lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Transcription coregulator. Part of the Wnt signaling asymmetry pathway, probably acting downstream of putative frizzled ligand mom-2, Wnt/frizzled receptors lin-17 and mom-5, and dishevelled homolog dsh-2. Activates or represses target gene expression, depending on upstream Wnt signals and interactions with transcription factors, such as pop-1. Required for the activation of Wnt-responsive genes in the E blastomere; thereby leading to a role in endoderm specification and gut development. Reciprocal distribution patterns of sys-1 and pop-1/TCF in the daughters of anterior-posterior cell divisions functions in specifying cell fate; a higher sys-1 to pop-1 ratio promotes the posterior cell fate, whereas a low sys-1 to pop-1 ratio promotes the anterior fate. Represses expression of homeobox ttx-3 in neuroblasts of the SIAD/SIBV lineage, perhaps acting by blocking its transcriptional activation by a complex consisting of ref-2 and pop-1. Required for early organization of the hermaphrodite, but not the male, gonad; involved in generation of regulatory cells, known as the distal tip cells (DTC), and in formation of the somatic gonadal primordium. Involved in regulating asymmetric divisions of the somatic gonadal precursor cells (SGP), Z1 and Z4.
Miscellaneous:
MISCELLANEOUS: Exhibits low sequence similarity to canonical beta-catenins but displays functional and structural similarities so that it appears to be a highly divergent beta-catenin.
Subcellular Localization:
Nucleus. Cytoplasm. Cytoplasmic granule. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Note=Centrosomal localization increases at metaphase. Maintenance of centrosomal localization requires trafficking of sys-1 by microtubule motor dynein and may enhance proteasomal degradation of sys-1. Localized to nucleus in a Wnt signal- and pop-1-dependent manner.
Sequence:
MHSTGEPQRGPAGPYHHPMPYHVDQIPTTSHPSWHQAPHPGLPTPPYHPQQHPNYISMQPPPSQQQQMTPQALSTQQQQQVQQQQQRQLYSSPSPSRGPAAPAQNQKFRTEQWINNQAWPYSQSPAPPVAPSVMSYHQGDDRMSMLSVNTTMTNQFPDSQRCYSSNGSTCENVNPEMMQMNITQAAEQAIRLWFNTPDPMQRLHMAKTIRTWIRQDKFAQVDQANMPNCVQQILNIIYDGLKPQPVQLPISYYAQLWYNLLDILRRFTFLPIISPYIHQVVQMFCPRENGPQDFRELICNLISLNWQKDPHMKHCANQVFQIFNCIIMGVKNEKLRTEFAQHLKFEKLVGTLSEYFNPQVHPGMINPAIFIIFRFIISKDTRLKDYFIWNNNPHDQPPPPTGLIIKLNAVMIGSYRLIAGQNPETLPQNPELAHLIQVIIRTFDLLGLLLHDSDAIDGFVRSDGVGAITTVVQYPNNDLIRAGCKLLLQVSDAKALAKTPLENILPFLLRLIEIHPDDEVIYSGTGFLSNVVAHKQHVKDIAIRSNAIFLLHTIISKYPRLDELTDAPKRNRVCEIICNCLRTLNNFLMMWIPTPNGETKTAGPNEKQQVCKFIEIDILKKLMSCLSCEGMDTPGLLELRSTILRSFILLLRTPFVPKDGVLNVIDENRKENLIGHICAAYSWVFRQPNNTRTQSTKQQLVERTISLLLVLMEQCGAEKEVAQYSYSIDCPLNLLNGNQVKPTFIHNVLVVCDKILEHCPTRADIWTIDRPMLEGLTNHRNSDIAKAANSLLSRFPENDLLAGIFSNREYF
The following text describes a protein:
Function:
Could mediate folate transport.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MAREEQNIENRGSVHVVERESNLRSVVCGPVRWLKMLASKLHWSYVFAVVSNCGINQGFGYSLGHVATDYYMKDVQKVQPSQYQALSAITRISWIIFKPLFGILTDVLPIFGFHRRPYFILAGVIGVVSLLFISLQSNLHLYLALFWMTISSAAMAIADVTIDACTTYNSNKHPSLASDMQSLCSLSYSIGELLGFFMSGILVHLVGSKGVFGLLTFTFALVSVVGVLFSEPRVHGFSFKQNFTNAMKAMWRTIKCSDVWQPSLYMFITRALGLDIKEGLFYWFTDSKDGPLFAQETVGFILSIGSIGSILGVLLYNLRLKDHPFRKLFLWTQLLFALSGMFDLILVLRLNLKFGLPDYLFIVVDGIVSKMIIRLTWMVIFVLNTKLCPHGIEGTFFALLMSIDNAGLMTSSWLGGKMLHVLKVTRTEFGNLWLAVLVRNVMRLLPICFLFLVPQGDQNTFKLPAEIMGEDSEEEGTRNLELASLVDYVDRS
The following text describes a protein:
Function:
Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-2-containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively; Hormone secreted by trophoblasts that promotes trophoblast invasiveness. Has glucogenic activity: is able to increase plasma glucose levels.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MAPTGRADFADFLDFLDCPDFSDFPEFLDFSDVPEIPDFLDFPDFPGFPRLPGFPRLPGFPRLPGLLGLLRHPGLPELPGHPRRSGLLRHPGLPGLLGLPERPRLLGLLGCPRHPRFPRLSGLPEFPRLPRILRLPGCSILPVLPGLPGLLRHPGLPRLPGLSRLFRGSGLPGLPGLPGLPRLLRHPGLPGLCGLPRLFRGPGLPGLPGLGPRSSPFMSHLWVSPGTATLNQTIDICKHFTNLCLNGRCIPTPSSYRCECNMGYKQDVRGECIGERSSHYYHYHKSYDIIINMDECIMNGVMCRNGRCVNTDGSFQCICNAGFEVTPDGKNCADHDECATTNMCLNGMCINEDGSFKCICKLGFVLAPNGRYCVDVDECETPGMCMNGWCLNTEGSFRCECLGGLAIGPGGRVCVDTHVRSTCYGALKEGACARPFPGAVTKSECCCASHEHGFGEPCLPPRQEPEFQALCSSGIGITADGRDINECALNPDICPNGVCENLRGSYRCICNLGYESDPSGKDCVDVDECAVNRLLCDNGLCRNTPGSYSCSCPKGFVFRTETDTCEDINECSSNPCVNGVCRNNAGSFACECSPGSKLDLGGTLCVDSMKGTCWLHIQEGRCEVNINGATLKSECCASLGAAWGSPCERCEADPACPRGFARMKGVSCEDVNECEVFPGVCTNGLCVNSAGSFRCECPPGLSLDASGRTCLDVRLEQCFLRWAEDESLPSRMGSGMGHSTPQHGHPQYYAVVIIIGALLFRLSPFLPFSDVNECKVFPSLCAHGTCRNTIGSFRCVCSSGFALDAEERNCTDIDECRISPDLCGHGACVNTPGSFECECFDGYESGFMMMKNCMDVDECERDPLLCRGGACLNTEGSFQCLCPPGHELTAEGSACLDINECSLSDNLCRNGHCVNVIGAYQCACDSGFQATPDRQGCVDIDECTIMNGGCDTHCANSEGSYECSCSEGYALMPDKRSCTDIDECEDDPDVCDGGQCTNIPGEYRCLCFDGFMASLDMKMCIDVNECDLNPNICLHGDCENTKGSFICHCQLGYFVKKGTTGCTDIDECEVGAHNCDLHAACINIPGSFRCKCRSGWLGDGLKCNDLDECATEAHSCNLNANCLNTPGSFRCACRDGFNGDGFSCSDVDECADNVNLCENGQCLNAPGGYRCECEMGFNPTQDSKACQDIDECTFQNICVFGTCQNLPGMFRCACDDGYELDRSGGNCTDVNECADPVNCINGLCVNTPGSYLCNCPQDFELNPTGVGCVDTRVGNCFLETQDRGDGGISCSAEIGVGVTRASCCCSLGRAWGNPCELCPPANTTEYKTLCPGGEGFRPNPITVILEDIDECQELPGLCQGGNCVNTFGSFQCECPLGYYLNEDTRICEDIDECSAHIGICGPGTCYNTLGNYTCVCPPEYMQVNGGNNCMDMRKSLCYRNYNDTCENELSFNMTKKMCCCSYNIGKAWNKPCEPCPTPATEYQILCGNQAPGFIIDIHTGKPIDIDECSEIPAICSHGVCINQIGSFRCECPIGFSYNNILLICEGESGPRANPIAPYRCECATGYKLSLSEACRNECQEIPNVCSHGDCVDTEGSFICICFNGFKATGDLTMCMDIDECDRQPCGNGTCKNTVGSYNCLCFPGFELTHNNDCMDVDECSSLAGQVCRNGRCLNSVGSFRCLCQEGYEHTPDGKNCMDVNECVSLPGTCSPGTCQNLEGSFRCICPPGYEVQNDNCIDINECEEEPNICLFGTCTNAPGSFQCICPPGFVLSDNGRRCFDTRQSFCFTRFDHGKCSVPKAFNTTKARCCCSKMPGEGWGDPCELCPQEGNGRTTAPGHPSQGQRQIDTNVNECSENPGICINGACINTDGSFRCECPFGYNLDYTGVQCVDTDECSIGNPCGNGTCTNAVGGFECACDEGFEPGPMMTCEDINECALNPLLCAFRCLNTLGSYDCTCPAGYTLRHDRRMCKDLDECAEGLDDCEAQGMMCKNLIGTFACVCPPGMQRRPDGEGCTDENECRTKPGICPNGRCVNAVGSYHCDCNEGFQSSPSGTECLDVRRGLCFTEVLQALCQMSSTNRQPATKSECCCAGGRGWGPQCELCPFPGTAPHRKMCPHGTGSATDGRDIDECRVLPSLCLHGQCINSLGSFRCHCHAGYGPDLTGTHCQDLDECSQSPKPCNFLCKNTEGSFLCSCPRGYSLQEDGKTCKDLDECATKQHNCQFLCVNVVGGFNCKCPPGFTQHHHSCIDNNECTAQPTLCGAKGHCLNSPGSYSCECQKGFALDGAGSSCEDVDECEGNHRCQHGCQNVLGGYRCGCPQGYVQHYQWNQCVGEWPAGKKGSGTTIEWVYYWCPTKRMVASHQRMLVLMGHQHRPTTGYWCPNREYWCPTKRMVVSHHKDVGCPIKSMMVSHQKLLVSHQEDGGVPPEDAGFNGTPASSHHRLLVS
The following text describes a protein:
Function:
Transposase that mediates sequence-specific genomic rearrangements.
Miscellaneous:
MISCELLANEOUS: Has been domesticated very early in vertebrate evolution, approximately 500 million years ago, in the common ancestor of cephalochordates and vertebrates.
Subcellular Localization:
Nucleus.
Sequence:
MAEGGGGSRRRAPALLEAARARYESLHISDDVFGESGPDSGGNPFYSTSAASRSSSAASSDDERERPAPPGTAPPSYAADPLELEEDETGGGWSAVLRDRPSPRFEDTGGPTRKMPPSASAVDFFQLFVPDNVLKNMVVQTNMYARKFQERFGSDGAWVEVTLAEMKAFLGYVISTSVSHCESVLSIWSGGFYSNRSLALVMSQARFEKILKYFHVVAFRSSQTTHGLYKVQPFLDSLQSGFDAAFRPSQTQVLHEPLIDEDPVFIATCTERELRKRKKRKFSLWVRQCSSTGFIIQIYVHLKEGGGPDGLDALKNKPQLHSMVARSLCRNAAGKNYIIFTGPSITSLNLFEEFEKQGIYCCGLLSSRKSDCTGLPPSMLTNPATPLARGQHQIRTKGNMSLICWYNKGHFRFLTNAYSPVQKGVIIKRRSGEIPCPLAVEAFAAHLSYICRYDDKYSKYFISHKPNKTWQQVFWFAISIAVNNAYILYKMSDAYHVKKYSRAQFGERLVRELLGLEDSSPAH
The following text describes a protein:
Function:
Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimers. Does not target the ODC monomers for degradation, which allows a protein synthesis-independent restoration of ODC activity. Stabilizes AZIN2 by interfering with its ubiquitination. Involved in the translocation of AZNI2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol. Probably plays a key role in spermatogenesis by regulating the intracellular concentration of polyamines in haploid germ cells.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
RCCVTTASLWVQGLCGAPDAPHAADVSLSSTGGSGVGSLKAPPVDNSHVGKGELLARQWSQEAVRLTFRCRLTENTEVGWETVLCQGRLFVQLPSCALPEGSREAFVTLLEFAEEQLGCDHVLVFFSKDRPDRASIVRTFMFLGFTTLTPGHRLVPPSASEGVLYMAYAIE
The following text describes a protein:
Function:
Odorant receptor.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MCSRNQTSQNQTASTDFTLTGLFAESKHAALLYTVTFLLFLMALTGNALLILLIHSEPRLHTPMYFFISQLALMDLMYICVTVPKMLVGQVTGDYTISPSGCGTQMFFYLTLAGAEVFLLAAMAYDRYAAVCTPLQYPLLMNQRVCQLLVSACWVLGMVDGLLLTPVTMSFPFCQSRKILSCFCETPALLKLSCSDVSLYKTLMYLCCILMLLAPIMVISSSYTLILHLIHRMNSAAGRRKALATCSSHMIIVLLFFGASFYTYMLPSSHHTAEQDMMVSAFYTIFTPVLNPLIYSLRNKDVTRALRSMMQSRMNQEK
The following text describes a protein:
Function:
Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA.
Subcellular Localization:
Mitochondrion.
Sequence:
MEGSLFFTNATPSTSILKITDYKYLRLEKNDSTFVAELVLCRPKQYNSMDDDFYNEFISIYDEIQNDSKIRCVILRGEGKGLTAGLNLGKIAPLITGDSEVSQSQNNLDLFKMIRRWQASLDKINKCSKPTIALIHGACIGGGVDMITACDIRLCSSDAKFSIRETKLSIIADLGTLQRISKIVGSGFARELALTGKDIDAKTAERFNLVNHVYPDHDTLLSEGRKLALSIAQNSPLVVQATKLTLNHADDHTIDEGLYRVALQNAAFLKSDDLNESATSFFEKRQPIFKCNL
The following text describes a protein:
Function:
Plays a role in short-term synaptic plasticity in a subset of GABAergic neurons in the brain.
Subcellular Localization:
Cell projection, dendrite. Cell projection, growth cone membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type I membrane protein. Early endosome membrane; Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Recycling endosome.
Sequence:
MLSLRKNMATPSMEFRMYLAITLTLFLFASVNCQTPSTDDESSFVSPYQDKDLDEQSSNTKAPTSADETTQAAQELTTSSPADRADFTIRDDNGKACIRACFSAVFNVFYTKKQNKNAQVKVPLPSKATAIGTCGSVNDHALLTIQWNEGKFNLKFAFENKTENGKESWKVKKLQFSYNTSDDTYFEDAAGGGMKTVQSEDDDDDMFKTPAEKSRKCETEDDIELVGIGNSTDKAILELRQLQLQPYHLLNDSFSKAQLCKNDKEALGTNIASIAVGATLALVILVVITGYAIGRRMGAITDRTSYSSME
The following text describes a protein:
Function:
Necessary for protein translocation in the endoplasmic reticulum.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MVANGDAPARGSAAAAASLRRRRTTSGAAAAGGGGGASTMLQFYTDEAAGRKMSPNAVLIMSIGFIAVVAVLHVFGKLYRTPN
The following text describes a protein:
Function:
Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
Subcellular Localization:
Mitochondrion matrix. Nucleus. Cytoplasm. Note=Predominantly in the mitochondria and in the nucleus.
Sequence:
MFAPPAARAMKVLDRSFFKKTIPTSAARIFNAKDISRCRKELTASRDTLPNNRVDPIRPDVDSERAQKGGKCLVLRPEVVHNDRTTWSPKLRDLEQDGTLGVIPFQLDLDYDFFTYSEITSAIIPPPETKQDDEIPQGFALAGHVAHLNLRERYWPYKYLIADVLADKNPMVKTVINKLDNVGTENAFRTFQYEVLHGPDDMNVELREQGCTFKFDFAKARQYATIMAGVGPFAIPAGKKKCFVWANDLNPESYKSLEDNIRINKVGDFVTPRNTDGADFIRQSAIDLLKSERSIPIYPKVKFSRSAPPTQKPVPDRTLVQPRTFQHYVMNLPASAITFLPSFIGLYSNIPGLSIGEAKKLFAPHTQQKLPMIHVHCFSTKSDDNVAETKEICAEISRQLQCEMTPETPDVNIHDVRDVAPKKRMFCASFRLPEEVAFREI
The following text describes a protein:
Function:
May catalyze the biosynthesis of cardiolipin from phosphatidylglycerol (PG) and CDP-diacylglycerol. May also catalyze the synthesis of phosphatidylinositol.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MEPVLTQNRVLTVPNMLSVIRLALIPAFVYVVLSAHANGWGVAILVFSGVSDWADGKIARLLNQSSRLGALLDPAVDRLYMVTVPIVFGLSGIVPWWFVLTLLTRDALLAGTLPLLWSRGLSALPVTYVGKAATFGFMVGFPTILLGQCDPLWSHVLLACGWAFLIWGMYAYLWAFVLYAVQMTMVVRQMPKLKGRAHRPAAQNAGERG
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:
MSEQWEVVSKSRKQKNLDKKVSAHNEQKRIAAQLPKLEELLPTQRYRNLFGSSNNNNSKSHSPAKSSSSASSSSKANKSPVKKHTAKNASTQKRTTSAAASKPKTLELALRNITRDDFAAQLEQVKLSCPGSELRWLSHIALYFNEALSYDCDPIFSGRSAQYPSNLASASLKYSIVEFLGSVGEQNLEYFFYSLLDSMSTDLNNNQTVAGYKLILQLIGQNWPNICSRNLAKTALLRNSYQNRSNICLSILWAIGQGGYQSLNEGVRVWQNLMLPNLELKQYTKFVVEYMERALSAAAVRKTADPLQINQQEFFATYNALNAPYNHLPKEWQQSLKRSARLLLQHYINSPVRHANIFLTLFREISAGSKQTNEIEGCISCLLSSGRDDCLRVWRMNYKKQQLPSLLLLKAINDNWTTSTHELATSTVYHSFLQDVANLNEELQGSKRNEGHLDDLKEVLLSVQEKSSAQQKKNKQKAAAEKKKCGCCKWTLGSIFIIALIAGALYYDTEVNGKGVFEKSATGKVLKNAGVLPHVQKSWYTVMGAGARGYKWAEVNVPPYAEPVIKTTCDLWKLARNAACNAYQNGKGYFGAKWPVVAKFIDQYVPNSSGKIEAFAAGVSDLAASSYEKAAALIKEKVLVGRLSPENINQALNQTRNAALEYYNQFHKKVDAYAKLK
The following text describes a protein:
Function:
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.
Subcellular Localization:
Nucleus.
Sequence:
MIRRAPTTLQLSHDDVTSLIDDLNEQKLKQQLNIEKTKYFQGKNGGSLHSNTDFQDTSQNIEDNNNDNDNDIDEDDDMSSYNDKAASVAHTRVLNSLHLSTDSNTAHETSNANDNHNPFYIREE
The following text describes a protein:
Function:
Probable transcription factor. Involved in motor neuron fate determination and maintenance, acting as a transcriptional repressor to counteract gene activation by transcription factor unc-3 in a subset of motor neurons. Required throughout development to repress transcription by unc-3, probably acting by binding to specific promoter elements. Represses expression of DA and DB motor neuron-specific effector genes, such as unc-129 and unc-53, in VA and VB motor neurons.
Subcellular Localization:
Nucleus.
Sequence:
MDVRFPPYIFSMPHLIYNSWLSLNAPKLAQLQLQSIKLVGQDKSINQSELPVNSENISIRVETETNIDSLAKEEKLSEHVHDEKADKIEKTSEDNDTSTLLKLKRRVACDICSKSFCDKGALKIHTSAVHLREMHTCTVTGCGKQFSSRRSRNRHSSNNNPKLHMPESLTLTGSGLSMKTSLDTFWPTRFLLGKDHPLDLSLNLV
The following text describes a protein:
Function:
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activity but no caspase-like activity.
Subcellular Localization:
Cytoplasm.
Domain:
In contrast to M.tuberculosis, the propeptide is required for correct proteasome folding and assembly. The propeptide is positioned strategically at the region where it can act as an assembly-promoting factor by linking its own beta-subunit to two adjacent alpha-subunits at the same time.
Sequence:
MTADRPALRTGDRDTRLSFGSNLSSFTDYLRGHAPELLPENRIGHRSHSTRGGDGMESGDLAPHGTTIVALTYKGGVLLAGDRRATQGNLIASRDVEKVYVTDEYSAAGIAGTAGIAIELVRLFAVELEHYEKIEGVPLTFDGKANRLASMVRGNLGAAMQGLAVVPLLVGYDLDADDESRAGRIVSYDVVGGRYEERAGYHAVGSGSLFAKSALKKIYSPDSDEETALRAAIESLYDAADDDSATGGPDLTRGIYPTAVTITQAGAVHVSEETTSELARRIVAERTEQGGSAR
The following text describes a protein:
Function:
Part of the ABC transporter complex FepBDGC involved in ferric enterobactin uptake. Binds ferric enterobactin. Can also bind ferric enantioenterobactin, the left-handed stereoisomer of the natural E.coli siderophore, and the apo-siderophore, enterobactin, but does not bind ferric agrobactin.
Subcellular Localization:
Periplasm.
Sequence:
MRLAPLYRNALLLTGLLLSGIAAVQAADWPRQITDSRGTHTLESQPQRIVSTSVTLTGSLLAIDAPVIASGATTPNNRVADDQGFLRQWSKVAKERKLQRLYIGEPSAEAVAAQMPDLILISATGGDSALALYDQLSTIAPTLIINYDDKSWQSLLTQLGEITGHEKQAAERIAQFDKQLAAAKEQIKLPPQPVTAIVYTAAAHSANLWTPESAQGQMLEQLGFTLAKLPAGLNASQSQGKRHDIIQLGGENLAAGLNGESLFLFAGDQKDADAIYANPLLAHLPAVQNKQVYALGTETFRLDYYSAMQVLDRLKALF
The following text describes a protein:
Function:
Exhibits significant esterase activity with a preference for short acyl chain esters (C4-C8) in vitro. Its physiological function is not known. Displays neither proteolytic activity using casein as substrate, nor peptidase activity when assayed with L-leucine p-nitroanilide and L-proline p-nitroanilide.
Sequence:
MRLTVFLSLFLGVMVFGAFDQEAFLFVQHLTSENFESALNMCSNQVKAQLSVQSLSNIWNSLKAQLSDFREIAGYEKIIQAEYEIYNFTLKFDRGEISALVTMDREGKVAGLFFKQATKTEYELPDYVDPESFEEKDITVNGLPGKITIPKGSGPFPAVVLVHGSGPNDMDETIGPNKIFKDIAYGLSSKGIIVLRYHKRTFVEKVDPTTLTVEKEVIEDALEAVKILKERKDVSRVYVLGHSLGAMLTPEIAERSKADGVVMIAPPARPLEEVMEDQLKYLQSLGLASNVEETLNILEKLKRKEIPPDEFVLGAPAKYFYDLRERDPASIAKRLTIPMLLIFGGRDYQVTEKDQEIWLKELSGRENVKILVFDDLNHLMISGEGKSTPVEYMKKGHVDKRVIDEIARWMVK
The following text describes a protein:
Function:
Catalyzes the conversion of 2-hydroxyethylphosphonate into methylphosphonate in the methylphosphonate biosynthesis pathway.
Miscellaneous:
MISCELLANEOUS: The existence of the methylphosphonate biosynthesis pathway in marine microbes may explain the supersaturation of the aerobic ocean with methane. Methane is probably released following degradation of methylphosphonate produced by MpnS.
Sequence:
MEKKIDFKPDSYLIRSGNNFLGILNDIKRRPEDAANELGVSIEEINSIISGKQKISPSLIEKAVNIWPVNERDFYIVSDDCSSGILIMTSQDSIKSSRIMERAGKPYYEYRDTAMSKTAPFRPEWILELCKVENNDPENPKAQWNNGHFMHQFTYFIGEVNFYYKDPEGKKHVAIMNTGDSMYITPFTPHTFTTRDGASQNGLILALTYGSKLTGDIQQELSSLSLDCGSQYALDFTNHENASLSLLEYYFELSNLTKEKFAKRTNFSMETLADFFTKKKLPTFDELKIIAKALNVNSRDLMPNDLTESKVIVKTHDQCDHWKYPESGNYEFYELASTTALPHSKAFEIDVSSSEDLNLDLKVGLHQYVYNIGDSALTINWNYENKTYQKSLNPGDSAYIKPFVPHNFRGNGKILILRIGGKISGDSQRELSFVGRENTQRAISETMQWFDPKGSNS
The following text describes a protein:
Function:
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Interacts with beta-1 and beta-2, but not with beta-3.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side.
Sequence:
MSSNSNLSSMQRLVEQLKLEAGVERIKVSQAAAELQQYCMQNACKDALLVGVPAGSNPFREPRSCALL
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Sequence:
MDGIDPETLLEWLQTGIGDERDLQLMALEQLCMLLLMADNIDRCFESCPPRTFIPALCKIFIDETAPDNVLEVTARAITYYLDVSNECTRRITQVDGAVKAICARLAAAEMSDRSSKDLAEQCVKLLEHVCQRETMAVYDAGGINAMLNLVRVHGAQVHKDTMHSAMSVVTRLCGKMEPTDLELAKCAESLGALLEHDDPKVSESALRCFAALTDRFVRKMMDPAELAMHSNLVEHLISIMVSSNDESSPVAASANILSIVLSLIGNLCRGSSLITEKVLTSPNMIKGLKATLTNKEERVVTDGLRLCDLLLVLLCEGRSALPLTSVVSGDYAAGSGAERVHRQLIDAIRQKDLTALVDAIESGQVDVNFADDVGQSLTNWASAFGSIEMVQYLCDKGADVNKGHKSSSLHYAACFGRPDVSYDAGLLLSQVVKLLLQRGANPDLRDEDGKTALDKARERSDDDHNQVANILESPSTFMRNSTLSQKTKASASQQPGTSTKQELPNPQLVRKVLHQLLPIFCDIFQRSLNRTVRRTSLSLMRKIVENIGDLRQSAGEDNAAVTRSARKMSADVTAGAESLVAVVVSVLDQEDDYEGHEQVLLILQSLLEKDSELWVTELIRLGVFERVEAMAKEPPKGLEEVLAAINLEGRSRVVPMEIDFQNQPSSSSNDIMDAAPPSADIAGEEPAQPSIEVLISNLGISSYMAEPEPSTPSTSSQIAAPKPRSTTGSSASSAILQVVSKLSGVANLDKSSAADKKPTKIVLNQGSPYRWKEWRIVRGPTSLFIWSDVLLIELPFQSNGWFRYLADNDSHVQFVTGTANVDQQMSDEEKENFKKTERHEMVSRWNAVKGVFDDDWSTVPVSVLGVPSSAKKVSQKLEVPAWELWSSKSSELQIKSVSSSAPSGQANTMVTTIKIQDDAGGFLFESGTGRKTNVMPEHALPPPFHTGWSSHGVTTRKMKFRQDIQKRKVQELAWKLWNDHLKEAHAKPREALVRLEEAARLIEVSSCLHSVKTASNYKHRSAKHARIERIQEYTAAIKILYDSVVDDRRLSTFEFSVSGIVPALFALLSAIEKSPTDFYMRRIFMESFRVGESLSQLSLKIVAVLEASEKFPQYLYDSPGGSSFGLQLLSRRVRSKLEMIPSEEGKENIDENIVNKTGKVIKCEPLASVGAIKTYLMKLVARQWHDRERSQYKYVKEIKELKEKGKSVVLKHTSDFDENGVIYWIGTNGKTVPTWTNPATVKAVKVTCSDPRQPFGKPEDLLSRDSNPINCHSSDDKNSHFTFDLGVFLIPTSYTMRHSRGYGRSALRNWTLQGSIDSKKWDDIINHVDDKSLGEPGSTATWHVPEKGTVAYRYYRIAQNGKNSSGQTHYLSCSGFEIYGDIVDAVTEKIFEDAPKKESIAGPSSSGPSSSSSLPPLTKEQVLDMLPAHENNNRLKSGLTIETVTAMMQRSRHRVRDSYKLSDSKAKVVRGKDWRWEDQDGGEGKMGRIISPPESGWVDVAWENGYSNSYRYGANGNFDIERVSSSGHRYSSPSMPSGIPSSVMDAVRRNRAFYTAKGSGPPSALFGVPSGSSRGGENSSSSSSSPFPNLPIPPWRTSKSSTSPAIASRLISTVTSSGASPTPPPSSTSSTLSSLASGLGFGLNRHKQHNKPGASTLSRFASVKNPAPAGVAASGSSSGVAIGKKSMSTTNLVDDRQASAGPSVASTGQAASAESLQHQTPSLENLLARAIPHAFGRIAENQEQEEEPMGGEESDSAASMRSAASSNSQISMDSAQQQQQQQQDSDMTPRDAAGTPSTPRDDKNQTLSVSAPDLAAARQRQASAEAEGDSNMDESNSEDKTVGGDDAMEEDDEEEETVEDEEDNDDDDDDDDESSNENQEKLVELLANERGLFDKLKEVITGESLSDASSSAKDANTNEAQKKGGSKKPKKWFKKMSSYTDVLKGLMQSRYPVTLLDPSAAGMEMDEMMDEDDYYDFSEDGPDDGDSVEDEVAAHLGMPVDSFATMVAARTPITWRQFSELMSGSNRERAAMARAVASSRGNPWDDETVVKCSFEALIPAFDPRPGRSNVNQTLEVELPAVVNDFGPSKTSAKRTKDSVRFFIRGPNMSGVDNITLEMDDDCSSVFSYMQKINNNANWATKSDRGRRIWEPTYSICYCSSDNQKVEVTKIPSEESSTPVQVNQCLETIRLLARLQESIPEAEISPNVFISDKLTLKITQVLSDALVVAARALPEWCSRLIYKYPCLFTVETRNMYMQVSFFFQNLALSLEYSAKVKLISQRKFFRQQLSVSRVLSFGFNNAAMQLLNVLEEVLKEVMLLPGNMIVIMNTVLDVSELVSDLHSSSTLSLQQSCKESLWRYGCVMMMIPMLRKMQKREKSILVKERNRQGIFYVRRMGGLFPAPLPPGTEETKKASDMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLVSPQVGEQPHGPNLHNVLTLDDFEEVNPVKGSFLKELIAVSNRKKMIEKEVMDQTMKRRKIAEIKLHIKGSSCKMEDLALNFTVNPPSKVFQYTEMELVDGGGDIDVTVDNVEQYVERCEEFYLNSGIAQQMRAFREGFDRVFPLSSLRGYSPEELQRLLSGEQCPEWSRDDILNYTEPKLGYTRESPGFLRFVDVMESLTAQERKNFLQFATGCSSLPPGGLANLHPRLTIVRKVESGDGSYPSVNTCVHYLKLPEYSSAEILRERLLTAINEKGFHLN
The following text describes a protein:
Function:
Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG. The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG. The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone. The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL. These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin. Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps.
Sequence:
MSFGTLYTHNPTPRSTTLIALAKLHNLDVKIIHAEKKNKEAFEELCRYNPLGQVPTFVGADGFVLSECIPLTLYCNDERSSLRILQWMSFANSDLFPAVGGVFLPRIGQRQIIQQDDGDSLRAMLQRCKYLDEHLKRSRYLVGESITIADFFAASLLMGAFAAFRRSMQERFGALCSWYDGVLEIGWFKKVAGGVPDLGLELEIPEDIKW
The following text describes a protein:
Function:
5'->3' double-stranded DNA exonuclease.
Subcellular Localization:
Nucleus.
Sequence:
MGIPGLLPQLKRIQKQVSLKKYMYQTLAIDGYAWLHRASCACAFELVMNKPTNKYLQFFIKRLQLLKRLKIKPYIVFDGDSLFVKNHTETRRRKKRLENEMIAKKLWSAGNRYNAMEYFQKSVDITPEMAKCIIDYCKLHSIPYIVAPFEADPQMVYLEKMGLIQGIISEDSDLLVFGCKTLITKLNDQGKALEISKDDFSALPENFPLGELSEQQFRNLVCLAGCDYTSGIWKVGVVTAMKIVKRYSEMKDILIQIERTEKLCFSKAFKQQVEFANYAFQYQRVFCPLSNQITTLNNIPKAVTNSHAEIIKIMKCIGSVVERGSGVRKDVINTKNIDHKVHEMIAKGELHPVDMASKLINRERKLKARKLFKVGLLGGESNSFNKKVEQPLVDTQDVLSERENSLDNKNASSIYMTSPAAISGTVPSIF