lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Contributes to spectinomycin and tetracycline resistance.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNRTQLLTLIATGLGLFMIFLDALIVNVALPDIQRSFAVGEDGLQWVVASYSLGMAVFIMSAATLADLDGRRRWYLIGVSLFTLGSIACGLAPSIAVLTTARGAQGLGAAAVSVTSLALVSAAFPEAKEKARAIGIWTAIASIGTTTGPTLGGLLVDQWGWRSIFYVNLPMGALVLFLTLCYVEESCNERARRFDLSGQLLFIVAVGALVYAVIEGPQIGWTSVQTIVMLWTAAVGCALFVWLERRSSNPMMDLTLFRDTSYALAIATICTVFFAVYGMLLLTTQFLQNVRGYTPSVTGLMILPFSAAVAIVSPLVGHLVGRIGARVPILAGLCMLMLGLLMLIFSEHRSSALVLVGLGLCGSGVALCLTPITTVAMTAVPAERAGMASGIMSAQRAIGSTIGFAVLGSVLAAWLSATLEPHLERAVPDPVQRHVLAEIIIDSANPRAHVGGIVPRRHIEHRDPVAIAEEDFIEGIRVALLVATATLAVVFLAGWRWFPRDVHTAGSDLSERLPTAMTVECAVSHMPGATWCRLWPA
The following text describes a protein:
Function:
Acts as a co-chaperone for HSP90.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
SRQPEVLWAQRSEKVYLTISLPDAKDVSLKCEPDGVFNFSAVGVNGDSFSVTLQLFGSISPERCKTNIGLRNILCSIQKEQKGWWPRLLKAPEKPAPYLKVDWNKWCDEDDEEYSDSEDGGVAYTGEDDESSDDGGMLYLPDLEKARGN
The following text describes a protein:
Function:
Chaperone required for the production of an active PaoABC aldehyde oxidoreductase. Stabilizes the PaoC subunit and is required for the insertion of the molybdenum cofactor into this subunit. Binds molybdenum cofactor. Binds the molybdopterin cytosine dinucleotide (MCD) form of the cofactor after its formation by the molybdenum cofactor cytidylyltransferase MocA.
Sequence:
MSYPLFDKDEHWHKPEQAFLTDDHRTILRFAVEALMSGKGAVLVTLVEIRGGAARPLGAQMVVREDGRYCGFVSGGCVEAAAAFEALEMMGSGRDREIRYGEGSPWFDIVLPCGGGITLTLHKLRSAQPLLAVLNRLEQRKPVGLRYDPQAQSLVCLPTQTRTGWNLNGFEVGFRPCVRLMIYGRSLEAQATASLAAATGYDSHIFDLFPASASAQIDTDTAVILLCHDLNRELPVLQAAREAKPFYLGALGSYRTHTLRLQKLHELGWSREETTQIRAPVGIFPKARDAHTLALSVLAEVASVRLHQEEDSCLPPSS
The following text describes a protein:
Function:
Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors.
Sequence:
MPPDISGKWILETNDRLEDYMKALNIDFATRKIALALSQTKLITQDGDKFTIKTCSTFRNYEISFTVGVEFDEHTVGLDNRHVKSLIKWEGDELVCTQTGQKANRGWKHWLQSEKLYLVGRKHHSFASHYCPFFSFLLKRIDCFSTGADV
The following text describes a protein:
Function:
Catalyzes efficient racemization of N-succinyl-L-Arg and N-succinyl-L-Lys, suggesting that these are physiological substrates of this enzyme. Has low activity with L-Asp-L-Lys, and even lower activity with L-Leu-L-Arg, L-Leu-L-Lys, N-succinyl-L-His and N-succinyl-L-Met (in vitro).
Miscellaneous:
MISCELLANEOUS: Part of a large, functionally divergent protein family. Protein modeling and substrate docking was used to predict the substrate specificity, prior to biochemical analysis.
Sequence:
MKITAIHLYAIRLPLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEGVADDHVTGESWESTFHTLKHTLTPALIGQNPMNIEKIHDMMDNTIYGVPTAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFPVTHVLSIADPENMAEEAASMIQKGYQSFKMKVGTNVKEDVKRIEAVRERVGNDIAIRVDVNQGWKNSANTLTALRSLGHLNIDWIEQPVIADDIDAMAHIRSKTDLPLMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVASSAGFHVAFSKKIITSVELTGPLKFTKDIGNLHYDVPFIRLNEKPGLGIEINEDTLQELTVFQDIVR
The following text describes a protein:
Function:
Divinyl ether synthase involved in oxylipin biosynthesis. Catalyzes the conversion of (13S)-hydroperoxy-(9Z,11E)-octadecadienoate (13-HPOD) to etheroleate and (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate (13-HPOT) to etherolenate. Has no activity with the corresponding 9-hydroperoxides (9-HPOD and 9-HPOT).
Sequence:
MASSGSSNLPTKEVPGSYGLPVLGAQKDNLDFLHLQGEVEFFKSRVAKYNSTVFKVNFIPGNPAFPDPRGIALLDQSSFPVLLDSSKVDKTNVFTGSYKASDDFTGGYRVLSYLDTTDPKHATLKNFAFEVLKRNGRKFLPEFQSAFHAAFDAAESELSSGKNKADMAPLLNQLAFQFLAKSIVNVDPLTTKLADQGPTHLLRWIGIQFAPVAPGNSTPLPGFAEDVVIRTAPLPFLLVKADYDKLCEFFQLATEMLDMGEKEFGLSREEAVHQLLFLVGMNSWFGFSARVLPNLLYRVGTLGAEFQKRLGDEIRAAIDVSDPAGSFYGALEKMPLLKSTVLEVFRFDPPVLYQYGRPREDMVVESHDAKFVIKKGQLLGGSQALVCRDPKVFEEPDQLIPDRFVGKEELQANVFWSNGRNTKSPTADDKQCAGKNFVETIARFYLVQLFARYKTFELSEDSTLNTPFLKSFARN
The following text describes a protein:
Function:
TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Domain:
Shows a remarkable charge distribution with the N-terminus being highly negatively charged, and the cytoplasmic C-terminus positively charged.
Sequence:
MASRKQWTFWALLFASLLLSSCVLRAAAAVDDDDVYEDDEEEVDLPPMEEEVTAPPERVQPQTITMYPEGLPGVETVFVFPNNVQRQVPAGAPVDLLVGLANNGDSSITVKMIAGYLSYSRDYSQVIQNFTQFPFDTTVEPGEQHSFAYTFATHKLLQPHEFGFTAAVYYESDGAVHSNVFYNGTVEVVEPSGILSGENAFLALLALALLSLLGYWAYSQVQKLTKKKGGRRKVVETGTRSDASDNEWLKGTSADPRRRSSGTIKVTKKKE
The following text describes a protein:
Function:
May bind androgens and other steroids. May be under transcriptional regulation of steroid hormones (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MRLSVTALLVTLALCYYEANAIVCPTFAADLTEFFYFPDLLYRLSLAKYNAPPEAVAAKMEVKQCTDRFSVKNRLIITNILGKILLNCTVTDVKAVLNPSSA
The following text describes a protein:
Function:
Positively regulates the expression of ver-1 in the amphid sheath glia of amphid sensory neurons. Together with ehn-3, plays a role in somatic gonad development and is required for proper gonadal primordium assembly and somatic gonad precursor cell morphology.
Subcellular Localization:
Nucleus.
Sequence:
MDELNACTECGFTTTVFSEFQGHIEKHENEHSRSSSGEMSNSQTIEWGDGIQSSTPSPRSTPPSDPTPSPDSDEHLEHHISITEITNTLIKKEPGTKGQKTVHVCPHCNFTTCMSQHMKSHLEAHERHQGQMYQCDICKMQFSQKANMHRHRMRHSGVKPYECRFCKKRFFRKDQMQEHSMTHIKTGFGFDCPVSQCNMQFSQHNALRAHLEETHTISSTNPASCKRCNLMFANSRRLLLHFQTRHDDSESSPKKENTPKRKKLSNGNALPMDPANMSITEQLQRMVKSEFSPPNTDTSDNSTSSEFDKIPPSFPMANPDILLMCLNQMNQFNGFGENIPRPMLNIPNIPLPALHNIPAVAAIVKQDQVQLWSEQTSSSVSVSAPSPSEQSHSPPANESSLSLTEKEKSPTPEKEDEENVECCHCGMMFYDNTMYLLHKSLHSDGDPFKCALCGTQCGEKYMFTTHVIFADHSTQATTSA
The following text describes a protein:
Function:
Component of the central kinetochore, which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle-microtubule attachments and proper chromosome segregation; Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Miscellaneous:
MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores.
Sequence:
MSLILDDIILSLTNANERTPPQALKTTLSLLYEKSKQYGLSSPQLQALVRLLCETSIIDTVTKVYIVENCFLPDGYLTKELLLEIINHLGTPTVFSRYRIQTPPVLQSALCKWLVHVYFLFPVHSEREHNISSSIWLHLWQFSFLQKWITPLVIWQATTPVDVKPWKLSIIKRCAMHPGYRDAPGSATLILQRFQCLVGASSQITESIITINCNRKTLKSHRNLKLDAHFLSILKRILSRAHPANFPADTVQNTIDMYLSEIHQLGADSIYPLRLQSLPEYVPSDSTVSLWDVTSLEQLAQNWPQLHIPNDVDYMMKPSLNSNVLLPRKVMSRDSLKHLYSSIILIKNSRDESSSPYEWCIWQLKRCFAHQIETPQEVIPIIISVSSMDNKLSSRIIQTFCNLKYLKLDELTLKKVCGGILPLWKPELISGTREFFVKFMASIFMWSTRDGHDNNCTFSETCFYVLQMITNWVLDDKLIALGLTLLHDMQSLLTLDKIFNNATSNRFSTMAFISSLDILTQLSKQTKSDYAIQYLIVGPDIMNKVFSSDDPLLLSAACRYLVATKNKLMQYPSTNKFVRMQNQYIMDLTNYLYRNKVLSSKSLFGVSPDFFKQILENLYIPTADFKNAKFFTITGIPALSYICIIILRRLETAENTKIKFTSGIINEETFNNFFRVHHDEIGQHGWIKGVNNIHDLRVKILMHLSNTANPYRDIAAFLFTYLKSLSKYSVQNS
The following text describes a protein:
Function:
Together with dys-1 and hlh-1, participates in a common muscular function.
Sequence:
MPVRKKHGPYDIIADDVYDCRIPLHNELAYQHGIHFEAKYVGSMEIPRPGTRIEIVAAMRRVRYEFKARGIKKRPVDITVSVDGVKVVLQRKKQKEKGLSWDESKLLVMFHPIYRIFYVSHDSQDLQIFSYIARDGASNTFKCNVFKCSKKSQAMRVVRTIGQAFEVCHKVAQDQMQEKHEDEAAKSKISMQSEDEAGPNALDVIEERGGREEDSRSSSPMEAPPVGGPLYGKRLSLFQPRKPSTTSSSGGTAIDTTAIPENVLEIPNTSHPILQPKAPELVPQLQPQTALPYQQKPQSLLNIQQQQFNTLPSQMPSTQTLPSLSENPGQSHIPRMMTMPPNMPYPTATLPHPRTWAPQIPSYPNSMQSLEQNVPMYYPQMPGMLPSSSSLPFGLSSPVMVSPYATLQLNMQSQQLDQPDHSGSQITMDQYNQQLMRSQLDQAQQSVQVAGCQVQLLRDQLTSETTARLEAQSRTHQLLSANRDLLEQVQNLVSRLQMLETKITSEIHHSSSQPPQHQPIYQPSTSTPLNPKMPLSIDHNDPRIPGNSSIRLNYPYQVQPLADLRAGSLPPVKESKERRKDEGTRTEPESNAEDTTDYSSSDQYERTSNVMKPSHFNILMSNPLVDINVPSGAAMSSRMEQFDMGDTPGTSSTPPKKEKKPSSGILRGENFSRMSFNPKLGREKEREQQQLMFEDTLEDDSPRSIPPSPPSKARNTTIDSLFKPQDDPPTIADREPQQLPPQPSQQNQKKNTAVNLLMPTMPASSSLVTAMYPPMRQPAVPVNKIQPKVDVFRKKTLKTLSMDIAEEPEPSEMDPNRNNLPSSTNSSMKRRGFLPPPNTDVEIKEIEDYINRNVDRSKLPETSLLTRLTRQAQGDNSLGNLPNGYPQ
The following text describes a protein:
Function:
Inclusion body (IB) resident protein that interacts strongly with lipid droplet (LD) proteins. Involved in LD-mediated IB clearing after protein folding stress, probably by enabling access to the IBs of an LD-stored soluble sterol derivative that acts as a chaperone in inclusion clearing.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Localized exclusively in cytoplasmic inclusion bodies under protein folding stress conditions.
Sequence:
MSKSQEQRLQNFVTVIQGLNDILDDKMDEATEKFKSGNSSFHLSGQAVVAFIQAVLTFEPSRFKDSQNRIDIAIKALSADKDDASKNNTFLSTFDPGVEYRVSIGLMLLLSALIGFCSESIVTSVKSVYKLRKAHSIFSKINKRHFDHFSAAFHSTGRSDVDLANEYVQTGTLLCTGLFTLLISLLPPKMITILNVFGYKGDRDWALQCMWMPALQRPTSFFAAVAFAALIQYYSGAVQLCSIYKKTPEEPDGWPDKRCFEILEKVEKAHPDGPMWPLHRAKLLSMVKKQDEAIVVLEELMAKPPPRLKQLEVLIVFEHALDCAFSHRYVDGANSFLKLSSLNDSSTALYSYFAAACFLQDVHVNANVEALEKASKLLEPLHDLVANKTAPLDVHIRRKVGKLIKRRASAGNQGGLAEYVGFSPLYELVYVWNGFRRMTDDELSKFDVERMEPWQDQDDDICQALIKATVLRNLGRTDEVFPILQKICAVTRTTETWAVAFAHYEMAVAFFESNGSKKEGLKHCDAYLRKARDFGGDNEFESRLIIRVQLARHVVRKCLQSMS
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with tut-1/ctu-1 that ligates sulfur from thiocarboxylated urm-1 onto the uridine of tRNAs at wobble position.
Subcellular Localization:
Cytoplasm.
Sequence:
MELGNFVTDLNGKKCVKCDKDAKFTGVDPKKAWYCQECFVQMVRNKFRSSLSKKKIYKDADARDTLIVFDGTLSGTFLLHQINDALKQITYKRLMVKPTVLVLVSLTEDTEIQMVIKRIQEIKKSVLENVRWVVAHLACSMYDEDFKLKENECNGVEKISDYNQLIASCSVPTYRKELERVLKEKCLQKIACSMGILKCMVPDHADDLGRLAIDQLCLGRGGSISTLVTVTDKRPDFMLIRPLCDISKKELAVYNYLCDIDKHCIHIAQQNNQQKSVQTLTDAFICTLENEKFYSTINTVLSTAAKIHNTSIGKDDSKCSFCNVEVADSVCSTCSAIRECTGDLLTLLF
The following text describes a protein:
Function:
Amidase with broad substrate specificity, catalyzing the hydrolysis of a wide range of N-substituted amides, and, to a lesser extent, the hydrolysis of non-substituted amides. Acid para-nitroanilides (4'-nitroacetanilide, Gly-pNA, Ala-pNA, Leu-pNA) are the best substrates for this enzyme. N-substituted acrylamides (isopropyl acrylamide, N,N-dimethyl-aminopropyl acrylamide, and methylene-bis-acrylamide), N-acetyl derivatives of glycine, alanine and leucine, and aliphatic amides (acetamide, acrylamide, isobutyramide, n-butyramide, and valeramide) can also be used as substrates but with less efficiency.
Sequence:
MTEQNLHWLSATEMAASVASNNLSPNEIAEAMIQRVDAVNPSINAIVQFDREQVTRDAAELSRQQEAGEKLGPLHGVPFTIKDLTAVDGLPTTFGMKPMADNIATGNAVVVDRLRGAGGLFLGKTNTPESGYYGGTDNHLYGPTHNPWKLGNSAGGSSGGASAAVAAGLGPLAEGSDGAGSVRIPSALCGVVGLKPTTGVIPQTILAGRFYNWAYHGPITRTVADNALMLDIMAGPDNADPLSIERAETSYVEASKGDVKGLRVAWSPNLGLGHVDPEVLAVCLDALAAFEELGAQITEATPQWGNPSESMWSGIWVPGFASEYDLLDWENQRGEVDDYLIEIMHEAERLTGVDVGRADAFRGDMWDTWTTFMNDYDVLVSPTLASATFPLRQFAPSWLEGASLREQLLDWLFTYPYNMLNNPAITVPAGFTADGRPVGLQIAARHRRDALVLRTAANFEAVRPWADKKPADSLVVA
The following text describes a protein:
Function:
Required for vacuole segregation and vacuole protein sorting. Possibly part of a complex which tethers the vacuole membrane to microtubules, either directly or via kinesin or dynein-like motor proteins. Probably functions in several interorganelle traffic pathways.
Miscellaneous:
MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
Subcellular Localization:
Vacuole membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MDLENVSCPICLRKFDNLQALNAHLDVEHGFNDNEDSLGSNDSRLVNGKQKKARSVDSSAQKLKRSHWEKFKKGKSCCHTCGRTLNNNIGAINCRKCGKLYCRRHLPNMIKLNLSAQYDPRNGKWYNCCHDCFVTKPGYNDYGEVIDLTPEFFKVRNIKREDKNLRLLQLENRFVRLVDGLITLYNTYSRSIIHNLKMNSEMSKLERTVTPWRDDRSVLFCNICSEPFGLLLRKHHCRLCGMVVCDDANRNCSNEISIGYLMSAASDLPFEYNIQKDDLLHIPISIRLCSHCIDMLFIGRKFNKDVRMPLSGIFAKYDSMQNISKVIDSLLPIFEDSLNSLKVETAKDSENTLDPKNLNDLARLRHKLLNSFNLYNTLTRQLLSVEPQSHLERQLQNSIKIASAAYINEKILPLKSLPAILNPEGHKTNEDGQKAEPEVKKLSQLMIENLTIKEVKELREELMVLKEQSYLIESTIQDYKKQRRLEEIVTLNKNLEELHSRIHTVQSKLGDHGFN
The following text describes a protein:
Function:
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules.
Subcellular Localization:
Chromosome, centromere. Nucleus. Chromosome, centromere, kinetochore.
Sequence:
MLTMSHIKTEEELALFDKSIDEFWTKFKNTWISEYSCQTVTLRDAHKEAIKALTERWSVKLKEEGQMVEKILEYKREIHRQNKIIKEKKDNLSELLSKIHDGQQQKEMWTQSIQNLKEELAKKKQIISTTNEANKEKLKGLNKSSEYFKDRLGLEIRNTHGGKLQFIFRNIDPKDHEKPFMFSLCLNEEGNYEVTESSPHLDCLAELQEKVRETNNFSAFLANVRKAFIGLVYN
The following text describes a protein:
Function:
p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-BMAL1 heterodimer in association with altered stability and subcellular distribution.
Miscellaneous:
MISCELLANEOUS: Cleavage of p35 to p25 may be involved in the pathogenesis of cytoskeletal abnormalities and neuronal death in neurodegenerative diseases. The p25 form accumulates in neurons in the brain of patients with Alzheimer disease, but not in normal brain. This accumulation correlates with an increase in CDK5 kinase activity. Application of amyloid beta peptide A-beta(1-42) induced the conversion of p35 to p25 in primary cortical neurons. Expression of the p25/Cdk5 complex in cultured primary neurons induces cytoskeletal disruption, morphological degeneration and apoptosis.
Subcellular Localization:
[Cyclin-dependent kinase 5 activator 1, p35]: Cell membrane; Lipid-anchor; Cytoplasmic side. Cell projection, neuron projection. Note=In the primary cortical neurons, p35 is present in the peripheries and nerve terminals; [Cyclin-dependent kinase 5 activator 1, p25]: Nucleus. Cytoplasm, perinuclear region. Perikaryon. Note=The conversion of p35 to p25 relocalizes the protein from the cell periphery to the cytoplasm, in nuclear and perinuclear regions. In the primary cortical neurons, p25 is primarily concentrated in the cell soma and is largely absent from neurites.
Sequence:
MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKVQPNSSYQNNITHLNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGGSSSVKKAPHPAVTSAGTPKRVIVQASTSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNEISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR
The following text describes a protein:
Function:
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Sequence:
MKQRKRSHIKYFPTPIIEGQYGVVPARAVPSHIQRPSYLSETKPIYGIYEGAPVVHNYDMIQSKLHDLKIELRKAAQIAAQTAYVAQKSVKQGMTTDDLDKIVHEFIISQNAYPSPIGFMGFPKSVCTSVNEVCCHGIPNLRPLDGGDSLNIDVTIFYDGVHGDTSVMAQVPDMNPEITKLIDTTQKALYEAIKICKPGQKFSKIGDIVEEVAADEGFTVCELFTGHGIGELMHMPPTIIHNFNDYPGVMVPGNVFTIEPILLMRHGQYSMWKDNFTVVSPDNPSGIVNLSTVAQWEHMVLITENGYEVLTKREDETGI
The following text describes a protein:
Function:
Part of the ABC transporter complex YclNOPQ involved in uptake of ferric-petrobactin. Petrobactin is a photoreactive 3,4-catecholate siderophore produced by many members of the B.cereus group, including B.anthracis. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MRNQMKIALLVGLAIVCIGLFLFYDLGNWDYTLPRRIKKVAAIVLTGGAIAFSTMIFQTITNNRILTPSILGLDSLYMLIQTGIIFLFGSANMVIMNKNINFIISVLLMILFSLVLYQIMFKGEGRNIFFLLLIGIVFGTLFSSLSSFMQMLIDPNEFQVVQDKMFASFNNINTDLLWLAFIIFLLTGVYVWRFTKFFDVLSLGREHAVNLGIDYDKVVKQMLIVVAILVSVSTALVGPIMFLGLLVVNLAREFLKTYKHSYLIAGSVFISIIALVGGQFVVEKVFTFSTTLSVIINFAGGIYFIYLLLKENKSW
The following text describes a protein:
Function:
Transcriptional activator that exhibits a unique DNA binding specificity for CpG motifs; enriched at promoters containing the trimethylation mark on histone H3 'Lys-4' (H3K4me3). Forms part of the SET2 complex and interacts with the SIN3S HDAC complex at promoters. Required for H3K4 trimethylation and plays a repressive role in the expression of heat shock and salt-inducible genes. Required for fertility, in cooperation with class I histone deacetylases (HDACs).
Subcellular Localization:
Nucleus.
Sequence:
MSNKEIEDNEDVWKERCMNCIRCNDEKNCGTCWPCRNGKTCDMRKCFSAKRLYNEKVKRQTDENLKAIMAKTAQREAAHQAATTTAPSAPVVIEQQVEKKKRGRKKGSGNGGAAAAAQQRKANIINERDYVPNRPTRQQSADLRRKRTQLNAEPDKHPRQCLNPNCIYESRIDSKYCSDECGKELARMRLTEILPNRCKQYFFEGPSGGPRSLEDEIKPKRAKINREVQKLTESEKNMMAFLNKLVEFIKTQLKLQPLGTEERYDDNLYEGCIVCGLPDIPLLKYTKHIELCWARSEKAISFGAPEKNNDMFYCEKYDSRTNSFCKRLKSLCPEHRKLGDEQHLKVCGYPKKWEDGMIETAKTVSELIEMEDPFGEEGCRTKKDACHKHHKWIPSLRGTIELEQACLFQKMYELCHEMHKLNAHAEWTTNALSIMMHKQPNIIDSEQMSLFNKSQSTSSSASAHGATTPISSTSSSSSSSSKNDDEMEDTAEFLANLAVQKEEETQNN
The following text describes a protein:
Function:
Deoxyribonuclease which catalyzes (in vitro) the decatenation of kinetoplast DNA, which are circular DNA catenated to each other, producing linear DNA molecules. Plays an important role in chromosomal segregation and cell cycle progression during eye development probably via its DNA decatenation activity.
Sequence:
MFQGCYGGTQKHEPDLHIVLERAWQQGLQKVIVTAGCLKDVDEALELASKDERIYTTVGTHPTRCEEFVPDPEGYYDQLRSRIKANRTKVRAVGECGLDYDRLHFCAQETQRLYFEKQLDLAAEFKLPLFLHMRNAAEDFMGILERNRNKIEECGGGVVHSFTGTLEEAQRILAFGGLYIGFNGCSLKTDENAEVVRKLPNDRIMLETDCPWCGIRPSHAGHKHVTTKFPTVKKKEKWTAESLIDGRCEPCQISQVLESIAGIKQEPKEQLAALYYQNTLDLFFGTGESKE
The following text describes a protein:
Function:
Component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions.
Miscellaneous:
MISCELLANEOUS: Present with 243 molecules/cell in log phase SD medium.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Vacuole membrane; Peripheral membrane protein; Cytoplasmic side. Note=Also localizes to membranous structures both proximal to, yet distinct from, the plasma membrane as well as within the cell interior, probably endosomal or Golgi membranes.
Sequence:
MVHRGRTLKSDTDVTSLNASTVSHQSKPFRQFSTRSRAKSNASFKGLRRVLTHDGTLDNDYFNKHNVSQKCKSSDALFRKRTISGLNMTALTRVKSNQGKRSASFHSPVHNTLLSPKNSSHSNTGTAGFGLKPRRSKSTQSVLSLRDAQESKKSESTTDEEVECFSEDNIEDGKVNNDKVIAEHVMPEEKKNVQQLNQNELQSPDSIDEQEEDKSGTDGKENHRAVSLPLPHLSSNNYFGESSHSIEHQKDGETSPSSIETKLNATSVINEEGQSKVTKEADIDDLSSHSQNLRASLVKAGDNISEAPYDKEKKILDVGNTLAAHKSNQKPSHSDEQFDQEDHIDAPRSNSSRKSDSSFMSLRRQSSKQHKLLNEEEDLIKPDDISSAGTKDIEGHSLLENYAPNMILSQSTGVERRFENSSSIQNSLGNEIHDSGEHMASGDTFNELDDGKLRKSKKNGGRSQLGQNIPNSQSTFPTIANIGSKDNNVPQHNFSTSISSLTNNLRRAAPESFHGSRMNNIFHKKGNQNLLLRSNDLNKNSAAPASPLSNEHITSSTNSGSDANRQSNSGAKFNSFAQFLKSDGIDAESRTQRKLWLQRENSIMDLSSQNDGSDSIFMAGNIDAKREFERISHEYSNVKRFYNPLDEALLRVQPIITGNANNIRKKSHNDAQSIAHSSSDTDHKDEDDLLFTNYDKKFDDLYPHLASAKIQAVLSGIWKSESYLFNKDVNPINKNRTTSTNHSVGHTASQNARNLLRGPMGSSTTLHHQRVINSLQPTTRAVNRRMENVGYMHTQPQQR
The following text describes a protein:
Function:
Subunit of the two-component enzyme NicAB that mediates nicotinate hydroxylation, the first step in the aerobic nicotinate degradation pathway. Mediates conversion of nicotinate into 6-hydroxynicotinate (6HNA).
Subcellular Localization:
Membrane; Single-pass membrane protein.
Domain:
The cytochrome c domains probably enable interaction with the electron transfer chain, possibly by delivering the electrons to a cytochrome oxidase.
Sequence:
MNHSQQVPSRDQLLAKTGVLLIVDQITPPSGPVAKGVTPTVKERELALFIAVSDDGMVYAFNGHVDLGTGIRTSLAQIVAEELDLRMDQVHMVLGDTERAPNQGATIASATLQISAVPLRKAAATARRYLLQQAALRLGCPPEMLRIEDGTVIASNGSTLSFAELVQGKNHQLHIADDAPLKAIEDYRLVGRSAPRVDIPGKATGELTYVHDMRLPNMLHGRVIRPPYAGHDSGDFVGNSLLAVDESSIAHLPGVVAVVVIRDFVGVVAEREEQAIRAAHELKVSWKPFTGKLPDLSDVAQAIRDNPRVQRTVLDQGDVDGGIANASQRLSRSYLWPYQLHASIGPSCALADFTAGQIRVWSGTQNPHLLRADLAWLLACDEARIEIIRMEAAGCYGRNCADDVCADAVLLSRAVQRPVRVQLTREQEHVWEPKGTAQLMEIDGGLNADGSVAAYDFQTSYPSNGAPTLALLLTGAVEPVPALFEMGDRTSIPPYDYEHMRVTINDMTPLVRASWMRGVSAMPNSFAHESYIDELAFAAGVDPVEYRLKHLSDPRAIDLVKATAERAQWQPHTRPMQTQAEGDVLRGRGFAYARYIHSKFPGFGAAWAAWVADVAVDRRTGEVAVTRVVIGHDAGMMVNPEGVRHQIHGNVIQSTSRVLKEQVSFEESTVASKEWGGYPILTFPELPAIDVMMLPRQHEPPMGSGESASVPSAAAIANAIFDATGIRFRELPITAERVRAALGGEGQGPDAPAPAQPSTKRSKWWFGSLAGVFGAALGMLATALPWRAEIAPVTPPGVGSWSAAMLERGRQVAAAGDCAVCHTVSGGKANAGGLAMDTPFGTLYSTNITPDPETGIGRWSFAAFERAMREGISRDGRHLYPAFPYTSFRNINDADMQALYAYLMSQTPVRQEAPANQMRFPFNQRPLMAGWNARFLQRGEYQPDPQRSAQWNRGAYLVDGLGHCTACHSPRNLMGAEKGGSSYLAGGMVDGWEAPALNALGKSSTPWSEDELFNYLSTGFSEKHGVAAGPMGPVVSELATLPKSDVRAIAHYLSSLEGEPQALAANAAPQVDTHVSLSNGERVFKGACLGCHSDGLGPKLFGVSPSMAVNSNVHSDLPDNLLRVVLHGIPTPATRDLGYMPGFKDSLSDRQVADLAAYLRHRFAADKPAWQGLASKAAQVRANPGSH
The following text describes a protein:
Function:
Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPTQQSSQDQPAGLSESTALPPASSDPPQRQSWSSTGCALPPTTEKPPSAPIEPTPAKDTPTIQPHSKHATHLFTLSYLVFFSIFGTLARLGLQALTFYPGAPVITGVLWPNVGGSLLMGFFLEDKNLFREEWSQPPPRNPSEDSDAARQYAQNHKSVKKTIPLYIGLTTGFCGSFTSFSSFIRDVFLALTNDLPDPSVSSITSRNGGYSFMALLAVLLTTVALSLSALICGAHLALAFDGFTPSFPFRPTRRVIDPLFVLLGWGCWLGAVFLAIWPPDRSGSSINAPDTWRGRAVFAIVFAPLGCLLRYYLSVYLNPRVPAFPLGTFTVNIFGTIVLAMCFDLQRVDGVGTVIGADARSAPYAILTSCQVLQGVMDGFCGCATTVSTWVAELNGLSRRRQAYVYGVGSVAVALGFFVVIVGSLGWTRGFVDPVCT
The following text describes a protein:
Function:
Plays a role in autotrophic carbon fixation via the 3-hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the acryloyl-CoA dependent NADPH oxidation and formation of propionyl-CoA.
Sequence:
MKAVVVKGHKQGYEVREVQDPKPASGEVIIKVRRAALCYRDLLQLQGFYPRMKYPVVLGHEVVGEILEVGEGVTGFSPGDRVISLLYAPDGTCHYCRQGEEAYCHSRLGYSEELDGFFSEMAKVKVTSLVKVPTRASDEGAVMVPCVTGMVYRGLRRANLREGETVLVTGASGGVGIHALQVAKAMGARVVGVTTSEEKASIVGKYADRVIVGSKFSEEAKKEDINVVIDTVGTPTFDESLKSLWMGGRIVQIGNVDPTQSYQLRLGYTILKDIAIIGHASATRRDAEGALKLTAEGKIRPVVAGTVHLEEIDKGYEMLKDKHKVGKVLLTT