lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Enhances NF-kappa-B transcriptional activity by regulating the nuclear localization of the NF-kappa-B subunit RELA and promoting the phosphorylation of RELA by PRKACA. Regulates the effect of the cAMP-dependent protein kinase signaling pathway on the NF-kappa-B activation cascade (By similarity).
Subcellular Localization:
Nucleus. Note=Locates to punctate spots.
Sequence:
MEYCLAAAALNGVDRRSLQRSARLGREVLERAKRRAVDWHSPERSRGNVGVLYRQGPYQERWSVPGSQRLLGEREERCPTLSSSFGAMAEFMDYTSSQCGKYYLSMPEEGGATHVYRYHRRKPPEMHMYSDTGHSQEQRNCRGETSVGQESIYQTSEHSQESSWPTENISKDLYIEVYPGTYSVTVGSSALSKKTHVVAVDPGQSVDLVFPV
The following text describes a protein:
Function:
Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Subcellular Localization:
Nucleus.
Sequence:
MGVSVSGSHSSGVTATRRPRPANSVLRPRKDHPGAASSPTHAAGGAGEPLPCVVPVAGGSQRCPFLILLSSYRALDPPSVSSAHIGQSNPSVSSVAFENERETVKPGPITLPGLIDELSLLPTQEIWAHQSPHSRLRRNTCPHSPPRNVSFSPSFRRHSNEKSADGITRAGGAERRERENPESMARRGGWRPRRRKASTSAADGDGDAGGAAEGGRPPPKGQGAATAAGGGFFCCYLLRSLCPRSKIRTYIGFTVNPRRRIRQHNGEIASGAWRTRRGRPWEMVLCIYGFPSNVAALQFEWAWQHPAESLAVRKAAAEFKSLGGIGNKVKLAYTMLNLPSWESLNLTVNFFSSKNTKFTAGCPSLPSQMKTVVCAMEDLQCSAEGPSSEDDDLSQDPQDQQEQSDSPLQDDEHSQHCWQQPSDSPLRYEHSELCWQQPSSDEDEQSGHCWQQPSSDEDEQSGHCWQQPSSDQAQPMVGQTGIAGPDVEEDPIDGFGPRKWSEILDIRTEVDEPRTSPRCSLSLSGDDCGTATEDEPGHLSPLLMFGAAGSDDGGGHILDGSADVVDLVTPTPVGRLRRRGCVASVCPKIIDLTSSPVVIQL
The following text describes a protein:
Function:
Regulatory subunit of the histone H2A phosphatase complex, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint.
Miscellaneous:
MISCELLANEOUS: Present with 1010 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSSTMLDDVDNNMMGIKSISLYELLSDVVKQGDKTRLVTAGPEQVLPDLIRHITETIPFDLFINLKNEMNDARNLVTRLNWLGKFLNDNFLQNHTFPFTILRICELCYDPFKYYKINELEKFVNALEKCCMVTSSWQVFDKTHGEKQEDDKEKDINFIKNQEDVSLMKIPWMTENNTRELAPFIREIDSIMSVNLGYDDEDEEEGFFDGDEDREMGNKSKRNVLLKDENFMVEEYYEDDCGINDDNSDNKGQNCQSDVTKNNSDDEDDDDNDDDYREDGADEDDEDDDHMGSTDDDEDDDEDRQAGESTKVQNFDKKNETPRKRKPTDLDNFEYDESPSFTNMDLTTPKKYKHTATGRFSIIESPSSSLLNAMDGSNEISSSQEEEKEDAHENHEGRSEGLLPGDELVSPSMSSSQEDKMVAIAGITYRENISSPLGKKSR
The following text describes a protein:
Function:
Required for chromosome condensation and partitioning.
Subcellular Localization:
Cytoplasm.
Domain:
Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible SMC hinge near the middle of the molecule. These domains are separated by coiled-coil structures.
Sequence:
MYLKSLTLKGFKSFAAPTTLRFEPGITAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGKMEDVIFAGTSSRAPLGRAEVTVSIDNSDNALPIEYTEVSITRRMFRDGASEYEINGSSCRLMDVQELLSDSGIGREMHVIVGQGKLEEILQSRPEDRRAFIEEAAGVLKHRKRKEKALRKLDTMAANLARLTDLTTELRRQLKPLGRQAEAAQRAAAIQADLRDARLRLAADDLVSRRAEREAVFQAEAAMRREHDEAAARLAVASEELAAHESAVAELSTRAESIQHTWFGLSALAERVDATVRIASERAHHLDIEPVAVSDTDPRKPEELEAEAQQVAVAEQQLLAELDAARARLDAARAELADRERRAAEADRAHLAAVREEADRREGLARLAGQVETMRARVESIDESVARLSERIEDAAMRAQQTRAEFETVQGRIGELDQGEVGLDEHHERTVAALRLADERVAELQSAERAAERQVASLRARIDALAVGLQRKDGAAWLAHNRSGAGLFGSIAQLVKVRSGYEAALAAALGPAADALAVDGLTAAGSAVSALKQADGGRAVLVLSDWPAPQAPQSASGEMLPSGAQWALDLVESPPQLVGAMIAMLSGVAVVNDLTEAMGLVEIRPELRAVTVDGDLVGAGWVSGGSDRKLSTLEVTSEIDKARSELAAAEALAAQLNAALAGALTEQSARQDAAEQALAALNESDTAISAMYEQLGRLGQEARAAEEEWNRLLQQRTEQEAVRTQTLDDVIQLETQLRKAQETQRVQVAQPIDRQAISAAADRARGVEVEARLAVRTAEERANAVRGRADSLRRAAAAEREARVRAQQARAARLHAAAVAAAVADCGRLLAGRLHRAVDGASQLRDASAAQRQQRLAAMAAVRDEVNTLSARVGELTDSLHRDELANAQAALRIEQLEQMVLEQFGMAPADLITEYGPHVALPPTELEMAEFEQARERGEQVIAPAPMPFDRVTQERRAKRAERALAELGRVNPLALEEFAALEERYNFLSTQLEDVKAARKDLLGVVADVDARILQVFNDAFVDVEREFRGVFTALFPGGEGRLRLTEPDDMLTTGIEVEARPPGKKITRLSLLSGGEKALTAVAMLVAIFRARPSPFYIMDEVEAALDDVNLRRLLSLFEQLREQSQIIIITHQKPTMEVADALYGVTMQNDGITAVISQRMRGQQVDQLVTNSS
The following text describes a protein:
Function:
Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Characterized by unusual gating kinetics by producing relatively small outward currents during membrane depolarization and large inward currents during subsequent repolarization which reflect a rapid inactivation during depolarization and quick recovery from inactivation but slow deactivation (closing) during repolarization. Channel properties are modulated by cAMP and subunit assembly. Forms a stable complex with KCNE1 or KCNE2, and that this heteromultimerization regulates inward rectifier potassium channel activity.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPVRRGHVAPQNTYLDTIIRKFEGQSRKFLIANAQMENCAIIYCNDGFCELFGYSRVEVMQRPCTCDFLTGPNTPRSAMSRLAQALLGTEECKVDILYYRKDASSFRCLVDVVPVKNEDGAVIMFILNFEDLAQLLAKSERRSLSQCLLSQRFLGSEGSHGRSSAQRPGTGRVKYRTIGQIPQFTLNFVEFNLEKHRSGSTTEIEIIAPHKVVERTQNVTEKVTQVLSLGADVLPEYKLQAPRIHRGTLLHYSPFKAVWDWLILLLVIYTAIFTPYSAAFLLSDQDESQRVDCGYTCSPLTVVDLIVDIMFVVDIVINFRTTYVNTNDEVVSHPRRIAVHYFKGWFLIDMVAAIPFDLLIFRTGSDETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNVERPYLEPKIGWLDSLGAQLGKRYNGSDPASGPSVQDKYVTALYFTFSSLTSVGFGNVSPNTNSEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLHRALLQHCPAFRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDDVVVAILGKNDIFGEPISLHAQPGKSSADVRALTYCDLHKIQRADLLEVLDMYPAFADSFWSKLEVTFNLRDAGGGFQSSPRPAPGNQDHQAFFLSDNQSAAAPSLSISDTSGLWPELLQQVPPRPRHSPPNPQGDPDCWPRELGSRLEQLQAQMNRLESRMSSDLSRILQLLQQAPPPGHTGYILGAPTSDDLTLFPTASATQSPGTRLPQGGLTPAQVPSCGDLDKFRLKQRNSSSRVPTLVTATDKILTLSSEREQPEGILSPRASPLHPLEVQGLICASRFPSLPEHLGPVPKQLEFQRHSSDPGLTGS
The following text describes a protein:
Function:
Calcium-dependent lectin that acts as a pattern recognition receptor (PRR) of the innate immune system: specifically recognizes and binds alpha-mannans on C.albicans hypheas (By similarity). Binding of C.albicans alpha-mannans to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes (By similarity). Also recognizes, in a mannose-dependent manner, allergens from house dust mite and fungi, by promoting cysteinyl leukotriene production. Recognizes soluble elements from the eggs of Shistosoma mansoni altering adaptive immune responses (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein.
Domain:
A short stretch of the intracellular domain (AA 8-14) proximal to the transmembrane domain is required for association with Fc receptor gamma chain.
Sequence:
MVQERHPQRKGVCWTLRLWSTAVISMLLLSTCFIASCMVTYQFTMEKPNRRLSELHTYHSSLTCCSKGTMVSEKLWGCCPNHWKSFGSSCYLISTKENFWSISEQNYIHMGAHLVVINTETEQNYIIHQLNESLSYFLGLSDPQGNSKWQWIDNTPYPNNIKFWHPHEPNLPEEWCASIVYWNPSKWGWNDVFCDSKHNSICETKKIYL
The following text describes a protein:
Function:
Involved in defense against pathogens. May contribute to disease resistance by potentiating disease resistance signaling, or producing phytoalexin-like secondary products.
Miscellaneous:
MISCELLANEOUS: The gain-of-function mutants Spl18 (T-DNA tagging) show a lesion mimic phenotype, express constitutively PBZ1, accumulate the phytoalexins momilactone A and sakuranetin, and display enhanced resistance to rice blast fungus (M.oryzae). Plants over-expressing SPL18 show a lesion mimic phenotype and display enhanced resistance to bacterial blight (X.oryzae pv. oryzae).
Sequence:
MVVTFTSRRSEPVLLRPARPTPRETKQLSDLDDQRTLRYYETVVGFFRRCDGGAAGAVGAPADPAKAIRAALAEALVYYYPVAGRLREVADGGGAGNRLVVDCTAEGVVFVEADADVRLEDFGQPLLPPYPCVGELLCDAGDTRAVVGKPLLLMQVTQLKCGGFVLGFHICHNIADGFGMAQLIMAIADLARGEPAPTILPVWRRDLLTAARLGSGAVARTPFASAAAASASASSPALQNGARRAAAAADAMLSTPPDRMVVEYFLFGPREVSYLRGQLPAHLADSTTVFELLTAVMWRCRTAALGYGPDLRVRLMITMNARGRWNAHTPLPRGFYGNAHVSPVAEAAAGDLLGRPLADTVELVRRTKRGMTRERMSAMVETVAQLREWPPSSMDRVYEVSDIKWTTVNLLKFGWAEFAGGGIPLAGDLTSKLGSDHTRCKNSAGEVSTVVSMLLPRVAMARFKKEMAVLLNKDDKKSLTIMSSL
The following text describes a protein:
Function:
Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MELVKRGFLRACKNHSYLSFELIDDILAPLCANHKTTKPGSKEAIRALVAEINDTISDLGQLLVFIKYPVKAEEYLVYAKTDATPDSVANTGLTAEECQYFSKLLDKIASEEDCHIAWNDAYNDIVLQASSKPLKKSRMQELLQKWIQMGYFMEVTDRIYLGPRSLVELSFYLSSNHADNIKNCTLCKCLVLWDIRCGSCNIQYHRGCIQTYLQRRDICPSCGNLWTTPIRRSIG
The following text describes a protein:
Function:
MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity).
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein.
Sequence:
MKNQAHPIVVVKRRRHKPHGGGAHGSWKIAYADFMTAMMAFFLVMWLISISSPKELIQIAEYFRTPLATAVTGGNRIANSESPIPGGGDDYTQQQGEVEKQPNIDELKKRMEQSRLNKLRGDLDQLIESDPKLRALRPHLKIDLVQEGLRIQIIDSQNRPMFKTGSAEVEPYMRDILRAIAPVLNGIPNRISLAGHTDDFPYANGEKGYSNWELSADRANASRRELVAGGLDNGKVLRVVGMAATMRLSDRGPDDAINRRISLLVLNKQAEQAILHENAESQNEPVSVLQQPAAAPPASVPTSPKAEPR
The following text describes a protein:
Function:
Dorsalizing factor. Antagonizes mesoderm formation by ventralizing BMPs.
Subcellular Localization:
Secreted.
Sequence:
MAECRPWLVLWVGCCGCLCLALGELLNDGLLAVGMGTGDAARQEEAALPLGDTVSEHMLRLYDKYRSGGGRAKESLRYRQALPDGNTVRSFRAMNGDEHKKCHYMFNLTSLTSSENILSATLHYYLGDLLNSSHRCPHSLFCTQHGHAKPEFTLYLTLWSFNALQNPTHVISNFLINVSASQRDHPLWQWKDITQAVRKAKEYGEAVLGFNLTIEYPNHRSIDILGLKPYILVYANDSAISEPDSVVSSLHGPHTPLALKPNRKTEKAEQRKKRSTEILLPLQNNELPGAEYQYSVDEEGWEERKPYKNLQGRQNEKDKNKKKLRKGSRQKSQTLQFDEQTLKKARRKQWNEPRNCARRYLKVDFADIGWSEWIISPKSFDAYYCSGACQFPMPKSLKPSNHATIQSIVRAVGVVPGIPEPCCVPEKMSSLSILFLDENKNVVLKVYPNMTVESCACR
The following text describes a protein:
Function:
Zinc phosphodiesterase, which displays tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. Can process the mitochondrial tRNA-like structures (t-elements).
Subcellular Localization:
Mitochondrion.
Sequence:
MLTSSMPQNLSLFGFSPLKSSSFALILRPFSLYPPIFASSSPAPSRRPPRTAGYRRSGPSPPRRKWSSFEEQKRKGRSPMEKDKAISFNHSSDSFEFNKRRAEGLDKVDKPKKNLKRNTRTLNPTNTIAYVQILGTGMDTQDTSPSVLLFFDKQRFIFNAGEGLQRFCTEHKIKLSKVDHIFLSRVCSETAGGLPGLLLTLAGIGEQGLSVNVWGPSDLKYLVDAMRSFIPRAAMVHTRSFGPSLNISDSAPQIGLSKPKDDAYVLVDDEVVKISAILLEPSRLEESGSKPGETAVIYVCELPEIKGKFDPKKAMALGLRAGPKYSYLQSGQSVKSDFKDITVHPSDVMGPSVPGPVVLLVDCPTESHAEELLSIPSMKTYYSCLDNSTDGAKLVNCIIHLSPASVTNSSTYRSWMKRFHSAQHILAGHEAKNMEFPILRASSRITARLNYLCPQFFPAPGFWSHQHDNNSINPTSLSKCFDSNLGESISAENLLKFTLRPHGNLGVDRSSIPSRLTALRVMDELLSEIPEISSKTEEIKQLWNGQHNKMMIEEPWLGESTVPSCLENIRRDDMEIVLLGTGSSQPSKYRNVTAIYIDLFSRGSILLDCGEGTLGQLKRRYGLEGADEAVRNLRCIWISHIHADHHTGLARILARRRELLKGLAHEPAIVVGPRSLKNFLDAYQRLEDLDMEFLDCRNTTTTSWASVETSRPEKNTSSGNAEGSLFSKGSLMQSIYKRPSSPLTDNSSALPFLKKLKKVLGEMGLEHLISFPVVHCPQAFGVSLKAAERKNIAGDEIPGWKMVYSGDTRPCPEMVEASKGATVLIHEATFEDALVEEAVAKNHSTTKEAIKVGSSAGVYRTVLTHFSQRYPKIPVIDESHMHNTCIAFDMMSINMADLHVLPKILPYFKTLFRNQVVEEEEEEEETDDDSLIRDKVPSFFIN
The following text describes a protein:
Function:
Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma-carboxylase ggcx. Binds 7 calcium ions with a low affinity (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane. Golgi apparatus. Secreted. Melanosome. Sarcoplasmic reticulum lumen.
Sequence:
MEIRPLLMCFALCVVYATSKPTEKKDRVHHDAPLSSKEHDDGTNFEYDHDAFLGEEEAKTFDDLTPEESKNRLGKIVEKIDADEDGFVTEAELKAWIKKAQKKYIYDNVERQWKDFDLNNDRMISWEEYKNVTYGTYLDDPEPDDGYNYKQMMARDERRFKMADGNGDHIADKEEFTAFLHPEEYEHMKDIVVLETMEDIDKNGDGFIDLEEYIGDMYNHEDEMDEPEWVATEREQFSEFRDKNKDGKMDREETMDWILPADYDHAEAEAKHLVYESDTNKDGKLTKEEILNKYDLFVGSQATDFGEALVRHDEF
The following text describes a protein:
Function:
Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Subcellular Localization:
Cytoplasm.
Sequence:
MTLQQKELFQKSPLLLENGETLSPVLVGYETYGTLSASRDNCILLEHALTGTAHAAKHFEDDAPGWWDDYIGPGKTIDTDKYFLVCTNVFGGCSGTTGPSSINPKTGEPFRLQFPGFSIKDIIKVQRELLEQLGVTRIVSVIGGSMGGMQATEWAIDYADITDSIINIASPLAAGPDAIGYNLIMRMAILNDPDFNGGNYVGQPEGGLATARMVGMMTYRTSELFSKRFERFTVAESSPAAFSKEHFQIESYLQYQGDTFVERFDANSYLYLTKAIDLFDVTAPAKDDLPAFSKIKIPYLLIGITTDQLFRIHDLRRGYELLKEWDVPVTYHEVASEYGHDAFLVEKEVPKFEPLIRSFLSNLPVKSI
The following text describes a protein:
Function:
Required for HemL synthesis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MIDTAMARLNEGTIVIYALSVLFYFIDFLQHNRKAGKMAFWLLSIVWTLQTVYLAYFMWVTGRFPVLNVTEALYFYAWVLVTLSLVLTKLLRVDFIVFFTNVIGFSMIAIHTFSPTEQQSAAFSGQLVSELLVIHITMAILSYGAFSLSFVFSVLYMFQYHLLKKKKWGKWLLRIEDLSKLDYMAYVLNVIGVPMLLLSLILGVIWAYVSLETLYWFDAKVLGSFVVLLLYSYYLYIRLIKELQGKVAALWNTACFLVLMINYFLLGSLSQFHWFS
The following text describes a protein:
Function:
Binds and cleaves RNA, particularly in stem-loops. Associates with pre-ribosomal particles in chloroplasts, and participates in chloroplast ribosomal RNA metabolism, probably during the final steps of 23S rRNA maturation. May enhance transcription by the plastid-encoded polymerase and translation in plastid via the stabilization of ribosome assembly intermediates. Required for chloroplast integrity. Involved in the regulation of the circadian system.
Subcellular Localization:
Plastid, chloroplast, plastoglobule. Note=Present in stromules.
Sequence:
MAALSSSSLFFSSKTTSPISNLLIPPSLHRFSLPSSSSSFSSLSSSSSSSSSLLTFSLRTSRRLSPQKFTVKASSVGEKKNVLIVNTNSGGHAVIGFYFAKELLSAGHAVTILTVGDESSEKMKKPPFNRFSEIVSGGGKTVWGNPANVANVVGGETFDVVLDNNGKDLDTVRPVVDWAKSSGVKQFLFISSAGIYKSTEQPPHVEGDAVKADAGHVVVEKYLAETFGNWASFRPQYMIGSGNNKDCEEWFFDRIVRDRAVPIPGSGLQLTNISHVRDLSSMLTSAVANPEAASGNIFNCVSDRAVTLDGMAKLCAAAAGKTVEIVHYDPKAIGVDAKKAFLFRNMHFYAEPRAAKDLLGWESKTNLPEDLKERFEEYVKIGRDKKEIKFELDDKILEALKTPVAA
The following text describes a protein:
Function:
One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-acids). In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from leucine (4-methyl-2-oxopentanoate, also alpha-keto-isocaproate) and isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), whereas transaminated valine, transaminated aromatic amino acids, and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins. The enzyme is also positively regulating the thiamine metabolism by a molecular mechanism that may involve thiamine concentration sensing and signal transmission.
Miscellaneous:
MISCELLANEOUS: Present with 2140 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MNSSYTQRYALPKCIAISDYLFHRLNQLNIHTIFGLSGEFSMPLLDKLYNIPNLRWAGNSNELNAAYAADGYSRLKGLGCLITTFGVGELSAINGVAGSYAEHVGILHIVGMPPTSAQTKQLLLHHTLGNGDFTVFHRIASDVACYTTLIIDSELCADEVDKCIKKAWIEQRPVYMGMPVNQVNLPIESARLNTPLDLQLHKNDPDVEKEVISRILSFIYKSQNPAIIVDACTSRQNLIEETKELCNRLKFPVFVTPMGKGTVNETDPQFGGVFTGSISAPEVREVVDFADFIIVIGCMLSEFSTSTFHFQYKTKNCALLYSTSVKLKNATYPDLSIKLLLQKILANLDESKLSYQPSEQPSMMVPRPYPAGNVLLRQEWVWNEISHWFQPGDIIITETGASAFGVNQTRFPVNTLGISQALWGSVGYTMGACLGAEFAVQEINKDKFPATKHRVILFMGDGAFQLTVQELSTIVKWGLTPYIFVMNNQGYSVDRFLHHRSDASYYDIQPWNYLGLLRVFGCTNYETKKIITVGEFRSMISDPNFATNDKIRMIEIMLPPRDVPQALLDRWVVEKEQSKQVQEENENSSAVNTPTPEFQPLLKKNQVGY
The following text describes a protein:
Function:
Mitochondrial GTPase involved in assembly of the large ribosomal subunit. Plays a role in expression of the mitochondrial translational machinery.
Miscellaneous:
MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein.
Sequence:
MHINVRGTRKIISNVSSFTPRYEFPKYSMPLTDFKGHQVKALKTFEKLLPQMNMIIELRDIRAPLSTRNVVFDRIARKEHDVMKLVVYTRKDLMPGNKPYIGKLKNWHEELGEKFILLDCRNKTDVRNLLKILEWQNYELETNGGYLPMGYRALITGMPNVGKSTLINSLRTIFHNQVNMGRKFKKVAKTGAEAGVTRATSEVIRVTSRNTESRNEIYLIDTPGIGVPGRVSDHNRMLGLALCGSVKNNLVDPIFQADYLLYLMNLQNLNDGRTELYPGSTNSPTNDIYDVLRRLQVNKSQNEKSTAIEWTNKWRLHGKGIIFDPEVLLNNDEFSYKNYVNDQLEKLGDLSYEGLSNKLKGNPNQVF
The following text describes a protein:
Function:
Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity.
Subcellular Localization:
Nucleus.
Sequence:
MEASLRAAELKVFAKAIQCVARIGEDLHLEAKDTTLELKTVSQARNAFARIVFHEPFFEHFKLRARDAATGSIGCCINAKAVLAAFKSLTNIDKTVQLCQLTLDVVQARLVIKLICFFDIVKTYNLYYEDFDDVTVVYSKTDCRNVLENNPRLLLEAVANFQSGLEEICFDVKTASSSSEGAGEFTLENYIEVEEDQNKPSLKTKLELHSSEFLTYQVLRPTRLVFCLQALKQLLSFLDSLNEPMTCHFDHSGRPIIFSQQRTDMSIDFVLATLEHENEYPEPALPSQSIRADSPSHSTHWDNATSGTMTQPRRTPLATPNTHPANAPNNGPTAGAWSSPAGPPHMMLSAPQHETPVSQLGAALPSVG
The following text describes a protein:
Function:
Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the eighth mannose residue in an alpha-1,6 linkage onto Man(7)GlcNAc(2)-PP-dolichol to produce Man(8)GlcNAc(2)-PP-dolichol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
VLLIVALLALYTCPHSKVEESFNLQATHDLFYHGRDASDSPYDHLQFPGVVPRTFIGAFFLSLIARFISWITPKQIFDAYVNRQSQQQSSSNGTQSLQSTSPTTTIASYYLLITASQFHIPFYSSRLLPNTFALILVTHAYAEWFRRNYRLTAMYLVFTSAIFRCDMLLLLFTVGLVLLIQRQMTIVQALSVGVTTGVLSLLLTVPLDSLLWGRLIWPEFEVWWFNTVDNRSGEYGEMVWHWYFTKALPKGMLLTALLVPLAFLRKGLIDLSLFGFFAPILGFITLYSLLPHKEIRFIFPALPMINVCAAYGMSRLHTLVFAKSQTKAKQWVCKGMYLCGVGCIALSMLGSLIFLRLSTDNYPGGVALEQLEQHGIHWENVHVHVDVAAAMTGVSLFGQRQIPFRIDKS
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. mdm34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
Subcellular Localization:
Membrane. Mitochondrion outer membrane; Multi-pass membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Sequence:
MSFVLKDWSSRFSDSFKERAVSLLSSTLNKGSTHSMIADRITVKELNMGTIPPDLEILEIGDLASDRFQGLFNLHYAGDAYLVLQTKVQANPLSVKQTPFPGLTSRRDMLAARAPLTVPMYLRLSEIKLNGIVVLVFSRQKGVTMVFRNDPLESLKVSSSFDSIPAIARFLKREIEVQLTSLFQEELPAIIYKLSRYWCAHMESPFSMSSVISRPPSQQRVSRSVPDVIETPPDYNESTKLDTNSPVKIGPLSTTTHPNLLAIASLVTSRRSLAPNASPCIPMAVYRSSNLDTLNSQIVQTEDGALPASQSPTLQFSRLENSNESKFPTPKNASATPAASIFGHSDSSKRRRERKKKHHFVKVFNRASGEKHKEKETKQDVIESADIKISTPANELSKIKDKIISKQGQEQFAKSLSRKAALDLAMFSHRDCAPFAIKLNGLQWYIHSKVML
The following text describes a protein:
Function:
Has bactericidal activity. Potent activity against E.coli ML-35, L.monocytogenes EGD and C.albicans.
Subcellular Localization:
Secreted. Cytoplasmic granule.
Sequence:
MRIVYLLLPFILLLAQGAAGSSQALGRKSDCFRKSGFCAFLKCPSLTLISGKCSRFYLCCKRIWG
The following text describes a protein:
Function:
Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, including leaves shape, pedicule elongation, inflorescence organization and fruit maturation, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MKGTKKKTPCNKKLGGYLKEQKGRLYIIRRCVVMLICWHD
The following text describes a protein:
Function:
Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MAEETKHGGHKNGRKGGLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLAKAKDFRYNLSEVLQGKLGVYDADGDGDFDVDDAKVLLGLTKDGSNENIDSLEEVLNILAEESSDWFYGFLSFLYDIMTPFEMLEEEEEESETADGVDGLKERSASKPTVPPEEAEPYPWLEEQVIEDSGPQNTEDEVQEVQIESLLHEAVYTEHGDDVQQEEDGQVREPQPEDDFLVGSDTDDRYEPLETGTFHEETEDSYHIEETASQAYNQDMEEMMYEQDNPDSMEPIVGDDARTYHEADDLTYQDYDEPVYEPPENEGLESSDNAGEDSNIILEEVYMPPAEEQQEVPPVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEALSAFQELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPNVPTDLLKLTLKRRSDRQQFLGHMRGSLITLQKLVQLFPDDMSLKNDLGVGYLLIGDNNNAQKVYEEVLNVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVHGLKAQPWWTPKETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCSLLDKFPETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDATSFRLIFIVDVWHPELTPQQRHSLPAI
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MASRKRGLKFCPETNDLLYPREDKERRVLEYYCKTCNYCVQADPSEWCVYVHATVVDEKDKITTLYDVTADPTLPRTRDVRCPKCNHNEAVFVSEPTEQGMTLYFHCVACREKWRDYV
The following text describes a protein:
Function:
Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MSRKNLILLAVYIVFTVGASLWLGQRAYQWLPPAAAQEAQPVGDLFSFLVSLGSVVFLGVAGAMAYSVIFHRFSLQNPQGAPIRGNARLEIFWTVVPIILVTWIAWYSYVIYQRMNVLGPLPVVEVPQLLGEKAIAADAPAELAMAQGSNINPERIGVEVKQWLWTFTYPNGGVTSHELHLPLDRRVTLNMTSKDVLHGFYVPNFRIKQDIVPNREIEFSFTPNRLGEYKLHDSQFSGTYFAVMTAPVVVQSLSDYQAWLESQKSLTPGELPNPALDEFKQTPTTPLKSGWPTVPPGTRQ