lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MERLPLSPAVLFLIIVLPILYLWIRYTAPARPHGKHLSLPPGPPRLPKIGNLHQVPRQIPWKKYKEWSDTYGPIMSVQLADTIAVVFSSWDLIKNHIERRNTIYSSRPSVPFFLHATGGLNASILPYGPEWKLQRAIRSSVLKPSMTVKYRDVQHVETTQLLHELLSTNDFPVCLRRCIASVFLTVAYGERCVDHAGLEAIDRLEELNRAIALHAEALFSGAAGILTQLVLPKALVDRLPVRWKKDADMLHNRLTADLVARTRAALVRPGWNWVKEFSMKDGIGSGDGDGEQGSKVELKRLAYMVGSLYEASMAASQALRVIILAGLLHPDATRRMHDELDAVVGTGRLPDFHDAAQLPYTQAFIKEAMRWRSLTPMGSPRATSDEDECRGYHIPCGATVLVNVWAINHDEAIFLDPFAFQPERWIENPDLPQLMYGMGQRACPGRHMGQDSLFLATARLFWAFDMALPDGADPIDQERFLDSGTTLAAFLPDFEVRFTPRSEKYQEVIENSMAVLPDVLSISATP
The following text describes a protein:
Function:
Peroxisomal docking factor that anchors PEX1 and PEX6 to peroxisome membranes. PEX26 is therefore required for the formation of the PEX1-PEX6 AAA ATPase complex, a complex that mediates the extraction of the PEX5 receptor from peroxisomal membrane.
Miscellaneous:
MISCELLANEOUS: Present with 1070 molecules/cell in log phase SD medium.
Subcellular Localization:
Peroxisome membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MAASEIMNNLPMHSLDSSLRDLLNDDLFIESDESTKSVNDQRSEVFQECVNLFIKRDIKDCLEKMSEVGFIDITVFKSNPMILDLFVSACDIMPSFTKLGLTLQSEILNIFTLDTPQCIETRKIILGDLSKLLVINKFFRCCIKVIQFNLTDHTEQEEKTLELESIMSDFIFVYITKMRTTIDVVGLQELIEIFIFQVKVKLHHKKPSPNMYWALCKTLPKLSPTLKGLYLSKDVSIEDAILNSIDNKIQKDKAKSKGKQRGVKQKIHHFHEPMLHNSSEEQVKVEDAFNQRTSTDSRLQSTGTAPRKKNNDITVLAGSFWAVLKHHFTRSVLNKNGLLLTGLLLLLCLKKYKSLMAIFKHVPAAFHTVYPQIVGLLKLLASI
The following text describes a protein:
Function:
Together with HP30-2 and HP20, triggers the import and insertion of transit sequence-less multi-pass transmembrane proteins (e.g. CEQORH) into the chloroplastic inner membrane.
Subcellular Localization:
Plastid, chloroplast inner membrane; Multi-pass membrane protein.
Sequence:
MVVGGGGEGDQKRSSGEMMAMASLFNDQQNPIQQFQVKFKEVETNFKTWLSKQSIPVEAAVVSTMSGVQGAFIGGLMGTLSPEMPQAGVDPQAIASMKQAQALVGGPWVQARNFAAITGVNAGIASVMKRIRGKEDIESAVVAALGSGFAYSLVSQGLQGQPMNAITTAAGFAVFQGVFFKLGERFSKPSTEDPFFTRGRTMLVKLGLEKYEKNFKKGLLTDPTLPLLTDSALKDANIPPGPRLMILDHIQRDPEIKGKRK
The following text describes a protein:
Function:
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
Subcellular Localization:
Cytoplasm.
Sequence:
MKSQFLLSVREFMQTRYYAKKTIEAYLHWITRYIHFHNKKHPSLMGDKEVEEFLTYLAVQGKVATKTQSLALNSLSFLYKEILKTPLSLEIRFQRSQLERKLPVVLTRDEIRRLLEIVDPKHQLPIKLLYGSGLRLMECMRLRVQDIDFDYGAIRIWQGKGGKNRTVTLAKELYPHLKEQIALAKRYYDRDLHQKNYGGVWLPTALKEKYPNAPYEFRWHYLFPSFQLSLDPESDVMRRHHMNETVLQKAVRRSAQEAGIEKTVTCHTLRHSFATHLLEVGADIRTVQEQLGHTDVKTTQIYTHVLDRGASGVLSPLSRL
The following text describes a protein:
Function:
Acetyltransferase enzyme. Acetylates histones, giving a specific tag for transcriptional activation.
Subcellular Localization:
Nucleus.
Sequence:
MVYELGHVSDRFKNNNNNIGVGDPCKEGGFVGNLHTKRRRCGGNNVSEFIGNIAKSYMETTEGENWASNLTSHLNSRFPTSIDTPKNFIQQDVHDANLHQIISAHSSLSDLLVSNSFFPPQNDKNLGYNCYSPASLNIYNPILCGGSAYDEYIQDVSYGGVNLISPLSVKQSDLDIITSPEQVSSITACSYSDMISDTEAFDSITAKSSFQQQPFYNNNSQYRSFAGNNMSAYNMDHSLLSMDDVQSPFPNSCNVQQSFQNLPEASDSLQNKSNNQDSSDAYDLKVLNAYVMYKKMPANLRKEVSFQNYMHVAECKENLCKCHLHLELSSHFDNCDHLNCGICGPERALCGSIGSFQMESRKRKLDQSVVTDDMGPTGTGTLLDALRTKYPKLESSLVGEDATNNDQRSKVNGSHDQQETTVVKQSDGIANNETMKRPKLDSSTVEEDACDQQETTVVNQSDNIANDEIMKYTKLESSTVGEDAMDDDQKAVVGAHDQHELTVVNQSDDVSSVGEDARDDEQRGVVNDACGQQELTVVNQNDSNANNEMMKYPTLERSTVGEDAMDNDQRGVVSGEHDQPESTVVNQSDNILNAEMTKSPQVCSDNLSSKEMTTDEKEKSGQAITEASNDLSSGADVADLHSNKSMTPNMSMVDCDSALGPDHTEIKIASLTDNEMTKPPQLCSDHLSSEEMSVGEKEKSGQAIIEASKDLSSGADVADLNSNKSITPNVSTVDCDSVLEQDNTSIKIASLTDNDSSLEPEKIKIQSVSLADFFTAEQIKEHLLSFTSQKVVSENRAPSIGSNTCQLCSMDKLVCAPAPIYCSSCDTRIKRNVGYYRSTNVVGTRHSFCMSCYRGSHGNSIVLRGYGHSMPKSTLQKARNDEEKEDSWVLCDKCQCWQHRICGLYNDEKDVEGKAEYICPKCYLEELESGTRVPLPQTTASGAKDLPRTNLSDHIEQRLFKRLDQERQEMAKVSGIEPNEVPGPEGLVVRVVVSVEKQLEVRQKFINILHGEDYPSGFTYRSKLIFLFQKIEGVDVCLFGMCVQEFGSECGGPNQRCVYISYLDSVKYFRPERKCVTGESLRTFVYHEILTGYLEYCKKRGFATCYIWACPLIKGEDYIFYCHPETQRTPKQDKLRQWYKSMLKKATEDNIVVDHTNLYNQFFVPNGEGNMKITAARLPYFDGDYWSGAAENIVRKLEVEESTGGLQSKLPNKRILKAMGQDKNDIAVKDVLVMQKLGQTILPVKENFMIVHLQYICTHCREVILSGSRWFCSHCKKFQLCSRCFNADKKISESKLHACHSSEKKQLSEVVVNDVTLDTKDTDDVFVNSFFETRDAFLNKCQKSHFQFDTLSRAKYSSMMILYHLIYKPVIKPTCTACHSDVMVEQCWHCDTCTKYYICESCYKMRHGAYHPHSLNPPSMDFEYASKSQLLQMQKDWPIRWVLDTLMHASGCDRIPCAYKECNTMRRLFYHAARCNVKVRGGCKYCQRVWTILKKHSQICTDSDCKIPRCMDIKKHKEMLAARSADQQVTMNDQQQEVVPVG
The following text describes a protein:
Function:
Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport across cell membranes, playing an important role in hepatic fatty acid uptake. Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake. Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. Can also activate branched-chain fatty acids such as phytanic acid and pristanic acid (By similarity). May contribute to the synthesis of sphingosine-1-phosphate (By similarity). Does not activate C24 bile acids, cholate and chenodeoxycholate (By similarity). In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. However, it is not critical for THCA activation and bile synthesis in vivo (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Peroxisome membrane; Peripheral membrane protein. Cell membrane; Multi-pass membrane protein. Microsome.
Sequence:
MLPVLYTGLAGLLLLPLLLTCCCPYLLQDVRYFLRLANMARRVRSYRQRRPVRTILRAFLEQARKTPHKPFLLFRDETLTYAQVDRRSNQVARALHDQLGLRQGDCVALFMGNEPAYVWIWLGLLKLGCPMACLNYNIRAKSLLHCFQCCGAKVLLASPDLQEAVEEVLPTLKKDAVSVFYVSRTSNTNGVDTILDKVDGVSAEPTPESWRSEVTFTTPAVYIYTSGTTGLPKAATINHHRLWYGTGLAMSSGITAQDVIYTTMPLYHSAALMIGLHGCIVVGATLALRSKFSASQFWDDCRKYNVTVIQYIGELLRYLCNTPQKPNDRDHKVKKALGNGLRGDVWREFIKRFGDIHVYEFYASTEGNIGFVNYPRKIGAVGRANYLQRKVARYELIKYDVEKDEPVRDANGYCIKVPKGEVGLLVCKITQLTPFIGYAGGKTQTEKKKLRDVFKKGDIYFNSGDLLMIDRENFVYFHDRVGDTFRWKGENVATTEVADIVGLVDFVEEVNVYGVPVPGHEGRIGMASLKIKENYEFNGKKLFQHIAEYLPSYARPRFLRIQDTIEITGTFKHRKVTLMEEGFNPTVIKDTLYFMDDAEKTFVPMTENIYNAIIDKTLKL
The following text describes a protein:
Function:
Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE). Required for proper cerebellum development.
Subcellular Localization:
Nucleus.
Sequence:
MAARITAPGFDVVNRAGRAGWHEGSQAGRKAGTLNGISGTAAVKLKRANSCLLPTKRQLTPQRVSIDIDCQIGTQIEIIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQSNAAYSCPRQKNCLIDRTSRNRCQHCRLQKCLAVGMSRDAVKFGRMSKKQRDSLYAEVQKHRLQQQQRDHQQQPGEAEPLTPSYGLSANGLTELHDDLSGYMDGHTPDGSKPDSAVSSFYLDIQPSPDQSGLDINGIKPEPICDFAPGSGFFPYCSFTNGETSPTVSMAELEHLAQNISKSHMETCQYLREELQQMTWQAFLQEEVESYQSKPREVMWQLCAIKITEAIQYVVEFAKRIDGFMELCQNDQIVLLKAGSLEVVFVRMCRAFDSQNNTVYFDGKYAGPDVFKSLGCDDLISSVFEFGKNLCSMHLSEDEIALFSAFVLMSADRSWLQEKVKVEKLQQKIQLALQHVLQKNHREDGILTKLICKVSTLRALCSRHTEKLTAFKAIYPDIVRAHFPPLYKELFGSDFEQSMPVDG
The following text describes a protein:
Function:
Involved in ribosomal large subunit assembly.
Subcellular Localization:
Nucleus.
Sequence:
MQSKLVMSLVAQCIGRLQMGDYRTVEAAAEQGGTSPHIEAEKYQIDWGSLVASDPTHHFQTIPSSRQELTRAYLEKGTELGQALADSLFALPSSDDPDGPVVLLPQPTTKLPREKHLPKPKPPTKWELFAKMKGIKKHKKEKHALDEQTADEPGEDPFSKRKAEKNKRIEKQEKNRPENLKQAAKVGALPSHVQLAATALPITGSQAPKKASKKELEDIAGMATTATASGGKFDKKVARGEISRHWEVSEVSAPCGRKGDELTREATNSKNSPPADVQKLS
The following text describes a protein:
Function:
Negative regulator of replication initiation, which contributes to regulation of DNA replication and ensures that replication initiation occurs exactly once per chromosome per cell cycle. Binds to pairs of hemimethylated GATC sequences in the oriC region, thus preventing assembly of replication proteins and re-initiation at newly replicated origins. Repression is relieved when the region becomes fully methylated. Can also bind to hemimethylated GATC sequences outside of oriC region. Binds, with less affinity, to fully methylated GATC sites and affects timing of replication. May play a role in chromosome organization and gene regulation.
Subcellular Localization:
Cytoplasm. Note=Localization is cell cycle-dependent. Localizes at midcell in newborn cells, then migrates in opposite directions toward cell quarter sites and remains tethered there until the cell divides.
Domain:
The N-terminal domain is required for multimerization. The C-terminal domain is involved in DNA-binding.
Sequence:
MKTIEVDDELYSYIASHTKHIGESASDILRRMLKFSAASQPAAPVTKEVRVASPAIVEAKPVKTIKDKVRAMRELLLSDEYAEQKRAVNRFMLLLSTLYSLDAQAFAEATESLHGRTRVYFAADEQTLLKNGNQTKPKHVPGTPYWVITNTNTGRKCSMIEHIMQSMQFPAELIEKVCGTI
The following text describes a protein:
Function:
Mediates the entry of L.monocytogenes into normally non-phagocytic mammalian host cells. Its host receptor is hepatocyte growth factor receptor (HGF receptor, a tyrosine kinase, MET) which is tyrosine-phosphorylated in response to InlB. Downstream targets MAPK1/MAPK3 (Erk1/2) and AKT are phosphorylated in response to InlB, which also causes cell colony scattering. Complement component 1 Q subcomponent-binding protein (gC1q-R, C1QBP) has been suggested to also act an InlB receptor, but this is less certain. Stimulation of Tyr-phosphorylation of MET by InlB is potentiated by the InlB GW domains and glycosaminoglycans such as heparin (By similarity).
Subcellular Localization:
Secreted. Cytoplasm. Cell membrane. Note=Approximately half the protein is secreted. Cell surface association is mediated by the GW domains and can occur when protein is added externally; externally added protein confers invasion competence. Protein is partially buried in the cell membrane; it binds non-covalently to lipoteichoic acid (LTA) on the bacterial membrane, and can be released from the surface by LTA.
Domain:
The N-terminus (36-79) resembles a truncated EF hand, the LRR region (80-240) has a curved form, while residues 241-321 form an Ig-like region; the whole region forms a curved tube. The LRR domain alone (31-241) binds mammalian MET and stimulates its Tyr-phosphorylation; the LRR plus Ig-like region (36-321) are required for receptor dimerization; adding the B-repeat allows the protein to scatter host cell colonies, and the GW domains, especially GW2 and GW3, potentiate MET activation. The cap, LRR and Ig-like regions all interact with residues 25-656 of host MET (the Sema, PSI and Ig1 domains) via the interior (concave surface) of the curved tube. Dimerizes via the exterior (convex surface) of the curved tube which probably induces host receptor dimerization; preventing dimerization prevents host downstream signaling (Probable). The B repeat region crystallizes in a SUMO-like fold. The B repeat region interacts synergistically with N-terminus of InlB, conferring on it the ability to stimulate cell motility; the B repeat does not bind to MET. Deletion of the B-repeat (exact residues are not given) slightly decreased protein activity in host; the authors suggest the B-repeat probably contributes to homodimerization rather than binding another host cell receptor.
Sequence:
MKEKHNPRRKYCLISGLAIIFSLWIIIGNGAKVQAETITVPTPIKQIFSDDAFAETIKDNLKKKSVTDAVTQNELNSIDQIIANNSDIKSVQGIQYLPNVTKLFLNGNKLTDIKPLANLKNLGWLFLDENKVKDLSSLKDLKKLKSLSLEHNGISDINGLVHLPQLESLYLGNNKITDITVLSRLTKLDTLSLEDNQISDIVPLAGLTKLQNLYLSKNHISDLRALAGLKNLDVLELFSQECLNKPINHQSNLVVPNTVKNTDGSLVTPEIISDDGDYEKPNVKWHLPEFTNEVSFIFYQPVTIGKAKARFHGRVTQPLKEVYTVSYDVDGTVIKTKVEAGTRITAPKPPTKQGYVFKGWYTEKNGGHEWNFNTDYMSGNDFTLYAVFKAETTEKAVNLTRYVKYIRGNAGIYKLPREDNSLKQGTLASHRCKALTVDREARNGGKLWYRLKNIGWTKAENLSLDRYDKMEYDKGVTAYARVRNASGNSVWTKPYNTAGAKHVNKLSVYQGKNMRILREAKTPITTWYQFSIGGKVIGWVDTRALNTFYKQSMEKPTRLTRYVSANKAGESYYKVPVADNPVKRGTLAKYKNQKLIVDCQATIEGQLWYRIRTSSTFIGWTKAANLRAQK
The following text describes a protein:
Function:
Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis.
Subcellular Localization:
Cytoplasm. Mitochondrion inner membrane. Mitochondrion matrix.
Sequence:
MSHRFLYSLRPIHQRQLSSFRFRPNKPNRFSTSSSHSPLSGLTTRAKLFSAKPTTNIHHFIFRPPLRTCHTTPCKMASSQRTYDDALSRLAQLQSNRTIVNLFGSDDSNNDSQSKKPAAKKDLNSLAIPEMLSWLARAGYTPSSLAATGLKCVHVAGTKGKGSVSALVSSIISQYPPPPSFHDDGGGGGAHIIQKPVVVGTYTSPHVLSVRERIQLDNVPVSREKFALYFFEVWDRLSAAARAARDPVQSEAEYDGPGTKPFYFRFLTILAFHIFVREGVKQAVIECGIGGEYDSTNFLSPQCVTASVVTQLGIDHVAMLGNTLEKIAWNKSGIFRKGVKGFTRRLDGETQKGVMEVLRNRAQEKEVERLVEVEDEQVEKWKGVEGAKLEGPFQKFNMALAVAAAREHLTRVGHKFAGAFGEEGWKLDDIPAEFEKGLKEASLKGRCESFRDPKGTEWFVDGAHTEDSLAGVGQWFSGKVKEGDVNVLVFNQQDRDPEVLLRALLAAAQKQSGTTTPVFTYAVLTRNEEKAPVEGEPERDLAVQLQGQKIIQEASAETETSVYNAVEPAMEQVQKIAEQARKDGKTCNVLVTGSFHLLGGVLKTVEYVEY
The following text describes a protein:
Function:
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Subcellular Localization:
Cytoplasm.
Sequence:
MAATTNNFDGLRVAALESRRADDMTRLICKFGGEAFVSPSMREVPIEPNRAAIDFAYRIITGDIGIVIVMTGVGFRYLLKATEKHVDQQRLIDALSDITTICRGPKPVAVMREFGLKPTHRVPEPNTWRELLQTIDAGIPIANQTIGIQEYGVSNKQLIAGLEARGAIAESVKVYGWEFPEDTQPLKANTLALAEGERDILLVTSAHQVVNLLRMAEDLGVSDSLRDGLSKTAIVSIGPTTSDMLREHDLAIAMEPSHPKMGHLVSESARDAKRLVDEVRARSSGSQSSTSQTSVSLRADDSSLISASKTPMPAIDDHPSQSSLFMRACRGEPTPRTPVWMMRQAGRYMQEYREVRSQQSFLELCANPKLCSEVMCTAVEKLNVDAAIIFSDLLPILVPMGFDLEFVKGDGPVIHNPVRSAADVDRVKGLDNPQDLGFVYETVKQTRADLPEGIPLIGFAGAPFTLASYAIEGGGSRQYSSTKALMRAGDGGWAALMDRLTDAIIVYLNEQISAGAQCVQLFDSWAGCLSPGDYREFVLPWMKRILEGVTPGVPLINFATGNPELLPLLRGDRRTVVGVDWRIELDVAWKRVGHDISVQGNLDPSVLLTDAKTIRAAVQDVLNKAGGRPGHIFNLGHGVLQQTPVENAIELVKAVKELSVRDDFSAENGGTDS
The following text describes a protein:
Function:
Critical mediator, in cooperation with CASP4, of endoplasmic reticulum-stress induced apoptosis. Required or the activation of CASP4 following endoplasmic reticulum stress.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAKKKSNNNNNNNNNNNNNNKIIIEEEIIDSDEEGWEEVPTKEQRNKEMNEKREKRKLEKEKKRQQEIIEHNEKQKKIAELFSDSSKAFNIKNRPAGYNPWDILDEDEDDITHTQEHQKRNGAKQTSENPNNGFHYPGSDRLSNSNDKLKKKKKQIQQQPQPQSPSDSKQSLSNAIQSFNFEKYYDLLKNIEKKFPKVVDVQIKCVAECLEEHFGSIPSDQSPFYQRIDYLSKFDDKFRKETTKFFSSRPMSNILPTVDKDAISSSGVGLEILLQLIFRYFPDSLLMNLQYFKSLSLQTLKPNVVSLYLWFFSQPIQNNLHSITASIWLQIVFPILYKAKVSNHSNLELFEKFTIQLLELKRVQKNGIEIEDTVLANSLDEFLNALILQTVQPIGMKYSDILFDLKKLFSNNKIPSSYFYVLLNYSAMPDEALRERFLNKVIECLNIDNNCFHYLKSRYVEFIAQINNLLLYVLLQWKSSEKKDGNKQHQHQHQPTLTKQSVYELALFCREENNSLLLKRQLQIQQHQQQQQLLQQQGKQLKKPQKSTFEVDDVNLCNITCDVSIIILMVPLVIVGSYYSRQMFCDGNINLNQYLPKENVDLLQKYLCQ
The following text describes a protein:
Function:
Is involved in the final hydroxylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Acts after beta-lysylation of 'Lys-34' by EpmA and EpmB. EpmC adds an oxygen atom to the C5 position of 'Lys-34' and does not modify the added beta-lysine.
Sequence:
MNSTHHYEQLIEIFNSCFADDFNTRLIKGDDEPIYLPADAEVPYNRIVFAHGFYASAIHEISHWCIAGKARRELVDFGYWYCPDGRDAQTQSQFEDVEVKPQALDWLFCVAAGYPFNVSCDNLEGDFEPDRVVFQRRVHAQVMDYLTNGIPERPARFIKALQNYYHTPELTAEQFPWPEALN
The following text describes a protein:
Function:
eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Sequence:
MSTEIQEMPEQGEIVLATVTKVMDHGAYVTLDEYDNLQGFLHISEIAPGWIRSVNRFVKDGEKKVLLVKKVNPQRGDIDLSLKQVSKDQKKQKLKEVKKFEKGKTLLQNVQEKAKLSDEDIEKLEDSIYSKYDSVYDAFIEIGRNGIDSIKELKIPKKTTGVIEEICSKIKLPSVEIRGIMEITNSKSDGIEIIRKTLLDELKKDSTIDITYLGAPKYRLSITSEDFKSAEKSLKPIIADIQSKIEKKRGTFKFTREESKKTREN
The following text describes a protein:
Function:
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
Subcellular Localization:
Cytoplasm.
Sequence:
MRLIDLKVINFRNLKNLSLNFFDVNIFYGENAQGKTNILEGIYFLFSGKSFRTKNEKEIIRWGEESFYLKGNVDWQSQNLILETALSGEEKRIKINQKNLKRYRDMVFLFPIILFSQEEIENFKKGPSQRRYLLNRFISTLSYKYHKALSEYYKALYQRNLTLKNERDVSLWNSTLIRLGGYILFERRNVMEEIKRKVKEVSNNLLGRDFLEVEYLSSVPLGDSEEEMLKNFETMLKEKEWEEKRKKYTLVGPHRDDVILRVIRDNVKYDLRKFGSAGEKKLGYIIWKLAQVEILSENRKEKPILLIDDLFGDLDEDKQRKVWEGIKNFQIFLTTPIRIEFLKDFPHFLVKNGEVILNA
The following text describes a protein:
Function:
Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
Subcellular Localization:
Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus.
Sequence:
MQQNSASNPFAMSTYVERPQMGLDVEFGADPASGAAFFQSDGRKHDDLKQMLDSNKDGLKLEAMKRIIGMIARGRDASDLFPAVVKNVVSKNIEVKKLVYVYLVRYAEEQQDLALLSISTFQRALKDPNQLIRASALRVLSSIRVSMIVPIVMLAIRDSAADLSPYVRKTAAHAIPKLYSLDADQKDELVMVIEKLLSDRTTLVVGSAVMAFDEVCPERVDLIHKNYRKLCNFLLDVDEWGQVIIINMLTRYARTQFVDPNADDEDLVNDGLGETPVSERFYDESSHSSSHSDDGSSDDEKNKSSTNNKNNGGGNGSRTPSSPSNSYHIDVDHRLLLRQTKPLLQSRNASVVMAVAQLYHHVAPKNEVQLIAKALIRLLRSHKEVQSVVLNCIASMSTKRKAIFEPHLKSFFVRTSDPTHIKLLKLDILTNLASAGSISLILREFQTYISSSDRSFVAATIQAIGRCASSIKEVTETCLSGLVHLLSNHDEHVVAESVVVIKRLLQTKAAEHFEIITQMAKLIDYINVPAARAAIIWLIGEYNEKVPLIAPDVLRKMAKSFVDEQDVVKLQVLNLGVKLYLTNPEQTSLLCQYVFTLARYDPNYDVRDRARFLRQIIFPASGTSSVLSQHARQVFLASKPAPVPESKYRDGNNFQLGSLSHYLNMPAAGYKELPAFPVIPPDSSVRNIAGFMQDKLPGEDSPSGHSKDKSGREGGKEKGAGGEKGFLSESDDKSSAYSESGSSSGSGTSDSESDSDGSGSSDEEEEEVQKQQPTKVSSVKERLIDAGSNELAATSSPVKATINTNNNARGSSGTSDSEDSSAYSGSSSDDSASGSDNEVKKNETKTDTGTKPEKLKEKHEKQPEQTAVKSNLDLLLDLDDIPPIGPVMTPSLGGFLTPGTPMMAGQAAPLQPQHARNRVELVGPSHIEFKHKELLNKVSGHGLHLAYRFTRSPHLYSSSMCSIELQFQNRGEKEITAIRLGQTTLPAGMQLNEFAPITVLQPQQTASGVLGVDFNDSTHAVDLELLSSAGSSRLQLKPPVGELVRSVQIGESCHREERAKLRGMNEHQCELRGLRQDLIDVVALRQKVFESINVAHTHSSSSGQLHCFAGQTLSSKSLVLLTLDWKTEDALTLLVNCEKMVIGSMVLNELRNALQLSFAM
The following text describes a protein:
Function:
Involved in the maturation of specific proteins in the endoplasmic reticulum.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAEERRKCLKARQKWGLRGGGALSAWGGKGRGLQPPLAGRGGPLGSSPARRVADMAGSRLPRHLFLQGVAAIFMFAFASLYTQIPGLYGPEGILPARRTLRPQGKGRWQQLWETPTLLWEAPRLGLDTAQGLELLSLLGTLLALGALLLSQLRHLLTYLLLWAAYLSVCQVGQVFLYFQWDSLLLETGFLAVLVAPLRQPPHRKQAPQSKLAGASPHEGLSFWLVRWLLFRLMFASGVVKLTSRCPAWWGLTALTYHYETQCLPTPAAWFAHHLPVWLHKLSVVATFLIEIAVPPLFFAPIRRLRLAAFYSQVLLQVLIILTGNYNFFNLLTLVLTTALLDDVHLLAESGSSRRKKMPTSWPRALLAMLALLLELAIYGLLAYGMVHCFGLEVDWEQYAIHSRTSECQLGAQRAGAGPPLLTPLSSAAFTFHQFSQWLKTVSLPTMWLGAASLAWELLTALWRWTQVRGWLQKFCAAAQLSIFGAATVALFMISLVPYSYMEPSTHGRLWTGAHRLFGTVEHLQLANSYGLFRRMTGLGGRPEVVLEGSYDGHHWTEIEFMYKPGNVSRAPPVVTPHQPRLDWQMWFAALGPHTQSPWFTSLVLRLLQGKEPVIRLIQNHAPTYPFHKQPPTYVRAQLYKYWFSQPGEQGRWWRRQWVEEFFPAVSLGDPTLETLLRQFGLQDKSPPRARSSSSPLTEALYWVRKQLSPLEAPTLLWGLLATVGAIRVMQALLGPRPSPPAREKQRPAPREDSGATSKQAAPAPSNSSRSQTPRRKK
The following text describes a protein:
Function:
May play a role in intercellular signaling and in connecting cells with the extracellular matrix. May take part in the regulation of cell motility, growth and differentiation. Binds hyaluronic acid.
Subcellular Localization:
Cell projection, cilium, photoreceptor outer segment. Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix.
Sequence:
MIGAALPLLFCLVTLCSARPQPASPQRIQWRSSGTLAGKVVLPCSFTMTSASHSASTPLPLSAEDLRIKWVKLEGQDEKLVLVAQNGMVKAGQRFHGRVSVQNHPPSVGDASLVMDNLRASDAGLYHCEVVHGLDNTRDTVSLNVSGVVFHYRANSSRYTLDFHQAKEACRSIHASIATPAQLDAAFQDGLDQCDAGWLADQSVRYPITRPRRGCEGDLMSHRGVRTYGVRDATEKYDVYCFIDQLNGEVFFPPSLSDKLTLQQAREACERHDAALASPGQLFAAWRAGFNRCDYGWLSDGSVRHPVTVPLPQCGGGLLGVRTLYKHKNQTGYPDPGERHGAFCFKAKLPELTPHEDTPAVSAVPPLTQTPSQPQQVELQAGATETTEFSRTERQPTSPHTTTSPNPPTTFDDYDVKDFEIPRLESIPSRGDTIPLPPLPSFEPQPPKLDISHDGGEGGAVDSSSSGAPPAGTDESRAVSLQTTTVEPSWSPKHAAEVGTPRQEVTTTPPPLPEVFTAELDPPSFSVEPGHHPAVVFKEHLPPGAASEPEQSGVVPAVADTFDPASVHIIIVSMPSSNHSVVPEMDVVLDLLNKPLNLSQSLPFHNDPTQLTSDGALGSGTSDPLDPFATSPPPMIRFINETEELSFEPELAEEARGDQFDIVTPGQPRTEEVDDTTAFDYIVSDPHMEKTVTEETTITEETTITEETTITEEMTDDLKTTSDPEKKVFDAVTDFKALRTEEPTQTTSTVLPSVLSNPLTTSSSVIYPSSSDGVLTFEVPEGSADSQAMPQAEGSADGVPTPASDRLPGGTEVFTFIPDTKPEETSTKTKTKDFEGSVFGEDVISEQEHYSIKLFTTPSKTPPIHSTLHTQKPPSGAMDDPTANAGTERGSGVEQLSGDEEGQPSGEPVGLFDPHGEVKVTVLPDVLVLSGDQTVSTTLETLTDLKNESTARTITKNQQVKLTTYTSVHQTKALPSTWSTTESPDGQPELLSSTWSTTESPDGQPDLLPSTWSTTESPDGQPDLLSSTWSTTESPDGQPDLLPSTWSTTESPDGQPDLLPSTWSTTESPDGQPDLLSSTWSTTESPDGQPDLLPSTWSTTESPDGQPDLLPSTWSTTESPDDQPELLSSTWSTTESPDGQPELLSSTWSTTESPDDQPDLLSSTWSTTESPDGQPELLSSTWSTTESPDGQPDLLPSTWSTTESPDGQPELLPSTWSTTESPDDQPDLLPSTWSTTESPDNQPDLLPSTWSTTESPDDQPELLFSTWSTTESPDDQPDLLPSTWSTTESPDNQPDLLPSTWSTTESPDDQPELLFSTWSTTESPDDQPGLLPLIKLSTQSPNHGTAAPSTSFTQTLHQTTRSTTSSIYTFDHSPQSIPHWALSPDPSATALPEEFVDYDKAIAPNLLESHPQLPVKMKTTEQPKTDAASTPFEESTTVNIRDLEPCLYSPCHNGGSCFQKETRDICLCAPGFTGQYCEIDVDECHSNPCLNGATCLDGIDSFTCACLPSYTGKLCEQDTEVCGSGWQKFQSHCYKYFKHRRPWEAAERECRLQGAHLTSILSQEEQTFVNRLGGDYQWIGLSDKMFERDFRWTDGQPMQYDHWRPNQPDSFFHDGEDCVVMIWHEGGQWNDVPCNYHLTFTCKKGTVTCGQPPVVKHARVFGAPKPHYEIGSMVRYHCKQGFIQRHAPTVRCRDNGEWDLPKVACIAAAAFHQSHDLPRRSGELRNRPHLHHSESPDKPDQNQEQSFSLLRSLWDPVQNRVETLWWPTREQKH
The following text describes a protein:
Function:
Transport of FAD from the cytosol to the mitochondrial matrix.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MVDHQWTPLQKEVISGLSAGSVTTLVVHPLDLLKVRLQLSATSAQKAHYGPFMVIKEIIRSSANSGRSVTNELYRGLSINLFGNAIAWGVYFGLYGVTKELIYKSVAKPGETQLKGVGNDHKMNSLIYLSAGASSGLMTAILTNPIWVIKTRIMSTSKGAQGAYTSMYNGVQQLLRTDGFQGLWKGLVPALFGVSQGALYFAVYDTLKQRKLRRKRENGLDIHLTNLETIEITSLGKMVSVTLVYPFQLLKSNLQSFRANEQKFRLFPLIKLIIANDGFVGLYKGLSANLVRAIPSTCITFCVYENLKHRL