lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Functions as a ssDNA-dependent ATPase; dsDNA, ssRNA do not stimulate ATPase activity, while other nucleotides (aside from dATP) are not hydrolyzed. Functions as a ssDNA nuclease; activity does not require ATP. Functions as an ATP-dependent helicase; helicase activity requires hydrolysable ATP. Unwinds both DNA/DNA hybrids and RNA/DNA hybrids, moving mostly in a 3' to 5' direction.
Miscellaneous:
MISCELLANEOUS: Found in the E.coli-type CRISPR4/cas system.
Domain:
Proteins of this family have an N-terminal nuclease domain and a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the domains are swapped, in others they are encoded separately.
Sequence:
MKHINDYFWAKKTEENSRLLWLPLTQHLEDTKNIAGLLWEHWLSEGQKVLIENSINVKSNIENQGKRLAQFLGAVHDIGKATPAFQTQKGYANSVDLDIQLLEKLERAGFSGISSLQLASPKKSHHSIAGQYLLSHYGVDEDIATIIGGHHGRPVDDLDGLNSQKSYPSNYYQDEKKDSLVYQKWKSNQEAFLNWALTETGFNSVSQLPKIKQPAQVILSGLLIMSDWIASNEHFFPLLSLDETDVKNKSQRIETGFKKWKKSNLWQPETFVDLVTLYQERFGFSPRNFQLILSQTIEKTTNPGIVILEAPMGIGKTEAALAVSEQLSSKKGCSGLFFGLPTQATSNGIFKRIEQWTENIKGNNSDHFSIQLVHGKAALNTDFIELLKGNTINMDDSENGSIFVNEWFSGRKTSALDDFVVGTVDQFLMVALKQKHLALRHLGFSKKVIVIDEVHAYDAYMSQYLLEAIRWMGAYGVPVIILSATLPAQQREKLIKSYMAGMGVKWRDIENIDQIKIDAYPLITYNDGPDIHQVKMFEKQEQKNIYIHRLPEEQLFDIVKEGLDNGGVVGIIVNTVRKSQELARNFSDIFGDDMVDLLHSNFIATERIRKEKDLLQEIGKKAIRPPKKIIIGTQVLEQSLDIDFDVLISDLAPMDLLIQRIGRLHRHKIKRPQKHEVARFYVLGTFEEFDFDEGTRLVYGDYLLARTQYFLPDKIRLPDDISPLVQKVYNSDLTITFPKPELHKKYLDAKIEHDDKIKNKETKAKSYRIANPVLKKSRVRTNSLIGWLKNLHPNDSEEKAYAQVRDIEDTVEVIALKKISDGYGLFIENKDISQNITDPIIAKKVAQNTLRLPMSLSKAYNIDQTINELERYNNSHLSQWQNSSWLKGSLGIIFDKNNEFILNGFKLLYDEKYGVTIERLDKNESV
The following text describes a protein:
Function:
[Heme A synthase etp1(cd)]: Catalyzes the second reaction in the biosynthesis of heme A, a prosthetic group of mitochondrial cytochrome c oxidase (CcO). Heme A is synthesized from heme B by two sequential enzymatic reactions catalyzed by heme O synthase (HOS) and heme A synthase (HAS). HAS catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8, in a reaction that involves matrix ferredoxin and ferredoxin reductase. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A; [Mitochondrial ferredoxin etp1(fd)]: Iron-sulfur protein that transfers electrons in a wide variety of metabolic reactions. Involved in heme A biosynthesis and in iron-sulfur cluster assembly. Transfers electrons from adrenodoxin reductase arh1 to heme A synthase etp1(cd), a heme protein that catalyzes the conversion of heme O to heme A. Required for the de novo synthesis of Fe-S clusters on iron sulfur cluster assembly protein isu1. Interact in its reduced state with isu1 to productively deliver electrons for Fe-S cluster synthesis. Essential for coenzyme Q biosynthesis. May transfer the electrons required for the hydroxylation reaction performed by coq6 (By similarity).
Subcellular Localization:
[Heme A synthase etp1(cd)]: Mitochondrion inner membrane; Multi-pass membrane protein; [Mitochondrial ferredoxin etp1(fd)]: Mitochondrion matrix.
Domain:
[Heme A synthase etp1(cd)]: The N-half (TM1-TM4) and C-half (TM5-TM8) domains are connected by an intracellular loop. Each domain is formed from four-helix bundles and they align in a pseudo twofold symmetry manner. The N-half domain is the substrate heme O binding domain and the C-half domain is the cofactor heme B binding domain.
Sequence:
MNISRSSGLMRQFLLQPLRKGCDISCLGRSSWRMSRSFSGSSVLNEINLSRTKNLFLNDCKFNKNSFEKFFARRLSNSVAPTPGGILQETEKIPSKKVAFWLLGSSALVLAIVVVGGITRLTESGLSITEWKPITGVIPPLTDEQWNQEFELYKKSPEFEKLNSHMTVDEFKNIFFWEWFHRVLGRGIGLTILLPSIYMIVTKRASPWLSKRLIGLTGLVGLQGVIGWWMVKSGLSEELFSDGSHPRVSHYRLATHLAAAVALYIGLVWTGHGILQRHAFLKSMKSGSTSQLTSMVSSVQKMKGFRTSVNSFVGLVLITLLSGAFVAGLDAGMIYCTFPEMGEGRLAPSKSELFDQRFCRKDDKSDLIWRNMIDNPSLVQLEHRILAITTFVAACGLFIFSRAKRNILPKKIKTSINVVTGVVTAQATLGIMTLIYVVPVPLAALHQAGSLVTLTAALSLAQRLHPEYALKNIRSWTKLISSPPKSSISSSILTQQRQFHTFRPSFHSEIKKPLPGTGIKVFFVTPEGREIMIEGNEEGACEGSVACSTCHVIVDPEHYELLDPPEEDEEDMLDLAFGLEETSRLGCQVLLRKDLDGIRVRIPAQTRNIRLERPKA
The following text describes a protein:
Function:
Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Sequence:
MIIGETPPPSGAFGVDAIAMTMRFGDFLALDNVELKVRPGSFHALLGENGAGKSTLVKCIMGYYHATEGDIIVGGREQAIANPKDAHALGLGMVYQHFTLVPAMTVAENLVLARDIVPAVVDWSKEMKQLEAFLARMPFKVPLSARVSDISAGERQKCEILKQLYLKRRFLILDEPTSVLTPAEADEVLGMLRDMVVKGELTILMITHKFREVMAFADEVTILRRGKLAGAGKVAELTPDAMARTMIGAEELTVQPPRTGEAGQARLELEKIRALDDAGAIAVHDVSLTVRAGEIVGIAGVSGNGQRQLVEVLAGQREAESGEVRVAGDPYHASREEMRRHKMSLLPEEPLKNACVGGMSVADNIAFREFDRAPFASGGWWLNRSAFRNDAMKKIGQYKIKTRTPDTPISALSGGNVQRAVLARELGGDVEVLIAANPCFGLDFAAVAQIHAEIMAARNRGAAVLLVSEDLDELLELSDRLVVMFHGEFVYEARTSEADLTVIGRHMAGH
The following text describes a protein:
Function:
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in endosomal cargo sorting.
Subcellular Localization:
Endosome.
Sequence:
MHTRMPSVNSQTFAVPEGSESEDHSESGSSYAGSSLNETALDVVVEQFTAQFNPARLDRSMAQQSQLSGQMNAKQREVDEAITKVTQRLEEMKRVVADGQKNVKQVNALLEKCAKKTDKLQAETKSQFPIEYAQAGEKYSDH
The following text describes a protein:
Function:
Required for protein transport between the Golgi and the endoplasmic reticulum. May contribute to tethering of coatomer-coated retrograde transport vesicles to the ER membrane through interaction with and stabilization of the SNARE complex.
Miscellaneous:
MISCELLANEOUS: Cells with a reduced level of SEC39 show a defect in post-translational processing of PRC1/CPY.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MLEEQLYLLACIFASRADTRNIKKLSTRLGSQSKYLEILCVLWPELDDPKNLLFLRELEEEVQSPEGEETTDEDVIVELLESDSSLIPLIESDTTTRSNRYHELQEFISKKLNNKTLENFEEWLRERILICNEMIPETPLLYSVLWETAKSKVLSTKFIGWVEGVLKPLDHLNKRLHLIFKINEWEKMPDSELFKIIFDGVEDMQGYIGIADVIEDELAPTLSYGKKWETFITEFFNKQQFSLKSDTNYQLFIKLYYSLEKGVKDNSEASRKLQSNVVDILFHNSENLFNLSSLTHKLDELWSILSGFPDEITIEEQKTITALEMKQFMEFFIKCSTKFSFKEIFAITQEEESAQLAHFSSLCHEEFNKANEISSFLQAMYETVLDISKDDKIFTRISMDEKLYSILEILLQMNEFAYIEAIIERFDYSNNTQIYELLVKFFWHFFNNASNGLRKEPEMKKASQTLQIIQKHMSQRAGTNLTKLEVLLEISDKLSHYSINLNKSHNGARDTAFKPSNILEYRDCPLDIISNLLELNPRLYKDLPTTKSLLFGIYDSLSINREGQTGKVEVDLMVLHIDYALVNLDFGTAYELGKQVFEICQEAGQHMMKALGDEHWLTFYQMGKFVDPNWVDNEIPTEIIVLQMSILGRLLEVCPLEEVEIVTSQWSTLELELSARDLVKDKYALDGQNDNKSKVGGIAREIFHNVTNF
The following text describes a protein:
Function:
One of the two proteins required for the splicing of precursor tRNA molecules containing introns. The ligation activity requires three enzymatic activities: phosphorylation of the 5' terminus of the 3' half-tRNA in the presence of ATP, opening of the 2'3'-cyclic phosphodiester bond of the 5' half-tRNA leaving a 2'-phosphomonoester and ligation of the two tRNA halves in an ATP-dependent reaction.
Sequence:
MEGPLAENMTVNDVKQLVTELETASQLTKRGKASKVLCTLKYSGIKVNSWRFNEWDYGKNNISMPCNARGLFIIDDPEKPEIVARGYDKFFNVEEIAATAWKELERTTEGPYEVSLKENGCIIFIAGRPDGELVVCSKHSTGPRDDTDRNHAEAGEQFLRKLLEEAGASVETLARELYAMNCTAVAEYCDDAFEEHIIPYARDRAGLYLHGLNKNTREFQTLPMPEVKSFAEKYHLKIVDYFVKPDIETLRSFLQQCSIKGSYNDQEVEGFVIRCRKRDGHAFLFKYKFEEPYLLYRQWREATKDYINSRMRTYNFKKHRFITNKYLDFVIPLLDQDPDLCKEYIQGKGIIKLRKMFLEDFGMSGLDIMNSKTIKELEEQYASELDKVDENTKFIFIPVATVGCGKTTVALALKNIFGESWGHIQNDNIVTKDKSKLMRDALEFLQKDTSRAVIVDRNNHMPFERKQLFEWLEKMKENYIPYNSAVKVVCLSFLTYKDVESVREITKSRVAERGDNHQSIKALSEPEKAIMILDGFLKRFRAVNDQRSPDNMFDKIIQLKVLEENSSLTNIRTILEELHASYPTLVPELPSDSVIEESFKNTLSYKPTFTKIIKSSPRNTKYKPTYWGAELSDPKLFINQVSDLIVRKRPEYLRGVLDIVEEAMIQKSFHVTLIHCSAKRGNKEEKDMWAEYNKRYANHLVKPEKAPCQPPKYIETTDFIKFSIDKLLWDDKIMTATVSTDKLIYDSTGEAVPILRLLNTYAHITVGTRKAGVQAVYSNELCRRFHEKHGEEEGSFSEGMNCIRFPEPVQVVAAVRINIY
The following text describes a protein:
Function:
May have a role in mesendoderm development during embryogenesis.
Miscellaneous:
MISCELLANEOUS: Down-regulated in 12-cell embryos from mutant worms lacking skn-1.
Sequence:
MLRYIFFAAILFFVFPNTESAGFLKFELTADRDCLLHLEHSSTYSETVRLLAYESRPLEIYTQGSINEIPVHFQLLHHFSGKALSEAKFQIFQLKNNGLWDSKVIDTDKVILSVRSTFYCENGYFGPICDRRSRTFAPKSDIQTSTPGYQTQVLKFDFKISDDIIIYSSLAFFVLLLIIFNCILCCYRPKKSQKYLDVSLGSPKVFSICGYSADKSGNTTEYLDAPSRFFSSTKIECVV
The following text describes a protein:
Function:
Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Cytoplasm. Cytoplasm, perinuclear region. Nucleus.
Sequence:
MAPFLRIAFNEFNLGELPPMTEQPFCAIKMKESLSTERGKTLVQRKPTMYPAWKSTFDAHIYEGRVIQVVLMKTAEEALSEATVGVSVIAERCKKGNGHAEFWVDLQPSGKVMMSVQFFVEDTDLDSKASMTAKDDDGILTINRRRGAIKQAKVHFIKNHEFTATFFKQPTFCSVCREFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTATNSRDTMFQKERFKIDMPHRFKTNNYMSPTFCDHCGSLLWGMVKQGLKCEDCGMNVHHKCQTKVANLCGINQKLLAEALNQVSLKSSTKRPDPTLSEIGIYQAIDKNVPADPSAEGSQYGKFWDITPAVPASTIVSTVRVSLNDFVFQKVLGKGSFGKVMLAELKGKGQYFAIKALKKDVVLMDDDVECTMVEKRVLALAWENPFLTHLYCTFQSKEHLFFVMEYLNGGDLMFHIQDKGRFDLYRATFYAAEIICGLQYLHSKGIVYRDLKLDNVMLDKDGHIKIADFGMCKENMIGENRATTFCGTPDYIAPEILLGQKYSFSVDWWSFGVLLYEMLIGQSPFQGDDEDELFDSIRMDVPHYPRWITKEAKDLLEKLFERDPTRRLGVVGNIRGHAFFKTINWPALEKREVSPPFKPKVKSSSDCSNFDREFLSEKPRLSQSDKNLIDSMDQTAFAGFSFINPKMESLIDK
The following text describes a protein:
Function:
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (By similarity). This system is involved in glucose transport. The system can also transport glucosamine; In addition, plays an important role in the phosphorylation of EIIA-deficient PTS transporters. The EIIA domain can transfer a phosphoryl group to EIIA-deficient PTS transporters, enabling growth with maltose, N-acetylglucosamine, sucrose or trehalose as the sole carbon source.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
The EIIC domain type-1 forms the PTS system translocation channel and contains the specific substrate-binding site; The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-1 domain; The PTS EIIA type-1 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-1 domain.
Sequence:
MFKALFGVLQKIGRALMLPVAILPAAGILLAIGNAMQNKDMIQVLHFLSNDNVQLVAGVMESAGQIVFDNLPLLFAVGVAIGLANGDGVAGIAAIIGYLVMNVSMSAVLLANGTIPSDSVERAKFFTENHPAYVNMLGIPTLATGVFGGIIVGVLAALLFNRFYTIELPQYLGFFAGKRFVPIVTSISALILGLIMLVIWPPIQHGLNAFSTGLVEANPTLAAFIFGVIERSLIPFGLHHIFYSPFWYEFFSYKSAAGEIIRGDQRIFMAQIKDGVQLTAGTFMTGKYPFMMFGLPAAALAIYHEAKPQNKKLVAGIMGSAALTSFLTGITEPLEFSFLFVAPVLFAIHCLFAGLSFMVMQLLNVKIGMTFSGGLIDYFLFGILPNRTAWWLVIPVGLGLAVIYYFGFRFAIRKFNLKTPGREDAAEETAAPGKTGEAGDLPYEILQAMGDQENIKHLDACITRLRVTVNDQKKVDKDRLKQLGASGVLEVGNNIQAIFGPRSDGLKTQMQDIIAGRKPRPEPKTSAQEEVGQQVEEVIAEPLQNEIGEEVFVSPITGEIHPITDVPDQVFSGKMMGDGFAILPSEGIVVSPVRGKILNVFPTKHAIGLQSDGGREILIHFGIDTVSLKGEGFTSFVSEGDRVEPGQKLLEVDLDAVKPNVPSLMTPIVFTNLAEGETVSIKASGSVNREQEDIVKIEK
The following text describes a protein:
Function:
Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MATELVSKESLQKAVVALRECCKKIDNKRLFNSDKLSVQLAVKKIINEPQKLNKILLPHTPIDVKSTDICLFVKDVDKKSRDYERTIAAYKDLLKEQGIQTKIDIFPMKKLKIEFNDYQAKRRLANLYDLFLCDSRIIRLMPAILGKHFYGKKKFPRQVRLARVDIKNEIEKSLRTSVYDVKNRGACWRMEECQINLHQVRTVGRSSYLRVIRSEVELDDKVKLPGKSDDLNIDSLENPSDLLLEQAEEVSTVTNGLVVVTDDGQVLVVGDDGDVINCDDDVMGDNDDDVRDHDGDDDDDDDDVVREDVEIGKRIMRMKRRVNSGDDDDDDDDGDDDDDDADDDDDANMGDKKMGKVSRKRKTTSSSSNNNNNDKERKNKDNKKFKLGTENNKNIDKRNNNSDKNNKSQQSKSVKFKNSNNKNNNNKGGEGSRVQRSKKRSSMNFAKRWVLRSALNIVSDGKSLEMEEICMLLNNQLANVTDKLSRRQSFILAVRNSFLSSKTPRTENHHINNMRSLLCTLVSPFNMLQHPLGKSPRN
The following text describes a protein:
Function:
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Sequence:
MVKKNEKGSDELRTAVEPTAINKVGDVFLPPSLSVKESNDLHTYTFRADVDDSVSRTQPFVLGVDEAGRGPVLGPMVYAVAFCPTELKLSEYGFADSKQLTAEKRTQLLQAVCDRNNPASTSIGWATTVMTARDISRGMLRRVDKYNLNAQAHDSTIALIQSVLKAGYNISEIYVDTVGPPAVYQAKLQNRFPQAKVTVTKKADSLFPIVSLASICAKVTRDAHLERTREALDIDNWGCGYSSDSQTTAWLRKNVHPVFGWKGHVVRYSWQTAKNLLEIGKNGMVDMDWHDEQDKQSVITMHKTTTDGRSWFGSSGNLFGA
The following text describes a protein:
Function:
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Sequence:
MHSLQAKILDPRLGSDFPLPQYATPGSAGLDLRAMLKEDSVLGPGQTLLIPTGLSIYIADPGLAALVLPRSGLGHKHGIVLGNLVGLIDSDYQGELMVSCWNRGESPFTIAVGERIAQLVLVPVVQAHFELVEAFDESQRGAGGFGHSGSH
The following text describes a protein:
Function:
Controls stomatal patterning.
Subcellular Localization:
Secreted.
Sequence:
MVTVVTNRSDFDQLDIDDILGILLSYEARLEQQHPPSIPLNSNPQNGSSLTIRGRSYGHEECEPITFHGGVSNFNPTWYPDSSATHHMILDIDNMQNRFDYGGSDQVKVSNKTQSTGREREERREREINNGGSVYSDVGQYGTTQHNFPHELTHTSATHSPFHKCLPETPSFWEFYNLALFTFSFPRTLYFLLSSDFNGNLVIFAVLRTPLPFISPSLLLPRIRVPRFSLSLCPEGKKEERTNLFLFLSLSHICCPVGVLFGFFDLDSXAIAIIASPPQSLSELLILPSTFLLTCAAFLAWRWAYYAISTSTSTTFTIIIIITVSLLQLLSLLSSLRPSPSRLSPRPPNWVCRIGLVGVSGVKLEKEEEEKRGGGLEALERLVTRRRLTGPGSSPPTCRFKCGSCSPCLPVHVPIQPGRSFPLEYYPEAWRCKCGNKLFMP
The following text describes a protein:
Function:
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MEKFSPLFYINLFGYKFGITSSLVIQWVIIAIVALLSIILTRNLKKVPDKRQTVMEMMLDLVRNLVNENMGEEFKSFIPFIGTLMIYLLLMNLVGLLGLKPPTLDYSVVLGMALISFVVIQGYAIRKTGLKSYFLGYGKPYLFLLPLNVIERVMLPVSLSLRLFGNITAAVLIMDLVYSALASISWFAQLVVPIPLHIYFDLFDGTIQMVIFVMLTMINIKVIAEH
The following text describes a protein:
Function:
Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.
Sequence:
MFFIATLEVFILEDNIVIKGNKEGLVVIINMNKFRDFNDMINSLIQKLSHGKQFYKGSTLKISTELKLINEKNLRRLKDVLFEEFMIKDCIFEDKEDRSNKPFSGIYEGRTKFIRRTVRGGQVVRYNGNLVIIGDVNSGAEIYAAGNVVVLGALRGHVHAGFTGNHKAIVAAFYLQPSILQIANVMTRSPEDNVKPQYPEVAKIKSSIIVVEPYLPDKFI
The following text describes a protein:
Function:
Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity). When associated as homohexamer, catalyzes the proteolyzes of Xaa-Leu dipeptides (By similarity). Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin (By similarity). Presumably involved in the processing and regular turnover of intracellular proteins (Probable). Regulates wound signaling and has a role in insect defense (By similarity); Functions as a molecular chaperone to protect proteins from heat-induced damage.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MATLRVSSLFASSSSSLHSNPSVFTKYQSSPKWAFSFPVTPLCSKRSKRIVHCIAGDTLGLTRPNESDAPKISIGAKDTAVVQWQGDLLAIGATENDMARDENSKFKNPLLQQLDSELNGLLSAASSEEDFSGKSGQSVNLRFPGGRISLVGLGSSASSPTSYHSLGQAAAAAARSSQARNIAVALASTDGLSAESKINSASAIATGVVLGSFEDNRFRSESKKSTLESLDILGLGTGPEIERKIKYAEHVCAGVILGRELVNAPANIVTPAVLAEEAKKIASTYSDVISVNILDAEQCKELKMGAYLAVAAAATENPPYFIHLCFKTPTKERKTKLALVGKGLTFDSGGYNLKVGAGSRIELMKNDMGGAAAVLGAAKALGEIRPSRVEVHFIVAACENMISAEGMRPGDIVTASNGKTIEVNNTDAEGRLTLADALIYACNQGVEKIIDLATLTGAIMVALGPSVAGAFTPNDGLANEVVAAAEASGEKLWRMPMEESYWESMKSGVADMINLGPGNGGAITGALFLKQFVDEKVQWLHLDVAGPVWSDEKKNATGYGVSTLVEWVLRN
The following text describes a protein:
Function:
Phosphorylates D-xylulose to produce D-xylulose 5-phosphate, a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis.
Sequence:
LYSRYCSYFIDTSFDTNNKPGRRCYSYLHFTIEETEVKVIAVDEKLNVTYEESVNFDKELPEFGTQGGVHVHSDKLTVTSPVLMWVKALDIILEKMKSSGFNFSQVKALSGAGQQHGSVYWKRGACKTLKNLSPDLPLHQQLKFSFSLSDCPIWMDSSTTVECRNLEKAVKGAQNLSDITGSRAYELSNFAASLFLGSYTPIDYGDGSGMNLLNIRKKSWSQLCLDACAPELEEKLGPAVPSSSVLGPISSYHVQRYGFNSECKVIAFTGDNPASLAGMRLEEGDIAVSLGTSDTLFLWIKEPTPALEGHIFCNPVNSQEYMALLCFKNGSLMREKVRDESASGSWDEFSIALRSTEIGNCGNLGFYFDVMEITPETTGRHRFNADNQKVSNFPKEMEIRALIEGQFMAKRIHAEKLGYRIVPRTKILATGGASHNRDILQVLSDVFNAPVYTIETANSACLGCAYRAIHGVAIGENISFTDVVKLAPEPRLAAVPTAGAAQVSTSGGKGEREGMEPFPDSFCNQSYLSILCVKPSKSQACISEIMSPVLRRL
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MAETAVSSQEESSTLLVGVGKAASAMSSKEIKNALEKGDTTARANALMAIIRLHVNGEPQNYLIMTVIRYITPIDDHLIKKLVLYFWEVVDKRDADGKLLSVIILICSFLRSDLLHPNEYVRGLTLRFLCKVNEVELIEPLVSAVVQNLSHKVAYVRRNAVLAVHYISKKFPKLLPDAPELVESAIRTETDVSTCRNGLDFLAAFAPERAASYLSDFRDSHTLSAVDGPFLMSVVEFCRQMIRANPYEKARYVPVLFSVLQSKSAAVRYQCATTLLSLSSSPTAIRQATLTYVDIIKVHSDNSVRLIVVEQLNQMRGSYLYVLQDSLLDILSVLQDGSMTIRERVIELAVELVTRRNAETFMQAMRKELLRTNSVDIEVEDANAAMAYRLLIIKAINTALLRHPPSAPSMLPVLLDYLCDTTSTSREVITLIKEVLLSQPELRRDTMKKLSEIFPMMTSGPVMRTALWMFGAYASSADEVLQTLRMLKDAVEPLPFETPKPVLGDAVSLSTTAATNNASSQSNMRAVTTVLEDGTYVTTYTTATPAPAATATNGHGEGDSNDVSSSGLRLALLKGDYFLAAALASTLTKLVVQLFTGEAKGSVDAATCNTAQSDALGILREVLRYGTEADSLHPISADTNEHLLLNIELLSNPQAPFMVDVSHASLEALGRAERRSARESGKTDGGGAATASAAAAVQLNAIDTPVVFSQLREGKDAVFEFEAAAEGPGAAAKEESSERKAQLFLKKLEDTMPLSGFNDPVYCEASITVHQFDVSVDWLLVNCTSKQLTNLTIELVSLGGMKLCERPQTYTLDPHETIAVRTSLKVSATESGVIYGTVLYDAPNNQHCSFILNDIHVDIMNYIHPGPCFSAEFREKWGIFDWENKIAVSTTKRDLTSLVRFIVQELNMQLLEPYEVEQQEEQDPELELLPTSEENEKCAYVSCNLYAQTAFGEDALANVSVESDGKGLVSGVIRIRSNTQTIAYGIGEKLNMLQKSGKL
The following text describes a protein:
Function:
Plays a role in mitotic exit and cytokinesis. Recruits PDCD6IP and TSG101 to midbody during cytokinesis. Required for successful completion of cytokinesis. Not required for microtubule nucleation. Plays a role in the development of the brain and kidney.
Subcellular Localization:
Cleavage furrow. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Midbody, Midbody ring.
Sequence:
MATKMLKSKLGSNSGDMEKLKKENETLKKTLEEMSKSKEKSDERRNKLLEVKVLLQEILESETLREHYSQEIAKKSEEIDSLTEELRYGREENGAFHVIDAEQVADDIQSQLSAVQNRINSITNYLQQDLEDSKKGEVANNLNLLESQLKDALEKNQKWLVYDQQREEYVKGLMCRIYELEQQLGNANKTIQQQAKDTPSAAKQDDEKQKYYDKLLLAAKKDLDNEKKIASQLRAHLAAMKAERDEERQSYKEKKQKLRAELEVSKQETEEEKKRTKELTNQIQAMSMSLLKQHQQQNQIALLEQQKNTSDICNIVPSWTLHTDFEEKLTIRAQHSPPHRRSLLDESLLECPNCKAVYPASQHRELLAHIDYCTS
The following text describes a protein:
Function:
May be involved in sperm differentiation and proliferation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MRPEGSLTYWVPERLRQGFCGVGRAAQALVCASAKEGTAFRMEAVQEGAAGVESEQAALGEEAVLLLDDIMAEVEVVAEEEGLVERREEAQRAQQAVPGPGPMTPESALEELLAVQVELEPVNAQARKAFSRQREKMERRRKPHLDRRGAVIQSVPGFWANVIANHPQMSALITDEDEDMLSYMVSLEVEEEKHPVHLCKIMLFFRSNPYFQNKVITKEYLVNITEYRASHSTPIEWYLDYEVEAYRRRHHNSSLNFFNWFSDHNFAGSNKIAEILCKDLWRNPLQYYKRMKPPEEGTETSGDSQLLS
The following text describes a protein:
Function:
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Subcellular Localization:
Cytoplasm.
Sequence:
MFNPNNGSEFARNRARLDDTPNPYEPEVGSLPEGDRSQAGSDTVNKTGTTIVGLTTQDGVLMASDMRASLGGRVISNKNVQKVEEIQPNAALSISGSVGGAQSFIRSLRAEANLYEARRGEYMSIDALSTMASNLLRGGPFFRVVPILGGVDDDGGHVFSLDPAGSSMSDTYTAQGSGMPYALGVLEQEYSEDLTMADAEQVAAHAVKSASERDTASGNGIHITKITHDGLTTVGHKEFDALL
The following text describes a protein:
Function:
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Subcellular Localization:
Cytoplasm.
Sequence:
MSQFSLVAMGGTFDIIHRGHITLLSSAFEISDKVIIGLTSDEFAKKRGKTLSNNYEKRLANLTETIFKEFPKSSFQISKLDNDFGPAVLEPEVQALVVSDETSSQGDVLNDLRAKKNLSPVEVITVPMHLAKDGSRISTTRIKNSEIDSEGNLLSVDK
The following text describes a protein:
Function:
A redox-sensitive transcriptional regulator. Maintains intracellular redox homeostasis by regulating catabolic metabolism and polyketide biosynthesis. Regulates expression of the redox buffer ergothioneine (ERG) in a carbon-source-dependent manner; loss of ERG or mycothiol (MSH, the other major redox buffer in this bacteria) leads to respiratory alterations and bioenergetic deficiencies that negatively impact virulence. In response to low external pH (like that found in host macrophage phagosomes) alters endogenous gene expression leading to acid resistance; MSH and WhiB3 are probably part of a regulatory circuit that mediates gene expression upon acid stress. Regulates pathogenic lipid synthesis, coordinating proprionate flux (and other host-derived fatty acid oxidation intermediates) into methyl-branched fatty acids (polyacyltrehalose, phthiocerol dimycocerosates, sulfolipids) and the storage lipid triacylglycerol, functioning as reductive sink. During intracellular growth M.tuberculosis uses host fatty acids as an energy source, generating large quantities of proprionate and NADH/NADPH, which are toxic and highly reducing respectively. WhiB3 is thought to help dissipate proprionate and NADH/NADPH by switching to the in vivo carbon source and via lipid anabolism. Responds to NO and O(2). Regulates expression of genes encoding modular polyketide synthases such as pks2, pks3 and fbpA. The oxidized apo-form of WhiB3 binds DNA (with 2 intramolecular disulfide bonds); holo-WhiB3 (with the 4Fe-4S cluster) binds DNA considerably less well. Discriminates poorly between specific and non-specific DNA-binding. Plays a role in virulence and nutritional stress. In its apo-form can act as a protein disulfide reductase; May respond to mycothiol (MSH) redox potential (E-MSH) which decreases at pH 4.5 for up to 72 hours, indicative of cellular reductive stress; deletion of whiB3 leads to a lesser E-MSH at 72 hours, indicative of cellular oxidative stress. Probably via its effects on production of polyketide lipids, regulates host gene expression, leading to blockage of phagosome maturation. Equilibration of extra- and intracytoplasmic pH kills bacteria.
Subcellular Localization:
Cytoplasm.
Sequence:
MPQPEQLPGPNADIWNWQLQGLCRGMDSSMFFHPDGERGRARTQREQRAKEMCRRCPVIEACRSHALEVGEPYGVWGGLSESERDLLLKGTMGRTRGIRRTA
The following text describes a protein:
Function:
Component of the transition zone in primary cilia. Required for ciliogenesis.
Subcellular Localization:
Cell projection, cilium. Membrane; Multi-pass membrane protein.
Sequence:
MSTRPRKHKHKDDMKQETVVQVHKTVKSDTSSDEKTKLNEDKNDNYNTNTPSREISVDEESQINSKILSLIESEMKRDANKHSHFTDSRPQSLSFYEDEKAPEELSGNLELLSPEERKHYKRRREYGQMDMDEMNAYNVIQDLYNSRDGDEIISSTKKSKSRKKRHGDSETGIGDSREMMIPKEKKKSKKKKRESSPTAKRKHKKRDDDFEPRNDITVALEELQDDVFENNEEFKIEKIRKSPKKSDKVYVQKKNKFEAVTKPSNLNRQSAYELEEDISGKKFQTYHPLELAIPFQEYWMRLTTFCHGLLGGLALGHWLYIVSNIYNQDSEFISHYSHFSDTYVSCFYFLCVICLMSVFEKIDFAHFEGAQFRNLFKFKKSSLVILIYFTCLVVHLSAARIDYKLGLVSYNDTISNITKSELTQWNHLSLWRSILAFLAWIIVGLSPQENMFYINLKGMEKYLPQK