lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Encapsidates the genome protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure. As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation. Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). Suppresses apoptosis probably through the inhibition of nuclear import of NF-kappa-B.
Subcellular Localization:
Virion. Host cytoplasm, host perinuclear region. Host Golgi apparatus, host cis-Golgi network. Note=Internal protein of virus particle.
Domain:
The N-terminus is required for chaperone activity and, in trimeric form, this region likely serves in high affinity vRNA panhandle recognition (By similarity). The N-terminus also contains a coiled coil region, which probably participates in but is insufficient to initiate N trimerization (By similarity). The YxxL motif is indispensable for the interaction with host MAP1LC3B. The central region is involved in specific RNA-binding. Has distinct cap- and RNA-binding sites so it can bind simultaneously both the vRNA and mRNA cap (By similarity).
Sequence:
MATMEELQREINAHEGQLVIARQKVRDAEKQYEKDPDELNKRTLTDREGVAVSIQAKIDELKRQLADRIATGKNLGKEQDPTGVEPGDHLKERSMLSYGNVLDLNHLDIDEPTGQTADWLSIIVYLTSFVVPILLKALYMLTTRGRQTTKDNKGTRIRFKDDSSFEDVNGIRKPKHLYVSLPNAQSSMKAEEITPGRYRTAVCGLYPAQIKARQMISPVMSVIGFLALAKDWSDRIEQWLIEPCKLLPDTAAVSLLGGPATNRDYLRQRQVALGNMETKESKAIRQHAEAAGCSMIEDIESPSSIWVFAGAPDRCPPTCLFIAGIAELGAFFSILQDMRNTIMASKTVGTSEEKLRKKSSFYQSYLRRTQSMGIQLGQRIIVLFMVAWGKEAVDNFHLGDDMDPELRTLAQSLIDVKVKEISNQEPLKL
The following text describes a protein:
Function:
Part of a rhi-dependent transcription machinery that enables the generation of piRNA precursors from heterochromatin while maintaining the suppression of transposon-encoded promoters and enhancers. Moonshiner/CG12721 recruits transcriptional machinery to heterochromatin to initiate the bidirectional transcription of piRNA clusters. Functions by forming a complex with transcription initiation factors TfIIA-S and Trf2, and interacting with del which is part of the RDC (rhi, del and cuff) complex that binds to repressive H3K9me3 marks in the chromatin. This mechanism allows transcription to occur in piRNA clusters despite the lack of proper promoter elements and in the presence of the repressive H3K9me3 mark.
Miscellaneous:
MISCELLANEOUS: The name 'Moonshiner' derives from its activity in the transcriptional 'prohibition' of heterochromatin.
Subcellular Localization:
Nucleus. Note=Expressed in nuclear foci.
Sequence:
MAKILPTDGIWIPESCSFPEDVMIDMMEGLFRDVPNLTHKEYLALADLQSRWMAKLANRQPESNPLPPKPKKRKKIAPKKQDQPVEEKGSEVDIYDVDDNEMVNNRIYIPRLRSAWRARYFNIMMRAFVIKRGLLNKHINWQILDKIMAAPDAEGQAELQAFVDKVVAGQEM
The following text describes a protein:
Function:
Required for CNS development; midline glial cells. Involved in the metabolism of insect hormones; responsible for all ecdysone 20-monooxygenase activity during embryonic, larval and adult stages. May be involved in the breakdown of synthetic insecticides.
Miscellaneous:
MISCELLANEOUS: Member of the Halloween gene group.
Subcellular Localization:
Mitochondrion membrane.
Sequence:
MAVILLLALALVLGCYCALHRHKLADIYLRPLLKNTLLEDFYHAELIQPEAPKRRRRGIWDIPGPKRIPFLGTKWIFLLFFRRYKMTKLHEVYADLNRQYGDIVLEVMPSNVPIVHLYNRDDLEKVLKYPSKYPFRPPTEIIVMYRQSRPDRYASVGIVNEQGPMWQRLRSSLTSSITSPRVLQNFLPALNAVCDDFIELLRARRDPDTLVVPNFEELANLMGLEAVCTLMLGRRMGFLAIDTKQPQKISQLAAAVKQLFISQRDSYYGLGLWKYFPTKTYRDFARAEDLIYDVISEIIDHELEELKKSAACEDDEAAGLRSIFLNILELKDLDIRDKKSAIIDFIAAGIETLANTLLFVLSSVTGDPGAMPRILSEFCEYRDTNILQDALTNATYTKACIQESYRLRPTAFCLARILEEDMELSGYSLNAGTVVLCQNMIACHKDSNFQGAKQFTPERWIDPATENFTVNVDNASIVVPFGVGRRSCPGKRFVEMEVVLLLAKMVLAFDVSFVKPLETEFEFLLAPKTPLSLRLSDRVF
The following text describes a protein:
Function:
Probable component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs (Probable). Required for CBs formation. Binds snRNAs and non-specific artificial RNA via the N-terminal part of the NOD domain and via the NLS2 region (212-282) of the IDD domain. The two sites are able to function independently and provide effective RNA-binding in a non-cooperative manner.
Subcellular Localization:
Nucleus. Nucleus, Cajal body.
Domain:
Contains a N-terminal ordered domain (NOD) (1-117), central internal disordered domain (IDD) (118-349) and a C-terminal domain (CTD) (350-608) with an atypical Tudor domain containing probably two large unstructured loops.
Sequence:
MEEEKVRVRLVFEDRRILSKYQKKQGLTRSWVVLNRKCHRTISEFSDHIFHTFSLCEACPHGLSLSMEGFVLPPFESSCVLKDKDIVCVKKKKESLLEIVGEDSDENVYNAIEVEERPQIRPGEMLLANEEFQKETGGYESESEEDELEEEAEEFVPEKKASKKRKTSSKNQSTKRKKCKLDTTEESPDERENTAVVSNVVKKKKKKKSLDVQSANNDEQNNDSTKPMTKSKRSSQQEESKEHNDLCQLSAETKKTPSRSARRKKAKRQWLREKTKLEKEELLQTQLVVAPSQKPVITIDHQATKEKHCETLENQQAEEVSDGFGDEVVPVEVRPGHIRFKPLAGTDEASLDSEPLVENVLWNGNMTKKKGQKWGTEKSGFSKRYAQDFNEDATTQPAEAETLANCPIDYEQLVAYTGSVKKGDVIAYRLIELTSSWTPEVSSFRVGKISYYDPDSKMVTLMPVQEFPIEKKTEEDDDFCMQPDTSLYKEDGSLEIEFSALLDVRSVKTSSSDSAEVAKSALPEPDQSAKKPKLSANKELQTPAKENGEVSPWEELSEALSAKKAALSQANNGWNKKGSSSGGSWSYKALRGSAMGPVMNYLRSQKEI
The following text describes a protein:
Function:
Sugar transporter involved in the transport of CMP-sialic acid from the cytoplasm into the Golgi. May transport important nucleotide sugars such as CMP-Kdo (2-keto-3-deoxy-D-manno-octulosonic acid) in physiological conditions.
Subcellular Localization:
Golgi apparatus membrane. Membrane; Multi-pass membrane protein.
Sequence:
MQRNGVMECTACRSRLVVPSPRSVSRAYDKHHNKITSKFRALKFLLVVGDCMLVGLQPILVFMSKVDGKFQFSPISVNFLTEVAKVIFAIVMLIIQSRKQKVGEKPLLARSTLMQAARNNVLLAVPALLYAINNYLKFIMQLYFNPSTVKMLSNLKVLVIAVLLKFIMRRRFSVIQWEALALLLIGISINQLRTAPAGDTAFGLPITAIAYIYTLIFVTVPSLASVYNEYAMKSQDTSIYLQNLFLYGYGAIFNFLGILGTALFQGPENFNILQGHSRATMFLICNNAAQGILSSFFFKYADTILKKYSSTVATIFTGLASAAFLGHTLTINFLLGISVVFISMHQFFSPIAKVKDDKPGELLELQDTQNHRSSDSSFVNMTAGAADDASHQLGTDERQPLLPI
The following text describes a protein:
Function:
Inhibits the binding of prostaglandin F2-alpha (PGF2-alpha) to its specific FP receptor, by decreasing the receptor number rather than the affinity constant. Functional coupling with the prostaglandin F2-alpha receptor seems to occur. In myoblasts, associates with tetraspanins CD9 and CD81 to prevent myotube fusion during muscle regeneration.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein.
Sequence:
SGSIAPPRLSPLIVAALCRGRVVRVPKGSLVRVEGTELVIPCNVSDYDGPSEQNFDWSFSALGGSFVELASTWEAGFPAQLYRERLQRGDIVLRRTANDAVELHIKNIQPSDQGHYKCSTPSTDATVQGNYEDTVQVKVLPDALRVAAGPQPSPGPSLREGEPFELRCSASTASPLHTHLALLWEVRRGPARRSILSLTHEGRFRPGPGYEQRYRIGDVRLDTVGSDGYRLSVSQALSSDQGSYRCIVSEWIGEQGNWQEIQEKAVDVATVVIQPTVLQVTVARNVSVAEGKLLDLSCNITTDRVDDVRPEVTWYFSRTPDSTLPGPHVLARLDRDSLVHSSPHVALSHMDARSYHLLVRDVSRENAGYYFCHVALWTPGHNRTWHKVAEAMSAPAGVAVTWLEPDYQVYLNASKVPEFSDDLTELECRIVDMKSTEAGIRFTVSWYYRLNRRSDDVVASELLAVMNGDWTLKYGERSKQRAQDGDFIFSKEHADTFNFRIQRTTEEDRGNYYCVVSAWTRQRNDSWVKSKDVFSKPVNIFWASEDSVLVVKARQPKPFFAAGNTFEMTCKVSSKNIKSPRYSVLITAEKPVGDLSSPNETKYIISLDQDSVVKLENWTDASRVDGVVLEKVQEDEFRYRMYQTQVSDAGLYRCVVTAWSPIRGSLWREAATSLSNPIEIDFQTSGPVFNASVHSDTPSVIRGDLIKLFCIITVEGAALDPDDMAFDVSWFAVHSFGLDKAPVLLSSLDRKGIVNTAERDWKSGLSLERVSVLEFLLQVHGSEDQDFGNYYCSVTPWVKSPTGSWQKEAEIQSKPIFITVKMDVLNAFKYPLLIGVGLSTVIGLLSCLIGYCSSHWCCKKEVQETRRERRRLMSMEMD
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:
MSLAISFLLLILISPSKAVLNNAHYYDQTCPQAEKIIFETVRNASMHDPKVPARILGMFFHDCFIRAWISIIQRIDDAKAKLEMACPHTVSCADIIAIAARDVVAMSGEPSWNVLTGRKNGRVSKANDTITLPAPTFNAMQLIQSFAKRGLGVKDLVALSGDHNLGFSHCSSFEARLQNFSSVHDIDPSMNTRFAGNLKRKCPKPNKDHSAGEFLDSTSSTFDNDYYKRDIEGKGIFGSYHALLGDYREFAASMVKLGKVGVIKNGEVRFKCRVVN
The following text describes a protein:
Function:
It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids; Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis.
Sequence:
MAPSRKFFVGRNWKMNGRKKCLGELIGTQNAATVPADTKVICALATLPRLLWLRRTESRGWCGPGALRRRVFGESDELIGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVILAYDPVWAAGTGKTTATPQQAQEAHKKLRGWLKSNISDAVAQSTGIIYGGSVTKATCKELASQPDVAAFLMSGVSLKPEFVDIINAKQ
The following text describes a protein:
Function:
Responsible for addition of first and second mannose residues to the outer chain of core N-linked polysaccharides and to O-linked mannotriose. Implicated in late Golgi modifications.
Miscellaneous:
MISCELLANEOUS: Present with 11400 molecules/cell in log phase SD medium.
Subcellular Localization:
Golgi apparatus, cis-Golgi network. Note=Golgi localization depends on SVP26.
Sequence:
MLIRLKKRKILQVIVSAVVLILFFCSVHNDVSSSWLYGKKLRLPVLTRSNLKNNFYTTLVQAIVENKPADSSPDLSKLHGAEGCSFANNVAAHDSGHDSDLSYESLSKCYNLNKTVQESLREVHSKFTDTLSGKLNFSIPQREALFSGSEGIVTIGGGKYSVLAYTMIKKLRDTGTTLPIEVIIPPQDEGEDDFCKNWLPKFNGKCIYFSDIVPSKPLSDLKLTHFQLKVFGLIISSFKRIIFLDADNYAVKNLDLAFNTTSFNDTGLILWPDFWRRVTPPAFYNIIGSSINIGKRVRFVSDDISPVSRYDPFVSNSNDYTPKERQEHFLKHVPLHDLDGTMPDLSSESGQMVIDKIRHFNTLLLALYYNVYGPTWYYKMISQGTAGEGDKDTFVAAAHALNMPYYQVRTNFEFDGFFYQKDDYKGLALLQHDFEQDYKQYQKAQQKVKANIEEFSKLDPDYTLDNGFLKTLMVNDDGSDLDIMFIHASFYKADPWTLYHENRFIGPNGEQVRGFRKPHRYGMDFELFLFNDMRGSFCTTPKSQVIKFKYFTDKVNTPEWDAMCEYLTNHVNYLESTHKEAMGEKN
The following text describes a protein:
Function:
Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction; Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity.
Subcellular Localization:
Secreted.
Sequence:
MKLAFLCLCFISIAAAWPVSKSRQHAISASSEEKYDPRSHHTHRYHQDHVDSQSQEHLQQTQNDLASLQQTHYSSEENADVPEQPDFPDIPSKSQEAVDDDDDDDNDSNDTDESDEVVTDFPTEAPVTPFNRGDNAGRGDSVAYGFRAKAHVVKASKLRKAARKLIEDDATAEVGDSQLAGLWLPKESREQDSRELAQHQSVENDSRPRFDSPEVGGGDSKASAGVDSRESLASRSAVDTSNQTLESAEDAEDRHSIENNEVTR
The following text describes a protein:
Function:
Antimicrobial protein. Has antibacterial activity against the Gram-positive bacteria M.luteus (MIC=22.7 uM) and L.monocytogenes (MIC=90.9 uM). Lacks antibacterial activity against the Gram-positive bacteria B.circulans, S.aureus, and S.lutea, and the Gram-negative bacteria E.coli D31, E.coli ATCC 25922, and S.typhimurium. Has antifungal activity against A.niger (MIC=90.9 uM) and T.harzianum (MIC=90.9 uM), but lacks antifungal activity against S.cerevisiae, P.pastoris, Z.marxianus, C.albicans, C.fructus, and F.oxysporum.
Subcellular Localization:
Secreted.
Sequence:
EADEPLWLYKGDNIERAPTTADHPILPSIIDDVKLDPNRRYA
The following text describes a protein:
Function:
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Subcellular Localization:
Cytoplasm.
Sequence:
MIISAYIMPLRLPKPGLRNIDGHLLYLEHAGPHMATLQIVNNVLSSEMTSAGQLVETVDLELFGKSLFIEHIIMITLYDEYIYHETLVHPTLLSLENPEKVLIIGGGDGGALREVLKHPVGEVTLVELDKSVIETVKKHIPEVPGGSFEDPRLKLIIGDGRKYVESCEEKYDAVILDLTDPYGQAVRLYTKEFYSMVRKLIRDGGLMVTHSEGVHVNRVTFQRIYRAIRETFKRHAVAKAYVPSFNDEWSFSFGSDYLVPPELDREKLERRFNERLKGKTRFYLPEIHYALFSLPAYLKAALEEEVPPSTDDNPAEIYEES
The following text describes a protein:
Function:
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit of the SDH catalytic dimer.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MFRSILKLNRNSLNSIRLFSSSTNGGKFTISSNVDKIPNNEISNVEKLRKKLLYQSKERGMLENDLLLGSFATNNIQKLTEQQLKDYDLLLQQPDPDIFNWILNKTVIPDEFETEVLKMIQHHCQNDPLGYTRK
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:
MEDNHVSEHPPESTTPASHLFDSIDSEGGAADDPFAQFGSEQDDYAPQRQVQEEEHKPGFQATTEGEAPTPVAQVEGSRTPIPANVLEKQTEEKAAYAPEETEEVQGGGKTQEFIGEQQGSHITSSPVQEPTAGHLFGPVSDGSGEDLFAQLAESEKDEFTQPEQSQDILKSEGIDQSEAQGQTEVSVPHEEKDYSDLLAEFEAENGMLEPPIGGPVKSHSESKGEGIQSLLGQSDTKNDQTPAASSLFIDDPNDSVFDNIIPESDSEPQEAPLSTTAGTLTNPSIQGLFSNDTTDFLNQGQIITEAQEAGGLDQSGVEPLDFDIPQGWYDDDGQWQWYTEEEKEQVKFAMMGPTSWQETEQAPPPLTAGAGATLTPVVPRSPALQSQAAMSENAARRTPQPEPIAAFDSSIYEPPVPASTQLATSTASYFPANQSGYTSAPPANVPPQVTRSATLPASSFSVTAAAPSPHVSSNPKSYNAYDPPVSTKPYHHRSYAPATQPTPSPYNPASLGNVFTSPTDATLAKSEPPKPRPQPQRAVSTAYDPPFLRTQEKISRPASAVSTGVSSAFGVSPIVPSHQIQAPPLPPSGPPKRSKGESRPPSRGPAFAPPPITPFGSPPPVPPLSVPPSGPPRRPTGTSRPPSRGPAYAPHPKPQSSVPPVPPLPTLPVEVPGSHTEDNSVAHGRDSLNFPGSSEVNEPSFTRPNVCSPEGGDEDRPPSRGSQAISPSLAPHTLSVSAEPIQAPPSAPPGQSIGTTELRGHNQTSAPSPMTHIPASSLSEKPTSYAPPEFQQKAQQPQPSSYEQVPYTHDGWEADRSLISAQLSSYEPTPHAPSDSHSDHEAETFKAIASAPAAESYEPSSYAPTQSDYYKPGPEATTQPTSYKPDPYAPSSTSAVGLQSQSSPYARTTSPAHSSAYGTSPPTNHIPSMAASGNTFVHAPYAGQSAYQSQNESSVRQSNLSMNRSSMPSSTSLYVPSQSSSNYNPVGSPAQSPTYGMSPPSTNYFQSMPAQRSASIDTSYVPQQVLEQKPISEDPLARTTLASRNAPIAVFGFGGVLITAFPGASESDNFAKGHARIPSYGYASGRGQLWIRNISEVVAPGALKSDQSAFPGPLVNDISGPKGAAGEKKKKEAVLAYLRDRAEEVERGLPYLKSSASRARREDEGRLVLLRLLEALVIGEGKLAGNPKVEDAIRVALSNPSSPNVPTAPGHVTTLSNGLYPSTSSKSASPVAANPSQLSRLSTLLAQGQKKEAAEYAIDHGLWSHALVISSAVGAELWKDTVMRFTAAELSARSEGTAGIRASYALIGGMSHSSLDDLINAATITEDPSQDQWREVISSVLFHAKPADLACLDELGSRFLQMGLVNAAHACFLLSPLSPFLDTTPASYERGIMMTHNTRDEESTIFVEIAEYARSLVPVPKGQEQITVGLPQLLPYKLARAWRLAELGEVALAKRYCAAIEAGAKPLTKSAQIQSLLPPAFMASLEDLLERLTGTPSIDPANVLGGGRKSSKPGFDKLGSWIEGRLTKFIAGEEGEKAIPKPAASSGKAEGPFAHFSSVSPDPSGSISRNPSMADVGSYSASNGFLGVQPMSRTTSPAVQGQYNPYGQQSQPYGAPPKSTLDVRSLSPATSHSAQAHNNLYTSQSQPSSSTSSSYGDSQGRRTDFGGGFTPWASNAGSEVQAEDGEMTPHAYEAPVGDDQAEFITPMAGLSIGPSTSGTLNYTPRASQPAYDLGDEGEDLGFGNTSLSKGRPTKTVGEGEGKGEASGGKPTKGGKEEPKKEEPTQPAKQEQHQSSSWLGRLWGKKEGGPVKANLGEETSMVYDPDQKRWVVKGAKGASAAPAAPPPPPRAQTASPSHTSRPAPSTRAMSAAPPPPGPSSSDGSFSTLPRSANVPPPPAGMSASTFAEGPDGGIRRMKSSLTMSQGQGPPSGPLSGPPSGPPSQPPSRTSSASATSASLDDLLSGSRPASKRPGSAMKKGARNRYVDVFQSEGS
The following text describes a protein:
Function:
In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape.
Subcellular Localization:
Nucleus.
Sequence:
MVNALKGILIECDIPMKQFIVSINDQLPNAQKFIIYDLDDTHLFVQPHVADMLQNKVKDFLDKITYEKPA
The following text describes a protein:
Function:
Copper amine oxidase that can use putrescine and spermidine as substrates.
Subcellular Localization:
Secreted, extracellular space, apoplast.
Sequence:
MVELSFSQLLVLLLSLLFLFTTLASSSKTPRFKYSLEKPHHPLDPLTTPEIKRVQTILSGHDPGFGSGSTIIHAMALDEPDKQRVIRWKKGDRLPPRRAEILAMSNGESHVLTVDLKSGRVVSDLVNPTFGYPILTMKDIIAVSQVPYKSVEFNRSIEARGIPFSGLICITPFAGWYGPDEEGRRVIKIQCFSKQDTVNFYMRPIEGLYLTVDMDKLEIIKIVDNGPVPVPKSTGTEYRYGFLNETVYMDRVNPMSMEQPDGPSFQVEDGYLVKWANWKFHIKPDQRAGMIISQATVRDSKTGEARSVMYKGFASELFVPNMDPGEGWYSKAYMDAGEFGLGPSSMPLVPLNDCPRNAYYIDGFFASPEGIPILQPNMICLFERYAGDTSWRHSEILLPGVDIRESRAKVTLVARMACSVGNYDYIFDWEFQMDGVIRVTVAASGMLMVKGTAYENVEDLGEKEDDSGPLISENVIGVVHDHFISFHLDMDIDGSANNSFVKVHLEKQRLPPGESRRKSYLKVKKYVAKTEKDAQIKMSLYDPYEFHLVNPNRLSRLGNPAGYKLVPGGNAASLLDHDDPPQMRGAFTNNQIWVTRYNRSEQWAGGLLMYQSRGEDTLQVWSDRDRSIENKDIVLWYTLGFHHVPCQEDFPVMPTIASSFELKPVNFFESNPVLGISPFFEKDLPVC
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein; Matrix side.
Sequence:
MYGGKSPQELLSGSFTKSWLHDKWAPLVGSVFGFIGACYVNYGTGRPALSGIQKHIAAALAVGAVATMADKWRDAHFAEKDATFRHYIQLHPEDFPTPERKKYADVLEYWQPIR
The following text describes a protein:
Function:
Transcriptional activator that may participate in the regulation of mRNA splicing.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MKILAMDERREELSAKSTVQNVKISEAPILDGKVNNEDSHMEIDQPEGSMEEDDHRQVKEKNTSENSVEQKRGRRMFGALLGTLGKFQQESEREQKSARKVKRAELEEKLAKRREQELQELEKQEKIEAEILESRLQEQRKVALDELELDRNDLKKVLDNKKSYYLRTKTQPSLFYRPYYLLPSQRTQLEQMKSEAP
The following text describes a protein:
Function:
Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Also plays a role in the assembly of the exocyst (By similarity).
Subcellular Localization:
Bud. Bud neck.
Sequence:
MPSIDVDEADILILSDGLKQVNELTREITGSLSKITSTTSKSSKLFAPIIETNTRLNVLKRNIESSFDSVSSIKDLASDASKYEIILEQEITQVGLRKFIKTLHKVDDIMDDLREKSKSTADFRGIVTHLEELTMIGEKNLQIYFANKLNQIQPFDPQVYMNKKQNFPYYYDEDLNDIAAILDYFGDTEQNPVTEIFMKQQGQLVLNSLAFLEPFTKQITSESNVPYQRGSSGFNSYTEAFITFVSGVSVLIDDVFVKLPDRRPAVFCKIVAPILHNYTKILRYNIDLVKDDINNYGLFSFELSENINRVHQLFKGKPLQNNEQLLECEAELKSISESLFKDLIQYIGQKTASLAQLPTDNGVTEATVDVMSRLRKFSEYKSGCLATIQSMTRESWLPNESKNVWTISMTPKNAQQLLSCFFSDAIDYLTISLERKAQKILNPNLEPEVGAPHKRIPQMQRIGFFVLTNITLIEQIVQRSEINTVLEDIGAARLVKLNARYVNYFASDWRDLASNLLDQVFVDSSGKISSKDKDQVKEKFRKFNEGFEQLVSNYKTCRITDPAMKKLLKQEIFALVAPMYERFHNRYKDSFKNPRKHIKYTPNELMNILNSLGR
The following text describes a protein:
Function:
Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
Sequence:
MIPYYYGSIIIGPSGVGKSTLCKGLLQMMEQIQRKSIIINMDPANEDSYEDYLCINILELITVEDVMKMFKLGPNAALLYCFQFLLDNIKWLFDKLLKYQDHYLIFDFPGQIELYLANDSIYNLIQSLTNKNNSTLQISLVAVQLFDCLNCYQVNTFISASLVSVTVSANLSLPYLAVLNKLDLVKQYGEMPLSLQYYLEGENLKYMLEVTDQCDEEGQKFKEKYGQLTYHIAELIDSKEVVSFEPLYVENKKLIMRLILKMDKANGYYFLENLPPIYKSIQEDVGEEIDFLPTELVMELETELFESN
The following text describes a protein:
Function:
Functions in trans to edit the amino acid moiety from mischarged charged Ser-tRNA(Ala). Has little activity against Gly-tRNA(Ala).
Subcellular Localization:
Cytoplasm.
Sequence:
MYSIEVRTHSALHVVKGAVVKVLGSEAKWTYSTYVKGNKGVLIVKFDRKPSDEEIREIERLANEKVKENAPIKIYELPREEAEKMFGEDMYDLFPVPEDVRILKVVVIEDWNVNACNKEHTKTTGEIGPIKIRKVRFRKSKGLLEIHFELLELENPS
The following text describes a protein:
Function:
Incorporated into fibronectin-containing matrix fibers. Plays a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Important for certain developmental processes and contributes to the supramolecular organization of ECM architecture, in particular to those of basement membranes; [Isoform a]: Involved in regulating the shape and adhesion of cells in the developing pharynx, intestine, body-wall muscle and gonadal tissue. During gonadogenesis, regulates the width of gonads and the migration of distal tip cells (DTC). Together with type IV collagen let-2 and downstream of metalloprotease mig-17, recruits nidogen nid-1 to the gonad basement membrane thereby inducing basement membrane remodeling required for the directional migration of DTCs. Acts antagonistically with metalloprotease gon-1 to maintain optimal levels of type IV collagen emb-9 in the gonad basement membrane during gonadogenesis. Required for larval development; [Isoform c]: Involved in the assembly of the flexible hemicentin-containing tracks found joining the pharynx and body-wall-muscle basement membranes.
Miscellaneous:
MISCELLANEOUS: Although involved in the same pathway as gon-1 and mig-17, it is probably not cleaved by these metalloproteases.
Subcellular Localization:
[Isoform a]: Secreted, extracellular space, extracellular matrix, basement membrane.
Sequence:
MRICFLLLAFLVAETFANELTRCCAGGTRHFKNSNTCSSIKSEGTSMTCQRAASICCLRSLLDNACDSGTDIAKEEESCPSNINILGGGLKKECCDCCLLAKDLLNRNEPCVAPVGFSAGCLRSFNKCCNGDIEITHASEIITGRPLNDPHVLHLGDRCASSHCEHLCHDRGGEKVECSCRSGFDLAPDGMACVDRNECLTRQSPCTQSEDCVNTIGGYICQRRISRLVPHRHRANRIGNAPRRMRDDPYSRAGEYREASQANTEFGCPMGWLFQHGHCVDVDECNLGSHDCGPLYQCRNTQGSYRCDAKKCGDGELQNPMTGECTSITCPNGYYPKNGMCNDIDECVTGHNCGAGEECVNTPGSFRCQQKGNLCAHGYEVNGATGFCEDVNECQQGVCGSMECINLPGTYKCKCGPGYEFNDAKKRCEDVDECIKFAGHVCDLSAECINTIGSFECKCKPGFQLASDGRRCEDVNECTTGIAACEQKCVNIPGSYQCICDRGFALGPDGTKCEDIDECSIWAGSGNDLCMGGCINTKGSYLCQCPPGYKIQPDGRTCVDVDECAMGECAGSDKVCVNTLGSFKCHSIDCPTNYIHDSLNKNQIADGYSCIKVCSTEDTECLGNHTREVLYQFRAVPSLKTIISPIEVSRIVTHMGVPFSVDYNLDYVGQRHFRIVQERNIGIVQLVKPISGPTVETIKVNIHTKSRTGVILAFNEAIIEISVSKYPF
The following text describes a protein:
Function:
Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate (By similarity).
Sequence:
MSSSEEDDGYVPFSKRPEWSDVKPLAQDDGPHPICPILYSEVFKDKMNYFRAILKSKEKSLRVLDLLEEVIQENPSNYTIWYYRREVLKAIEQDETIEYDIQQEMNLLNDMGETDPKNYQIWNHRRFIVEKYIGSDNKEKEFLSGVLLEDAKNYHAWSHRQWLLKTYRDWNGELAMVDKLLSLDHRNNSVWNHRFFVISNLNPSPFPLSLIEREVEFAFNHIRHSPNNESPWSYLKGLFKGQKISTIYPSLLDILLEMKSKYIGCSHVNSIILDIYQEQNTKISLENSLNICKLLSETIDPIHKNYWNFKYNTISDQLKLIN
The following text describes a protein:
Function:
Serine protease inhibitor. Inhibits trypsin.
Subcellular Localization:
Secreted.
Domain:
Avian ovomucoid consists of three homologous, tandem Kazal family inhibitory domains.
Sequence:
MAMAGVFVLFSFVLCGFLPDAAFGAEVDCSRFPNATDKEGKDVLVCNKDLRPICGTDGVTYTNDCLLCAYSIEFGTNISKEHDGECKETVPMNCSSYANTTSEDGKVMVLCNRAFNPVCGTDGVTYDNECLLCAHKVEQGASVDKRHDGGCRKELAAVSVDCSEYPKPDCTAEDRPLCGSDNKTYGNKCNFCNAVVESNGTLTLSHFGKC