSGEAADIISQVADSHAIKYYNAADWQAEDNALPSLAELRDLVINQQKRVLVDFSQISDAEGQAEMQAQFRKAYGVGFANQFIVITEHKGELLFTPFDQAEEVDPQLLEAPRTARLLARSGFASPAPANSETNTLPHVAFYISVNRAISDEECTFNNSWLWKNEKGSRPFCKDANISLIYRVNLERSLQYGIVGSATPDAKIVRISLDDDSTGAGIHLNDQLGYRQFGASYTTLDAYFREWSTDAIAQDYRFVFNASNNKAQILKTFPVDNINEKFERKEVSGFELGVTGGVEVSGDGPKAKLEARASYTQSRWLTYNTQDYRIERNAKNAQAVSFTWNRQQYATAESLLNRSTDALWVNTYPVDVNRISPLSYASFVPKMDVIYKASATETGSTDFIIDSSVNIRPIYNGAYKHYYVVGAHQSYHGFEDTPRRRITKSASFTVDWDHPVFTGGRPVNLQLASFNNRCIQVDAQGRLAANTCDSQQSAQSFIYDQLGRYVSASNTKLCLDGEALDALQPCNQNLTQRWEWRKGTDELTNVYSGESLGHDKQTGELGLYASSNDAVSLRTITAYTDVFNAQESSPILGYTQGKMNQQRVGQDHRLYVRAGAAIDALGSASDLLVGGNGGSLSSVDLSGVKSITATSGDFQYGGQQLVALTFTYQDGRQQTVGSKAYVTNAHEDRFDLPAAAKITQLKIWSDDWLVKGVQFDLN
The following text describes a protein:
Function:
The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin.
Sequence:
MSLTKAERTIITSMWGKISSQADTIGTETLERLFASYPQAKTYFPHFDLNPGSAQLRAHGSKVLAAVGEAVKSIDNVSAALAKLSELHAYVLRVDPVNFKFLSHCLLVTLASHFPADLTAEAHAAWDKFLTIVSGVLTEKYR
The following text describes a protein:
Function:
Component of Polycomb group (PcG) multiprotein complexes; the complex class is required to maintain the transcriptionally repressive state of some genes.
Subcellular Localization:
Nucleus.
Sequence:
MAAQRKHLVRDFNHFITCYVCKGYLIKPTTVTECLHTFCKSCIVQHFEDSNDCPKCGIQVHETNPLEMLRLDNTLEEIIFKLVPGLREKEQQQEIEFWRKNNSKENGEGESPKSKRARIEDEEEENGDQDYHRSDPQIAICLDCLRNNGQSGENVVKGLMKKFIRCSTRVTVGTIKKFLSLKLKLPSSYELDVLCNGEIMGKDHTMEFIYMTRWRLRGENVTFLKQSTVYVVHKSICFSERSYPMVLEYRPRIDFG
The following text describes a protein:
Function:
Cleaves peptide substrates after methionine, leucine, and norleucine. Physiological substrates include EZR, alpha-tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and subsequent apoptosis of target cells (By similarity).
Subcellular Localization:
Secreted. Cytoplasmic granule. Note=Granules of large granular lymphocytes.
Sequence:
LLLLLALKTLWAVGNRFEAQIIGGREAVPHSRPYMVSLQNTKSHMCGGVLVHQKWVLTAAHCLSEPLQQLKLVFGLHSLHDPQDPGLTFYIKQAIKHPGYNLKYENDLALLKLDGRVKPSKNVKPLALPRKPRDKPAEGSRCSTAGWGITHQRGQLAKSLQELDLRLLDTRMCNNSRFWNGVLTDSMLCLKAGAKGQAPCKGDSGGPLVCGKGKVDGILSFSSKNCTDIFKPTVATAVAPYSSWIRKVIGRWSPQPLT
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein; Matrix side.
Sequence:
MSGYTPDEKLRLQQLRELRRRWLKDQELSPREPVLPPRRMWPLERFWDNFLRDGAVWKNMVFKAYRSSLFAVSHVLIPMWFVHYYVKYHMATKPYTIVSSKPRIFPGDTILETGEVIPPMRDFPDQHH
The following text describes a protein:
Function:
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette; In vitro catalyzes a concerted transesterification reaction on branched DNA, as would be expected during integration of protospacers into the CRISPR leader sequence; Cas2 is not required in vitro. This reaction requires a 3'-OH group at the branch point. Binds ss- and dsDNA and ss- and dsRNA with approximately equal affinity. May be able to anneal complementary DNA strands.
Sequence:
MISVRTLVISEYGAYVYVKKNMLVIKKGDKKVEISPSEVDEILITVSCSISTSALSLALTHGISVMFLNSRETPWGILLPSIVTETVKTKKAQYEAIVVRKDNRYGEEIISSKIYNQSVHLKYWARVTGTKNDYKELLDKDEPAAARVYWQNISQLLPKDIGFDGRDVDGTDQFNMALNYSYAILYNTIFKYLVIAGLDPYLGFIHKDRPGNESLVYDFSEMFKPYIDFLLVRALRSGFRLKVKGGLIEENSRGDLAKLIRKGMEENVKEESDHNPKTLIQAIRAHAVKLASSIREGKEYRGFKLVM
The following text describes a protein:
Function:
As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores. Through the acetylation of histones, affects the assembly of nucleosomes at immunoglobulin variable region genes and promotes the recruitment and positioning of transcription complex to favor DNA cytosine deaminase AICDA/AID targeting, hence promoting somatic hypermutations.
Subcellular Localization:
Chromosome. Cytoplasm. Nucleus, nuclear pore complex. Nucleus, nucleoplasm.
Sequence:
MNQISHELAKQPETSSETSAKSIRFPHHDSSASGKGSGRSKMYGTLGSHSELGTANSAQTVGIGSARKTEHSTELHVASSHMASSPPATYFFKTDEERPTFNSVTSFGDLPSISHLRYSSGEPSRYVIRKSKCSFQSPEKLMFESLLSAGLDKTANQMTRLPCRHSCSLNGEPEGQKTSYFSQEPFFPAMRTNVHFANRARSTNLPFSFTSSHSSRKGNRAKKAPEPPFERTISNFTSTPSGESLRVSQRTKQEQKNVQASTRPRKRLQYDAFKKQEHGPMGDHSVNKYFNPLNRSFKDALATMTQNNSETTTQMTLTEADQFAKQQSRKFKKQKTEYMERIKKGTTDFSLPHRNQNSAKSDHLLPNGRSAIQCKHIPYHLNNKVVLKKYFSQFGNVQEVYIKRNKYMAVIYFGDHVSAGAALAKEKGKRLHRNIVMFWHNQKSRIGKEEYLAKGKKIRKNNKSEEENHQNFSLQKPSVKSLGNDNLPSKSLSLTKLELLRGLNQEEELFSSDAQMKHPESVRSAVYGVSSLMSRTAKTSEEKYRILEQRDKILRLAHIKRTDLDKAKPIVGTCPDMCPEKERYMRESRQQLSIFELLPGTSKVDHTAAIKEYSRSSADQEEPLPHDLRPSSVLSMTMDYLITHVMNKMEGNTREWYDFIWNRTRGVRKDITQQNLCDPLTVSLLEKCTRFHIHCAHHLCEEPVSSFDAKINNENMIKCLQSLKEMYQDLANMDIYCKREAEFRAYSVLLNLNNGDVLRELQQFQPTLCNSPEVVFAAQALIALNTNNFVKFFKLVQTASYLNSCILHSYFNQVRRNALKILNTAYTINSQRSTTFPLRDLMHMLLFRDDKEAADFVTYYGLHVSNGWVQLNRLRFKESKRCFKPKISAFIKEKLTGSIGEIINGGPLPSVIQHIPVCSFNKENLYTGENSEIEPSNSDQKTNLNMTALPERSKGDLGSVVHPDRVPPAQPWTRPPSACDSLPQSPFQGLSQKEHRQRPPFDFQSQPRFYHPLSISAPPLAPTLTEQPPPHLSRPVLPSLNAFLELDIKEVVEELVQDIVEEECQEIINFSTALCYTPKEGQRAQIFSCSEETCINLVTLFLEDEIFQTARETLQEFQHFHKCLWRWRNVVINQKKMKRKLRVFPAAPCYVENTNELKALLPSAECPIPKEYFSKGILDLGHAGKLGISCIRLNRLRNEMIHQMKVQYFYQKLLREAAWTPLDLPSLISEHLALQREHVFWKVVLVLPDNEMHPSGDLSRILGNWLKVKFMGAEISKKVNNNAKDKIQTLALFQYIKQQEDWATQVNVCVKVVQGILSDAELETAKSQKDFLGTSGFILLLPVREKNEDSTKIDEFWFSALLQLRKLLEAKPVLPVIPLIILVPIQGKDEIEKDVEKGLLLQDLISSELISDYIIVKISSFLNDLEANLQVSKAVKWLASHSPRHPKLCCQTLSQFVEDGVHREFSRRFFWDRKERRLAGLASQKPGPIIDLYNSVLQFLADVISSEWLSNLSWPVPEFAEPEGTGQLPHLYWNTPRHLAWLKEAVLSFQIPQIDIPPSAPWNFICTTIFQYISQIPSSHQTQPVLQVQVENLLSGIYFKLKDKELASSGEGGFSVKDIPWDAIISLCINHRLKDWMPLTLPTVSEALSRDGEIRVYFSKDHLSEFTRPSSWERARLRTQREIQQSYERSVSDSNQSSKPNDGLGMTVERNDGRGRVTPGKKKEYLPVEASDPSFSREELLSAHLSTCLQQEREESKKFEDQIQQWLTEDPGQLKVSLPQQFTPVNLLQPVALGVNTPALIELQVSRQMENTRSMQEPSTSLSKRLRHLENLIRATREEDRVFDLQLSTLRDLGGI
The following text describes a protein:
Function:
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Subcellular Localization:
Cytoplasm.
Sequence:
MEGLSFGPLSILPSLAEELNPHRVAFLTNTTVERLWLEKAAEGIEEPIRIVIPDGEKYKSLETAVAIWKRLQEEGFTRKSLLIGLGGGVVTDIAGFVASTYMRGTLLGLVPTTLLAQVDAAIGGKTGVNFNGKNMIGTFYLPNFVLIAHETLSTLPEEEIRNGLGEVAKYALLDRKVYALARNFEGISETLIRECALFKVEVVEKDLGESGLRRILNLGHTAGHAIEKLSNYRIKHGLAVSMGLMVASKVGEELYGFDSGKTEELLKKLGLPTGHPFRAEEILEEMRLDKKAWYGRITFVIPVEIGDVVVEEVDEAVLKRALEATRDDSGSGDCQKPGGSA
The following text describes a protein:
Function:
Carrier protein involved in proton-driven auxin influx. Mediates the formation of auxin gradient from developing leaves (site of auxin biosynthesis) to tips by contributing to the loading of auxin in vascular tissues and facilitating acropetal (base to tip) auxin transport within inner tissues of the root apex, and basipetal (tip to base) auxin transport within outer tissues of the root apex. May be involved in lateral roots and nodules formation.
Subcellular Localization:
Cell membrane. Endomembrane system; Multi-pass membrane protein.
Sequence:
MMDGVHILSTPYTLKEAGWISMVLMVLFTVICCYTFTLMRYCFESREVITSYPDIGEVALGKYGRIIVSIILYTELYSCVEFITLEGDNLTGLFPGTSLDLGSFQIDSEHFFGLLAALITIPTVWPKDLRIMFILSGFVMTLTGSLFIIVEVARSNLWNSRNIFISAGYREHS
The following text describes a protein:
Function:
Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. May have a role in synapse differentiation and growth.
Sequence:
MGEILHTDLDSSASPARLEYTSEKHSRHTLEAVNLLRLHRELCDVVLLVGNRKIFAHRIVLSACSPYFHAMFTGELAESRQTEVTIRDIDEHAMELLMDFAYTSHIVVEEGNVQMLLPAACLLQMAEIQDVCCEFLKRQLDPTNCLGIRAFADTHSCRELLRIADKFTQHNFQEARCEEFLLLPVNQLVDIISSDELNVRSEEQVFSAVMSWVKYNVTERRQNLGQVLQHVRLPLLSPKFLVGTVGSDLLIKSDEVCRDLVDEAKNYLLLPQERPLMQGPRTRPRKPVRRGEVLFAGERGNAGADDRRKKRRACAHAYGRSERKEGNGSARSCGGWHCALVAHDETGCTQPVQSRFPAPHEGLHCFVNGSIKLETLQLCATRVPQNAVTEEPNVREVFFFPRYDPQTNRWTKVAPMSTKRLGVAVAVLGSYLYAMGGSDGTSPLNTVERYDPRTNRWSSIASMGTRRKHLGCAVYSNMIYAVGGRDDTTELSSAERYNPQLNQWQPIVAMTSRRSGVGLAVVNGLLYAVGGFDGTTYLKTIEVYDPEQNQWKLCGSMNYRRLGGGVGVVRLPQHEAHYW
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Subcellular Localization:
Cytoplasm.
Sequence:
MTVPAPSQLDLRQEVHDAARRARVAARRLASLPTTVKDRALHAAADELLAHRDQILAANAEDLNAAREADTPAAMLDRLSLNPQRVDGIAAGLRQVAGLRDPVGEVLRGYTLPNGLQLRQQRVPLGVVGMIYEGRPNVTVDAFGLTLKSGNAALLRGSSSAAKSNEALVAVLRTALVGLELPADAVQLLSAADRATVTHLIQARGLVDVVIPRGGAGLIEAVVRDAQVPTIETGVGNCHVYVHQAADLDVAERILLNSKTRRPSVCNAAETLLVDAAIAETALPRLLAALQHAGVTVHLDPDEADLRREYLSLDIAVAVVDGVDAAIAHINEYGTGHTEAIVTTNLDAAQRFTEQIDAAAVMVNASTAFTDGEQFGFGAEIGISTQKLHARGPMGLPELTSTKWIAWGAGHTRPA
The following text describes a protein:
Function:
Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate.
Miscellaneous:
MISCELLANEOUS: Present with 2660 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Chromosome. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. At anaphase, the MCD1 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.
Domain:
The flexible SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC1, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable MCD1 protein, forming a ring structure (By similarity).
Sequence:
MYIKRVIIKGFKTYRNETIIDNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREERQGLIHQGSGGSVMSASVEIVFHDPDHSMILPSGVLSRGDDEVTIRRTVGLKKDDYQLNDRNVTKGDIVRMLETAGFSMNNPYNIVPQGKIVALTNAKDKERLQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLYDRELNEVINQMERLDGDYNNTVYSSEQYIQELDKREDMIDQVSKKLSSIEASLKIKNATDLQQAKLRESEISQKLTNVNVKIKDVQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRDLILKKGEYARFKSKDERDTWIHSEIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDSINGPDTKGQLEDFDSELIHLKQKLSESLDTRKELWRKEQKLQTVLETLLSDVNQNQRNVNETMSRSLANGIINVKEITEKLKISPESVFGTLGELIKVNDKYKTCAEVIGGNSLFHIVVDTEETATLIMNELYRMKGGRVTFIPLNRLSLDSDVKFPSNTTTQIQFTPLIKKIKYEPRFEKAVKHVFGKTIVVKDLGQGLKLAKKHKLNAITLDGDRADKRGVLTGGYLDQHKRTRLESLKNLNESRSQHKKILEELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAIILKLEKLNTNRTFAQEKLNTFENDLLQEFDSELSKEEKERLESLTKEISAAHNKLNITSDALEGITTTIDSLNAELESKLIPQENDLESKMSEVGDAFIFGLQDELKELQLEKESVEKQHENAVLELGTVQREIESLIAEETNNKKLLEKANNQQRLLLKKLDNFQKSVEKTMIKKTTLVTRREELQQRIREIGLLPEDALVNDFSDITSDQLLQRLNDMNTEISGLKNVNKRAFENFKKFNERRKDLAERASELDESKDSIQDLIVKLKQQKVNAVDSTFQKVSENFEAVFERLVPRGTAKLIIHRKNDNANDHDESIDVDMDAESNESQNGKDSEIMYTGVSISVSFNSKQNEQLHVEQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQYRTAVATLLKELSKNAQFICTTFRTDMLQVADKFFRVKYENKISTVIEVNREEAIGFIRGSNKFAEV
The following text describes a protein:
Function:
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Subcellular Localization:
Cytoplasm.
Domain:
The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Sequence:
MQYATITGWGKCVPPATLTNDDLATFIETSDEWIKSRTGISQRHISHVNTSELASVAAKRALAAAGIEGSEIDMIILASASPDTLIPNIASTVQANIGANCAAFDINAACSGFLYGLGLASSQIKSGQCKKVLVVGAERLSFYLDWSRRETAVLFGDGAGAVVVEATDIPGGVLGYELNNDPDGRDILKAGFGTAMDRFSADSLDFYIQFDGQEIFKRAINGMNKLSTQVLEKCGVDKDEVDLVIPHQANERIIDTLVSRMKIPKEKAFVNIANYGNTSAATIPIAICDALEKGLIKPNQTILSCAFGAGLTSAALLLQWGERVTPVQISDAQLPPCDQSGIELVKRAVDYFCK
The following text describes a protein:
Function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Sequence:
MLGARLIYNAAKRPGIPPVLSRSLSLASQMHSYKYVNAREEATDLKSVTDRAAQTLLWTELFRGLGMTLSYMFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAACPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEVEIGANIQADFLYR
The following text describes a protein:
Function:
Monomeric globin with a bis-histidyl six-coordinate heme-iron atom through which it can bind dioxygen, carbon monoxide and nitric oxide. Could help transport oxygen and increase its availability to the metabolically active neuronal tissues, though its low quantity in tissues as well as its high affinity for dioxygen, which may limit its oxygen-releasing ability, argue against it. The ferrous/deoxygenated form exhibits a nitrite reductase activity and it could produce nitric oxide which in turn inhibits cellular respiration in response to hypoxia. In its ferrous/deoxygenated state, it may also exhibit GDI (Guanine nucleotide Dissociation Inhibitor) activity toward heterotrimeric G-alpha proteins, thereby regulating signal transduction to facilitate neuroprotective responses in the wake of hypoxia and associated oxidative stress.
Subcellular Localization:
Cytoplasm, cytosol. Mitochondrion matrix. Note=Enriched in mitochondrial matrix upon oxygen-glucose deprivation.
Sequence:
MEKLSEKDKELIRGSWESLGKNKVPHGVVMFSRLFELDPELLTLFHYTTNCGSTQDCLSSPEFLEHVTKVMLVIDAAVSHLDDLPSLEDFLLNLGRKHQAVGVNTQSFAEVGESLLYMLQCSLGQAYTAPLRQAWLNLYSIVVAAMSQGWAKNGEDKAD
The following text describes a protein:
Function:
Heterotetrameric enzyme that catalyzes the condensation of farnesyl diphosphate (FPP), which acts as a primer, and isopentenyl diphosphate (IPP) to produce prenyl diphosphates of varying chain lengths and participates in the determination of the side chain of ubiquinone. Supplies nona and decaprenyl diphosphate, the precursors for the side chain of the isoprenoid quinones ubiquinone-9 (Q9)and ubiquinone-10 (Q10) respectively. The enzyme adds isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.
Subcellular Localization:
Mitochondrion.
Sequence:
MACLSTSGRVVCGSRRQQAHKLLYQLFGSRPGYTAPSAATGLFSPPKVQQQAMRLYHGLSFSMGKDYPDLLQSPHKCSQSLQYSQSSKANLRQHSSVHTQQPAGPVREFQIDPYIILDDDLKYFYDDVRYLLKSGTSQPELDTIASYYFDGQGKALRPMVTMLMAKAINYHLNNESHQLVHKQRQIALFSEMVHSASLVHDDVIDQSDFRRGKPSVNALWNHKKVTMAGDYILSIASIMIARLRSDDVTIVLSQILTDLVQGEFMQLGSRETENERFAHYLTKTYRKTASLIANALKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEKYPELNPMVMRRFSEPGDVERAFELVHKSHGLEQTRFLAKKHCNEAIRLAQELTESPYQKGLQVVADLVINRMK
The following text describes a protein:
Function:
Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3. Binds RNAs which might negatively affect its histone methyltransferase activity (By similarity). COMPASS recognizes ubiquitinated H2B on one face of the nucleosome which stimulates the methylation of H3 on the opposing face (By similarity). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Implicated in the epigenetic inheritance of lifespan over several generations. Acts in the germline to limit the longevity of the soma, probably by regulating a lipid metabolism pathway that signals from the germline to the intestine, thereby preventing accumulation of mono-unsaturated fatty acids. Methylation in the germline is required for germline development and fertility, possibly by ensuring genome stability. May act redundantly with mes-3 and mes-4 proteins in the development of a fertile germline. Required for RNAi. Functions as an antagonist of hpl-1 and hpl-2 activity in growth and somatic gonad development. Cooperates with jmjd-3.1 and egl-27 to ensure robust transdifferentiation of the Y rectal cell to the PDA motor neuron during larval development.
Subcellular Localization:
Nucleus. Note=Localized in mitotic and mid-late-stage meiotic nuclei but is undetectable in early pachytene nuclei.
Sequence:
MSTHDMNHHPPRKSHSKRDKPSSSNSGPKIENHKCKWAWQKVFETGKSFLRRDGFPQDCKSKEDFERIKRTGVRKTSENMLEDPRKNFESLQQSSVYQTNSFRNPRYLCRAHLRVDSYYCTIPPKREVSLFNMDDNCTEVLLRDFAKDCGKVEKAYVCIHPETKRHMKMAYVKFATVKEAHNFYSMYHAQNLLATKCTPRIDPFLSILNEEYEVATNGQVLPILPDDLASIDPSVLRDLRANFLRDQNEKYELAMRNTYEDEGGMLSGVIMDTSDHYERDYTMDHDVGPSSMKMSPIPPPPIKEESPPPPPPPPVASVSNLAPVPSVQLPYYNNIQPSSSTMHMPEFRPTEPPPSYSREDPYRSTSRSSLSRHRNRSRSPSDGMDRSGRSSSRRTHRRPESRNGSKNANGDVVKYETYKMEKRKIKYEGGNKKYEQVHIKERTAVIRGKNQLENVSSESASGSSSVDTYPDFSDEERKKKKRPKSPNRSKKDSRAFGWDSTDESDEDTRRRRSGRSQNRSSERKFQTTSSSSTRRELSSTHTNSVPNLKSHETPPPPPPKGHPSVHLQTPYQHVQPQMIPATYYNLPPQHMAPPPITTSLPPFCDFSQPPPGFTPTFKPITNAPLPTPYQASNIPQPGLVQIAALSAAPEPFSSIPGPPPGPAPIQEDVGRAESPEKPSLSERFSGIFGPTQREEPAQVEVEYDYPLKHSESHDDRHSLEDMDVEVSSDGETVSNVEKIECMEEKKRQDLERIAIARTPIVKKCKKRMMDELSRKVAEDIRQQIMRQCFAALDEKLHLKAIADEEKRKKEREEKARQEAEKPSNHLIADMMTLYNNQSFASSSRGFYRKQKPIPKSHPKHQEHHHHAKASVSTPVHSSSTSRNSSVAPTPQRTVSTSSSSSSAATSARVSEDESDSDSTPGEVQRRKTSVLSNDKRRRRASFSSTSIQSSPERQRDVSSSSRTSSSSSTSSMKQEETADEKSRKRKLIMSSDESSTTGSTATSVVSSRQSSLEPQQEKTDGEPPKKKSQTDFISERVSKIEGEERPLPEPVETSGPIIGDSSYLPYKIVHWEKAGIIEMNLPANSIRAHEYHPFTTEHCYFGIDDPRQPKIQIFDHSPCKSEPGSEPLKITPAPWGPIDNVAETGPLIYMDVVTAPKTVQKKQKPRKQVFEKDPYEYYEPPPTKRPAPPPRFKKTFKPRSEEEKKKIIGDCEDLPDLEDQWYLRAALNEMQSEVKSADELPWKKMLTFKEMLRSEDPLLRLNPIRSKKGLPDAFYEDEELDGVIPVAAGCSRARPYEKMTMKQKRSLVRRPDNESHPTAIFSERDETAIRHQHLASKDMRLLQRRLLTSLGDANNDFFKINQLKFRKKMIKFARSRIHGWGLYAMESIAPDEMIVEYIGQTIRSLVAEEREKAYERRGIGSSYLFRIDLHHVIDATKRGNFARFINHSCQPNCYAKVLTIEGEKRIVIYSRTIIKKGEEITYDYKFPIEDDKIDCLCGAKTCRGYLN