lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (By similarity). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (By similarity). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (By similarity). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (By similarity). Within the complex, RAD50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11. RAD50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the MRE11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form.
Subcellular Localization:
Nucleus. Chromosome. Note=Localizes to DNA double-strand breaks (DSBs).
Domain:
The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11 homodimer.
Sequence:
MSKIEKLSILGVRSFGPHHPETIAFNTPLTLIVGYNGSGKTTVIECLKYATTGELPPNSTRNGAFIHDPDLVGEKEVRAQVKLSFRSTIGESYVVTRNIQLLVQRNNKRTQKTLEGSLLLRNNGERTVISTRVAELDKLVSEKLGVPPAILDAVIFCHQDDSLWPMSEPAALKKRFDEIFEAQKYTKVIENIRLLKKKKGDELKILKEREVQDKANKERAEKVDRLMAQLTREILEAREKCNELSKQMEEESAKIKDKYEQANSFLKIMNDLQTKTEKLEYKKDAIVELRSRIEELPDPDEVLRNTLDEYEQTINRIVADRDHKAAQFHDLQAELKSARDQHTAKAAEQGKHQSDKEKYERQLVARERMIREAAERHEIRGYNGDLDDRRIAIFNERIQKILNDKRRELERLQRENQEELDRKTAVIAERESRKQSVIRDRKAAKDRIISLGKDMASIQGELSSIDIDEGTEEMLRAEMKELQARIEAAKADEQNANLDAQIKEVNEEIWKLESLSAKLARELVECTRLASERAQLDLRRKQLAERKRELEIMTNTWNEQFSTLLGEGWRPETLERDFSDVLKQQQLLVGEHRKKKDATQQELKQAEYQLSNARNLHNKLTNEMEACMRAVQTAMKEARDLDSAPPVDEYITMLETDEKELAEVETALKLYDELKKHYSTIKDRALRFNKCYICDRDFTNQEAAKTRLLEKVAKRLGDEEKKELLEDQAAFMKSLDILRAVRVKYDTYQRLSSELPQLSREIDSETNRREDLVRRLEDQDLAFREADNKLQEMETLNKHVMKITQLLKDISDAEKQVERSQQLSNIETRSADEINEEQTTCAEQTRAAQAKLTKLTAEKQRLKDLVRQLEVERLQLENKISSAVQQLERKKRLQESIARHKEDQNQARNAVQEADEELERLEPEIAGARAALDEARQACRAKEQKVAAERDAIAQTVSELNMINSEIQEYLDRGGPSSLAANQRAIANLETQMANLEGEMRELTVQINKLNKEIDNSDAKKRNIADNLTYRKNLREKDALEREIAELEARNAQEDYDRLIKEAHYLEAHRSKLNADRERLMGMMSTKDEEFRRLNEEYELDLKDAKAKYKETHIKVETTKAAIEDLGRGMAAVDHAIMQYHSKMMEQINRTIAELWQSTYQGTDIDTIQIRSDVESTTSSDSGTRRNYNYRVSMVKGDTEMDMRGRCSAGQKVLASIIIRLALAESFCANCGLIALDEPTTNLDSDNIRSLAESLHGIIKARQAQGNLQLIVITHDEEFLKYMQCSDFCDDFYRVKRDEKQNSVIVRESITRITE
The following text describes a protein:
Function:
Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).
Subcellular Localization:
Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass membrane protein.
Sequence:
MGTIIQFLVVSCLLAGAGSLDPAALMQIGVIPTNVRQLMYYTEASSAFIVVKLMPTIDSPISGCNITSISSYNATVTKLLQPIGENLETIRNQLIPTRRRRRFAGVVIGLAALGVATAAQVTAAVALVKANENAAAILNLKNAIQKTNAAVADVVQATQSLGTAVQAVQDHINSVVSPAITAANCKAQDAIIGSILNLYLTELTTIFHNQITNPALSPITIQALRILLGSTLPTVVEKSFNTQISAAELLSSGLLTGQIVGLDLTYMQMVIKIELPTLTVQPATQIIDLATISAFINNQEVMAQLPTRVMVTGSLIQAYPASQCTITPNTVYCRYNDAQVLSDDTMACLQGNLTRCTFSPVVGSFLTRFVLFDGIVYANCRSMLCKCMQPAAVILQPSSSPVTVIDMYKCVSLQLDNLRFTITQLANVTYNSTIKLESSQILSIDPLDISQNLAAVNKSLSDALQHLAQSDTYLSAITSATTTSVLSIIAICLGSLGLILIILLSVVVWKLLTIVVANRNRMENFVYHK
The following text describes a protein:
Function:
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Subcellular Localization:
Chromosome, centromere, kinetochore. Nucleus.
Sequence:
MRRQTLGMLNIGNQPRQPQEKKKSLGSRRQSTGGRLSLSGRPSGIRRSSQYGAGSSQVVKDPRPLSDKGYQQKMIRTLTEFLTEFNYPHPISNRILSAPPMKEFKRIFLFIYKYVNDSSKVQTAIEKKPEEEIPKILKMLGYPFNISKSSMFSVGSPHTWPNLLGALCYLIELIRYCIELSDSDNILFLEDACEGADAGDGPSYFDKCYFEYLEKSYSAFLMGKELDELEEYDHDFYQQIRSKYNAKYQELDELKTENAELENELAKLEGMSMLQDCIQQKKGLAADEEKFRKYIGDLKRHSTKMEESDAQTEEEIQAIRLELEEITRENTQLQTQLNQQELSPADVENMKKEKQECKKMVQTLEQKRDGIDQQIWEQEMKFAKTHEETHKLVSEYNVTARKLKLIPASAPNALGLDLEMRFNPMDMQPDFGKHFKAKIKNPLISLKQKIAESTREIQSHKITEVESLDQITDMVESKKEEAEALEAKLAGLDKGLEWRKDVMNKEYTRLASELQAQEDKVLNMKQQVQAGTEKKEQELREVQERAESRLQEMANMHKEYDDFLGRAGMLVMDHKTIMQVMNKEYTRLASELQAQEDKVLNMKQQVQAGTEKKEQELREVQERAESRLQEMXNMHKEYDDFLGRAGMLVMDHKTIMQNRVSEIQQLAKDQLNQAKRPNS
The following text describes a protein:
Function:
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Sequence:
MLVVAAMRVWNPEEGWANRVGRKREGKIVEILRRVTMTAHGLSHFPRQLLRMPRAALRKPNPALDLDSWLKTPEDLPATINSQTLFGNDQPLEIEVGSGKGLFIQTESDRRPEHNYFGIEIARKYAAHAAARLAKRERANAKMLAGDATPLFAVTDEGKRIEDGSLDGVHVYFPDPWWKKRHRKRRVLSHDNILNFSRCLRVGGRLHFWTDVLDYFELTVELIAEIAPELGVPLPETQRESTHDLDFHTHFERRSRKMGIPVYRVCYRKRS
The following text describes a protein:
Function:
Beta-1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAc-beta-1-3GlcNAc, on N- and O-glycans. Has no galactose nor galactosaminyl transferase activity toward any acceptor substrate. Involved in alpha-dystroglycan (dag1) glycosylation.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein. Endoplasmic reticulum.
Sequence:
MRSAAAALSVCVLAVLLHWICWTDRSAELLGFRAADRPKADVREVLVGVLSARHNHELRQAIRDTWLGYLKQHPHFQNRVLVKFIIGAQGCSVPLEDLEDQYSCSQLELSEAAVSGQEMAILSVPDSSALLQSDVPVLSLDFKVLHSVVITQLGVFPNKPPHYLKGNITVRLLQVDQEEAVISARFSSVSPGTAADGMFYKPVEQFILPKGFEGTLLWEAEDSTALMSVNTSALRLNNGGGVLHFRSIEEGTLPHRNALGFPGLAGGFTFTVYDVEVLSEMLRGRSGRQKIREAQLKGEDEALQEESLRHGDMVFVDVVGTYRNVPSKLLQFYKWSVENADFSLLLKTDDDCFIDVDAVLMKMQRRRLTHTSLWWGNFRQNWAVDRVGKWQELEYASPAYPAFACGSGYVVSRDLVQWLASNAQHLKAYQGEDVSMGIWMAAVGPRKYQDSGWLCEKECYVDMLSSPQHSAEELRLLWSRKNKCGDPCGCS
The following text describes a protein:
Function:
Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.
Subcellular Localization:
Secreted, extracellular space.
Sequence:
MAATGRFTAFWNVASVPALIGILPLAGSHLRAVLCPVCIWRHSKAVCAPDTLQAMRAFTRVTAISLAGFSCFAAAAAAAFESLRAVPDGWIYESTPDPNQPLRLRIALKQHNVAGFEQALLDMSTPGHSSYGQHFGSYHEMKQLLLPTEEASSSVRDWLSAAGVEFEQDADWINFRTTVDQANALLDADFLWYTTTGSTGNPTRILRTLSYSVPSELAGYVNMIQPTTRFGGTHANRATVRAKPIFLETNRQLINAISSGSLEHCEKAITPSCLADLYNTEGYKASNRSGSKVAFASFLEEYARYDDLAEFEETYAPYAIGQNFSVISINGGLNDQDSTADSGEANLDLQYIIGVSSPLPVTEFTTGGRGKLIPDLSSPDPNDNTNEPFLDFLEAVLKLDQKDLPQVISTSYGEDEQTIPEPYARSVCNLYAQLGSRGVSVLFSSGDSGVGAACQTNDGKNTTHFPPQFPASCPWVTAVGGTNGTAPESGVYFSSGGFSDYWARPAYQNAAVESYLRKLGSTQAQYFNRSGRAFPDVAAQAQNFAVVDKGRVGLFDGTSCSSPVFAGIVALLNDVRLKAGLPVLGFLNPWLYQDGLNGLNDIVDGGSTGCDGNNRFNGSPNGSPVIPYAGWNATEGWDPVTGLGTPDFAKLKALVLDA
The following text describes a protein:
Function:
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Sequence:
MFPSLFRLVVFSKRYIFRSSQRLYTSLKQEQSRMSKIMEDLRSDYVPLIASIDVGTTSSRCILFNRWGQDVSKHQIEYSTSASKGKIGVSGLRRPSTAPARETPNAGDIKTSGKPIFSAEGYAIQETKFLKIEELDLDFHNEPTLKFPKPGWVECHPQKLLVNVVQCLASSLLSLQTINSERVANGLPPYKVICMGIANMRETTILWSRRTGKPIVNYGIVWNDTRTIKIVRDKWQNTSVDRQLQLRQKTGLPLLSTYFSCSKLRWFLDNEPLCTKAYEENDLMFGTVDTWLIYQLTKQKAFVSDVTNASRTGFMNLSTLKYDNELLEFWGIDKNLIHMPEIVSSSQYYGDFGIPDWIMEKLHDSPKTVLRDLVKRNLPIQGCLGDQSASMVGQLAYKPGAAKCTYGTGCFLLYNTGTKKLISQHGALTTLAFWFPHLQEYGGQKPELSKPHFALEGSVAVAGAVVQWLRDNLRLIDKSEDVGPIASTVPDSGGVVFVPAFSGLFAPYWDPDARATIMGMSQFTTASHIARAAVEGVCFQARAILKAMSSDAFGEGSKDRDFLEEISDVTYEKSPLSVLAVDGGMSRSNEVMQIQADILGPCVKVRRSPTAECTALGAAIAANMAFKDVNERPLWKDLHDVKKWVFYNGMEKNEQISPEAHPNLKIFRSESDDAERRKHWKYWEVAVERSKGWLKDIEGEHEQVLENFQ
The following text describes a protein:
Function:
Heme-binding protein which promotes neuronal but not astrocyte differentiation.
Miscellaneous:
MISCELLANEOUS: Non-classical progesterone receptors involved in extranuclear signaling are classified in 2 groups: the class II progestin and adipoQ receptor (PAQR) family (also called mPRs) (PAQR5, PAQR6, PAQR7, PAQR8 and PAQR9) and the b5-like heme/steroid-binding protein family (also called MAPRs) (PGRMC1, PGRMC2, NENF and CYB5D2).
Subcellular Localization:
Secreted.
Domain:
The cytochrome b5 heme-binding domain was proven to bind heme, although it lacks the conserved iron-binding His residues at position 73 and 106.
Sequence:
MLRICGLGVVLSLAVAAAAVLAVWLMDWWGSHPSIRLFVPEELARYRGGPGDPGLYLALLGRVYDVSSGRKHYEPGAHYSGFAGRDASRAFVTGDYSEAGLVDDVNGLSSSEILTLHNWLSFYEKNYVFVGRLIGRFYGKDGLPTSELTQVEAMVTKGMEANEQEQREKQRFPPCNAEWSSAKGSRLWCSQKSGGVHRDWIGVPRKLYKPGAKEPHCVCVRTTGPPSDQQDNPRHSNRGDLDNPNLEEYTGCPPLAVTCFFPL
The following text describes a protein:
Function:
Cleaves a number of carotenals and carotenols in the all-trans configuration at the 15-15' double bond producing retinal or retinol, respectively. Also shows activity toward lycopenals and the corresponding alcohols. Does not cleave beta-carotene or lycopene.
Sequence:
MVTSPPTSSPSQRSYSPQDWLRGYQSQPQEWDYWVEDVEGSIPPDLQGTLYRNGPGLLEIGDRPLKHPFDGDGMVTAFKFPGDGRVHFQSKFVRTQGYVEEQKAGKMIYRGVFGSQPAGGWLKTIFDLRLKNIANTNITYWGDRLLALWEGGQPHRLEPSNLATIGLDDLGGILAEGQPLSAHPRIDPASTFDGGQPCYVTFSIKSSLSSTLTLLELDPQGKLLRQKTETFPGFAFIHDFAITPHYAIFLQNNVTLNGLPYLFGLRGAGECVQFHPDKPAQIILVPRDGGEIKRIPVQAGFVFHHANAFEENGKIILDSICYNSLPQVDTDGDFRSTNFDNLDPGQLWRFTIDPAAATVEKQLMVSRCCEFPVVHPQQVGRPYRYVYMGAAHHSTGNAPLQAILKVDLESGTETLRSFAPHGFAGEPIFVPRPGGVAEDDGWLLCLIYKADLHRSELVILDAQDITAPAIATLKLKHHIPYPLHGSWAQT
The following text describes a protein:
Function:
Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MENHRSVFSNVIGDIVEKPPKQLVEVKRSVQRHARGFPAVSRTLPKRESKSMSAYKEKMLRKNKESPGLEGKGNLDDQGIDEENRVRLERMNDLEIEGAQEEIRATIRDDLLEMLKKRAFKKKAERELAQRKDRSSQVNTPDLSQRPSDDSFLSNEKLRSSEKLNRNLQSVLSSEAVDSSSGSPSPPMALSQAEIRSRQTKRVMFPDKAEELTKIFSLPTLAPIKGNEEDDASEDAKHSPKKHSPALSDGTTSNDGAPLEFDTTHLPEKQVTLDPNDPSFYEQLHDKYFPNLPVDEKQMQWLHDPSPAENSYHPSVESLHAHEIRFGFKGEIITPSQSQTIPVNEGLHHHGDAPFSAGYTLVELAHLLRSSFPTQRCIAIQTIGRIIYRLNSGEFREVLSPELHTLVEDAHIYELLAAAASDQVKHLTVRSLAIEALWLCSQSQHGSSRSAV
The following text describes a protein:
Function:
Plays an essential role in viral DNA replication. Does not seem to participate in the initiation step but is rather important for the amplification of DNA. Also required for expression from the vp39 and polh promoters.
Subcellular Localization:
Virion. Host nucleus. Host cytoplasm. Note=Colocalizes with the active viral DNA replication sites in the nucleus of infected cells.
Sequence:
MANASYNVWSPLIRASCLDKKATYLIDPDDFIDKLTLTPYTVFYNGGVLVKISGLRLYMLLTAPPTINEIKNSNFKKRSKRNICMKECVEGKKNVVDMLNNKINMPPCIKKILNDLKENNVPRGGMYRKRFILNCYIANVVSCAKCENRCLIKALTHFYNHDSKCVGEVMHLLIKSQDVYKPPNCQKMKTVDKLCPFAGNCKGLNPICNY
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER).
Subcellular Localization:
Cytoplasm.
Sequence:
MGREHLSNEEFFAQLGNLFEHNRKKGHGTVYLTQKRLAFDSASVPPSPQKVADDPLWDTHPETPLPILIRAHNNKSDKKAGTDRKDVDKIVLSTVVKPDDLDGFYVRYAEACKTGMSGLKKRDRKKGKKDKKKKKVAV
The following text describes a protein:
Function:
Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Subcellular Localization:
Cytoplasm.
Sequence:
MAFKSSFDELIKDIKSISFSNNPSNGETAQPASSKPDNGVNMKSKFLETWNNFRYVKNMRSDPSFKKDSPLWLLGKCYHLKKPSLSSDTSENAGEPTQNNLTVILIHLKLFLVDFHSKLWFTYRKGFPTLNDTNLTSDTGWGCMLRTAQMMIAQSFIVHLLGRNWRWTPSRLSMEQSDIHRNIITWFLDEQNIRCPFSLHQLTEIECIALHLGILVCYLIAVLLHSKNAPLHLFLIKSLQTTGLSYRCKPGNWYGPNTAAYIMQDALECAKGKTELLNNIMVYIAQDSTVYIDDVIEMCEWKNTASDADLKTSTTSSNRSVIVLIPVRLGEATLNPIYIPCIQSMLTLDQSVGIMGGKPKHSLYFIGFQDEYLFYLDPHYCQQADHPAAFKNDLLQNYHCNSPRKTNISKMDPSCCLGFYCRDYKDFQSFVCEANKFLSPPKQKMSYPLCLIMKGSALDHFSLASTKSLLTNIYKSKSPKPDRKFRSMEEEFELL
The following text describes a protein:
Function:
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in endosomal cargo sorting.
Subcellular Localization:
Endosome.
Sequence:
MSDDVDSETRSRTPSISSRQFIIPEDELATLDSENSSLDSGGEEASSGGSDAYSAAGGSTPVFSRLGQHPSTFFTGSQVAPIFDTSLYLFESLTQSLDSVDFSEALSLQTKTSATINSKSRELQLLVGEVQTHLRRLQTAFEQGQHTAQRVRHNLRDITRGVESLKQTFARSYPIEYHQALERAYERRAE
The following text describes a protein:
Function:
Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. May play a pivotal role in the control of anaphase.
Subcellular Localization:
Nucleus.
Domain:
TPR repeats 1-7 mediate homodimerization while TPR repeats 8 and 10-13 bind to hcn1, burying its N-terminal acetyl-methionine.
Sequence:
MVVKRTQTDSRMQSTPGNHNHPDAHANAAYMTPPSMGALNANNSNSQLSTLTISPMTYLANNTSTDGSFLKERNAQNTDSLSREDYLRLWRHDALMQQQYKCAAFVGEKVLDITGNPNDAFWLAQVYCCTGDYARAKCLLTKEDLYNRSSACRYLAAFCLVKLYDWQGALNLLGETNPFRKDEKNANKLLMQDGGIKLEASMCYLRGQVYTNLSNFDRAKECYKEALMVDAKCYEAFDQLVSNHLLTADEEWDLVLKLNYSTYSKEDAAFLRSLYMLKLNKTSHEDELRRAEDYLSSINGLEKSSDLLLCKADTLFVRSRFIDVLAITTKILEIDPYNLDVYPLHLASLHESGEKNKLYLISNDLVDRHPEKAVTWLAVGIYYLCVNKISEARRYFSKSSTMDPQFGPAWIGFAHSFAIEGEHDQAISAYTTAARLFQGTHLPYLFLGMQHMQLGNILLANEYLQSSYALFQYDPLLLNELGVVAFNKSDMQTAINHFQNALLLVKKTQSNEKPWAATWANLGHAYRKLKMYDAAIDALNQGLLLSTNDANVHTAIALVYLHKKIPGLAITHLHESLAISPNEIMASDLLKRALEENSLTSGFLNSKYVFEDEVSEYMQQSNLNTSDKSMSMEDQSGKVTESVNDRTQVLYADSRSEMMMDDIEGNVSEQR
The following text describes a protein:
Function:
Constitutive protein of the cell wall. Antigen target of host humoral immune response.
Subcellular Localization:
Secreted, cell wall.
Sequence:
MPNIKSLHKLTDKQTDSKMHFKLSTAVLATLVGVALSGPLVARDAATILSDLSTIKTDINTLTQHFNEFTGDLLQALAAQAVEQQLESDIDQATADAKATSALSAADSTSVTNALLGLKPDIVTSLDAIVAKKPQVDSAGVGSLVLSDLNALQSKTDALSGALQDIATATDKDTIASGTQDIDAAFSSAIAVFS
The following text describes a protein:
Function:
ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Subcellular Localization:
Mitochondrion matrix.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MLKQLSRSLGIRSSPIVANLIRSKQVCTRGFHISLVKQNTSSKVNEITDITSDSLKVKEDAAGSDLPSTKTDKKSKSESFQPVKFEDFKGKGYIHDSIINSLHKNDFKELTPIQQKSLVPIFNTEKGLVCRAKTGTGKTLAFAVPTLQYAYKNRGKGVSTVVLVPTRDLAFQIEEEYRKLISHLKYNERPNLELIIGGQRTSFNPRRPAEIVIATPGRLEKELQTDRKLAKCFSNVTYRIYDEADRLLDVGFESVLNEIDGLLYKVRTTPKPIKSLLFSATVDEAISEFSKKHIHPEYEFLNTVTKDDLEIPENIHQQLIECTDGIDKVNVSLSELHGIMKQHNDYKVIVFLPTKTAVDWFYEYITNALDDELFELFSKPPRVFMLHGGRSVRQRSAALKGFKVAKKGILISTDVAARGIDVKDVTNVMQMFPSVEIADYIHKVGRTGRAGKKGKASLFATPAELPYVSLLKRKRKVKFQEVIQSEKLNSSNIIDQIESPLDSTKEFLATMVGYLQQLQSAHRLDYDSLVIENMELYRKLVRDDKAMLESRILSRIGKGISAHVKRRYFTRTRYQSHDDAEFDSYSDFSRSGMSQRPRSNDRSSKMTFNGRGKYGNNRNNDWSYQNKNRYNNNNNRQTERSYDSDRKSHNDWKYEKKFEHRRIRDHDE
The following text describes a protein:
Function:
With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine). Cannot use (S)-ornithine or (R)-alpha-lysine as a substrate.
Sequence:
MAHIVTLNTPSREDWLTQLADVVTDPDELLRLLNIDAEEKLLAGRSAKKLFALRVPRSFIDRMEKGNPDDPLLRQVLTSQDEFVIAPGFSTDPLEEQHSVVPGLLHKYHNRALLLVKGGCAVNCRYCFRRHFPYAENQGNKRNWQTALEYVAAHPELDEMIFSGGDPLMAKDHELDWLLTQLEAIPHIKRLRIHSRLPIVIPARITEALVECFARSTLQILLVNHINHANEVDETFRQAMAKLRRVGVTLLNQSVLLRDVNDNAQTLANLSNALFDAGVMPYYLHVLDKVQGAAHFMVSDDEARQIMRELLTLVSGYLVPKLAREIGGEPSKTPLDLQLRQQ
The following text describes a protein:
Function:
GTPase-activating protein for p21-rac.
Subcellular Localization:
Membrane; Peripheral membrane protein.
Sequence:
MAASSNSSLSGSSVSSDAEEYQPPIWKSYLYQLQQEAPRPKRIICPGEVENRPKYYGREFHGIISREKADELLGGVEGAYILRESQRQPGCYTLALRFGNQTLNYRLFYDGKHFVGEKRFESIHDLVTDGLITLYIETKASEYISKMTTNPIYEHIGYATLLREKVSRRLSRSKNESRKASVTNEEHTPVEKISSLVRRAALTHNDNHFNYEKTHNFKVHTFRGPHWCEYCANFMWGLIAQGVRCSDCGLNVHKQCSKHVPNDCQPDLKRIKKVYCCDLTTLVKAHNTQRPMVVDICIREIEARGLKSEGLYRVSGFTEHIEDVKMAFDRDGEKADISANIYPDINIITGALKLYFRDLPIPVITYDTYSKFIEAAKISNADERLEAVHEVLMLLPPAHYETLRYLMIHLKKVTMNEKDNFMNAENLGIVFGPTLMRPPEDSTLTTLHDMRYQKLIVQILIENEDVLF
The following text describes a protein:
Function:
Catalyzes the oxidation of glycine, leading to glyoxyl imine and hydrogen peroxide as primary products; glyoxyl imine is used for the biosynthesis of the thiazole ring of thiamine. Otherwise, glyoxyl imine is spontaneously hydrolyzed in water to produce glyoxylate and ammonia. Can also use sarcosine (N-methylglycine) as substrate.
Sequence:
MSERVVVVGAGVIGLLTARELALAGLRVTLVERGESGREASWAGGGIVSPLYPWRYSPAVTALAHWSQDFYPALGQRLLDETGLDPEVHTVGLYWLDLDDQTEALQWARKHTRPLKEVPIEEAYAAVPGLGAGFQRAVYMSGVANVRNPRLARSLRASLQQFANLELHEQTEVRGWLRDGDRVVGVATSRGEIRGDKVLLAAGAWSGELLKPLGLELPVVPVKGQMILYKCAADFLPRMVLAKGRYAIPRRDGHILIGSTLEHSGFDKTPTDEAQESLRASAAELLPELADMQPVAHWAGLRPGSPEGIPYIGPVPGFDGLWLNTGHYRNGLVLAPASCRLLADLMSGREPIIDPAPYAPAGRL
The following text describes a protein:
Function:
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.
Subcellular Localization:
Microsome membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MALKWTTVLLIQLSFYFSSGSCGKVLVWAAEYSLWMNMKTILKELVQRGHEVTVLASSASILFDPNDSSTLKLEVYPTSLTKTEFENIIMQLVKRLSEIQKDTFWLPFSQEQEILWAINDIIRNFCKDVVSNKKLMKKLQESRFDIVFADAYLPCGELLAELFNIPFVYSHSFSPGYSFERHSGGFIFPPSYVPVVMSKLSDQMTFMERVKNMLYVLYFDFWFQIFNMKKWDQFYSEVLGRPTTLSETMRKADIWLMRNSWNFKFPHPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSMVSNMTEERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRVDFNTMSSTDLLNALKTVINDPSYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWFQYHSLDVIGFLLACVATVLFIITKCCLFCFWKFARKGKKGKRD
The following text describes a protein:
Function:
Required for the formation of transport vesicles from the ER. This function involves the cytoplasmic domain of the protein, which is thought to interact with the small GTP-binding protein sar1.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type II membrane protein. Note=Cycling between endoplasmic reticulum and the early Golgi.
Sequence:
MAELHLSFPAYSLCWINNHQMAVGGGGGTTKSGVKNKLKLLSYEDYEPEVGEGHTKFIEHGEIELKHSDDAVMSLGYFKNELIAGINNTIDGKLIDHLRLYGRKDKLFEEKNALRLTDFDNDEQYQRLCLFEPLHDAICISCTNKSFFIISKNDHKVLFEKHGSDVYDVSSTEDKLAIAVDDRVEIYDWNTFELVQVLYMPVERATVRGVSFLPNQSIVAAYNYIKDSKRFASLVRFDYSSKNQLWRFGMIRDLKNAKGVTCFCCDKENGMIIVAGADCSIRFMSLDLTKLSQVYKHSLPVTDMQLSPDSEALVSVSADGLLCLQFVGKFKNLSAVKLEDAGVILRLSLMFPFVLAILYFYLQLLFPDEKLDAIHRFFSFILHIFSKYTIRNYDL
The following text describes a protein:
Function:
Represses the expression of the hex regulon (zwf, eda, glp and gap).
Sequence:
MNMLEKIQSQLEHLSKSERKVAEVILASPDNAIHSSIAAMALEANVSEPTVNRFCRSMDTRGFPDFKLHLAQSLANGTPYVNRNVNEDDSVESYTGKIFESAMATLDHVRHSLDKSAINRAVDLLTQAKKIAFFGLGSSAAVAHDAMNKFFRFNVPVVYSDDIVLQRMSCMNCSDGDVVVLISHTGRTKNLVELAQLARENDAMVIALTSAGTPLAREATLAITLDVPEDTDIYMPMVSRLAQLTVIDVLATGFTLRRGAKFRDNLKRVKEALKESRFDKQLLNLSDDR
The following text describes a protein:
Function:
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Subcellular Localization:
Cytoplasm.
Sequence:
MKKAGVIHLGCSKNQVDTEVLMGFLKNLGYTFTPHSEEADLILVNTCAFIKPAWQEAEENISLLEKYKKINENLKIVVVGCYVERFKEELENKYPFVDLFIGPGEYEKFVSLITSNGKRGIYSSPASSFIYNHKMPRILISPNFWVYVKIAEGCNNFCSYCTIPFIRGRLRSRSIEDIVKEIEIWIGKGVKEVNLIAQDTTRYGEDLYGRPSLVDLLRNIEKIRGDFYVRILYSYPSRISEKLIEAIKNSEKVVPYFDIPIQHVSDVILKRMNRSYKKDDIIKLWHRIKENFENAVIRTTVMVGFPGETEENFEELIDFIKKYPFDRLGAFIYYNENGTISKGFENQVDEDEKLRRYEILMETQKKISKKLNAKLLGKEFDVIIEDEKGKYFVGRSWREAPEVDGLIMIPKEKEKTLKIGSKVRVKIKKYRSYDLLGELV
The following text describes a protein:
Function:
Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol.
Sequence:
MKQKLLLFIFSILILLIAAEAKMFKDIWKSCGKSTDTFQIKNVTISPDPPVRGQTVSIYASGELKDTISGGDVNIQIKFGIITIIRETKPICSSDNPFPCPIQPGDYTHSVDIAIPDNAPRGKYSGNFVLTDQANDEIACINVNMQL
The following text describes a protein:
Function:
Might be required for polymerization of melanin onto the core structure of melanosomes with enzymatic function of tyrosinase.
Subcellular Localization:
Melanosome lumen. Note=On the fibrous matrix structure of the premelanosome.
Sequence:
MRLHGAIVLLAALLALVTAQQRGGGRSRGGVKGSAWGGRPAPFRSWDTARYRPWQEGTARQNDCWRGGDVTFDISNDAPTLVGARATFSIALRFPGTQTVLPDGRVVWSQNCTVNGTRMLQGDPVYPEQLAEGSDGVFPDGQPFPRSAWGKRGRFVYVWWTWGRYWQVVDGATSQLTVGTDGVALGSYTMEVVVYHYRGRQRFIPIGHASTQFSITDQVPIAVDVTQLEVAAGDGGSFVRNRPVAFNVRLHDPSHYLRDADISYSWDFGDQSGTLISRSPTVTHTYLQAGSFAARLVLQAAIPLSSCGTSAPPVVDPTTGPVPSLGPTATQPVGPTGSGTATAPSNLTGSGTAAAPGTTAAPRASGAPAEPTGVSVAVLSDSAATEPLPDPVLSTAVADAAAGTDPTADPLPPTSVSSGGDAPGTVAPTAVEGSVAAGVGTAEDVAAATPGATAADVAVDTAGATDGDAVGPTAAATAESIADPTAGATDGDAVGATAESIADPTAGATDGDAVGPTAAATAESIADPTAGATAVSSGSATAGATAEPLLLVKRQAPEAEPTGCVLYRYGTFSTELNIVQGIESVAIVQVVPAAPEGSGNSVELTVTCEGSLPEEVCTVVADAECRTAQMQTCSAVAPAPGCQLVLRQDFNQSGLYCLNVSLANGNGLAVASTHVAVGGASPAASGTTLTVGLLWAPLIAAALGTAAYTYRRVKYSPLLPTAPTAPRPHSWLPPGATLRLLLRQAFGGAPSGESSPLLRANAV
The following text describes a protein:
Function:
Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor.
Sequence:
MDTLRIGLVSISDRASSGVYQDKGIPALEEWLASALTTPFEVQRRLIPDEQEIIEQTLCELVDEMSCHLVLTTGGTGPARRDVTPDATLAIADREMPGFGEQMRQISLRFVPTAILSRQVGVIRKQALILNLPGQPKSIKETLEGVKADDGSVSVPGIFASVPYCIQLLDGPYVETAPEVVAAFRPKSARRENMSD