lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Involved in the behavioral responses to octanol, nonanol, and pentyl acetate.
Miscellaneous:
MISCELLANEOUS: The atypical heteromeric and topological design of the odorant receptors appears to be an insect-specific solution for odor recognition, making the OR/Orco complex an attractive target for the development of highly selective insect repellents to disrupt olfactory-mediated host-seeking behaviors of insect disease vectors. Odor-evoked OR currents are independent of known G-protein-coupled second messenger pathways.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MFYSYPYKALSFPIQCVWLKLNGSWPLTESSRPWRSQSLLATAYIVWAWYVIASVGITISYQTAFLLNNLSDIIITTENCCTTFMGVLNFVRLIHLRLNQRKFRQLIENFSYEIWIPNSSKNNVAAECRRRMVTFSIMTSLLACLIIMYCVLPLVEIFFGPAFDAQNKPFPYKMIFPYDAQSSWIRYVMTYIFTSYAGICVVTTLFAEDTILGFFITYTCGQFHLLHQRIAGLFAGSNAELAESIQLERLKRIVEKHNNIISFAKRLEDFFNPILLANLMISSVLICMVGFQIVTGKNMFIGDYVKFIIYISSALSQLYVLCENGDALIKQSTLTAQILYECQWEGSDRIEIQSFTPTTKRIRNQIWFMILCSQQPVRITAFKFSTLSLQSFTAILSTSISYFTLLRSVYFDDEKKLD
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:
MSGVSVVPYTLAPAAGAGAKPSKKRKKRSKSSASDAKASMVDGGWSKVDIEDMQLEGFQDGCAFELEELTDYHVESAEDEDADVREEKEVVKQEKRDDEEDAPKKTKKKTKRGGKAAKRKEEAVDTVDMKDVHLPKWNKYKLHPLLMQSLQTCDFSAPTRIQERTLLPALVDNRDVVGAAPTGSGKTLAFGLPILSQLLHEREQPGYMKDCKALILTPTRELAIQIHQHLEKMVRHREIGVVTLVGGMAVQKQKRLLTYKPEIVIGTPGRLWDIIDSNHEHMNDLANTLRFLVVDEADRMLQPGSYPELEKIFDTLRRKNNSASSELSNLSDEEDEESEDEDDNDDNDEEDDGEDIDMSTFASGSKVMMLDDVLKMQKKKQEKEKKNAAAKENKKAASPKVETVAPPRHTRQTFLFSATLTIPEGGRFQNGKAKKHRNALSVLERVMKRVGLRGKPAVVDMSIAEADNMGVPGAKAIISEEAQRQMKKQQANVALSLPAGLELCQHEVTESTRDTFLYYFLTQYPGRTIIFLNAIQQVRKLTGLLNLLNLPVFALHAEMQQRQRLKKLDGFRAHAKGILVATDVAARGLDIPSVDYVVHYHIARSTEVFVHRSGRTARADKDGLSISLVSPTDAKYHVQICKMLQRPTGLSDFPFDHRYMQTIDERMRLAKSINDQENAAGKLKSETTWFEQMAAAADLDMDDDLLFELGAKKRNQDGKKKTTANQSVQALRSQLNRLLSTSLRPVGSTRKFRQLHKEIGSQISGDGEYRARDASEDLASKGKKSYKRFRRRK
The following text describes a protein:
Function:
Transcriptional activator that binds to the consensus sequence 5'-[AT]GATA[AG]-3'. Predominantly directs the transcription of intestinal genes such as ges-1, cpr-6, pho-1, ftn-1, vit-2 and lev-11, and itself. Required for gut-specific differentiation, specifically acting with the GATA region-binding transcription factor elt-7 to control normal gene expression and promote normal formation of the intestine. Regulates intestinal gene expression in response to hypoxia to promote longevity. Modulation of longevity may, in part, be the result of regulation of expression of daf-16 isoforms d and f in the intestine. Regulates tissue specific gene expression at basal levels and in response to bacterial infection in the intestine to control innate immunity. Plays a role in the induction of metal-responsive genes, activating gene expression from zinc-activated promoters and iron-dependent promoters and enhancers. May regulate the expression of genes that control sensitivity to oxidative stress, in a mab-3-dependent manner, and osmotic stress, in conjunction with the GATA region-binding transcription factor elt-3. May play a role in sphingolipid signaling by regulating the expression of the sphingosine-1-phosphate degrading enzyme, sphingosine-1-phosphate lyase. May act with the Notch signaling pathway to promote endodermal gene expression. Has a protective role in response to infection by Gram-negative bacteria such as S.enterica, E.coli, P.aeruginosa and B.pseudomallei, Gram-positive bacterium E.faecalis and fungal pathogen C.neoformans. An association with the 26S proteasome regulatory subunit rpt-6, in part, controls gene expression in response to infection by P.aeruginosa. Regulates gene expression during the recovery phase following a bacterial infection. May act with p38-activated transcription factors to control p38 gene induction in response to bacterial infection. Controls lysosome formation in the intestine by controlling lysosomal gene expression.
Subcellular Localization:
Nucleus. Note=Expressed in discrete foci within nuclei of the gut in embryos.
Sequence:
MDNNYNDNVNGWAEMEPSQPMGGLRLPTQNMDPPEQNNESQLSELPRMKIDNDYASPIERQSVITSGTNNYEPKVETVTSFFHTGIDYSNFGMLDQTTMQPFYPLYSGIPVNTLGTFSGYTNSIYDKPSLYDPSIPTINIPSTYPTVAPTYECVKCSQSCGAGMKAVNGGMMCVNCSTPKTTYSPPVAYSTSLGQPPILEIPSEQPTAKIAKQSSKKSSSSNRGSNGSASRRQGLVCSNCNGTNTTLWRRNAEGDPVCNACGLYFKLHHIPRPTSMKKEGALQTRKRKSKSGDSSTPSTSRARERKFERASSSTEKAQRSSNRRAGSAKADRELSTAAVAAATATYVSHADLYPVSSAAVTLPDQTYSNYYQWNTAATAGLMMVPNDQNYVYAATNYQTGLRPADNIQVHVMPVQDDETKAAARDLEAVDGDS
The following text describes a protein:
Function:
Acyl-CoA synthetase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins. Within the pathway, FUM10 is involved the addition of the tricarballylic moieties to the carbon backbone. FUM10 catalyzes the CoA activation of citrate to form tricarballylic acid. The biosynthesis starts with the FUM1-catalyzed carbon chain assembly from one molecule of acetyl-CoA, eight molecules of malonyl-CoA, and two molecules of methionine (in S-adenosyl form). The C18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain. This step is catalyzed by the pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8. The resultant 3-keto intermediate is then stereospecifically reduced to a 3-hydroxyl product by reductase FUM13. Subsequent oxidations at C-10 by the cytochrome P450 monooxygenase FUM2, C-14 and C-15 by FUM6, FUM12 or FUM15, tricarballylic esterification of the hydroxyl groups on C-14 and C-15 by acyltransferase FUM14, and C-5 hydroxylation by 2-keto-glutarate-dependent dioxygenase FUM3 furnish the biosynthesis of fumonisins. The tricarballylic moieties are most likely derived from the citric acid cycle, and their addition to the carbon backbone may involve FUM7, FUM10, FUM11 and FUM14 (Probable).
Sequence:
MDTLTHVLVLPEALERLDSPSIIIPRTANTSEEVVPYAHLTDLTQSLQHDLATLGISVGSKVAIVLPNGLAFVTVLLATIRQRAISAPIHPNSTREECKQIFSLMTPDLVAVMPSEASPAAAAVLAAQDLGLPVASCHRYPQSGRLSFCLALKLVNRGDETSNPSPCMVYSRDHVLAEDKVLELFTSGTTGAPKSVQLTHTNILVAMRIITSAHKITFKDRSFLITPLFHIIGIAGSLLPTLFTGGCAVIPASLPATFWQDCQDYSITWYHAVPTLHHLLLSFPMPKGGVPATLRFIRSGGSDMSLDLFNRLQKLGVPLLEVYGMTETAPAIFCNPFPVTETSTAIKRHPGQYPIPDAVDVMILPPERAPGLEPNGDLDGIENTEPVARLTKELGVKGEICLRGKNIMAGYTNNPAANREAFLPNGFFRTGDLGVIKPRQYLALIGRVKEIINKGGEKISPAEIEHVARLHDQVNDAACFRISDEIYGEVIGLAITAKSAITITAVKKHMRHHVVMFKVPDKVLLVQEIPYNRTGKPRRTLLSEMYDRGELA
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
Domain:
Consists of two domains, an N-terminal nucleotide-binding domain and a C-terminal dimerization domain.
Sequence:
MKNVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDLEALKALDIIVTCQGGDYTNEIYPKLRESGWQGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVDWVSVATYQAASGGGARHMRELLTQMGHLYGHVADELATPSSAILDIERKVTTLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSREEWKGQAETNKILNTSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHNPWAKVVPNDREITMRELTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAAEPLRRMLRQLA
The following text describes a protein:
Function:
Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Subcellular Localization:
Cell membrane.
Sequence:
MFKFFYLLFLTLGHLLGAPFIFFWSFKEKYRHSLKARFFLKDNFLKSEPVFWFHACSYGEVKSLEPIIHALKEPILISVTTNTGFELAAQTYQHSKHIEVRYLPFETLLFAWKKNLKRLKTLVVTEAELWFNVFDTAQKLGAKTMLINARISVRSYPKYQRFSFFYALLFKRIDLILAQSKEDKKRLLNLGAKKVVDFLNIKRFSKPVITSFYPKNPSALNIVLASTHEGEEELGLKAFLELKKTFKNARLIVVPRHPERFKSVQDLLQNTLKTTPFSWECFSSKGFVECDILLVDSLGELNNFYQIADIVILGGSFVKMGGHNPLEPAFFNARLITGEYIFNQVALFELVKPYKIVPKEDLLDALLDYKNLGMARFLENGHDLNELLAFIKH
The following text describes a protein:
Function:
Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Subcellular Localization:
Nucleus.
Sequence:
MSEDGQAPRKRLSLKSRKANKKAKLDDTDKKTMSHRPSSSTSSSSSNSIMSAFARQKVPTFASCPVCNKRLPISWMNSHLDNGCLQSVDSENVCKQMVPQGNATNPATKYVDAVFKNDKVNDCDIFEDDMQVESLASPSRPSEENVCKSATKRKHQPMGSTSPYFKKTTPPPRPSIDGEKLASMSKKISKLSRKLKADRPAQSRYKNKRTKPVEKEEMTNVDQHQETQESHTCTNSVSVLKKSVKTTNTRDCKVVSLPNMGANFLYLDVKELLPNFDDVIAQELALFQMSQTSNADERDINAGLPSDNIVKEDVLPDVTSELSREGGATSHLHEDMSSMDSSSFDDFKSQSSVPSSQSQGFVEDTIDSSKGESVDDSGREDKPRIPYYLQNFNTILTSVLANENDKSLFNEEDMKCIEAFNGLEEAAQKLYVRLFQRKLTWHRQGKLQYPEIAEDLSPVCNMLVKEGFLQNERDLTDVTEVLQHLSAPDLKTLAKSLHIPTTSLPRAQLVQSILNHGKVQRTIFGDGSAMILKRARKLLGGCVRLTKDPRAVFTRVLLLFNLSSSAEEEEKGSGGQQQLQTILMVKMGKVTYPDIPINRPTKIFHSREDLLRYEQAMQFENDIMVAMETNKFHLAHQLHLSAAEVFSSIQQEPEIARYDASLPSFLRCFTASWVYTGILSRGVEVYEKLRQYREAVDLLNSLLSDNLYCSDSHGRWYDRLALNLESHLKQPEEALQAILRGLADPQVRSGHRLALMIRAHRLCDSNNNPKLRARKADVPPIPLRDLPKVTITGRVYPVNQPGYKNVFITTDSYTEDSQDVTICSVEELSLAHYRGQGYEEGIHGEGSTYWTLCLLLLWDVVFMEGVADVFRSPYQSCPLDRYADSFYTSRKAAIDSRLEEIRQADTQTLQDWVSSSWSSHDGQACAGLNWDRFTSVEHAQGLVACMGGQFLAGVCARLLRDARHCRSGLPDLTVWSTVSRKFKVVEVKGPGDRLSQKQMLWLDYFLSLGAQAEVCHVVATGAKKLQKSST
The following text describes a protein:
Function:
Catalyzes the hydrolysis of ATP coupled with the export of sodium and potassium from the cell. May export potassium less efficiently. May transport other cations such as lithium. Sodium/potassium efflux ATPases are involved in salt tolerance and maintaining the membrane potential across the plasma membrane in high salinity (Na+) or alkaline (K+) environments. Is negatively modulated by SIS2/HAL3.
Miscellaneous:
MISCELLANEOUS: Present with 688 molecules/cell in log phase SD medium.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MGEGTTKENNNAEFNAYHTLTAEEAAEFIGTSLTEGLTQDEFVHRLKTVGENTLGDDTKIDYKAMVLHQVCNAMIMVLLISMIISFAMHDWITGGVISFVIAVNVLIGLVQEYKATKTMNSLKNLSSPNAHVIRNGKSETINSKDVVPGDICLVKVGDTIPADLRLIETKNFDTDESLLTGESLPVSKDANLVFGKEEETSVGDRLNLAFSSSAVVKGRAKGIVIKTALNSEIGKIAKSLQGDSGLISRDPSKSWLQNTWISTKKVTGAFLGTNVGTPLHRKLSKLAVLLFWIAVLFAIIVMASQKFDVDKRVAIYAICVALSMIPSSLVVVLTITMSVGAAVMVSRNVIVRKLDSLEALGAVNDICSDKTGTLTQGKMLARQIWIPRFGTITISNSDDPFNPNEGNVSLIPRFSPYEYSHNEDGDVGILQNFKDRLYEKDLPEDIDMDLFQKWLETATLANIATVFKDDATDCWKAHGDPTEIAIQVFATKMDLPHNALTGEKSTNQSNENDQSSLSQHNEKPGSAQFEHIAEFPFDSTVKRMSSVYYNNHNETYNIYGKGAFESIISCCSSWYGKDGVKITPLTDCDVETIRKNVYSLSNEGLRVLGFASKSFTKDQVNDDQLKNITSNRATAESDLVFLGLIGIYDPPRNETAGAVKKFHQAGINVHMLTGDFVGTAKAIAQEVGILPTNLYHYSQEIVDSMVMTGSQFDGLSEEEVDDLPVLPLVIARCSPQTKVRMIEALHRRKKFCTMTGDGVNDSPSLKMANVGIAMGINGSDVSKEASDIVLSDDNFASILNAVEEGRRMTDNIQKFVLQLLAENVAQALYLIIGLVFRDENGKSVFPLSPVEVLWIIVVTSCFPAMGLGLEKAAPDLMDRPPHDSEVGIFTWEVIIDTFAYGIIMTGSCMASFTGSLYGINSGRLGHDCDGTYNSSCRDVYRSRSAAFATMTWCALILAWEVVDMRRSFFRMHPDTDSPVKEFFRSIWGNQFLFWSIIFGFVSAFPVVYIPVINDKVFLHKPIGAEWGLAIAFTIAFWIGAELYKCGKRRYFKTQRAHNPENDLESNNKRDPFEAYSTSTTIHTEVNIGIKQ
The following text describes a protein:
Function:
Zinc chaperone that directly transfers zinc cofactor to target proteins, thereby activating them. Zinc is transferred from the CXCC motif in the GTPase domain to the zinc binding site in target proteins in a process requiring GTP hydrolysis.
Sequence:
MPVPILLVTGFLGAGKTTVVNHLLAHAEGRRIAAVVNDFGAINIDAELIAGASDGVVSLANGCICCSLEGDLLRTLSTLLRRDPKPEYIVIETSGVADPSDIVRNLMDPVILREAPLETVLCVMDAGTPPSALDDALVRAQLRVADIVALSKLDLADEGAGARMREAIRVLRVPAVVVDAQHGEIPAALLFPATIDSAPATREPGPRRPAEERFETLSWTSDHPISLPRLQQAIGRLAPKLARAKGLFETVEQPGRLTVFQFAGGRATLAPGEAPTPGVPRSRIVFIAELGVLSKAELDGILAECVASG
The following text describes a protein:
Function:
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems; Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs).
Subcellular Localization:
Cell membrane.
Sequence:
MPVSTNYRLITPSTTDENLPRMADPLSAGEGTCETLHPRERSKQIDRYLKRESTRFKHYMRKTMRLLLVGAGESGKSTIVKQMKILHKGGYNESERREFTPIILENVRECIMSLVEAMPRLHPPVELKDPELMPSLEYIRACEPKCEVTPEFLSNTQRLWEDDGVQDCFSRANEFQLLDSANYFLDKIEFIMDPDFIPSDQDIVRTRKMTTGVVETWFDINNVTFHMLDVGGQRDERKKWIQCFSDITALIFVVACSGFDLQLREDDSKNRLAESLSLYERLWKNRFLKETSVIVFLNKQDILADKIRSGRTKMQYYFPEYDDYTPPPTIEPAEEQCCCFVTRSMQERQRRKESTFPELGMIQSREFFKVKSFIKDKFTELSTVQNTAIKFRKCCYPHYTCAVDTENIKKVFHYCEDIIQRENLKKYELL
The following text describes a protein:
Function:
Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia. Its preferred substrates in vitro are the diamines histamine and 1-methylhistamine and it could therefore play a role in allergic and immune responses. Has a broad specificity for diamines and can also act on cadaverine and putrescine, two products of amino acid catabolism. It could also act on polyamines, like spermidine and spermine though less efficiently, and regulate various biological processes.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Extracellular side. Secreted, extracellular space.
Sequence:
MGREKLALGWTTVAAVLLVLHMASAEPSPQTLSSKAGVFADLSSQELKAVHSFLWSRKELGLQPSRAPTMAKNSVFLIEMLLPKKHHVLKFLDKGEKRPVREARAVIFFGAQEHPNVTEFAVGPLPRPYYMRALSPRPARRPSWASRPISAAEYTLLHQVVQEATKPLHQFFIDTTGFSYQDCHNRCLTFTDVAPRGLASGQRRSWLILQRSVEGFFLHPTGLELLVDHGSTNAQDWTVEQVWYNGKFYRSPEELAQKYADGEVDVVILEGPLPSGQGAESMEEPPLFSSYKPRGDFPTPINVDGPRLVQPQGPRYKLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERVAYEVSVQEAVALYGGHTPAGMQTKYIDVGWGLGTVTHELAPGIDCPETATFLDTFHYYDADEPVRYPRALCLFEMPTGVPLRRHFDSNFSGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVLEAKMHATGYVHATFYTPEGLHYGSRLHTHLMGNLHTHLVHYRIDLDVAGTKNSFQTLQMKLENITNPWSPSHHLVQPTLKETQYLRERQAAFRFGRTLPKYLLFASPKENPWGHKRSYRLQIHSMADQVLPPGWQEERAVTWARYPLAVTKYRESEQCSSSIYNQNDPWDPPVVFEEFLRNNENIEHEDLVAWVTVGFLHIPHSEDIPNTSTPGNSVGFLLRPFNFFPEDPSVASKDTVIVWPRAEGPNHVQRWIPEDQDCLMPPPFSFNGTYRPV
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:
MDNRIGEMQVFLRVVEAQSYSEAARRLLMTPSTVSKLIGRIEARLGVRLFERSTRRLSLTSEGRMYHDKSVALLAELDGIERGISRGAAAAGGTIRVNTTVSFGIFGLEPLLPAFWQAHPEIVVDISLSDEIVDMYLDRTDVAFRVGPLQASAMVARRIGVVKRRIVASPDYINRLGEPKRVQDLSRHNCLGFNFRRSAPVWPLKESGRIADRAISGSLLANNAQSLRRMAIAGIGLARLADYHVRDDISAGRLVEVLKGTAGDEEQIHALYHGGPRLPFRVRAFLDFMCPRLTDFMEGRARDGRQAVQASGGRIAASSARRSSRKAGS
The following text describes a protein:
Function:
Promotes the exchange of RAS-bound GDP by GTP. This protein is essential for mating.
Sequence:
MRFQTTAISDYENSSNPSFLKFSAGDTIIVIEVLEDGWCDGICSEKRGWFPTSCIDSSKIQNFFSSFHSSNEKDPNAQCCAPFHVEAHLQDSAWFEKHGVQAINSIPSSEEFLRKNLQNDIHHLVKGILTTAAAVSQSIKKEGTQVIVFGIETVRSMVLSFPLIILSTLDENFLSEVAQVFSSLNLLPELSRMGCTYGELCIRFTKLLKQLANKFLFFFRPDVSFPSYFLGSLIAHEIHFLPWDFNMLCSNSVQSAHTNLQPDITSFVAILSLSHEAYHCTENEFWNLEAQKLTENTTQKVLQLVAEDALEAWKLDILEDIDRCIQCCRRFLSANQRINYSSSENNPFSFTSQDVEALKDELSSNLCDLYLWSIDLEQISPSDCLLDNYSLFVDLLVTLKVSLLRIKSIIVQFSERIVFLSLEYKFLTNIQPELNDAEKSQLDGFDLNKTNWFDSKGLVCYLMKQTSPEPLLIRNLLFSFWSCNGKIEQDGKIKTATLVFIINYLLRTDIDSTFFTTIFLNTYASMISSSDLFSILGAHFRFICSLNFGKISFISHEFYRVSKRFLDILLIWFESYLVEELDNSKSIFFLFKIYKVFEVFVVPHFASAEELLHSLSHLLHHPSTKRSHKMLEGKELSQELEDLSLHNSPDPIIYKDELVLLLPPREIAKQLCILEFQSFSHISRIQFLTKIWDNLNRFSPKEKTSTFYLSNHLVNFVTETIVQEEEPRRRTNVLAYFIQVCDYLRELNNFASLFSIISALNSSPIHRLRKTWANLNSKTLASFELLNNLTEARKNFSNYRDCLENCVLPCVPFLGVYFTDLTFLKTGNKDNFQNMINFDKRTKVTRILNEIKKFQSVGYMFNPINEVQELLNEVISRERNTNNIYQRSLTVEPRESEDQALQRLLIDSGIF
The following text describes a protein:
Function:
Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites.
Subcellular Localization:
Nucleus.
Sequence:
MAEAELVSLFEKASNAAEKAVSDGAVLAAEEMRCQEALKAMGAVEVSTSILLSTQVGKRLRKLTKHQSSKISGSAQQLLEKWKKVVADEAAIKSGTSKEVSPTIKPETPGRTPPATVVKKEVKTEVKVYTSKTSRADTKNAVPSPKVESTNVSPSPRVETKNVRAMPQPHPAGKSATPLAPQSHVAGKIAASSTAPSSSANSTANGTANGSGFQPKVGNLTKAGDSTRDRFREFLIEAFKKCCSEVTDEHLAMVKKTDLVRVAVAVESALFSKLGQSKGSEKAKYRSIMFNLKDQNNPDFRRRILIGEIKPEEIANMTADDMASDARKKENESIREKALFECERGLQNVASTDQFRCGKCGQRKTTYFQLQTRSADEPMTTFVQCVNCNARWKFC
The following text describes a protein:
Function:
Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme.
Sequence:
MLRCSGLPFLPGNTFQDIGRSKFHKSHHFDQRNQVCILVDAKRPGIGGKPLLATDSPEYTLPSLYPPSYGPSRPGWLEYDRQVLCFYGYFQESLGNVDRIPYQIRNVRILYYLEDDTMQVSEPRTLNSGIPQGCLVTRQRIPRPPPYDSEFTSLLDLNINHTVQLFDRVYTITGCDDFSRRFLNRLGVAVPGAVEQPRDPATELRQQQDSAKMARRPAYKIDTLGKFLQYDRKVLRFKGVWDDRGSVFGDVHELEVLYHLSDDTFEIKEKLPVNSGRDSNGMFLRRGRLPKTFDHLPAMGASTPVTVLNVVGGGLKGGRYLNDSVGIGKADGNYYRDADLRIGARLNVYGRMVLLTGCDQFTESYYRESYGLEDFTPLYGYSAPREQFVAGRRTERELPPFNGWGTHEDSEGNCLTLEPKPPKINFRKFVAYDRCSLRFGARMVSKIQENNDRFFVISYYLSDDTISVYEIPIRNSGFLGGEFIKRRKLALPQQDPYAAERPACYGPQHFYLGATVRLQDHQFHITNADIYALRFMEQHCEEFPLSNLGKIVSKLRDAMQPQYKEYVAKHMAKIAQVKIDGRTVSTITYEALREILIELLGERIVDQEIVTLCRLFSAESEQPEPCDRELVRSAVHAELNRALWSDLERTKEHIYHLEPTGAEWLTPQRIRTIVKACKIPLDCALVDKMLQVLNKNGEGNISMEDFLTMLNPAAVPSKPIQPLNIKHDVCHFTPYRVTGKLVNWDELLAHIDLERTLTNQTS
The following text describes a protein:
Function:
Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MFEEPEWAEAAPVAAGLGPVISRPPPAASSQNKGSKRRQLLATLRALEAASLSQHPPSLCISDSEEEEEERKKKCPKKASFASASAEVGKKGKKKCQKQGPPCSDSEEEVERKKKCHKQALVGSDSAEDEKGKRKCQKHAPINSAQHLDNVDQTGPKAWKGSTTNDPPKQSPGSTSPKPPHTLSRKQWRNRQKNKRRCKNKFQPPQVPDQAPAEAPTEKTEVPPVPRTDSHEARAGALRARMAQRLDGARFRYLNEQLYSGPSSAAQRLFQGDPEAFLLYHRGFQSQVKKWPLQPVDRIARDLRQRPASLVVADFGCGDCRLASSIRNPVHCFDLASLDPRVTVCDMAQVPLEDESVDVAVFCLSLMGTNIRDFLEEANRVLKPGGLLKVAEVSSRFEDVRTFLRAVTKLGFKIVSKDLSNSHFFLFDFQKTGPPLVGPKAQLSGLQLQPCLYKRR
The following text describes a protein:
Function:
In the soluble state, catalyzes glutaredoxin-like thiol disulfide exchange reactions with reduced glutathione as electron donor. Displays weak glutathione peroxidase activity. Can insert into membranes and form chloride ion channels. Membrane insertion seems to be redox-regulated and may occur only under oxidizing conditions. Modulates the activity of RYR2 and inhibits calcium influx.
Subcellular Localization:
Membrane; Single-pass membrane protein. Cytoplasm.
Domain:
Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as chloride channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion.
Sequence:
MADPEIELFVKAGSDGESIGNCPFCQRLFMILWLKGVKFNVTTVDMTRKPEELKDLAPGTNPPFLVYNKELKTDFIKIEEFLEQTLAPPRYPHLSPKNKESFDVGCNLFAKFSAYIKNTQKEANKNFEKSLLREFKRLDDYLNTPLLDEIDPDSAEELTVSRRLFLDGDQLTLADCSLLPKLNIIKVAAKKYRDFDIPAEFSGVWRYLHNAYAREEFTHTCPEDKEIENTYASVAKQKS
The following text describes a protein:
Function:
Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MAPGDSPAIPIPVLTLLLFSFLVLSPVQAIVVYTDREVHGEVGSKVTLHCSFWSSEWISDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGAFKERIQWVGDPRWKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYVFDKVPTRYGVVLGAVIGGILGLVLLLVLLFYLIRYCWLRRQAALRRRLSAMEKGKLHKSSKDSSKRGRQTPVLYAMLDHSRSTKAASEKKSKGLGESRKDKK
The following text describes a protein:
Function:
Potential disease resistance protein.
Domain:
The LRR repeats probably act as specificity determinant of pathogen recognition.
Sequence:
MAEAIVSVTVQKLGQLLLEEPLFLFGIGDQVKQLQDELKRLNCFLKDADEKQHESERVRNWVAGIREASYDAEDILEAFFLKAESRKQKGMKRVLRRLACILNEAVSLHSVGSEIREITSRLSKIAASMLDFGIKESMGREGLSLSDSLREQRQSFPYVVEHNLVGLEQSLEKLVNDLVSGGEKLRVTSICGMGGLGKTTLAKQIFHHHKVRRHFDRFAWVYVSQDCRRRHVWQDIFLNLSYKDENQRILSLRDEQLGEELHRFLKRNKCLIVLDDIWGKDAWDCLKHVFPHETGSEIILTTRNKEVALYADPRGVLHEPQLLTCEESWELLEKISLSGRENIEPMLVKKMEEIGKQIVVRCGGLPLAITVLGGLLATKSTWNEWQRVCENIKSYVSNGGSSNGSKNMLVADVLCLSYEYLPPHVKQCFLYFAHYPEDYEVHVGTLVSYCIAEGMVMPVKHTEAGTTVEDVGQDYLEELVKRSMVMVGRRDIVTSEVMTCRMHDLMREVCLQKAKQESFVQVIDSRDQDEAEAFISLSTNTSRRISVQLHGGAEEHHIKSLSQVSFRKMKLLRVLDLEGAQIEGGKLPDDVGDLIHLRNLSVRLTNVKELTSSIGNLKLMITLDLFVKGQLYIPNQLWDFPVGKCNPRDLLAMTSLRRLSINLSSQNTDFVVVSSLSKVLKRLRGLTINVPCEPMLPPVDVTQLVSAFTNLCELELFLKLEKLPGEQSFSSDLGALRLWQCGLVDDPFMVLEKLPNLKILQLFEGSFVGSKLCCSKNLENLEEWTVEDGAMMRLVTVELKCCNKLKSVPEGTRFLKNLQEVEIGNRTKAFKDKLISGGEDFYKVQHVPCVVFENCEL
The following text describes a protein:
Function:
Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has also ATPase activity. Involved in the late cytoplasmic maturation steps of the 40S ribosomal particles, specifically 18S rRNA maturation. While NMP activity is not required for ribosome maturation, ATPase activity is. Associates transiently with small ribosomal subunit protein uS11. ATP hydrolysis breaks the interaction with uS11. May temporarily remove uS11 from the ribosome to enable a conformational change of the ribosomal RNA that is needed for the final maturation step of the small ribosomal subunit. Its NMP activity may have a role in nuclear energy homeostasis. May be involved in regulation of Cajal body (CB) formation.
Subcellular Localization:
Cytoplasm. Nucleus, nucleoplasm. Nucleus, Cajal body. Nucleus. Note=Displays widespread diffuse nucleoplasmic distribution but not detected in nucleoli. Detected in Cajal bodies but not in all cells.
Sequence:
MQSSSANSPQILHLAVTHSFYSASILTAKTVSGTLRSKFPSRQNSDLPALFFMFGVRVTSIVLLPSVSEEYLMVYFLSYSLELIENQLLRKYCFHKAHKSLLGELYDGYDEEYDCPILDEDRVVDELENQMSEGGVIVDYHGCDFFPERWFHIVFVLKTDNSVLYKRLETRGYNEKKLKDNIQCEIFQVLHEEALASYKEEIVHQLPSNTPEDLEDNINQILKWIEQWVKDHSS
The following text describes a protein:
Function:
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Sequence:
MKSGRFIGVMSGTSLDGVDVVLAAIDETMVAQQASLTWPIPVHLKKGILDICQGQPLTLSQLGQLDTQLGRLFAQAVNALLAQQRLQPRDIVAIGCHGQTVWHEPTGEAPHTLQIGDNNHIVAHTGITVVGDFRRRDIALGGQGAPLVPAFHHALLGHPTEKRMVLNIGGIANLSLLFPGQAVRGYDTGPGNMLMDAWIWRQCAQPYDKDAAWAKEGQVILPLLQKMLRDPYFAASAPKSTGREYFNYGWLERHLAAFPGADARDVQATLAELTAVSIAQQVLLNGGCERLMVCGGGGRNPLVMARLAALLPGIEVSTTDKAGISGDDMEALAFAWLAWRTLAGLPGNLPSVTGATEASVLGAIYPANPITQS