lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MASGEHAKENNTFSMLRRSESGPSFSIGNDDDFNEPVVELPHPQLPNLTLQTPSREETPQTLHVEDVKNSTSSWSQDNSLVSSPITGVMDHSIFGERPEAFGNEMVTDQQFYDRIMDEQTSSYGQSLTSTDSFALLAEHQARERLDYARSEQDIVFGRERYDPFAPSQTRSPVSPHIPPVIITDPDANSMEGPSFSFGVADESFGAAEERVPQSSSEHERHHGSLSIQEGFVPYEAEPSHSERRDFNVFMPQLETSVPSHPPAYQSNEHEGSPIQENDDSEESKELESSYVPEKPTVEQPQRSVEEVDTNKSPKAEGIDNGSENPEQLDTINGSLVEENAAHEEHADVVDADIATKEASLTPHSVEAAKEDISAPAPATRESTTISVEKATDAEADLEQQETVQAHSTPSDKNALETEMMIDSKVSDAGAKAEVLDTPASPSAQENSNPEDTGNDVVETEPNVPREASSVSSPKATVESNTSANVASSGASPPTKEALQASNTVTAVPEVEEKLTEDDLFFKNIAAVSPVPEPTHSVNEEIYSSAPVQRQEPPSQPQDASPLKTNETNVQSPISATQQESQPQDASPLKTNETDVRSSISAAQQESQPQMQKTASPKTSDADADFFASLGAAEGSSKPLDTEEVNDEELLDDSEFDALMNSFIESSPAERPPQRAMTYQPSFHQQIPIMHPKPPYTIPASAPPTMSSQKKVNSFVATHDSYSSPYDLPMEIVQKAQRKRAEVQHTIQRKSPAAAFSQMSRPPFGRPPSVPPSMPSSSRTSPSMQRAFPPNATSMSRSSSYGRTYPTNLSLPPKTSPQHAPFTSTAAGSAAQNTQPLHGHDEIPAKPTYAPYIPSPYAPQNVATQQMQHAPIGTQQPSLNRMYSAPVSQYNSPTSTVPRMPPTRSSSSYTPPSVSQPAVVTANVPYAPRYTPQQRTLPSEVNDQPPRAAPQTARRSPYAPVSASITSPEIKVSSAPAPLPIQQPMNYTPVSGLTTQQKPVLPALSTSNLSAAPLNVPTPMSRQSSHQSVSRYAPVAPSTAETPVSIARVASNEGSETYPLQPVSSITQMVRSPVDAYTPTSATHHGEELNSMPQVSDEQALKQETPINMTPMEQRPMQTPPYLNPAMSLQNDSQMMQVDTQASDALYQPSASVLDLRATRSHAPLPAEPYMAHVQPEVNHGLHLPHPLVSFGPCGTFLTMCPFQSERFTSEGLVMKSTPGLLRFHSLKDFVPEENLFLTDFQGPYIGSNGKIDKAKRKQALAWVEKRLHYLEDQGENEEKLYIYKALGLMLGTDDKHRIRDGVREMLLPNFVPPETKNSTKTVAELMNPSLDEDNTPVVATSSVTAGFLQKIHNFLLVGDRESALTCAMNRKNWAYAILLASSLGKETFQSVVHDFIKSDLMSETQTANVEVNLRVIFQLLSGASLAFSELSSSCPLLSLTQANSAEGNQDLQWKELLCMLLANDVPEQVQAFRHLGELLLQQGRTYAAHLVFLLSMSPIICLYNGKERNPMPLVGLVNPNAYSDSTELLESVMLTEVWELILNLHANKETISYAHLQIFKLYHARVLADYGQLALAKRYCECIGQYLKMASKKSSASIDPSLVSGVRDLSRQVLESSNTNTEVSNSWLGRTVSRPKLDSFWSALESKFSKFVAGDANFDITKDNTVDGPFAKVAEVQETITRASSALALRDDEVVGERVMPYGSVPQSVPTSRVPSPYQPLDQQVHAGPHSANPYVGAAGIRRDTGHVSSSGPYLEIPSAQTSPKRGPYALPVRPTYTPTTTAGYNPYVPQTLSTPAQAAEPAAYQLGQPVRSTPPQGPMSPAEVSAFAPAPPTAETPTRNTYGPTPAAVSPVYAPSLSPQQPYQNLPSRTHSRVPSASSDISVGRSMNQLADAMGGMNIDTDRAAEAKQSASKIAEEMIKREEEEEAKKKQAASTKKSGGMGWFSKLLHRGGNNESANNGQPVYKAKLGEKSHLRYDKEKKRWVNEDGSDLSNQAAPPPPPPKMSMMPRRTATTSVPPPAMPASNLGTIPESMSGLAGPPSSSGAVAQQPLATGPIPPASSPAPLSATTPTAPVPPATAPPAPTPRAGLPRPPLGGTASTTKKTDLLDELLSAPPTAPSERRHKKVSKRYVDVMNMQ
The following text describes a protein:
Function:
Part of the pafABC operon, but PafC does not seem to be involved in pupylation or substrate degradation. Appears to play at least a small role in resistance to reactive nitrogen intermediates (RNI) in vitro.
Sequence:
MSALSTRLVRLLNMVPYFQANPRITRAEAAAELGVTAKQLEEDLNQLWMCGLPGYSPGDLIDFEFCGDTIEVTFSAGIDRPLKLTSPEATGLLVALRALADIPGVVDPQAARSAIAKIAAAAGAVAAVAEQAPTESPAAAAVRAAVRNSRALTIDYYAASHDTLTTRIVDPIRVLLIGGHSYLEAWSREAEGVRLFRFDRIVDAAELGEPAVPPESARQAPPDTSLFDGDLSLPSATLRVAPSASWMLEYYPIRELRQLPDGSCEVAMTYASEDWMTRLLLGFGSDVRVLAPESLAQRVRDAATAALDAYQAAAPP
The following text describes a protein:
Function:
Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding.
Sequence:
MGCCGLLQAHGHRHDPQKYIIRGEIEIDRSPWFSLCASGSSVVFRLYSQDEMDPTTRKGVESENAYVMKGKELEKKKHEVLSMKVPTKVIKFELKFEVTRDFGIPGAFVVENRDKKHEFFLKSVTLHYIKHPDLEKRKFHFYCDSWVYPITKTGFKRIFFSDQLYLPKETPKGLAELRKKELLKLQAPRLKGEWNPWDRIYDYDVYNDLGDPEKGRSYDRPVLGDSTKFPYPRRLKTGHLNCQHDHSRESGPARCFQFYVPPDERMSDEKLQELKNNFVEALIRFLAQESTPPHLWDRECPDFVTKVAHFFVPKAAISKKDVRFIRSIIDFCRKLKLPSSHGGPSRSDPSEEQDIFDDIIGFYADKEVEELDDSDRQRLEKLVPKEILDQVVATLALKRQHVSAQLPSIIAEEKFAAFEEEEFGRQMLAGTNPVRIRRLKEEDFSLLMENFQERYPGIKLEDLENLLKEKMKASRAFILDHHYLEQFLKMINGKGVHAYATRTILIADDPSSEGIVPVAIELSLPEDSDDGRSMFLVEENCSGVLWELAKFHVASNDTAYHQLVSHWLHTHAVVEPFIIATRRRLSVMHPIHRLLDPHFKDTLHINALARAIFLNAGGIVETLLFTGEYSMELSSHLYKEWRFDKQALPEDLLERGMAKPRVRDEVVSGPMEHVESDKSSNKAAKGAEQEMFEVDAEVELVLEDYPYAKDGIEIWTAIETWVTEYCNVFYHNDNDVKEDEEIQEWWNEIKTRGHVDRKEGWYDINTFESLVKALTTLIWITSGLHAAVNFGQYGYGGWPPNRSMLLRKFLPKEDEVERMDIMKFVEEMLPDKFQMKLAIAVMDLLSRHTSDEVYLGQTSPQKEWPLIEDDDIIQKKFKEFRENLEAIEQNIKERNKEYLLMNRWGYAKIPYKLLYPDTSKSMPPTSKEKGKHHPERTDINESGIPNSISI
The following text describes a protein:
Function:
Nutrient transporter (By similarity). Involved in maintaining the osmotic homeostasis of the digestive vacuole (By similarity).
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MTNNDKEKQPLLSSINNEDDNGATINIVEPVPWYSNIPQKIKNSMSKETITILIYVVLYVTSGVINSVLLKKVMNKFTNYAFFLSQLTNFGYVPIFGAVTAYKIFFTKDIPQETRDFPTRKFAIMGALDAITGFFVVIGGVSTSGPLQQLLNQAIIPFTMIASFIFLKERYSLIQLGGALVIIGGVVTSLIPSLLGGSSGGNKPFWNFFYLLSVIPGALSNVYKDIGFQAVADMDVWYLQYWDSLYQSIFGLFLFPVNNWLPPPATVKFEQILPFMKEGAECLAGINSIIPSYINGTSSFTATSCTYAPDATITCDDCHNAWIVIILYMTINIIYNIFILLVLKHAGATVYSIANTLRLPLTNIVFSIHFIMGSAVSPFSGLSVAGLVIILVGLGGYRVGSMIKQKKAAAAGGAIKVIPSYGPAGMDNIIPVQKEYIEPKSQAHLRNQFFGKLGINVPEARYRAANNNNYGDA
The following text describes a protein:
Function:
Isoform MOCS1A and isoform MOCS1B probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP). MOCS1A catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate and MOCS1B catalyzes the subsequent conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cPMP.
Sequence:
MFTSRPCSVLINRTPCVACHIWKVSVLGSSSSPHPHPQSSHHHHHLVAPRRSLHRSTSTFPSSKQASSAKVKFFQEDTILPFSAFLTDPFQRHHNYLRISLTERCNLRCQYCMPEEGVTLSPKERLLSTEEILHLAKLFVSEGVDKIRLTGGEPLVRKDIVEIIEGLRELEGLKQIAMTTNGVTLAKRLPALKKAGLDLINISIDTLVPQKFEFISRRKGWHHVMRGIDAALEHGYDPVKVNCVVMRGLNEDELCDFVALTEDKALDIRFIEYMPFDGNRWNDKKLITKDEIVQTIRGRFPDFGPIDNLPNDTSVAYSVPGFVGQVGIIASMSKPFCGSCNRLRLTADGNLKVCLFGSDEVSLRDALREGRSDEELLQVIGAAVGKKKKQHAGMFKIAKMQNRPMILIDSSPMEIGMLGAPHHRNQDSFYSSSSVGNQHVLPVSILFNHGARSYKPYHSPRASFHSSTKSCMAKDSSDGDRSRLTHVDRSGQAEMVDVSGKETTVREAVASGKVRLGREAFYLVQENKMTKGDVLRVAQLAGIMAAKQTSSLIPLCHNIPIQKVDIDLQLEEESFSVLVRSKVKCIGRTGVEMEALTAVSVAALTIYDMCKAVTHDMVIAEVRLEQKTGGQRGDYHREVN
The following text describes a protein:
Function:
Required for mating and morphogenesis. Interacts directly with scd1 and with cdc42. May bridge and facilitate scd1 and cdc42 interactions.
Sequence:
MLKIKRTWKTHSRILDKDPFSIEPPRKVIRALYDYTARKATEVSFAKGDFFHVIGRENDKAWYEVCNPAAGTRGFVPVSHFEEIGKTVKSERDSDGSGQISFTDLTTNSSTTRSSISELHSGSQPLFGIVQFDFAAERPDELEAKAGEAIIIIARSNHEWLVAKPIGRLGGPGLIPLSFIQLRDLKTGAVIKDVSEAVLRISCIPRVEDWKRAAADYKKSSIPLGKFSDGETQTMPSLSPSTENLQINNDVTYQAATDNSSTFPGSVANELTPLQTLESRTASIASKNKKDMSSEPTVVAAMVENYMIRDDQYWYLVRAVMSDGKHRNLCRYYEDFFNFQTKFLELFPNEAGRGDERRVIPYMPGPVDDVNELISSQRAMDLDVYLKEMCRLPARLLENELVKLFFLPLDGDVESPHPTSTMPEALPREPLSFSLPEKAPEKATNISIPESAPTTAGSTCKVKVRLGDETFALRVPSDISFEDFCERLTNKLGECEHLSYRDTNANKVLPLNNVDDLRKACSQESGVLLFAERRRF
The following text describes a protein:
Function:
Links the unfolded protein response and programmed cell death and mediates mitochondrial-dependent apoptosis. Induces cell death and disruption of the mitochondrial transmembrane potential (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein.
Sequence:
MPANYQSVPQDDPSVPNLAQAPPAYSEYNESATENPAVDQFKNTTPVAECAKSIRMAFLRKVYAILTAQLFVTSLFGGIFYLHPAFSFWVQMHPWFLILNFFISLVVLFGLIMKPYSYPRNYIFLFLFTALEGLTLGTAITFFSARIILEAVFITLGVFVALTAFTFQSKWDFSRLGGFLYVSLWSLILTPLIFFFVPSTPFIDMAFAGFGTLVFCGYILFDTYNILHRYSPEEFIMSSLMLYLDFINLFIRILQILGMLQNNDNN
The following text describes a protein:
Function:
Regulates cell junction organization in epithelial cells. May play a role in the transition from adherens junction to tight junction assembly. May regulate F-actin polymerization required for tight junctional localization dynamics and affect the junctional localization of PARD6B. During podocyte differentiation may negatively regulate activity of FYN and subsequently the abundance of nephrin.
Subcellular Localization:
Cell junction, adherens junction. Membrane; Multi-pass membrane protein.
Sequence:
MASAGSGMEEVRVSVLTPLKLVGLVCIFLALCLDLGAVLSPAWVTADHQYYLSLWESCRKPANLDSWHCESTLGSDWQIATLALLLGGAAIILIAFLVGLISICVGSRRRFYRPVAVMLFAAVVLQVCSLVLYPIKFIETVSLKIYHEFNWGYGLAWGATIFSFGGAILYCLNPKNYEDYY
The following text describes a protein:
Function:
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
Subcellular Localization:
Nucleus.
Sequence:
MSYAQYGGSGRNPGVEARIVGNLKLEYTSFEDSVTPGTTERPLLMENMLRQKNVSIDVMEGYNPIIPESVNQHSIYHLYEYESQTKFLDKIPRPLIGDTEFRTRFLCCRYVICSIDDWMTRRKPAELLAIRKNGDIYIGANKSLEENSSSTNEAAYGGLNFGTKVTHRATPFESRKHHSVVKQWYLENRKTHRSMSIFISSVARAFDSRGEVVELKTVGSKVQGKIQNLPGAKARNWWLRALLSGATRIVYGLRMDDMIVNEILEAHIDEFTHGHFKFSATRLFTEIYKIFEKVDKKLSNEGDMCLITLQRYDVDITIANDDDLNKSPFW
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MKLFGLSVVTLLATIGSVVADKQLENRQLFRTVDLSKSYVREFIAVNVYNDGTSDETDYIVSIPPGFVDDLAKLDIKESSHEAPLKVIRLARDEHGEHWSAILPEPIKPGSQVQLQLFLSYVNQLQPVPQTIKQSEQQHLVYDGLKTFYSLYPTKSQTNRVKIMAQNMQEINMDENSTPSTEAEGGAQYGPFGPMGSFEVEPLVLRYDYPLPIPRVDSLKRDIWISHVSNSIAIEESYNLTNAGAKLDGSFSRTDFFAHHGKPSSASASIIELPFTLPLGAHDVYYTDLVGNVSTSHFRGGKEVSLLELRPRYPVFGGWNYNFTIGWEMPLTSVSRTTGADEYVVGLPLLNGPVDAQYRQIESNYILPEGAENVQVVTSEPALSKEESVTFSYLDKKGRPTIQVRHVNFVDQHRGGIVFLKYTLPGSAATIKPIFIATVIGSIFLAIFSLSQLDFTISQRPKKTTKE
The following text describes a protein:
Function:
May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MGQVGSGCKGCVLFLQRPGSQSPPNEGVFLRQSARAREQAGSRFWRRFHVGGAFGSSRRFQRHLALEEGRGEEKEALLCRLAGPFRLSSRAGGLKGVSRRDGLRAGGLSPGSRPHSGTSYSCAGIAGDSVSCLSRPRSGRGEKGVLSPALAAWGPRTNLRRGSSRSYSWRWQQAMAAALEELRKDLEEVKELLGKATRKRVRDVLTAEKSKLETEIKHKTKQKGEEKRETAEIEKPAAVVAPISVGYTVKINNYGWDQSDKFVKIYITLTGVQNAPPENVQVQFTERSFEVLVKNLNGKNYSMTVNNLLKPISVEGSLRKIKTDTVLVLCKKKQEQKWDYLTQVEKECKEKEKSSFDNDTDPSEGLMNVLKKIYEDGDDEMKRTINKAWVESREKQAKGETEF
The following text describes a protein:
Function:
Serine protease inhibitor that specifically inhibits clotting factor C. Does not inhibit clotting factor B or proclotting enzyme.
Subcellular Localization:
Secreted. Note=Localizes in the large granules of hemocytes (By similarity). Secreted in hemolymph in response to external stimuli (By similarity).
Sequence:
MKLGDWKFCLLLFQLMFLTNVCLSDLSFNPYKWPVNQLRRVIGAVKVTNTSNYFGFSLYENLNSNGNVFISPYSLASVMAMLYLGARGVTKNEMDLTLGYNSVNLNSEDLVLGFQQSLLLLNAESKEYQLETANSLMIQNTFNILDNYKRMLEDKFGANVQDVDFINKAELVQRYINAWVAFKTKNKIPILLNEPLKPETRLAFFNAVYFKGVWETKFDSALTRRATFYNNGYVPTQVPMMMLRGIFPFAYVSSLRSYVLELPYKGHEVSMLLLLPKDRNGISDLERDLSSSSLDSVTSNLREIGVLVTIPKFKLEETYEDDLKQSLESMGMTSLFSEANANLEGITGHRDLFVTKITHRTLIEVNEEGTEASGISSVVAGVRSGWKRPTFTADHPFVFFIRHNRSGIILFMGRVSQL
The following text describes a protein:
Function:
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
Sequence:
MAYQVLARKWRPKTFADLVGQEHVVKALQNALDEGRLHHAYLLTGTRGVGKTTIARILAKSLNCENAQHGEPCGVCESCTQIDAGRYVDLLEIDAASNTGIDNIREVLENAQYAPTAGKYKVYIIDEVHMLSKSAFNAMLKTLEEPPEHVKFILATTDPHKVPVTVLSRCLQFVLRNMTAQQVADHLAHVLDSEKIAYEPAALQLLGRAAAGSMRDALSLLDQAIALGSGKVAENDVRQMIGAVDKQYLYELLTGIINQDGAALTAKAQEMAACAVGFDNALGELAILLQHLALIQAVPNALAHDDPDSDILHRLAQTISGEQIQLYYQIAVHGKRDLSLAPDEYAGFMMTLLRMLAFAPLAAASCDANAVIENTELKSPSAQTAEKETAAKKPQPRPEAETAQTPVQTASAAAMPSEGKTAEPVTNQENNDIPPWEDAPDETAAGTAQASAKSIQTASEAGTPPKNQVSKNEAADNETDAPLSEVPSENPIQATPNNEALETEAFAHEAPAKPFNGYSFPNDDYLVEDGAEIPPPDWEHAAPADAEEENNADESSNNEDHTPYAPPPEFSTENWAAIVRHFARKLGAAQMPAQHSAWTEYHPDTGLMVLAMTAEARATADKKRLDKIRDTLAQAYGLQLTLQTQDWRDEAGRETPAMQDKRVQAEDRQKAQALLEADPAAQKILQAFGAQWQPESLELAANRP
The following text describes a protein:
Function:
Functions in trans to edit the amino acid from incorrectly charged Cys-tRNA(Pro) via a Cys-tRNA(Pro) deacylase activity. Probably compensates for the lack of Cys-tRNA(Pro) editing by ProRS. Is also able to deacylate Cys-tRNA(Cys), and displays weak deacylase activity in vitro against Gly-tRNA(Gly), as well as, at higher concentrations, some other correctly charged tRNAs. Does not cleave Pro-tRNA(Pro).
Miscellaneous:
MISCELLANEOUS: Reaction mechanism involves exclusion of catalytic water from the active site and substrate-mediated catalysis: the sulfhydryl side chain of the Cys substrate acts as a nucleophile and attacks the carbonyl center of the ester bond, leading to the cleavage of the Cys-tRNA ester bond and formation of a cyclic cysteine thiolactone intermediate. In contrast, the INS editing domain of ProRS catalyzes Ala-tRNA(Pro) hydrolysis via nucleophilic attack by a catalytic water molecule.
Subcellular Localization:
Cytoplasm.
Sequence:
MTPAIDLLKKQKIPFILHTYDHDPNNQHFGDEAAEKLGIDPNRSFKTLLVAENGDQKKLACFVLATANMLNLKKAAKSIGVKKVEMADKDAAQKSTGYLVGGISPLGQKKRVKTVINSTALEFETIYVSGGKRGLSVEIAPQDLAKVLGAEFTDIVDE
The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MTTQNQWSELNLEPIIQKVIANEFKFQYLMPVQKAAIPHFIKNYDVAVEAQTGSGKTLTFLVPLFNQFSKQKYSDHQLFGLVLSPARELAQQIYDVAKNFQNVNQAKIAFAIGGTSNEHDVKYLNEKGCNILIATPGKLRQLLDMADLQVNVKTLEYLIFDEADRLMSNEYSDDIRFILSKLPKQRRTGLFSATLSSAKIHDLMKLGLRNPVQVKVNANETMPAKLRNYYHIFENRMDKISGLVDLIEKKCQNNKSIIFFNTCCSVVYYSIIFKQLFPDCNFLSMNGQMAQKKRQKIVANFKSTNSVILFTTDVLARGLDFDDVPLVIQFDPPQDPSFFIHRSGRTARQGRDGEAILLLEQHERGFIQFLGRSNIEMNQLEDVAFDCQFQQLKEKCLKIVTTDRDIIEKGKAAFISFIRSYKEHKLQILFQFNQLNIGKVACSFFLLRIPRIKEILSKKIEFEQSQIDPNSIPFLDKNQEKQYLQKRENKDKKLEEKNIQQLPKQQVPKKQEKNIKNIKSIRKKVKQQHVQEDDEELRAEQNLVRKLKQGKITLQQFKDRMKDFDPEDLQDADYDKDDL
The following text describes a protein:
Function:
Endonuclease important for programmed cell death; it mediates apoptotic DNA fragmentation.
Miscellaneous:
MISCELLANEOUS: The active site contains 1 hydrated magnesium ion that has only 1 direct interaction with the protein; all other interactions are via water molecules.
Subcellular Localization:
Mitochondrion.
Sequence:
MIGKVAGTAAIAGISFLAGKYSNDDLPIFRNVQSATNVPMNQIQVSEPMTVKPASLNADAMGPSRSAEIMKHGYPGFTNVRTYEDFVLSYDYKTRTAHWVCEHLTPERLKHAEGVDRKLCEFKPDITFPQKFLSQNTDYKCSGFDRGHLAAAGNHRKSQLAVDQTFYLSNMSPQVGRGFNRDKWNDLEMHCRRVAKKMINSYIITGPLYLPKLEGDGKKYIKYQVIGDNNVAVPTHFFKVALFEVTPGKFELESYILPNAVIEDTVEISKFHVPLDAVERSAGLEIFARLDPKSIVKENGAKKGGLLW
The following text describes a protein:
Function:
Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Domain:
Class I metallothioneins contain 2 metal-binding domains: four divalent ions are chelated within cluster A of the alpha domain and are coordinated via cysteinyl thiolate bridges to 11 cysteine ligands. Cluster B, the corresponding region within the beta domain, can ligate three divalent ions to 9 cysteines.
Sequence:
MDPNCSCVAGESCTCAGSCKCKQCRCASCKKSCCSCCPVGCAKCAQGCVCKGASDKCSCCA
The following text describes a protein:
Function:
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Subcellular Localization:
Mitochondrion.
Sequence:
MNRLPSRLGRMRMPATRSYSIFARTSSKKSLPNPKGEPSAAPDSGKTGKKQPFVHDYSVRPTTYVYRMEDNAESFSKYPLMTSKKLSKSSSRPRGVRMTAKDFMDDSLYNPYYGYFSRNVEIFTTDKPFDYTNINDVDDFLNTWTGEYSKYAANSPTLTGKTKDTSHSGTFPAQDKDFTSRGASKQLWHTPTELFKPYYGEALARYLLVNYKLSLYPYKDLIIYEMGGGNGTLMTNILDYIRDTQPEVYERTRYKVIEISDQLAHKQQSALHTKASETGHRSKVEIINKSIFDWKEPVNDPCFFVALEVFDNFAHDIVRYDNRTLQPYQGHVLVDANGDFHEVYTQKLDEWTKLFLQIRTEALEDYSPDSRLGFHPLSTPWLYKEARNLMWPFHSELSDPEFIPTRYLEFLYILKKYFPQARLLSSDFTHLPETTTSRFSGYNSPVVQTVLDNQMVTTNTHMVLQGYFDILFPTDFELAAQLLRHVCGRVPEISTHQEFLEQWADLDATTTKTGENPMTSFYRNAAFLTN
The following text describes a protein:
Function:
Directs RNA polymerase II nuclear import.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MATVVRIKRKADENPADTIVLAPKAAKLWHDEDRDFTLTYAGTFKDPNCKEADEAIRQVKDSKKQLRTDPKTHTVDIASKVREEHRSASKKSRLKLLLQHRAIIEEVHSEEIDDKDLESPHKTVNSLFRLYDVVAEDFQKEENASHEDAATENASTITCNDVAMVLEKVKPPELEEDFVYDVYYSHSELNLLDKPDLSVFQCLAPEDFEPEAAYESDLGLDDDDSDSNAEDNWRNYYPDEETDFERQLDYYGDYSDDGGTDFVSDRVRSLCLDIDDDLSTED
The following text describes a protein:
Function:
Redundantly with pde-1, plays a role in the AFD thermosensory neurons to regulate microvilli receptive ending morphology, possibly by regulating cGMP levels.
Sequence:
MDDASVLKYLQENPKLVEDFVVSNEISPETFKRWAVRRTMKYKNVKNGTSGGTGAWTEPDLSMKRRVILETSDNRTRILYEITQCCGQLIGTNSIELIVQNDEGAFSCRKTENGELKLKKVKTSKSADYIQTIVNAGNQTIAEIHFYTQLDSTEKSIVNAVCTWAAATNYYSELYTHKQEGSDGQDIHENIAKQRKLSNFLLDVARSIFHDIVSMDAVIIKVMNFAQKLVDADRASLFLVDSKNAQIYARIFDVGTGDEEHVRVNSEGQKEIRFDMSKGIAGYVASTGEGLNIENAYEDERFNADVDSKTGYTTKTILCMPILIRGIVIGVVQMVNKHDGVFTRQDEDAFEIFAVYCGLALHHAKLYDKIRRSEQKYRVALEVLAYHSVCNADEVNKLKKIEINNRIVELETIDFNGMRLSELEKPLYAVYMFKTLFADTLRFDTEDLIRFVLTVRKNYRRVAYHNWAHGWSVAHAMFATLMNSPDAFTKLEALALYVSCLCHDLDHRGKNNAYMKTMSTPLASIYSTSVMERHHFNQTVTILQQDGHNILKSLSSEDYKKTLSLIKHCILATDLALFFSNKAKLNVILDNNTFDINRQEHRLLTQAVMMTGCDLVASAKPWNIQTETVKVIFEEFYDQGDAERLSGKEPIPMMDRQQAHMLPQMQVGFMRGICMPCYDLIARIFPKNDKMRERCEYNAKKWEELAEEQRKKQEALAQQNGEANETQE
The following text describes a protein:
Function:
Catalyzes the conversion of alpha-L-mycarosylerythronolide B into erythromycin D in the erythromycin biosynthesis pathway.
Sequence:
MRVVFSSMASKSHLFGLVPLAWAFRAAGHEVRVVASPALTEDITAAGLTAVPVGTDVDLVDFMTHAGHDIIDYVRSLDFSERDPATLTWEHLLGMQTVLTPTFYALMSPDTLIEGMVSFCRKWRPDLVIWEPLTFAAPIAAAVTGTPHARLLWGPDITTRARQNFLGLLPDQPEEHREDPLAEWLTWTLEKYGGPAFDEEVVVGQWTIDPAPAAIRLDTGLKTVGMRYVDYNGPSVVPEWLHDEPERRRVCLTLGISSRENSIGQVSIEELLGAVGDVDAEIIATFDAQQLEGVANIPDNVRTVGFVPMHALLPTCAATVHHGGPGSWHTAAIHGVPQVILPDGWDTGVRAQRTQEFGAGIALPVPELTPDQLRESVKRVLDDPAHRAGAARMRDDMLAEPSPAEVVGICEELAAGRREPR
The following text describes a protein:
Function:
Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin-arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export.
Subcellular Localization:
Cytoplasm.
Sequence:
MPEALQIASLILHCRPERLPAVKANLALLDGLEIYQESPQGKLILVLEAEREEQILDTLGQLQNLPGVLNAVLVYHEILHDDDSNDAAAMTDRAIPCSPEETIDEPHPS
The following text describes a protein:
Function:
Required for myoblast differentiation into myotubes, possibly acting as a transcriptional regulator of the myogenic program (By similarity). Required for cardiac adaptation to stress through integrated regulation of the AKT/mTOR pathways and FOXO1. Regulates cardiac homeostasis and plays a role in the protection against cardiac hypertrophy. Binds chromatin (By similarity). May act as a transcriptional cofactor for ISL1, repressing its transcriptional activity (By similarity). May also repress MYOCD transcriptional activity (By similarity).
Subcellular Localization:
Nucleus. Nucleus envelope. Nucleus, PML body. Cytoplasm, cytosol. Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MTSCVLAGSIETTPKVSPGDSEAKPLIFTFVPTLRRLPTHIQLADTSKFLVKIPEEPTDKNPETVNRFEYSDHMTFSCESKEERDQRILDYPSEVSGKNSQRKEFNTKEPQGMQKGDLFKAEYVFIVDSDGEDEATCRQGEQGPPGATGNIATRPKSLAISSSLASDVVRPKVRGVDVKVSSHPEIPHGIAPQQKHGQLTSPTTSEQLAHKPPAFSFVSPTNQKTPPVPAKVSGTTVLEEFHIRRLDVHGASEEETATYFHTTAHDSPLPAWKGASTLVFSPSAQLPGSSLCGSNVADHTRGLAPEAQKKVSTSSALNPREDVRTSPSPASGASLRSPSASYIPVRIVMHSLSPSPKPLTSSSHGSLSTVCSQTSSSGNLSKSGLKSPVPSRLSLLTAILKSNPSHQRPLSPASCPTFSLNSLASSTLTLDQKIKQTPSTPKKSLSSCSLTTGSTEQEQASAESHQPCHLSFFSKTTPLSQAQPPSPPALASSSYAATDTEKIPGSTLRSSTTPPQSQTDLFSLADVPSVTPGLSPLSSSKGRKDGDLRAPEKNRNICTRPSTLSFIPPINESTALSSSGKCFHPSPALSDLIDRSKRTCSQRHSDQRPNPSALPTPPVSRAGSASHPHLGYSILPPESSLTQALQRSPSALHPSCGSATCPSRTGMPDSTASNRSSRVSTPSLPVSLTRTKELISPCALSMSAGPENKKPKQYKTKSSYKAFAAIPTNTLLLEQKALDEPARTESNSKASVSDLPVELCFPAQLRQQTEELCATIDKVLQDSLSMHSSDSPSRPSQTMLGSETIKTPTTHPRAAGRETKYANLSSSSSTTSESQLTKPGVIRPVPIKSKLFLKKEEEVYEPNPFSKYLEDSSGLFSEQDMAIPHKPVSLHPLYQSKLYPPAKSLLRPQTLSHADCLTPGPFSHLSSFSLRDEQEKSPTLLSQDTYNKPGHPMVTIPEHDTLDSKE
The following text describes a protein:
Function:
Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
Sequence:
MSRDRGGIELVSHGRGVRDCFEENESASDAPDGGMEWVSSGDASEECVNDVDDIYSNRDDSGADEEGNEFGREYEDDRGEFRSGFATAFSNILARDLEIQQRHCQQVEGAGVDVNPRVATADGQVATAGAKEKICCICKDKSVYTCPGCGARTCSMTCVRVHKAQFNCSGERNVAEKVPLSEFTDKQLERDFHFLEDTRRVISNCERTFPKMWRYTFRALPPPLYALRKAAKQRGVVCQITSEGMSKRDANTSRFDRRTETIIWRCQFNFHTPNFTVSTDWGNERHKLGDILTYCWAKNPPVHCFHINRRYNRASKWIGIEGEREGKEVEREEEGEKDKENVENGREENESVEFRCSGASDTLADISTRKEDSNDEDGAVGPLFVEVGDKQQQQQVWKPSVLDISPQSPEETKSKETVSAFLSLGPVIILAQAERLGLEKKYFRLSPSQTLNETLRTLFFINEFPVFEVIHASDLESYALVTDADKERIRESFRAAPRPTKPERPPRPTKSTLTPEERDRYAQVPCRLFLAGCCKLGEEECPYRHCEYQDVPVCRSFMKFASCEKGNRCVFRHDATAVATARKRMREERQAVQLGRRRF
The following text describes a protein:
Function:
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Sequence:
MEGGLWNKELLLKFVVLAVAVVNTLQRNGERHVCRVLFEHMSTCCVHWSDPTLAGPILRMHFHFCDASVLIAGDGGTERTAGPNLNLRGYEVIDDAKAKLEAVCPGVVSCADILTFAAPDSVVLIIFLTLPTGRRDGMVSIGTEALSLPGRNDNVATQKDKFLKKGLNTEDLVILADTRTFQLNSIFNPKGTDPSFLPFLRQNQPTKRVALDTGSQFKFDTSYFKYLATAPFKVQFGKSMIKMSNIGVKTGSLGEIRNKCYAIN
The following text describes a protein:
Function:
Transcription factor that plays an essential role in anti-viral immunity. It mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. IRF9/ISGF3G associates with the phosphorylated STAT1:STAT2 dimer to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state.
Subcellular Localization:
Nucleus.
Sequence:
MASGRARCTRKLRNWVVEQVESGQFPGVCWDDTAKTMFRIPWKHAGKQDFREDQDAAFFKAWAIFKGKYKEGDTGGPAVWKTRLRCALNKSSEFKEVPERGRMDVAEPYKVYQLLPPGTVSGQPGTQKSPSKRHHSSVSSEREEEEDAMQNCTLSPSVLQDSLNNEEEGASGGAVHSDIGSSSSSSPEPQEVTDTTEAPFQGDQRSLEFLLPPEPDYSLLLTFIYNGRVVGEAQVQSLDCRLVAEPSGSESGMEQVLFPKPGPLEPTQRLLSQLERGILVASNPRGLFVQRLCPIPISWNAPQAPPGPGPHLLPSNECVELFRTAYFCRDLARYFQGLGPPPKFQVTLNFWEESHGSSHTPQNLITVKHEPLPRYLLQQKQTARSKQSSLF
The following text describes a protein:
Function:
Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity).
Sequence:
MDDTQVNAQLDQMKNFILQEAQDKANEIKTKATQEFTSEKGRIFQNEKIKIIKEYEKKQKLIEVQKKINLSNELNKSRLSVLKVREECLRDVIKEAQKKLATISDDKDKYQTILKNLIYQGFVKLNENKIQVVGRKEDAGLLEKATTEAAAQYKKNVGKSIDVSVDKERFLPQGPKSDYNGPTCCGGVILSALEGRIICKNTLDSRLEICFDQLTPVIRTQLYGASTSRKFFD