lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Involved in nucleotide excision repair.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MGQRNWLLFEYASKKYFIEVDINDTFGKFKQIVENKIGTRLPENIAFIKQGGDDKYEDMTQTFKDAGITEMSTLTITNSASAPTRTKSVSAKPAPAQPAPQKTEPVKAQPIKPAQPAPAPQPVPQPAPARPAPQPAPQPARSDLSDQIQQISQVTGETDHSKIEALLRQNNESVEAVVNAILDERSQTNVVTQTSQYSNAVQEQFNQFTQAEKDAIERLKSNGFSFSQCVEMFVACDKNEELALSLLLTG
The following text describes a protein:
Function:
May inhibit cardiomyocyte growth.
Subcellular Localization:
Secreted.
Sequence:
MHQENLSHLKGTWTPWSKLVGVSGMPSMGPIQPQRTAPLWARLLLVALLVPGTWSLLTDQQEEMLVELHNHYRGQVSPSAAAMLPLKWDGNLKLVAEGYAAKCIWEHNTELEDTGENLFAGTGKLDLSEAVEKWFLERLDYSYENNSCDEDKMCGHYTQMVWADTHRVGCAVHFCNTIENLDWNNVSYLVCNYFPAGNYDDERPYVEGDWCSRCPEDLDVCQNHLCVKKEVGDTDEEEMTTDSPLMTDIVTAASNPPSVHDSFADVTPIILEKESDDTPSPWSAMETVSSPGLQPTPLGEEEENSEPNNLDEEKQRKESVHRQEETQKILEPARTSAASVLAASFLLACLTGLLNLDL
The following text describes a protein:
Function:
Involved in the assembly of an N-linked disaccharide that decorates the S-layer glycoprotein and flagellins. AglC catalyzes the transfer of 2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (Glc-2,3-diNAcA) from uridine 5'-diphospho 2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (UDP-Glc-2,3-diNAcA) to the AglK product Dol-P-GlcNAc to yield Dol-P-GlcNAc-Glc-2,3-diNAcA. AglC is specific for the monophosphate-linked Dol-P-GlcNAc.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNFISIIIPTFNEEKYITKCLENWFNQDYPKENYEILIFDGKSTDKTLDVIKELQKKHNFENIKIYTNEKRKQVYAFNEGIKNANGDFFIIFGAHAYPEQDFLKNNIETYQRIKKEEPKLAGVGGIINKISENMSAEIAKVIYSTPLSGGSSFWYAKEGFFSNTVVYGMYDTKMIKESEILFDTDFITGQDFEFNLHLIKEGFKLYTNPNIVSSYYTRSSVKKFIKQTISYGAAKGLMIRKGYFNILWLFPFGFLFMLLSIIITGLLIFIYIMAILIDTIRLLIKTREPLYIALPILLFLFHCLISYGFFKGLIKGNSTFK
The following text describes a protein:
Function:
Mediates the transfer of all common phospholipids, cholesterol and gangliosides from the endoplasmic reticulum to the plasma membrane. May play a role in regulating steroidogenesis. Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol. Also binds fatty acids and fatty acyl Coenzyme A (CoA) such as phytanoyl-CoA. Involved in the regulation phospholipid synthesis in endoplasmic reticulum enhancing the incorporation of exogenous fatty acid into glycerides. Seems to stimulate the rate-limiting step in phosphatidic acid formation mediated by GPAT3. Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs; Plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids. Catalyzes the last step of the peroxisomal beta-oxidation of branched chain fatty acids and the side chain of the bile acid intermediates di- and trihydroxycoprostanic acids (DHCA and THCA). Also active with medium and long straight chain 3-oxoacyl-CoAs. Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol between membrances, in vitro. Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs.
Subcellular Localization:
Cytoplasm. Mitochondrion. Peroxisome.
Sequence:
MPSVALNSPRLRRVFVVGVGMTKFMKPGGENSRDYPDLAKEEIQRGRAALQLLYVYTLGVQVLCFSVGESTCGQRAIYHSLGLTGIPIINVNNNCSTGSTALFMAQQLVQGGLANCVLALGFEKMEKGSLGTKYSDRSNPLEKHIDVLINKYGMSACPFAPQLFGSAGKEHMETYGTKVEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEIMKSRPVFDFLTVLQCCPTSDGAAAAIVSSEEFVQKHGLQSKAVEIVAQEMVTDMPSTFEEKSVIKMVGYDMSKEAARKCYEKSGLGPSDVDVIELHDCFSTNELLTYEALGLCPEGQGGALVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAAVVTLYRMGFPEAASSFRTHQISAAPTSSAGDGFKANLIFKEIEKKLEEEGEEFVKKIGGIFAFKVKDGPGGKEATWVVDVKNGKGSVLPDSDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGNMGLAMKLQSLQLQPDKAKL
The following text describes a protein:
Function:
The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MATINMTPGDLELGRDRGRIGKPIEIPLLENFGFDSQLGPFYLGFWNAVAYITGGIFTFIWLMVMFAQVNYNPVAFAKYFVVLQIDPPSSRYGLSFPPLNEGGWWLIATFFLTVSIFAWYMHIYTRAKALGIKPYLAYGFTGAIALYLVIYIIRPVWMGDWSEAPAHGIKALLDWTNNVSVRYGNFYYNPFHMLSIFFLLGSTLLLAMHAGTIWALEKYAAHEEWNEIQAPGTGTERAQLFWRWCMGFNANAYSIHLWAFWFAWLCGITGALGVFFSMPDFVNNWFQWGIEAGINYPQGPTPPVSLP
The following text describes a protein:
Function:
GTPase that may function in chloroplast ribosome assembly (Probable).
Subcellular Localization:
Plastid, chloroplast.
Domain:
In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern; The DARXP motif is also sometime designated as G6 region.
Sequence:
MFAQLAPSPSPSPANVSHFVHRRTFRQCTYAVSASLPTANSSRPPPIQIVGGKDLNLDVTRKDDSIGFKLEANEDEIDWMNLESDIRLWTRALRPVQWYPGHIMKTEKELREQLKLMDVVIEVRDARIPLSTTHPKMDAWLGNRKRILVLNREDMISNDDRNDWARYFAKQGIKVIFTNGKLGMGAMKLGRLAKSLAGDVNGKRREKGLLPRSVRAGIIGYPNVGKSSLINRLLKRKICAAAPRPGVTREMKWVKLGKDLDLLDSPGMLPMRIDDQAAAIKLAICDDIGEKAYDFTDVAGILVQMLARIPEVGAKALYNRYKIQLEGNCGKKFVKTLGLNLFGGDSHQAAFRILTDFRKGKFGYVSLERPPL
The following text describes a protein:
Function:
SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity.
Sequence:
MRILHTSDWHLGQNFYSKSRAAEHQAFLDWLLETAQAHQVDAIIVAGDIFDTGSPPSYARELYNRFVVNLQQTGCHLVVLAGNHDSVATLNESRDILAFLNTTVIASAGYAPRLLHRRDGSPGAVLCPIPFLRPRDIITSQAGLSGSEKQQQLLHAIADYYQQQYQEACQLRGERKLPVIATGHLTTVGASKSDAVRDIYIGTLDAFPAQHFPPADYIALGHIHRAQCVGGTEHIRYCGSPIALSFDECGKSKCVHLVTFEQGKWQSTESLAVPVTQPLAVLKGDLASITEQLEQWRGVEQSPPVWLDIEITTDDYLHDIQRRIQTLTESLPVEVLLVRRSREQRERSLANERRETLSELSVEEVFARRLALEALDPPQRERLNQLFSSTLYALNEEHEA
The following text describes a protein:
Function:
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.
Sequence:
MRKMKKMDADTLTAILAFQRLSGTGKSLLEGAAKDAEAGRYSIIAINPVHEIKVYQHDYYIDGTHQVVADPLKEIELFIEKAREDELELPLDSGAIGYVGYDVIALYEDLGEIPVETRDIPDIRFYVYESFVIMDHQAEELILVQDNCYSGRSEADLDKALESMLTELTTPKKDEHKAVHVPKMSYKSNYTKDEYMGLVKKAKTYIQEGDFFQIVLSQRLEADFTVKPFDYYRKLRLLNPSPYLYFIDFGDTVLIGSSPESLIKTKGRTVITNPIAGTRRRGATKQEDELLASELLSDEKELAEHRMLVDLGRNDIGKIAETGSVHVPVYLTIERYRFLMHLVSVVEGTLKTGLTAIDALRSTLPAGTVSGAPKIRAMERIYEWENVKRGPYAGAVGYLTKNGDSDFALSIRTMVLHNGKAYVQAGAGIVYDSDPESEYLETLQKAKALLEVGE
The following text describes a protein:
Function:
Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Subcellular Localization:
Mitochondrion.
Sequence:
MLSRLLVRNYSSSTFQETKRIVESSTLSNGLKVVSLVGGYTGPAVSLGLYIKSGSRNETQATAGLNQVLKGLAFESNTNKLGIEVQREIETSGSTAFVQAGRDNLLISTQTLPNQSLQMLKNLANITQPTLPYHEVRDVAEVIAEESEAYNHCPTTSILESAHQTAFRGKTLGRPLVAPLCNLSNISQEVVSDYVNATYKPNNMVLVGVGLSHGELVEEAEKVTFGTTVNSTTTVPREAAKYIGGESLTYATGNTKVVLAFEGSAQTNIKNVAALTVLQTILGNGSPKVAPGNGRASRLFSLTQNNTGIVRSEAFNLSYADTGLFGVLVEVEGSNVAKTLSLLTSEISASTKATGKELERAKALAKVDVLEQADSRSGALEFIGKQAIYSDKIYTPVEFAEEINNVTAEDIQRVAKTLVSSKPTLVVVGDVSDVPTFESLKL
The following text describes a protein:
Function:
Actin-organizing protein that may cause stress fiber formation together with cell elongation (By similarity). Isoform 4 may play a role in actin filament polymerization in cardiomyocytes.
Subcellular Localization:
Cytoplasm, cytoskeleton. Note=Main part of the protein localizes to actin fibers and the remaining part displays filamentous staining; [Isoform 4]: Cytoplasm, myofibril, sarcomere, Z line. Note=Threonine phosphorylation in isoform 4-specific sequence TDTDEEEEVE is required for targeting to myofibrils in cardiomyocytes.
Domain:
The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity).
Sequence:
MATLACRVQFLDDTDPFNSTNFPEPSRPPLFTFREDLALGTQLAGVHRLLQAPHKLDDCTLQLSHNGAYLDLEATLAEQRDELEGFQDDAGRGKKHSIILRTQLSVRVHACIEKLYNSSGRDLRRALFSLKQIFQDDKDLVHEFVVAEGLTCLIKVGAEADQNYQNYILRALGQIMLYVDGMNGVINRNETIQWLYTLIGSKFRLVVKTALKLLLVFVEYSESNAPLLIQAVTAVDTKRGVKPWSNIMEILEEKDGVDTELLVYAMTLVNKTLSGLPDQDTFYDVVDCLEELGIAAVSQRHLNKKGTDLDLVEQLNIYEVALRHEDGDETTEPPPSGCRDRRRASVCSSGGGEHRGLDRRRSRRHSVQSIKSTLSAPTSPCSQSAPSFKPNQVRDLREKYSNFGNNSYHSSRPSSGSSVPTTPTSSVSPPQEARLERSSPSGLLTSSFRQHQESLAAERERRRQEREERLQRIEREERNKFRYKYLEQLAAEEHEKELRSRSVSRGRADLSLDLTSPAAPACLAPLSHSPSSSDSQEALTVSASSPGTPHHPQASAGDPEPESEAEPEAEAGAGQVADEAGQDIASAHEGAETEVEQALEQEPEERASLSEKERQNEGVNERDNCSASSVSSSSSTLEREEKEDKLSRDRTTGLWPAGVQDAGVNGQCGDILTNKRFMLDMLYAHNRKSPDDEEKGDGEAGRTQQEAEAVASLATRISTLQANSQTQDESVRRVDVGCLDNRGSVKAFAEKFNSGDLGRGSISPDAEPNDKVPETAPVQPKTESDYIWDQLMANPRELRIQDMDFTDLGEEDDIDVLDVDLGHREAPGPPPPPPPTFLGLPPPPPPPLLDSIPPPPVPGNLLVPPPPVFNAPQGLGWSQVPRGQPTFTKKKKTIRLFWNEVRPFDWPCKNNRRCREFLWSKLEPIKVDTSRLEHLFESKSKELSVSKKTAADGKRQEIIVLDSKRSNAINIGLTVLPPPRTIKIAILNFDEYALNKEGIEKILTMIPTDEEKQKIQEAQLANPEIPLGSAEQFLLTLSSISELSARLHLWAFKMDYETTEKEVAEPLLDLKEGIDQLENNKTLGFILSTLLAIGNFLNGTNAKAFELSYLEKVPEVKDTVHKQSLLHHVCTMVVENFPDSSDLYSEIGAITRSAKVDFDQLQDNLCQMERRCKASWDHLKAIAKHEMKPVLKQRMSEFLKDCAERIIILKIVHRRIINRFHSFLLFMGHPPYAIREVNINKFCRIISEFALEYRTTRERVLQQKQKRANHRERNKTRGKMITDSGKFSGSSPAPPSQPQGLSYAEDAAEHENMKAVLKTSSPSVEDATPALGVRTRSRASRGSTSSWTMGTDDSPNVTDDAADEIMDRIVKSATQVPSQRVVPRERKRSRANRKSLRRTLKSGLTPEEARALGLVGTSELQL
The following text describes a protein:
Function:
Together with PMI1, necessary for chloroplast and nuclear photorelocation movements via the regulation of chloroplast-actin (cp-actin) filaments in pavement cells.
Subcellular Localization:
Cytoplasm.
Sequence:
MSKVNSEESSSSQKLLKEVEKISEALYVNKNPRGSVAGSNKTPTKPLSRSNLAEPKEKKSFWNWPLRAINHVRNRRFNCCFSAQVHSIEGLPPIFQDLSLTVHWKRRDESLSTRPAKVSNGRAEFKDKLTHTCSVYGSRSGPHHSAKYEAKHFLLYVSLVGSPEIDLGKHRMDLTKLLPLTLEELQDEKSSGKWSTTFQLSGKANGATLSMSFGYTVVGDTRNPASSGSTQNFRSSSNVKQTSNNTGLTRAISAKSSLGNGKSASRRYDHSIVNRESHPLSQNMEEIKDLHEILPAVQSDLGSSVNTLYQKFDEEKVDPANESQFEFDVVTKHIEPVESISHEKEDANALQSELVTGNETVVPFEEIKKAGEVPTAGSDEVGAENFPLEEPLVNGNETDVPFELLKKAGEVPTAGRDEVGTEILPPEEPLVNGNETDVPFEELMITGEASIARSEEAVEIVTEELAPEEGNKISPKNEESVVPKDAEEVMNGEKDLKEMIMKDLESALKSVEMLEATASEDEEDRKKHGDKDKYFITPMKETVPSCSRDVAESVACEFLDMLGIEHSPFGLSSESEPESPRERLLREFEMETLAAGSLFDFSIEGDDPQLECDENFPNEYESDFEEGFDLASLVHDIEEEYQLEAQARVSHPRAKMLEGLETESLMREWGMNENTFQNSPPHNGRDAFHPADFPVKEPFDLPPLGDGLGPVVQTKNGGFLRSMNPLLFRNSKAGGSLIMQVSTPVVVPAEMGSGIMEILQKLATAGIEKLSMQANKVMPLDDITGKTMEEVLWETSPTIDIGDRDHVSERESGDASGFVRGGERRTSFAAKPKKFGSSSGNNNFDSEYVSLEDLAPLAMDQIEALSLEGLRIQSGMSDEDAPSDITAQSIGDISAFQGKSGCVGLEGAAGLQLLDIKDDGDDDDDGLMGLSLTLDEWMKLDSGDIGDEDEINERTSKILAAHHANPLNFIRKGSKGEKRKGKKGRKCGLLGNTFTVALMVQLRDPLRNYEPVGAPMLSLIQVERLFVPPKPKIYSTVSELKKTDEEEEADASDAKKEEKPMEEQGIPQYKITEVHLTGMKSETDKKPWGITTQQQQVQSGSRWLMANGMGKGNNKLPLMKPKLGSAKPGDKLWSVSGSGSKWKELGKMGKSNTHIRNPNVIMPK
The following text describes a protein:
Function:
Major capsid protein that self-associates to form hexamers, building most of the capsid in association with pentons made of the capsid vertex protein and one dodecamer of the portal protein. The major capsid protein self-associates to form 160 hexamers, building most of the T=13 laevo capsid. Folding of major capsid protein requires the assistance of two chaperones, the host chaperone groL acting with the phage encoded gp23-specific chaperone, gp31. The capsid also contains two nonessential outer capsid proteins, Hoc and Soc, which decorate the capsid surface. Through binding to adjacent gp23 subunits, Soc reinforces the capsid structure.
Subcellular Localization:
[Major capsid protein]: Virion. Note=Part of the capsid icosahedric shell of the immature virion. The capsid is made of 930 copies arranged as 160 hexamers; [Mature major capsid protein]: Virion. Note=Part of the icosahedric capsid shell of the mature virion.
Sequence:
MTIKTKAELLNKWKPLLEGEGLPEIANSKQAIIAKIFENQEKDFQTAPEYKDEKIAQAFGSFLTEAEIGGDHGYNATNIAAGQTSGAVTQIGPAVMGMVRRAIPNLIAFDICGVQPMNSPTGQVFALRAVYGKDPVAAGAKEAFHPMYGPDAMFSGQGAAKKFPALAASTQTTVGDIYTHFFQETGTVYLQASVQVTIDAGATDAAKLDAEIKKQMEAGALVEIAEGMATSIAELQEGFNGSTDNPWNEMGFRIDKQVIEAKSRQLKAAYSIELAQDLRAVHGMDADAELSGILATEIMLEINREVVDWINYSAQVGKSGMTLTPGSKAGVFDFQDPIDIRGARWAGESFKALLFQIDKEAVEIARQTGRGEGNFIIASRNVVNVLASVDTGISYAAQGLATGFSTDTTKSVFAGVLGGKYRVYIDQYAKQDYFTVGYKGPNEMDAGIYYAPYVALTPLRGSDPKNFQPVMGFKTRYGIGINPFAESAAQAPASRIQSGMPSILNSLGKNAYFRRVYVKGI
The following text describes a protein:
Function:
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Sequence:
MSVRELVVLGTASQVPTRHRNHNGYLLRWDGEGILFDPGEGTQRQMLRAGVAAHDLNRICVTHFHGDHSLGLAGVIQRINLDRVPHEITAHYPRSGQRFFERLRYATAYRETVALTEVPVAADGPLAVTPAYTLDARRLSHPVESYGYRLTEPDGRRMLPERLAAHGITGPDVGRIQRDGSLGGVALDEVSEVRRGQRFAFVMDTRLCEGVHALAEDSDLLVIESTFLDEDETLATDHGHLTAGQAARVARDAGVRHLVLTHFSQRYSDPEEFGRQARAAGYAGELTVARDLTRVPVPKRR
The following text describes a protein:
Function:
Accessory component of the proton-transporting vacuolar (V)-ATPase protein pump involved in intracellular iron homeostasis. In aerobic conditions, required for intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation. Necessary for endolysosomal acidification and lysosomal degradation (By similarity). May be involved in Golgi homeostasis (By similarity). Binds 20(S)-hydroxycholesterol (20(S)-OHC) (By similarity).
Subcellular Localization:
Cytoplasmic vesicle, COPI-coated vesicle membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Partial colocalization with GOLGB1.
Sequence:
MASSLLAGERLVRALDPGGELEREQLPRKLRAQLEAALGKKHAGSDNATGPRRLVSFRLIRDLHQHLRERNSMLYLHELLEGSEIYFPEIVKPPRNPELVARLEKIKIQLANEEYKRITRNVTCQDAQCGGTLSDLGKQVRSVKALVITIFNFIVTVAAAFVCTYLGSQYIFTEMASRVLAALIVASVVGLAELYVMVRAMEGELGEL
The following text describes a protein:
Function:
The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2.
Subcellular Localization:
Nucleus, nucleoplasm.
Sequence:
MANSLDRLREHLKNGDKLVLKNNEGQSTDDITKATMVETLSSDGSTQDSFPLNEETEIEIDGSLVQLRIIVHCWMNKDSSAADYLADCQNKQLTNVSFLQRTDLINWLSGNTESSQYLKAPGQKGETSDKVDIENKTLAGELSTVKSTTSASLENDSEVSDPVVVETMKHERILVDHNSALRGAKPINFGYLIKDAELKLVQSIKGSLRGSKLPPGHKGAHGRISKTNGSSGGPRKDPIILIPSAASSILTVANIKQFLLESKYVNPRNLPSVPNGLVNIEKNFERISRPIRFIIVDNTRMFTKPEYWDRVVAIFTTGHTWQFNNYQWNSPQELFQRCKGYYFHFAGDSVPQHVQQWNVEKVELDKNKRFKDVEVVRYFWHSLEKELISRGYR
The following text describes a protein:
Function:
Activates cdc-42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP (By similarity). May play a role in regulating the actin cytoskeleton and cell shape (By similarity). Required for normal lifespan.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MKYDMNHRKNSDDTPPASRTVKEMMAEFQNKLDDGDNRFRKQPPPPPSPRRAPPPPPHRKPASLSPPPDDENTIRPPSSSESSENIPEEPQELITPNTTRRSLGPKPTVAPKPLFLNGLLPSSSTSDVSSQNSPKCDPHPSCTTPTILVSPATSEYSNGVFFGANETNGSGVKDRARQLVNMGFVPRMQNGGTGTPSERPISQVSTLSQVSDEFDEGDTSASDEESMNSEKHLRRHRHEDDFDELPLPKNERKTTTVAATHSEIMNEMEHLFVRGGKKNNGVHKQQRRQSNIDEIPSDVGKLRDNRKGRHNSLFVSPTSGMSSSSTDDFSRITSMTSDRSSILTSHSGGEDSTDGASPVPDYETGDEKDDQRLKKLHYAAVEFLKVQNNYVQYLKEMAVLYPEYMERFGKRVGRDLLASHNGHENVVLQIKKIMVQILPIHEMLLKEIDKVCSNWDSRYPNMSKTIGTFADFLKCCQPFLDNKADFLNKLLQLRNEDKEFDEATYMFETEVFKRGKKGAVIQQLDQVHQNFMRYKLLMLRYSEYLIDDCDEKEKAQEAIQKLENVTQAVNQKMGLPTTEELTKLYYRFQCQFNVLEPGRVLIRQSEVMKQTRKELQPRYLVLFTDYLWICRVSSSGQFDINRSYRIPLEYMKFERMEEDERIRCLQIRSRVKSALIIFSSEKERNQWTDDLTKAQYDRKSYKRRQSTAVQRHDENKKKMNKLLMLTPEVPDASDLERPQLIDSRSRSMSCESQDELSSVPVTPLDNGEIDETLGFGEVTRNGSGKKPPSEMIKPVWLPDNISNECLMEGCSTEFNIINRRHHCRDCGWLICKFCKGQAPLSKYDFTKQNVCSECFDRHYKAYKDGVLFPSKNMIVQSDETILVKIGKRNDKEIVDPRKLFKAPVNYGFRHRNVEEKRAQSIVFGRVYLSFRSRKTETVRHALLRRDDLKLVFYKAELDSKSVLELLIYGYFYRETPLDDGWLFELVHRNQIRTDDTKDDVISFRVDNSASAKKWSAAFADKLELDPTRG
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MESGLAGASRGDGLLMKIKQEKPEWLLQTTVPQAALSEKDKENIFQQHRGLPPCQTMGKPRALGEQEETGGPRWTPPTEQDRRLAARAPGAAPGPLSPALSAVEGHFVCLDCGKRFSWWSSLKIHQRTHTGEKPYLCAKCGKSFSQKPNLARHQRHHTGERPFCCPDCARRFSQKQHLLKHQKTHSRPATLSCPECERCFRHQVGLRIHQRAHARDRQSARAGLHELLRDAAARRACRLRPGPPRARPEWAWLGLCQGWWRQPEARTAVPTAAGPGEQRQFICNECGKSFTWWSSLNIHQRIHTGERPYPCPECGRRFSQKPNLTRHLRNHTGERPHPCQLCGRSFRQKQHLLKHQRTHLPGAQAARCPSCGQSCPSPAALRAHQRAHAAAEAQLLCPGPAGLGAAPRSEPPVEAPPGLSAQPRSPQPALGPGGALWGRARAGLAVPGEQRQFICNECGKSFSWWSALTIHRRIHTGERPYPCPECGRRFSQKPNLTRHRRNHTGERPYLCAACGRGFSQKQHLLKHQRVHRGALAPTPGAKNEGL
The following text describes a protein:
Function:
Involved in the tetrapyrrole biosynthetic pathways leading to chlorophyll and bacteriochlorophyll (BChl). Catalyzes the anaerobic formation of the isocyclic ring (E-ring) in Mg-protoporphyrin monomethyl ester (MPE) to yield protochlorophyllide a (PChlide a) via a six-electron oxidation and the formation of an oxo group at position C13 using oxygen from a water molecule.
Sequence:
MRILFVHPNYHSGGAEIAGNWPPSWVPYLAGHLKKAGFDDIHFIDAMTLNVSHDELRKKFAELQPDLIGVTSITPSIYEAEETLKIAKEVVPNAVRVLGGVHATFMFRQVLSEAPWVDAIVRGEGEEIMVELAKCVSEGRWPEDRASIKGLAFHDGTEIVATQAAPTVKDIDSLKPDWSLIDWKHYIYIPLGVRVAIPNMARGCPFTCSFCSQWKFWRDYRVRSPKAVVDEIEDLVNNYDVGFFILADEEPTINKKKFVEFCQEMIDRGLNHKVKWGINTRVTDIYRDRDLLKFYREAGLVHISLGTEAAAQLKLDLFNKETTVAENKEAIRLLREADIFTEAQFIVGLDNETKETLEETFQMAWDWQPDLANWSMYTPWPFTPLFQELRDQVEVFDFSKYNFVTPIMKPKALTRGELLDGVMKNYRRFYMRKALFHYPWRGTGFRRRYLLGCLKAFLKAGVGRTFYDLGKAGYWGPQTKDTVDFHFDETRKIAEAQVADWEAAADRSRKHKERQEALRAQMKDRAADRNTANFVMPADAEDEFDLSAETHEARSAEHAAMACGGGKDQMVDAAE
The following text describes a protein:
Function:
Involved in resistance against the herbivorous insect brown planthopper (N.lugens, BPH). Member of the BPH3 (BPH resistance locus 3) cluster which contains LECRK1, LECRK2 and LECRK3.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MAPLLFLPILQLLLLYCTKSAQAQLNISIGSSLTPQGINNSWISPTADFAFGFLAVDGNSSSYLLAVWFNKIADKTVIWYAKTSSNRQDDTIPIQVQAGSILKLADGALSLRDPSGNEVWNPRVTDVGYARMLDTGNFRLLGTDGATKWESFGDPSDTILPTQVLPLGTALHSRLLATDYSNGRFQLNVQDDGNLVLYLVAVPSAYYHDPYWASNTVGNGSQLVFNETGRIYFTLTNGSQINITSAGVDSMGDFFHRATLDTDGVFRQYIYPKSKQARSLWQEQWRAVDALPENICQTIQTKVGSGACGFNSYCTFDGTKNTTNCLCPQRYKFFDNERTYKGCRPDFEPQSCDLDETAAMVQYEMTPIDRINWPLSDYEQYSPIDETECRRLCVIDCFCSVAVFNKPSNTCYKKKLPLSNGNMDSSLQATVLLKVPRSTNSPSMISSGSSKWKKDKKYWILGSSLFFGSSVLVNFLLIFVLLFGTYCSITSRKKTQLSQLPSNSGLPSKIFTYRELEKATGGFHEVLGTGASGIVYKGQLQDECGTNIAVKKIEKLQQEAQKEFLVEVQTIGQTFHRNLVRLLGFCNEGTEKLLVYEFMSNGSLNTFLFNDSHPHWSLRVQVALGVSRGLFYLHEECNKQIIHCDMKPQNILLDDNFVAKISDFGLAKLLPVNQTQTNTGIRGTRGYVAPEWFKNIGITSKVDVYSFGVILLELVCCRKNVELEVADEEQTILTYWANDCYRCGRIDLLVASDDEAIFNIKKVERFVAVALWCLQEEPSMRPTMHKVMQMLDGAVQIPTPPDPSSYISSLA
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. bL19m is essential for respiration.
Miscellaneous:
MISCELLANEOUS: Present with 4150 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1.
Sequence:
MWSRNVRLLGSWTRSYMVPATKRKTIPVYPPVQRIASSQIMKQVALSEIESLDPGAVKRKLISKKNKDRLKAGDVVRIVYDSSKCSYDTFVGYILSIDRKQLVQDASLLLRNQIAKTAVEIRVPLFSPLIERIDLLTPHVSSRQRNKHYYIRGTRLDVGDLEAGLRRKK
The following text describes a protein:
Function:
Inhibitor of the WG signaling pathway. Down-regulates beta-catenin (armadillo=ARM). Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B (zeste-white 3=ZW3).
Subcellular Localization:
Cytoplasm.
Sequence:
MSGHPSGIRKHDDNECSGPRPPVPGEESRVKKMTEGVADTSKNSSPSYLNWARTLNHLLEDRDGVELFKKYVEEEAPAYNDHLNFYFACEGLKQQTDPEKIKQIIGAIYRFLRKSQLSISDDLRAQIKAIKTNPEIPLSPHIFDPMQRHVEVTIRDNIYPTFLCSEMYILYIQQMSAQQERCTSSGATGSGSAGSSGSGGSSLAGACALPPTTASGKQQLPQLVPPGAFINLPVSSVSGPPAGTCSASGSVYGPSTSASSSGSISATDTLPRSSTLPTLHEDSVLSLCDDFEKVQMQEGGGSLGSGSVGAGARAPDYPIRLTRDLLIATQKRRLEIRPPGAHGYVYNPSTTNTSYVPNSRVDSERASVSSGGRTDSDTMSISSCSMDGRPYIQRRHSSTESKAIRQSAMANKETNTFQVIPRTQRLHSNEHRPLKEEELVSLLIPKLEEVKRKRDLEERARERNPGAALLTNERSSASDRAFAEAIREKFALDEDNDQDILDQHVSRVWKDQTPHRSPGTMSPCPPIPSRRRTATHDSGMVSDGAMSLSGHSMKHSKSMPDHSSCSRKLTNKWPSMNTDSGISMFSADTVTKYKDASSRSGSSTASKLEEAKRRLEDEPRRSRRYAQPPMQHLSQQPLASFSSSSSGGSISLPHQPPPLPAKPPETIVVFSFCEEPVPYRIKIPGTQPTLRQFKDYLPRRGHFRFFFKTHCEDPDSPVIQEEIVNDSDILPLFGDKAMGLVKPSD
The following text describes a protein:
Function:
Required for flagellar hook formation. May act as a scaffolding protein.
Sequence:
MSIAVTTTDPTNTGVSTTSSSSLTGSNAADLQSSFLTLLVAQLKNQDPTNPMENNELTSQLAQISTVSGIEKLNTTLGSISGQIDNSQSLQASNLIGHGVMIPGTTVLAGTGSEEGAVTTTTPFGVELQQAADKVTATITDKNGAVVRTIDIGELTAGVHSFTWDGTLTDGSTAPNGSYNVAISASNGGTQLVAQPLQFALVQGVIRGNSGNTLDLGTYGTTTLDEVRQII
The following text describes a protein:
Function:
Could be efficient in the degradation of transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions.
Subcellular Localization:
Periplasm.
Sequence:
MVKKTFFTTLAAVSFSAALETALFFSGCGSSLWTTKAHANSVFSSLMQQQGFADIVSQVKPAVVSVQVKSNKKKKEWFFSDFFSTPGFDQLPDQHPLKKFFQDFYNRDKPSNKSLQRSHRLRPIAFGSGFFISSDGYIVTNNHVISDGTSYAVVLDDGTELNAKLIGTDPRTDLAVLKVNEKRKFSYVDFGDDSKLRVGDWVVAIGNPFGLGGTVTAGIVSARGRDIGTGVYDDFIQIDAAVNRGNSGGPTFDLNGKVVGVNTAIFSPSGGNVGIAFAIPAATAKQVVQQLIEKGLVQRGWLGVQIQPVTKEISDSIGLKEAKGALITDPLKGPAAKAGIKAGDVIISVNGEKINDVRDLAKRIANMSPGETVTLGVWKSGKEENIKVKLDSMPEDENMKDGSKYSNEHGNSDETLEDYGLIVAPSDDGVGLVVTDVDPDSDAADKGIRPGDVIVTVNNKSVKKVSDITDTIKNAQKLGRKAILLQVRTNDQNRFVALPIFKK
The following text describes a protein:
Function:
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Has high alpha-isopropylmalate synthase activity and low citramalate synthase activity.
Miscellaneous:
MISCELLANEOUS: Is missing the C-terminal regulatory domain compared to orthologs.
Subcellular Localization:
Cytoplasm.
Sequence:
MKQDSQSENESIVCDLSVSEDQRNVKFFSDLQTPIPKHLPFFMDVTLRDGNQALRRPWNLEQKETIFKQLLKLGVQGIEVGFASSNNQEFEACKYLSSIAPDNVVISSLSRAVEKEIEVSWKAIRFAPKPRIHIVYPVSAFTIQNVLKISPEKVLDRISQSVAYAKSLVGSKGEVQFSGEHFGDSLENLDFAAEAFQIALNNGADVVNLPNTVERYRPWLFVSMVKAVANLLPEDTRISIHTHNDLGMATATTVESYFAGAVQLETALNGLGERAGNTNTYEVAIALHNCGVEVPLNFSTIYETSRLVSYLSEIPIYEKAPLIGEDVISHRSGIHQDGVAKTRHLQKGAYRAFDAALIGRPEGDRIEFTNQSGKSAVYCILKDAGENITLEEAGRLQPILKKISEDLGRRELTLEEIRIEWNRLLRAI