lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Primarily acts as an independent SigF regulator that is sensitive to the osmosensory signal, mediating the cross talk of PknD with the SigF regulon. Possesses both phosphatase and kinase activities. The kinase domain functions as a classic anti-sigma factor-like kinase to phosphorylate the anti-anti-sigma factor domain at the canonical regulatory site, and the phosphatase domain antagonizes this activity.
Miscellaneous:
MISCELLANEOUS: Overexpression switch off espA induction under osmotic stress.
Domain:
Multidomain protein in which the components of the entire signal transduction cascade for SigF regulation appear to be encoded in a single polypeptide. Contains an N-terminal PAS sensor domain, followed by an adjacent PAC (PAS domain-associated C-terminus) region, a phosphatase domain, an anti-sigma factor kinase domain, and a C-terminal anti-anti-sigma factor domain (or substrate domain) (Probable). Phosphorylation at Ser-600 leads to a change in the overall shape of the dimer.
Sequence:
MAAEMDWDKTVGAAEDVRRIFEHIPAILVGLEGPDHRFVAVNAAYRGFSPLLDTVGQPAREVYPELEGQQIYEMLDRVYQTGEPQSGSEWRLQTDYDGSGVEERYFDFVVTPRRRADGSIEGVQLIVDDVTSRVRARQAAEARVEELSERYRNVRDSATVMQQALLAASVPVVPGADIAAEYLVAAEDTAAGGDWFDALALGDRLVLVVGDVVGHGVEAAAVMSQLRTALRMQISAGYTVVEALEAVDRFHKQVPGSKSATMCVGSLDFTSGEFQYCTAGHPPPLLVTADASARYVEPTGAGPLGSGTGFPVRSEVLNIGDAILFYTDGLIERPGRPLEASTAEFADLAASIASGSGGFVLDAPARPIDRLCSDTLELLLRSTGYNDDVTLLAMQRRAPTPPLHITLDATINAARTVRAQLREWLAEIGADHSDIADIVHAISEFVENAVEHGYATDVSKGIVVAAALAGDGNVRASVIDRGQWKDHRDGARGRGRGLAMAEALVSEARIMHGAGGTTATLTHRLSRPARFVTDTMVRRAAFQQTIDSEFVSLVESGRIVVRGDVDSTTAATLDRQIAVESRSGIAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECVLVAPPGSPAHHVLSLVQLPVVGADTEDIFAQE
The following text describes a protein:
Function:
An odorant receptor which affects chemotaxis to the volatile odorant diacetyl. Specifies AWA neuronal cell fate via the odr-7 pathway.
Subcellular Localization:
Cell projection, cilium membrane; Multi-pass membrane protein.
Sequence:
MNTAIKNDVQNVAFSMAFITNCTLILLIFSRSPFKLGTYKYLMVYFASVSLFYSFLECLLNPLLLSYKDCFQVIVKLQFSNPKVDRYILYYGCGICGVLMPMFVVHFIFRYFAMQRKGNLKYFEGWYFLYWLSVPLISGFLWAQTLFAFLYEDTESSDYMREILLENYGLNISDITYVGVLYYKKSISGSGTEPNFTGLQGVCVLGTIMTVCFCFIIYFGTLTYKRIMHLILEGRSEYTRRLQKQLYQALVIQTIIPIFFLILPLTIYFYSPLFHFGNQTIGDWTALSTAIYPIIDPLPVIFVIDNYRLAVLEFFGCIKPQRTVSINVTSSSNAAVEN
The following text describes a protein:
Function:
Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 25 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 (10% abundance) and VP2 (90% abundance), which differ by the presence of an N-terminal extension in the minor protein VP1. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. VP1 binds DNA and may therefore play a role in viral DNA encapsidation.
Subcellular Localization:
Virion. Host nucleus.
Sequence:
MSKIPQHYPGKKRSAPRHVFIQQAKKKKQTNPAVYHGEDTIEEMDSTEAEQMDTEQATNQTAEAGGGGGGGGGGGGGGGGVGNSTGGFNNTTEFKVINNEVYITCHATRMVHINQADTDEYLIFNAGRTTDTKTHQQKLNLEFFVYDDFHQQVMTPWYIVDSNAWGVWMSPKDFQQMKTLCSEISLVTLEQEIDNVTIKTVTETNQGNASTKQFNNDLTASLQVALDTNNILPYTPAAPLGETLGFVPWRATKPTQYRYYHPCYIYNRYPNIQKVATETLTWDAVQDDYLSVDEQYFNFITIENNIPINILRTGDNFHTGLYEFNSKPCKLTLSYQSTRCLGLPPLCKPKTDTTHKVTSKENGADLIYIQGQDNTRLGHFWGEERGKKNAEMNRIRPYNIGYQYPEWIIPAGLQGSYFAGGPRQWSDTTKGAGTHSQHLQQNFSTRYIYDRNHGGDNEVDLLDGIPIHERSNYYSDNEIEQHTAKQPKLRTPPIHHSKIDSWEEEGWPAASGTHFEDEVIYLDYFNFSGEQELNFPHEVLDDAAQMKKLLNSYQPTVAQDNVGPVYPWGQIWDKKPHMDHKPSMNNNAPFVCKNNPPGQLFVKLTENLTDTFNYDENPDRIKTYGYFTWRGKLVLKGKLSQVTCWNPVKRELIGEPGVFTKDKYHKQIPNNKGNFEIGLQYGRSTIKYIY
The following text describes a protein:
Function:
Probable corepressor protein acting as a component of a complex that represses transcription (Probable). May play a role, as part of a CoREST-like complex, together with the chromobox protein homologs hpl-1 and hpl-2, in the formation of the vulva and in fertility.
Subcellular Localization:
Nucleus.
Sequence:
MDSYTSSDEDASRKENISDEGLNMLNASPEPMEEDDPEEQAEQEEETSRMARPIRSMRKRETTSGESMGDEDEDLEDEEDEDEEAEAREHHESGAHDTSFSNPLSNVDNLIHVGTEYQAIIQPTAEQLEKEPCRDQQIWAFPDEMNENRLTEYISEATGRYQLPIDRALFILNKQSNDFDAAMVQAMRRKEIHDDWTAEEISLFSTCFFHFGKRFKKIHAAMPQRSLSSIIQYYYNTKKVQNYKTMINVHLNETDTYDELFKEVNHLERVPSGYCENCNAKSDLLILNRVMSRHECKPCILYFRLMRVPRPASLRALTKRRQRVLCPEYMKIYVYGYLELMEPANGKAIKRLGIGKEKEEDDDIMVVDDCLLRKPSGPYIVEQSIEADPIDENTCRMTRCFDTPAALALIDNIKRKHHMCVPLVWRVKQTKCMEENEILNEEARQQMFRATMTYSRVPKGEIANWKKDMMALKGRFERFTPELDTTATNGNRSGKVRINYGWSPEEKKNAIRCFHWYKDNFELIAELMATKTVEQIKKFYMDNEKLILESIDTYRAELKSKLGK
The following text describes a protein:
Function:
E3 SUMO-protein ligase; facilitates UBE2I/UBC9-mediated SUMO2 modification of target proteins.
Domain:
Binds UBE2I/UBC9 and two SUMO2 molecules via its N-terminus. The most N-terminal region interacts with the SUMO2 chain that is covalently bound to the UBE2I/UBC9 active site, while the second region interacts with another SUMO2 that is non-covalently associated with the same UBE2I/UBC9 chain.
Sequence:
MGDPGSEIIESVPPAGPEASESTTDENEDDIQFVSEGPSRPVLEYIDLVCGDDENPSAYYSDILFPKMPKRQGDFLHFLNVKKVKTDTENNEVSKNHCRLSKAKEPHFEYIEQPIIEEKPSLSSKKEIDNLVLPDCWNEKQAFMFTEQYKWLEIKEGKLGCKDCSAVRHLGSKAEKHVHVSKEWIAYLVTPNGSNKTTRQASLRKKIREHDVSKAHGKIQDLLKESTNDSICNLVHKQNNKNIDATVKVFNTVYSLVKHNRPLSDIEGARELQEKNGEVNCLNTRYSATRIAEHIAKEMKMKIFKNIIEENAKICIIIDEASTVSKKTTLVIYLQCTIQSAPAPVMLFVALKELVSTIAECIVNTLLTTLNDCGFTNEYLKANLIAFCSDGANTILGRKSGVATKLLENFPEIIIWNCLNHRLQLSLDDSISEIKQINHLKIFIDKIYSIYHQPNKNQTKLLGTVAKELETEIIKIGRVMGPRWAACSLQAATAVWHAYPILYMHFSHSYSGLAKRLANINFLQDLALMIDILEEFSVLSTALQSRSTNIKKAQKLIKRTIRALENLKIGTGKYESQIEDLIKSDKFKDIPFNKNNKFNALPRSILLDNIIQHMNLRLLSDRNHEDIFNYFDLLEPSTWPYEEITSPWIAGEKTLFHLCKILKYEVDLNDFREFVNNNIKSNNVSIPTTIYKAKKIVSTIAINSAEAERGFNLMNIICTRVRNSLTIDHVSDLMTINLLGKELADWDATPFVKSWSNCNHRLATDTRVRQKSTKVFHENQLAIWNLK
The following text describes a protein:
Function:
Extracellular metalloprotease that contributes to pathogenicity; Inactive carboxypeptidase that may play a role in cell wall organization and biogenesis.
Subcellular Localization:
Secreted.
Sequence:
MRTSPHTCVLLLCAASVIATPQRQAPIQLPLSASSPSSESFAPVQRYDGDQVWRVKLGGEDIRRIEDIVDLVENLQLDIWRTTSRSLDIRLNELQKNDLQELLHPDTLFEPFITNVQSLVDFTTPSYYSDIIDSSLEVNADQSLRNGQPLQISKKNKKPKIDPFNLTTLATPFHDSYHTLKDVHQFGDALVETFNGKEGIEVWSFDVGTTWEGRPIRGWSARLMRNESDVNNSQRRRRSRVTEEDEELQKEIVIISGQHGREWVGPSSALYFLHSLLLTSLSSPSSEAALMLSKFTFSVIPTINPDGFVYSQSHRMWRKNRQPVGHKSCVGIDLNSNWAYKWKKEKKEKPCNEGYRGKAAFEAYETKAVGEWLAKGAERGTRVRAFVDLHSYGQLFMFPFAHSCNDFPADAEMLMEAGLGVAKAIRTAHGETYETGQACDLTYRAPGDSVDYAYGVTDIRWSYSAELRDTGTYGFMLPKTLIRPTAEEISAGILHLAKFIYVLEIAD
The following text describes a protein:
Function:
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
Sequence:
MPTPIHVLPPHVARLIAAGEVVSRPLDVVRELVENALDAGASRIEIEVDGGGLERVQVRDNGSGIAAQSVPLAPARHATSKLTAGPETGSLSVTTLGFRGEALWAAAQAGELELTTRPAAQVGAARLRAQGDAVEVSRTSAPAGTTVTVSQLFARLPARLRTQASAAAEVRDITALLGRYVLHHSALHWRLTVDGDPRLTHAPADHRGAVATVYGPLSANRVLTLDTPGVRGVVSRPELTRARRDRMHFAVNGRPIVAPPELERAVIDAYAELLPAGTAPLCVLDLTVAPEDYDPNIHPAKQVVALADLPAVALRVRDAVAGALAGHPLVRAAPALIAPPEPHPAPTAGNFPDLTLLGVYQELYLLAQGEGDLWVVDAHAAHERALYERLGRELGTAAPLELPTPELLHLTPEQTARLHERGAELRGWGLTIEDFGAGLARLRTLPAALAALPVPRLHEVVVETALSGGPDPRREVLARLACLPALKAGMLDAERGALVLAALRECEQPWACPHGRPTVLRLSERDLAHAFGRRGVRDVARGRDSVV
The following text describes a protein:
Function:
Functions as a nucleotide exchange factor (NEF) for Hsp70 chaperones which accelerates the release of ADP. Required for fully efficient Hsp70-mediated folding of proteins (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MDPNMNNLLKWGIQNSTATQQTSDSNNNASQAPRSNITPEMLSALFGGPSEADLMKAAMEALRSDEVDLENKLIAFDNFEQLIESIDNANNLEPLGLWTPLVELLKHEEPDMRRMAAWCIGTAVQNNEKAQDKLIVMNAIPTLVSMSTQDPVPAVRKKAVYALSSAVRNYQPGTNELVKHLPGGYASGKVDAADMDTIDMIMDKLRAHPVSSSPPSAA
The following text describes a protein:
Function:
Probable ligand for integrin in the brain. This is a non-catalytic metalloprotease-like protein.
Subcellular Localization:
Presynaptic cell membrane; Single-pass type I membrane protein. Perikaryon. Cell projection, axon.
Domain:
A conserved motif [AVN[ED]CD] within the disintegrin-like domain could be involved in the binding to the integrin receptor.
Sequence:
RRHHSPLLVSLIGGQTFKSSHSGAAYFGGICSPTHGGGVNEYGNIGAMAITLAQTLGQNLGMMWNKPRTTTGDCKCPDLWRGCIMEDTGFYLPQKFSRCSVDEYSKFLQDGGGSCLFNKPLKLLDPPSCGNGFIEIGEECDCGSPAECNKSRAGNCCKKCTLSHDAMCSDGLCCRGCKYEPRGTVCRESLNECDVPEACPGDSSACPANLHKQDGYFCDNEQGRCFGGRCKTRDRQCHALWGRGASDRFCYEKLNIEGTEKGNCGRDRQNWIQCSKQDVLCGYLLCSNISGIPQIGELNGDITSMSFYHQNRYLDCRGGQVTLPDGSCLGYVEDGTPCGPNMICLDRRCLPASAFNFSTCPGSWNGVICSDHGVCSNEGKCICHPEWTGKDCSVYDPLPVPKPTGVVEKYKGPSGTNIIIGSIAGAVLIAAIVLGGTGWGFKNIRRGRSGGG
The following text describes a protein:
Function:
Guanine nucleotide exchange factor for SEC4, catalyzing the dissociation of GDP from SEC4 and also potently promoting binding of GTP. Activation of SEC4 by SEC2 is needed for the directed transport of vesicles to sites of exocytosis (By similarity). Required for filamentous growth.
Subcellular Localization:
Bud neck. Bud tip. Cytoplasmic vesicle, secretory vesicle. Note=Localizes to the spitzenkorper, a structure found in fungal hyphae which is the organizing center for hyphal growth and morphogenesis.
Sequence:
MSSQADYDKRLAEEVGSLSTRLVTAVNKQVELEETILELRKQVSALKLKNEQLNQSDIKLKTILPKYIKLQDDYRETLTKKKEAESQNTKLQGEVEDLTASLFDEANTMVSNASRETHNFKIKNRKLYEELDEKNIIINDLQEQLQDLKQMFIKMEEQSKIQSYSQSNTPKIESSTDFNETNSIHTNTNFSESKLSKYNTRSTLGDEESQNYNLQQLQRIIYSPLITSIRFDLNNYNIDFKGFVYQLIKPDFQFDLSHLKTIPFFKSIWQSEIENCIHYIPSLPATTTLLNRWQKGKTFWGSLIEGKVSIEPIKGSNETFKLTYKGNNASGNSSNENTESISNRSSATGSVVPVAIKDPCTFCGEARNDSLEHCRLYHLKLFESNTANNSGNNSTNQDQQGNNDNTHVIASYPLCNYCLIKLRNLCDFFAKIRLIRSNIFKLKQNDSFDEFIVVPGSFGQFKRSNTISNRNGTYSSSSTSSSSTSSVSSSSATTANGESLNSTTHNIQLERTEESKLIKLYIMMLLIRSKIFWSKLGFWDTIDQINEINLDEIHYEAFSYLIPKPTQQQQQQQGDIRSQSNFNSPRQSVDGRSVLSGSISSPRQPNLDKQQKDSIVDETVAQLQRDGVVRSETASAEEKFEDAISDETNGQEQLRSEKLQTGKTVTEPNSVSESEPVQEPEQVRSKSNNNTNNKNKDTKIEDSDAEHTFSLKRSHSKQFKDQLNKELDQTLEMLAENIDFDESSNGNGNGN
The following text describes a protein:
Function:
Restin potently inhibits angiogenesis; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MTHRRTAQGRRPRWLLSIISTLLSTVLQTRAATGSASQDHLDLTELIGVPLPSSVSFVTGYGGFPAYSFRPGANVGRPARTLIPSTFFRDFAIGVAVKPSSAQGGVLFAVTDAFQKVIYLGLRLSRVEDGRQRVILYYTEPGSHVSQEAAAFSVPVMTNRWNRFAVTVQGEEAVLFMDCEEHSQVLFQRSSRPLTFEPSAGIFVGNAGATGLERFTGSIQQLIIYSDPRTPEELCEAQESSASGEASGFQEMDEVAEIMEAVTYTQAPPKEAHVDPISMPPTSSSPTEDTELSGEPVPEGTPGTDLSITGHSSPEQGSGEILNDTLEVRTVDGNPSTDGGSGDGALLNVTDGQGLSATATGETRVPVTTALEVENGSMPTGSPTLAMFTQSFREVDMLDLENLTTASGDGEVPTSTDVDTEAGTLPTGGPTLKPREEATLGSLGEEWSTTVVSKVPLNAFEEEEASGTAIDSLDAFTPTVVLEQASGTPTDIQAALTTTVAPEQVFTAAPTDGEDLVTSTEESDEEGSGSTLPIGPPLSKPTVTPERQVTLAGVEAEGSDPVWGVDVGSGSGDIVGNEDLLRGPPGPPGPPGSPGIPGKPGTDVFVGPPGSPGEDGAPGEPGPQGPEGQPGLDGASGQPGMKGEKGARGPNGSVGEKGDPGSRGLPGPPGKNGEVGIPGAMGPPGPPGPPGPPGPGCTTKLGFEIEGSGDTQLLSKPRISGPSSPSGPKGEKGEQGAKGERGTDGISTMGPPGPRGPPGRVEVLSSSLINITNGSMNFSDIPELMGPPGPDGVPGLPGFPGPRGPKGDTGVPGFPGLKGEQGEKGEPGAILTGDIPLEMVKGRKGEPGVHGAPGPMGPKGPPGHKGEFGLPGRPGRPGLNGLKGAKGDRGIMLPGPPGLPGPPGPPGPPGAVVNIKGAVFPIPARPHCKTPVGTAHPGDPELVTFHGVKGEKGSWGLPGTKGEKGDQGAQGPPGPPVDPAYLRHFLNSLKGENGDAAFRGESSHNLFVSGPPGLPGHPGLAGQKGEAVVGPQGPPGIPGLPGPPGFGRPGVPGPPGPPGPPGPPAILGAAVPLPGPPGPPGQPGLPGSRNLVTALSDMGDMLQKAHLVIEGTFIYLRESGEFFLRVRDGWKKLQLGELIPIPADSPPPPALSSNPYQPQPPLNPILSANYERPVLHLVALNTPVAGDIRADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFSLPIVNLKGQVLFNNWDSIFSGDGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCANRLIVLCIENSFMTDARK
The following text describes a protein:
Function:
RNA-binding protein involved in post-transcriptional regulation. Component of the ASH1 mRNP which transports the ASH1 mRNA to the distal tip of the bud, where the ASH1 protein is translated and targeted to the daughter cell nucleus. Binds to the ASH1 3'-UTR containing the PUF consensus UUGU segment and represses its translation. This silencing of ASH1 mRNA is critical for asymmetric seggregation of ASH1 to the daughter cell nucleus.
Miscellaneous:
MISCELLANEOUS: Present with 21500 molecules/cell in log phase SD medium.
Subcellular Localization:
Bud tip. Nucleus, nucleolus.
Sequence:
MAPLTKKTNGKRSAKEVSHSEKKLAKKPRISIDSSDEESELSKKEDAVSSSSDDDDLDDLSTSDSEAEEEADELDISDDSEEHENENEEKEGKDKSEGGENGNHTEQRKLLKERKMQRKSGTQVQQIKSVWERLRVKTPPLPKQIREKLSNEIWELSKDCISDLVLKHDASRIVQTLVKYSSKDRREQIVDALKGKFYVLATSAYGKYLLVKLLHYGSRSSRQTIINELHGSLRKLMRHREGAYVVEDLFVLYATHEQRQQMIKEFWGSEYAVFRETHKDLTIEKVCESSIEKRNIIARNLIGTITASVEKGSTGFQILHAAMREYVKIANEKEISEMIELLHEQFAELVHTPEGSDVACTLVARANAKERKLILKALKNHAEKLIKNEYGNIVFITILNCVDDTVLVFKTFSPTVKEHLQEFIIDKFGRRPWLYILLGLDGKYFSPIVKNELLRYIELSKATSKKDPLQRRHELLSKFAPMFLSTISKDYSSILTENLGCQFIAEVLINDELYAQLNEKDQEKYQQVLNNILTTFKGDITEEEHPIHRAFSTRLLKALIQGGKWNNKEKKVIPLKNVQGLGVPFAEKLYDEIIDSSNLLEWINNADSSFTIVALYETLKDQKEGKPFLKDLRGVQSKITTDESNKGSQLLAKLLK
The following text describes a protein:
Function:
Endonuclease that resolves Holliday junction intermediates made during homologous genetic recombination and DNA repair. Exhibits sequence and structure-selective cleavage of four-way DNA junctions, where it introduces symmetrical nicks in two strands of the same polarity at the 5' side of CC dinucleotides. Corrects the defects in genetic recombination and DNA repair associated with inactivation of ruvAB or ruvC.
Miscellaneous:
MISCELLANEOUS: Encoded by the cryptic lambdoid prophage DLP12. Normally not expressed. Complete suppression of ruv mutations by RusA is dependent on the activity of RecG.
Sequence:
MNTYSITLPWPPSNNRYYRHNRGRTHVSAEGQAYRDNVARIIKNAMLDIGLAMPVKIRIECHMPDRRRRDLDNLQKAAFDALTKAGFWLDDAQVVDYRVVKMPVTKGGRLELTITEMGNE
The following text describes a protein:
Function:
Glucoside hydrolase that cleaves the alpha-1,3-glucosidic linkage in nigerose. Has very low activity towards maltooligosaccharides, soluble starch, nigerotriose, kojibiose and trehalose.
Sequence:
MKIKTILTPVTCALLISFSAHAANADNYKNVINRTGAPQYMKDYDYDDHQRFNPFFDLGAWHGHLLPDGPNTMGGFPGVALLTEEYINFMASNFDRLTVWQDGKKVDFTLEAYSIPGALVQKLTAKDVQVEMTLRFATPRTSLLETKITSNKPLDLVWDGELLEKLEAKEGKPLSDKTIAGEYPDYQRKISATRDGLKVTFGKVRATWDLLTSGESEYQVHKSLPVQTEINGNRFTSKAHINGSTTLYTTYSHLLTAQEVSKEQMQIRDILARPAFYLTASQQRWEEYLKKGLTNPDATPEQTRVAVKAIETLNGNWRSPGGAVKFNTVTPSVTGRWFSGNQTWPWDTWKQAFAMAHFNPDIAKENIRAVFSWQIQPGDSVRPQDVGFVPDLIAWNLSPERGGDGGNWNERNTKPSLAAWSVMEVYNVTQDKTWVAEMYPKLVAYHDWWLRNRDHNGNGVPEYGATRDKAHNTESGEMLFTVKKGDKEETQSGLNNYARVVEKGQYDSLEIPAQVAASWESGRDDAAVFGFIDKEQLDKYVANGGKRSDWTVKFAENRSQDGTLLGYSLLQESVDQASYMYSDNHYLAEMATILGKPEEAKRYRQLAQQLADYINTCMFDPTTQFYYDVRIEDKPLANGCAGKPIVERGKGPEGWSPLFNGAATQANADAVVKVMLDPKEFNTFVPLGTAALTNPAFGADIYWRGRVWVDQFWFGLKGMERYGYRDDALKLADTFFRHAKGLTADGPIQENYNPLTGAQQGAPNFSWSAAHLYMLYNDFFRKQ
The following text describes a protein:
Function:
Involved in DNA repair and RecF pathway recombination.
Sequence:
MSGKTYRATGINLRRMPLGESDLLMTILTRENGLVRAVARGARKANARIGGRTEQFVVNDLQLYRGRSLDQLTQAESLRTFPGLLQDLGRLTAAQYLAEGVLQEATEGQAQEDLYDLLLVHLERLAATPSHQIAARLVHGVYQLLAVGGVAPEVHFCTVSHRPISAESAGFSVEGGGLVALECLSHERVGFRLDIEQVAALQLLADADLTPASLDWNYLWIGLERLLRRHIEFHFDRPLRAATLLEICFEPLAVPAAASPQ
The following text describes a protein:
Function:
Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids.
Subcellular Localization:
Membrane; Peripheral membrane protein.
Sequence:
MNQLNISHNWKIKSFTSITFCDHCGSMLWGICTQGFQCSDCNFSAHSHCTNLVTLHCNNNKNNSKPNEKPATITAAAASSSTTTTTTTETSTNTAASTTTTTNNIDIKNKDKTPTTSPFSSPILSSYNNNSGNEFCSNRQHKFHKTSKSITKFCNYCRETTFTISGEPVMCSECRYIAHGHCQTKVPLNCIIPYSSPINTINDGGNVRHHWVEGNLKKSKKCIHCMEPCEKSFSLAHYKCLWCHKYLHSSCFDKHNPICDFGSLSDMILPPSSIRLLSTTATTTNKIEKLIIEEQQPQLSSSPSSPRLNINNNNNNNEIIEWELIENSNMPEKVLFVFVNSKSGGQFGSTLIRKLSSLLNPLQIIDLIKCGGPDSTLQMINRYLAKHPEQTNRFRILVCGGDGTVGWLFKQMTKHLVPSTIPIGIIPLGTGNDLARSLGWGIGYDGEKLIEILKSINEAKTIQMDTWSIEMWDDDKPEDRRVIEMNNYFSIGLDAMVALGFHLARNANPQLFTGRTVNKLWYTKIGLEEFVTKNFVSLARIVKINVGTREIRVDRSIEGIIILNLGSYAGGVDLWGANRKDNQTHSDGTGNQFIDDQTLEIVGVTSLPHLGSCLSSISSPIKMGQADEIRIQVSMPSIILKDKSNEIETAFQVDGEPEPIEVRNCTFKISFFKKVSMLSNRSFKPRIENHDSDLSTFQISQSPNLYSPPSFKNPPPNLNQYQQPHQPPQSQPQPQPQPQQSLQSPQSPEPINNNTNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNNNNNNISNDLTNNSEVNPEKSTNNEKTNDNNNNNNNNINTPFEPISLPDENNNNNNNNNNNNNNNNNNNNNNETNSEKSYTNNCDEVD
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Subcellular Localization:
Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MPMRSDSRTCPYAGRNIIIDVNIQWDYPKSPPGINITSAILHPHLSKEVSALGCNAKARWHDKLDVVRALQAVHYLLDCPILRNNNACGEFMCTQQRPSTQQARSYFPDNILEFVRKAAEFGVDLKNPAEVAAKDAVLARADVCDRRTRTVDVKNTMTARSTDTPDILKHYVSDISLANAPPVAKTMQIKCTCQRELRDHLPLWMQQISDGDALVMASRDRCSCSLFNLEASLYTIKGILILDNDGNRVLCNVCCRWLCLSVCCAPACAHAPLCPQYYDDALPTVKEQRAFEKKLFQKTAKANAEIIMFDGITCVYRSNIDLFFYVFGAASENELLLATVLGAYYEAISLIVNRDTLEKASLLEQMDTVLLITDELVDKGIVLNTDAESLARIATTTKSAASSSSGEKGLSSALNKASGLIRKHLLQ
The following text describes a protein:
Function:
Toxin that seems to act by forming pores in the membrane of the cell. Has a hemolytic and a leucotoxic activity. Promotes host AMFR-mediated inflammation by mediating 'Lys-27'-linked ubiquitination of TAB3, TAK1-TAB3 complex formation and phosphorylation of TAK1/MAP3K7. In turn, activates host NF-kappa-B signaling pathway.
Subcellular Localization:
Secreted.
Sequence:
MKMNKLVKSSVATSMALLLLSGTANAEGKITPVSVKKVDDKVTLYKTTATADSDKFKISQILTFNFIKDKSYDKDTLVLKATGNINSGFVKPNPNDYDFSKLYWGAKYNVSISSQSNDSVNVVDYAPKNQNEEFQVQNTLGYTFGGDISISNGLSGGLNGNTAFSETINYKQESYRTTLSRNTNYKNVGWGVEAHKIMNNGWGPYGRDSFHPTYGNELFLAGRQSSAYAGQNFIAQHQMPLLSRSNFNPEFLSVLSHRQDGAKKSKITVTYQREMDLYQIRWNGFYWAGANYKNFKTRTFKSTYEIDWENHKVKLLDTKETENNK
The following text describes a protein:
Function:
Endogenous secreted peptide that acts as elicitor of immune response and positive regulator of defense response. Amplifies the immune response triggered by flg22, the active epitope of bacterial flagellin. Acts as a negative regulator of root growth.
Subcellular Localization:
Secreted, extracellular space, apoplast.
Sequence:
MMMNKNVLSSILFFMLIGSVLVESRPLGLTKTEEKFVASLFDGLSLGSIKDSGPSPGEGHKVVDRKDTFRFVKHSGPSPSGPGH
The following text describes a protein:
Function:
Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens, such as bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma gondii. Confers protection to several pathogens, including the bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma gondii.
Subcellular Localization:
Cytoplasmic vesicle.
Sequence:
MESGPKMLAPICLVENNNEQLLVNQQAIQILEKISQPVVVVAIVGLYRTGKSYLMNHLAGQNHGFPLGSTVQSETKGIWMWCVPHPSKPNHTLVLLDTEGLGDVEKGDPKNDSWIFALAVLLCSTFIYNSMSTINHQALEQLHYVTELTELIKAKSSPRPDGVDDSTEFVSFFPDFIWTVRDFTLELKLNGHPITEDEYLENALKLIQGNNPRVQTSNLPRECIRRFFPKRKCFIFDRPTNDKDLLANIEKVSEKQLDPKFQEQTNIFSSYIFTHARTKTLREGIIVTGNRLGTLAVTYVEAVNSGAVPCLENAVITLAQRENSAAVQRAADYYSQQMAQRVKFPTDTLQELLDMHAACEREAIAIFMEHSFKDENQEFQKKFMETTMNKKGDFLLQNEESSVQYCQAKLNELSKGLMESISAGSFSVPGGHKLYMETKERIEQDYWQVPRKGVKAKEVFQRFLESQVVIEESILQSDKALTDREKAVAVDRAKKEAAEKEQELLKQKLQEQQQQMEAQDKSLKENIAQLKQKLQMEREQLLREQIMMLEHTQKVQNDWLHEGFKKKYEEMNAEISQFKRMIDITKNDDTPWIARTLDKLADELTAVLSAPAKLIGHGVKGVSSLFKKHKLPF
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity).
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane.
Sequence:
MSSKLFCLRSFPSVQRTAWQRLVLPSTRKFSLTPTTFDKTPSGRIPPDQKAANIISSVPSTSLLTKSGVLTVTAAALATAISKGIYVVNDESIVVASFLGLVGVFGTLGRKAYNEWSDKTIAKIGGIMQAARNDHTSAIRERIDQVASLQEVESVTQALFHTSKETARMEAEIFELEQRVALAKEAKSVLDSWVHHEANVRAEQQERLVEDVLARVNSKVSTQKFQQDALNESLGEIEKVLASA
The following text describes a protein:
Function:
Cardiac hormone which may function as a paracrine antifibrotic factor in the heart. Also plays a key role in cardiovascular homeostasis through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MLGSRLTFCYGFLHLLLQTHVLVCAYPNSDAVVRDTDTLKTLLQRLEEAYLLTVRAESLERGQVADGMPEEQSYEAEDGSQERLAEESAIGYITLDAEEARLPDRNSNGFLNPLRNTKRYSGCFGRRLDRIGSMSALGCNGGSRLSYKRS
The following text describes a protein:
Function:
Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are part of the biosynthesis pathway of coenzyme B. Can also catalyze the hydration of maleate to (R)-malate, and that of cis-aconitate. Cannot catalyze the hydration of citraconate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate.
Sequence:
MIIKGRAHKFGDDVDTDAIIPGPYLRTTDPYELASHCMAGIDENFPKKVKEGDVIVAGENFGCGSSREQAVIAIKYCGIKAVIAKSFARIFYRNAINVGLIPIIANTDEIKDGDIVEIDLDKEEIVITNKNKTIKCETPKGLEREILAAGGLVNYLKKRKLIQSKKGVKT
The following text describes a protein:
Function:
Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MAHYAIGDIQGCFDELTALLGKIGFNHGTDTLWLTGDIVNRGPKSLETLQFCIRHENSVQIVLGNHDLHLLAVGCGEGAPKRSDTIEPILKHPDGKKMLDWLRAQPLLIREGSRVMVHAGILPQWRITKAESLAREAEAELRGKKYVKFFSKMYGNKPAAWDEGLKGYARLRFIVNAFTRMRALTFKNELDFDYKSTVKKMPPYLRPWFKAPDRQNLDAHHLRTLVLAGLHECRQRHLAGHRRAVGRTADRRQPRNGRNYPSPSRRRHRLEKLRKITDRPTMHKILPIAHVLSRLGMLFSFILLIPAALSYAFSDGAYTAFATTATVTLSGSCIVRLATLRFRRELRPRDGFTLVLMLWLAFAAMAAMPMYLYFPNMGFTDAFFESMSGLTTTGATVIPHVDGLAPSVNFWRHMLNWLGGMGIIVLAVAILPMLGVGGTQLFKAEIPGIDKESKMSPRISQVAKKLWFGYTLITILAAACLHFAGMGWFDAVCHAMATLSLGGFSTHDASIAYYNSPLIEAVIIVFTIVGGINFANHFAALNSRSLKTYWKDEECRTMLLLLSGSILAAALYLWHTGYYAGFTESLRYTAFNFVSIGLANGLANTDFAQWPLLISLWMFFLANILANSGSTGGGIKTIRALVLFKFSLREMMVLLHPKAVRTVKISGKAIPDRLALTVMSFIFIYFMTVVLFSFLLMASGMEFTTAFTAVIACITNAGPGLGEVGPAGNYAGLDVMQKWICVTAMLLGRLEIFTVFILFTPAYWKK