lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
Domain:
The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence:
MSLETFPYGDHDLQTVTVAKPYPARAPLHAENIDNESGYWVILIHGGAWRDPTQTSTSYLAPTLSILSSSESKSPKSQSQHIRGLASISYRLSPHPSHSQDASTTMESHLRNAKHPEHINDIQLALSFLQRKYRFGKRYILVGHSCGATLAFQAVMASLSVQGREGLVNDYIAPLAILGMAGIYNLRLLRDSHRDISAYQEFIEGAFGKDEKVWDAASPGVVRGVNGVEGWKEGRLVVLAHSKEDELCDMEQSEKMKEFLDGWKGNDQKRLVQFLDIKGRHDEVWENGEELARGILFTIEELQSLRE
The following text describes a protein:
Function:
Catalyzes the reversible hydration of fumarate to (S)-malate. Functions in the generation of fumarate for use as an anaerobic electron acceptor. To a lesser extent, also displays D-tartrate dehydratase activity, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Is required for anaerobic growth on D-tartrate.
Sequence:
MSNKPFIYQAPFPMGKDNTEYYLLTSDYVSVADFDGETILKVEPEALTLLAQQAFHDASFMLRPAHQKQVAAILHDPEASENDKYVALQFLRNSEIAAKGVLPTCQDTGTAIIVGKKGQRVWTGGGDEETLSKGVYNTYIEDNLRYSQNAALDMYKEVNTGTNLPAQIDLYAVDGDEYKFLCVAKGGGSANKTYLYQETKALLTPGKLKNFLVEKMRTLGTAACPPYHIAFVIGGTSAETNLKTVKLASAHYYDELPTEGNEHGQAFRDVQLEQELLEEAQKLGLGAQFGGKYFAHDIRVIRLPRHGASCPVGMGVSCSADRNIKAKINREGIWIEKLEHNPGQYIPQELRQAGEGEAVKVDLNRPMKEILAQLSQYPVSTRLSLTGTIIVGRDIAHAKLKELIDAGKELPQYIKDHPIYYAGPAKTPAGYPSGSLGPTTAGRMDSYVDLLQSHGGSMIMLAKGNRSQQVTDACHKHGGFYLGSIGGPAAVLAQQSIKHLECVAYPELGMEAIWKIEVEDFPAFILVDDKGNDFFQQIVNKQCANCTK
The following text describes a protein:
Function:
Forms chloride channels.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane.
Sequence:
MLPLLLLAATAVTTAELQGNNAQIGWMAGKWRSEFSGKIFWPTVPTMTFGEELYILEAPSARSASLQFLNFSARAWSHSTKDHFHDEWGFLTVDATGNATLMTAGNNGFTTYEVGTVEPNKLVLTLKDIGRISFSRDLPVEDLRRTFIRHDDRYMEQILEMRTATHPKSGYLEHTRVIYTRKKEGRGMTVPYTRDIASASYWASTRLLFRWRGSIWKSVLPEFSAWMAIFYGFLTAFYIGEFNFALTVNAFIRGDNRIVKLARQTVIRHAILAQILIYRDVSISVRKRFPSLESLIDAGYLKRDELKLLERSSNQYNIFHVPFVWITTLLSKLRLDGHILSDPTFVNLITEMKEFRRKLETVFNYDCVPIPLAYPQIVSVAVRMHVIVNMIGKLFIFSRKDGIWKLNGNFGLVNGPEIFVFLAWLKVAEILANPLGEDDDDLELNHIIDRNYFISRSIIEIHDQCPILEETEMNPTPKYDEHAKNLGGASHRLMGSAVGSKVDVGRMVEVEPTHKPELRHRVCIPDLLGSFTDKGMDDKMALVEHAEDMGRTSSLLKIRYFNIALDNLTVFCVEVPSIYDQRSLRSLTQEEICERYGGDRRLETSLIDMSDPSPLSASRLATSSNIAYDNNSCRL
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:
MASRALLSSVITAMLFVMIFSRRSTRLPSFQHMSQNAICVSRSHHSYMMKPSRVLSVPPAFSSALAEYEKMHSKCYHSLKQSITNPAAGGSCKYLVHYELDGLGNRLLGLVSTFVFSLLTNRVLLIDPKGQSAKLLCEPFANSSWLVPQEFPHFHLDQAQSLEKAVQSKKFGSMVHVWVASLHRDQDIFHHQVRSKLKNVTWISLTSNLYFVPRLFTFPEFWKPLMSLFPDVRMAFTHLTRYLLLPQDHVWEKIVRFDSTYLSGPGKQLGIQIRLHHRDDPGEFDQRSFDRILECLIGKEFLPMMMNSTTEIISAHPPKRIKVFVASLQGRYFQELKQMYLKYPSVDGSLVQIYTFSQEGVQNESIQQATNALAEMWLLGFSDVLVTSSSSTFGYIAQGIAGVRPYVLHIRPEDLKNCSLPACSRRLSPAPCNHQPYFEEEENLERSTEHLQWMNVHIRRCQDNWHGVQIV
The following text describes a protein:
Function:
Mitochondrial protein involved in the maturation of mitochondrial [4Fe-4S]-proteins in the late stage of the iron-sulfur cluster assembly pathway. Operates in cooperation with ISCA2 in the maturation of [4Fe-4S] proteins; Involved in the maturation of mitochondrial 2Fe-2S proteins in the late stage of the iron-sulfur cluster assembly pathway.
Subcellular Localization:
Mitochondrion.
Sequence:
MATAALLRGATPGRGGPVWRWRLRAAPRCRLAHSSCSPGGDPTAGAAWACFRLDGRTLLRVRGPDAAPFLLGLLTNELPLPSPAAAGAPPAARAGYAHFLNVQGRTLYDVILYGLQEHSEVSGFLLECDSSVQGALQKHLALYRIRRKVTVEPHPELRVWAVLPSSPEACGAASLQERAGAAAILIRDPRTARMGWRLLTQDEGPALVPGGRLGDLWDYHQHRYLQGVPEGVRDLPPGVALPLESNLAFMNGVSFTKGCYIGQELTARTHHMGVIRKRLFPVRFLDPLPTSGITPGATVLTASGQTVGKFRAGQGNVGLALLWSEKIKGPLHIRASEGAQVALAASVPDWWPTVSK
The following text describes a protein:
Function:
Converts proline to delta-1-pyrroline-5-carboxylate.
Sequence:
MFERLMKMTFYGHFVAGEDQESIRPLIRHNKAFGVGFILDYGVEEDLSPEEAERKEMESCTSEAERDGSGANKREKQYQVHPAFGDRRDGVISARTYFYASEAKCDNYMENLLQCIEASGGASDGGFSAIKLTALGRPQFLLQFSDVLTRWRQFFHQMAAEQGQAGRPAVDTKLEVAVLQESIAKMGISSRAEIERWFTPETLGVSGTVDLLDWNSLIDSRTQLSRHLVVPNVQRAREAGVRLMIDAEQSYFQPAISRLTLEMQRRFNVDKPFIFNTFQCYLKDAYDNVTIDMELSRREGWCFGAKLVRGAYMAQERARAVEIGYEDPINPTYEATNAMYHRCLNYVLEELKHSTKAEVMVASHNEDTVSFTLCRMKELGLHPADGQVCFGQLLGMCDQISFPLGQAGFPVYKYVPYGPVMEVLPYLSRRALENSSIMKGAQRERQLLWQELCRRLRTGSLFHHPA
The following text describes a protein:
Function:
Required for the assembly and the contraction of the actomyosin ring at the bud neck during cytokinesis. Seems to be involved in additional tasks during cell division like axial bud-site selection and targeted secretion by recruiting the spatial landmark BUD4, the septin CDC12 and the secretion landmark SEC3 to the bud neck. May be regulated by calcium ions.
Miscellaneous:
MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
Subcellular Localization:
Bud neck. Note=Forms a ring at the bud neck in a MLC1-dependent manner, which contracts at the end of cytokinesis.
Domain:
The calponin homology (CH) domain binds to actin filaments and is required for their recruitment to the bud neck; The IQ domains provide the interaction surface for the myosin light chain MLC1; The Ras-GAP domain is required for contraction of the actomyosin ring and is needed for the interaction with TEM1. It probably does not stimulate GTPase activity.
Sequence:
MTAYSGSPSKPGNNNSYLNRYVENLGTNVTPPLRPQSSSKINSSLNIASPSHLKTKTSASNSSATILSKKVESSVSKLKPSLPNKLVGKYTVDLSNYSKIELRYYEFLCRVSEVKIWIEAVIEEALPSEIELCVGDSLRNGVFLAKLTQRINPDLTTVIFPAGDKLQFKHTQNINAFFGLVEHVGVPDSFRFELQDLYNKKNIPQVFETLHILISMINKKWPGKTPALTNVSGQISFTKEEIAACKKAWPRIRDFKSLGTNINTAPASPEEPKEKRSGLIKDFNKFERPNIPVEEILITPRKNITDANCSDFSNTPSPYNEAPKMSNLDVVVEKRKFTPIEPSLLGPTPSLEYSPIKNKSLSYYSPTISKYLTYDTEFYTRRSRAREEDLNYYQTFKYSPSHYSPMRRERMTEEQFLEKVVQLQNICRGVNTRFNLYIQKRLLNLFEQDILRFQACLRGNKFRVLSSMYLPIRRAKIDVPHVEAIQSRIKGSRIRYKYDKLKFTLSRFSCTVELLQAYCRSKLLKTTVNTKLNDIEISHYPLTKLQSYMRASYVRKKVMSLNTKLNDERESIMKFSAIIRGNVVRCSEDAILSAVHDVHKENISKLQSLIRGIFTRSCLASIIYSLGKENCNIIQLSACIRGNAVRHKVQSLFAPENNLSETVHDLQGLVRGILVRYTLDLVDDIVEYNNLALFQAFSRGALVRESLDQKSSFYKRNVRSVIMIQSWIRKSLQRSAYLELLDCPNPSLWAVKKFVHLLNGTATIEEVQNQLESCQASLDSENMKKERLLKSIRQQLNINGVLDKFGLLKDKDHELGISDSTIPKSKYQKYEKLFYMLQVDPSYWKLLYLKEPEFVAKNVYMTFGTVNQRMNDRERSYFTRFVCEMLQNAINEAPSIESFLDNRSQFWQTILQDFLRRESPEFFSIIVPVLDYLSDPVVDFESDPYKIYQEIHGFSSPQHCSPVDDASTKNKFIDNLRCLWHAIEMVAEIYTRKVHTIPVEIRYLCTKIFCYAADKNIEEIDSLRAISSILVNVFVSEYLVNREYYGYKDSNVQKNNQKIDILMKSLATVFEIKNFDGFLDPLNQYANEIKPHIKDVLYNVLVDPEYEQEGDRLIYLDMVSPSPKLELLTEKVLEISGKFEEYLNEFPEADILHDILEKNLDNSSFPRSGRVTLELDASAYRFLVSDDKMRKIYDQVKRAFVYMMQIEDVDTNLYDLSISTILPQDEPNFANFLEQNPKIRDDPMIQKLKPLKYFTLKNVTLKKIHELESTGTFCSSDNKLQNFLNDIANTIKNPNYAIDYVTQEIYITKETLTKISEMNHSLDIELSRLKKHVDHTIKDFQKAKDFSPVHKSKFGNFKNAVKKVQGRERSELQGMKFKWNTKQLYERGVLKTIRGEKLAELTVKVFGSSGPKFPDIIFKISTSDGSRFGIQMIDKRKGPDKRYSDDVDSFSFKDLIKTQVEPKIETWKLFHSNVVVNNSQLLHLIVSFFYKRNAL
The following text describes a protein:
Function:
Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts (By similarity).
Subcellular Localization:
Endomembrane system; Peripheral membrane protein. Cytoplasm, cytoskeleton.
Domain:
The CRIB domain mediates interaction with CDC42.
Sequence:
MPGPQGGTGAPTMSLGKLSPVGWVSSSHGKRRLTADMISPPLGDFRHTMHVGRGGDVFGDTSFLSNHGGRSGNTHRSPRSFLARKLQQVRRVGVPPRRMASPAAPSPAPPPISPIIKNAISLPQLNQATYDSLVMGKLSFDSTPASSTDGHSGYGLESGFCTISRLPRVEKHSNRDRDRDPDHSQDREQSSFPSEPTPNPELRRSDSLLSFRFDLDLGPSLLSELLGVMSLSEAPAAETPVPTANPPAPAANPAPTAKPPAHAITTLDAVTSLPASAVTSLPAPAAASSPSRGHFPNGVTSVLGPAAEAKPSPVGEGPQVPSNMTFDRHGASWGASRASWGASRASRHYTEMDARRELAGVLPQVHGSWESLNEDWSTPPASVRAPVPTSVQVNAFEFADAEEDDEVKV
The following text describes a protein:
Function:
Nicotinic acid adenine dinucleotide phosphate (NAADP) binding protein.
Subcellular Localization:
Cytoplasm.
Sequence:
MAAPGECFSVGSQVSCRTCQEQRLQGEVVAFDYPSKMLALKCPSSSGKPNHADILLVNLQYVSEVEIINDRTETPPPLASLNVSKLANKARMEKEEKLSQAYAISAGVSLEGQQLFQTIHKTIKDCKWQEKNIVVMEEVVIAPPYQVENCKGKEGSALGHVRKIVEKHFRDVESQKVMQRSQAQQTQKESALSS
The following text describes a protein:
Function:
Negative regulator of brassinosteroid signaling. When associated to the membrane, limits the interaction of BRI1 with BAK1 by binding to the kinase-inactive form of BRI1.
Miscellaneous:
MISCELLANEOUS: BRI1 is not required for BKI1 association with the plasma membrane, but the BRI1 kinase activity is necessary for the membrane release.
Subcellular Localization:
Cell membrane. Cytoplasm. Note=Once phosphorylated following brassinosteroid treatment, displaced from the plasma membrane into the cytosol where it is inactive.
Domain:
The c-terminal part (253-337) is necessary and sufficient for the interaction with BRI1.
Sequence:
METNLQQVKNSSQTFSEKQNPKQEASPSPISSTCSSPSHDFSFTISLQPLSSSSKHISPTLRSPSKTTSSYQQTDPFAVDLSPADEIFFHGHLLPLHLLSHLPVSPRTSTGSYNDGFTLPVKDILPDQPTNNNNNTENAITNISTEAKDDNTEDKAEGEIRVKTKPIKSFSLFGLSKWRKGFESNEREQEQQQQKIKKPMSLDLSHAVKKYIRMLFQKRGNGTQFWNRRQTSSYSFSSSLMGPNGNSKTMINGSYNKRDLIRGRRGELFSAPASMRTSPTNSGHLRVSTAGLSSSSGSTSSSSSDSTMEELQAAIQAAIAHCKNSSAVDRDDKVKDS
The following text describes a protein:
Function:
Transcription factor that binds to the DNA sequence 5'-CANNTG-3'(E box) and the G-box motif. May play an important role in the regulation of cell proliferation and differentiation during spermatogenesis (By similarity).
Miscellaneous:
MISCELLANEOUS: The helix-loop-helix and basic motifs form a SPZ1 specific bHLH different from the classical one.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MADSDSSSEMPAHSPSPSPIPCAKQKPPNTGITISLLEIGSLPTFCCSSFSEPNNNMCPIRKQGKVQKFSNLLKDVKDVLKNIAGFEEKTTDGDPFDDTYIPEDLSELNIRGFDKRNKLRFKDDLFIHFDPERENTMRQEMLFKSHSAKNMVQKFARDLCNSEEKRGCDGVQLNAKRRRTGSVHIRGEYRKLRNNMEQLLQEADHWSKQHNELSELMRSYQECHKEIKDIVDCSRVCSQTQNNNEVPSKQKLEEQVKKLSQDTHSLHLIAALLENECQILQQRVDILRELHLHEAGPGHEKPLQTSGEQDKKCGEQDKKCGEQDKKCGEQDKKCPKLAEAEKMDGSKHTMKTTEGTITRKPKIFRCPNDCLTKKARNNRFNARVAKKSLVGKRRTISSFR
The following text describes a protein:
Function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Sequence:
MHPLTLNIASEETTEARVFHVIENFGNSFCIDLLKKMLLIREFEIRGEEAYLEGLVGGFYHSYIGQEAVATAAIACTGKDHWFFSSYRCHGVALLLDIPLRQLAAELLGKETGCALGRGGSMHMCGDRLPGGFGIVGGQIPLAAGAAFSMKYQNSSSISMCFIGDGAVAQGVFHETLNFVALHSLPLMLIIENNGWSMGTALHRAIAKQPIAESQAISYGLSSITLNGFDLFNSLIGFREAYHHMQQTGSPIIVEALCSRFRGHSISDPNLYRSKEEMQCLLKRDPILFAKEWLIRANVLSEDDFKDLRQTSKTAVLEAVAQARLDPEPAVATLEEGVYA
The following text describes a protein:
Function:
Anti-apoptotic protein which functions as a caspase regulator, using its E3 ubiquitin-protein ligase activity to smother caspase activity. Binds, ubiquitinates and inactivates initiator caspase Dronc, and effector caspases Drice and Dcp-1. Acts as a Nedd8-E3 ubiquitin-protein ligase for Drice. Suppresses apoptosis by targeting the apoptosome for ubiquitination and inactivation. Plays an important role in cell motility. Overexpression suppresses rpr and hid-dependent cell death in the eye. Interaction of Diap1 with Dronc is required to suppress Dronc-mediated cell death through Diap1-mediated ubiquitination of Dronc. Acts as a positive regulator of Wnt signaling.
Sequence:
MASVVADLPSYGPIAFDQVDNNTNATQLFKNNINKTRMNDLNREETRLKTFTDWPLDWLDKRQLAQTGMYFTHAGDKVKCFFCGVEIGCWEQEDQPVPEHQRWSPNCPLLRRRTTNNVPINAEALDRILPPISYDICGANDSTLEMREHAYAEGVIPMSQLIQSIGMNAVNAAGSVTGTAAPQPRVTVATHASTATQATGDVQPETCRPSAASGNYFPQYPEYAIETARLRTFEAWPRNLKQKPHQLAEAGFFYTGVGDRVRCFSCGGGLMDWNDNDEPWEQHALWLSQCRFVKLMKGQLYIDTVAAKPVLAEEKEESSSIGGVAVASTQASEEEQQTSLSSEEAVSGDVAPSVAPTAATRIFNKIVEATAVATPSTNSSGSTSIPEEKLCKICYGAEYNTAFLPCGHVVACAKCASSVTKCPLCRKPFTDVMRVYFS
The following text describes a protein:
Function:
Salivary chemokine-binding protein which binds to host chemokine CCL2.
Subcellular Localization:
Secreted.
Sequence:
MTRNWSFRVIFVSAMWCALLKFATLEAPKDDFEYDGGCPFVVLDNGTHVKPAGCSHLCNGAPETLDNIECYNVTEEVAKRMTPGIPYACWLGWCSKGECKRDNRTEVCYRGSEEE
The following text describes a protein:
Function:
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Peripheral membrane protein.
Sequence:
MSCSHLSTAWSSSALASSSTRRRGASSSSSSSLVVRCSLRDLRNRIESVRNTQKITEAMKLVAAAKVRRAQEAVVSSRPFSEALVEVLYNMNQEIQTEDIDLPLTRQRSVKRVALVVLTGERGLCGAFNNNVLKKAESRMEELRQLGVEYTVISVGKKGNAYFQRRPYIPSERFLELAGIPTVKDSQAICDLVYSLFVAEEVDKVELLYSKFVSLVRSDPIIQTLLPMSPKGEICDVNGICVDATEDELFKLTTKEGKLTVEREKIKIETQPFSPVVQFEQDPVQILDALLPLYLNSQILRALQESLASELAARMSAMSSATDNAIDLRKNLSIIYNRRRQAKITGEILEIVAGADALSG
The following text describes a protein:
Function:
Modulates negatively AKT-mediated GSK3B signaling. Induces CTNNB1 'Ser-33' phosphorylation and degradation through the suppression of the inhibitory 'Ser-9' phosphorylation of GSK3B, which represses the function of the APC:CTNNB1:GSK3B complex and the interaction with CDH1/E-cadherin in adherent junctions. Plays a role in the regulation of cell cycle and cell adhesion. Has an inhibitory role on AR-signaling pathway through the induction of receptor proteasomal degradation.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MTTTTTFKGVDPNSRNSSRVLRPPGGGSNFSLGFDEPTEQPVRKNKMASNIFGTPEENQASWAKSAGAKSSGGREDLESSGLQRRNSSEASSGDFLDLKGEGDIHENVDTDLPGSLGQSEEKPVPAAPVPSPVAPAPVPSRRNPPGGKSSLVLG
The following text describes a protein:
Function:
NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. Stimulates promoter activity in the presence of p49- and p50-NF-kappa-B. Neither associates with DNA nor with p65-NF-kappa-B. May play a role in the regulation of the circadian clock (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MFAPSLAAFRAMALPIPRLAPVMKSVQPASFPVLGSMAARLSTARGGRGLRAGRRPPGGPKGAAAAEEMAVPIGAALQDPNVGMAPVNDDLEIIEEVMKEDGFQPDPPPPGSPHDPPKLIPRGLGVPVGRRDPPRDPPRLIITEQPKKTGMRFRYECEGRSAGSILGESSTEASKTLPAIELLNCQAIPEVQVTACLVWKDWPHRVHPHGLVGKDCSNGLCQVRLQPHANPRHSFSNLGIQCVKKKEIEAAIEKKLQLGIDPFKAGSLKNHQEVDMNVVRICFQASYRDGSGRTRQLSPVLSEPIFDKKSTNTSELRICRMNKESGPCTGGEELYLLCDKVQKEDIAVVFRKEPWEARADFSQADVHRQGAIVLRTPPYRCVQLSEPVQVEVFLQRLTDRARSRGCPYTYLPRERDAYGVKVKRKRGMPDLLEELSGADPYGIEAKRRKPPPGFMDHFAPLPAADEAFALLADPLDPLSHLPPPSTPQILWGRSYFRTPPPTETPTPPTASWGPICSQGTSEGGGGRTSPRYRPPPPLKWGSQWAPPHQ
The following text describes a protein:
Function:
Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. The pattern of activities varies according to subcellular location, PGP phosphatase activity is higher in the cytoplasmic membrane, whereas PA and LPA phosphatase activities are higher in the outer membrane. Activity is independent of a divalent cation ion and insensitive to inhibition by N-ethylmaleimide (By similarity).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell outer membrane; Multi-pass membrane protein.
Sequence:
MFKRLSLYTLLLCLVPFFIWGISYQWHGNSQLTQADYWLYLLTETGSVPYALITCVLFTLLFAFLFKNPKQWILGVIVMGISVIATQAAKTGAKALFEEPRPFTVYLAEQTHSTPENFYKNDRTLRAEIAKNFYSMDAITPAWLVHHYENETGYSFPSGHTIFAATWLMLAVGFTQLLGNRSFKAKLLVVGIAVWGLLMLISRVRLGMHYPIDLLVATLLAWLINSIIFAFLKKKAIFVMK
The following text describes a protein:
Function:
Component of the ribosome.
Sequence:
MSLHWSNYQKSKTSDPIELVVWLPQLCRRQEVPFCFIKNKARLGALVHQKTATCVALTDVRKEDQAEFDNLARDLRQHYNENHELLRTIGGGQVGIKSKHQYGGYQESF
The following text describes a protein:
Function:
Catalyzes the synthesis of dihydrouridine, a modified base, in various RNAs, such as tRNAs, mRNAs and some long non-coding RNAs (lncRNAs). Mainly modifies the uridine in position 47 (U47) in the D-loop of most cytoplasmic tRNAs. Also able to mediate the formation of dihydrouridine in some mRNAs, thereby regulating their translation.
Sequence:
MSESTEIQIKKEKDVEELEVKEESEINPIQIKKESEIDPIQIKKESAIDPIQIKKESAIDPNELQIKKEYVLSIRERVLCTDLLSAKDRVLIDGADNSKSKENDTDTIVKEDLKLISVKLKGQNKNRPPPMRFDITERICPSLVDVAEGEEPKVCPYNPTCRYRHDVVEYMKERKPDMLPGGCPNYQSSGRCSRGISCLFGDEHVTPEGKNKINPNPTRPGSEYFNFLSKDLQKSLRKKTYNFKKAESFAKKNNKDQGNSNNKDKKEKITEENGESINVNAVALKVESNTEKIIGPITNEDIITLKTEEKKKIDWRGKLYLAPLTTVGNLPFRRLCKALGADITCGEMAMAETLVGGGQQEWALVRKHKSEDLFGVQICGANPYILGKCSQLLEENTEIDFIDLNLGCPIDMVYQKGAGSGLMRRKGPLESSIKTMSQLLKIPFTVKMRMGVYTDHPFAHQLVEKCRDWGVSMVTVHGRSREQRYTRLADWDYIGNCVKAADPMPIFGNGDLMSYEDYERVVDQSGAAGVMIARGALIKPWIFTEIKERRHWDISSSERFQYMKDFCNYGLEHWGSDSQGVERTRRFLLEWQSFAHRYVPVGLLERPPQKMNLRPPPFRGRDDLETLLGSPNAGDWVRICEMFLGPAPDGFQFLPKHKANSWK
The following text describes a protein:
Function:
Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MQKQAIFQSKLLPYALVAPQLAIVLIFFYWPALQAVIQSFLLQDAFGLSSTFVWFDNYIELFRDPAYFEAIVRTFFFSFAIAVSSLSFALLLAVMADKPLRGSMLYRTLLIWPYAVAPPVVGVLWIFMLHPSLGVLSRYLRSLGVDWNPLLDGNQAAALIILAAAWKQISYNFLFFLAGLQAIPKSVLEAAAIDGARPMRRFWTVTFPLLSPTIFFLLVVNIVYAFFDTFGIIDTMTRGGPGTSTVTLVYKVYSDGLLGGNLGSSAAQSVILMVMVIVLTGIQFRFVERKVTY
The following text describes a protein:
Function:
Represses expression of Rv2025c and its own expression. Acts by binding to the promoter regions.
Miscellaneous:
MISCELLANEOUS: KmtR has tighter affinities for nickel and cobalt than NmtR.
Sequence:
MYADSGPDPLPDDQVCLVVEVFRMLADATRVQVLWSLADREMSVNELAEQVGKPAPSVSQHLAKLRMARLVRTRRDGTTIFYRLENEHVRQLVIDAVFNAEHAGPGIPRHHRAAGGLQSVAKASATKDVG
The following text describes a protein:
Function:
May act as a component of the auxin efflux carrier.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MISLADVYHVIAATVPLYFAMILAYVSVKWWKLFTPEQCAGINKFVAKFSIPLLSFQVISENNPYKMNLKLILADFLQKLLAFLVLFALTKLSSRGGLSSIITGLSLSTMPNTLILGIPLLRAMYGDKSATLLAQIVVLQSLIWYNLLLFLFELNATKAASEITVAVSQASGDEEAPEEAQGKEGGEETQTRARKSKTMLIFLTVGKKLVANPNTHATLLGLIWASIQFRWNIKFPAIVEKSIAILSSGGLGMAMFSLGLFMASRPSIIACGIRMAAVAMIMKFIAGPALMAAASATLGLKGKLLRVAIVQAALPQGIVPFVFAKEYNVHPDILSTGVIFGMLIALPVALVYYLLLAL
The following text describes a protein:
Function:
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane.
Sequence:
MPLRMLSRFWGQLNNLDLPYWLRRPTFYLYVWMFNCRPDEVIVQDFSRYKNLSEFFRRLLKPGLRPIDKAVLTSPVDGRVLHCGRVQNGTLEQVKGVTYSLSGFLGPLNFNVVNHSNFEKLNYFGQMRKKSVRPDSSVNESDAFINGQLIEGKHKSDVIDADDDVVDNNIDDEERKAKANSSNDENEIKSVSKSDDKHLSQYNFDINNINNNKIGINSTPFKSSNMNKAPPLLCDPTMNGLFYCVIYLAPGDYHRFHSPADWFVQMRRHFPGELFSVKPSVAHWLKGLFNMNERVVYFGRWAHGFFSMSPVGATNVGSICVYIDKSLKTNVYRNNKLLIHYDKSFINNKNNDDDDKNNNSTSGKNDSNVNNTIDVKSIDPRLSQIHQQPQQPQPHQPQQPQQQKQQPQGIYLKKGKLFGEFNLGSTIVLLFEAPNNFRFAVVPGQKIQYGQAISVE
The following text describes a protein:
Function:
Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Mainly present in the nucleus and part in the cytoplasm.
Domain:
The PHD-type zinc-finger domain is required for interaction with LRSAM1 and negative regulation of autophagy.
Sequence:
MLEAMAEPSPEDPPPTLKPETQPPEKRRRTIEDFNKFCSFVLAYAGYIPPSKGAPDSATLLEKMKLKDSLFDLDGPKVASPLSPTSLTSRPPAALTPVPLSQGDLSQPRKKDRKNRKLGPGGGAGFGVLRRPRPAPGDGEKRSRIKKSKKRKLKKADRGDRLPPPGPPRAPPSDTDSEEEEEEEEEEDDEEETTVVGGGGVPAPVLPTPPEAPRPPVTVHPEGAPPTDSEGKDAGSTETSQDGDGSSSEGEMRVMDEDIMVESGDDSWDLITCYCRKPFAGRPMIECSLCGTWIHLSCAKIKKTNVPDFFYCQKCKELRPEARRLGGLPKSGEP
The following text describes a protein:
Function:
Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins.
Sequence:
MMSSNLLVCILLAIALSTQLIVKAFIVGKASGFAAGTTGGGSIESVYPQNLQELETFLGDDEPRVIILNKEFDFLGSNGTTTEQGCRPKIMEQCIAENNGFKGQDVILREGDTTFTQTGGCDQAVGVEVTYDNAAKNPLVVKGNKTLRGIGQAGVVKGRGLWLNGDNIIIQNIHITELNPQYVWGGDAIYLQGTESGPMKNIWLDHIKISRIGRQMLVIAFGGAESLTISNSDFDGRTDWSSSCDGRHYWAFIIGGEPTHITFVNNFVHSTSGRSPKIISEMGTNPIVVGHIVNNYWADNSGHSFEPGLNAFVLAEGNLIQDTAQPILADDKATIFTAADSNDCTSYLGRACVANVLENSGALDSVNGERAMETVKEFKEISSYAPGAAMKLSVNLENFGVGLLQGTTTEQTQESVTQEEVVQDYGQSESVLRSSTCKAKRRT
The following text describes a protein:
Function:
Secreted enzyme that regulates the endogenous N-fatty acyl amino acid (NAAs) tissue and circulating levels by functioning as a bidirectional NAA synthase/hydrolase. It condenses free fatty acids and free amino acids to generate NAAs and bidirectionally catalyzes the reverse hydrolysis reaction. Some of these NAAs stimulate oxidative metabolism via mitochondrial uncoupling, increasing energy expenditure in a UPC1-independent manner. Thereby, this secreted protein may indirectly regulate whole body energy expenditure. PM20D1 circulates in tight association with both low- and high-density (LDL and HDL,respectively) lipoprotein particles.
Sequence:
MAFRIINILLASFLALALILVIRTLVFTLNRKVEDPCLSTDEDFITADSSALERFSQALRYRTVAWGPGDYNRTELLKFKEFILREFSYVFHHPLVTFEVINNYSLLIQVHGSNSTLRPYMIASHLDVVPAPGSWDVPPFDGRVKDGYIWGRGTLDVKNGVMASLEAVQALLKLGQKPKRSFYLAYGHDEEVQGADGARNIGMLLKARNIKLEFIVDEGMVIVKNVFPGLTTPYAIIGVAEKGYMMVELSVHTSGGHASMPPKESSIGILSKAIASVLGETPSTNSMIRTTTAVTMFKAGVKGNVIAPDATATVNHRVHPENTIGEVVEHDRKCIGDNRVHLRVTASQDPSPVSSWDSHAIGYQAIAQSVRQVFPGVGVAPGLMIANTDTKHYLHLTDAVYRFTPSLLEPSDLKRIHGVNERIGVKNYEQTINYYYHLIRNTDLVHSRDRLKSEL