lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase OPG063 that creates mRNA's poly(A) tail. In the presence of OPG102, OPG063 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.
Subcellular Localization:
Virion.
Sequence:
MYPSLFKKRPRDDDAKSISLSFPPAVVEHYPSKLSFPVIIDANFPAQEYCSRGASVKSSIHWGQRKLLLSEIQLLCLYARPDVSYHIVYAGSAPGTHLAYLDEMFRGRHTWELVDPGKFDRPVLEKHPNFTLRNEFFTNATAYGINARRLSNVCPALGAIYEHVAVDSADPRLKDLHQKLQTVIGTHDVARGTESIPSMYEPQRQLPVGFELLCAVARERERPLLFISDIRSGSVNLPNFEDHVAENMKAQKCWCQILQGEFSMLKFRLPYTHRGKGVGEGRKKVPSHLIGKDGTVTYLKGDLLLPIWTRPTSTEGRLVVACGAPQVSYNVQYVENQFFFFNAHLRERVHFNHLLPPDLDLDHHYDAAAEVNCLLAYLKFIDPNLRNAPADVLAREVKRVSSSITAQLRTTFQDAIRRRDALVLKHARGGNLDDEDGGESDGEEPGDSPQCAADHQRHNKNGCAGSPMEEMAKALIAAAAKERARVLWKRNVEESETDPLSGVWVTTKMKQ
The following text describes a protein:
Function:
Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release.
Sequence:
MSEKTSTVTIHYGNQRFPVAVNLNETLSELIDDLLETTEISEKKVKLFYAGKRLKDKKASLSKLGLKNHSKILCIRPHKQQRGSKEKDTVEPAPKAEAENPVFSRISGEIKAIDQYVDKELSPMYDNYVNKPSNDPKQKNKQKLMISELLLQQLLKLDGVDVLGSEKLRFERKQLVSKIQKMLDHVDQTSQEVAA
The following text describes a protein:
Function:
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA; Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. 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. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Subcellular Localization:
Nucleus.
Sequence:
MAAAPPRPFDYLESLPGTVFNKLYQQPSTALAIFRRMLPDLAKCFVMALLYLKDPLPAADLEAWVRPGSLKERDNALSILGRLHIMTSTTTSDNIKAYTVTDPFASSLRQALTGAEQTQSFGVLSQISDKEAVSIADLDEYSRRQWEGVLGYMVGTSGLGMQRDVSLSKGVKELLQAGHLVEIRDRRVEITQDGFAFALQDVGTQVWHILVLYVESAAAIGMDSVEVLSFVFFLSSLELGKSYEKKQLTSNQLRTLTDLADFGIVYQETPDATHFYPTRLATTLTSDSSTLSNPLAGSLSGPTGTSSSKAGSGFIIIETNYRLYAYTSSPLQISLIALFTTLKYRFPNLITGKITRQSVRRAVEMGITADQIISYLSTHAHPQMRKHNVSRSTSNQAGMPVSVLPPTVVDQIRLWQLERDRVKATHGFLFRDFNTLAEYEAPCRYAEEIGVLVWKSDRKRMFFVTRHHQVAAFLKSRRK
The following text describes a protein:
Function:
Hydrolyzes p-nitrophenyl phosphate (pNPP) in vitro. Involved in the swarming motility process.
Sequence:
MYPVDLHMHTVASTHAYSTLSDYIAQAKQKGIKLFAITDHGPDMEDAPHHWHFINMRIWPRVVDGVGILRGIEANIKNVDGEIDCSGKMFDSLDLIIAGFHEPVFAPHDKATNTQAMIATIASGNVHIISHPGNPKYEIDVKAVAEAAAKHQVALEINNSSFLHSRKGSEDNCREVAAAVRDAGGWVALGSDSHTAFTMGEFEECLKILDAVDFPPERILNVSPRRLLNFLESRGMAPIAEFADL
The following text describes a protein:
Function:
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA (By similarity). Promotes Holliday junction (HJ) branch migration in conjunction with RuvB.
Subcellular Localization:
Cytoplasm.
Domain:
Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Sequence:
MIAGISGRVLKKSGNVLLVETKSGVVFEIVCDVQTSEEVKEGGECFLHTFLSVSQDGITLYGFSNEMKKELFLSLTKVSRLGPKTALKIISNEDAETLVAMIASQDVEGLSKLPGISKKTAERIVMELKDEFESAGIKDMRIYHESLEALVSLGYPEKQAREAVKQVYREGMKTSELIKEALKFLSHR
The following text describes a protein:
Function:
Involved in spermatogenesis. Has a probable role in anterograde intraflagellar transport which is essential for the formation of sperm flagella.
Subcellular Localization:
Cell projection, cilium, flagellum. Note=Mainly located in the mid-piece of sperm flagella.
Sequence:
MRAAGPWRAASPAPCTRYLARCKPGFRPSSSFVVDLLVDSGDPGLEDVALTECLSPPSLSCSNSTLSLLSPLGHQSFPFGADDSEGEDEEALDEDARESESKVESLEGIEFQQRSSCEVESQDKQEKLVLLQHGSLTPWEMWFVGKEKEERGRLQQKFLEELNQQIEKRKEMEEREKRKIIAEVKHKEWVQKKNKQERKEREQKINKEMEEKEAKKREKEHLQEKAKEKYQEWLKKKKAEEYEKKKKEKEKEKQRQAELQEKKEIAEKKFKEWLENAKNKPRPAAKSYGYSSGKLTGFYSGNSYPEPTFYNPIPWKPIHMPPPKEAKSGPGKKSKRHAASQPLPSSSLAVHNAKSSLCLGALCRGQR
The following text describes a protein:
Function:
May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)-dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface.
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein. Recycling endosome membrane; Single-pass membrane protein.
Sequence:
MFPEPPTPGPPSPDTPPDSSRISHSPVPPWALATIVLVSSLLVLSCCFCLYRKCCRRRTGKKSQAQAQVHLQEVKGLGQSYIDKVQPEVEELEPAPSGPGQQVADKHELGRLQYSLDYDFQSGQLLVGILQAEGLAALDLGGSSDPYVRVYLLPDKRRRYETKVHRQTLNPHFGETFAFKVPYVELGGRVLVMAVYDFDRFSRNDAIGEVRVPMSSVDLGRPVQTWRELQAAPREEQEKLGDICFSLRYVPTAGKLTVIVLEAKNLKKMDVGGLSDPYVKVHLLQGGKKVRKKKTTIKKNTLNPYYNEAFSFEVPCDQVQKVQVELTVLDYDKLGKNEAIGRVAVGAAAGGAGLRHWADMLANPRRPIAQWHSLRPPDRVRLLPAP
The following text describes a protein:
Function:
Inhibitory receptor that plays a role in the modulation of immune responses. Suppresses T-cell activation by promoting the generation of mature immunoregulatory dendritic cells. Upon binding to its ligands PVR/CD155 or NECTIN2/CD112, which are expressed on antigen-presenting cells, sends inhibitory signals to the T-cell or NK cell. Mechanistically, interaction with ligand leads to phosphorylation of the cytoplasmic tail by Src family tyrosine kinases such as FYN or LCK, allowing subsequent binding to adapter GRB2 and SHIP1/INPP5D. In turn, inhibits PI3K and MAPK signaling cascades. In addition, associates with beta-arrestin-2/ARRB2 to recruit SHIP1/INPP5D that suppresses autoubiquitination of TRAF6 and subsequently inhibits NF-kappa-B signaling pathway. Also acts as a receptor for NECTIN4 to inhibit NK cell cytotoxicity.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
KVFLVARPTQFTYLLRVLSVGDIVFAELVFSETLFSHRLSFTTSAVGQFRWQKRPHLLPGGPLGRSMQWCLLLIWAQGLRQAPLPASGAVTGRIVTVGNISAEEGDSVTLQCHLSSTTAEVTQVNWEQQDQPLAVYHPTLGWYIYPVFRKRVAPGPNLDLILQSLTVNDTGEYFCTYYTYPDGIYKAKLFLEVLQSSVAEHSAGFQILLVGAMATGLTVICMAAIVVVVLAIKRKSLRMRSAENDLRRTSSEQEERNPSAPSFPRSCVQAEAAPASPCREQRGDDYAEPHDYFNVLGYRSLRSFVFLAETG
The following text describes a protein:
Function:
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Sequence:
MSERKSDPDRDDSERAFFGRRKGHKLRQHQAELIDHLLPHLALDIAGEAPGNACEIFDPAASDVRLEIGFGGGEHLAAEAQNFATTGFIGCEPYVNGMAKILAQIEAGNIANIRLFAGDAAELLAWLPKASLSRIDLIHPDPWPKRRHWKRRFVQDRTIAAMARVLKVGGEFRFVCDIDDYCAWTLSHLARSADFKWLAERADDFRQPWDGYTMTRYGRKAAREGRKAAYLRFRRS
The following text describes a protein:
Function:
Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Subcellular Localization:
Nucleus.
Sequence:
MTIFSGPRGLFACYCLVAESSESPKRCYIGFTNNPLRRIRQHNRKIAGGARKTSRYGPWRMVLFVGGFSTKVSALKFEYIWTYPTRSRYVNCISATSQKLRLACPRSISTALDVLVTLLIHPPFSLQPLYVVLLDAEGNRVKSQLEQHSVPVFVSTMEALQIEPGVRAPSDIIYAQCTSSNGTTDTTFTDVCPICQDGVSPSNVQCMQCSARFCITCAGKLFTRRNTLIPCFGKCPICKREFQWKEMLRKRAEELVAGRKSVPHKTQAVDGQSSLSQNSSYDDYDTISLLSSSSEPEKDDISRDESGTVASVQPVSSVALSDSSRSPATTSPTKPLAIDPLLSSPRPCALPSDVISITD
The following text describes a protein:
Function:
Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase (By similarity).
Miscellaneous:
MISCELLANEOUS: Dimerization and MBL2 binding requires calcium ions.
Subcellular Localization:
Secreted.
Sequence:
MRLLIFLGLLWSLVATLLGSKWPEPVFGRLVSPGFPEKYADHQDRSWTLTAPPGYRLRLYFTHFDLELSYRCEYDFVKLSSGTKVLATLCGQESTDTEQAPGNDTFYSLGPSLKVTFHSDYSNEKPFTGFEAFYAAEDVDECRVSLGDSVPCDHYCHNYLGGYYCSCRAGYVLHQNKHTCSALCSGQVFTGRSGYLSSPEYPQPYPKLSSCTYSIRLEDGFSVILDFVESFDVETHPEAQCPYDSLKIQTDKGEHGPFCGKTLPPRIETDSHKVTITFATDESGNHTGWKIHYTSTARPCPDPTAPPNGSISPVQAIYVLKDRFSVFCKTGFELLQGSVPLKSFTAVCQKDGSWDRPMPECSIIDCGPPDDLPNGHVDYITGPEVTTYKAVIQYSCEETFYTMSSNGKYVCEADGFWTSSKGEKLPPVCEPVCGLSTHTIGGRIVGGQPAKPGDFPWQVLLLGQTTAAAGALIHDNWVLTAAHAVYEKRMAASSLNIRMGILKRLSPHYTQAWPEEIFIHEGYTHGAGFDNDIALIKLKNKVTINGSIMPVCLPRKEAASLMRTDFTGTVAGWGLTQKGLLARNLMFVDIPIADHQKCTAVYEKLYPGVRVSANMLCAGLETGGKDSCRGDSGGALVFLDNETQRWFVGGIVSWGSINCGAADQYGVYTKVINYIPWIENIISNF
The following text describes a protein:
Function:
Catalyzes the reversible conversion of fructoselysine 6-phosphate to glucose 6-phosphate and lysine. Functions in a fructoselysine degradation pathway that allows E.coli to grow on fructoselysine or psicoselysine.
Sequence:
MLDIDKSTVDFLVTENMVQEVEKVLSHDVPLVHAIVEEMVKRDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYSVVLEMITRLAPNAEIGKIKNDLKQLPNALGHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHTTERAINFVKQRTDNVIVIDYAEISQGLHPWLAPFLMFVPMEWLCYYLSIYKDHNPDERRYYGGLVEY
The following text describes a protein:
Function:
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence:
MKHVNVLLAGGASRRFGEPKAFVKWKGRMLYECAKEALGEQTVIISRPEFIDRFQENGENEVYQDAEPFQGMGPLAGIYTAFKKTDGDLYTVLSCDTPLIQRRTMLELKRLMIAGADAVVPISDGQVQPLIAIYHKRIMPVLYDQLSEKRLRISDLLGRISVCYVQAENIGANPAEFININTRDDFSCLEEKSNSLKRD
The following text describes a protein:
Function:
Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. Selective for MG, does not use glyoxal as substrate. Plays a role in detoxifying endogenously produced MG, particularly when glycerol is the principal carbon source. Important for viability in stationary phase (By similarity).
Sequence:
MVKVLLALTSYNETFYSDGKKTGVFVVEALHPFEVFRKKGYEIQLASETGTFGWDDHSVVPDFLNGEDKEIFDNVNSEFNVALKNLKKASDLDPNDYDIFFGSAGHGTLFDYPNAKDLQKIATTVYDKGGVVSAVCHGPAIFENLNDPKTGEPLIKGKKITGFTDIGEDILGVTDIMKKGNLLTIKQVAEKEGATYIEPEGPWDNFTVTDGRIVTGVNPQSAVKTAEDVIAAFECN
The following text describes a protein:
Function:
Essential cell division protein that activates septal peptidoglycan synthesis and constriction of the cell. Acts on both sides of the membrane, via interaction with FtsA in the cytoplasm and interaction with the FtsQBL complex in the periplasm. These interactions may induce a conformational switch in both FtsA and FtsQBL, leading to septal peptidoglycan synthesis by FtsI and associated synthases (Probable). Required for full FtsI activity. Required for recruitment of AmiC to the septal ring.
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein. Note=Localizes to the septum. Localizes to the midcell via interaction with the early cell division protein FtsA and via the periplasmic SPOR domain. FtsA-dependent localization precedes SPOR-dependent localization, and both are needed for efficient localization. Localization depends upon FtsZ, FtsA, ZipA, FtsQ and FtsI.
Domain:
The cytoplasmic region is required for interaction with FtsA. The periplasmic region is composed of a membrane-proximal region containing three short partially formed helices (H1, H2 and H3), followed by an unstructured glutamine-rich linker, and a C-terminal globular SPOR domain. Essential function of FtsN is accomplished by a small region of at most 35 residues that is centered about the H2 helix. The SPOR domain, which exhibits a ribonucleoprotein (RNP) fold, binds peptidoglycan and is a strong septal localization determinant, but it seems not essential for cell division.
Sequence:
MAQRDYVRRSQPAPSRRKKSTSRKKQRNLPAVSPAMVAIAAAVLVTFIGGLYFITHHKKEESETLQSQKVTGNGLPPKPEERWRYIKELESRQPGVRAPTEPSAGGEVKTPEQLTPEQRQLLEQMQADMRQQPTQLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAQQSRTTEQSWQQQTRTSQAAPVQAQPRQSKPASSQQPYQDLLQTPAHTTAQSKPQQAAPVARAADAPKPTAEKKDERRWMVQCGSFRGAEQAETVRAQLAFEGFDSKITTNNGWNRVVIGPVKGKENADSTLNRLKMAGHTNCIRLAAGG
The following text describes a protein:
Function:
Protease involved in the processing of a variety of prenylated proteins containing the C-terminal CAAX motif, where C is a cysteine modified with an isoprenoid lipid, A is an aliphatic amino acid and X is any C-terminal amino acid. Proteolytically removes the C-terminal three residues of farnesylated proteins, leaving the prenylated cysteine as the new C-terminus. Target proteins include the a-factor mating pheromone and RAS. Its substrate specificity is overlapping but distinct with that of STE24.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MLQFSTFLVLLYISISYVLPLYATSQPEGSKRDNPRTIKSRMQKLTIMLISNLFLVPFLQSQLSSTTSHISFKDAFLGLGIIPGYYAALPNPWQFSQFVKDLTKCVAMLLTLYCGPVLDFVLYHLLNPKSSILEDFYHEFLNIWSFRNFIFAPITEEIFYTSMLLTTYLNLIPHSQLSYQQLFWQPSLFFGLAHAHHAYEQLQEGSMTTVSILLTTCFQILYTTLFGGLTKFVFVRTGGNLWCCIILHALCNIMGFPGPSRLNLHFTVVDKKAGRISKLVSIWNKCYFALLVLGLISLKDTLQTLVGTPGYRITL
The following text describes a protein:
Function:
Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes.
Subcellular Localization:
Nucleus.
Sequence:
MEGNTVAQTLTADQLGQIQTIQTQGAQAGGQQIQLQLQGQAGAGRRGWTDPIRGSANHAAGRRGQAGTTQLQQLAQTLQVVGAGGQVQQIQLIPTQQLQGANQATQGQTQVVQTQSSTAQGQQQQQQQQQLQEQTQQQAQQIQIVQPQQVQATNQQGXAGATHHCPAATGQHSTTGTTAAAAATTTAAATAAADTVAAAYNCRRADDLLSAVVAGDNQVTLPGTQLQSTTSGTGGGAGDNNGVMQLQTTNQVQQAPANTAAASGNQLLQVAANNGTDNSIVMMIPGSGGVPTMQRIPLPGAELLEEEPLYVNAKQYHRILKRRQARAKLEAEGRIPKERRKYLHESRHNHAMNRVRGEGGRFNSGEGEEDMIPSPSMLKSSHHQLHRQQQLPTMVQLPQGMTLATGPDGHVTQEGMINLSMLTGGGTSTSAQVLIGQGNTIATLAANGVRGVSQ
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 involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE; this reaction does not require ATP in vitro. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MQNLTLLALDTSTEACSVALLYRGEKTHINELAQRTHTKRILPMIDEILANSGLGLNQVDALAFGRGPGSFTGVRVGAGIAQGLAFGADLPVIPISNLTAMAQAAFELHQAENVVAAIDARMNEVYFSQVVREKVRSDFGEFFQWREIISEQVCSPEQAINQLQNDNAFRVGTGWAAYSQFTEKNLTGSDIALPNALYMLELAQVEYLQKHTISALEIEPIYLRNEVTWKKLPGRE
The following text describes a protein:
Function:
Mediates influx of magnesium ions. Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MEEASSSLRPVAAYFHSSFDRQRTKTSLATMTTTFHCTTLETSMQMQSCHLFWHNSTLSIVLKRELADCAPSREVPVLHVKRHSLFGGDLEIDLGGSVHPVRMLPVSGKDVRNLRFGLVYGPKRKRVRFRAPDLATYDSWEMVLELAVEKAATERPTFPTWPYPGTSPSLSALEEGYISEEFGFSDGETTSDESKLSEFRHKRAQAMQNPMTGSFEDFIDPPTPKSSSRDDGTESELDRIPSTESEYDSVNRESEMPGPMDFYAVDEDTPLLRDLVAPDASPRSDSELSSYPPHVNSGGSTRRSLQTTELELSVDKISFLFSPTARPGYGSPSNYKSFADVPLNGALQDDDELNMLDPYFDVTASRLRVAFEGAGPEGDGELSYEGFRAALETLGIRCSDDSVFLKLVGSIDRLKSERITLAQFDAAVHRLKLMHMFEEGTVQEMKTVGYQQAALSVSDFSSTRLQSFVLKQENLHEFFTAHRPEWVSVRWINLDGRDSVNLKRLAIKYRLHPLAIEDTIEGHERPKFDRYDGHLFLVFPVLRMQVADKGLPLQRKRNRLFSEAKGTPLPTFVKERRGPLHRSMSVITDDTENEDEDPLKLWIEHVFIFVVDNDTVITVKDGGDSDIWNELNRRLAVPYSKLRHNDAKFLVYTVLDVIVDQVTNVVDSITECLIELEGQLDVERHRFELRSLRFLKNELFRLPRLLKPAREVLKNIIDSKDFDATVTDYVRDVHDHVVQVLDDIEQQLQMCRQLTEEYRDAKANQMNYVIYTLTVVTTVFLPGQFLTGVYGMNFDDMPELHERYGYALFWVLAIAIAAALQLYFRYKQWI
The following text describes a protein:
Function:
A component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation (Probable). Two crystal forms have been seen; a form with a closed central pore that has 3 very small (1.1-2.2 Angstroms) channels per trimer lined by acidic and aromatic residues. A form with a large central pore (8-12 Angstroms) has also been seen; this is probably a functional pore which allows molecules to enter and exit the BMC in a selective, gated manner. Another group only sees the central pore in the presence of Zn(2+); soaking crystals in ZnCl(2) leads to dramatic conformational changes that open a central pore of about 12 Angstroms. Whether Zn(2+) binding is physiologically relevant is unclear, however it suggests a gating mechanism exists. Ethanolamine-binding by the small channels has been hypothesized to stabilize the EutL central pore in a closed (non-transporting) state. An open pore is thought to be large enough to transport ATP and/or cobalamin (By similarity).
Subcellular Localization:
Bacterial microcompartment.
Domain:
Has 2 BMC domains which can evolve independently of each other.
Sequence:
MPALDLIRPSVTAMRVIASVNADFARELKLPPHIRSLGLISADSDDVTYIAADEATKQAMVEVVYGRSLYAGAAHGPSPTAGEVLIMLGGPNPAEVRAGLDAMIAHIENGAAFQWANDAQDTAFLAHVVSRTGSYLSSTAGITLGDPMAYLVAPPLEATYGIDAALKSADVQLATYVPPPSETNYSAAFLTGSQAACKAACNAFTDAVLEIARNPIQRA
The following text describes a protein:
Function:
3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'.
Subcellular Localization:
Cytoplasm. Cytoplasm, P-body.
Sequence:
MKDPVAPQIFPEHWSLPKVNEAMQSGRVFSCSLRVNAHNRSEAYATVDGLSVDILIEGACAQNRALEGDLVALVLDPPNLWPRMKGLNNNRTDRVVTASSIAVTNQSFSSGEGVQVSREIRLEEEVVIESVGSSNQVVESSEDSGSLLSGPGSTALEKVQALLQATPGKRPTGKVVSILSKSRRRDAVVGFLSVKFQPPTRNQMVLTPVDAKFPKMVVLPDSLPEVIAQRLRDGDRKMGNELLAACVDRWDCNSPYPLAIITHCLGQAGELEAQTAAILFEHAVHSAEFPPEAMACLPRVPWSIPKKELQRRRDLRSRRVFTIDPVTARDLDDALSVEHLGDGLTRVGVHIADVSYFVHAGSGLDKEAQQRSTSVYLIEQVLPMLPRLLCEELCSLQPGVDRLAFSVMWDLDSTGQIVKQWIGRTAIKSCCKLSYGDAQEIIDGTFSEKPGLSGNFSWQEVAADIKTLYNIAKQLEESRIRDGALRLDTGKLVFALDGDGNPHETSFYEQMESNKLVQEFMLLANVSVAKVISRAFPDCALLRRHPEPSSRKLLEFQEFCKKHGFVLKTDSSADLHASLEVLREELKDDPVLLSIVTLYATKPMQVAKYFCTGRDKDGDWGHYALAMPVYTHFTSPIRRYPDIVVHRTLTAALEAEKVLNKSLTGPEDLVSTKDYEVLQLAASKHRISDPAEMALLADHCNERKMASKNVQEATDRLYLWTMLQRRKGLLSDACVVGLGPKFMSLYVSKIAMERRLYYDEVEGLKVDWLENTGTLVLDYCRPRQHSRKAKCRSISDVAVVSNPAMDPDDETGNLDRLTRIEPEAMPLTLRLFSHIPVLIHALGGDSSPLDIGVRVYVTSYFFS
The following text describes a protein:
Function:
Component of the MMS22L-TONSL complex, a complex that promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication. It mediates the assembly of RAD51 filaments on single-stranded DNA (ssDNA): the MMS22L-TONSL complex is recruited to DSBs following histone replacement by histone chaperones and eviction of the replication protein A complex (RPA/RP-A) from DSBs. Following recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of RAD51 filaments and subsequent homologous recombination. Within the complex, MMS22L acts by binding ssDNA.
Subcellular Localization:
Nucleus. Chromosome. Note=Localizes to DNA damage sites, accumulates at stressed replication forks. Recruited to stalled or collapsed replication forks; directly binds replication protein A complex (RPA/RP-A)-coated single-stranded DNA (ssDNA).
Sequence:
MENCSAASTFLTDSLELELGTEWCKPPYFSCAVDNRGGGKHFSGESYLCSGALKRLILNLDPLPTNFEEDTLEIFGIQWVTETALVNSSRELFHLFRQQLYNLETLLQSSCDFGKVSTLHCKADNIRQQCVLFLHYVKVFIFRYLKVQNAESHVPVHPYEALEAQLPSVLIDELHGLLLYIGHLSELPSVNIGAFVNQNQIKLFPPSWHLLHLHLDIHWLVLEILYMLGEKLKQVVYGHQFMNLASDNLTNISLFEEHCETLLCDLISLSLNRYDKVRSSESLMSDQCPCLCIKELWVLLIHLLDHRSKWFVSESFWNWLNKLLKTLLEKSSDRRRSSMPVIQSRDPLGFSWWIITHVASFYKFDRHGVPDEMRKVESNWNFVEELLKKSISVQGVILEEQLRMYLHCCLTLCDFWEPNIAIVTILWEYYSKNLNSSFSISWLPFKGLANTMKSPLSMLEMVKTCCCDKQDQELYKSSSSYTIFLCILAKVVKKAMKSNGPHPWKQVKGRIYSKFHQKRMEELTEVGLQNFFSLFLLLAAVAEVEDVASHVLDLLNFLKPAFVTSQRALIWKGHMAFLLMYAQKNLDIGVLAEKFSCAFREKAKEFLVSKNEEMVQRQTIWTLLSIYIDGVQEVFETSYCLYPSHEKLLNDGFSMLLRACRESELRTVLSFLQAVLARIRSMHQQLCQELQRDNVDLFVQSSLSAKERHLAAVASALWRHFFSFLKSQRMSQVVPFSQLADAAADFTLLAMDMPSTAPSDFQPQPVISIIQLFGWDDIICPQVVARYLSHVLQNSTLCEALSHSGYVSFQALTVRSWIRCVLQMYIKNLSGPDDLLIDKNLEEAVEKEYMKQLVKLTRLLFNLSEVKSIFSKAQVEYLSISEDPKKALVRFFEAVGVTYGNVQTLSDKSAMVTKSLEYLGEVLKYIKPYLGKKVFSAGLQLTYGMMGILVKSWAQIFATSKAQKLLFRIIDCLLLPHAVLQQEKELPAPMLSAIQKSLPLYLQGMCIVCCQSQNPNAYLNQLLGNVIEQYIGRFLPASPYVSDLGQHPVLLALRNTATIPPISSLKKCIVQVIRKSYLEYKGSSPPPRLASILAFILQLFKETNTDIYEVELLLPGILKCLVLVSEPQVKRLATENLQYMVKACQVGSEEEPSSQLTSVFRQFIQDYGMRYYYQVYSILETVATLDQQVVIHLISTLTQSLKDSEQKWGLGRNIAQREAYSKLLSHLGQMGQDEMQRLENDNT
The following text describes a protein:
Function:
May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MPSFVVNPLSLCIPQSSFEAWLKDKGFLEILEKCTLDNAIIAGQGSFVALCKLLKLNPFESLTVEDLGKKPVPWTAEFLDCGKGPAETYSWPMSVTQVKFRMDENLKRYTGNYLVLIAITFACVLYKMPLALLGVVSLFGLWDGLRILINKFKIQRHGVLFRLLVALGNVGTMLLLMYCRVALALICAAALSFTVLVLHSSMRKITPPNT
The following text describes a protein:
Function:
Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Sequence:
MTLRQAIDLAAALLAEAGVDSARCDAEQLAAHLAGTDRGRLPLFEPPGDEFFGRYRDIVTARARRVPLQHLIGTVSFGPVVLHVGPGVFVPRPETEAILAWATAQSLPARPLIVDACTGSGALAVALAQHRANLGLKARIIGIDDSDCALDYARRNAAGTPVELVRADVTTPRLLPELDGQVDLMVSNPPYIPDAAVLEPEVAQHDPHHALFGGPDGMTVISAVVGLAGRWLRPGGLFAVEHDDTTSSSTVDLVSSTKLFVDVQARKDLAGRPRFVTAMRWGHLPLAGENGAIDPRQRRCRAKR