lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Implicated in the mating and sporulation pathway. Probably coupled to mating-factor receptors. May act in concert with Ras1.
Sequence:
MGCMSSKYADTSGGEVIQKKLSDTQTSNSSTTGSQNARVPVLENWLNIVLRGKPQNVESSGVRVKGNSTSGGNDIKVLLLGAGDSGKTTIMKQMRLLYSPGFSQVVRKQYRVMIFENIISSLCLLLEAMDNSNVSLLPENEKYRAVILRKHTSQPNEPFSPEIYEAVHALTLDTKLRTVQSCGTNLSLLDNFYYYQDHIDRIFDPQYIPSDQDILHCRIKTTGISEETFLLNRHHYRFFDVGGQRSERRKWIHCFENVTALLFLVSLAGYDQCLVEDNSGNQMQEALLLWDSICNSSWFSESAMILFLNKLDLFKRKVHISPIQKHFPDYQEVGSTPTFVQTQCPLADNAVRSGMYYFYLKFESLNRIASRSCYCHFTTATDTSLLQRVMVSVQDTIMSNNLQSLMF
The following text describes a protein:
Function:
Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the transfer of 2-methyl-3-n-amyl-pyrrole (MAP) to 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC) to yield prodigiosin. It is able to use substrates with a variety of monocyclic rings in place of the pyrrolic ring A of its natural substrate.
Sequence:
MNPTLVVELSGDKTLEPHRLGGKAHSLNHLIHAGLPVPPAFCITAQAYRQFIEFAVPGALLDTGAPGNVRDMILSAAIPAPLDLAIRHACKQLGDGASLAVRSSALEEDGLTHSFAGQYDTYLHVRGDDEVVRKVQSCWASLWAERAAQYSRTSAAQSDIAVVLQIMVDADAAGVMFTQDPLTGDANHIVIDSCWGLGEGVVSGQVTTDSFILDKASGEIRERQIRHKPHYCQRDPQGRVTLLQTPEARRDAPSLTPEQLQQLARLARQTRMIYGAELDIEWAVKDDRVWLLQARPITTQAKPVQMLYANPWESDPTIKERAFFSRMDTGEIVTGLMTPLGLSFCQFYQKHIHGPAIKTMGLADIGDWQIYMGYLQGYVYLNISGSAYMLRQCPPTRDEMKFTTRYATADIDFSGYKNPYGPGVQGWAYLKSAWHWLKQQRHNLRSAGATVDAMIALRQRETRRFLALDLTTMTHQELERELSRIDGYFLDSCAAYMPFFLQSFALYDALALTCERYLKGRGNGLQNRIKASMNNLRTIEVTLGILSLVETVNRQPALKALFERHSAQELVTVLPTDPESRAFWQSDFSAFLFEFGARGRQEFELSLPRWNDDPSYLLQVMKMYLQHPVDLHTKLRETERLRHEDSAALLKAMPWFGRMKLKFITKLYGVMAERREATRPTFVTETWFYRRIMLEVLRRLEAQGLVKSADLPYVDFERFRAFMAGEQSAQEAFAADLIERNRHQHLLNLHAEEPPMAIVGGYQPRMKAPTAENAAGMLSGLAASPGKVVAKARVITDLLAQAGELQPNEILVARFTDASWTPLFALAAGIVTDIGSALSHSCIVAREFGIPAAVNLKNATQLINSGDTLILDGDSGTVIIQRGERADG
The following text describes a protein:
Function:
May be a cell surface adhesion protein.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MAAASASHILLTLAPLVLLLVLPQIQAQAPAPAGPVNLTGILDKNGQFTTFIKLLISTQVANQIQSQINSSSEGMTVFAPTDNAFNNLEKGLLNNLDNQKQVQLVLYHVTSKFYRQSDLLLVSNPVRTLASGQDVWGLNFTGQGNQVNVSSGVVETPINSVLRQNFPLAVYQVDKVLLPEELSAAKSPSAAPAPEGKKPTEGSNKKVPAASEPAPADDKTGAGGRLNAGLGFVVGLALLCMGVLS
The following text describes a protein:
Function:
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Sigma-S contributes to the protection against external stress, thus playing a role in cellular fitness and survival.
Sequence:
MEDINAILKKAQSGDNEAIDLILKEYSKLLSFNAQKYYLVGAEKEDLVQEGILGLLKAIKFYDETKSSFSSFAFLCIRREMISAIRKANTQKHMVLNEALKTNAILEDSAYFDDEGHNINNYKSSESNPEEAYLLKEEIEEFKKFSENNFSKFEKEVLTYLIRGYSYREIATILSKNLKSIDNTIQRIRKKSEEWIKEEENIKR
The following text describes a protein:
Function:
Involved in genotype-specific nodulation of soybeans.
Sequence:
MNRATPRRRRWRIGELAEATGVTVRTLHHYEHTGLLAATERTEGGHRMYDRESGQRVHQIRALRELGFSLVEIRKAMEGTTSLTDLLRKHLERIEVQVARTTLLRDRLRNMTIDSEAQVSVDELPATLNAMSRAETRSQTSRCTCNLAAEREDRWRRIRDDLRDCMDGGEHPCGERAKAVAVAARLLISEIAGDDSRVSMILKVLARLSAPRSLAGWDPCLMQYLDLALGGLEDQPY
The following text describes a protein:
Function:
Mannose-specific lectin. Shows agglutinating activity towards chicken erythrocytes. Has antifungal activity against A.alternata and Collectotrichum species.
Miscellaneous:
MISCELLANEOUS: Mannose-binding activity stable when incubated at 85 degrees Celsius for 10 minutes, and increases 3 to 4 fold when incubated at 85 degrees Celsius for 10 minutes in the presence of 0.14 M 2-mercaptoethanol. Mannose-binding activity decreases to 27% when incubated at 85 degrees Celsius for 10 minutes in the presence of 0.35 M iodoacetate. Antifungal and hemagglutinating activity stable when incubated at 100 degrees Celsius for 5 minutes. Antifungal and hemagglutinating activity increase when incubated at 100 degrees Celsius for 5 minutes in the presence of 0.14 M 2-mercaptoethanol.
Subcellular Localization:
Secreted.
Sequence:
MAFSISSTMIFLLSLALFSTLVSADNHLLPGERLNPGNFLKQDRYMLIMQEDCNLVLYNLNKPEWATKTANQGSRCFVTLQSDGNFVIYDEHEQEGRNEAIWASKTDGENGNYVIILQKDGNLVLYSKPIFATGTNRFGSTAVVVAKRNRKAHFGVEQNIIEVTTNL
The following text describes a protein:
Function:
Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde.
Subcellular Localization:
Mitochondrion.
Sequence:
MATETLDKQKTIDLRKKHVGPSCKVFFDHDPIKIVRAKGQYMYNEKDEKYLDCINNVAHVGHCHPDVVSAGAKQMELLNTNSRFLHDSLVLYAQRLQATLPEKLSVCYFVNSGSEANDLALRLAWQYTGHKDIITLDNAYHGHVSSLIDISPYKFHQMAGAEPSQHVHVALSPDTYRGKYREDHPDPATAYAENVKEVIEEAHKKGHEIAAFIAESLQSCGGQVIPPMGYFQKVAQHVRNAGGIFIADEVQVGFGRVGTHFWGFQLQGEDFVPDIVTMGKPIGNGHPMSCVITSREIAESFMSSGMEYFNTFGGNPVSCAIGLAVLNVIEKEDLQGNALHVGGYLTQLLEDLKKRHPLVGDVRGRGLFVGLELVRNQSKRTPATAEAQEVIYRLKEQRILLSADGPHRNVLKFKPPMCFSREDAEFAVEKIDQILTDLEKAMVLQRPEAAILETGHIKRKDASDENGLVHPSNGNSHKHTSTIPLSKKTKRN
The following text describes a protein:
Function:
S-adenosyl-L-methionine-binding protein that acts as a sensor to signal methionine availability to the mTORC1 signaling pathway. Associates with the GATOR2 complex in the absence of methionine to inhibit mTORC1 signaling, but dissociates in the presence of the methionine derivative S-adenosyl-L-methionine; S-adenosyl-L-homocysteine binding does not induce dissociation. Required for mTORC1 pathway response to methionine starvation. Exerts a protective function on developing egg chambers by inhibiting mTORC1 signaling under starvation conditions. May also function as a N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine (By similarity). It is unclear whether this protein has retained N-methyltransferase activity or if it is an evolutionary intermediate whose substrate binding ability has been co-opted to function as a nutrient sensor for mTORC1 signaling (Probable).
Miscellaneous:
MISCELLANEOUS: The name 'unmet expectations' refers to the loss-of-function phenotype of female germline cells, which fail to sense and adapt to low-methionine (un-Met) conditions leading to their degradation.
Sequence:
MSSMDCATFPMHPKMDEQLARTFVINEEEEEKHIQKVQNAFLYYGPYACQRLKRSMDYLNSLSGEDQIMLAKYRGHLECVRTCIDRNQAVIREILRGRVLYPTDEATGDPSEFDEPPPNVRHGDMDQIDIPFDEADVEPLKILKAQSTLKLIARDWSTEGALEREQSYKPIIDSIVAYFKHSDFELKDIKILVPGAGLGRLTYELACLGYSCEGNEFSYFMLIASNFVLNLCDNENKYVLYPWVHQYVNNLRREDQVAPVRFPDVCPLKNPPKGHFEIAAGDFLEVYKTPNAYNCVATCFFIDCANNVIDFIRTIYKILVPGGIWVNLGPLLYHFSDVSGQNSIEPAFEDLCIIMESVGFVIEKSRTGIRTKYAQNPSSMKQSEYQSLFWVCRKPDLFEEQRGKRKASREPHDLIVREDSEEEGEQQPERNETEEKQQLKPLATANCETEIKEQPS
The following text describes a protein:
Function:
Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix, basement membrane.
Sequence:
MTLRVRARLAALTAATVLLLLVLTTTSANENTHYLPPLECVDPYGRPQRCIPEFENAAYQLQVEATNTCGDETDTDFCVQTGYSNRKSCDVCHAGQHSPQFLTDFHDPNNPTWWQSETMFEGVQYPNQVNLTLGLGKSFDITYIRIVFHSPRPESFAIYKRVTPNGPWIPYQYYSATCRDTYGLPDSLSVMNGEDESRALCTSEYSDISPLRDGNIAFSSLEGRPSAINFDHHLELQQWVTATDIRITLDRLNTFGDEVFGDAQVLKSYFYAIADIAVGARCKCNGHASECTTSTALDGQRTRVCKCMHFTDGPDCDRCLPFYNDAPWGRATSKNVHECKPCNCNGYSTKCFFDRHLYNLTGHGGHCIDCGANRDGPNCERCKENFFMREDGYCINCGCDPVGSRSLQCNAEGRCQCKPGVTGEKCDRCDSNYFNFGPHGCQPCNCDERGSLDNTPSCDPVTGVCSCKENVEGRHCRECRLGYFNLDAENKFGCTPCFCYGHTLECTSASGYSIVSTTSNFNKHKEKWTAISDTGVPVDVKYNSHSQSIGVGANGHRTVYFLAPDRFLGDQRASYNRLFKFRLQLVGQPRVEVSPYDVVLQGGNSSISLPIFAQNQRMPSEESHEFAFRLHENPEYTWHPSNSGRGFMSILSNLTAVKIRAIYGDYGEAILDDVELQTAHRGAAGRQATWIEQCTCPEGYLGQFCESCAPGYRHNPARGGPFMPCVPCDCNKHAEICDSETGRCICQHNTAGDTCDQCAKGYYGNALGGTPYDCKRCPCPNNGACMQMAGDTVICLECPVGYFGPRCELCSDGYYGDPTGVYGSVRMCQPCDCNGNVDPNAVGNCNRTTGECLKCIHNTAGPHCDQCLPGHFGDPLAEPHGSCEECSCYPRGTEQTEKGISICDAINGNCHCKPNVIGRTCNECKNGYWNIVSGNGCESCNCDPIGSYNASCDTYSGDCFCKPGVVGKKCDKCAPAYYGFSEDGCHACDCDPSGSKGSQCNQYGQCPCNDNVEGRRCDRCKENKYDRHQGCLDCPACYNLVQDAANDHRAKLAELNQILQDIQSKPIVIDDSEFAGKLHAVQEKIDILVEDAKSGSGGGEKTLNEILRELEARLQEVQKLLDNADQSQEVTNHKISKGGYNATLANGKIQDARRQLDNAIELLQTEGNTALARAKDISGHLGNQTNQISGISREARQYADRFKAEADANMKQAQEAHKKASEALKKANDAFNQQANITKELDTSISSEIAQAREKLNTVSKLTEQALTRAREVNDEALTLFAAVNRTAPPNIDIDKIKKEANQYNREADRIAEDLANKMRDHAQLLENVGTNIELAETLLDRASLQKEDAVDALKQLKYAKEQAEKAVAEGDGTLQKANYTYQTLAGFKNQVEESSRRAEEALNLVPNIERQIVNSRDLLQRAEEALYAASRNAEDARKNAQTAQDKYAEEASKLAENIKKRANATKNTARDLHHEADQLNGRLAKTDNRLEEREAQIRKDLNLTNEAKEKVGQAQLNSNEAKSQVDKAMREVSLIMSELANLREIDVNSLDDLERRLSAAEKELEDAQLTKRLSSLVEAKNIQNQNIRSYQKELADLRLEVANIELIANSLPPGCFKRTHLEP
The following text describes a protein:
Function:
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Sequence:
MKESLISFIKEKIEEYNYRGAVVGVSGGVDSAVVLSLCVQALGKDRVFALILPERDSSKDSLKDAVDFCERLGVEYRKRSITPILRKIGVYRLFPPRLFLPDSIVKRYVLNRWNTLSKDPFLDDLRNTGPEEFLKGLAYYRIKHRIRMCLLYFEAEKRGYAVVGTTNRTEYLTGLYVKWGDEAVDIEPIMHLYKTQVFELAKEMNVPEKILKKPPSPDLIPGITDEMAFNMSYLELDRILMKLEKNEDLSDEDPKKVERVKKILELSEKYRRDIPITFDRI
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER. The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (By similarity). Binds signal recognition particle RNA (7SL RNA) in presence of SRP68 (By similarity). Can bind 7SL RNA with low affinity (By similarity). The SRP complex possibly participates in the elongation arrest function.
Miscellaneous:
MISCELLANEOUS: Present with 11800 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum membrane. Nucleus, nucleolus. Note=Transiently localizes to the nucleolus during biogenesis of the SRP. The SRP-RNC complex is bound to the endoplasmic reticulum membrane due to the interaction of the SRP with the membrane SRP-receptor (SRP101-SRP102).
Sequence:
MAKDNLTNLLSQLNIQLSQDEHSQVEQTCVKLLDSGCENPADVFRRCLVAVIQQDKYQKALHYLKKFKHIDDKYGRKFALEKLYIFYKLNMPDEFNTLYTAIITDDLDTVLKKDIESLRGILHVRAQYCYKNGLYQEAFKIYQHLASHNEKDQDSQIELSCNERVPLSVATELMNRSPLVTPMDESSYDLLFNESFIMASVGKYDKAIELLEKALQGATNEGYQNDINTIKLQLSFVLQMVGKTAQSKEILKGLLQELKADSPFSLICQNNLNAFVDFSKYNTNFNLLLRELNVEKLNTFNLQTFTHEQWSNIQRNVLFLRLFNNVKIHSQESLLSRTFDKYSKLVDNVTLESYKTQAKKLYHHTTKTILSGTDGSTIGILLLTIQLLIIEKEWENAIRIGELFLNESWKSSFEKFNDSQAIVCYILFELYKIKGRNNSKSVLLKKLGSVRVQLSGKIQENIPFWKHVGFELLSMGNAKESKALLREISNFSKGDADVLVDRVVSSDSLDIAQGIDLVRDIDIDKLIQLGVKPLESSAKRSKNTAVSKVQKRKVLELKKKRKIKRLEKFLQGRDTSKLPDPERWLPLRDRSTYRPKKKQQGAKQTQGGAMNKKSEQALDISKKGKPTVNKKPKNKKKGRK
The following text describes a protein:
Function:
May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MADQHRGAPMPGLLEDLRSFVYSIPTVTRYLVFCTFCFSLGAMAGLCKPDQLLLDYYTVFRRFEVWRLFTAHFYCSGQAMIWHLFMLYQNSLSLENDHFASRPADYATFVLFVMGVLDVISYFFEFPILTESFGMAVTYMYAMSKGDAIVTFMFGMQFKAKFLPWVLIVFNMLMGGGYFMSLIGIAVGHLYYFLDVVYPQQSGGNRLLVAPGFISNWFGPPPNVMGTTGNIPNMGNAGRTTAHTTSSGSTRGYTWGAGNRLGSE
The following text describes a protein:
Function:
Endogenous ATPase inhibitor, which inhibits specifically the reverse ATPase reaction of mitochondrial F(1)F(0)-type ATP synthase. It limits ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(0)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(0)-ATP synthase enzyme acts as an ATP hydrolase. Functions through inserting its N-terminal part into the catalytically active F1-ATPase, thereby blocking its rotational movement and subsequently the ATP hydrolase activity.
Miscellaneous:
MISCELLANEOUS: Present with 981 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion.
Domain:
The inhibitory N-terminal region (residues 23-59) is entrapped between the C-terminal domains of the alpha(ADP-bound)-beta(ADP-bound) (ATP1-ATP2) subunits in one of the 3 catalytic interfaces of F(1)F(0)-ATPase.
Sequence:
MLPRSALARSLQLQRGVAARFYSEGSTGTPRGSGSEDSFVKRERATEDFFVRQREKEQLRHLKEQLEKQRKKIDSLENKIDSMTK
The following text describes a protein:
Function:
Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)).
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Prevacuolar compartment membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MMVESDGTADATRRLNVKKQTLDDAYAVPANFLEIDVVNPLTTMAAGKKRYTDYEVRMRTNLPVFKVKESSVRRRYSDFEWLRNELERDSKIVVPPLPGKAWKRQMPFRGDEGIFDESFIEERRKGLEAFINKIAGHPLAQNERCLHMFLQENVIDKNYVPGKIRNT
The following text describes a protein:
Function:
Forms chloride channels.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane.
Sequence:
MTVTYTSEVTTCRGISCFLKLLLRWRGSIYKLVWVDLFVYLLLYYSISLCYRFIPDQLWQQYFEKVIKYCDTYSNRIPLSFVLGFYVSLVMTRWWSQYCSIPFPDNLAIIIGASVKGQNEHARVVRRTMVRYVCATFTITLTMLSPRVKKRFPTLDHFVSAGLLTKDEVKIMNDLDNEFPSYSKYWLPLAWAANVVTRARHEGLIRDDVSVKTILEELNLFRSKCGGMLDYDWISVPLVYTQVVTLVVYCYFVVCAIGRQYITSDETNGNIDLYFPFFLVIEFFFYMGWLKVAEVLINPYGDDDDDFEVVWMVDRHLQVCYLLVDKIHQEHPKLMRDAHWGETAPNSLPFTIASKNYMHEYPFPSTMNVKVNRSAQDLLLPVEDSISQPDGVRRRSGPYLWRLGGLQMKKQSRTKNFPLTKIITYDDANNQVNVYDSDVQSDEPKTTETPCEEFENLKRNRIESHKKKMLEIIQIWKGTTGEKHVST
The following text describes a protein:
Function:
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
Subcellular Localization:
Nucleus.
Sequence:
MLFRRGIMNKIAQVPYASNETWEFGVTLHKGTIYIEEHESIEKQKSKFGATDRDAMFTYWGYKFESLSTIPIPPNQLEHDDPVLKNRETAVVNTNIQFCSVFKTNYGSHSVVMGAEVDCVTREIETGTSPQSVYAELKTTQVIDTDRKRHSFEKFKLLRIWLQSYLAGVPKVIIGFRTGDGHISHVQEFDTSELPRLVRGKPGMWDPNRCIAFGDQFLAWVKQVVTIDDWNTVYTVRFDSNKQMIEMLAPVTGGDQVFIPKDFSLEK
The following text describes a protein:
Function:
Probable transcription factor, involved in determining neuroblast cell fate, morphogenesis and aspects of terminal differentiation in both left/right symmetric and asymmetric neuronal lineages.
Subcellular Localization:
Nucleus.
Sequence:
MAKKNQVARNERERKRVHQVNHGFDVLRNRLQPKNHTKKWSKADTLREAVKYIQQLQVLLNQDPQQPSVSSSTPDYTMNNSNNFNNYAVKEEFSMYLPQNYCPQNQMSVPHGDVSHNFNSPTSSVSSSSYSPTQMCYPPVSYSNYPHH
The following text describes a protein:
Function:
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A.
Subcellular Localization:
Nucleus.
Sequence:
MHGCGAESDPVVNAEVDSMGGVLEGGVGIGNITSSRRSAIEEVQAELRQEYCFLEEKRRELEFLEKGGDPLDFKFGNAASLSVQSTSLTDQPPDQLVTSEAKGSFAITASPHGDSVESSDRLGAPQLCEPNSADNLMLFDGENEYTEGDRSSRHPGTSNLTPSEQSFNLDRSRNAKELGDSAAFGVPRKAYKRRYRPRPNGDGTRSSSTDVILARGGHGTSLPSQHFSKDVKGLVSDGENPKDQNSSLNIAVPSSSNGCMPVKTLASDNLLESEVDGVKAADSTTYLKTDDLADSIPEASSSRDLLDNQHDQNSHTGVKEMSIREGPERPPSSLGEEGVGSAGQEGQSCTAAAGFGKQASFSQINGFSCGKSDQKSIPNDAQSSDAALGTKGLDSESSCTRTTHTVDQNNDSEMIMNPKNLDSKGDLKEQLSVPEGTPIIESNLKEQKEVKAGDGCGLTNEVCNSGPKKHQNYFLDTSQEEFVSSEPNLPCEVKDNITTIVEAVGPSPSETERKPSTNTSDSSNRQKGNACIIGRQASVESTIPEPSQHGVSNLSPEAQASGINFKLATKGDEDSILKEAQIIEAKRKRIAELSAVTFPVENRRKSHWDYVLEEMVWLANDFAQERLWKMTAAAQMCHRVAFTVRSRFQEQNSSWELKKVAHIMAKAVMGFWQSIEGKSKKLERAIFRKDHTLAIREYAMRFLKYNDSDVPQSLAEAPVTPERVSDAGIIDAPQEDHFREENLFYAVSLGAMDAYRKSIESHVLHYAKFGMHEEVETSACNTVPDWGSQDYAFEEDEGETSPYDISVAIEGNKLSRFSQKKRKILIKAYNGRSYDVRTDVPFTQRAENRLGTHQSXGTHQSMQLGKRPASNLNVSIPTKRMRTASRQRVLSPYSATTSGCAQLPIKTDASSGDTSSFQDDQSTLHGGSHMPNSLDVESVGDFEKHLPFDSSEVSKPKKKKKSKILGSAYEQRWKADSNFQNEQRDFSRKRLESHQLDSNGSNGLVGQHITKKPKMMRQSLENSFENIGAGGGFVPSPAASQMSNMSNPNKLMRMLSGRDQGRRAKTLKTSAGQPGSGSPWSLFEDQALVVLVHDMGPNWELVSDAFNSTLQFKCIYRKPKECKERHKILMDRSSGDGADSADDSGSSQPYPSTLPGIPKGSARQLFQRLQGPMEEDTLRSHFEKMILIGQKYLLRKNQGYKHDPRQLQQPHDSHTHVLSKHCTNNLNGGPIFTPLDLCDAPSSPDYLSVGCQGPHPSELSISSQCALNSVLPASGANSAVQGSSNMISGNNFPSSPLNASVRDGRYVVPRSASLPVDEQQRFQQYNQMRNMQSNIAAPGVLAATDRGGARILSSGNSTGMMCGINRGIPMARPGFQGVASSPMLNSGSMLSSGMGAMPNTVNMHSGVSSNQVNSMMRPHDGSHMIRPPQNQEVQRQMMVPELQGNSQVVSPFGGLSSSFPNQSASPVTSYPLHHRQSHQPPMLSPHRPHLQGANHATNSQQQAYAIRLAKERHLQQRLVQQQQFSHSQPQLPISASLQNSPKTTSQSSSPPVSLSPLTSPASMTPMPQHHALPNHGLARTAQSGGSSVTTQMSKQRQRQVGQQQLQQAGRHHPPQRQQSQSQQQAKLLKGVGRGNMMMHQNLQIDPSLLNGLSNNQTNQSAEKGEQATHLMQGHGLYSGTAHSPVQLAKQAVAPHSSSQPQPKIYSGQLVPSTKHLQQQMPNQDNSNQGPGSLAPSDTISSQQSVPSSVTGSSNHQGLVHQQPQVQPQPKLMNQSQATVQRVLQQNHVVNSDQSKKLQAGEPQAEQHPMCKTSQIGAITSMPQDVNDATNVADVSTLSANQWKGTEPLCDSIGTPPTNSAGSESVPQISQGVSQRQSSGNLAPTGPDSFNWQQKSSQLQPPSSVTQPQLQQQLSTLQHSQEQAQILQAGNSNSFARPNDCRLD
The following text describes a protein:
Function:
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Seems involved in the regulation of cell proliferation. Essential in leaf polarity establishment, probably having a role for translation in leaf dorsoventral patterning to specify leaf adaxial identity.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm.
Sequence:
MAFVKAQKTKAYFKRFQVPFKRRREGKTDYRARIRLTNQDKNKYNTPKYRFVVRFSNKDITAQIISANITGDMILASAYSHELPRYGLEVGLTNYAAAYCTGLLLGRRVLKLLEMDDEYQGNVEATGEDFSVEPTDTRRPFRALLDVGLIRTTTGNNVFGALKGALDAGLDIPHSDKRFAGFSKDSKQLDAEVHRNYIYGGHVAAYMRILMEDEPEKYQSHFSEYIKRGIEADNIESLYKKVHAAIRADPSAKKSEKAPPKQHKRFNLKKLTYEERKAKLIDRLHTLNAAAGADSEDED
The following text describes a protein:
Function:
Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to negatively regulate the level of HIF1A expression, although this effect could be indirect.
Sequence:
MASPFSGAVQLTDLDDFIAPSQDCIKPVKVDKKLGSSGAKIYIEDDGNYFQVSADGGTRKLEKAKISLDDCLACSGCVTSAETVLITQQSHEELRKVLDANKTAAPGQQRLVVISVSPQSQASLAVRFQLNPTDTARKLTAFFKRIGAHYVFDTAFSRNFSLLESQREFVRRFRGQAGSQQALPVLTSACPGWICYAEKTHGRALLPHISTARSPQQVMGALVKDFFAQQQHLTPDKIYHVAVMPCHDKKLEASRPDFFSQEHQTRDVDCVITTGEVLKLLEEEGVSLSALEPAALDSLCSTVSDQEPTSHRGGGSGGYLEHVFRYAARELFGIHVTEVTYRPLRHHAPPRREPGHTTRTARFASPQEQGPPGGDFGAGGPGPAALCCSLRLPQHPEPGAEAQARAVPVPLRGGHGLPCWLPEWRRPAQGPRHTWQGAAPAGGEAVCHGQDTGAGGRTRGPGAVQALAAGRGLRAGQPAAAHKLPRGGEGWLQPQHQVVTPRKARGVQGSHTRGPRTHRKMLAELQEHRDLWRKGTPGSWPAKTTSLRSPGLPAIGPGGATDFQNLSVGPEPRLVPWLFLVVAAKL
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Domain:
The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence:
MDLDLNEEPLYSSNDSLLGLTTMWNELETTNGLIEERIRQLEAVTFRARQRQRWRQSHITPQTVSISVEPATINVRSEGRLLIGEASVATEERRDEMNKFGKRNSAYLLAKALGRNGNGKEARNDRSVFYCNICLDMAQDPVLTCCGHLFCWPCFYQLSYVYSNVKECPVCMEEVTDTSIIPIYGNGNSNDNNKHRLKESGLKVPPRPSAQRVESVRQQLINRGVFSSSIEERMRHFGNVLIAMGEIPRSEDLDDTHLESERISLLENQAITSLALPSTGAEVSQDYHSVHVSRLLFQGAASLSSFSSAVNSAMNSAVESAERLVEDLEAVLHNHRGRRNHHQSSRPADRDSFSSIAAVIQPDIQNLDTVADADSMLPHSASSSRPDDAATVSQLESHSMGTDIESNSTVPISSTSSRRNLVSRLSEVDISLQTNPLSSRRRIEVSRVSDADNGQNRGRRRRRLS
The following text describes a protein:
Function:
Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSEASKAGMDALHSLKSAEPPLWLTPSATLSQTSRAASQHLFSCLKPHAPKSPFDKLLVEGFDAEQIWQQIDLLTQPLLSSIRHQVRNLEKNPEEIKLVIEKKESEVGEEGENKESKELHEFEEDDDEDADMEDFEDDEDGDDNDDDEEEENVEREGGIEDKFLKIKELEEYLEEDEAREYGLDSMNIKKKKQKIFNDSDKEEDDEDEEEDESDDEDDKLDDEDEDAEELGNARYEDFFGAKKKTDSKRKSNLDDGSDEDSGSEVEKEGDLSTHQKQREKLKSEIEQMEKANLEPKTWTMRGEVTAADRPKNSALEVDLDFEHNVRPAPVITEEVTASLEDMIKSRIAEGRFDDIQKLPSLPSTAPREVKEMDENKSKKGLAEVYEEEYVQKTNPAAAPISFSDEQKKEASILFKKLCLKLDALSHFHFAPKPVIEDMSIQVNVPALAMEEIAPMAVSDAAMLAPEEVFSGKGDIKEEAELTQAERKRRRAKKKRKFKAEGVKRMAKRARDNTTLPDHNDGNLSSALIGGLFS
The following text describes a protein:
Function:
Involved in the regulation of shoot gravitropism. Involved in the regulation of inflorescence branch angle. Functions redundantly with LAZY2, LAZY3 and LAZY4 to control plant architecture by coupling gravity sensing to the formation of auxin gradients. Involved redundantly with LAZY2 and LAZY4 in the regulation of both shoot and root gravitropism. Mediates gravity signaling in statocytes downstream of amyloplast displacement, leading to the generation of asymmetric auxin distribution in gravity-responding organs. Regulates the direction of polar auxin transport in response to gravity through the control of asymmetric PIN3 expression in the root cap columella. Regulation of auxin flow by the three proteins LAZY1, LAZY2 and LAZY4 in statocytes influences plant architecture by controlling the growth angle of lateral shoots and lateral roots.
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Nucleus.
Sequence:
MKFWGWMHHKFRENSKEPLKDASTGNSYSILSAHPSLDSQEVYPTACAGSRYNTGFRKQVNLFQESSFAGPKQYTEEDFKDERNSDFFDGFLAIGTLGGETLLDEQPATPTFGMSFEDPAIDDADVTENDLKLISNELDKFLEAEAKEGHHQPSGRNSDTNTIASTIEAIEGVDDEEDNQPMKFPLQEYFFGSLIELPESKIAGKKDRASLGELFQITEVQDKQSENIYGKKKKQPNSAHKSAKHLVKKVLKKIHPSSRGSVSGKPEVDSTKKKFQKMVQVFHRKVHPEESIMETKIYSSVANPKSSKANSIDLTFEKVNHCHEASKRCIQYELRSSRSAKNGEHWIKTDEDYFVLEL
The following text describes a protein:
Function:
Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
Sequence:
MISFKEALKIHSSIPIKPLEIEVISLFESIGRILAEDIICIHALPKFNQSAMDGYGFKMQDLGKKTQVVQRIFAGDDVSALEVKENECVKIMTGAMVPKGIETIVPIECMLESHTNFALAPKDFKINANIRQKGENASLNSVLVPKNTRLNYGHIALIASQGLKEIKAFRKLKIALFSSGDELVPLGQNALECQVYDVNSVGIFNMLKNYNTHFLGVLKDDKNLQLKILESQDYDVILSSAGVSVGDKDFFKDALKEKNALFYYEKVNLKPGKPVTLARLNQSMIIGLPGNPLSCLLVLRVLILPLLERLSLNKDFKLKPFKAQINAPLKLKGERAHLILGNYSNHQFIPYNNNRYDSGAIQALARVDSIALIDEGVRLVQGEIEILRFEN
The following text describes a protein:
Function:
Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Localization:
Cell projection. Cytoplasm, cytoskeleton. Membrane; Single-pass type I membrane protein.
Sequence:
MVHRGAFLLKAVGILLLTSTIQLSNASGYFELQINSIQNIAGQLSSGNCCDGVKDYDGSCTQDACDTYFRVCLKEYQGNXSASGTCTFGRYTSPVLGGNSFSLSNNGNNAGRLRLSFVSWTSGYTLILEAWDRDNSSRTDGLIDSYSVSGMIHPGNTWQNFQYNGPTAVIDYKIRVLCDEHYYGSNCSRLCRPKDDFVGHFTCDQNGNKVCREGWMGADCKTPVCRVGCNTAHGHCSVPGQCRCQYGWQGPLCDQCIPYPGCVHGSCHSPWECLCDTNWGGLLCDKDLNFCGRHQPCLNGGTCHNEDPDEYRCECLEGFSGRSCEIAEQPCVSNPCQNGGQCTEVSNGFRCTCALGWTGDTCDIDIDDCKEPNPCAHGGRCVDELNGYHCQCPPGWLGSTCQIDDNECEDSPCEHAYACRNLIGDYVCDCQPGWTGKNCHINIPDCTGQCQNGATCVDLVNGYHCECTLGFEGRRCQRNINECLSNPCRNGGQCVDGDNSYTCRCPLGFVGRNCEIDVDFCNPNPCQNDAQCYNLETDYFCQCRDGFEGKNCTHLKDHCRTGPCEVIDSCTVAVSSNTSSDGVMIISSNVCGDHGNCISQPDGDFTCACNRGYTGTFCQENINDCAVNRCLNGATCVDGINSFQCVCAEGWEGILCNQNKNECSPNPCRNNGTCVDHVADFSCHCKRPWKGRTCNNLHSHCDDMTCAHGGTCIDLGDTFTCLCSPGWEGFTCHIAKNHSCASNPCQNGATCINSGDSYTCMCKEGFEGPQCQDNVNDCNPHPCYNGGSCVDGVNWYRCECAEGFVGPDCRININDCASHPCAYGSTCLDGINDYTCKCPAGRTGRHCELVLGDLQRQPCWGSGGLFAHGTKWEDECNTCSCRNGEVVCSQIWCGPEVCFAGDGNTMDSMECPPGQYCMVPTEDSCFTPPCGRWGHCRTPGLDLPSGPVSRTTTCLPNTTELDNNCAKITLMFDKGVCVEDICNTLRHLPVLDEHAWDKSLLLLCDTVEDINNSIAVAVSTEDTTGGRDNVVREVVNAIADYISKKQSNSSILAAIVEVKVETTIINYKDTLMVPLICAVVGSIVLISLVVVLIWCLGRRRKRRPPNPDHRINLENKTNNKQEDVNVQRYRNPIYQPIDKGTHSRNSLDSVDNQHREKVTHKNQRVLYKRDSYRDRGKHNLDKRKNIKDINTRSSQSVASIELIV