lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Subcellular Localization:
Peroxisome membrane; Single-pass membrane protein.
Sequence:
MERIHALLSWQFCNLGTELAKPTNEAPQNAAADNVKSTSTPSVFVNSEPIREEQVQNAVKFLSHPKVQGSPVIYRRSFLERKGLTKEEIDEAFRRVPDPTPSAQPTNVSPDPQSKSSANVQPQSSSQALQPAAAAPAGVISSVVTTTRPRFRWIHAAYAVGFLAVSGAGTAVLLKNAIIPRFKCWIRKVISDEENDVLKRTNAGPSLEEETAAAAKAAAAAAADVAKVSQEMLNSKVEERKYFGELVKLLDVQLQEMKSMSTAIQKLEGHANTSGALSQFNHEDHGGLVTIPKQPFANGRAEFESRSGGYIKEPRSSSPPGSSEPSAAPHPKSYMEIMAMVQRGERPPNVKDINDSPPNPHQQIPNPRLAPRAKPWETIQTQNNSSNVYQYQSSAEAWNYNAQDNGIIDQSNGDASAPWWQRKNARITEIDHDEDLKTGQPVQRAWVPPQPPPIAMAEAAEAIRRPKPAAQKEQSSDETASRSSDVTDELQKITKFSESGGAESTSEMSSGMNLTEIQVEQE
The following text describes a protein:
Function:
Has a role in promoting meiosis whereby it is involved in establishing the mating pheromone signaling pathway. It also has a role in suppressing meiosis until the conjugation process is complete.
Sequence:
MFLEIILDSATYSFDRVITGKICFETNAATSPRSFQIQLRIKGYAVYHHGFLSSPSHKHPTTASASDSDEATEIFTHSQPLPIPAGPSSKSHAIDFKFKFPSKSASSLPCSKSNDSMVNICYMLKATISKRYAFLGSSQSAKAELIMVPPNLAGKPLSANSSFGSSAKTFQLPEFDSVTPSASLYKQPSFNSNPAPITTSSATHTSQFSTSSSSSVNSVHTPVMVPNPYFQYNSSMTAPSSSSSSVAPFVPRRQFSVSSASDPPQTPISMSPPIPPTPSQFSAFMYQNQQSYLSPQSHYENPLSISSRPSPCCPSTPSSAVTLSNGFDSQSNAYNNSGTGPPMLYKFPQRSYTAPNTSFNSQRRMSSITSLPTASFCPVKHGVSPPSLAGNQPSPLSSPLTNSNVSPSTICSPDNNVTFVNLAPGEKLTFKIEPNDLMDEEEVVENSNMYSIPGKTVATTVCHSSSSSGDFSALSCHRNLSFSESLPTAEDQVHNNHCAVSPSRRSSSNALYLATLPMGYERSNSVSYCSDSSLSSPLPDDNMLQDPHALNMAYAKEFDVLINEVLQSL
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the uridine in position 3485 of 28S rRNA.
Subcellular Localization:
Nucleus.
Sequence:
MKTMLAAPTASSNGRPIGPHKSWKKVNEERKALKRQRKQDKLLKELQQAKEAESQAGKAANEVQAKDKPNPSTLSIAVPGSILENAQSNELRAYVAGQIARAACIFRVNEVIVFDDVGIATARETKRSYEADGEGSSTGTVRSSSLQLARILQYLECPQYLRKYFFPLHKDLKYSGLLNPLDTPHHLRQQSKFRYREGVICDKKAKEGHSYANVGLLNDVLVDKAIEPGVRVTVKMEPQSESCRKQRGTLVSPDEPRRETGVYWGYQVRIAHSMSEIFTKSPYATGYDVTVGTSDRGTNVHEVPNRSYNFNHMLIVFGGLQGLESALANDEKLTVDDPELLFDHYVNVLPRQGSRTIRTEEALLIALAALQEKLQPQVADVEIDLTDLLPKSEDSGIAVRRDVLVSKKQKKRKQVEDTPDETVVDEPSFSKPLPKVARLTANPFADSSEELAKNTPAQDDFEVVSSTTVSGTSHSCADDDLSRFD
The following text describes a protein:
Function:
Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Sequence:
MSAFRELGSVEDTAMDAANAKLSAVQRGYYHDRYIGCFVPQELKQLPPMNLGYYVRTQAIYVAVKKFHEIHGSNMQVVVLGCGYDTLFWRLRDEKITVKNWFDLDMQHVVNKKSKVINSNSFEPMDNYHLFYADLSKPEMVKQELNSHGFEDIPTIFIDECTLIYVDPVSVDEILKFAASLKSNAFISYGMVKPDDQFGKMMVKNFDGFGAPLKGIKMYPTVASHKDRCINAGFKHAKSIDLNQTMKVVIPRENFMKIMRLEMQDDPDELAYMLQHYVLAVAGSDSEFVSII
The following text describes a protein:
Function:
In its thiocarboxylated form (CysO-COSH), is the sulfur donor in the CysM-dependent cysteine biosynthetic pathway. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis.
Sequence:
MNVTVSIPTILRPHTGGQKSVSASGDTLGAVISDLEANYSGISERLMDPSSPGKLHRFVNIYVNDEDVRFSGGLATAIADGDSVTILPAVAGG
The following text describes a protein:
Function:
Regulatory peptide encoded by the primary transcript (pri-miR164a) of the microRNA miR164a that enhances the accumulation of its corresponding mature miRNA. Acts probably as a transcriptional activator of its corresponding pri-miRNA.
Sequence:
MPSWHGMVLLPYVKHTHASTHTHTHNIYGCACELVFH
The following text describes a protein:
Function:
Repressor for the uxuRBA operon.
Sequence:
MKSATSAQRPYQEVGAMIRDLIIKTPYNPGERLPPEREIAEMLDVTRTVVREALIMLEIKGLVEVRRGAGIYVLDNSGSQNTDSPDANVCNDAGPFELLQARQLLESNIAEFAALQATREDIVKMRQALQLEERELASSAPGSSESGDMQFHLAIAEATHNSMLVELFRQSWQWRENNPMWIQLHSHLDDSLYRKEWLGDHKQILAALIKKDARAAKLAMWQHLENVKQRLLEFSNVDDIYFDGYLFDSWPLDKVDA
The following text describes a protein:
Function:
Plays a role in tight junction biogenesis and in the establishment of cell polarity in epithelial cells (By similarity). Also involved in adherens junction biogenesis. Required for polarized epithelial organization, cell-cell adhesion and remodeling of myocardial cells during heart tube elongation during embryogenesis. Functions in cellular patterning of the retina and development of the retinal pigmented epithelium. Also required for embryo body axis specification.
Subcellular Localization:
Apical cell membrane; Peripheral membrane protein. Cell junction, tight junction. Note=Localizes to the apical region of the cell membrane, in the vicinity of junctional complexes in the neuroepithelium and the photoreceptor layer. Enriched in the areas immediately apical to the adherens junctions-associated actin bundles.
Domain:
The PDZ domain is required for apical location.
Sequence:
MTTSHMNGYVTESDGGGGTDIVEEGVQRHREMAVDCPSELGARTLPVRRSAQLEKIRQQQEDRRRREEEGRSRQELDLNSSMRLKKLSQNPKVGIDNPTFEQMEGPGGSAGGLQSLIAPPALLELEDLLMSLKQVQHSLNDSQSQEDVELVLQLVQKPDFQKAFSIHNSVAHYMNRPSPPYPLTDHAQTLAQEVEVMVQNSSHKEGLELSSLLSTSHMQALMMAHDSVAEQEMQLEPLVPSVNASETLTQWGGETVKIVRIEKAKDIPLGATVRNDMDSVVISRIVKGGAAERSGLLHEGDEILEINGVEIRGKDVNEVFDILADMHGVLSFVLIPSAQIKSPPIKETVVHVKAHFDYDPSDDPYVPCRELGLCFQKGDILHIISQDDPNWWQAYRDGDEDNQPLAGLVPGKSFQQQREAMKQTIEEDKEPEKTGKLWCAKKTKKKRKKMQYNANKNDDFDNEEILTYEEMALYHQPANRKRPIALIGPPNCGQNELRQRLLSTEPDRFAGPVPHTTRSRRDAEANGRDYHFVSRQAFEMDSAAGKFIESGEFEKNFYGTSTDSVRQVINTGKICLLCVHTQSLKVLRSSDLKPYIIFIAPPSQERLRALLAKDNKNPKPEELRDIIEKAREMEQNYGHLFDAAIVNTDLDKSYQELLRLINKLDTEPQWVPSSWLR
The following text describes a protein:
Function:
Binds to the 23S rRNA.
Sequence:
MELHQLKSVSKSRNHKSKVVGRGHGSGLGKTSSRGQKGQKARKSGLTRLGFEGGQTPLYRRLPKYGVANKGILKKRWVVLNLNKVAKLNLKTVTRATLIEKKVISKKNNLPLKLIGNTKLTTPIHFEVQKISKNALNAVQTSKGSVKIIT
The following text describes a protein:
Function:
Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes.
Subcellular Localization:
Nucleus.
Sequence:
MLPCARSVLRRRGLALLRGFAEGECGRGEPLANARCAATLAGLGRGRGGVGRWADPPARGEPRRLGAGWPAGAQTRSFLGCGDGEEGSVLSKVYEERRVMGYSPEQMYAVVAAVDLYEDFVPWCQRSRVIRRYDNGSFDAELEIGFKFFVESYVSHVEMEKPKYIKTTASQSGLFDHLINVWEFKPGPVPGTCDLYFLVDFKFQSPLYRQVASMFFKEVVSKLVGSFSDRCFRIYGPAVPVLEKSYGHGR
The following text describes a protein:
Function:
Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity).
Subcellular Localization:
Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Nucleus.
Sequence:
MVKVGINGFGCIGRLVTRAAFDSGKVQVVAINDPFIDLDYMVYMFKYDSTHGRFKGTVKAENGKLIINDQVITVFQERDPSSIKWGDAGAVYVVESTGVFTTTEKASLHLKGGAKRVVISAPSADAPMFVVGVNHEKYENSLKVVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHAFTATQKTVDGPSGKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKITGMAFRVPTPNVSVVDLTCRLQKPAKYDDIKAAIKTASEGPMKGILGYTQDQVVSTDFNGDTHSSIFDADAGIALNENFVKLVSWYDNECGYSNRVVDLVCHMASKE
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:
MDSLVSMRVFCLVAELKSFATAAQRLRISPAMASKHVMQLEKRLGTRLLNRTSRRVSLSESGALYFEQARQMLDSLDEVEAAVSKATVVPRGTLRLTAPVWMANAIFAGVLADYQARYPEVCLDVDLSGRLVNLVEEGFDLALRATGTPDEALIARPITKVPFLLVAAPAFLKRAGRPTKFADLAGQALLHYALYPGESFSLNRNGTVETIKLNPVLRSGNETLLHMAALEGMGFAFLPKWLVADDIAAGRLVHMLPDDIIFEGRLFAVYPSRKYLSAKVRTFIDFIAADKRMR
The following text describes a protein:
Function:
Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MIETTTLRFSHGDTTVLDGVDFTAETGDVTVLFGRNGAGKSTLLRHFNGLLEPDAGTVSVGGTPIAYDDDSLTELRLRVGLIFQNPDDQLVAPTVQQDIAFGPRNAGIEDTDRIEDVVSTFDLSEQAERLCNTLSGGEKKRVSLAGVLAMDPEYVLLDEPTAGLDGAGCRTIVEFVSSLAADGITTVIATHDVGFGLTVADTVTVLEDGVIDYRGDTLSQSLAAEYDLRSYVFDDWSDVSVE
The following text describes a protein:
Function:
Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MCLRACTQERNLCRIPCASWMLYLLFLLTFMCPLPICNQATNLTEELNLLHCSDWFVYAYALRDMLYDRSIARVFLVLTTLLYVYYVVWIGVTPFIVSSHFTQNFFPPREYGIFVAAAVMTLMLGVTVTLASVRTILWAGAVGPEESG
The following text describes a protein:
Function:
Ribosome preservation factor that protect a small pool of nontranslating, vacant ribosomes in cells under nutrient starvation conditions. Under nutrient-limiting conditions, cells reduce ribosome biogenesis and degrade ribosomes via autophagy (ribophagy) or proteasomal degradation. To avoid excessive degradation during starvation, STM1 binds to and protects 80S ribosomes from proteasomal degradation. Under nutrient-sufficient conditions, TORC1 phosphorylates and inhibits STM1 to prevent formation of dormant 80S ribosomes. Acts as an inhibitor of mRNA translation by promoting ribosome hibernation: clamps the two ribosomal subunits, thereby preventing their dissociation, and inhibits translation by excluding mRNA-binding. Acts via its association with eEF2, promoting ribosome stabilization and storage in an inactive state. May also repress translation by preventing association of eEF3 with ribosomes (By similarity). Binds specifically G4 quadruplex (these are four-stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs. Extends chronological lifespan when overexpressed.
Subcellular Localization:
Cytoplasm.
Sequence:
MSVASKNLFDLLGEETPAATTTEKKTAASRDKKRSDSPPVPRELVAQSTTSRKRDPNQPTPRERTVNKKADQPRRRRQAPQGNEAFAREGKEARANNAAHPVDATGAPSNRRNARARRGREFDRHSQTGRVDTKKATERGWGDLVNSAANPDVAENEGNTPSGAQTPAAEEENVKTLDEYLSERKSAAKPVGRTVEKLENATKVEKSAPEELFASLKKSASQKKSAAKESKPKKVLLDIEQTFTARPARGGRPNRAPRRGPSETASKTQQAPPTLSETDFPALA
The following text describes a protein:
Function:
Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.
Domain:
A pair of annexin repeats may form one binding site for calcium and phospholipid.
Sequence:
MADVQGTIFPAEDFDAEVDAETLYEAMKGWGTDEDPIIDVLANRSNEQRLEIREKFKQMYGERLIDRLKSELKGDFEEVVVALLTPPAEYLARCIKGAMKGMGTDEQALIEIMCTKDNQEMEELKSTYAEVFDGDSLEDDIEGETSGHFKRLLVSLCNAGREEGDENDVDEGLAEEDATEIYDAGEGQRGTDESKFNSVLALRSFPHLRVMFDKYLELSGNSIDNMIDEECDGAIKDGYMAIVYCVRNIPGFFAKRINDACKGIGTDDSTLIRCVVSRSEIDLQQVKEVFETRYGRPLSEAIKDECGGDYKNMLLAIVKDASVNPFPDFDAEEDAKILRKAMKGFGTDEDAIIEILCHRSNDQRQEIDTMFKQAYGKDLIDELKSELGGNFEKAILAMMQKPAVYDATCLRKAMKGAGTDEATLIEIMCTRKNDELTAIKEAYNAEFDRDLEEDLKSETSGHFERLLVSMCQANRDESYEVDEEEAESDAQELFDAGEGKFGTDESTFNMILALRNFNQLRAIFRAYERIAGTDILDSIKGECTGSLEDGYLTIAKGAMDTPALFAERLYKSMKGLGTDDKTLIRIVVTRSEIDMEYIKAKYEEMYEKPLADAIADDCGGDYKKCLISLLG
The following text describes a protein:
Function:
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
Subcellular Localization:
Cytoplasm.
Sequence:
MHVARLSIHRLRRFEAVEFHPASTLNLLTGDNGAGKTSVLEALHVMAYGRSFRGRVRDGLIRQGGQDLEIFVEWRERAGDSTERTRRAGLRHSGQEWTGRLDGEDVAQLGSLCAALAVVTFEPGSHVLISGGGEPRRRFLDWGLFHVEPDFLALWRRYARALKQRNALLKQGAQPQMLDAWDHELAESGETLTSRRLQYLERLQERLVPVATAIAPSLGLSALTFAPGWRRHEVSLADALLLARERDRQNGYTSQGPHRADWAPLFDALPGKDALSRGQAKLTALACLLAQAEDFAHERGEWPIMALDDLGSELDRHHQARVIQRLASAPAQVLITATELPPGLADAGKTLRRFHVEHGQLVPTTAAD
The following text describes a protein:
Function:
Required for pre-mRNA splicing as component of the activated spliceosome. Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MATSLGSNTYNRQNWEDAVSVPALPEGGGRRRRGQAVGGRAGTRLRRGPGNLREKPRCGLAWPRLEAGGPPFCGLDRESSARLQDQPVPLSARGPFSWPRRKCRQRPSRGPARPALDLGFLPCSPALLLARPPAAPLWPRWQGLRSLAFNQIPLFHQDFPILCQTCLGENPYIRMTKEKYGKECKICARPFTVFRWCPGVRMRFKKTEVCQTCSKLKNVCQTCLLDLEYGLPIQVRDAGLSFKDDMPKSDVNKEYYTQNMEREISNSDGTRPVGMLGKATSTSDMLLKLARTTPYYKRNRPHICSFWVKGECKRGEECPYRHEKPTDPDDPLADQNIKDRYYGINDPVADKLLKRASTMPRLDPPEDKTITTLYVGGLGDTIAETDLRNHFYQFGEIRTVTVVQRQQCAFIQFATRQAAEVAAEKSFNKLIVNGRRLNVKWGRSQAARGKEKEKDGTTDSGIKLEPVPGLPGALPPPPAAEEEASANYFNLPPSGPPAVVNIALPPPPGIAPPPPPGFGPHMFHPMGPPPPFMRAPGPIHYPSQDPQRMGAHAGKHGSP
The following text describes a protein:
Function:
DnaJ-like chaperone required for the folding capacity of the endoplasmic reticulum.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MNGYWKPALVVLGLVSLSYAFTTIETEIFQLQNEISTKYGPDMNFYKFLKLPKLQNSSTKEITKNLRKLSKKYHPDKNPKYRKLYERLNLATQILSNSSNRKIYDYYLQNGFPNYDFHKGGFYFSRMKPKTWFLLAFIWIVVNIGQYIISIIQYRSQRSRIENFISQCKQQDDTNGLGVKQLTFKQHEKDEGKSLVVRFSDVYVVEPDGSETLISPDTLDKPSVKNCLFWRIPASVWNMTFGKSVGSAGKEEIITDSKKYDGNQTKKGNKVKKGSAKKGQKKMELPNGKVIYSRK
The following text describes a protein:
Function:
Beta-apo-4'-carotenal oxygenase involved in the last step of synthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigment and leading to orange pigmentation. Converts the aldehyde beta-apo-4'-carotenal into neurosporaxanthin. Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme al-2 first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase al-1 then introduces 5 desaturations to lead to 3,4-didehydrolycopene via the intermediates phytofluene, zeta-carotene, neurosporene and lycopene. Al-2 cyclase activity then converts 3,4-didehydrolycopene into torulene. Al-2 can also convet lycopene into gamma-carotene which in turn is converted to beta-carotene by an additional al-2 cyclization reaction. Torulene is the substrate of the dioxidase cao-2 that breaks the molecule, removing five carbon atoms to yield beta-apo-4'-carotenal, whereas the aldehyde dehydrogenase ylo-1 mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).
Sequence:
MAASKVEIAPFEVTPLDAIPAVCSTARATFASHKTKNLQWRLVQLRKLYWALDDFKASLMAALQQDLRKGGYESDFTEVDWVKNDCLHMINNLETFAKTEKLKDLPVTYSMMNFRVKKEPLGTVLIIGPYNFPIQLVLAPLVGAIGAGCTAVIKPSELTPACAMAMKEMIESRLDRDAFAVVNGGVPETNALMEEKWDKIMFTGSAQVGSIIARKAAETLTPVCLELGGRNPAFVTKKANLALAARRLMWGKVLNAGQVCMSHNYVLVDKDVADTFIEFLKIAYKDMFPNGAKASPDLSRIVNARHFNRIKKMLDETKGKIVMGGEMDESELYIEPTAVLVDSLDDPMMQEESFGPIFSIYPVDTLDQALSIANNVHRTPLALMAFGDKSETNRILDEMTSGGACINDSYFHGAVHTVPFGGVGDSGWGAYRGKASFDNFTHFRTVSETPTWMDRFLRVRYMPYDWSELRLLQRWTNKKPNFDRQGTVAKGSEYWMWYFLGLGTKGGVKGALMRWLVVVAGYYLSAYMKARRA
The following text describes a protein:
Function:
Involved in the maturation of [NiFe] hydrogenases. Involved in the biosynthesis of the Fe(CN)(2)CO cofactor. HypD may act as a scaffold on which the Fe(CN)(2)CO cofactor is formed. In complex with HypC, accepts the cyanide ligand generated by HypF and HypE, and also coordinates the carbon monoxide ligand. Required for the formation of all three hydrogenase isoenzymes (Probable).
Domain:
In addition to the iron-sulfur cluster, contains two additional oxygen-labile iron ions.
Sequence:
MRFVDEYRAPEQVMQLIEHLRERASHLSYTAERPLRIMEVCGGHTHAIFKFGLDQLLPENVEFIHGPGCPVCVLPMGRIDTCVEIASHPEVIFCTFGDAMRVPGKQGSLLQAKARGADVRIVYSPMDALKLAQENPTRKVVFFGLGFETTMPTTAITLQQAKARDVQNFYFFCQHITLIPTLRSLLEQPDNGIDAFLAPGHVSMVIGTDAYNFIASDFHRPLVVAGFEPLDLLQGVVMLVQQKIAAHSKVENQYRRVVPDAGNLLAQQAIADVFCVNGDSEWRGLGVIESSGVHLTPDYQRFDAEAHFRPAPQQVCDDPRARCGEVLTGKCKPHQCPLFGNTCNPQTAFGALMVSSEGACAAWYQYRQQESEA
The following text describes a protein:
Function:
Involved in DNA non-homologous end joining (NHEJ); required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (lig4). The lig4-xrcc4 complex is responsible for the NHEJ ligation step, and xrcc4 enhances the joining activity of lig4. Binding of the lig4-xrcc4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MNESSVSRFENITDDSGNTNGGFYYLKCNWQYNSFTIYLTDLTNVWSSNVTTKYIENILKPQGMSFDQYFQLLKKSLLKQDQTKREFDYKIDKYKRKNNNNINNNNEDIEFIIIIILSEFDNINVKSSIPLIKLSNHFTTFQHYFDWLFDKYQSLSLQNQTLTLQTQSLQSQFNQSLEQNKLFQLEKDRIESNLIEKFIIILNEKKKKIKEYKQPINNLLLEQKSISSSLSNCKCNNNNNNNNNKSIVNNNKNKSPSKQQVYTTPKKKKRNYQSNLINIDNDDDDDLGNNDNVNNINDENDNDNDNDNEEDYKPTFNNSTPPLLDLLSNDYDSYYNVPTNVRKKFKPTPTLTTTTTTTTTTTTASIIKTPTKKRNSISPQKSPHHHRNINIKKNNNNNNPSSPMKKYNANGTLIPNNNINSLIPITPMKSKSKLFNFNDDDNHDIGASELLNDL
The following text describes a protein:
Function:
May be involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MGEHPSPAPAVAACAEAERIEELEPEPEPEPEEPLPMAPEDHWKVLFDQFDPGNTGYISTGKFRSLLESHGSELDPHKREVLLALADSNSDGHICYQDFVNLMSNKRSNSFRQAILQGNRRLCSKALLEEKGLSLSQRLIRHVAYETLPREIDRKWYYDSYTCCPPPWFMIAITLLEIAFFLYNGVALDQFVLQVTHPLYLKNALVYHPQLRAQAWRYLTYIFMHAGIEHLGLNVVLQLLVGVPLEMVHGAARIGFVYVAGVVAGSLAVSVADMTAPVVGSSGGVYALVSAHLANIVMNWSGMECQFKLLRMAVALICMSMEFGRAVWLRFHPSAYPPCPHPSFVAHLGGVAVGITLGVVVLRNYEQRLQDQSLWWIFVAMYAVFVLFAVFWNVFAYSLLELRLPPPP
The following text describes a protein:
Function:
Co-chaperone required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria. Stimulates the ATPase activity of the mitochondrial Hsp70 chaperone ssc1, to mediate the transfer of iron-sulfur clusters from isu1 to grx5.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MLKQAGNQSFRPFISFAQKSLFNRQITGNHWIFARFKFYPLNKIVNYNHFHSSSCQSEAKNFYKQFEGDISDPPPKGPFDIDLGALKSSYLRKMKTLHPDVAQGKDAALAQRDSAELSKAYNTLKAPLTRAEYILQLQGINPVSEDISNSDPEFLMEIMDVHENISASRDSPEKLLQLSQENQGRKVQEINEIRKAMESSNWDSALLYVNRLRYWNTIDKILHDL
The following text describes a protein:
Function:
Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
Sequence:
MEEEGTLIQGDGSYGLYIREQSTSSIPLVLVTENQNKSFYKLAMEAGVPEISIHMPAICRICFDEDVKAEQMYSVALCGHQFCVDCVKQHIESRLLEGCVPRCPHDQCEYKLTFRSCANLLTPKTKSDSSIYLLLKTLKLGDVVSNAVNPFASTAKFHGIVTCHAVITRGVAIRFATHVVPNGSKEVALTA
The following text describes a protein:
Function:
Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Subcellular Localization:
Peroxisome membrane.
Sequence:
MSDQLSSLEENRPETPPVREDLVNTAIKFLENPNVLKTSLGEQQRFLKRKGLTDEEIRQACEKSGAYKYHEQRNRTPPLPPSSLIPYPNSATVQISLFDKVKEVVHNVAIFSFVAYVVYKFYMKFIAPFFFGKKKKSVEESIDELDKSFKQSVNDLKNNLLSVKVEVDKISQGAESSTQRQLSDLKSEIATVKGLLLSRNQFPPVSKSSVVRPSIPAWQKTSISQDSDPDSDPERKAEELMEVGSGSGSSEHEHAAKNSDSSLDIISFSSKDSDFRRHKSKDVDDDDDDDKD
The following text describes a protein:
Function:
Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. Prevents helicase DHX37 to be recruited before post-A1 state.
Subcellular Localization:
Chromosome. Nucleus, nucleolus.
Sequence:
MAAERELDSSELPGSEALLDAVLRTLYDLGETEGETEQKRTRKKKEKKRDSETVADRAAEPLPLPASPGRDQRKSASSFFKKLREELQSAPAAPSEVPAATTAVSLFPLENDSKLVEVVEFHSRSEKRKPKSEEDKPAKNKTKVLEKDVVIQEFNLEKARLEVHRFGITGYGKGKERVLERERAIMLGAKPPKNTYVNYKVLQEQIKEKRTSMEEEKRAAQETDIFKRKKRKGRSQEDRRSKKLAPSILSSGRAAQVGKFRNGTLILSPADIKKINSSRVSK
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:
MFDSTKLPASEFEQRYGRVPDHGETIWSDLVAEGVTAPEGKSHMTNLTFQALGDNKVLTADLSDSLNKMNFTNMSEVQARTVLPALKGEHMLVKAKTGTGKTAAFCIPALQRARDAKIIDGVQGLKSLVISPTRDLAQQTLAFLKQVTAKGPLKDLTVAEAVGGTSVRHLLNETVNDYDGGADFLVATPGRLLFLLKDPQAAEYFANIDSVILDEADTLLDQGFEADLCEIVRLISTYTKDPYQRNFYSATLDDRVKRFAIKNCQGRVRVVDAVGKESPAQDLVEQRFVKIEELGDMLTIMAQDMKRDAAETLPKEPFKAIVFCPTKRLTETNHAILKQLVYEQGDIFGCEARNVFSLHSDMSQNGRLRAAENFRNTPHSILVTSDVAARGMDFPNVTHVYHYGVTNQFEPYVHRMGRCGRNGATGVSTMYMMEHSKWYLTMLKRNKMLDNADKVKILEEEPEESVKENVAKATKAAFSSGKDKTPNGHDASRIASAVTSFMGYYNSCSPDMKPNDKPKQVFSSFVSLCRSLGMEGNLNFQSLDRSGMFSQNFGIDRRDISQLAIPRRDAVPQSISETLFGVDANDIDYNDTTSQADRLRAQRGGSRGGNRGGYNSRGGDRGGYNKRGGDRGGYNSRGGDRNNYRNDRGDRNYDRNDRNDRNNNRYNNRNDRNDRSGGNWGKREQY
The following text describes a protein:
Function:
May be involved in cell wall biosynthesis.
Subcellular Localization:
Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.
Sequence:
MVLIFSCLYFSAKVPVSSENLDEFGLLPIIELNDTELRERRVKLLENFITSLQESTRLATGGEDESDWFTEEARVKWNRENPCLSRREMRLQYKQRKHVPYVEPNSQWQEVLREYSKLHRTCLHRIGDPVAYFTSQNSTVECKFTILDTELAAGLGNRLVMIASAFAYSLITQRVLLIARPGILPPQLLCEPFEGSSWLHFDPNQLVTPFNRDSRGLGSYWNKSGSFHSRIDIARGAEGGDDTSQLIMDYAVANGEGGYTEQLDSRFFCDTEQDYYKNVTWVYIMGCIYFAPKLYAVPSFRPVLDALFPDKMMLTNLLRDVMSPSDVVWEQVKSIQRDYGLQRADRRLGIQVRYRYQKEQFDRMDRVVEARIWQCAINNHLLPPVVTNSRRMLPHVSNRTTSVFVASLFDGVKNNLSDTFATYPTETGEHVEVFQFSHEGLQKFGVKIFQDALAEIITLSYSDYLFVTPQSTFSGVAQAYGGLIPWFIGFRDELETRPPCTRGQTVDTCFQVPLDYVFQCRYDSAVHRKEISTVYPDIQKCLEADTPGLQLITKQPEIP
The following text describes a protein:
Function:
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Miscellaneous:
MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MIELTKPRIVTMILVTTVASALIAGSATLTLIDWFWLMIGTALIAGSAGAANQVWECRIDRNMPRTANRPVPGGRMSYAVAVALTASSGIAGSIILWLGNGLVPACVGIATWLIYVLVYTPMKTRTAWNTTVGAIAGALPVFIGYTAAGGTLTELPGWMLFGVLACWQYPHFMAIAWLYRTQYAEAGFCMTTTVEPTGRHAAWQSILGSVALATCGVVLAWFPDGQWVASAASVLATVLILAASWPLLRASLNFRANPNDKTARKMLRWSLVVLPAVLLVMTLRASL