lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
Sequence:
MWVFGYGSLIWKVDFPYVEKLVGYIMCYSRRFWQGSTDHRGVPGKGCVWGVAYRLPEGKEEEVKAYLDFREKGGYRTSTVVFYPKDPSIQPFNVLLYIGTCDNPNYLGPAPLEDIAEQILNAVGPSGRNTEYLFELANSLRNLVPEDADEHLFSLEKLVRQLSEAHRNLNHL
The following text describes a protein:
Function:
Microtubule-binding centrosomal protein required for centriole cohesion, independently of the centrosome-associated protein/CEP250 and rootletin/CROCC linker. In interphase, required for anchoring microtubule at the mother centriole subdistal appendages and for centrosome positioning. During mitosis, may be involved in spindle assembly and chromatin alignment by regulating the organization of spindle microtubules into a symmetrical structure. Plays a non-essential role in ciliogenesis.
Miscellaneous:
MISCELLANEOUS: The N-terminal 3D structure (head domain) resembles that of NHEJ1/XLF, PAXX, SASS6 and XRCC4.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Cytoplasm, cytoskeleton, cilium basal body. Note=Localization at the centriolar satellite is dependent on intact microtubule network. Localizes at the centriole subdistal appendages and proximal ends. Localized to centrosomal/satellite-like structures with the onset of centrosome separation in early G2.
Domain:
The coiled-coil domains are involved in microtubule-binding.
Sequence:
MEQPAGLQVDYMFRGVEHAVRVVVSGQVLELEVEDRMTADQWRGEFDANFIEDLTHKTGNFKQFSIFCNMLESALTQSSESVTLDLLTYTDLESLRSRKLGGRPGPCPRSAQLNSKRYLILIYSVEFDRIHYPLPLPYQGKPDPVVLQGIIRSLKEELGHLRGMNGGQDARETEIWHLREQVTRLASEKRELEAQLGRSREEALAGRAARQEAESLRGLVRGLELELRQERGLGGRAAGRRSQDCRRLAKELEEVKASERNLRARLKTLNCELAMYRRGRRTLPAGAREDRALSSRERSTSRGRTATRSSSRESNRGARSHGRPAHPSPSPTGSRVPRFDPTAFVKAKEKKQREIRMKRQQQQQQQRNRMGSGGSGDGPSVSWSHQTRPPAAVTGRGDAANRSRNRSSSVDSFRSRCSSVSSCSELEDFSQSVSKSRRCRGRGKPPSPIPWSGSKTKSTTRERNNHQRHLASSGAWVPIKEYSSDYQGADMAEIDARLKALQEYMNRLDTRS
The following text describes a protein:
Function:
Involved in the anabolism of D-lysine and D-arginine. Under aerobic conditions, the arginine succinyltransferase (AST) and arginine transaminase (ATA) pathways are 2 major routes for L-arginine utilization as the sole source of carbon and nitrogen. The D-to-L racemization of arginine by DauA and DauB is necessary, before to be channeled into the AST and/or ATA pathways. DauB catalyzes the synthesis of L-arginine from 2-ketoarginine (2-KA) and ammonium.
Sequence:
MSAATPLIVQQAEAEQLLARIDVLQAMRQLFLDLAAGQALQPAQQLVEFPAGRGDFINYLGVLAQEQVYGVKTSPYIVREQGPLVTAWTLLMSMQTGQPLLLCDAARLTTARTAATTAVAVDALAPAEACRLALIGSGPVAHAHLQYVKGLRDWQGVRVHSPCLDERRLQSLRAIDPRAEAAGSLEEALDEADVILLCTSSARAVIDPRQLKRPALVTSISTNAPRAHEVPAESLAAMDVYCDYRHTTPGSAGEMLIAAEQHGWSPEAIRGDLAELLSAQAPRPEYRRPAFFRSIGLGLEDVALANALYRLRQAG
The following text describes a protein:
Function:
Dictates male development. Probably plays a direct role in cell signaling during C.elegans sex determination. Inhibits the function of tra-2a.
Miscellaneous:
MISCELLANEOUS: [Isoform Long]: Active; MISCELLANEOUS: [Isoform Short]: Inactive.
Subcellular Localization:
Secreted.
Sequence:
MRYLPIFVFLGSFGYTETTLTKELIKDAAEKCCTRNRQECCIEIMKFGTPIRCGYDRDPKLPGYVYKCLQNVLFAKEPKKKINLDDSVCCSVFGNDQNDSGRRCENRCKNLMTSPSIDAATRLDSIKSCSLLDNVLYKCFEKCRSLRKDGIKIEVLQFEEYCNATFIQKRTFRGV
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; Peripheral membrane protein. Mitochondrion intermembrane space.
Sequence:
MASGFGYSGGRTRCFPFWQEFSKCYANAEKPSDCVAPKDDYMECLHNTKEIARAKQVKSHFVQKELQESHDSRKAAEKAATGVIVSLGLVEEEGK
The following text describes a protein:
Function:
Transcription factor involved in the regulation of gene (e.g. drought-regulated and flavonoid biosynthetic genes) expression and stomatal movements leading to negative regulation of responses to drought and responses to other physiological stimuli (e.g. light). Promotes guard cell deflation in response to water deficit. Triggers root growth upon osmotic stress (e.g. mannitol containing medium).
Subcellular Localization:
[Isoform 1]: Nucleus; [Isoform 2]: Nucleus.
Sequence:
MGRPPCCDKIGIKKGPWTPEEDIILVSYIQEHGPGNWRSVPTNTGLLRCSKSCRLRWTNYLRPGIKRGNFTPHEEGMIIHLQALLGNKWASIASYLPQRTDNDIKNYWNTHLKKKLNKSDSDERSRSENIALQTSSTRNTINHRSTYASSTENISRLLEGWMRASPKSSTSTTFLEHKMQNRTNNFIDHHSDQFPYEQLQGSWEEGHSKGINGDDDQGIKNSENNNGDDVHHEDGDHEDDDDHNATPPLTFIEKWLLEETSTTGGQMEEMSHLMELSNML
The following text describes a protein:
Function:
Circadian regulator that acts as a transcription factor and generates a rhythmic output with a period of about 24 hours. Oscillates in antiphase to the cycling observed for period (PER) and timeless (TIM). According to PubMed:9742131, reaches peak abundance within several hours of the dark-light transition at ZT0 (zeitgeber 0), whereas PubMed:9616122 describes bimodal oscillating expression with maximum at ZT5 and ZT23. Clock-cycle heterodimers activate cycling transcription of PER and TIM by binding to the E-box (5'-CACGTG-3') present in their promoters. Once induced, Period and Timeless block Clock's ability to transactivate their promoters.
Subcellular Localization:
Nucleus.
Domain:
Contains three polyglutamine repeats which could correspond to the transactivation domain. The length of the repeats is polymorphic. In the arrhythmic mutant JRK, deletion of this region leads to the loss of circadian rhythmicity and altered light response.
Sequence:
MDDESDDKDDTKSFLCRKSRNLSEKKRRDQFNSLVNDLSALISTSSRKMDKSTVLKSTIAFLKNHNEATDRSKVFEIQQDWKPAFLSNDEYTHLMLESLDGFMMVFSSMGSIFYASESITSQLGYLPQDLYNMTIYDLAYEMDHEALLNIFMNPTPVIEPRQTDISSSNQITFYTHLRRGGMEKVDANAYELVKFVGYFRNDTNTSTGSSSEVSNGSNGQPAVLPRIFQQNPNAEVDKKLVFVGTGRVQNPQLIREMSIIDPTSNEFTSKHSMEWKFLFLDHRAPPIIGYMPFEVLGTSGYDYYHFDDLDSIVACHEELRQTGEGKSCYYRFLTKGQQWIWLQTDYYVSYHQFNSKPDYVVCTHKVVSYAEVLKDSRKEGQKSGNSNSITNNGSSKVIASTGTSSKSASATTTLRDFELSSQNLDSTLLGNSLASLGTETAATSPAVDSSPMWSASAVQPSGSCQINPLKTSRPASSYGNISSTGISPKAKRKCYFYNNRGNDSDSTSMSTDSVTSRQSMMTHVSSQSQRQRSHHREHHRENHHNQSHHHMQQQQQHQNQQQQHQQHQQLQQQLQHTVGTPKMVPLLPIASTQIMAGNACQFPQPAYPLASPQLVAPTFLEPPQYLTAIPMQPVIAPFPVAPVLSPLPVQSQTDMLPDTVVMTPTQSQLQDQLQRKHDELQKLILQQQNELRIVSEQLLLSRYTYLQPMMSMGFAPGNMTAAAVGNLGASGQRGLNFTGSNAVQPQFNQYGFALNSEQMLNQQDQQMMMQQQQNLHTQHQHNLQQQHQSHSQLQQHTQQQHQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQLQLQQQNDILLREDIDDIDAFLNLSPLHSLGSQSTINPFNSSSNNNNQSYNGGSNLNNGNQNNNNRSSNPPQNNNEDSLLSCMQMATESSPSINFHMGISDDGSETQSEDNKMMHTSGSNLVQQQQQQQQQQQILQQHQQQSNSFFSSNPFLNSQNQNQNQLPNDLEILPYQMSQEQSQNLFNSPHTAPGSSQ
The following text describes a protein:
Function:
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. In fact, can act as a protease that specifically degrades TsaD in vitro; therefore TsaB may post-translationally regulate cellular pools of TsaD via proteolytic degradation. Does not show sialoglycoprotease activity against glycophorin A.
Miscellaneous:
MISCELLANEOUS: TsaBCDE are necessary and sufficient for tRNA(NNU) t(6)A37 threonylcarbamoyladenosine modification in vitro in E.coli.
Subcellular Localization:
Cytoplasm.
Sequence:
MRILAIDTATEACSVALWNDGTVNAHFELCPREHTQRILPMVQDILTTSGTSLTDINALAYGRGPGSFTGVRIGIGIAQGLALGAELPMIGVSTLMTMAQGAWRKNGATRVLAAIDARMGEVYWAEYQRDENGIWHGEETEAVLKPEIVHERMQQLSGEWVTVGTGWQAWPDLGKESGLVLRDGEVLLPAAEDMLPIACQMFAEGKTVAVEHAEPVYLRNNVAWKKLPGKE
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MADILTQLQTCLDQLATQFYATIGYLSTYHDNSPAIPPPDVPDAAPALAKIPKNSTAPPVPAGAPVPALSQASPPAQNPAHGAAGAGTSVGEGAQTPGPAAGAGADPNLPAPDSPRTFASRQRELARDLIIKEQQIEYLISVLPGIDSSEAEQEKRIRELEGELRQVEEERELKMRELKRLRRTLENVLTAVETGLYGDRELLEKYA
The following text describes a protein:
Function:
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Sequence:
QIMMEQTQRRKQEIENRLSEEKKRSEMIKASLEKADQLTNSMVTILNQFDERLHKLEDTILPVHRKTKDLQRLQDNIEKTLSSLDHVISYHHVAHDVEPIVRQGPSRQVDKYLSCMERLVQAVNFFSENNPDSPELNTVNTLFTNGKDGLEKEFQAHLSRHTKPMPPQKVVEMIKAENMFLTAESYTNLPEKTMSDLSQMAEWLSGAGKSQSFVNVYSDIRSNNLIKTLNGLSDHIKGNNLNTGRKISVAVTTPKKPGNRRASNFRKPSTLLRKESLQSLSSMGGITIEMITSLIICDKVGVVDGCFINCDEIQPFQPNYIQHATRPKHSHIAMENAGLGKSSHAPIAEEEIIEIEIEPFVAMVSACAKLFVVEQSMIQSVIPEKNRRQVFDSIITESLKSVEQAGNKIVEYAKQCITRHDHPSIVNVFPAIKHLKTTLPSYQAVLKGVSEMNRLRMPRLIGELETVGVKVLEDFSDCVKSDPEKESNMPKDGTVHELTSNTMLFMQQLADNVEIVGGMLASKFESQQSMEKIRSCLADYISQVLGALKLNLENKSRVYENLSLAAVFLLNNYHFIITALNRHNLLGLAEIATPGIENLYRGFIDHQKQAYLQCWNKFDNYLKNKNKGVEIQAQPGGKLKDKDKLIVKDKFKTFNNDFDDLVKTHQQWAMPSSEVRKEIRNSVKTKLVQPYAELHEKYRMVQFTKNIEKYLKYTPESVAENIDRMFGQNAS
The following text describes a protein:
Function:
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body.
Subcellular Localization:
Nucleus.
Sequence:
MTDAVFQAPKRRARVYECFEAALPVPLNSADDGDHTLLCRAEIIGHHVSVTDPAHIQQLYHRGYFGKGVFSRSRPEHMISPQWKYVGDRCLPVISLSEYQKRLSLARAALVMQDLEEESVNKALQILTEPVEFNTEEQQEPISKSNCDESLMDQTMDTDLIPDQTESAKPQRQGNPLYDPLAEIYPEKLDQSLKADEKCRDHNDWISQCGCRANEERMNRTMHKSQTYEYVLVEESEDERSQHITQENSSTDQPAELVCRINPFPMLEYLQLSYEEAFFLVYALGCLSIYYNGEALSVAQLWTMFRSLQPNFCFSYAAYHYYRSKGWVPKSGVKYGTDLMLYRKGPPFYHASYSVVVDTVDASFRRSSLRPFSWRSLATLSRTTGNVSKELMLCFIITPSDVTGDLLVSPQCLKRFSVQEVLMSRWVSSKERTEQEEI
The following text describes a protein:
Function:
Probable E3 ubiquitin-protein ligase involved in either protein trafficking or in the distribution of cellular structures. Required for spermatozoon maturation and fertility, and for the removal of the cytoplasmic droplet of the spermatozoon. E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer it to targeted substrates.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MLCWGNASFGQLGLGGIDEEIVLEPRKSDFFINKKVRDVGCGLRHTVFVLHDGTVYTCGCNDLGQLGHEKSRKKPEQVVALDAQNIVAVSCGEAHTLALNDKGQVYAWGLDSDGQLGLLGSEECIRVPRNIKSLSDIQIVQVACGYYHSLALSKASEVFCWGQNKYGQLGLGIDYKKQASPQLIKSLLGIPFMQVAAGGAHSFVLTLSGAIFGWGRNKFGQLGLNDENDRYFPNLLKSLRTQKIVYICCGEDHTAALTKEGGVFTFGAGGYGQLGHNSTSHEINPRKVFELMGSIVTQIACGRQHTSAFVPSSGRIYSFGLGGNGQLGTGSTSNRKSPFTVKGNWFPYNGQCPTDIDSEEYFCVKRIFSGGDQSFAHYSNPQNCRPPDDFRCTDPSKQIWTVNEALIQKWLSYPSGRVPVEIANNDDHYKTGAKFSGVDMNAARLLFHKLIQPDHPQISQQVAASLEKNLIPKLTGSLPDVEALRFYLTLPECPLMNDPNNFITIAIPFGRALVNLEKAPLKVLEKWWSVLEPPLFLKIVELFKEVVVHLLKEYKRSIASPERRIFNSFLHTALKVLEILHRVNEKSGQIIQYDKFYIHEVQELIDIRNDYINWVQQQAYGMLADIPVTICTYPFVFDAQAKTTLLQTDAVLQMQMAIDQAHRQNVSSLFLPVIESVNPCLILVVRRENIVGDAMEVLRKTKNIDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDSRLIWFSDKTFEDSDLFHLIGVICGLAIYNFTIVDLHFPLALYKKLLKKKPSLDDLKELVPDVGRSMQQLLDYPEDDVEETFCLNFTITVENFGATEVKELIVNGADTAVNKQNRKEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLQLFQPNELQAMVIGNTNYDWKELEQNTEYKGEYWAEHPTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSLKLAIQSTGGGEEYLPVSHTCFNLLDLPKYTEKETLRSKLIQAIDHNEGFSLI
The following text describes a protein:
Function:
Inhibits host transcriptional machinery, by producing modifications to the phosphorylation state of the C-terminal domain (CTD) of RNA polymerase II. Inhibits phosphorylation at serine 2 in the heptapeptide repeat (YSPTSPS) of the CTD of RNA polymerase II, suggesting that the elongation step of transcription and/or 3'-end processing is prevented. Inhibition of host transcription machinery leads to shut off of host cell protein synthesis and inhibition of the host innate immune response. NSs also seems to be involved in the nuclear relocalization of host PABP1 (By similarity).
Miscellaneous:
MISCELLANEOUS: [Isoform NSS]: Produced by alternative initiation in the N gene, but encoded on another frame.
Sequence:
MMSHQQVQMDLILMQGIWTSVLKMQNHSTLLQLGSSSSMPQRPRLLSRVSQRGRLTLNLESGRWRLSIIIFLETGTTQLVTTILPSTDYLGI
The following text describes a protein:
Function:
Component of the exocyst complex.
Sequence:
IQLLEDIPEDAHDPTDIGTWIQRADLQMLQLFGKELVALIDRSIQEINREHGQARGASEMRRLLKLAVVITMLPTSPDLLPVILRLYATLGTFPIDQLNGITKELRKCVRKILRRVCSLSQTQSGLYHVAQRGGVHKITLYVMNYVKFLWEHDSVINNIIAYQADGESENGEEWTQVDSFVQHFIGRLDALLERMARHESMMGLECISLLNNAHFILNRLRKLEVKSALQQDWILRYENQVKHQITRYLELSWLPVMSCLDAHTPTQALFPCFHLPLTTRFYEMLESTCAEQQNWRIEDPKLRNNVRKAVSSHVVQCYQAHLQKKGMKLHKYIPQEIENKLMELFEG
The following text describes a protein:
Function:
Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. Functions cell autonomously to regulate wing cell hair polarity and number.
Subcellular Localization:
Cell membrane. Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MLLSETHFWTTLREDVVRIKSQDLGAFRYLRQRDKEQEQQDLACLAKRDYTERRNGLAVLKNSGRKSTGRLKDNLKKLEDLLRQHRIIHSEWQDAAQVLLLFSHGLIAHICVDIYTGDILRMVFEKYLVGKLASEVITDAFFTRSHIVLAYNTNQLTVVHLQRPNARSQGPEKIANMDPRIFHVIIPGATERKLSRHLTVNASFDLFVVWTQSSQNEVYPWRPTIRDQDRANIHVFKIKGLQLESIAYCWSENDPLCVDFLRSSESQIITLEQKVSRKGDISAEICSYELAAGKMQRTAITSIPMGAQICSFAFSPDQEKLFLGSVDRNICLHDLVQQSTKYANQIEIVPNQCAWHCDSAMLCVANERSVLQCFDLALATIGHQLVSENVTPSSLLDLSHYFVAQPTLLSVAFSRKPDLSTFKHTYAQTDCLLLLVYEQGPLACMRIFGGTGMRGDIHNSGLTADVIADKYLRLQQPDRAVNVLAALNWETYGAMCLITLHKIANYVFFGGDQRRPRIELMARALKTFAHTLSEETKDEFSDQVYDLKRRFCFYLLRKNLFAEAFEIAQDVADYDIFMDLYNLTKCISSLSEFAQVAFSQAAAIIHEEDRANGNLSLTCDLRSESACSLSTCSDMLRGQGAGTAPETGLGASQPQSQQVLKNYVPPLPSFKSKVFNAEMIKINIPKPELRPPLPKVSIAPPTSSLASLTLKSNSSLQQAPAKSLHPNGNLWSQDVPDQTVGLPMASSPLPRLPPSNIPDQSAQLGQFSTMPASPPPTGSYQPKFYQHPLVSGNIPAMLPSLTSEDYQKRLLQKKPTASILSNPANPAPTNGEAPATPAKSQTAEKNKVKFSDTIQVAVVPEIPRKEKPMPPKRNGYSRPAARHLTNPKKELADSLPLCHPNDEYLKDFNPITTNVTKPPIRRREEEPKSSSKGGNSSSSSSSIKVVHFGVV
The following text describes a protein:
Function:
Has ADP-ribosyltransferase activity toward GLP1R.
Subcellular Localization:
Sarcoplasmic reticulum membrane; Lipid-anchor, GPI-anchor.
Sequence:
MQMPAMMSLLLVSVGLMEALQAQSHPITRRDLFSQEIQLDMALASFDDQYAGCAAAMTAALPDLNHTEFQANQVYADSWTLASSQWQERQARWPEWSLSPTRPSPPPLGFRDEHGVALLAYTANSPLHKEFNAAVREAGRSRAHYLHHFSFKTLHFLLTEALQLLGSGQRPPRCHQVFRGVHGLRFRPAGPRATVRLGGFASASLKHVAAQQFGEDTFFGIWTCLGAPIKGYSFFPGEEEVLIPPFETFQVINASRLAQGPARIYLRALGKHSTYNCEYIKDKKCKSGPCHLDNSAMGQSPLSAVWSLLLLLWFLVVRAFPDGPGLL
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MVTAVLLVQKANLETITQFHDQISNELPTAKGKWNFNFKIFRNNQYSIPQELVDTHEQAPESKFLFTLSPSYLRDSTITLINGKSAGVFTNSIEEELSELGHPSDLSIPNDHLRRGATTGLNDKFDNFIGAKLQSLWTQRQLIKGDGGQIYELENGNLCIRTSNVFLHGNFRGLLIQIEMSNSLCDTNNHNSFKEHFNKIVEKYGFPEGNLCCDVLDKKNLDKYGDLCLQYSKILNF
The following text describes a protein:
Function:
Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MEKPVQVTLYDTNTIKQTLDDSIIKYLTTQLNYTQHQKLNYTKVLLGFFGCVLAAIAQFYPIPFPKNKPVLILCQAKINQKIKVSSVLPKYDPIYSVKIEDSKNPKISHPFTKSIDLYFDTKGTFLESAFHNDLVGQFKSFSKLSKKD
The following text describes a protein:
Function:
Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp), albeit with 500-fold lower efficiency. Displays no proline racemase activity.
Sequence:
MHTIDVIDSHTAGEPTRVVLAGFPDLGDGDLAQCRERFRSDFDHWRSAIACEPRGSDTMVGALLLPPRDPSACTGVIFFNNVGYLGMCGHGTIGVVRTLAELGRIAPGQHRIETPVGTVGVALADDGTVSIDNVESYRHAAGVEVDVPGHGRVRGDVAWGGNWFFITEQAPCALGLAQQRELTAYTEAIRLALEAAGITGEAGGEIDHIEISGVAPDGSGAARNFVLCPGLAYDRSPCGTGTSAKLACLAADGKLAEGERWLQQGILGSAFEGSYRHSGRGIAPRISGHAFITARSQLLIDPADPFAWGIVA
The following text describes a protein:
Function:
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity.
Subcellular Localization:
Nucleus.
Sequence:
MDNTKEKNNFKDALLLRMGLNDNKAGMEGLDKEKINKIIMEATKGSRFYGNELKKEKQVNQRIENMMQQKAQITSQQLRKAQLQVDRFAMELERNRNLNNTIVHVDMDAFYAAVEMRDNPELKEKPIAVGSMSMLATSNYHARRFGVRAAMPGFIAKRLCPQLIIVPPNFDKYRAVSKEVKEILAEYDPNFMAMSLDEAYLNITQHLQERQGWPEDKRRYFIKMGNCRKIDTPRQEADELTERERSISPLLFEDSPPDLQPQGSPFQLNSEEQNNPQIAQNPVVFGTSAEEVVKEIRFRIEQKTTLTASAGIAPNTMLAKVCSDKNKPNGQYQIVPSRSAVMDFIKDLPIRKVSGIGKVTEKMLLALGIVTCTELYQQRALLSLLFSESSWHYFLHVALGLGSTDLARDGERKSMSVERTFSEINKTEEQYSLCQELCTELAHDLQKEGLKGRTVTIKLKNVDFEVKTRASTVPSAISTAEDIFAVAKELLRTEVTAGSPQPLRLRLMGVRMSTFSNDDDRKHQQRSIIGFLQAGNQGLSPTGCTADRTDKTELVKPLETSRKKSFFDKKRSERIPNCQDPPRCKIAGEQALQASEPSQALKKMSESFKTSENSNDPQTFICPVCFREQEGISLEAFNEHVDACLDGPSTSENSEMPSYSHASSADIGQQAHRAVPLWEKRGHGDGEITSGDGADLTETEDRSPKAASMDAVGNNHSEGEGYPDSQGKSCPLSPANETVSTLSREDSAQPCTDEVVTGRALVCPVCNLEQETSDLTLFNIHVDICLNKGIIQELRNSEVNSVKQPKGSTRSTDRLQKASGKTKRAGRKTKGSTSKRTKPRDPRHTLDGFFK
The following text describes a protein:
Function:
Expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic.
Miscellaneous:
MISCELLANEOUS: P.bifermentans strain Cbm (subsp. malaysia) is toxic to Anopheles mosquito 3rd instar larvae and less toxic to Aedes aegypti larvae.
Domain:
A beta-sheet wrapped around a long alpha-helix. Structurally similar to tubular lipid-binding (TULIP) superfamily proteins. The structure of OrfX1-OrfX3 is very similar to OrfX2 from C.botulinum type A2 (AC C1FUH4, PDB:6EKV). The structure of C.botulinum type A2 P47 (AC C1FUH7, PDB:6EKT) is very similar to OrfX3 in the OrfX1-OrfX3 complex.
Sequence:
MIGKRQTSTLNWDTVFAVPISVVNKAIKDKKSSPENFEFEDSSGSKCKGDFGDWQIITGGDGSNIRMKIPIYNFKAELVDDKYGIFNGNGGFESGEMNIQVKLKYFPHDKISKYKDVELVDLKVRSESADPIDPVVVMLSLKNLNGFYFNFLNEFGEDLQDIIEMFFIELVKQWLTENISLFNHIFSVVNLNLYIDQYSQWSWSRPSYVSYAYTDIEGDLDKSLLGVLCMTGGRNPDLRQQKVDPHAVPESSQCGFLIYEERVLRDLLLPTLPMKFKNSTVEDYEVINASGESGQYQYILRLKKGRSVSLDRVEANGSKYDPYMTEMSISLSNDVLKLEATTETSVGMGGKVGCDTINWYKLVLAKNGNGEQTISYEEVGEPTVINYVIKEGENWVWDVIAAIIAILATAVLAIFTGGAAFFIGGIVIAIITGFIAKTPDIILNWNLETSPSIDMMLENSTSQIIWNARDIFELDYVALNGPLQLGGELTV
The following text describes a protein:
Function:
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular Localization:
Endosome membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Plastid, chloroplast.
Sequence:
MPSSSSSATAAVFLLLVSLLATSLASDSDHKYQADEQVTLWVNKVGPYNNPQETYNYYSLPFCRPSLNDVHKWGGLGEVLGGNELIDSEIPIKFLKNVDRNVICKLELDELKVEHFKDAIESSYWFEFFMGFVGELQSDKNGENGKHVLYTHKNIIVKYNKDQIIHVNLTQDNPRPLEAGRTVDLTYSVQWIPTDVTFARRFDVYLDYPFFEHQIHWFSIFNSCMMVIFLTGLVSMILMRTLRNDYAKYAREDDDLESLERDVNEESGWKLVHGDVFRPPFSLVLLSAVVGTGAQLALLILLVILMAIVGTLYVGRGAIVTTFIVCYALTSFVSGYVSGGMYSRSGGKHWIKCMVLTASLFPFLCFGIGFILNTIAIFYGSLAAIPFGTMVVVFVIWGFISFPLALLGTVVGRNWSGAPNNPCRVKTIPRPIPEKKWYLTPSVVSLMGGLLPFGSIFIEMYFVFTSFWNYKVYYVYGFMLLVFVILVIVTVCVTIVGTYFLLNAENYHWQWTSFFSAASTAVYVYLYSIYYYYVKTKMSGFFQTSFYFGSGWILGIKPVCKENLQKHQMRLEISIEQTPNSLRSLPAANTQSLFGLKSSTSRGGRVTAMATYKVKFITPDGEKEVECDGDTYVLDAAEESGLDLPYSCRAGACSSCAGKIVSGSVDQSDQSFLDDGQISEGFVLTCIALPTSDVVITTHQEDAMI
The following text describes a protein:
Function:
Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs (By similarity). Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription (By similarity).
Subcellular Localization:
Nucleus, nucleoplasm. Cytoplasm. Note=Predominantly nuclear. Shuttles between the nucleus and the cytoplasm (By similarity).
Sequence:
MGDSDDEYDRRRRDKFRRERSDYDRSREREDRRRDDWNDRRPSAREWDRGRERRSRGEYRDYDRGRRERFSPPRHDMSPQQKRMRRDWDDHGGDPYHGGYDLGYGGGGGPSYAPPQPWGHPDMHLMQPHHGIPIQARLGNIHDMDLGPPPPVMKTFKEFLISLDDSVDETESVKRYNEYKIDFRRQQMQDFFLAHKDEEWFRSKYHPDEAGRRKAEAHSALQNRLGVYMYLMDNNWFESVSLDIERAPQITKILDAAVIKMEGGAENDLRILEQPSEEEEERERLSSGGTPSEPSKRDEPKPADTENKPSEEKDKMEEGEESAEKDGEKASAGGSEGEEKTEKEAPAEPIPEPKKLSKKRKRKHSGDSEDEASASESESDSDSDSNSHCSEKPSEREREPEEVEEKEEEEEEEGEAADGKEQTDEQTEREKEKEKKVKDDQPPRPRPLHRTCSLFMRSIAPTISKAEIVALCRRYPGFMRVCLSEPQPERRFFRRCWVTFDRGVNIKEICWNLQNIRLRDCELAPGVNRDLARRVRNVNGITQHKQVLRNDIKLAAKLIHALDDREKLWSQKPREETPTLELPAQNPILKNITDYLIEEVSAEEEELLGSAGGGDSEDGSKEGNPTEITVERDEKLVKVLDRLLFYLRIVHSIDYYNTCEYPSEDEMPNRCGIIHVRGPIPPNRITLREVSDWQKTFEEKMGPLFSVKENLSEDEAAKMGRKDPEQEVEKFVVANTQELGKDKWLCPLSGKKFKGPEFVRKHILNKHGDKIEEVKKEVVFFNNFLMDAKRPCIPEMKPPPHPGPGQGVLSPGGLPFPPQGPQGLMGFGQPRPPLMGYGGGPPYPPNQYGGGRGNYDNFRGQGGYPGKPRNSRVMRGDPRNIIEYRDLDAPDDVDFF