lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Also regulates the migration of developing neurons. Participates in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway. Phosphorylates reticulophagy regulator RETREG1 at 'Ser-134' under endoplasmic reticulum stress conditions which enhances RETREG1 oligomerization and its membrane scission and reticulophagy activity (By similarity).
Subcellular Localization:
Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Synapse. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Colocalizes with the cortical actin cytoskeleton by binding to F-actin in hippocampal cells.
Domain:
The CAMK2 protein kinases contain a unique C-terminal subunit association domain responsible for oligomerization.
Sequence:
MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSVGRQTTAPATMSTAASGTTMGLVEQAKSLLNKKADGVKPQTNSTKNSSAITSPKGSLPPAALEPQTTVIHNPVDGIKESSDSTNTTIEDEDAKARKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRPDGKWQNVHFHCSGAPVAPLQ
The following text describes a protein:
Function:
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Sequence:
MDSKVVIYTDGACAGNPGPGGWGALLQFNDTSKEIFGHELDTTNNRMEITAALEALRILKKSCNVEIYTDSKYLQQGITAWIHNWIKNNWCKSNNEPVKNADLWQKLYAELNKHTIIWKWVKGHANNSGNIAADKLAMQGRETAIEILKCRG
The following text describes a protein:
Function:
Sequence-specific RNA-binding protein which acts as a translational repressor in the basal unstimulated state but, following neuronal stimulation, acts as a translational activator. In contrast to CPEB1, does not bind to the cytoplasmic polyadenylation element (CPE), a uridine-rich sequence element within the mRNA 3'-UTR, but binds to a U-rich loop within a stem-loop structure. Required for the consolidation and maintenance of hippocampal-based long term memory. In the basal state, binds to the mRNA 3'-UTR of the glutamate receptors GRIA1 and GRIA2 and negatively regulates their translation. Also represses the translation of DLG4, GRIN1 GRIN2A and GRIN2B. When activated, acts as a translational activator of GRIA1 and GRIA2. In the basal state, suppresses SUMO2 translation but activates it following neuronal stimulation. Binds to the 3'-UTR of TRPV1 mRNA and represses TRPV1 translation which is required to maintain normal thermoception. Binds actin mRNA, leading to actin translational repression in the basal state and to translational activation following neuronal stimulation. Negatively regulates target mRNA levels by binding to TOB1 which recruits CNOT7/CAF1 to a ternary complex and this leads to target mRNA deadenylation and decay (By similarity). In addition to its role in translation, binds to and inhibits the transcriptional activation activity of STAT5B without affecting its dimerization or DNA-binding activity. This, in turn, represses transcription of the STAT5B target gene EGFR which has been shown to play a role in enhancing learning and memory performance (By similarity). In contrast to CPEB1, CPEB2 and CPEB4, not required for cell cycle progression (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Synapse. Cell projection, dendrite. Postsynaptic density. Note=Predominantly cytoplasmic in unstimulated neurons but translocates to the nucleus following neuronal stimulation. Nuclear import is mediated by importin IPO5.
Domain:
The N-terminal Gln-rich region is required for the formation of amyloid-like oligomers and for the stability of long-term potentiation and spatial memory.
Sequence:
MQDDLLMDKSKTQPQSQQQQRQQQQQQQQLQPEPGAAEAPSTPLSSEIPKPEDSSAVPALSPASAPPAPNGPDKMQMESPLLPGLSFHQPPQQPPPPQEPTAPGASLSPSFGSTWSTGTTNAVEDSFFQGITPVNGTMLFQNFPHHVNPVFGGTFSPQIGLAQTQHHQQPPPPAPQPPQPAQPPQAQPSQQRRSPASPSQAPYAQRSAAAYGHQPIMTSKPSSSSAVAAAAAAAAASSASSSWNTHQSVNAAWSAPSNPWGGLQAGRDPRRAVGVGVGVGVGVPSPLNPISPLKKPFSSNVIAPPKFPRAAPLTSKSWMEDNAFRTDNGNNLLPFQDRSRPYDTFNLHSLENSLMDMIRTDHEPLKGKHYPNSGPPMSFADIMWRNHFAGRMGINFHHPGTDNIMALNTRSYGRRRGRSSLFPFEDAFLDDSHGDQALSSGLSSPTRCQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQEESSVQALIDACLEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHNDIDKRVEVKPYVLDDQMCDECQGTRCGGKFAPFFCANVTCLQYYCEYCWASIHSRAGREFHKPLVKEGGDRPRHVPFRWS
The following text describes a protein:
Function:
Probable ATP-dependent RNA helicase involved in RNAi-mediated gene silencing. Specifically required in the endogenous siRNA pathway for biogenesis of secondary endogenous small interfering RNA (siRNA) intermediates called 22G-RNAs. May associate with and recruit rde-10 to primary siRNA-targeted mRNA for secondary siRNA synthesis. May be recruited to target mRNAs by rde-1 and/or ergo-1.
Subcellular Localization:
Cytoplasm, perinuclear region. Cytoplasmic granule. Cytoplasm. Cytoplasm, P-body. Note=Colocalizes with pgl-1 in perinuclear P granules. Colocalizes with rsd-6 in a subset of germline and embryonic foci.
Domain:
The C-terminal region is necessary for localization to P granules.
Sequence:
MSSFGNNAGGGGREYHDDRSNRDHRHGNGGSDAGQRRREDHNSSYQSYRRPDGRQDSYGGGHQGNHGNSYGRREDDRSHSRDNHGGSRYGERDDRGNNGRSADNRYSQSNYNYDSNRGGQHYQRDNHGSKDDRGPMNQYNDHGSNHNSNSRNDQYRQGSYQGDGHSGYRRDDDRRRNDNDQARPYQSNRDSDRNSPRDHHNYNSQSSPRSHQGGQDRYSAPKEDNQRRYDNHQGGHDSYRGQNSGGYSGNNSGEYRNDYRSQQDSRDHRSGGNNSSSGFKNDGGFGGNDNRGFGNNGGGSFGNPNNSYRGNSNNIGGFHRSDGSNSEGVNAPVRAPRDWVPVTRDIDELVRETADRLADCDVGQDRAVEIRNAEKDVRLTSWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDEETRNKARQDDGPLALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQDMKKDPLGHLGAIIKDAGFMESAATRQTIMTSATFNASVMTVANELMKRLPGQDEMIKIVLANGRLSKRVNLEFFECKGLAEKNAKLREILKQNVNGKTLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSNRVNLLVTTDLLSRGIDVSDLDRVINFDLPDGDPDQGADTFIHRAGRTGRTGRKENGLCVSFVDPQSDRDSLLAPKLVELIISQNLPDLKVPDFLDAMAKSSRGKSGTSGFGQRGGYGGRGGGFGGTGRGRGGGVFGGGGRGGDFGGSGNFGGSGGGGSFGGSGGGGGFGGVKPSGFGGSRNNAEPTSSGGGFGAPKAPTGFPSDNNDASEDAPAAGGFGFSTKAAQDAKKAEESATLGSSTFGTANNADEEPTETGADGNDDDEW
The following text describes a protein:
Function:
May be involved in microtubule nucleation.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm.
Sequence:
MNSTFVQIPKLNINKQVKKKTDSITANTLLPKLMNDTSIQQPNQQQQQQQPQQPQQVTNGITILQNYQPQQPQPATTTTQQLNSANNTPTLVSTKKSVIGINEIPEHLLIRDIIYVFQGIDGTYIKYNKQSDSFKIDENTSNTLVNGEPAYISKPKRDLVYRLCEFGWLFKKVRLFITNNDFKKTGLTNQSFCSAINDELIELYRIIAILETQVYKKFDMVNYGGGGGGSGGSGSGSGLESPSSVSSGGTTTSTEIPFIDGDSLTLIRLFVWIQSPLKRLKVLGTCVDSITVDMKGGEILSKIDTLSKHGDQDIRILIHNIMFKICQPLFSMIRLWMFKGEINDPYQEFFIRQYESVQLEKTWKEKFAIVARLLPSFISLPLSKRILIIGKSINYMKQFCNNFKEDKNDRYYYYNQEDDDDDDEDHDDNDDDDENENQGEDDEIIERKLLIKESKIIKEKTKELNYINKEVLQEIIELVSRQSSERLLKIVLNRFKFMNHVKALKKYLLLGQGDFIQYLMDLIGEDLLKPTSQIQRHKLVGWMDTAIRNSNAQFEEQDIVNRLDIALLPERPGNIGWDIFSLDYHVDTPLNTILSPNDILRYKKIFHFMWGIKRVEYSLASIWRKIRSSTSLSILSPIGGDIHKSHLIMNEMVHFISNFQYYLMFEVLECSWKNLEKFIDQEATDLDQLIEAHHQYLQDICNKMFLSNSDSCYECFKKLLSIIIKFTLLQTKLINLSIAIQNEKNFNETHQAQVNKEFNSFRNHLNNLYQEYTTSFYKFQSEILKVKVNQDLNPISLQYMLDFNEYYEEKKDN
The following text describes a protein:
Function:
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Sequence:
MPKRVVAGIVTSDKMSKTRRVEIARLVKHPKYKKYIRRRTVCHVHDENNESGVGDKVEIIESEPLSKLKRWRLVRVLEKSTAVDVVALRAARKNAEAEGLAAAHAGEPETESAATDA
The following text describes a protein:
Function:
E3 ubiquitin ligase which accepts ubiquitin and transfers it to substrates such as the beta-integrin subunit pat-3, promoting their degradation by the endoplasmic reticulum-associated degradation (ERAD) pathway which is a pathway involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Negatively regulates the unfolded protein response to reduce endoplasmic reticulum stress. Required for the cessation of distal tip cell migration at the end of larval morphogenesis. Plays a role in germline and gonad development.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MGQHGAIRLQNEVQEGMPPPHELTEEEQWAEEHRKMHEKHKGHEAMHMEMMVIFMISVIVGQIFLVTWKRKHFKSYQMCTLIGMLTIPVYVCFNRSWYRFLATWLVFCIFSAFIWLKASAQHISGGTPRFVYKWFLFLHKLSYVLGVVGYLIMMGALLGFHVLFGVSQPTLMDAGILFMFYGVYYGVLGRDFAHICTARMASRIGYYTPEGLPKKHLEDGVCAVCGGRLDDSEHVHDADAVVTTKMVEDEDEKLYKLSCGHVFHEFCIRGWVVVGKLQTCPYCKERVDLQRMFKNPWEKPHLFYGKLLDWIRYLVCWQPLIVTAVQGLTTWMGLE
The following text describes a protein:
Function:
Serves as a slightly cation selective porin. Major antigen on the gonococcal cell surface and it may have pathogenic properties in addition to its porin activity.
Subcellular Localization:
Cell outer membrane; Multi-pass membrane protein.
Sequence:
EVSRVKNQGVKTKTATQIADFGSKIGFKGQEDLGNGMKAIWQLEQKASIAGTNSGWGNRQSFIGLKGGFGTVRVGNLNTVLKDSGDNVNAWESGSNTGDVLGLGTIGRVESREISVRYDSPVFAGFSGSVQYVPRDNANDKDKYTHKQSSRESYHAGLKYENAGFFGQYAGSFAKYADLKDNAERVAVGTTGAHPVKDYQVHRVVAGYDANDLYVSVAGQYEAAKNNDTNPATNGKKLEQTQVAATAAYRFGNVTPRVSYAHGFKAKVNGKKAARYQYDQVIVGADYDFSKRTSALVSVGWLKEGKGVNKTEKTASM
The following text describes a protein:
Function:
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Localization:
Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and vesicles.
Sequence:
MADLFDGDFMEPAAAPTTDTSAAVEEDPAAAFLAQQQDEIAGLENEVLGGNEPTVNGFGEPGEQVADAVPANGKAYNSVSNPSQAYAAIAVADARLEELRTEPEKIRVWREENTKLLAEKDRESERKQQEWLAQARKELEDWDRNRLEQVEKTKESNRADVSHIELLCCYSYKRTAEEQFLKDRDQAAPGSEWERVSKLCEFNPKSTKSTKDVTRMRSTLLHLKQNPRPISVPEM
The following text describes a protein:
Function:
Probable transcription factor required for embryogenesis, vulval development and cell fate specification of the postembryonic mesoderm (also known as the M lineage). Specifically, required for the specification of sex myoblast cells and their development into the muscles that are necessary for egg-laying. In addition, may be involved in RME GABAergic motor neuron progenitor cell fate specification.
Subcellular Localization:
Nucleus.
Sequence:
MDLQKPPNFMLDCGMAPHMMPPINWAAAAIAVASSTSGATNATSSNSVATSQQLQHHPYGTAAGGYKHAQQAIPKSVTPYSDATNCKKSSNHIKRPMNAFMVWSQMERRKICEHQPDMHNAEISKQLGSRWRSLTDEEKAPFVAEAERLRVCHMQEYPDYKYKPRKKPKKNPDGTLQQPAQPQAPQQQQAPPRGASPQARQRKRPNTDQQSETQQFQNFKSVKVEQDWMGNAHMSHAQKMPFHPSYPSPSEFGHAPLTPESGFYDDYFTQQHHQQHFASQHHNSAGSPLRMTNLGMDMGMPPQMMGHNSGFGAGNHPFYLHTSPPSVDQDDMRSLSSGSSGYADCSASEQSTSSPNSAGVVTMATAATTTTHLDDLEQICPTVTTGELVNYPWSDALGIDINFS
The following text describes a protein:
Function:
Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair.
Subcellular Localization:
Chromosome. Cytoplasm, cytosol. Nucleus, nucleolus.
Sequence:
MAEASDKLYRAEYAKSGRASCKKCGDNIAKESLRLAIMVQSPMFDGKVPHWHHYSCFWKRARVLSQGDIYGYTELRWEDQEMIKKAIETGGAAAGAGGDSKGGKGEMTLNDFAAEYAKSNRSACKGCEQKIEKGQIRISKKSVDVERPQLGMIDRWYHPDCFVSSREELGFLPSYSASQLKGFTILSAEDKDSLKKKLPAVKNEGKRKADEVDGHSAATKKKIKKEKEKESKLEKLLKEQTELIWHIKDELKKVCSTNDLKELLIANKQQVPSGETNIVDRVSDGMAFGALLPCEECSGQFVFKGDAYYCTGDLSAWTKCVAKTQTPNRKDWVTPKEFHEIPYLKKFKFKRHDRAFPPCAAPTPISPPAAPEPKPTVEETFPEGKPLTNTKVLLIGKLSKNKDEVKTLIEGLGGKVAGSAHKANLCISTNKEVEKMSKKMEEVKAANVRVVSDDFLKEVESGKSVQELLSQFGISSWGAEIKQEAVQPTEKQPSSGPVAGKSSGKVKEEKGSNKSEKKMKLTVKGGAAIDPDSELEDSCHVLETGGKIFSATLGLVDITRGTNSYYKLQLIEHDRDSRYWVFRSWGRVGTVIGSKKLEEMSSKEDAIEHFLNLYQDKTGNAWHSPNFTKYPKKFYPLEIDYGQEEDVVKKLSVGAGTKSKLAKPVQELIKLIFDVESMKKAMVEFEIDLQKMPLGKLSKRQIQSAYSILSQVQQAVSESLSEARLLDLSNQFYTLIPHDFGMKKPPLLNNLEYIQAKVQMLDNLLDIEVAYSLLRGGADDGEKDPIDVKYEKIKTDIKVVAKDSEESRIICDYVKNTHADTHNAYDLEVLEIFKIDREGEYQRYKPFKQLHNRQLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHAMPGSPIGLILLGEVALGNMHELKAASQITKLPKGKHSVKGLGRTAPDPSATVQLDGVDVPLGKGTSANISDTSLLYNEYIVYDIAQVNLKYLLKLKFNYKGGMMW
The following text describes a protein:
Function:
Component of the Fanconi anemia (FA) complex required to recruit the FA complex to DNA interstrand cross-links (ICLs) and promote ICLs repair. Following DNA damage recognizes and binds 'Lys-63'-linked ubiquitin generated by RNF8 at ICLs and recruits other components of the FA complex. Promotes translesion synthesis via interaction with REV1 (By similarity).
Subcellular Localization:
Nucleus. Chromosome. Note=Following DNA damage, recruited to DNA interstrand cross-links (ICLs) sites by binding to ubiquitin generated by RNF8.
Domain:
The UBZ2-type zinc finger binds both 'Lys-48'- and 'Lys-63'-linked polyubiquitin with preference for 'Lys-63'-linked polyubiquitin.
Sequence:
MEEERRLRGRLSRRRPPAGGGPPNCRPWFLSEESKSEPWAALLRSTVGGNTDWTPNSQPLPPLPAFPSQESLPDPESTVPPEVFTVGSKTFSWTPFPPALRGSGSSCRLLRCPEGSPGSPAPSLKGCPALDSRQTPSTQECVQSQLVLLNCPLCQKAFDPKLTQLDVDSHLAQCLAESTEDVVW
The following text describes a protein:
Function:
Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MNFSKSLLLIAFGGTIGSIFRYLLQYWFGNVLGYSLPWGTLTANLLGSFLIGVVYAISDRFPLFDPQWKFLLASGFCGGFTTFSTFSYETFQMLKSGHYILFLGYICLSVVGGIGFAFAGVWMIKNF
The following text describes a protein:
Function:
Involved in the biosynthesis of mycolic acids. Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension. Can use dodecanoate (C12), tetradecanoate (C14) and hexadecanoate (C16). In vitro, displays a preference for long-chain over medium and short-chain fatty acid substrates.
Miscellaneous:
MISCELLANEOUS: Was identified as a drug target. Inhibited by a series of 4,6-diaryl-5,7-dimethyl coumarins that directly inhibit the acyl-acyl carrier protein synthetase activity of FadD32 and kill M.tuberculosis. They effectively block bacterial replication both in vitro and in animal models of tuberculosis. Quinoline-2-carboxamides have also potent anti-tubercular activity.
Sequence:
MFVTGESGMAYHNPFIVNGKIRFPANTNLVRHVEKWAKVRGDKLAYRFLDFSTERDGVARDILWSDFSARNRAVGARLQQVTQPGDRVAILCPQNLDYLISFFGALYSGRIAVPLFDPAEPGHVGRLHAVLDDCAPSTILTTTDSAEGVRKFIRARSAKERPRVIAVDAVPTEVAATWQQPEANEETVAYLQYTSGSTRIPSGVQITHLNLPTNVVQVLNALEGQEGDRGVSWLPFFHDMGLITVLLASVLGHSFTFMTPAAFVRRPGRWIRELARKPGETGGTFSAAPNFAFEHAAVRGVPRDDEPPLDLSNVKGILNGSEPVSPASMRKFFEAFAPYGLKQTAVKPSYGLAEATLFVSTTPMDEVPTVIHVDRDELNNQRFVEVAADAPNAVAQVSAGKVGVSEWAVIVDADTASELPDGQIGEIWLHGNNLGTGYWGKEEESAQTFKNILKSRISESRAEGAPDDALWVRTGDYGTYFKDHLYIAGRIKDLVIIDGRNHYPQDLECTAQESTKALRVGYAAAFSVPANQLPQTVFDDSHAGLKFDPEDTSEQLVIVGERAAGTHKLDHQPIVDDIRAAIAVGHGVTVRDVLLVSAGTIPRTSSGKIGRRACRAAYLDGSLRSGVGSPTVFATSD
The following text describes a protein:
Function:
Transports zinc from storage in the vacuole to the cytoplasm.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MEKIPRWLLFSLISSVLCILGALCVPLLSVAFDSKRNSQSKLVNYGLSLSAGSMITTSLYMLLPRIEKSNRFKVFPGLLLGICLSFFLNYLVHAFASESLVHCADSGDHATGSHIHSKSHSHSHSHSHADSHSNFSNDHDLENAPSEHGYATSSSSVSENDPLITKDSDRPQMKKKMSLIDLLTRRKSEGECCDLNKCTPLLQSEQPEYIACVPPVIKSSQSERNVPHGCEGSEDNGQSDDKDHRGLVCVENNIGYDLENLSLYRKNFLSSRHHHSSESPENYGSNQLSHSFSSPLGNDVTENPAALADTQYHPENGSLYPHHHHLETPFSKLLSIGMQTCLVLALHKFPEGFIIFYTNRSDSSKSLGFSIFLSLTIHNFVEGFAMTLPFYTVFESKWVAILITAVLGGGSQPLGALIGYFIFKGSTPRDHEPNMDFLLSVTAGFLLVIGLQMFQTGIGFSDGHHHHQGEGDEEMKQSHSSGTTCLKWCCTGVLLILASALFT
The following text describes a protein:
Function:
Phosphoserine phosphatase that mediates dephosphorylation of phosphoserine in the serine biosynthesis pathway. Also able to dephosphorylate other substrates such as phospho-L(or D)-threonine, with lower activity. Shows phosphoserine:homoserine phosphotransferase activity by transferring the phosphoryl group to homoserine using phosphoserine as the phosphoryl group donor.
Sequence:
MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWLRERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTMLSEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKASSRSLSL
The following text describes a protein:
Function:
Probable constituent of the synaptonemal complex during meiosis. May interact with HOP1. Required for meiosis I chromosome segregation.
Subcellular Localization:
Nucleus.
Sequence:
MEGLKKKIFGVCLKNDLAQTRNETKGIHYGLMTLETSKQLQEFLHLLVIKREVIQNFELLFHIINVAVKITDSNLPSDDIWHFILKLRFSSEINIDEDSKVLNYLLETGIAMENPVSWKCLAVISSILSSVPQSKKIITNLIETEHAKKIGQLFDNIQDLQQGNFLVEILSNCFKKSASNSKKVEKIPQLWQSRSKNKFFFENEFYPFSSKNGSLQTCQFLCNNFMSTLSFTGILRQVSYSGSETLKNLRIFKKKDDENSYFIQCIYNKIYLWLDEKAPLEFERKKIRITKNLKNKIQIKLRQPFHECVRTTADKTALLFNKTKGFQLEFEDEKLGETFFHNVNNIPKISEVQNFLVLDYIEEEPENEGEEEEQIGRADEQKEDEEEESLDELSTPMVYPIKSSIPHNHNEKVQLVTPDRSVSIRSDEWDLKSNTEDEEGNVLADLKISSTKETKRQTDYVHIDSEDQSPVVSAQMRKMRRESTKTLEILRQEFKDKDVQNKEDQSEQIQNPFVNTSSLVVGKSCLVNPKEKPNIDQTVVGITELKSNSSIKKRDINILDTIFGQPPSKKQKQFHKKEKKKQQKKLTNFKPIIDVPSQDKRNLRSNAPTKPKSIKVSKLRTDKKVTGEKSSPETAAEKVDDQTVRSNDEQAMSRATKEKCFPDVNEGKEITKDDAKVSLESKKNNETFVDSSVVEKHTPPDKDCNNCNITDILESTTVIDLQSPHGLSAPGQNTFTNKLQEQIYSSINHFSNELVRKISIINQELNKKILKELSEKYQKLFSELQDNFQNDTNEMLKFMGEIKDMMNLPEDQLVHAIRTRKFDNNKR
The following text describes a protein:
Function:
Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
Subcellular Localization:
Nucleus.
Sequence:
MSRRKAPVSYSGLDTSDVSDEDFEVEDEVSTPKRRKTTSPRKQTPRRTASPRKAPGTPSPVKRSLHDKSARKKANRTLLDQSLGLVSEDEDEIELAERIIGESRAPILDSSNDFHTDERSLANVGALIAAEDRVLFLDSSEGYFDQHKTRGRGNANTMAKAPAIDHSVFFKYTNQANELFHADQKKMLRHAYRGMFSQWIFELSEGFSLLFYGLGSKRELLTDFVCEKVDSEIPILVINGYNASVQFKSVLNSVVDVLYENHEDIFAKKGFVVRNKLPKDVDLLVKLVVDTMRDIEAGSKPSLVVLCHNVDGESLRIDKASTHLSQLMSISQIWFVASVDHIMAPLMWDSAKLASYNFVWHDVTTFAPYTVETSFDDPLLLGKKAEAQGAKGVKYVLESVTPNHRSLYKNLIYCQLEEFHNVADKRKLPEAEVGALTGSTSISVDYDKVLTECLNELTVSNKKDFQEKLKEFMDHKMVVAFDDKMGMKKLYIPFSKDVVQQILEGYLDA
The following text describes a protein:
Function:
Probable transcription factor. Binds to the DNA sequence motif 5'-[AG]GGCGCCG-3' in the promoters of target genes, including micro-RNA genes, in order to repress expression, and acting redundantly with flh-2.
Sequence:
MYSPESMNSNISSPSPPSSSSLNAPSLADAPEVRSDDGEAETSEPSTSVTAVPMEIVSQASTSAPVNQLLASGIDMSSVIKNNAVLQALLASASAGGFGDNAGLTMSKLLTAALANGSTAVAKRDAGSPRTDIPKKTRLKVFSNGFFMTFDKLSSCQKKYFWRCEYKNTCKARMHTDIVTEKILTFIHEHNHSAPIDEEVRLYGLDPTNIERNRVYIVGNVADPNQRRKIRKQVADREAAAKRLVQQQEEEQQKQQSASSIVAARAAYAQAMQNGSIPTSSGVASFLQSTSATAPMTSHSMLLAQMPFLNNIKTEMSNMVKNEQFTPERYTQHMSPNLPLQTATIAPLIIPTENYDSPSYRQPAIKRKATDLTNEEHDLRRDPMFQPTFELARKLRKLWKGEPNRYPRTTTTPTHHFEFFLSKNDGTDEHLYVPMRINLRDEAHLKEALQDFCGQQCIGMLLFGISPKISVMFNQPMLNNWDNNQFFLLDISNPSRWRLMYVDDQAV
The following text describes a protein:
Function:
Oleate hydroxylase involved in the biosynthesis of ricinoleate (12-hydroxy-cis-9-octadecenoate), that is present at high levels in C.purpurea sclerotium tissue. Exhibits delta(12) hydroxylase activity on 16C and 18C monounsaturated fatty acids (i.e. oleic and palmitoleic acids), and, to a lower extent, gamma(3) hydroxylase activity on ricinoleate.
Subcellular Localization:
Microsome membrane; Multi-pass membrane protein.
Domain:
The histidine box domains may contain the active site and/or be involved in metal ion binding.
Sequence:
MASATPAMSENAVLRHKAASTTGIDYESSAAVSPAESPRTSASSTSLSSLSSLDANEKKDEYAGLLDTYGNAFTPPDFSIKDIRAAIPKHCYERSTIKSYAYVLRDLLCLSTTFYLFHNFVTPENIPSNPLRFVLWSIYTVLQGLFATGLWVIGHECGHCAFSPSPFISDLTGWVIHSALLVPYFSWKFSHSAHHKGIGNMERDMVFLPRTREQQATRLGRAVEELGDLCEETPIYTALHLVGKQLIGWPSYLMTNATGHNFHERQREGRGKGKKNGFGGGVNHFDPRSPIFEARQAKYIVLSDIGLGLAIAALVYLGNRFGWANMAVWYFLPYLWVNHWLVAITFLQHTDPTLPHYNREEWNFVRGGACTIDRDLGFIGRHLFHGIADTHVVHHYVSRIPFYNADEASEAIKPIMGKHYRSDTAHGPVGFLHALWKTARWCQWVEPSADAQGAGKGILFYRNRNKLGTKPISMKTQ
The following text describes a protein:
Function:
Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities. Can catalyze three types of transacylation reactions: (1) acyl transfer from 1-acyl-sn-glycero-3-phosphocholine (1-acyl-GPC) to the sn-1(3) positions of glycerol and 2-acylglycerol (sn-1 to -1(3) transfer), (2) acyl transfer from 1-acyl-GPC to the sn-2 positions of 1-acyl-GPC, 1-acyl-sn-glycero-3-phosphoethanolamine (1-acyl-GPE), and other lysophospholipids (sn-1 to -2 transfer) and (3) acyl transfer from 2-acyl-GPC to the sn-1 position of 2-acyl-GPC and 2-acyl-GPE (sn-2 to -1 transfer). Mediates the synthesis of 1-arachidonoyl species of phospholipids by transferring the arachidonoyl residue from 2-arachidonoyl lysophospholipid to the sn-1 position of 2-acyl lysophospholipid.
Sequence:
MARAVGPERRLLAVYTGGTIGMRSELGVLVPGTGLAAILRTLPMFHDEEHAQARGLSEDTLVLPPASRNQRILYTVLECQPLFDSSDMTIAEWVRVAQTIERHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLVVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAERGLVIVNCTHCLQGAVTTDYAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGLSLDDRKELLTKDLRGEMTPPSVEERRPSLQGNTLGRGVSWLLSLSGSQEADALRNALVPSLACAAAHAGDLEALQALMELGSDLGLVDFNGQTPLHAAAWGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLSTQELEEAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLAVVAFLQSLEGAVGAQAPCPEVLPGV
The following text describes a protein:
Function:
Regulatory protein of the TOL plasmid xyl operons. XylS activates the xylXYZLTEGFJQKIH operon required for the degradation of toluene, m-xylene and p-xylene.
Subcellular Localization:
Cytoplasm.
Sequence:
MEQITHLSSGIPGIRLIDAEHNRFSFPRHFHLEYHIGLLLQGRHRYAAGGERRLAGAGDALLMAPESIHDGSSAGEEGYRIRVLALDADWLERASRDFSDGRRGAPRLTSSLVRDERLQQRLRQLHLGMLGGAAALENRLALEEHLWQALACLLSLGSSLRLEEGDREGFGQRDWTRLRDWLESRLEYPPNLEELAAFCGLSPWQVLRRFRRHCGLPPHQWLTQLRLERALPLVLRGEQPLSQVAQQFGFYDQAHFTRLFRRTYGLPPARLRQR
The following text describes a protein:
Function:
ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.
Sequence:
MSLSRTENNGTTSDTPAREFNNNERNAPVNNGGAGRGGRWAFRGDFRSDEGGERKGKPWGRFPQGDGERGNRGYGGGYRGRGGRGRGGGGGGGFREGSFGFENRAQQQPPREGLMNDQAPQEERQPTEESEPVQRGRFDVDFYDRPRRRGRGRQYGGRGDNDGERGFFGGDNNERQPQKQRQQNPKPFGQQQQLEPQQEDEQEAVASPQQQYNQQQRQPERRPDTAPTMDPISTNPNRTQRAPRFRKNCRDEREIEKLFESHHQQKGISLENYASIPVDIVPRDIDAVESFEDLFVEPALALNIAKCGYKEPTPVQRYGIPVCLNGNDLMACAQTGSGKTAAFLVPVVHYILKNGVSPAKDRISHPIAVIMAPTRELALQIYDEVRKLTFRTDIFYDVVYGGTPYPTRFENDILVACPGRLKDIFDRNIVSFSCVKFLILDEADRMLEMGFEEQIEYLVASRYSDMPSSEERQTLMFSATFPQRILNLAKRYLRPKYYLLTVGRVGSTTKNITQKLERVPEAEKKDKLFDIIYKQKQTDLVLIFVETKRSAEQLHSALKSSGIPSTTIHGDRRQSDREIALKDFKSGITPILVATDVASRGLDIPNVAHVIQYDLPKEMDDYTHRIGRTGRAGNKGVATSFYDRNNRNLAVELYHYLREHEQEVPMWLENEKDAVEGERFVGGTRGGNRRGGGESRAAAPLGNSTWGEAATGRGGRQGGQQQQERKESNVDDGGF