lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins. Within the pathway FUM14 catalyzes esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone. The biosynthesis starts with the FUM1-catalyzed carbon chain assembly from one molecule of acetyl-CoA, eight molecules of malonyl-CoA, and two molecules of methionine (in S-adenosyl form). The C18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain. This step is catalyzed by the pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8. The resultant 3-keto intermediate is then stereospecifically reduced to a 3-hydroxyl product by reductase FUM13. Subsequent oxidations at C-10 by the cytochrome P450 monooxygenase FUM2, C-14 and C-15 by FUM6, FUM12 or FUM15, tricarballylic esterification of the hydroxyl groups on C-14 and C-15 by acyltransferase FUM14, and C-5 hydroxylation by 2-keto-glutarate-dependent dioxygenase FUM3 furnish the biosynthesis of fumonisins. The tricarballylic moieties are most likely derived from the citric acid cycle, and their addition to the carbon backbone may involve FUM7, FUM10, FUM11 and FUM14 (Probable).
Domain:
FUM14 encodes a nonribosomal peptide synthetasecontaining two domains, a peptidyl carrier protein domain and a condensation domain. The condensation domain catalyzes a C-O bond (ester) formation and can convert HFB1, a precursor of fumonisin B1 lacking the tricarballylic ester, to fumonisin B1.
Sequence:
MNSLDQWRDTWAKVLSIQPSEIDDQDSFFDLGGDSVKAIQLLSEAAQSAINVDLQTFYDNFWNIISPQLRGENRSGPIDRGGSIATGEADDSIGLLKTDVNLEVVEKALSKVNIARESVCRMAPISSIQEFFLYLGLNGHVGLINYVYQVEGRDLKQGLARLVKHLEAKNPIFRTVMIEDDTGKFTQVQLSHSISTWTYPTDLQAYLDETMTGRQRLGASPVRYSLVLKDERHKGQNFFVISLDHTHCDAFSRYLIDKEILQILKQPTEYASLQNPERPWYGDFVKHNRAHILDEQLSRYWASYMQGATLANVHPLSEAVVGGELDGEMVEIVPIPVVSQSRGTRGQTNPSHVILAAWAMALSKHSGLKDITFGLARHGRSSDSFTDLRRVMGPLVTGTPFRVTLNDTQERTEQLLNRVKEEVLKTARWEQGMVPNIHPDAEGNPWVQSMVNLKSELYGFGNESWTGDEAEADITAIKMRRDLQQYEFKSNWAILLSTLQKQGQLRLRMYYQSQLLSHDKAQALFASFKSLIAELAAADGSLVTGLLD
The following text describes a protein:
Function:
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Sequence:
MVSLQFITHQTDRYTYFESALMALEGGCKWIQLRMKEAPCEEVEAVALQLKPLCKEKEAILLLDDHVELAKKLEVDGVHLGKKDMPIDQARQLLGEAFIIGGTANTFEDVVQHYRAGADYLGIGPFRFTTTKKNLSPVLGLEGYTAILSQMKEANIELPVVAIGGITREDIPAILETGVNGIALSGTILRAEDPAAETRKILNMKRIIK
The following text describes a protein:
Function:
Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MLAHFQRGSSEVDWCELNYVHSNSIAEFFNTISNAIFLVIPPFLMYLFRPYANRIGYGINVILLLMVVIGLCSAYFHATLSLVGQLLDELAILWVLMAAFALWAPRWLFQNGPFYGKRCRLAYIMATIGVMGTILGFIYPAANAFALMLLGIPWAGLLFTEVFRYPSKQVRRLGVFCIIWWFTALACWINDRIFCDMWKQLSFPYLHCGWHIFIFIASYIACVLSAYIYAASEFPQYKPSIMYWPGPTYHFAVPYVAVHENTDKDIHL
The following text describes a protein:
Function:
Enhances the incorporation of serine into phosphatidylserine and sphingolipids.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGLVASCFGGLAAYAAESVACCCGSAACSLCCRSCPSCTNSTSTRITYAILFFLSSIAAWIMLDKDVSKGLMKVCCYHSTLFRLVLFTQPAIKTTTNVVPWGELGVMRIMFSVCLFHLFLSLCTIGVSSSKDPRSSLHNGMWFIKLILLVGAMVGSFFISNSFFIGASWSWIGLVGAVLFMIVQFILLVDFAYSWNDSWVGKLEEGSKCAGFGSYRLISATVMLMAFVITLTVLMFHFYTNGDCKLSNFFIGFNLALALLVTLTSMLPSVREALPSSGILQSSVVAAYATYLVWSAVSGVPSTCHPLIAVAPLFLSSRGFLPPLPYVALKPAECGGDAGTNTAAIVIGALLTFISVAYSSIRTSSKSQLGKLGLQQGSNENIYLMDDKAADFDEDDEDRRLQRVVDNEQDAVRYSWSFFHLTFAVAALYLMMVLTEWDSSDADVRIGKGWASVWVQVVSSWVIFLLYGWTMMAPVCLPDRDFS
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MPTPESAAFLAKKPTVPPTFDGVDYNDTKRLKQAQDAIIREQWVRVMMGRLVREELSKCYYREGVNHLEKCGHLRERYLQLLSENRVQGYLFEQQNHFANQPKQ
The following text describes a protein:
Function:
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Sequence:
MSLENYKFHKEHTWVKISGKTKKVKVGISDYAQESLGDIIYIELPEIDNHVEADTEMAEIESTKTSSPVIAPVSGTIVEINEELIDHPEIINEDPYGKGWIAVIEMDNPRELEDLMDYEDYESYLEEERE
The following text describes a protein:
Function:
Required for sperm flagellum axoneme organization and function. Involved in axonemal central pair complex assembly and/or stability.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: Due to intron retention.
Sequence:
MLSSNDQKLEKLDSFYRPPVSKQRTSAEIISEARNALRTVRTQRPFTPREDQRKLFGPASSRSPENRPPSSFSLHASSFELSDSKPISGTRLRPLELKPKAPASPGTEDACLSFPKAPLDPAKIRKISGARARFYRAASQGMLLPDRSPPAAHSKTVDESSKPVSVGSSTARRNGTHLTASSATGQLKSPPLLTCDQGFQETTEQEVSLLSQLRRGGDPGKRRARASSCPSSSDLSRKETRAASRASSQEQETDTEVDEVFWKARIVPILHELENEEDIEEMCAACTQLHRTLEEARMLGKKFKRRTVLLKALYKLVDADSDPLSLKLAKLILALKVSGKNLLNVCKLIFKISRNEKNDTLMQEDNILESLLEVLRAEELQSNTEAFLYCMGALKFVSGSPGFLTEMVNKGAVEILAQLIKEMTEDTEKHGVCLPDSGHLLVQTTATLRNLVDSPLTRSKLLNMGAFPHLCTVMEQHADDKDICTNIARIFSKLTSYRDCCAALASYSRCYALFLSLLNKYQKNQDLVIRIVFILGNLTAKSNQARELFSRETGSVETLLTLFQSFYHHKENSPKLQLSEAKPQAEAEDVLVKLTRVLANIAIHPRIGPVLAANPRVVGLLLRTLESKSLGDCEELVINTIAAINNLSFYQVKSSVLQHRKLYVAELLLRLLVSNNMERILEAVRVFGNLSQDHDVCNFLMQKNVHKFMITLLEAKHQDICFSACGVLLNLTVDKEKRAILKEGGGIKKLVDCLRDFGPSDWQLACLVCKTLWNFSENITNASECFGDDVANTLLILLSTFLDEELALNGSFDQDLESYHRLHWETEFKPVAQQLLQRIQSHHSLLEPLPVPSF
The following text describes a protein:
Function:
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGVFFHALYVLSIFDIYFTSPVVHHIESVGYTDAPPAKRVVVFVADGCRADKFFEAERVSFLRDVMQKRGSWGVSHTRVPTESRPGHVALFAGMYEDVSAVTKGWADNPVDFDSVFNQSSRAFLFGSPDIVPMFARHVPQALEEHYSHAEEDFAKGDASELDVWVFRRLQKLLNEATEGSDRFEQLHAEGVVVFCHYLGIDSNGHAHRPNSKDYLNNIALVDELVDKTHRMVEDFYGYDGRTAYVFTADHGMGLKGAHGDGDPANTRTPLVVWGAGVRAQLQAQEEQERAAVGEWGALGNLVRRDVMQADVAPLISALLGLPYPRNSVGVLPFSYLAKGAYRANAVRSNAQQLYLHALRKEQEKRSRTLLRFVPYGPFRDRVPELSKLLAEAYDASIQSDNDSEAYERVEELSQELIEICLATLEYFQRYDWFFLLSVVVLGYVGWMLVVGVAYLHPRDFSLKWLLGVGGKQLDIKLSIVLFASFVYLALEGSPTTYYLYVLFPLLFGVFTWNHADLIQQAWASGVSESKSKTSWKRWAECALILLCLELVVFGYERREIFGVLFSLLALWPYVGTSADEDDGQECGCGWTGGFPSPSRCWTISCLLISVFPYLPSEYGEHTALVNIGSLLTFFFTGAVLTAFGSSWMNSSFILNASPLVLSLLTLHATMQYLDGERSKPPLSLTVANWLLSGVPIVQLLQAEVGRYVRRLIQVMLAFAPSFILLSIAYEVLFYVVLCGVLVSWLLLEAQASLASSSSMWREVQRAFVFLLLVNIAFFGTGNVASMSSFEISSTYRFVTVFAPFTMGALLVGKILIPFMVVACTFHLILLLPSATSPTDARKARLPATRYFLLVVAMSDVLALHFLFMVKNEGSWKEIGNSISMFGIVNAQIVFIPLLFLLAR
The following text describes a protein:
Function:
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Subcellular Localization:
Cytoplasm. Mitochondrion intermembrane space.
Domain:
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation; The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters; The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
Sequence:
MESVSHLVSNGQSVLLVWSQGGQLDTLANFTSSLRERVGTNGTVAVENINRLSQSSYGSSTFDVALSNVVSSYCCKHTSEQLAQILKMLKPDCKCLLRDTSPSDQIRSELILAGFTNISIVAEDNATVKVNARKPNFEIGSSAALPFANKISLGGNSKMETAKMWTLSSQDFVDDDIDIIDENTLIEEDDFLKPDPSSLRSQECDSAKKKRKACKNCSCGLAEEIESEKKTNGNPVSSCGSCYLGDAFRCSSCPYLGMPAFKPGEKVALPSRLLQADV
The following text describes a protein:
Function:
Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.
Sequence:
MGKKLKTKTKKVQQQEPLADAESGDLGLQEASKSTEEAAVSASDWEQCGHYSRDNPHLDKVLLDFMSSKHVASCEHCRDDGPRKKGGKQQKKKGGGGAAKTQAKVEKSDMWICLDCGRHFCGGAVSETKPYGHARRHAKQDRHWWAARYDEPTVAYCLSCENKVSIEMPIVESVVAAPADDKVFGAVDSNALVLANCHGNVIKGLPNLGNTCFFNAVLQSLLALDRLRSKMSGPDVPTGALTMSLKKLFVETSASNDAGGALSPKSLFSSICSKYPQFRGYQMQDSHELLRCFLDGLRTEETEARKLLEEASSSGVTTIVDSIFGGQLSSTVSSTECTHGSVKYDQFLDLSLPVPSRRPPSKSVSSPPAKRTNQSIRDRNRNRRYGKITTTRASPTVVENSKERVETVAECNDSQILGSELGQVVNEKEPEPSEGSESCASVSNQELKAASYVEDDISWLDFVADADETRSEILDSVCFTEAGQICDSNGATHGSYDSRDDALPKEQVLSSEHSCENIVDDAACLQPVILLPYKELCTTANEIYESSQNPKDVGPAPDISPVTENNAHPLSGGNGEQDDYIGLGDMFNEPEVTSEAKEETTAGDIDVMAWSSNSADDEVDVSNAPVSVEGCLALYTEPELLSESWHCEHCSSTAARPNTNEGKGGDKMVASANDRKDSEKIMASGDARQGGDKVMMNCSKKEDIDQIMTTDCCSDNVDPDLCCNKVGCANPDAENTSNGNSPDTGNATLLNTGLIVEQPDSKHDGNTADIAAQEASAPVSCGDNDSPSCSTTIDRMVESGANAEEVVTSSLSSQTQSILLSAKDNEDVTTRNMGRGKRVKMVGKAHKGQDNQNKQKEDETKVFRAAMRRILISKAPPVLTITLNRFSQDSHGRFKKLKGHVCFKETLDVRPFIHPRSKENDNTTYRLVAVVEHMGTMTGGHYVAYVRSGKIGGRQQQRRASKSWFYASDAQVREASLEEVLNCEAYILFYERVVE
The following text describes a protein:
Function:
Choline transporter.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MGCCESKETPIQRISQNGKPAVPIRAKRPKDLLFLILYIAMLGGMGYIAFICIKNGDPSRYLHGVDSWGNICGKKNNEIIPGVNTSGLDRSNYTYELNMRLALDPSSLLKTGSGAAVLCVKECPAKLIQCKQLLSDNTYNLSMNVINERICTMPYGWIPAHTHIFNRCVPLQLLQVSCINQTNGTSSAQQNSAVSVIAHQMVTSVVNNWTNIVYMVLISLGISLLMIVLLQIFNRVIVVLIVILAGIGSVAATSYLWYCYAVSTGFINSTDVENTVNAVRDFQYLLPLCIAVTVATLIILILLVWVRKSLCLVVKLFDEASLAVFNMPGVLLQPFITLTSILVVLTYFLIVSAYIFSIEVPKVDISGMVSFVQNPDLSTTALIAPHIFGCLWMMEFVSGCQQVIIAEAVSSWFFNQRQKTCKYDMCPTLRPTLHLILFNLGSVALGSLVIAIVQFFRVILAYIQRQLRGKESKTVRFVLKCMACCLACFEKVLKYISRNAYICVAMYGDSFCTGAKHAVSLLIKNAQNVLALNCVSGFCLFLGKVSVVVLTAFVGVAWFTAKLGTRASAVDYGAPLTISCFCSFVIASAFFNVYSMAIDTIFLCFCDDQERNNGSDRPYFSSVALQKYMTRPPGGKTKKNKKTPAKSARTRSIHPGWWLGSGYKSK
The following text describes a protein:
Function:
Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular Localization:
Nucleus.
Domain:
The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence:
MAGESSNPGTVEEIFKDFRGRRSAFLQALSVDVDKFYSLCNPEMENLCLYGHPNGTWEVNLPAEEVPPELPEPALGINFARDGMQRQDWLSLVAVHSDCWLLSVSSYFGARLSRNEKNRLFSLINDLPTLFEVVTGRKTIKDKPSMDHESKYQNGLKRSIEGEMKITRKLMEESCEDEEDEHGDTLCGSCGGHYLNVEFWICCDVCERWYHGKCVKITPAKAESMKQYKCPSCCTKKGRQ
The following text describes a protein:
Function:
Negatively regulates the expression of genes encoding pectinase and cellulase, which play a major role in virulence, and the expression of the blue pigment indigoidine, which is implicated in pathogenicity and protection from oxidative stress. Represses the expression of genes involved in indigoidine biosynthesis by binding to indA and indC promoter regions. Also binds to promoter sites in the pecS-pecM intergenic region and negatively autoregulates its expression as well as that of pecM.
Subcellular Localization:
Cytoplasm.
Sequence:
MARYLEVSDIVQQWRNERPDLDVEPMLVIGTLSRVSLLIDRALDKVFSKYKLSAREFDILATLRRRGAPYAISPSQIVNALMINNSTLTSRLDRLEQAGWLRRMPIEGDRRSVNIQLTDEGFALINRVVEEHVENERDILSPFSEEEKTHLRALLGRVEKHLVNNR
The following text describes a protein:
Function:
Binds to DNA non-specifically. Could be a regulatory factor involved in maltose metabolism.
Sequence:
MLFSPPLQRATLIQRYKRFLADVITPDGTTLTLHCPNTGAMTGCATPGDTVWYSTSENTKRKYPHTWELTETQSGAFICVNTLRANQLTKEAIQENRLPALAGYNILKSEVKYGAERSRIDFMLQADFRPDCYIEVKSVTLAEKENGYFPDAITERGQKHLRELMGVAAAGHRAVVVFAVLHSAITRFSPARHIDIKYAQLLSEAQNKGVEVLAYKAELSAQKMELNEPVPITL
The following text describes a protein:
Function:
Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration.
Subcellular Localization:
Endomembrane system.
Sequence:
MKSIYKTGKRFFKVRLSFRLTYCNPFFNHNYKRNNEGGCERAHELHLELTGEKKDKSKSKRINALKKVVSNMTYGYDMSSLFQDVLACMNTTNLEIKKLCFLYILNYASIKPTIAAEAIPIMLRDLDDPDPLVRAFSLRTMSSIHVKKFWLAVLDPLVVANALAALSIITERSSNLKIQISRSVASNLLTCLDECSQWLQAVILDSVQLFTPQERGIAEQFADRILPWLQHANAAVCMGAVKAILYFTNYMQSDERVNEYLYKIGPPLVSLVAGKSPALQYVVLRNIQIILDLNPDIFKQDIHIFYCKYDDPIYIKLEKLSVLVKLADEHNLSDILSEFVDYATEIDVEFVRKVLRYIGLLALKVESKADECVDHLLELAETKITYVVQEIVIVMRDILRRYPGRYEHLISELLEEFESFEDAEAKGAIIWILGEYAERIDGSITLLSEFFDGFSDEPVTIQQTLLTAAMKLFLKMPTQGSELITAVLKRVVDESSDPDLRDKGIMYSRLLSLSPDLARNVVLSKKSDIDVETGTSDPDLTEQLLLNLSTLASVYHKPPNQFIKGARTIYPAYSPVLRQRLDRRNGVDEPEEQNESVNSTPPRPVRSSSSFSSEGYMYNGAPNDLWRTSRNFGNAGTLGYSNVAEDFDPNVTIGPVATNFRNSINPSKGLLDL
The following text describes a protein:
Function:
Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity).
Miscellaneous:
MISCELLANEOUS: The atypical heteromeric and topological design of the odorant receptors appears to be an insect-specific solution for odor recognition, making the OR/Orco complex an attractive target for the development of highly selective insect repellents to disrupt olfactory-mediated host-seeking behaviors of insect disease vectors. Odor-evoked OR currents are independent of known G-protein-coupled second messenger pathways.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLTKKDTQSAKEQEKLKAIPLHSFLKYANVFYLSIGMMAYDHKYSQKWKEVLLHWTFIAQMVNLNTVLISELIYVFLAIGKGSNFLEATMNLSFIGFVIVGDFKIWNISRQRKRLTQVVSRLEELHPQGLAQQEPYNIGHHLSGYSRYSKFYFGMHMVLIWTYNLYWAVYYLVCDFWLGMRQFERMLPYYCWVPWDWSTGYSYYFMYISQNIGGQACLSGQLAADMLMCALVTLVVMHFIRLSAHIESHVAGIGSFQHDLEFLQATVAYHQSLIHLCQDINEIFGVSLLSNFVSSSFIICFVGFQMTIGSKIDNLVMLVLFLFCAMVQVFMIATHAQRLVDASEQIGQAVYNHDWFRADLRYRKMLILIIKRAQQPSRLKATMFLNISLVTVSDLLQLSYKFFALLRTMYVN
The following text describes a protein:
Function:
Functions in replication-dependent translation of histone mRNAs which differ from other eukaryotic mRNAs in that they do not end with a poly-A tail but a stem-loop. May participate in circularizing those mRNAs specifically enhancing their translation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MDDKPSPGLDLRHGFVHKIRKQLVKRDQSEKDFETEKMEVAKRQLAGMKKPTVRRPTQVTYCPPARRERSNSTSSAVSTSPNPSSTSASGDSDVLTATAVAREPATQYSTNGTTTVNTPPTQISPPASNKQDNMAGRGQGWGVPAAESVTVDNNNYDISGFGEEAQWYIRQALQDPTSLRKQDLCQVFNVLMWRAMEEPDYARTGAELCHAIIQVEVEKEQYDCVPTRVFQSHLRLKLLEQEMEAETLHEQSVSAWVGFVRFLCLCYHVIRVKGSPLMTMVDSVFNCLSLLALPGPLKNEMQVDCLYNLLVQMGPSLDQTVQDKMEDLFSLLRDRFLSFKTPPLARHRLLQLIELRSGGWEMEPGIQDYYSRAGKELRG
The following text describes a protein:
Function:
Acts as a positive regulator of ciliary hedgehog signaling. Required for cilia biogenesis.
Subcellular Localization:
Cell projection, cilium membrane; Single-pass type I membrane protein.
Sequence:
MQLLCWWQVLLWVLGLPAHGLEVAEDSGHPWREERPVPALQVGAVYLHEEEVAQDHRDQARAAEPMEASLGPRGDPMVVLSVVPGAAEDQRSPEAHDGTCSAQGEEDPSCGRENLFGLQGAGGFQDREEEYYAEPGVTEAEPVATEDANSTDSLKSPKVNCEERNVTGLENFTLKILNMSQDLMDFLNPNGSDCTLVLFYTPWCRFSASLAPHFNSLPRAFPTLGFLALDASQHSSLSTRFGTVAVPNILLFQGAKPMARFNHTDRTLETLKIFIFNQTGIEAKKNVVVTQADQMGPLPSTLIKTVDWLLVFSLFFLISFIMYATIRTESIRWLIPGQEQEHAE
The following text describes a protein:
Function:
Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity).
Sequence:
MANLFNWLPLLSGRQADGIKAKVEIYTWQTCPFCIRAKLLLWWKGVKFIEYKIDGDDQARQAMAARAEGRRTVPQIFVNDQGIGGCDQLYGLDSRGQLDPLLATPPNPA
The following text describes a protein:
Function:
Permease involved in the transport of the cationic neutral or acidic amino acids.
Subcellular Localization:
Plastid, chloroplast membrane; Multi-pass membrane protein.
Sequence:
MEVQSSSNNGGHSSFSSLRVYLNSLSATPSRLSRRAISVSTSSDEMSRVRAVSGEQMRRTLRWYDLIGLGIGGMVGAGVFVTTGRASRLDAGPSIVVSYAIAGLCALLSAFCYTEFAVHLPVAGGAFSYIRITFGEFPAFFTGANLVMDYVMSNAAVSRSFTAYLGTAFGISTSKWRFVVSGLPKGFNEIDPVAVLVVLVITVIICCSTRESSKVNMIMTAFHIAFIFFVIVMGFIKGDSKNLSSPANPEHPSGFFPFGAAGVFNGAAMVYLSYIGYDAVSTMAEEVENPVKDIPVGVSGSVAIVTVLYCLMAVSMSMLLPYDLIDPEAPFSAAFRGSNGWEWVTKVVGIGASFGILTSLLVAMLGQARYMCVIGRSRVVPFWFAKIHPKTSTPVNASTFLGIFTAALALFTDLNVLLNLVSIGTLFVFYMVANALIFRRYVPVGPTKPWPTLCFLTLFSITSLVFTLIWKLVPEGKPKAFMLGASAVVAIAIVLSFQCVVPQARKPELWGVPFMPWTPCVSIFLNIFLLGSLDAPSYVRFGFFSGLIVLVYLFYGVHASSDAEANGSFGVKDGQVMKELIEV
The following text describes a protein:
Function:
Plays a role in modulating the host immune response. May act as a secreted virokine by mimicking interleukin-17A (IL17A), and thereby binding to the IL17RA receptor, leading to activation of the IL17 pathway and increased secretion of pro-inflammatory factors. Contributes to the cytokine storm during SARS-CoV-2 infection when secreted by unconventional pathway. May act by down-regulating major histocompability complex class I (MHC-I) at cell surface. May inhibit expression of some members of the IFN-stimulated gene (ISG) family including hosts IGF2BP1/ZBP1, MX1 and MX2, and DHX58.
Miscellaneous:
MISCELLANEOUS: Similar to some Bat coronavirus ns8 genes, but is entirely different from SARS ns8a or Ns8b (Probable). Elicits strong specific antibody response.
Subcellular Localization:
Secreted. Note=Is secreted during a normal viral infection by unconventional pathway. Its mRNA is expressed in cytoplasm and not spliced during a viral infection, but is spliced when expressed from cDNA in nucleus. Splicing changes localization to host endosome and/or cytoplasm. May also localize in nucleus when fused with GFP.
Sequence:
MKFLVFLGIITTVAAFHQECSLQSCTQHQPYVVDDPCPIHFYSKWYIRVGARKSAPLIELCVDEAGSKSPIQYIDIGNYTVSCLPFTINCQEPKLGSLVVRCSFYEDFLEYHDVRVVLDFI
The following text describes a protein:
Function:
Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Sequence:
MTTRKPFIICDFDGTITMNDNIINIMKTFAPPEWMALKDGVLSKTLSIKEGVGRMFGLLPSSLKEEITSFVLEDAKIREGFREFVAFINEHEIPFYVISGGMDFFVYPLLEGIVEKDRIYCNHASFDNDYIHIDWPHSCKGTCSNQCGCCKPSVIHELSEPNQYIIMIGDSVTDVEAAKLSDLCFARDYLLNECREQNLNHLPYQDFYEIRKEIENVKEVQEWLQNKNAGESSLK
The following text describes a protein:
Function:
Choline transporter.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MNFYVTVIQIYNLFCLYWGLCFVSSVSENVLAGAFGSLYSARNKPRDVPIYALTQSFYRTTFNRGTIAYVSSIAIMRSFQILPEYLIKKWHLDFECCGEIICCCRHSRSCFTRAFIFVWDHFLYVSGTGTYLCVIAALEGKKFSVSASKAKLRKLNRVNEVASVANLLIFISRLLVSTSVGILIFFVFTDRIGYLPPTHYKVVAAATTLFAAHFISGLFFGVYAVAIDTIAICFDEDQKRNNVTLADPLYSSEELITILG
The following text describes a protein:
Function:
Catalyzes the decarboxylation of malate to pyruvate. In vitro, shows malolactic enzyme activity in the presence of NADPH. However, it is unlikely that this activity is of relevance in E.coli, which produces little NADPH.
Miscellaneous:
MISCELLANEOUS: Cannot use NAD(+).
Domain:
The-C-terminal phosphate acetyltransferase domain is responsible for oligomerization, and is responsible for inhibition by acetyl-CoA and activation by glutamate, aspartate, and glucose-6-phosphate as shown by its deletion. The isolated domain does not catalyze the interconversion of acetyl-CoA and acetyl-phosphate.
Sequence:
MDDQLKQSALDFHEFPVPGKIQVSPTKPLATQRDLALAYSPGVAAPCLEIEKDPLKAYKYTARGNLVAVISNGTAVLGLGNIGALAGKPVMEGKGVLFKKFAGIDVFDIEVDELDPDKFIEVVAALEPTFGGINLEDIKAPECFYIEQKLRERMNIPVFHDDQHGTAIISTAAILNGLRVVEKNISDVRMVVSGAGAAAIACMNLLVALGLQKHNIVVCDSKGVIYQGREPNMAETKAAYAVVDDGKRTLDDVIEGADIFLGCSGPKVLTQEMVKKMARAPMILALANPEPEILPPLAKEVRPDAIICTGRSDYPNQVNNVLCFPFIFRGALDVGATAINEEMKLAAVRAIAELAHAEQSEVVASAYGDQDLSFGPEYIIPKPFDPRLIVKIAPAVAKAAMESGVATRPIADFDVYIDKLTEFVYKTNLFMKPIFSQARKAPKRVVLPEGEEARVLHATQELVTLGLAKPILIGRPNVIEMRIQKLGLQIKAGVDFEIVNNESDPRFKEYWTEYFQIMKRRGVTQEQAQRALISNPTVIGAIMVQRGEADAMICGTVGDYHEHFSVVKNVFGYRDGVHTAGAMNALLLPSGNTFIADTYVNDEPDAEELAEITLMAAETVRRFGIEPRVALLSHSNFGSSDCPSSSKMRQALELVRERAPELMIDGEMHGDAALVEAIRNDRMPDSSLKGSANILVMPNMEAARISYNLLRVSSSEGVTVGPVLMGVAKPVHVLTPIASVRRIVNMVALAVVEAQTQPL
The following text describes a protein:
Function:
Mediates zinc uptake. Has broad metal specificity and can also mediate the uptake of cadmium, cobalt, iron, manganese and possibly copper. Has a slight preference for zinc.
Miscellaneous:
MISCELLANEOUS: The proton motive force but not bicarbonate or other ions might be involved in ZupT-mediated metal-uptake. In an alternative model, metal-uptake might be driven simply by the concentration gradient of labile transition metal cations.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
Contains an asymmetric binuclear metal center in the transmembrane domain: one metal-binding site, M1, binds zinc, cadmium, and iron, while the other, M2, binds iron only and with higher affinity than M1. Zinc is transported from M1, while iron is transported from M2. Iron transport from M2 does not inhibit the zinc transport activity but slightly stimulates it.
Sequence:
MSVPLILTILAGAATFIGAFLGVLGQKPSNRLLAFSLGFAAGIMLLISLMEMLPAALAAEGMSPVLGYGMFIFGLLGYFGLDRMLPHAHPQDLMQKSVQPLPKSIKRTAILLTLGISLHNFPEGIATFVTASSNLELGFGIALAVALHNIPEGLAVAGPVYAATGSKRTAILWAGISGLAEILGGVLAWLILGSMISPVVMAAIMAAVAGIMVALSVDELMPLAKEIDPNNNPSYGVLCGMSVMGFSLVLLQTAGIG
The following text describes a protein:
Function:
NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of the anamorsin/DRE2 homolog, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins.
Subcellular Localization:
Cytoplasm.
Sequence:
MLTALKQPTGDIVIAAMENKRKLLVLYATETGNAQDVAERIAREAERRYYAPVLQSTASYEPSALPSEENVIIVASTCGQGDPPAAMKVFWRQLLRKSLGQDWLEGMHYAVFGLGDSGYQKYNLVAKKLDRRLSDLGAKPIVPKGLGDDQHRSGYEAALDPWLANLWTALRERIALPYGLQDPDNNDMSSTQLDCPKFSVKFHNSASASQMESLTIADIDATRAVQEKWVDYQKARVMLESAAGDAPTSMEPEVPGYGPDQPMFAKMTANKRLTAEDHSQNVRHLEFDLGPNGVKYHPGDILTLIPRQNPDDVEAFLQRLSLDGDSYVTVEASQSELTCSWNDPQLLQLGPVKLRTLVEGVLDVSSASPRRYFFEVMSHFAAAEHEKERLQYFATSEGRDDLYQYNQRERRSVLEVLLDFPSVQLPLEWVLQIVPRLKPRSFSIASSQRAHPQQAHLTMAVVEWMTPFKRKRHGLCSTWLAQLDPSVGEVYVPVWITRGALKLPPPSVPLILVGPGTGCAPFRSFVEDRNILSQTEPVAPILFFFGCRNQAKDYLYKDFWQSCTTDHKVMSPDSGGGLHVAFSRDQGQKVYVQHKIRENRKLVWRLLQSGAAIFISGSANKMPAQVTSAFEEIIASEAGISREAAIRWLKQMELKGRFSVEAWS