lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular Localization:
Bacterial flagellum basal body.
Sequence:
MNATTALQRCRFGLVWITLSLTAAGGCTSFWKRDQNDPSNNPKLAKLLKVPDPPDLIREAAIPHGMQSVRVNGVAIVNALPDSGGPALPSTFRDMLLEEMKRKEIPNPNDFLELNTTALVQVLGTIPPGSRRGDTIDLEILTPTKTEATDLHGGWLLDTRLRHQKVLDSAVRSSDVLAVGTGPVLTRGDHEGEADGALRVQGTVLSGGVVQNDRKLGLVLRPDFQHVKMSAAIAQAINHRFYFFDGSTRRGIAEPIEDDFIQLDVHPRYRNSVSRLMAVIRAIGVAPESSNTQVRLTELGERMKLPAKAADAALQLEGLGEPAIPTLLDAVQSSNPELRFYAAEALAYLDREEAVDPLIAAIRAEPAFRAPALKALEDMQHHNVVEGLQRLMDSPSLETRYGGFSTLRNREDGRQKLAGQNLRGTYRLYQVASTAKPAVVVSLRRNPEIVLFGDVQPLQIETFFLGPSGIMIRSVPETGQLRISRFQAGKDDAFAEVDNTLAGMLEGLTEVGGGYGDAVALLRMAKTQGILPDQLAFDPLPKNLRTYYRNEGSDEDDSDEDSKGFASDSDEESDGV
The following text describes a protein:
Function:
Has a role in resistance to insecticide lufenuron, but no other insecticides.
Miscellaneous:
MISCELLANEOUS: Bari1 transposable element insertion in the 3' end of the gene leads to ten-fold more abundant expression than in flies lacking the insert.
Subcellular Localization:
Mitochondrion membrane.
Sequence:
MLKVRSALSLIQSQKATLSLATQKRWQTNVATAEAREDSEWLQAKPFEQIPRLNMWALSMKMSMPGGKYKNMELMEMFEAMRQDYGDIFFMPGIMGNPPFLSTHNPQDFEVVFRNEGVWPNRPGNYTLLYHREEYRKDFYQGVMGVIPTQGKPWGDFRTVVNPVLMQPKNVRLYYKKMSQVNQEFVQRILELRDPDTLEAPDDFIDTINRWTLESVSVVALDKQLGLLKNSNKESEALKLFHYLDEFFIVSIDLEMKPSPWRYIKTPKLKRLMRALDGIQEVTLAYVDEAIERLDKEAKEGVVRPENEQSVLEKLLKVDRKVATVMAMDMLMAGVDTTSSTFTALLLCLAKNPEKQARLREEVMKVLPNKNSEFTEASMKNVPYLRACIKESQRLHPLIVGNARVLARDAVLSGYRVPAGTYVNIVPLNALTRDEYFPQASEFLPERWLRSPKDSESKCPANELKSTNPFVFLPFGFGPRMCVGKRIVEMELELGTARLIRNFNVEFNYPTENAFRSALINLPNIPLKFKFIDLPN
The following text describes a protein:
Function:
Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for storage lipid synthesis (Probable); Upon expression in E.coli functions as a triacylglycerol synthase, making triacylglycerol (TG) from diolein and long-chain fatty acyl-CoA. Prefers C(26:0)-CoA over C(18:1)-CoA. TG synthesis activity increases in M.tuberculosis upon oxygen depletion and NO treatment, with concomitant accumulation of TG in inclusion bodies. As disruption of the gene encoding this protein obviates TG synthesis this seems to be the major enzyme involved in production of TG. Has no wax synthase activity to produce wax esters.
Sequence:
MNHLTTLDAGFLKAEDVDRHVSLAIGALAVIEGPAPDQEAFLSSLAQRLRPCTRFGQRLRLRPFDLGAPKWVDDPDFDLGRHVWRIALPRPGNEDQLFELIADLMARRLDRGRPLWEVWVIEGLADSKWAILTKLHHCMADGIAATHLLAGLSDESMSDSFASNIHTTMQSQSASVRRGGFRVNPSEALTASTAVMAGIVRAAKGASEIAAGVLSPAASSLNGPISDLRRYSAAKVPLADVEQVCRKFDVTINDVALAAITESYRNVLIQRGERPRFDSLRTLVPVSTRSNSALSKTDNRVSLMLPNLPVDQENPLQRLRIVHSRLTRAKAGGQRQFGNTLMAIANRLPFPMTAWAVGLLMRLPQRGVVTVATNVPGPRRPLQIMGRRVLDLYPVSPIAMQLRTSVAMLSYADDLYFGILADYDVVADAGQLARGIEDAVARLVAISKRRKVTRRRGALSLVV
The following text describes a protein:
Function:
Not directly activated by nematocin. May modulate activity of the nematocin receptor ntr-1, leading to reduced intracellular cAMP production. Plays a role in male mating behavior.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNNNTLNITNQRTAAAMSQIYFLVVYQTAVMIVSLLGNLFLLFVIFRANQVMKRRVSPVQLLIIHTCVADLLFALLSLGTEILTLRTYPQYYGSNFVCKLMRYVQMFPMYASPFLLVAISADRYQAICRPLAHFRSSRYRRPNWMAAIAWGLALVLSIPQFFVWTKHSKTGRCSTIYGQNKNTVKITYVIMFNTLAWLLPSILAAVFYYCVCKAVRLSSTKSVRAMDSQKRNGKYSSGATEDYIEELRKKSKGFRQQMSEFDRKRVQTVRLTITIVACNFFLWMPFCLINVIQALWPEISHIMFINYVAILGNLNSCLNPWIYILFNRSHVRKALCRSRRSFTEVTKKRSFENFECSSTATMNNNYNNCHAYTAFSNRSQLKFDSYATDSTSLKTNSN
The following text describes a protein:
Function:
Highly cationic protein that has multiple functions. Acts as a chemotactic factor that mediates lymphocytes recruitment to epithelia through binding and activation of the G-protein coupled receptor GPR15. May be a tumor suppressor; together with SUSD2 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest. May regulate keratinocyte proliferation. In addition, through activation of Mas-related G protein-coupled receptors (MRGPRs) contributes to pruritogenesis by activating itch-selective sensory neurons and mast cells degranulation (By similarity); Has antimicrobial activity against Gram-positive bacteria, including Staphylococcus aureus and Actinomyces spec., and Mycoplasma hominis and lentivirus.
Subcellular Localization:
Secreted.
Sequence:
MRLLTLSGLFFMLFLCLCVLSSEGRKRPAKFPKLRPCCHLSPRSKPITWKGNHTRPCRPCRKLESNSWVVPGALPQI
The following text describes a protein:
Function:
Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
Sequence:
MEEEESSKSSTKGVCEECKNKASKYKCPGCYLRTCSLPCINAHKHRTGCNGRRNNTRFVPLSQFDDNLLLSDYNLLEETKRVAESARRTRSKLCSNYFPHFKLPFVLRTLRAAAASRRTKLLFLPAGMSKRETNQTRFHQSLPSFITSLPKPNSNDVVNMSKLIFKQISPFKFALKKFISWTIEWRFHSTDVVLFDHGVHEDTTLCSVIENHLKPGPWNHPLRPFCQEQLDCLKFFIRKYPKGPKSPFQELDMKAPIRQQLADTVILEYPVIHVFLPSEHYEFEVVRENHSVTHRPEVKDSGSADNEIQKGVTFKEEKIEEDDSSLDPQVFDLMKHVISSPMHQIPYENKSEKAGAGNRVHSSSQTKDSGVFQGMEFDFDQDLIDAYSDLIAEINPDDFLDLEGEFAKQSETEHRRDLSNSRGDFFSEELEEGEIVD
The following text describes a protein:
Function:
Required for activity of HDA1 histone deacetylase complex. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
Miscellaneous:
MISCELLANEOUS: Present with 1500 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSRKNSKKLKVYYLPVTLTQFQKDLSEILISLHAKSFKASIIGEPQADAVNKPSGLPAGPETHPYPTLSQRQLTYIFDSNIRAIANHPSLLVDHYMPRQLLRMEPTESSIAGSHKFQVLNQLINSICFRDREGSPNEVIKCAIIAHSIKELDLLEGLILGKKFRTKRLSGTSLYNEKHKFPNLPTVDSTINKDGTPNSVSSTSSNSNSTSYTGYSKDDYDYSVKRNLKKRKINTDDWLFLATTKHLKHDQYLLANYDIDMIISFDPMLEVELPALQVLRNNANKDIPIIKLLVQNSPDHYLLDSEIKNSSVKSSHLSNNGHVDDSQEYEEIKSSLLYFLQARNAPVNNCEIDYIKLVKCCLEGKDCNNILPVLDLITLDEASKDSSDSGFWQPQLTKLQYSSTELPLWDGPLDIKTYQTELMHRAVIRLRDIQDEYAKGTVPLYEKRLNETQRQNQLDEIKNSVGLTFKKKQEVEKSINDSEKRLKHAMTESTKLQNKINHLLKNRQELENFNKLPSNTISSENHLEEGSALADKLKEYIDKNATLFNKLKELQQANAEKSKLNDELRSKYQIESSKAAESAQTLKILQESMKSLENEVNGPLTKFSTESLKKELERLQNDFQSLKARNKFLKNYITLMNRQYDLKNKNNVQVEKAAANGTRFRSTRSNTPNYT
The following text describes a protein:
Function:
Putative acyltransferase (Probable). Plays a role in the morphogenesis of a vulval toroid cell, vulF, which is located where the vulva and the uterus connect. Not required for specifying vulval cell fate.
Subcellular Localization:
Apical cell membrane; Peripheral membrane protein.
Sequence:
MLTCIQPSSSSIGGFGKADDNVRILLMASVRNEFGDTSIFSRLGVTALGQHYVLVTKKKMFGGYTTHMITANMRNRPFISIPFKVSSGAQSIEESRDLISRLTTVLGRPGMFSFDDPPIGSQFPVGKELIQLDEVPVGVHDRQDKYLEKGDEVFCEVNVSGVKFYHSGIYAGDGMCYHFVCDAQESESFADALAVFSGASAHVVYDTWFEFVYALVEVSDVPPKIFRASHPLICRSGEQVVKYAEHLQRELENYDIRRCNCQHFSSECSTGVPFSYDMTSNFKYLACTVLKPTSTVVNAMTRPNRDRSSFASSSTSS
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that plays a key role in endosome organization by retaining vesicles in the perinuclear cloud. Acts as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1 through interaction with the ubiquitin conjugating enzyme UBE2J1. Ubiquitinated SQSTM1 attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport. Also acts as a regulator of type I interferon production in response to viral infection by mediating the formation of 'Lys-11'-linked polyubiquitin chains on TMEM173/STING, leading to stabilize TMEM173/STING. Also required to limit type I interferon response by promoting autophagic degradation of IRF3.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MELVLLLLRGLRLALDLLLLLLDLNFFLVSSLVTALLWLLTTAASLPGAATAGMWACWNGLLGGLCGLAEAACGLALGAMQGLGGLLRGCCSALEGLKVLGHLLTHLGLRGRELLQRGLCSLLGSGQALLREAGEGLAIGVSLLAYLVNSMVNLCLLGTQNFFTLLLALWDSVVSPVLRVADLLAAFMAHVSSSAIAISILLWSPCQLAFELLVSTTELLIGIFFVNVYGLALLLAIIVVSTVIFNPGLLLTLLGHVLGYFHTLPAYPRLQQEVWRLYQMAVLMMGMALTSQTWRRLVDWSLQVTNWSRGGRTMNRESDRRGTAQGLGRLMLAGDSHAAAQQEEQPDAEQVPQAHPSLSRSTVSGQRLQAPRDEPSTSWGKAPRREQLNAAAGDGAGVPDDDPWMLLKEQEERKKCVICQDQTKTVLLLPCRHLCLCQECTEVLLQQAIYQRNCPLCRQMILQTLNVYL
The following text describes a protein:
Function:
Functions as an inhibitory receptor that plays a constitutive negative regulatory role on cytolytic function of natural killer (NK) cells, B-cells and T-cells. Activation by Tyr phosphorylation results in recruitment and activation of the phosphatases PTPN6 and PTPN11. It also reduces the increase of intracellular calcium evoked by B-cell receptor ligation. May also play its inhibitory role independently of SH2-containing phosphatases. Modulates cytokine production in CD4+ T-cells, down-regulating IL2 and IFNG production while inducing secretion of transforming growth factor beta. Also down-regulates IgG and IgE production in B-cells as well as IL8, IL10 and TNF secretion. Inhibits proliferation and induces apoptosis in myeloid leukemia cell lines as well as prevents nuclear translocation of NF-kappa-B p65 subunit/RELA and phosphorylation of I-kappa-B alpha/CHUK in these cells. Inhibits the differentiation of peripheral blood precursors towards dendritic cells (By similarity).
Subcellular Localization:
Membrane; Single-pass membrane protein.
Domain:
ITIM (immunoreceptor tyrosine-based inhibitor motif) motif is a cytoplasmic motif present in 2 copies in the intracellular part of LAIR1. When phosphorylated, ITIM motif can bind the SH2 domain of several SH2-containing phosphatases, leading to down-regulation of cell activation.
Sequence:
MPLHSVIVLVLVLCLGWKSNTQEESLSDFTICAEPGPVIPQGNFITIVCSTSGEYDTVRLEKEGSTFMEKKTEPHGKQHRFRIGPVNETITGYYNCIFEKNYVWSQRSNDLQLKVIKENVTQGLAPGPSMTSDTSWLKTYSIHILTVVSVIFLLCLSLFLFCFLSHRQKKQGLPNNKSQHQRSQERLNLATNGLEKTSDIVMDDSLSEDRQTETWTPVAGDLQEVTYAQLDHDSLTQRTVKDVTPQNRVIMAESSTYAAIMRC
The following text describes a protein:
Function:
The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MSRGALRNDSFSGMTVLQRLMLSDSHISAIAPGTFDDLIKLKTLRLSRNKITHLPGALLDKMVLLEQLFLDRNELKVIDQNMFQKLVNLQELFLNQNQLAFLPLSLFTTLGNLKLLDLSGNNLTHLPKGLLGAQAKLEKLLLHSNQLVSLDSGLLNSLRALIELQLDRNHIRFIAPGAFDRLQNLSYLTLSRNHLEFLPSALFLHSHNLTLLTLFENPLEELPEVLFGEMAGLQELWLNGTRLRTLPAAAFRNLSRLRVLGVTLSPLLSALPEGAFRGLGELRVLALRSNSLASLPDGLLRGLRRLRQVSLRHNRLRALPRALFRNLSSLEEVQLDHNQLESLAGDVFEALPRLTEVLLGHNPWRCDCGLGPFLEWLRQHPGLVSRVEPPRCRGPGQRAGRPLLALGDGDLGCPSTRGPPPYSPADSSSAAPTQPALPAASTHPAWVPRSSEPWARAQPLAQGKHQDHSLFWALYFLLLVTQAIITGIIVFAMIKLGGLFRKLIRDRALEY
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. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition.
Subcellular Localization:
Nucleus.
Sequence:
MMKKKNIDIEELKRLIEESSMKKRFVKDIKRNCEIKSIRFGIMSKEDIIKYSEVKIMNREMYKNNSGIPYPYGVLDLKLGAHKSNSVCETCNKKLINCSGHFGYIELNYPVFHIGYYKYIIHILYCICKYCSSLLLSKEKIDFYCNLKKKSTDDSFYKKHLFKRILNNCKKVNKCYICGNPQGVIKKIIKPSLDQFMKLKHILKVKENGKMIIKEEDLNSLYVLKLFKNINPYHVKLLNIENPEKLIITALLVPPNTIRPSVIIDEHGTAEDDLTCILSEITQLNNTIYNQCTNGYQTNQFLGNVEFLQLQITRFINSDSPAVSQLLATQNISKPGRGICQRLKGKEGRFRCNLSGKRVDFSSRTVISPDPNISIDEVVIPKIIAMRLTYPETVNKYNIDKLKMLIKNGCNKWPGANYIIKKSKKGIDPYSDISTSYNNNSNNISSIGCSNIFNVVNNYINNNCKNVRYNIKDVNNNVLLKDMCDINNMNNDINNNINNIYKNTSETNLCNVNNHNNNNNIYCNNQTQDNEEERKNSQFNKISLKYANKNHVIQNLNIGDVVERHICDGDIVLFNRQPSLHRMSIMCHKAKIMDFKTFRFNECVCSPYNADFDGDEMNLHVPQTEEARAEALYLMNVKHNLITPKNGEVIIALTQDFLSASYIITNKDTFLDRDTFCLLCSYFSDASLYIELPIPAILKPKELWTGKQLISVLIKPNKKENTIINFEIQEREYSNKFGDLKHLCLNDSYVCFYKSELICGSLGKKVLGSSKYGLFYYLIHHNSSHIALKIMNRLSKLTSRYFSNKGMTIGIDDVRPSQTLTEKKKDLLLKGYEKVNNEIILYNEKKMQIQPGCTLEETLEIKVKSILDDLRNDAGKTCNQYLHYLNKPLIMFNSGAKGALINIAQMIACVGQQNVAGQRIQNGFINRTLPHFHFHCKDSESRGFVQNSFYTGLSPTEFFFHTMSGREGLVDTAVKTAETGYMQRRLMKALEDLSIHYDYSVRSCDKQIVQFIYGDDALNPSYIDNNNTYLDQFDKVFDHIVSISSSHLLLSYKNKIPYLPHVQHQNKTSNMNNIYNNMNNINNNDSNRSIIYNNDSNMNNINNNDSNMNNINNNDSNMNSIHNNNSNMNNIHNNDSNRSIIHNNDSNMNSIHNNDSNMNSIHNNNSNMNNIHNNDSNRSIIHNNDSNMNSIHNNDSNNNNNYKDCTHNPYICNESLIIRNIMNRLIYQNIAQEDLFIPLEHDEFLVNKIMESYTDQECNYEDIIRSLDLNKNVSYIHNDQGKHLSLQMCAEEHITINNTNNDNTYVEQIEMKELSKNKTKEKQSFKGTIRDMHEDSEEQMNKFITKKAKFFIEKKKGKMHECNDDIEYNNTQYDNIQYNNISCNYIKSQNLENTHHQVNNDLSFIKNNVILPPKEYHSIFHFVNDYRNVVEIKNLMDKKKIFLNNSEKNVVQSKYNRMSKNLKKKIEIINNIYRNEKKKLNRWKTKMDNDDNYWSSDDDSIIAKKIIKIKNKEKRKYHPKEEKENFDRNNYKMITDNNNNDNNNNNNDNNNNDNNNNNNNNSNNNNYYYNLHDDVNNLGVTNYNTNIYPNDCNGIYEKETNNNELTTNSNMCDKNNDFSDEFFNNINENDLLYDNKYYRQIFKNVIGFVSVFEYVESYKQHYILFPYEIIKWTSFLLEYLTEIIPTNIFLHTKLSKKEKPTHQKNTGKMKIYIEEIKKWLFIKAINIYKYFSFKKSIELIKKKDYFNYIIKNYDISHRYIIHDYSFINLKQLYLFIFFNIYKYFKYISTPGDAVGSISAQSIGEPGTQMTLKTFHFAGVASMNVTLGVPRIKEIINASNSIQTPILNIPLEVNDNYNFALMMKSKLEKTTIRDICMYIKEDYTSRGVFLSVKFNEELIQKLFLNINAYNIKDIILKQSHINKIKINKIHINVINKYKLHISLKNDEFIFFQMESLKKGLLDLLIYGDKDIKRCIIKKEDIEVTDNEDEICDDMDEYYNVSQGTELYERKCNSKEENKNAIRVKKEEIDDNLEKEENIIYVSEKDSVNQLKSEKKKDINDDNNNNDDNNNNDDNNNNNDDDNKINDTIFNDDINSDRNNLKENGSKLENVGEHIIERLSYKMKEKNVKKEHIKKEPNLINLDTINLDTLNFDEINVHNINNEKIEFYDEHLNICQGNKKHIQKKKKKKTVYSILVEGNSLNYVLGLEGVDFKHIISNHVINVFQVLGIEAARITIINEIKKCVEAYSIDIDIRHIMLLADIMAFTGDILGINRFGIQKARQSTLMLASFEETNEHLFVSSFFKNVDEINNISESIIVGKNIPIGTGAFQLLYDYKFEKETKNLTLLEKAERETAMNY
The following text describes a protein:
Function:
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in chromosome stability (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSKQNIDKSTEHSAGENALSEKNHTIESNKNNIDSEEDDEEDEDYDPEKKNEAENEGGVSSDEEEDNDQYKDGKTSKIPDYSTIESSTSQVKTRSQRLHEKLSNQSRFIGNFEVDSKTGLVKDQSNIDVNSIFENLKNGSPSIDNSEELNIDSEKTANSQQQQKQQSNIEENELQGPKQIKIQINYTFAGKLITETKYVDENSQEAKAYLNSTSNISSSNSNEDIPYRRSQVKVIRTDPVTNETKELRIKLKRPSLIDRFLSINGNSKKMKLSTLEKSRLDWASFVDKRNINEELKIHNKAGYLDKQDFINRMNSKRDDLYLQAKEKEKIRKQQLLQK
The following text describes a protein:
Function:
Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division.
Subcellular Localization:
Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MATSTAFNAANHGLQIGNNSGSITAEFHVARAYTTEDIDRICLHALRCPDSLAVKNRLKESKDRLVYQSIQWILEDAQYKDWENGDDVGLLWIKGGAGKGKTMLSIGLIEQLARAQDDSTVVIYSFCQNADYELNTLEAILKGLILQLANRQPELKESLRRRWDTIQESFSEDVTSWQSLWNILFEMLARCKYSRVYMVVDALDECQDNDMVDFLKSIVRKGLDQPGKVKWMLTSRPWDGAERVLLAGQDQVQINLDGEHNSQSVSGAVEAYITSKVEELSRQHKYGATLKSEIETELTERSEGTFLWVSLVCKALESVSRDDALSTVQSLPPGLHPLYDRVLNQLNEGELAEVQKCMRLLKAMMTVYRPLKVEEVASVIGLTDEEDTIRALVDCCASFIRLREDKIEFVHQSARDYLAAGTGLSILDSHGRFGHEEIALACLTYLSEYLKPNLVNLPRPDATRDTLGLGNGPTNGVLSRVDYAAMFWVSHLKNTSNDSDKSQVSVFLHTKLLEWLECLSLLDRLPRAIDALRALEEILKLTKDDCQALAFVQDAMRFLLRHYHTLSHWPLQIYSSAIIFSPESSVVKGENLHKVPVWLGRAPPMEDSWTPMIQTLTGHSEAVWRVAFSPDGKQIASGSDSGLIKLWDTTTGSLQKTLSGSHPKRRYQIQQEQVKAMAFLPDSKLIISGYYDGSVMLWDTTTGDRQEIADHFGISKVNYTYLQPPEQGGYGLHAGAFSADCKQIAAFGWSRDSTCIMLFDTATGDLQKILKGHSHECSTMAFSSDSRQLVTGSVDCTVRLWNTTTGDLEKTFVGHTGTVLSVAISSDGRQIVSGSIEAVKLWDAATGDLLKTLASGFAGSVAFSPDSRQIAAGFKDGKIFIWDAAGTLQKTLERHPGAIMSIAFSPDVKQLVTCSTDSTIKRWDITIGGVQEAVGHSKHVTTMVLSPDGKVIASGSADKTIKLWDAATGDLQKTLTGHLDTVEKVVFSLDNRQIVSCSSEAVKIWDAATGKVQNSFESDDVFTIVAVSPDGKHIASGHCNGRIKLWDMATGSLLKTMAGYRSKFDSLVTTEVFDIQLQEAIFNTQITGLVFSPDAKLILSTSTDRAIKLWDAATGDLQKRLPCHSDSIITDAFSRSSGYPNWIFSVAFSSDGQHIAAASADKTIRVWSIEKSLKASKYLGRAVGSHIKSSRPWKEIKPSAQVYDVIFSPGNQYLATDIGPIPLESTPTKGEGERPVRSDSDSDSDSLQSLCHRDQWLCYGAMPFLRLSPDFYVTRWDAHGDRVVVGYDNGQVSSFNIDRRSLQADWGTLEL
The following text describes a protein:
Function:
Oxidizes preferentially the aliphatic diamine putrescine with production of the corresponding aldehyde, ammonia and hydrogen peroxide. May be involved in the regulation of developmental programmed cell death (PCD) in both vascular tissue and the root cap. Required for jasmonic acid-(MeJA) mediated early protoxylem differentiation associated with putrescine levels reduction and H(2)O(2) accumulation in roots.
Subcellular Localization:
Secreted.
Sequence:
MNTSILAILFLIQCVFTLGLHFHPLDPLTPQEINKTSFIVKKSHLGNLKDLTFHYLDLEEPNKSHVLQWLSPNPSKKPPPPRRRSFVVVRAGGQTYELIIDLTTSKIASSRIYTGHGFPSFTFIELFKASKLPLTYPPFKKSILDRSLNISEVSCIPFTVGWYGETTTRRELKASCFYRDGSVNVFTRPIEGITVTIDVDSMQVIKYSDRFRKPIPDKEGNDFRTKHRPFPFFCNVSDTGFKILGNRVKWANWKFHVGFTARAGVTISTASVLDPRTKRFRRVMYRGHVSETFVPYMDPTYEWYYRTFMDIGEFGFGRSAVNLQPLIDCPQNAAFLDGHVAGPDGTAQKMTNVMCVFEKNGYGASFRHTEINVPGQVITSGEAEISLVVRMVATLGNYDYIVDWEFKKNGAIRVGVDLTGVLEVKATSYTSNDQITENVYGTLVAKNTIAVNHDHYLTYYLDLDVDGNGNSLVKAKLKTVRVTEVNKTSSRRKSYWTVVKETAKTEADGRVRLGSDPVELLIVNPNKKTKIGNTVGYRLIPEHLQATSLLTDDDYPELRAGYTKYPVWVTAYDRSERWAGGFYSDRSRGDDGLAVWSSRNREIENKDIVMWYNVGFHHIPYQEDFPVMPTLHGGFTLRPSNFFDNDPLIG
The following text describes a protein:
Function:
May act as a pheromone.
Subcellular Localization:
Secreted.
Sequence:
NDYAELEGKWDTIAIAADNDAKIKEEGPLRLYVRELYCNEDCSEMEVTFYVNANNQCSKTTVIGYKQADGTYRTQFEGDNRFQPVYATPENIVFTSKNVDRAGQETNLIFVVGKSQPLTPEQHEKLVEFAHENNIPEENIHNVLATDTCPK
The following text describes a protein:
Function:
May act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Shuttles from the cytoplasm to the nucleus when associated with KIN10.
Sequence:
MILSKRPHLMIRKLSEMLVPRSRSAAIKPEEYTASPRSPLDLNFPSPVHSKRFGSGGVGLGIVAALEETSNGINRHDPVRYSGRFRCPEIDLSDEEYTYVTSPNGPTKVYYNDDGFELSENDYRRVHKPMVTVDEPPVIERQSVRGPTEFLSSCCLCKKKLQGKDIYMYKGEMGFCSAECRSVQIMNDERQEQCKTQVSRNADVLSSPYAAGQRLSAGVFVF
The following text describes a protein:
Function:
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein. Endomembrane system; Single-pass membrane protein.
Sequence:
MLEFNNWFFVLMVQFFILMFILNAILFKPMMELFRQREQTIKGALEEAQLMNEKKEKAIAQMNADLAQAKAQAKQIINALREEGLAYQREVVSNAEKEAVQMIEKARAEVKAETDKIRNMLRQEVERLSEEIVNKLVKA
The following text describes a protein:
Function:
Ligand for members of the frizzled family of seven transmembrane receptors.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MPCQGQSRKKMAVLKVLRGREAYDKLVSSIQKGAKLGLQECRSQFRNEKWNCTMAVKTKNKSTSKQNPAYVMSMVPHATREMAFAHGISAAGVTFALTMDCRLGAFEDCSCIHGKSEGNKGNWWGGCNENVKFGEVMARHFLEALQSGKDEHSLLNVHNNEVGRKAVRATLKRECRCHGISGSCSTRTCWRKLSSFAEVGQYLVEKYSTAKRVIFQNGNFYELTMLGTRPISKKDNNFIYSESSPDYCQRNMTVGSAGVLGRECEGSKDELVRCRQLCDSCRFDTQEFTEIKNTFCNCKFHWCCKVKCMTCKETTRKTRCVARQQAL
The following text describes a protein:
Function:
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular Localization:
Cytoplasm.
Sequence:
MVAAKKTKKSLESINSRLQLVMKSGKYVLGYKQTLKMIRQGKAKLVILANNCPALRKSEIEYYAMLAKTGVHHYSGNNIELGTACGKYYRVCTLAIIDPGDSDIIRSMPEQTSEK
The following text describes a protein:
Function:
Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis.
Subcellular Localization:
Cytoplasm. Mitochondrion inner membrane. Mitochondrion matrix.
Sequence:
MLYSPKDRSYEEAVNALLSLQSNQSVIIQSTLQRKNDKETMGKIILEEMTQYCKSIDIDFDKLSVIHVAGTKGKGSTCAITESLIRNQGFTTGLFTSPHLISPRERIRINGEMISKELFTKYFWICWDTLIKDFDTQLPNYFRYLTLMALKAFQDQGVQCIILEVGIGGRMDATNVVPKTAVSGISALGFDHMNLLGDTLPEIALEKACIMKKGVPVFTVASQAPEAMKVIENHSKLMESPLSVAPTLLQYNFSGDIGLKGEHQRENASLAVALANCWIAQQKHIPLNQIFNSNNNNKYNLYNSQINNYSSEYFTPLLESFEKGLRDCQWPGRAQHFTSEHFPNIDFYLDGAHTPESSVVCVNWWKSVASNDSNTIHAMIFNSTGGRNPNSFLKPIIDSIDNKEIPIFNLVLIPTLSIGKAIDNKYYIKEIKNQSNNSNNNNNNNNNIGSNVIPDKAATIQPKEDTWEDYCVNRYIEISTNNPHPVEAFENIESSIEKIKELGQNGKKNVKVLVTGSLYLIGGVLQTLLKEKSFT
The following text describes a protein:
Function:
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity).
Sequence:
MTKRILNVAEKPSAAKEIAAILSNKRATVREGFSKYNKLWDFKYNILNFNDCEMTFTSVTGHLMEIDVVEQFKPWASCDPIQLFDAPIRKTVPSDKEPLKKTLEREIKKADILILWLDCDREGENIAFEVLEVCKNAKKKFEFYRAHFSAIIPREIDRACKNLAKPNEKDSIAVDTRMEIDLRIGAAFTRFQTLYLKKFKIISNSDNQPKTTTPANGNILNNSNNNSSGKEIISYGPCQFPTLGFVVERYFRIVNFKPEDFWHLSVVHEKMDTSSGKMIPVTFSWCRNRLFDYTAAFILYEKCLDNTEATVVDVTSKESRYRPVPLTTIELQKAASKKLRISSVQTMQYAEELYTKGLISYPRTETDSFQAGTDLKGLIGNQASNPEWGAYASRLINNNQFVYPKSGKNNDNSHPPIHPTSSATGLSGNLKKIYDFITRRFLACCSEESVFANTTVTIDIQGERFSETGTMVLKLGYLEVYPFDKRNDKLIPTYQKGERFTPKRIDLTKGTTVAPHYITEAELLTAMDNNKIGTDATMATHIQTIQDRFYVKKNESNQFVPSNLGVSLVASYELMGFEFSKPNLRAAIEADVDKISRGQKTKQEVLLSTIEKYKQLYQLANQNINCFDRSFREYYEPADPKGGEFRVLVSQFSRCGKCNGKMQYKSDQNPEAPKRILFCPQCIDTFDLPKNGDISQLVTSMGVPQNCPICQYQVLSVRNPINDKSYTICPKCRNSPPDPIHKKPFHCFQCTFNCNLATGNKQQQQQQQQQQQQTNYNRNNNNNNTNSARPITTRTTRTTTQHRTFTASNNNFNNNNRNSDRNNNNFIF
The following text describes a protein:
Function:
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular Localization:
Cell outer membrane; Lipid-anchor. Bacterial flagellum basal body.
Sequence:
MQKNAAHTYAISSLLVLSLTGCAWIPSTPLVQGATSAQPVPGPTPVANGSIFQSAQPINYGYQPLFEDRRPRNIGDTLTIVLQENVSASKSSSANASRDGKTNFGFDTVPRYLQGLFGNARADVEASGGNTFNGKGGANASNTFSGTLTVTVDQVLVNGNLHVVGEKQIAINQGTEFIRFSGVVNPRTISGSNTVPSTQVADARIEYVGNGYINEAQNMGWLQRFFLNLSPM