lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Amino acid aminotransferase showing activity for D-Asp and D-Ala as amino donors with 2-oxoglutarate as an amino acceptor. Can also use D-Met, D-Tyr, D-Phe, D-Gln, D-Trp and D-Asn as substrates, but no activity with L-Asp, L-Ala, L-Leu, L-Ile or L-Val. Also catalyzes the reverse reaction where an amino group is transferred from D-Glu to pyruvate or oxaloacetate to produce D-Ala or D-Asp, respectively. Also involved in folate biosynthesis, acting as an aminodeoxychorismate lyase converting 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate (PABA).
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MAGLSLEFTVNTWNLRSLSQVPCPLRHGFRFPRRLTRRRTILMCSDSSSQSWNVPVLSSYEVGERLKLARGGQQFLAMYSSVVDGITTDPAAMVLPLDDHMVHRGHGVFDTALIINGYLYELDQHLDRILRSASMAKIPLPFDRETIKRILIQTVSVSGCRDGSLRYWLSAGPGDFLLSPSQCLKPTLYAIVIKTNFAINPIGVKVVTSSIPIKPPEFATVKSVNYLPNVLSQMEAEAKGAYAGIWVCKDGFIAEGPNMNVAFVVNGGKELVMPRFDNVLSGCTAKRTLTLAEQLVSKGILKTVKVMDVTVEDGKKADEMMLIGSGIPIRPVIQWDEEFIGEGKEGPIAKALLDLLLEDMRSGPPSVRVLVPY
The following text describes a protein:
Function:
Required for 60S pre-ribosomal subunits export to the cytoplasm.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSTAAELLALQSNIKKDPDGYKDEFLLQYRHYQALLEIFKLKPSKDSREFGEVVMFMAQVSRAYPKTMTGFAAEVAGLLDTHHQELDSTLRRTLVGALILMRNRAQVDAMTVLPLFFRLFRCQDKALRQQLFRHIVSDLKAANKKCRNERLNRAVQNFMYTVVSDDNEAAAKRGLAVLTEMWRRHVWRDARTVNVIASAAFHKSPRVLLAVMKFFLGQDRDDEDGSDKEGEGEGDEEDAKPKGPSKEDIYSAYHKGTSSSKKKKQKKLKRVIATVKKADRRKSAAGGGAESFAAIHLLHDPQAFAERLFGRLSGGGERFETRLAVMAVVSRIIGVHKLLVLNFYPYLQKYIAPHQRDVTQVLAALVQAAHDLVPPETLAPVLRQLVDQFVHDKARPEVMTVGLKTVRELVLRCPLVMEADLLTDLAQYKKFREKQVATAARSLIGAFRDINPEMLAKKDRGRGADMALKPRDYGDARVATRVDGAELLEAALAEGRTGSDGDEVDLGLDDSSSDDDDDGDGGSGGWEDVSEEEGDGGAKEGAGEGEGEEGGEDSDLESLSGEGEGEEDGSSDWEDVSEEGEEEEEAAAAAGKGKAKGKAAAKAKAKPAATAGRKGKKGAPANEDDEEEEDVEEEESGSDADLEDLDSEESEEASEEDEEDDGGRRGKRGGKPQPAKPKVEAKPDSIASLKRKLAEAKEKAAAKRAREEPAGDGEGGEEGQAPAGVPIEAERILTQEDFDRIKRLKQKALVEAALAKAGVTSAASKAKKQRALESAEEEAAELLALQERLTTIGESKVNAADLTGKHKARKDKEARLASVLEGREGREKFGARSSLKKKKTAGLSEREKQRRKAMPMAARVQQIRRRNAAARGKKMGKNFKGHVRG
The following text describes a protein:
Function:
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Subcellular Localization:
Cytoplasm.
Sequence:
MSEQTQQQNSEEAVENVEAVETVETVGNADGVQEQAAAEPAYEDLQARIAELEAQLKDEQLRALANEQNLRRRHQQEIADTHKFAGQKFAVEMLPVKDYLEMALLDQSGNFDALKMGVQMTLNELQKAFDATQIKEINPKAGDKLDPNIHQAMQAVASEQEPNTVVGVMKKGYTLSDRVLRPAMVTVAQKEA
The following text describes a protein:
Function:
Involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles.
Subcellular Localization:
Cytoplasm. Endosome.
Sequence:
MKTHLLVVPSKKTEEVNWVKPLNNYLLSIYGNTLQYQDDINSLNKLRQDIRGVNADDTGLKLYYSYYSKLELIDLRIPFHDLNKSKKLQFEWFDSFSSLPYTQNSLAFEKANVLYNIGAILSRFAQFKYNESQQLNGPEGETAFKQSISMLQQSSGIHQFINKNFLHAPSQDLAQSTIKFLSKLMMAQSQEIFTLKVISGDLNQSKNSLIAKLCKSTSVLYEDCYNMINKNKKEGFKITNESYDGNDYEDDLDDDDCDDLEGFLERPEDTEDSDNRYVAAELDSSWISIIYFKYEYYKSLAYYFNGLHLDANRKYGDAIAYLTKSQEVLNGVHSSTLKQVSKGSGDVYELLDNYKYQKDAVTIRLNDLNKDNDLIYHDIVPNLVTLPEIKPMDSTKIIKLGDNAMFHEINEKNYNNFLVNVVPVNIHELSSYYSEEKSQYLRNEIDHFEVSNEEVSSVLEYLKLPKALVSIKESLRGTSSKGNTRNIDELLSQSVIDKVNEISSQYSNDIQRKNTIENSRKEIYQLIKFLTENNCQDDAIQLKKILYDASVSDTKLFALVDETYHQTLGKGIQSTEFKSLFKTVDNKSSNQDSEISLLDIIDDDDDDNTNQDKQIKNIEDYLNDLNNIKQAKFKLIEKLKKEIHNDDISDILVLNMKLKSTNEIKSIIFPEELKKFNPFTNELDKLITNEKSIIEQLKSRWNQLISNPQIKNLQTETNSKNRLIISQSEKIDQFYGNWLKYHNGLIAGEKFYNQLLDQFKNFRNNIDNQLNQGMRSLNIGQQFPTQPMLNRTQSSGLQSNYTGQSSISHSGSLSGQPSGGYNQPQPQQQQLQQQQQQQQQAQFSGAYNQQYSQPHGGYTQFQGYGQGQGQSQTGYQRQPPPPPPQLPPKQSMGSYNFATTLQQQQLPPQQQQQPQQQRTPQNESNLIYDNPSTYNPNMYNFFSSK
The following text describes a protein:
Function:
Structural component of the gap junctions.
Subcellular Localization:
Cell junction, gap junction. Cell membrane; Multi-pass membrane protein.
Sequence:
MLAELSTLKGIVKVDVVKIDSNIFRCHYKLTVIVLTISAMLISLKQYVGDPIDCIINAEKSPVESDVLDNYCWIHSTHTLPNQPGMKTNGSRPIPGLGTPQEGEQMIYHKYYQWVGFFLIFEAITFFIPRLVWKFSEGGRMRTLLEDLRFSPVETPEQKNAKASLVDYLFTNVCQHQVYASSYFVCEALNAIIILGNIFLVDAFLGGEFLEYGGNVVAASVMDPEDRIDPMSYVFPKLTKCLFKMYGPSGTIQQYDALCILPVNILNEKVFIFLWFWYVILAILTGIDLVVRGITLLFPRVRLFFLKRQAGRNIDFDHVETVFRRCQIGDWFVLMLISSNINQWTFQEILRGLALKFRGKDI
The following text describes a protein:
Function:
Oligopeptidase that may be involved in the degradation of proteasome-generated peptides (By similarity). Binds salicylic acid.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MASEDTLSSNPLLQNFDFPPFDSVDAHHVRPGIRALLQQLEAELEQLEKAVEPSWPKLVEPLEKIIDRLSVVWGMINHLKAVKDTPELRAAIEEVQPEKVKFQLRLGQSKPIYNAFKAIRESPDWNSLSEARQRLVEAQIKEAVLSGIALEDDKREEFNKIEQELEKLSHKFSENVLDATKKFEKLITDKKEIEGLPPSALGLFAQAAVSKGHETATADTGPWLITLDAPSYLPVMQHAKNRALREEVYRAYLSRASSGDLDNTAIIDQILKLRLEKAKLLGYRNYAEVSMATKMATVEKADELLEKLRSASWDPAVQDIEDLKSFAKNQGAAEADSLTHWDITFWSERLRESKYDINEEELRPYFSLPKVMDALFGLAKTLFGIDVVPADGVAPVWNSDVRFYCVKDSSGNPTAYFYFDPYSRPSEKRDGAWMDEVFSRSRVMAQKGSSVRLPVAQMVCNQTPPVGDKPSLMTFREVETVFHEFGHALQHMLTKEDEGLVAGIRNIEWDAVELPSQFMENWCYHRDTLMSIAKHYQTGETLPENVYKKLLAARTFRAGSLSLRQLKFATVDLELHTKYMPGGAETIYEVDQRVSIKTQVIPPLPEDRFLCSFSHIFAGGYAAGYYSYKWAEVLSADAFSAFEDAGLDDIKAVKETGQRFRNTILALGGGKAPLKVFVEFRGREPSPEPLLRHNGLLAASA
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase which may be involved in endosomal trafficking. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.
Subcellular Localization:
Cytoplasmic vesicle membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein.
Domain:
The RING-CH-type zinc finger domain is required for E3 ligase activity.
Sequence:
MTTSRCSHLPEVLPDCTSSAAPVVKTVEDCGSLVNGQPQYVMQVSAKDGQLLSTVVRTLATQSPFNDRPMCRICHEGSSQEDLLSPCECTGTLGTIHRSCLEHWLSSSNTSYCELCHFRFAVERKPRPLVEWLRNPGPQHEKRTLFGDMVCFLFITPLATISGWLCLRGAVDHLHFSSRLEAVGLIALTVALFTIYLFWTLVSFRYHCRLYNEWRRTNQRVILLIPKSVNIPSNQQSLLGLHSVKRNSKETIV
The following text describes a protein:
Function:
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane.
Sequence:
MMQMSEYKVLPQNAPQDENGAVVLQPQAANVGNNANGPENWMSIPVGMPNCPQGLEYLTALDQLLVSQKIEKLELLTGFETKNRFKVKNSLGQNVYFAYEESDCCTRNMLGRSRPFEMKILDNFQNEVLHLYRPFKCDILCCFPSCMNAVEVSAPPGQVIGSVSGLHLHAAQVQHQEHMRRYRPADRGTRLSLQVLQRYQLQGIERQQRGDRQNQQTMVRTGKGAVHRCGLLQRHLPPESGCPHEGAHIRSALFD
The following text describes a protein:
Function:
G protein-coupled receptor activated by the neuropeptides vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating polypeptide (ADCYAP1/PACAP). Binds VIP and both PACAP27 and PACAP38 bioactive peptides with the following order of ligand affinity VIP = PACAP27 > PACAP38. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors. Activates cAMP-dependent pathway.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MRPLSPPPAGWFCVLAGVLACVLGPVGSWAVGLQQEECDYLQMIKVQHKQCLEEAQLENETSGCSKMWDNLTCWPATPRGQVVVLACPLIFKLFSPTQGLNVSRNCTDEGWTPLEPGPYPIACGMDDKASGLDEQQTVFYNSVKTGYTIGYSLSLAALLVATAILSLFRKLHCTRNYIHMHLFISFILRATAVFIKDLALFDSEESDHCSKGSVGCKAAVVLFQYCVMANFFWLLVEGLYLHTLLAVSFFSERKYFWGYIFVGWGVPSTFIMVWTVVRIHFEDYGCWDTIHSSLWWIIKAPILASILVNFILFIRIIGILVQKLRPPDVGKSDNSPYSRLAKSTLLLIPLFGVHYIMFAFFPDNFKAEVKMVFELIVGSFQGCVVAILYCFLNGEVQAELRRKWRRWHQQGVLGWDSKYQHPSGGSNGDTCSTQVSMLTRVSPSARRSSSFQAEVSLV
The following text describes a protein:
Function:
Catalyzes the reversible oxidation of malate to oxaloacetate.
Sequence:
MVKIAFIGVGKIGQTIAYSVIFDGLASEAILYDIVPELPEKFEHELRHAIATRGLSTEVIGTNSLDDVTNADIILIMAGKPRKPGMSRRDLFIDNAKIQIDLAKQLPPKNPGALYIMVANPVDMMASVFMRFSKQFTISTGDAVETMRLRSYIAKKLKVPANKVTGYVAGEHGEDAVVLWSTVKVNGKPFEEVAKGLTKEEVENYVKSIPGEIIRVMGGTTWGPATIIKDIVRSVVFNEGRVMSIATPRTYQGEIIHISVPIVVGAEIGPSLEGVLPESDRQRLNKSVEDFYRVYKENLDHLLQTVKQ
The following text describes a protein:
Function:
Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MPVAVMAESAFNFKKLLDQCENQELEAPGGIATPPVYGQLLALYLLHNDMNNARYLWKRIPPAIKSANSELGGIWSVGQRIWQRDFPGVYSTINAHQWSETVQPIMEALRDATRRRAFALVSQAYTSIVADDFAAFVGLPVEEAVKGVLEQGWQADSSTRMVMPKKPVAGALDVSFNRFIPLSEAAPVPPIPNEQQLARLTDYVAFLEN
The following text describes a protein:
Function:
Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to murein peptidoglycans (PGN) of Gram-negative bacteria and activating the imd/Relish pathway. Has no activity against on Gram-positive bacteria. Binds to diaminopimelic acid-type PGN (DAP-type PGN), an activator of the imd/Relish pathway. Functions synergistically with PGRP-LC in producing resistance to E.coli and B.megaterium infections, which have the DAP-type peptidoglycan. Acts both upstream and in parallel with PGRP-LC in the imd/Relish pathway, and is required for infection-dependent activation of melanization. Required for Relish processing and nuclear translocation following proteolytic cleavage. Its localization suggests a role in the recognition and subsequent activation of the signaling at the first point of contact with invading bacteria.
Subcellular Localization:
Secreted. Note=However, no signal sequence are predicted by sequence analysis tools.
Sequence:
MSESGIKKLSQERTREWLASQEDEELESIAESSVVDSLDYDYTEEEEDADQNTSEEISTMTLGTQIATKKHSIISDTIRDLMNSINSIQTLGNVNISNSTNVHIGNVTNINGNIQIIADGLTQNRRDRRHVSPPRDNAPKTPTHFEDDYQDESEERVRSDVFIRRQKFKIPKELSAIIPRSSWLAQKPMDEPLPLQLPVKYVVILHTATESSEKRAINVRLIRDMQCFHIESRGWNDIAYNFLVGCDGNIYEGRGWKTVGAHTLGYNRISLGISFIGCFMKELPTADALNMCRNLLARGVEDGHISTDYRLICHCQCNSTESPGRRLYEEIQTWPHFYNIEEEEQ
The following text describes a protein:
Function:
Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. Also recognizes sulfated glycans. Also involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. Ubiquitination of CHEK1 is required to ensure that activated CHEK1 does not accumulate as cells progress through S phase, or when replication forks encounter transient impediments during normal DNA replication (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MALVSINQLPENILLEVFMHVPARQLLRNCRPVCCLWRDLIDLVSLWKRKCLREGYVTEDWDQPVSDWKVFYFLCSLRRNLLRNPCAEEDMKSWKIDSNGGDQWKVESLPGAHGTGFPDSKVKKYFVTSYDMCLKSQIIDLKAEGYWEELLDKFRPDIVVKDWFAPRADCGCTYQIRVQLASADYLVLASFEPPPVTIHQWNDAKWTEVSHTFSDYPPGVRHIFFQHGGKDTQFWAGWYGPRVTNSSVVISHRVTRNPPHAMAQP
The following text describes a protein:
Function:
May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase.
Subcellular Localization:
Membrane; Single-pass type III membrane protein.
Sequence:
MDRWYLGGSPKENEDPFYYDYETVRNGGLIFAALAFIVGLVIILSKRFRCGAKRQHRQIPEDGL
The following text describes a protein:
Function:
Mitochondrial protein enriched in neurons that acts as a regulator of mitochondrial respiration. Associates with the ATP synthase complex and facilitates ATP synthesis. May be a chaperone protein involved in the turnover of the subunits of mitochondrial complex I N-module. It facilitates the degradation of N-module subunits damaged by oxidative stress, and contributes to complex I functional efficiency (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MAAARCLGWTLSPLWRWWQVRGLPPSSATGLCSRGRTYSRTALYELLGVPSTATQAQIKAAYYRQSFLYHPDRNPGSAEAAERFTRVSEAYLVLGSTILRRKYDRGLLSDQDLRGPGVKPSKTPVADPAPPRPPPYTPRAPGGSRASPGDGRTMFDFDAFYQAHYGEQLERERRLRARREALRKKQENQANKGTSWDDTRDATFFVVLFLIFVFVGFRI
The following text describes a protein:
Function:
Part of a binding-protein-dependent transport system.
Subcellular Localization:
Cell membrane; Lipid-anchor.
Sequence:
MNNLFALCQRSAVIFSIIFTVVACDKLDSPKPISPQIETQKNTQLESNRVELKRGVYSDLTLQPWQAQSEEQTQLLRDLFEGLTAYDVQGNLVPAVAENWQTEDNKTWIFTLRENAKWSNGEPITASDFVQSWQTLSQSESPLKNYLAFMNLKNAKAVLEKALPVESLGLFAENDRTLRIELDKASPYLPSMLAHVSLLPHYAKSTEIFISNGAYQLQRQAENQHILTTNPYYWAKEKVIFQQVKYQKISVDADLSDFDVVMNPKKVNQNIQDYPQLCTYFYEFNLSDPVLQKSAVRKAIVSMISTNNLVADIAHLYPNNTFLPKSMLGEQESVWEPVVAEQLFSQNQISETRPLKLRIRYDDLSLNQTIAMRLNHQLSQSDLLRVENQGMSWQELQTARTKGDFQLIRSGWCADFNDPAAFLNLFYSKSPDNKNGYKNAEFDRLFESAMTTISEKVRLENYAKLKGIVQQEHLVLPIFQYSTPVYLVPSIMGAQVNSVGVIYSKDLWRKVQSQ
The following text describes a protein:
Function:
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Sequence:
MEHKIREEMRVLPSIDPQFEIERRVAFIKRKLTEARCKSLVLGISGGVDSTTCGRLAQLAVEELNQQHNTTEYQFIAVRLPYGEQKDEDEAQLALSFIRPTHSVSVNIKAGVDGLHAASHHALANTGLIPSDPAKVDFIKGNVKARARMVAQYEIAGYVGGLVLGTDHSAENITGFYTKFGDGACDLAPLFGLNKRQVRLLAKTLGAPEQLVYKTPTADLEELAPQKADEAALNLTYEQIDDFLEGKAVPAEVSQRLVAIYHATQHKRQPIPTIYD
The following text describes a protein:
Function:
Chromatin-associated protein which contributes to the modulation of chromatin structure (such as super-helical structure of DNA) and function (By similarity). Binds to chromatin of protein-coding genes throughout the genome to regulate nucleosome occupancy and chromatin accessibility, and to modulate the expression of target genes (By similarity).
Subcellular Localization:
Nucleus. Nucleus, nucleolus. Note=Associates with chromatin (By similarity). Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei (By similarity).
Sequence:
MATETLDEKTPEVNSPAKEEIDVVPKEEKEVEKEKVDSPRIGEAEEEKKEDEEEGEAKEGELGEKDKEDDVESEEEEEEEEGSGSKKSSEKETVTPTSERPTRERKKVERFSLSTPMRAPPSKSVSIEKGRGTPLREIPNVAHKLSKRKADDNLMLLHTILFGKKAKAQMVKRNIGQFSGFAWSEKEEEKQRARIKEKIDKCVKEKLIVFCDVLDIPISRSNVKKEELAVKVLEFLESPKETRDVIIADQEKAKKRKSTPKRGKSGESSDTPAKRKRQTKKRDLPSDTEEGKDEGDADSEGTNDPHEEDDAAPEEESDHEKTDTDDEKDEVEVEKPSKKKSSSKKTVEESSGSKGKDKQPSAKGSARSGEKSSKQIAKSTSSPAKKQKVDHVESSKEKSKKQPSKPQAKGSKEKGKATKKGKAKAEPTRKEMLEVVSKILKEVDFNTATLSDILQKLSDHFGVELSHRKPEVKDVITEAINAMTDDEEEDEEEEAEAGSDKEKEEVKGEEEEEKAEAESDKEKEKEEPKD
The following text describes a protein:
Function:
Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. May play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MNTPRCSGVCAMMRLLALFIHVLSTTAKRHVVYWNSTNTRLTGDDYSVQVNLSDYLDILCPHYPGDHPSGASVETLALYLVAESQFRGCVDTKEAIKRWECNQPFAPFGPVRFSEKIQRFTPFSLGFEFLPGHHYYYSSLSTDDGPPLPCMKLRVTVCCPPTTAGSSRQEATETPSHSTTVQNMTLTQLFLLLIPFLLSYFL
The following text describes a protein:
Function:
Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. May act as a zinc sensor that controls, via c-di-GMP, post-translational events. Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to other classes of translation inhibitors. The c-di-GMP produced by this enzyme up-regulates poly-GlcNAc production as well as the biofilm synthesis protein PgaD, although c-di-GMP is probably not the main inducing principle. C-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.
Domain:
Contains an N-terminal CZB (chemoreceptor zinc binding) domain and a C-terminal GGDEF domain.
Sequence:
MIKKTTEIDAILLNLNKAIDAHYQWLVSMFHSVVARDASKPEITDNHSYGLCQFGRWIDHLGPLDNDELPYVRLMDSAHQHMHNCGRELMLAIVENHWQDAHFDAFQEGLLSFTAALTDYKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNAEPLNLYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIIIVKAANDEEACRAGVRICQLVDNHAITHSEGHINITVTAGVSRAFPEEPLDVVIGRADRAMYEGKQTGRNRCMFIDEQNVINRV
The following text describes a protein:
Function:
Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates to a subcomplex that specifically deubiquitinates histones. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery.
Subcellular Localization:
Nucleus, nucleoplasm.
Sequence:
MSASSQSKPDPIRWENVPETEIRADAEAALEMSGKTKEIRQFLSQNRAIEDWRKEIRELCRNMINEIGIDNVNPDMLYDLLAAQGHDQLPAEVVTEVTTRIKTFLNTQFEEHP
The following text describes a protein:
Function:
ATP-dependent protein-folding chaperone for the eIF2 complex. Binds to the gamma subunit of the eIF2 complex which allows the subunit to assemble with the alpha and beta subunits.
Subcellular Localization:
Cytoplasm.
Sequence:
MPLLDPDTRSPAESSAAQPQRLPFPPVTYSHILHCSYHHWQPRYRTLTPKSRAIPLTPSFVSYLRADGIVLPPETTRPQGDDDLDTFSDDGADEESDPSVEWQEIHSQIKSTISEFGGKVTPKLNWSAPKDAVWMSATNDLQCRTPNDIYLLLKSSDFITHDLEHPFDGCVPDTDDSSEAPATQPDIPYHLVLRKYVNFNPSLEFRCFVRNRVLLCMCQRDQNHFDFLFSLRDTLRSRIQAFFDEKLKDTFPDPNFVFDVYIPEPHQRVWLIDINPWADRTDPLLFSWLEILQMKDPIGIKEEDADGPEESFVRLSLNGANPTVVEVNGDEDCESEEEDVGSADDGDDLPFLPEFRLVKRDDPEAYSFSTPQYSAHKLPREVVDASLSGPGGMSEFLGKWQDILAKQTQEDTDSDDGR
The following text describes a protein:
Function:
Antimicrobial activity against Gram-negative bacterium E.coli.
Subcellular Localization:
Secreted.
Sequence:
ALFSILRGLKKLGKMGQAFVNCEIYKKC
The following text describes a protein:
Function:
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
Subcellular Localization:
Cytoplasm.
Domain:
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex; The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.
Sequence:
MNYNPLHLLPLPPTALDPKPIPTSLTLDPFSDVLWVGASSGIVSALCSPLTLARNVHFPAHGCKIGGGGFSAQGVSAVREVRVTDRDVWTLTEGGIGGRKRGGAPKWIVSDVTRSLRTMSPNPTNSHELITGGSGSLLLANTARGEVVRSIENSSPVVKLAPLHRTVLAAGLSGQVTVLDPRTGFKAAQNISPVQAHTGGLSGADVQGNIVATWGWTHMQGHPLPDPLIRLYDVRALRPLPPISFSSGPAFVLLHPSSSSHIVVSSQQGMLQTIDMSLGPSATVFQQLDVSSYITSMALSSRGDYLAFGDGDGQLHVWTTNETGENAAVDENGSIVLPPFNGYDGVKPEWPDQVDPLPTIAWEESTPLNLVGMPYYNEALLSQFPSECYATSTSPLFNPPATIPQPVLSSMKMVDFVGYAPNPKELRGKRYVLRAVPGAEGRARGKGRRDSGPRFRSEKDKKGTYKDKEEIEEELNDGEVPKYYRKVEIKYSKFGIEDFDFEFYNRTNYSGLETDILNSYTNSLLQALHYTLPLRAIATAHICVDCKKEHCLLCEAGFLFRMLEDAKGRNCQASNFSRAFSATSQAYALGLMDENTNSKSTAPYGSLIQNFNRWLLSTFSTESIVDGETFHLRPFPQKTSGLDGLSMNDGPSAIDQVLGVKIKTTNTCRHCGFVSSRDSTLHVVDLVYPKKMNPRLSFSDILRSSLIRDSTTKAICSSCKAFAPLDSRRSLSPSSGHPLPPVLSVNAMVTNSDVYGFWKDKKDVKEKDGVRRFLPKRVTIREVGKLENGQEEGVKYSIRSMVVQIQESPDAVAHLVSFVKMPSKDGSSAWIMFNDFLVRPVSEDEVLSFPDQWKVPAVIILERENAEELLNLEVLPKELDREILFKDVSIAWNRKQDMIKHKILQREEMPKRGTLVAIDAEFVALQQEEMEFRSDGTKNILRPSHMSLARVSVLRGEGEMEGKPFIDDYIHTSEAVVDYLTEFSGIKAGDLDPNNSPHTLVPLKVAYKKLRLLVDLGCIFVGHGLSKDFRTINIFVPPEQVMDTVLIYTLPGSQRKLSLRFLAWYLLHQDIQTNSHDSIEDAHFALLLCKLWMDYASESEEAFEIVMEDIFAEGKKLAFKPPSSAGNMMAEQQLSPVSFPPLSNGDQTVARAVVKSRMATPPPPTKLGLPQWASQNSPSPLRR
The following text describes a protein:
Function:
Involved in pre-mRNA splicing as component of the spliceosome. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs.
Sequence:
MTTAARPTFEPARGGRRKGEGDLSQLSKQYSSRDLPSHKKIKYTQTTQDAPEEVRNCDFRRELEERERAAAREKNRDRPTREHTTSSSVSKKPRLDQIPAANLDADDPLTDEEDEDFEEERDDDDTAALLAELEKIKKERTEEQARKEQEQKAEEERILSGNPLLNLTGPSQPQTNFKVKRRWDDDVVFKNCAKGIDDQKKDKRFVNDTLRSEFHKKFMEKYIK