lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Plays an important role in maintaining outer membrane integrity. Supports proper folding and function of BamA under envelope stress conditions. Binds specifically to anionic phospholipids via the BON 2 domain. This interaction is essential for function and guides the protein to the cell division site. It was reported that DolP is a potential upstream regulator of the amidase activator NlpD. However, later studies suggest that DolP affects cell division and may impact daughter cell separation, but likely not as a regulator of NlpD.
Subcellular Localization:
Cell outer membrane; Lipid-anchor; Periplasmic side. Note=Localizes to the cell division site. Localization to the division site is dependent upon interaction with anionic phospholipids. Upon envelope stress, loses its association with the mid-cell.
Domain:
Composed of two BON domains that form an interconnected opposing pair. The N-terminal BON domain interacts with BamA. The C-terminal BON domain binds anionic phospholipids through an extensive membrane:protein interface.
Sequence:
MKALSPIAVLISALLLQGCVAAAVVGTAAVGTKAATDPRSVGTQVDDGTLEVRVNSALSKDEQIKKEARINVTAYQGKVLLVGQSPNAELSARAKQIAMGVDGANEVYNEIRQGQPIGLGEASNDTWITTKVRSQLLTSDLVKSSNVKVTTENGEVFLMGLVTEREAKAAADIASRVSGVKRVTTAFTFIK
The following text describes a protein:
Function:
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular Localization:
Cytoplasm.
Sequence:
MATIVNTTEEEPMLAVVRSTAQLAWADAGPEVADPEVARLCAEAQQHLLAGRWLDMATLMLASADLLLLSPSAPDKGQPAPPLSVSVSVRSFLNCAALLCAAADLECILTVICNLVTKAGSEDEALEIAKLICAKLTHQPPADKPTLRIKVLFSLYNLLPSLSGKAMVYRKALEVAAAAAGKAAADCVVPTFKNIDAFVAYWGIGKPEQRELFLAVTRILKDHKGMTKDYFKFLNKYLATFDGSADDADAIGAAKEEAAAAIVEFVKSSDLYQCDLLDMPAVAQLEKDDKYQPVYELLKIFLTQRLESYLAFQTANSTLLQGYGLVHEECITKMRLMSLLDLSGHCSGEIPYSAITKALEINDDEVEYWIVKAISSKILDCKVDQLNQLVIVSRHTVRVFGMPQWQSLRSKLGVWRGNIANAINTIQANKVTEDGGQGMQGLMIR
The following text describes a protein:
Function:
Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein.
Sequence:
MEIDLQTAVGIAGIIVGAFSYFRPVIVFMKTVQRQWTTGDLSATPCLLTYVKCTFFMWYALPDVSRGNHLLFICNFVGFLFASIYIVTFLWLSPRVVVLKNVGAIFVAIAISTAHLVLPRAWLHGYERQLLCGLVAAGFSICTCWPSVKIIDSVMKTKNVEFMSFSASISMFLNGSLWFVFGLHGLDPFVMLPNGFTSVLGALQVILYLVYRNNKSEAERKKKIKYNSNDTIMKKNSK
The following text describes a protein:
Function:
Might be related to the phospholipid scramblase and tubby-like superfamily of membrane tethered transcription factors.
Sequence:
MELVEETIPKEGKKMGERIVVDKAYLYQEDKPLTVCKTSLFYTGDGFAAYDCRGDIIFRVDSYGPDTRDNDEIVLMDATGKCLLTVKRKRPTLHQRWEGFLGERSEGQKPIFSVRRSSIIGRCTMEVEVYDGTGEEYIIDGDFSQRSCLIYDTKKCTVAEIKRKVDASTNVMLGRDVFTLEIKPGFDGAFAMGLVVVLDQINGDDPVEIGDEQVHPFVED
The following text describes a protein:
Function:
Involved in spliceosome assembly.
Subcellular Localization:
Nucleus speckle. Nucleus, Cajal body.
Sequence:
MASGLQSPEELQENLRQYKEQLAQVEQLLMMGSDEEMPGQDLQDMYQSLSEVIQLTEELLKDALEQQRAAGAAVAGLSAAAAAAVAAGVAGAEAAAGEAAAAADANPVAKIVTPPELNLPAILPASVADQIRKAQVRAALTGQAPAEWAIGAQCQAVYSADGQHYDATVEAISAAGNFIVVFEGYGNKEEVGLTGIRPRPGADEGYKGVAAPKRKRVEDEPVVNEIPKWLAIKETDDEKTKARKKKLLKSMKSKIRFQQKDLAQKQKQDSWQSFLKGKGSKKKTGFLTGSIKKGSIFSVPEGVNAKVGVVGSGRGMTEYGKKSRHEFEEADEEQ
The following text describes a protein:
Function:
Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly.
Subcellular Localization:
Mitochondrion matrix. Nucleus.
Sequence:
MASKTKLLSNKVYLQVLGTCSLDTTPSLLLFTDSQRYLFNCGEGTQRLFNEQKIKYNKLNNIFFTRICWERCGGLPGMAMTLRDSKKTTINIYGPENLKDLMNGTRFFIFHEKMKYVCTQYNGIKDTAFTDENLTLTPVVIQGINNDKSHDRKDENLNSEQQHPDKKIKLDPGLLKESISCYICQLVSVPGKFLLNKAKELGVPKGPLYGKLKNGENIILEDGTEVCPEQVTEPTSPGPVVLFIDCPCVDYIPNIVNNHSLCAFHEGPSNMAPVIIVHMVPMAVYNHPDYVSWSKKFGERTEHLLINSEVCSDHVAFRRQATIQCKLNTLDPSIFPLLYQSPKKDLPQFPIRTVPGAFCLQYHLRPLKQQGYSTSDVPEPLNVQELKNEAITAIKDIKKREDNSLGQGSVDDFDFEVVFIGTGASLPSKYRNVSSTLLSISNEHSVLLDCGEGTLGQLYRHYGNKADDVIRRISCVFISHMHADHHLRILKRCFSVKQVSDTAAHTLVIGPLRMRSWLTEYSSLCEHLDFRFDRDRFDRDRFDRDRFDRDRFDRDRFCRDRFCRDRFGRDKFVRVGLSISVVPVDHCAFAYGLVLSHVTGWKVVYSGDTRPCKELIDAGAGATLLIHEATLEDEMTSEAIEKKHSTTTEAISSGLEMSARFIMLNHFSQRYPKIPVFNEKFTKHTGIAFDHMTIRPRDFDKIPSLLPALKVLFAEEVEELTQNTEIRRNKLNANES
The following text describes a protein:
Function:
Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
Sequence:
MQADSEQEAVRGIQWVKNYKFDFRFQQWGQSNVTFTCVAGHIVAQDFPDRFRKWHSCQPADLFDAPIQSSIAEVRTNARVPASSLTDKTQDKKIVASNIEAQARYASILFIWTDCDREGEHIGTEIRDIALKVNPNMQVYRARFSNIERAWVILFPVDFNHVIQASQNPIRLDEAQANAVSARIELDLRLGAAFTRMQTMALQNMIPTQGDERGKVISYGSCQFPTLGFVVDRYLRVRNFVPEPFWYIKVAHTKDKIDVKFNWRRGHLFDRLAVIIIFERCLLAKTAKVMKMAKKPTKKWKPLPLTTVELQKNGSRFLRMTSQEVMKVAEDLYTKGWISYPRTETDQFDRGMDLRALVARQTQDNAWGQFAQSLMDGGFKQPRDGRNNDKAHPPIHPVNYVAPTQLNQNEKRVYEFVVRRFLACCSEDAAGEATDIEIDYGGEFFHAHGLTVIARNYLNVYPYDKWVSSQELPQYTVGETFEPTEANMHDGQTSAPAYLTEPELIALMDANGIGTDATMAEHIAKVQEREYVIARPKGGGAPANNDDGGGRGRGRGRGRGGARGGRGGRGGSAAQNERGATTGIQEFIPTTLGIALIEGYDNVGIETSLSKPFLRKEMEVQMKAICDGRTTRQEVVQQNIEQYRAVFTRTAQQINVLKSTGRLCEVLQAIRKYVLGEANHG
The following text describes a protein:
Function:
Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment (By similarity).
Subcellular Localization:
Nucleus, nucleolus.
Domain:
Although it shares weak sequence similarity with GTF2B/TFIIB, displays a similar subdomain organization as GTF2B/TFIIB, with a N-terminal zinc finger, a connecting region (composed of B-reader and B-linker regions), followed by 2 cyclin folds.
Sequence:
MHSAKNEKCNACGGYRFSVNDGFKYCDRCGALFENFEELEEEEGGLQQTVGQGKVKVRKNDDQKRVRNNAAPVNLPKAQVMREALEKRSDFLQQQAIKGEELELPHDATPDYLYRLALRLFSFTQILAKSGHILVHELNFESRVQENILATFQKYLAHCQVAFCHSEQCGNDEHLRFVAVMENLRYEQEEREEKQRKRMAKRGKGVNALSKSAAAWTLLTQGNITEHLDIASDEDGDQDAQGGQQLDDLTLETTQNPDESIRVNDTTMGFVRKVTTALSKEALRRASQLILNLEMLVAILHSALMSSGYQTILTSDVVRWIREDRFRISRRSIRLIRQSQPERMKQGEVVKPTIVDYAEPFLRFPLYEIMRTCTIFHQSLKLASSMAPQSFESMSARLVDNLNLPSDILSRMLILESIIPCDVSPQLLKQVDVDMGYNCGQLAAMSPNVYYSGFLTSFGRKERGTQDADFCDEVLLSPDAKLIAYLLLTLRLTFQLDNAQCALQDDQYFDVDSWIHQLEMRIKCWQGHNMSLVMRSSSHVPEMVVDPPFGTNYLFHQEKGAPQVSCRRRQAGFQKCIPTEMSFNSTSTLPTVFDVRHMGLLTERCQMEALISPVKFQRTVLGNEIERDPLTFENVDRQSKNTFFKHFSAFKTTESCDTFEEYFPCAKNYLLFKRPDWIQNCTARQTHFNPVTGPIRFYLSNQSCDDLLGTAATSFSRRFQFLLDALSLIIGEDKKAVYAAFVMLEMHLTSSERIQSIRDDLLTSSPITLKCQKFRNSTHHIPRKYGVISEVPIDRIENLRYFRLSRQFFEHEEMPTTINMELIDYRNQEIRDSVTETEVQRAQNRIMKLCYEFEQFFGILAVKFW
The following text describes a protein:
Function:
Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1. Does not enhance nucleosome sliding activity of the ACF-5 ISWI chromatin remodeling complex.
Subcellular Localization:
Nucleus.
Sequence:
MAAQESRLVSLPLSRIRLIMKSSPDVSNINQDALMVTAKATELFVQFLASHSYKHGTGKLTNTLTYTDLSSAAEESDTFQFLSDILPKKILASEYLEMLKAEQERDTDEEDSEEEEEEEDDDEEEEEDDDEEEEAGEEQEDD
The following text describes a protein:
Function:
Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNFSDQSVHECPMMDPMGLEEYLPDRNETGSNDSWFDNIPIAKYKQPMYIIIIFVVLYVIVFLLCIVGNLVVCCIIARTATLRDVTHSFILNLAVSDLLVGVFCIPFTLVGHIFTENYLGDVMCKVSPMLQGMSVATSVFTLTAIAFDRYCVIVHPTRDRLTVRQAVYLIIAIWVVAAIIMAPQAIVRRDESFQFGELNLSVCGEFWPSPLLRKAYSAFLFVICYAAPVLINTFLYGRTGYKLWMTKSAAAPKACSNQTEQRSRIIKMMVIIVAVFAITWMPLYSCWLLEDFGQLTHDQSAMLHSYIYPIAHVMAFANSAVDPFIYGLYSSNLRSRVAEICSRKKTKGNVLARDNNNDKKTPNIVCKPQSFTMNFQAVADNRIIPNESQE
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:
MDFEEETTVCTICHENKSKYTCPACEIKTCSLSCYNKHKYERDCTGKVDSNKYLNRNELAADPVHLNRDYNFLNNVDRKIHVGKEDIVKSAKNVFKRTRNQSQASGNKRYKRNEEDNTDKRITAVKKIFLNDPNISIKRENTLIVSLPIGMSRSNTNKTGFDKKLNSFVWTIEWIMLNEQGEQVTKFISYRLKESLVLQDSVPMNIINNKFTKPVEKCYLKFYLHDVIHKGKMIRLNGGDKISDVLKDKIVLEYPTIYVAANDECLQDRIIDSLQLAEEEEDDTTDSSEDDSSDSESDDDDSDSGSETSSIGDGSGEDNDSDSAPEETSSKLPPFSQKFFEASAEPKPIIEEIGSNKTVEEP
The following text describes a protein:
Function:
Transcriptional activator that binds specifically to the cis-acting element GCC box 5'-AGCCGCC-3', or to the CRT/DRE element 5'-[AG]CCGAC-3'. Plays an important role in root development via root cell expansion regulation. Transcriptional activator involved in the hypoxic stress response. Plays a role in low oxygen signaling and contributes to tolerance to anoxia stress by enhancing anaerobic gene expression and ethanolic fermentation. Plays a role in the regulation of hypoxia-induced root slanting. Contributes to the promotion of adventitious root elongation under hypoxia, an adaptation response that strengthens the root system in upper soil layers where oxygen shortage may last for shorter time periods. Transcriptional activator involved in the osmotic stress response. May play a role in defense response against the fungal pathogen Fusarium graminearum downstream of ethylene signaling.
Subcellular Localization:
Nucleus.
Sequence:
MCGGAIISDFIWSKSESEPSQLGSVSSRKKRKPVSVSEERDGKRERKNLYRGIRQRPWGKWAAEIRDPSKGVRVWLGTFKTADEAARAYDVAAIKIRGRKAKLNFPNTQVEEEADTKPGGNQNELISENQVESLSEDLMALEDYMRFYQIPVADDQSATDIGNLWSYQDSN
The following text describes a protein:
Function:
In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum lumen. Nucleus.
Sequence:
MSVVGFDFGNESGVVAVARQRGIDVVLNDESKRETPAIVCFGEKQRFLGTAGAASSMMNPKNTISQIKRLIGRQFSDPELQRDLKALPFSVTEGPDGYPLIHARYLGEMRTFTPTQVLGMVFSDLKTIAEKNLNAAVVDCCIGIPIYFTDLQRRAVMDAATIAGLHPLHLIHETTATALAYGIYKTDLPENDPLNVAFIDVGHASLQVCIAGFKKGQLKILAHSFDRNLGGRDFDEALFQHFAAKFKEEYKIDVFQNARACIRLRAACEKLKKVLSANPEAPLNIECLMDEKDVRGFIKREEFEQISIPILERVKKPLEKALAEAGLTTENIHAVEVVGSSSRVPAIMRILTEFFGKEPRRTMNASECVAKGCALQCAILSPTFKVREFQVNESFPFPIALSWKGPAPDAQNGALEYHQSTIVFPKGNPIPSVKALTFYRSGTFTIDVQYADVSELQAPAKISTYTIGPFQSAKGERAKLKVKVRLNLHGIVSVDSATLLEEEEVEVPVVKEAVKEPAKMETDEASGDAAAPTTSESDVNMQDAKGAGDASGAENGVPEFGDRPVKMETDAKVEVPKKKVKKTSIPVTEIVYGAMAAADVQKAVEKEFEMALQDRVMEETKDKKNAVEAYVYDMRNKLSDKYQEFVIDSKREQFIAKLQEVEDWLYEDGEDETKGVYIAKLEELKKQGDPIEQRYKEYTERGSVFDQFVYCINSYREAAVSNDPKFDHIDLAEKQKVLNECVEAEAWFREKKQQQDVLPKYANPVLLSADVRKKAESLDRVCRPIMTKPKPVRPATPETPSSQPPQGGEQQPQGAESPNSGNANATEGASAGSEVPPATEPMDTDKSETAPSAS
The following text describes a protein:
Function:
Promotes megakaryocyte differentiation by up-regulating RUNX1 expression. Regulates RUNX1 expression by activating the proximal promoter of the RUNX1 gene and by enhancing the translation activity of an internal ribosome entry site (IRES) element in the RUNX1 gene.
Sequence:
MSHGHSHGGGGCRCAAEREEPPEQRGLAYGLYLRIDLERLQCLNESREGSGRGVFKPWEERTDRSKFVESDADEELLFNIPFTGNVKLKGIIIMGEDDDSHPSEMRLYKNIPQMSFDDTEREPDQTFSLNRDLTGELEYATKISRFSNVYHLSIHISKNFGADTTKVFYIGLRGEWTELRRHEVTICNYEASANPADHRVHQVTPQTHFIS
The following text describes a protein:
Function:
Displays esterase activity toward palmitoyl-CoA and pNP-butyrate.
Sequence:
MKHDHFVVQSPDKPAQQLLLLFHGVGDNPVAMGEIGNWFAPLFPDALVVSVGGAEPSGNPAGRQWFSVQGITEDNRQARVDAIMPTFIETVRYWQKQSGVGANATALIGFSQGAIMVLESIKAEPGLASRVIAFNGRYASLPETASTATTIHLIHGGEDPVIDLAHAVAAQEALISAGGDVTLDIVEDLGHAIDNRSMQFALDHLRYTIPKHYFDEALSGGKPGDDDVIEMM
The following text describes a protein:
Function:
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Subcellular Localization:
Nucleus. Mitochondrion.
Sequence:
MPPRTRLRTATLQRTKSAPASSVQKLPAKDASPMKRPAPSQGTSPEKSPSKKKPKTIVKQALLIPVPPPARWKETYGLIEEQRKTFIAPVDTMGCDKAGDVGPDYQLKSASDSTISQDKIDQLKQRSERDRRLSCLVSLMLSSQTKDEVTAQATLNLRLHLKDSLTVDSLRNASLTEIENCINKVGFWKKKAQYIKLMADDLFLKHESDVPKTLDELVALKGVGPKMAFLALSNAWAINLGIGVDTHVHRISNRLGWLQTSDPEATRINLESWLPRDLFQEINHLLVGFGQVICLPVGPKCEDCYVGKVPGLCPSSKVEANRQKLKLQSTKRAKFTASSTPSPKKPSRAHIAIKLEETDAVDHPDQKTSKQSPRLRSSRFFQNGHHSVKQEGQDPVIKDEDQDQGEKPEVDNKPTRPKSENGNLSQEINNNSEKLIHSPLVSSPLSEIDDDSNPLLCSPSPALAW
The following text describes a protein:
Function:
Involved in the biogenesis of the 60S ribosomal subunit in the nucleus.
Sequence:
MPKIQKIKAAEKVVHPYSRKAGYLAREESKLKKKERLKNEKATRLNNIGEKLLWFQSQLDSTKSNYTRKDACEIIERYLHRFDAELEQIDLMNGIKGRQGRLHGAREAAIKQTVERERAQYEGIGFEIPDIMNGKHLKTFREWTGDLRKLPNIKLRKVSNKGLGTKNEGKEDVEEEHKEDKDDCSYEDESAQMSDSH
The following text describes a protein:
Function:
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MIFKFHHINTKQVGCLCLDYLAQFLLFEEDNPSETNGNSSLMVLCDVDSAKEFILCDYNRDAHSYRSPWSNKYHPPLDGGMYPSPELRTHEIEENEVLGVYRDQYYEGGTSSVYLWKDDEKEGFLACFLIKKRSVLTVGPEVEGMADYCITSTVMLSMTIDHENSGNFSLSGSMLRLYQVSLPEGSLKPSSLKCLELSDTKSEEMVIAISQD
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; Multi-pass membrane protein.
Sequence:
MFTKSHKTFRFDSIVKSKHTETAITVCVREMVKSATTKDDAHALFHSLRSAYSATPTNLKIIDLYVVFAVFTALIQVVYMAIVGSFPFNSFLSGVLSCVGTAVLAVCLRIQVNKENKEFKDLPPERAFADFVLCNLVLHLVIINFLG
The following text describes a protein:
Function:
ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell. Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane; Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MVVAEVASPAVAASTILSSLLTHPLHRVRALMAVSGELHAQNKADILAVCSPSACAQWQFKQGGVESIWHGALDSIALGLVPSLLLRPIIESLCMPAADASPATRIGLALAQSLLHLSLTYPLSLCALKTTQDVPVNGHYRYTSGFHALREAFSAGVESAVPRLYRGLGLSVAGVLVYRLSYAGMLSLMPSRIGPANTFLTAIAAGMLAYPLDVLRRRYIALDPVDMRSSWQYARDMIRSEGFQAFYFGNMMAMVENLSNRIALMQIYPLVARTRTFGGLSS
The following text describes a protein:
Function:
Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin.
Sequence:
MITILLFANLREEVGSDRLVISEKQEMTVQQLKEWLKASYCLQSLDKVMVAVNEEFVMNEEMIKAGDIVALIPPVSGG
The following text describes a protein:
Function:
Catalyzes the carboxylation of acetone to form acetoacetate. Has a reduced activity on butanone, and no activity on 2-pentatone, 3-pentatone, 2-hexanone, chloroacetone, pyruvate, phosphoenolpyruvate, acetaldehyde, propionaldehyde and propylene oxide.
Sequence:
MNVTVDQSTLAGATRGIVRGGETLKEHRDRLMAATKATGRYAGLKTLELREREPILYNKLFSRLRAGVVDARETAKKIAASPIVEQEGELCFTLYNAAGDSLLTSTGIIIHVGTMGAAIKYMIENNWEANPGVHDKDIFCNNDSLIGNVHPCDIHTIVPIFWEGELIGWVGGVTHVIDTGAVGPGSMATGQVQRFGDGYSITCRKVGANDTLFRDWLHESQRMVRTTRYWMLDERTRIAGCHMIRKLVEEVVAEEGIEAYWKFAYEAVEHGRLGLQARIKAMTIPGTYRQVGFVDVPYAHEDVRVPSDFAKLDTIMHAPCEMTIRRDGTWRLDFEGSSRWGWHTYNAHQVSFTSGIWVMMTQTLIPSEMINDGAAYGTEFRLPKGTWMNPDDRRVAFSYSWHFLVSAWTALWRGLSRSYFGRGYLEEVNAGNANTSNWLQGGGFNQYDEIHAVNSFECAANGTGATAVQDGLSHAAAIWNPEGDMGDMEIWELAEPLVYLGRQIKASSGGSGKYRGGCGFESLRMVWNAKDWTMFFMGNGHISSDWGLMGGYPAASGYRFAAHKTNLKELIASGAEIPLGGDTDPENPTWDAMLPDAQIKRDKQAITTEEMFSDYDLYLNYMRGGPGFGDPLDREPQAVADDINGGYVLERFAGEVYGVVVRKGADGQYGVDEAGTAAARAQIRKDRLAKSVPVSEWMKGEREKILAKDAGTQVRQMFAASFKLGPRFEKDFRTFWSLPDSWTLPEEEIGVPTYGSRYSMDISELPDVHTVQFVEE
The following text describes a protein:
Function:
Required for the positioning and movement of chloroplasts. Interacts with profilin and actin independent of its polymerization status. Regulates chloroplast localization by anchoring chloroplasts to the plasma membrane and forming a bridge to the actin cytoskeleton.
Subcellular Localization:
Plastid, chloroplast outer membrane; Peripheral membrane protein; Cytoplasmic side.
Domain:
The N-terminal region (1-25) is necessary and sufficient for targeting and anchoring the protein in the chloroplast envelope membrane; The coiled coil domain(123-341) interacts with the plasma membrane and anchors chloroplasts firmly on the plasma membrane; The actin binding motif (346-356) can function in vitro as an actin binding site; The proline-rich domain (648-705) mediates the interaction with profilin.
Sequence:
MFVRIGFVVAASIAAVTVKRLNVKPSKPSKPSDNGEGGDKEQSVDPDYNLNDKNLQEEEEEEEEEVKLINSVINQTRGSFSDYLDDDILPEFEDLLSGEIEYPLPDDDNNLEKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYYGLKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVREEVNNLKHNNEDLLKQVEGLQMNRFSEVEELVYLRWVNACLRYELRNYQTPAGKISARDLSKNLSPKSQAKAKRLMLEYAGSERGQGDTDLESNYSQPSSPGSDDFDNASMDSSTSRFSSFSKKPGLIQKLKKWGKSKDDSSVQSSPSRSFYGGSPGRLSSSMNKQRGPLESLMIRNAGESVAITTFGQVDQESPGTPETPNLPRIRTQQQASSPGEGLNSVAASFHVMSKSVDNVLDEKYPAYKDRHKLAVEREKHIKHKADQARAERFGGNVALPPKLAQLKEKRVVVPSVITATGDQSNESNESNEGKASENAATVTKMKLVDIEKRPPRVPRPPPRSAGGGKSTNLPSARPPLPGGGPPPPPPPPGGGPPPPPGGGPPPPPPPPGALGRGAGGGNKVHRAPELVEFYQSLMKRESKKEGAPSLISSGTGNSSAARNNMIGEIENRSTFLLAVKADVETQGDFVQSLATEVRASSFTDIEDLLAFVSWLDEELSFLVDERAVLKHFDWPEGKADALREAAFEYQDLMKLEKQVTSFVDDPNLSCEPALKKMYKLLEKVEQSVYALLRTRDMAISRYKEFGIPVDWLSDTGVVGKIKLSSVQLAKKYMKRVAYELDSVSGSDKDPNREFLLLQGVRFAFRVHQFAGGFDAESMKAFEELRSRAKTESGDNNNNNNNNSNEEESVN
The following text describes a protein:
Function:
Negative regulator of the Ras-cyclic AMP pathway. Negatively regulate the activity of normal but not mutationally activated Ras proteins. The down-regulatory effect of RPI1 requires the presence of one of the two Ras GTPase activators, IRA1 and IRA2.
Miscellaneous:
MISCELLANEOUS: Present with 1340 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MYLEYLQPKLNLMDESSTISKNFPDYSPNLNTPITSNFNEETGSDCSLVTPRIISSSNSNSNSNSNSNSNSNSGSIDENELNNSNSSSSSARQIRKKWKEPEDIAFITTIMNNSQLLTFVEYFKPMKNFWKKISKILFQQYGYERNSRQCHDRFKVLYTKSLKVHPSKKSKQKKKKSKQEAGSNLNFDPSKLSRMQYLLVQLQNTFSFVNGNIILKSQKTLKPNKNGTNDNINNHYYNNCNNNNNNINNSNNSNNNNSNNINRNSNHSTNVFSTPEHIQSSINLDKLESLPALDTKGEPSFISPAQFSLLSSAPADNLILQTPPSPFFQQTMPIQLPRDAQQEQISPVFSTDVIYMWQTMFNTIENLKEQVNCLKNEVKQLNHKFYQQNKPLHNMSTSDSENFMQQH
The following text describes a protein:
Function:
Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates.
Miscellaneous:
MISCELLANEOUS: Present with 3500 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MTIEKPKISVAFICLGNFCRSPMAEAIFKHEVEKANLENRFNKIDSFGTSNYHVGESPDHRTVSICKQHGVKINHKGKQIKTKHFDEYDYIIGMDESNINNLKKIQPEGSKAKVCLFGDWNTNDGTVQTIIEDPWYGDIQDFEYNFKQITYFSKQFLKKEL
The following text describes a protein:
Function:
Catalyzes the decarbonylation of fatty aldehydes to alkanes. Requires the presence of ferredoxin, ferredoxin reductase and NADPH for in vitro decarbonylase activity (By similarity). Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane.
Sequence:
MPQLEASLELDFQSESYKDAYSRINAIVIEGEQEAFDNYNRLAEMLPDQRDELHKLAKMEQRHMKGFMACGKNLSVTPDMGFAQKFFERLHENFKAAAAEGKVVTCLLIQSLIIECFAIAAYNIYIPVADAFARKITEGVVRDEYLHRNFGEEWLKANFDASKAELEEANRQNLPLVWLMLNEVADDARELGMERESLVEDFMIAYGEALENIGFTTREIMRMSAYGLAAV
The following text describes a protein:
Function:
Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). Involved in mid-late stages of complex I assembly.
Sequence:
MIKKILFNSQLYKFCVHQKIYKPKSKKGLNLLLFLFSLGFINQYTKYRDYMSNIFLSQQEVADFHKNKQLQVDKKTLRYHEINIKRNKDTETAVIIGGGIVGLSQALKLLQKGYSVILIEKEQFISTKCSAFNGNIYNPYLFNPLISKYSIKTMLNNYINPTDTATQRFSFNSLLEPGGIIWLINALRLSTSDEQFDKSIQDMTKLGQIQEQEFEKIKKMGLLEKQLTAEGELSFYKSAEYGKRISQSFENAGIEFKEVDKTKFNQHDIDRHLFQNYPYVIKLDKENNLDTKQLSINTLKYCQKHYPNKFNILYGTDFKEFIMNNNRYVLGINTNKGVIYGDAFIICAGLHSKYITKKLGVTLPIMPCRGWIIESELPQSAKGSVLDKMVLKLPTLSVTNLNNKLRISGCQLIDQEYKSDDPLNEWGAQILIKQMKEQFNIDLDRQSISVRDCCRPLTPDDKIILSKLQLNRNVYVNAGHGSRGMSQCHGCAEVIYQLMKGQQNKEDYSAFDLTRFLFV
The following text describes a protein:
Function:
Binds preferentially DNA with A/T-rich content.
Sequence:
MSTHKPTAAVISAQPESNGETRNGQSFKSYPPATAQFEDIVRSSDLFWEKLKAFHKSFGTKFMVPTVGGKALDLHHLFVEVTSRGGLEKVIKDRKWKEVIGVFSFPSTITSASFVLRKYYLSLLYHFEQVYLFQKQGPSVSIPDAMNGNFVNGSAAQDEGATVNQFPGPELQLGTSVTGYIDGKFDDGYLVTVNLGCDQLKGVLYHIPQAFVSQGSNSSDVPPRRRRKRSRLSLHDPSQPKSYRSGYNFFFSEHYALLKPLHYGEEKLICKKIGMLWNNLTDAEKQVYQEKGLKDKERYRTEMLECRSSVAQ
The following text describes a protein:
Function:
May be involved in synaptic plasticity regulation through the control of Rac-GTP levels.
Subcellular Localization:
Postsynaptic density.
Sequence:
MSSGSVLSLGNSRLPARVSHTFSGSGSWRACCLERWMTCGSRASSPRIVKLGTLGTMQRAGAGARRASDCGPAPYRPRCIAKFAQYVGSFPVDDLDTQESVCLVQQHLWALQDCSRRRAVILKFSLQGLKIYSGEGEVLLMAHALKRILYATWNPAACQFAFVARNPRSPASKLFCHLFVGSQPGEINILYLLLCRSFQLAYLLQHPEERAQPEPSLVPGGDMSLKPLCSPGVAPALVREPFSRDQLSQNVHALVSFRRLPAEGLLGSNGKELPEPEGRGGTRHIRLGNPYCSPTLVRKKAIRSKVIRSGAYRGCTYETQLQLSAREAFPAAWEAWPRGPGSPSCLVENEGSLTENIWAFAGLSRSCALALLRRDVHGAFLLWPEPGTSGQWSLSVRTQCGVVSHQVFRNHLGRYCLEHLPAEFPSLEALVESHAGMERSLFCPLSMGRLNPTYEEQDSGPEGRFPRTLRPLSHAKSEAELQGLG