lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Acts as a DNA damage-response activator of rhp51. Binds to part of the DNA damage-responsive element (DRE), (5'-NG[GT]T[GA]-3').
Subcellular Localization:
Nucleus.
Sequence:
MSEHSPEASSTYAQVTSNDELSSNKIYMNADQNNSRKKEMDGSLQNNGGRLQNVNPLGGNESMSAVATSAASSLPTAENGVSLNAASPTIHSNTPTVVSHPVMSGSELKGEESHNSPGTLNGTSVANASKQPNMPNATFRCDKCDMMFVKQSGLTNHKRTYHQVETVVIIGHRRYVWRRNENGRFQCVCGRQNWRRPVNFASHAKQCPSFLAMDPNNIPPEINKVSPHDDLRPLSDSRRRARRPHPSDTIPPGASMARSDPSQVPESNPSAAAAVAAAAVAAAANLTNGVNPPEVPRNLNSSLVDAAESLANVSQQQHHRHPFARQPDYSAHSIPRTAAPYAPSMNMFAQNGPNTSLLPTAMPSDVSISSSLQQQPIHPSYDSRFSKAPQGTDALAALGYGTPSSAATLCPLYRDTPAAIVSEKLHLRLANLRIAYCEDCREFISLNAALDHRRSHHQQNITGDLVHVYSDFLDFQNC
The following text describes a protein:
Function:
Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localizes to the Z ring in an FtsZ-dependent manner. Targeted to the membrane through a conserved C-terminal amphipathic helix.
Sequence:
MTGLDRTQTPKTRQMPHKRGGLVACLDIGTSKIACMIARLKPSAPSEALRGRTHAVELIGYSQIQSRGMKAGAVVDLGECEQAVRQAVGLAEKMAKVRVESVLLSVSGGRLSGQLVEAAADIRGGAVTPADVSRVTSTGMRHATGEGRTVLHALPVGYTLDGVKGIRDPRGMVAHQFGVDMNVVTCDATVARNLMLAVERCHINVEAMAASPYVAGLSVLTDDEADLGAAVVEMGAGTTTMAVYAGGRFVHAAGFAVGGQHITMDLARGLSATIADAERIKTLYGTVITGGSDSRELMSVPTAGDEQDLPQIVSRATIANIVKHRAEEIFEMVRDRLKDSPFASEPNGRVVLSGGASQLTGLVELGTQILGRPVRVGRPLGFGRLPNEAKNAAFAVPAGLLVYPQYVHQEHVEPRHTRQQVRTGTGGYFGKVGRWLREGF
The following text describes a protein:
Function:
Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
CAVLSNRLLKATAQAGVRFQGTTARAAPSAPRAAVGGFSFDLTDQQKEFRETARKFAREEIIPAAPHYDRTGEYPVPLIKRAWELGLMNSHIPEDCDAGGMGLGIFDSCLITEEIAYGCTGIQTAIEANSLGQMPVIIAGNDQQRKKYLGRMTEEPLMCAYCVTEPIAGSDVAGIKTRAERKGDEYIINGQKMWITNGGKANWYFLLARTDPDPKAPAGKAFTGFIVDADAPGVQPGRKEMNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGATGLAQRALDEATKYALERKTFGRLIAEHQAVSFLLAEMAMKVELARMAYQRSAWEVDEGRRNTYYASIAKAFAGDIANQVASDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTAQVQRMIIAREHIGKYKQ
The following text describes a protein:
Function:
tRNA nucleus export receptor which facilitates tRNA translocation across the nuclear pore complex.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Shuttles between the nucleus and the cytoplasm.
Sequence:
MEDLCRAVDVAFSHTAQPAIKAEATAYCNQVRESARGWELAVRILAAADTRQDSGSSYSLEVRFYCFQILEDMLRHRSDNLTQDEHLFIQQSIWELVRQYYSDPSRPSYLKNKLSVVIVLLFKAQYPTKWPTFFDQLLSLLSDSGAQRSLIMAFLHICAVIDEEVVCLYVPRTPEDVVRNNAIKDWMREGPVEALIRSWMSLLRSHYMSDAEITNACVGLFGVYASWADINLILQSEFVDALLGFLSVPDLRIAACDCIAEIVGKGMKVADKLQLLQLLRLPAIIDTFEYGPEDFDEQVAKLINCIGMELCHCCQEGQSSLERDQSLVVLQQVFPYLIKYLGNEYDDTVSALLPFVQALLLLMKRIKKSTVTSEQRKFLTQLLQVLVGKMKFLDDDEFRLGPDAGESEALFADLRKSFKALLESIASIDDGLFVSCISSTVLQNFELMIHGVQAGKAPQHILKWPDVEIALHLLHVFIEAKPFKASPIYILESGNLSPLGQMLSKLFECDAVSYPHISVPILYFEILVRYSQFFEQCPHYLPQALNAFIGARGLHHPNMAIRLRLNYLFLRFIKHLRQLIGTYADGILSSIEDLIVIVQRKPSLTDVSNGDTPSQLTKVTVVENSAEFDSQLYLFECAGHLISADLVEPSKRALLLGKILSPMIYVIESSMQQLLQGNPASQQITILLADTITAIGSVSKGFPDYVGDHLVANSADIAPSSQSSIKRIMETQVVQIFQEVLHRILLVLERLSDSSLIREASRSSLQCMVGCVGPVILDHLPTFLSAGLLSSTTATELIDFLPFIGLMIYKFKFSIADILVELWTPLREKIFLFLNQQAVGTDDIIQQISLRRSYLTLFTALFNSEMQAILTCSANVAHLSTTLMSIMLCLDENSDVTVHKLVFSLFSKMVYCWAGDDIQSSANAGTQQSGSHASDGHIVKPPVVGAARGRDATLKRTPLNGFNQFVFENILPIMFELPLRQSFNPADGQALVLLGEIASLHKVCVEVLGAEYVDFIAKNYLPSRGCPPETAQLFATNLLNLDKKELKKYIQTFVQATRSIPTR
The following text describes a protein:
Function:
Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMOs to their mature forms and deconjugation of SUMO from targeted proteins.
Sequence:
MKERDLSVYDFNEDDELRDTCHQWSKLSNPKFDNDVAMTKYQFLQHASSGSIAQVKEIRTVKQIHVVAIDDDDDRGFVNDISGQPQNESVKAASEQSEVFGALSDRILQKHCQFSGDSVKPQCPSLDMEIGISCPVELPSGNGHISHSAPESPCSNDSVDAGTSDDCDSIQESAPSTSGSEQEENYDSMDGQSDGGWEMEEMETSILTDYVSYGDKYLPGCRILFTKTSLKLEASALEEESGTSRSEWKLDEIFSIESQWSGIARIAEVKVRLFTRDAAQEEIAHGMEGIEVLEFLAYDPHWIERRERIMTFNTRYQALWSIGLNGKLCEGGPYPLENCESSSDPYLPHFDEPFEEVVYPKGAADAVVISKRDVDLLEPDTFLNDTIIDFYIKYLENEISSSERARFHFFNCFFFRKLADPDKNPSGVFDGKAGYQRVRKWTRKVNLFEKDYIFIPVNYNLHWSLIVICHPGEVANINDENVGESVKVPCILHMDSIRGSHAGLKDLVQSYLSEEWKEKQKETSEDIISKILNLRFLSLELPQQENCSDCGLFLLHYAELFIAEVPKNFSPFQINKFENFLKPDWFMPAEASLKRVHIQRLIYGLLEVAPPENASTCNHNSEPSAFPEIKENDSGLEFISEMSPGKSLNSLHSQSVQGMEMGLLDNISGIADVGMRELFEQRQHYDHGASFRRPGCTMSPIREEVEEVDHLDPPTSAQTELLQRHEMTSEACDIGYTPTDFSNGFEWNSKISDHEENSSPPSNCLSDDSEEMMIIEFGNGLQGAASSGQDQNLDQPKDDNIDSLTESYASASSDMMLTPAEDSQELAQIYGNNDLDVFTPNQEQAKEPPHIDLEELQTPNQTEAKETSLIDLEKSHTPNQTEAKEPSHIDLDTPIQEQAKESSHDFLELHAPNQEQAKESSHGFLELHAPNQEQAKESSHDFLELHTPNQEQAKESSHGFLELHTPNPEEAKEPSNNDLEKSHILNQVQTKKPSSYPEFEIIEDDEDTIAVNEVVEDSGSDPDEVHAAKRIRLTPLGGDGEREIVRSISKELEV
The following text describes a protein:
Function:
Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Sequence:
MSGRTTANEHDLLSANIRALGDALGRVIIGQHGSEALALVEQVRRMAKDLRNAPTNTDPQALPQLIADLDLPQLRSLVKAFTLYFGLVNLAEGVERLRVLRARDLRHAPAPRAESIADAIELLKRHGVPAPAIQEWLDHALIMPVLTAHPTESRRRTILIKLRRIFDTLVDLTFGERLVLPADRQAALTRIEREIVGLWQSDDVRNRRPSVLDEVENGLFFFQTVLWELLPHIYREMSDALQAAYPDHPWRLPPFLRFGSWMGGDRDGNPFVTPEVTVETVRLMRSAMLRYLIDCLDRLITDLSQSVQQVKVDTAIIDRIAEYRELMPDAAATLNPHYRCEPYRQLCHFIQARLHNTLQYTLDYTPRWGIDPPLARRPDIYYHSRELLADLDLIDASLRNNGSTLIAEGLLRDVRTLVAVCHLHTATLDVRQHASRHTAALSEILAAAGVVDDYEALDEAERIAVLSVEIRRPRPLTPSRLSHFSPATAETIHTFRVIAAISEQLDPEIFQTYIISTTSQVSDLLAVLLLCRDAGLYQPGQASQLHIVPLFETGDDLQRAPALLDELLRLPVYREHLALRDNLQEVMLGYSDSNKEGGFVAANWALYRAQVELTAVTDRHGVRLRLFHGRGGAVGRGGAVGRGGGPAGQAILAQPPGTLHGQIKVTDQGEMISDRYLDPRTAHRHLEQVVNAVLRAGFPGMARQPEPTWLAAMEEMATTARTVYRQLVYEDPDFLIYFRSATPVAEFNRLRIGSRPVSRRKSDRIEDLRAIPWVFSWMQSRHTIPGWFGLGSALEAFVEADPHHLHLLRTMYQHWPFFSTLLDNAQMIMLKADMNIARAYASLVPDRHLAERIFQRIESEFRRTERMICQITERNDLLAHQPVLQRAIRQRNPYIDPLSFVQIELLRRLRAAPPEEQGELETVLLMSINGIAAGLKNTG
The following text describes a protein:
Function:
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Subcellular Localization:
Cytoplasm.
Domain:
Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.
Sequence:
MRMSLLFYRTSKNANKEASVLSYELLQKAGYLFKTSKGIYSYTPLFQRVILKMTEIIREELNAIGGQEVCLPLLQPAELWEKTGRWKAFLSEKLLYVLKDRENKAMCLAPTHEEVVSEFVAQWLTGREQLPIHLYQIGTKFRDEIRPRFGLMRAKEFLMEDSYTFSDSPEQMEEQYAKLRLAYQRIFDRLNLKYVIVAADGGKIGKGKSEEFHVLCSLGEDTICVSGSYGANVEAAQAIPPSYVYDSNLLPVEEVATPNIRTIEDLEVFFNTPKHKILKTLVVKTCQKDSEKFFAICIRGDRQINLTKVASFLQVDDCELASEEEILKHLHVEKGFIGPLYCPIPCYADETTRPMTNFICANNQKDVHCKHVNWGRDIPLPAFGDFLLAEAGDLCPQNGGAPYEIFQGVEVAHIFNLGTRYTESFSVGFQDKNGDKQLCWMGTYGIGVGRTLAACIEQLADNKGLVWPLAVAPFSITILYNGGDTEGEATALQLYQSLNTEGFEPLLDDRNERLGFKLKDSDLLGIPYKLIIGKSFQSTGLLEIESRSGEKCNVSPENLLDWCSKNLPCHTRKIPPLREQN
The following text describes a protein:
Function:
V-SNARE binding protein that facilitates specific protein retrieval from a late endosome to the Golgi. Modulates the rate of arginine uptake. Involved in pH homeostasis. Required for the correct localization of IST2. May be involved in ion homeostasis together with IST2.
Subcellular Localization:
Cytoplasm. Late endosome.
Sequence:
MFSIFNSPCVFEQLPSFSQPLHSRYFDCSSPVSYYPECKRRKAIKANLRAPKKSDANCSEPLRYALAETPNGYTLSLSKRIPYELFSKYVNEKLGELKENHYRPTYHVVQDFFGNQYYVEDEADEDALLRSALKDLDFRAIGKKIAKDLFQDYEIELNHRGDELSILSKKDKIFKEFSLDQVFEDVFVIGCGVENIDDGSREKYALLKIGLVKHEEEISEGGINEPKMPIIESKIDESHDDVNMSESLKEEEAEKAKEPLTKEDQIKKWIEEERLMQEESRKSEQEKAAKEDEERQKKEKEARLKARKESLINKQKTKRSQQKKLQNSKSLPISEIEASNKNNNSNSGSAESDNESINSDSDTTLDFSVSGNTLKKHASPLLEDVEDEEVDRYNESLSRSPKGNSIIEEI
The following text describes a protein:
Function:
Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position.
Sequence:
MEPSASSSSAEATALQCASDQDLRVPFYCEENAWRVAFRHTHSSDNRKPSNEEEDVWEYYVVFISNQLRCCPLFKQRAVAPDEYVSWDYHVIVIRTMESCSTSSDGDNKNATEVLDVDSWLQYSCPIEEYLDGTFPHTTNEDLDPKYMPMFRVIPTKQYLKYFYSDRMHMYGDGKWSRPPPSYAPIMNGLEFASGEPLTTGDAASDDCNGVRASNLDSFIDMSEAKNQTTYGEVFTLDQLCARFGVELS
The following text describes a protein:
Function:
Involved in the development. Negatively regulates tyrosine phosphorylation and activation state of dstC/STATc, probably by activating a dstC/STATc phosphatase.
Domain:
The truncated N-terminal protein kinase domain lacks most of its classical characteristics and in vitro, has no activity; The protein kinase domain 1 is predicted to be catalytically inactive.
Sequence:
MDSFNNNNNNNNNNNNNNNNINGEGITLRTLLNSCTNTSSNEQLIVNNVNKNSNIINNININNTPSPISTCINVNKIELRGSSNGIFLNSKIKVPLPNSTLLEQQQDGADEQDKKQQSLSDKNILFSSGDKEFLNHGSNNIITDQNTLLYQLQQQQQKEKEKENDEIMNHDDIIGYNEENEDNFFNEGMDPILAHSIEHHLHNHHHHHGEFDTQENEDTSGESSDESENIDEVLVYTEDIESEKEKKRERLITSPPSFDPHTLYSMSQSLLNCSLNNNNNNNNSISSPSSSINNSGNNINLNNSGNNNVNSNNNTNIINNSNDNFISQPLFNPLSMPNNEQYELLPNPTTTTSTITSTTTTTTITNLPPALPSFPSSSSIKSLKNSFGSNSITSSGELNNVFSSSMSPPMSPPNRNVRSLTFPGTNPINCINTSVINSITANTNCINHHHHHHQHNHHNHHQGHNNINNSGHIRKSADDTVTLSPTLSSGSSSTSSSNPHHPNHNHQKGLNNKTLEKLSCTRKEIYELIEKKESLIEKQNLIDEGYSENADSFENLSEEIQKINEKIIELENLITSLSNSNSNWSLNGSSTSTISCNPLSPRSMNPSSSTSSTSSNLTNSLRKFSQELKIELRPLDLRAELYSSINTSPRGSASISGGSGSGGGGNNNGCFKTSSNSSINSPIQFFENENESIDSYEKKNEEQFESLTQLIRENQLYTKPIEFKEIKLLEKLESNSKSSNIWQIEYKSTQLVLKQPKDQDSDKNIEKRKQLFNGSNVSGSNNSGSSGGNNHNHHHCNNSNGSNSEVIPSKYTMIQHKNLGLLVGWCGDSIIFESFKGMNSLHDLIHRDGLKIDMALFIKISKDIASVMGLLHSKDVAHGNLTSRSIYLDRFQIVKVSFPKLNATDLNNPAIEPRYMAPEMTRMEEDQISCSIDVYAYAFVLWEALTSHLPFRKFNDISVAAKVAYENLRPKIPTSCPLIIRKLINRCWAPLPSDRPTFNDILKLFDHLEGKLFFSSPGILWSLNNDQEVERELQKKERFNEITEFLRGKKEIKFDEVAIVEKVGAGSFANVFLGIWNGYKVAIKILKNESISNDEKFIKEVSSLIKSHHPNVVTFMGACIDPPCIFTEYLQGGSLYDVLHIQKIKLNPLMMYKMIHDLSLGMEHLHSIQMLHRDLTSKNILLDEFKNIKIADFGLATTLSDDMTLSGITNPRWRSPELTKGLVYNEKVDVYSFGLVVYEIYTGKIPFEGLDGTASAAKAAFENYRPAIPPDCPVSLRKLITKCWASDPSQRPSFTEILTELETMKSKFIKQLSFLNDLIQNPDDDYNNNLNYDEEVDS
The following text describes a protein:
Function:
FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Bacterial flagellum basal body.
Sequence:
MKHEVSPVSLMGLEDFAGKRNEAGKAHIDTVSDISIELGVKLGKSSITLGDVKQLKVGDVLEVEKNLGHKVDVYLSNMKVGIGEAIVMDEKFGIIISEIEADKKQAALMKAQSQMQDKE
The following text describes a protein:
Function:
May play a role in microtubule-mediated transport or vesicle function.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MDLIRALDILSAQVDTGDDHNLRKEKIEACRTISEQICAPSLRNTADFPRFLSIAISLLLRAHGDKDLNVYSVAEESLNRTIKILIYSYHERILFELFKVLKGKPQQQQDGKRLSTSYNGSEISNSLATQGGSIPSTPVMNMGSNLSSTNTTPSFSSPLSSNNLTNIINNLGGSTQTPTPSSSSNANSLFNTASQILSKPFPIKSQRIALVKFGEVCSFIRPSKCRKYILSLVPPINILLQIHDDESLQESIATSMENISKILIPYLKENEVHQLIDLFAKNLSQTSAAVRRAASLSITSICRHYPKPLFEYTIESLFSYTFPNSPPIASITSSQCIPNSTSTNTQSNSKILGVLFSYLQLIKLSEELSLSDIKILDSFSLKIQFFVHFILKYIQLPDNDNEQYDHNVVGLSLELLQQLLVTFGPYEHSWPKPLVQQVISQLRSLCFQQHASIRVSLKAVVLNCLAQSVKYFPKLFNQEFFSNQYQQQNAYISSISPSDLNFKLFTPITQQEQQQQKSQGAPPLSASTASTNQSFLFNLEPKEEFLNYLTDSDPLLRGGTALMIGCLIRGFLETDHITSNQIYPTDVPLLQDNISIPTLLIFLLRALMDSSSVTAKLACTGIGECLPTLCQSKYSDWALVTLRHLLCVSSSTYWLVKLEILETLSKIDYIVIEYLEQNVQHRSNVMNVSINNSTDGGLNNSTGINNSSSSSGEKETGGAVAIPIQSKVLDFLIEQLSDNDFRVRNSAGQALVSIIPRLVFTAPLERHSMKGISSNVRESFDVPDYENTVLKKRKIFANLSHVIGFLVNQLSNPHPDDKIRGCYHALNLICQTYSFPPDTPQECRSLSSILPNPMLSFVGDILPLALDRVGLTWVATDFDVHIDIIEVLGYLSRGAENVLGSYCYNVLRHIVRIINIATNIIQFRPTPPLKEVKSNPSGIVNSPLLKAPTHLGAFTHSIHYIKLYSKLLAARVNSITIFGSDRFSQLRQSCFETLAVILKCAGKTILPYTEEIIGYLTTHFEQEPVSVIKCINELFLVTMKPTPLVSISSLSQKSKDLNNIGGSSSSSSSSSLKQYEPRSIESHSSSSNPHDEMFLNSKSVFSSLLTFGTPNLKQHYEYAHEVPSSHNINYSYSNQEINRIISGEDRKVYFKLFEPLIVGSMVEYQTTHNHHLKIAILLMFSKFSKFGLDLSLFDKEQHFPTYFINELKETNCLLSKPYKVLSYSYDLLGSIFIHRKLYPDLNIGLDDLKKLFYQQAPVSNPSASASKASQSLDSTPMLASNNNINQASQSLNNSSLLNQSSHPYSYTIPTIIENCHSFVRYLYDPLDKYPDTEFRDGFLNFLLSNLQYSQTIDLLILIVTLIKSNNPLYSKYSQQISHQLFTSLSLGDSPFFIINSIEEVEKLYVLIDKLHNSSLSASRWADALLSVSPQFVNNTNKPNTNTPTPSQATTTTTSDPLQRKRILLLRESILEAYELRWLPPLLVILRTGCKLPEESRISAARQSRYLSNHDNKQQSSPSANIISHVILKLIRNAVQVFSLYKPKNILFTQLINHLLYYSSIFFNKNLVPHITPSTTNVTSPHSTSPNIVSSTSPLSMSSHLMKQPSATSLLGIASNNLFTDSLKIIIATNEGSPIIHDIVNSLLSYGGTSTSIHVVKFLLLLGRDDQVWKSYAMSSYWQTCGCEHFLTHHIIFLLYCQAIIILKLPIDLTETFLDKMVLLINEFTIKKLIESIKGEYTETLTNHLKKILSRASNSLDLRKKQKLLRLLSYLPANRETIELLIVNFIQTDDISLQVSGERILNLKINTLIEEYGTTKSLDIIQELYQIFMSNFVKSTTNLSVQSLFLKLIKNLSPNSNITITPTIQVIKQDYNSNDENHEEKEEHNENKDNEELINNNISIEKLTELQIETLKSGYLNDYHQLSTIPWKYFIELIKSRYFIHMNQHSFNHISILSQIDKEATVQLLESNRLDSTLLPEFISSNYSLDYQDEIQNYLLKKMDKLLAKAGEIGSDPLKGGPPFLSDPVWDELRETTRCLSNFINKFGINDLCESNLLQVSTWAFIESFRRWRAEIINPYDFKLVLELSRSIILKSTASILTITDDSSWCSLLLCLYKLYCLVIRPHFGYISGQRELEENFSQDPTQISLTQSNEMVKFLVSLLTNSKSYSPMPGSHIGQLIFDSFIRAIIPLATKAFDFIYPTLTASDENEFGGGIIPNCPIFSSIVSPEQNIRALVRFIHFVEIDNEEKFGQVWRILEPIFVAQLGDAEIGTDEITEESKCVALSGMTSMIIKVCFEISGVNSQVNLLETSTIPKPIYNHIPREKDLIFLNTPIGKKLNNLLSIIYGGMPQSELPLGGGVGTIGTSSTLSAYHFNIERSFSSNSFGSDQISLQDLRLFKVPSFIGINFTPLIKKLLESFEGFLLNQMCPPMLKKEILRSVVTLSDLFNRDQVCWMFRTFQAIITTDEIDDFFLKQHLILGICKSIAILQHPPNIADINAHAVGIFEMLKAALEHPNISLQVSALDGILYLLEGKVNKYIQGPLLQYLFRWIPTRLSSSHSPPVSLTLRVLATMFLMIEQYSREAEETLFTKRAVTTCIQLGQQSSTPAPIVYGVFRGLDRLLGSFSLSHSQRESISQFSLKSLPSENPIRSLLALGLMVTCIYTGDETGITSPSKSSVSSIGSSGINSLTAFEGLSFNPSSDSPLNFSGTSSSNGSISSIINNHNINNNDSDDNSDPERNKFSRVNNMEKVKMLFDKIRLVSHFSYEAYVLSQVIPTVIIDLFPSVDQLLSFILGEFLKQSKSNPKLMCQIISKVFDYLLENDKDKTNQHLINYWIIICLQNFFQIQNPNHCLWALTYLFLTSSPLKSFKLLESEFASKIQTNEKLFLIIAAEFYFNKDLTKENKQLFKDSFSKLKSEPYISLMKVIKNQ
The following text describes a protein:
Function:
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
Subcellular Localization:
Cytoplasm.
Sequence:
MNLRLLQLADSAFPTGAYAFSDGLETLTQRGEVRTADDLAAFLAGQLAHGWGQQDAPACALAWGAGADDLSDLDALLSDLKLVEGPRRASLRVGANLRRAARHLWPDELAGVPPTTHHATTFGAVACVLGAGREDAMTAYVSAWLLGRVTSATRLMKLGGLDAQRCAARCEAAAQSCVGFALSATPDDLGGFAPLLDIAAQEQATLDQRLFQS
The following text describes a protein:
Function:
Transposase responsible for transposition an insertion sequence (IS) element. Transposition occurs in 2 main steps, excision from the donor DNA 'top strand' into a single strand circle and its subsequent reinsertion into the DNA target. This increases the copy number of the IS.
Sequence:
MSNYRRDFTKGGLYFFTIVLQDRTKSYLTDYINEFRSAYKQTCEHYPFETVAICILPDHIHLLMQLPENDDNYAIRIAYLKTQFTRQLPKECRQFNKNRQKYRESGIWQRRFWEHLIRDDKDLANHLDYIYYNPVKHGYVEVVKDWPYSSFHRDVKAEIYPEDWGGNPDLKIKGDI
The following text describes a protein:
Function:
Important regulator of cell cycle progression. Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry.
Subcellular Localization:
Cytoplasm. Endosome. Nucleus.
Sequence:
MSKVRVSNGSPTLERVDPRQADHGKPPVCRSLFGAVDRQEFAKDVREQMREIERASAEKWNYDFAENRPLAPGDYEWQEVDADEVPDFYTRPPRVKRPSSAGTVDHNGNHDYFLTAPSPSPESGAGNSERADAGNRSLSTPRKRPSTEDQDDLRRSKRPSVHASEADPCPDATSSLERAPCEPDPKT
The following text describes a protein:
Function:
Controls the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR, in cooperation with the RNA stabilizer ELAVL1. Decreases the stability of the leptin mRNA by antagonizing the function of ELAVL1 by inducing its atypical recruitment from the nucleus to the cytosol. Binds to cardiolipin (CL), phosphatidic acid (PA), phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidylserine (PS) (By similarity).
Subcellular Localization:
Cell membrane; Lipid-anchor. Mitochondrion membrane. Mitochondrion. Note=Interaction with C1QBP and phosphorylation is essential for its mitochondrial localization. Localizes on the microtubule in the form of small granules.
Domain:
Both PH domains are essential for its mitochondrial localization.
Sequence:
MGNSHCVPQAPRRLRASFSRKPSLKGNREDSARKLAGLFGTEARPDGDTAANRIFHYIPGTDIPGPEHHPENLEQPFLSVFKKGWRRTPVRNLGKVVHYSKVRLRFQHSQDISDCYLELFPSHLYFQAHGSEGLTFQGLLPLTELNICPTDGSREHAFQITGPLPAPLLVLCHSEAELSHWLYHLEKQMALLGLQRCHSAPPQGSLGDKPPWTQLRRAYGCGSMSGAICASRVKLQHLPSQEQWDRLLVLYPASLAIFSEEPEGLSFKGELPLSAIHINLEEKEKEIRSFLIEGHLINTIRVVCASYEDYSQWLLCLRTVSRRDGAHLPPGPESFPGLQKPTQLVGRGRGSLSSNGRSSWKLECPVFPTSQSLPESSVPTTIGFPAPPVPNQTDSNCVSTGQKKMKPSDSSPSPRGRAQREVSGSTVPLPLPLDLTKMSALNLDSGPEAQDHSLDIPHSPLYADPYTPPATSRHKITDIQGLDEFLCAIQTSPGPDLSSPFPPVSVSVPVSESSSGISSSPGPLGSHLLTKKGALQPRASQRHRGSFKSRGPQPSDFPQLVTPAREGKPSSLPPPPDEEAPIWNKTSSPSHPKWPQPRKPAVEGGFIQWI
The following text describes a protein:
Function:
Positive regulator of the bkd operon for branched-chain keto acid dehydrogenase complex.
Sequence:
MAELDRIDLKILRALADDGRLSWRDLAQKVGLSLTPTLRRVRRLEEEHYIQGYFARLDEERLSGAMSVFVSVSLEKQTGDYLARFEERIVDAPQVMSCFQMTGDADYMLRVVVKDLAAYQAFLTNTLTCIPGVAGIKSAFALKSVMLRSAPPL
The following text describes a protein:
Function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH also oxidizes malate to the non-canonical enol form of oxaloacetate, enol-oxaloacetate. Enol-oxaloacetate, which is a potent inhibitor of the succinate dehydrogenase activity, is further isomerized into keto-oxaloacetate.
Subcellular Localization:
Membrane.
Sequence:
MAALLLRHVGCHCLRAHFSPQLCTRNAVPLGITAKEEMGQFWNKNTSSNCPKSPHITIYSWSLPMAMSICHRGTGIALSAGVSLFGVLALLLPGNFESYLERVKSLCPGPALIHTAKFALIFPLMYHTWNGILQLYQSRVVVLVLTVLSSVGLAAM
The following text describes a protein:
Function:
Cell wall protein that plays a role in adaptation and resistance to cell wall stress.
Subcellular Localization:
Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
Sequence:
MLSNAKLLLSLAMASTALGLVSNSSSSVIVVPSSDATIAGNDTATPAPEPSSAAPIFYNSTATATQYEVVSEFTTYCPEPTTFVTNGATFTVTAPTTLTITNCPCTIEKPTSETSVSSTHDVETNSNAANARAIPGALGLAGAVMMLL
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MVKVANKYAKALFDVSLDTNNLETINEELTVINEAVKDKIEQLRMVDSNPTQTAEQRRELINGVFTDINPYIKNMMYVLADNRHISLIADVFKAFQSLYNGHYNQDFATIESTYELSQEELDKIVKLVTQQTKLSKVIVDTKINPDLIGGFRVKVGTTVLDGSVRNDLVQLQRKFRRVN
The following text describes a protein:
Function:
Essential for hedgehog signaling regulation: acts both as a negative and a positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways, acting downstream of SMO, through both SUFU-dependent and -independent mechanisms. Involved in the regulation of microtubular dynamics. Required for proper organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes. Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing of the transcription factor GLI3 into its repressor form. In keratinocytes, promotes the dissociation of SUFU-GLI2 complexes, GLI2 nuclear translocation and Shh signaling activation. Involved in the regulation of epidermal differentiation and chondrocyte development.
Subcellular Localization:
Cell projection, cilium. Cytoplasm, cytoskeleton, cilium basal body. Note=Localizes to the cilium tip.
Sequence:
MGLEAQRLPGAEEAPVRVALRVRPLLPKELLHGHQSCLRVEPERGRITLGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASLHEDEQGIIPRAMAEAFKLIDENDLLDCLVHVSYLELYKEEFRDLLEVGTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRLPRPAAGHLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVNWHPEAERVPEEQAAGARGPPRHRSETRIIHRGRRVPCPAVGSAAVAAGLGAECARCRARTSAAYSLLRELQAEPGLPGAAARKVRDWLCAVEGERSTLSSASGPDSGIESAPAEDQAAQGTSGRKGDEGTQQLLTLQSQVARLEEENRDFLAALEDAMEQYKLQSDRLREQQEEMVELRLRLELAQPGWGAPGLLQGLPPGSFVPRPHTAPLGGAHTHMLGMMPSTCLPGEEVSSEQQVVSGKEVKAEVLAQADKLRSASSTTSEEEGEEEEEEEEEEEEPPRRTLYLRRNGISNWSQRAGLSPGSPPDRKGPEVCPEEPAAAIPAPQAVGSGKVPVQTRQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQLLLQQGRDHLGEGLADSKRQYEARIHALEKELGRHMWINQELKQKLSAGSTAGQSQGCERRSLCLENRQCLGNEDGLHPAAPEPLWQSSLLEGVSRVWDESRDLVHAPLPLTWKRSSLCSEQGSSEESRVRETTEPPVGRVLPMGEVGLSWNFGPLPKPRWEPRRTSPGMIDVRKNPL