lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Acts as a regulator of the SsaN/SctN2 ATPase activity (By similarity).
Subcellular Localization:
Cytoplasm. Note=Detected in both the soluble and membrane fractions.
Sequence:
MSFTSLPLTEINHKLPARNIIESQWITLQLTLFAQEQQAKRVSHAIVSSAYRKAEKIIRDAYRYQREQKVEQQQELACLRKNTLEKMEVEWLEQHVKHLQDDENQFRSLVDHAAHHIKNSIEQVLLAWFDQQSVDSVMCHRLARQATAMAEEGALYLRIHPEKEALMRETFGKRFTLIIEPGFSPDQAELSSTRYAVEFSLSRHFNALLKWLRNGEDKRGSDEY
The following text describes a protein:
Function:
Fungal-specific subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). 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. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition, and virulence via providing the ability to damage and invade host cells such as oral epithelial cells.
Sequence:
MSGGPVPVWKKYTTRPQGIWEKIRQLLVLVPNRSSGNPLVSLFRQVPPGERIKEAQNYKDPVTIPAGDIKGNPYFKRDYRRNYPQVHTFNQTKISGLLNLGSESNPRISIGEKGNKELAVFTNGQDVSLASTLKSVPASVVKGEVLGKSGEPIVAPSLNKFKWEILPEPVHGMYSEAYPCRIFTEKKVRSQSSA
The following text describes a protein:
Function:
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
Subcellular Localization:
Cytoplasm.
Sequence:
MTPSALFHKRLIEQFTIFLSVDRGISPLSVQAYCQDVLLFLQRASIEATDRINQESVFLFVEKCHKAKESETTLARRLIALKVFFHFLKDAKMLDQQPFIEHPKIWKRLPSILSTEEVNSLLDQPLNIPNLDTHIASRDAAILYTFYATGIRVSELCDLCIGDISDDFIRVTGKGRKTRLVPISIKAKQAIDAYLSSFRDELQKKNPSEEHVFLSIRGKKLDRSCVWKRITFYAKLVTTKRISPHSLRHAFATHLLNNHADLRIIQEMLGHSRISSTEIYTHVASESLIEKFHTYHPRDI
The following text describes a protein:
Function:
Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the first glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Man(9)GlcNAc(2)-PP-Dol to produce Glc(1)Man(9)GlcNAc(2)-PP-Dol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAIGKRLLVNKPAEESFYASPMYDFLYPFRPVGNQWLPEYIIFVCAVILRCTIGLGPYSGKGSPPLYGDFEAQRHWMEITQHLPLSKWYWYDLQYWGLDYPPLTAFHSYLLGLIGSFFNPSWFALEKSRGFESPDNGLKTYMRSTVIISDILFYFPAVIYFTKWLGRYRNQSPIGQSIAASAILFQPSLMLIDHGHFQYNSVMLGLTAYAINNLLDEYYAMAAVCFVLSICFKQMALYYAPIFFAYLLSRSLLFPKFNIARLTVIAFATLATFAIIFAPLYFLGGGLKNIHQCIHRIFPFARGIFEDKVANFWCVTNVFVKYKERFTIQQLQLYSLIATVIGFLPAMIMTLLHPKKHLLPYVLIACSMSFFLFSFQVHEKTILIPLLPITLLYSSTDWNVLSLVSWINNVALFTLWPLLKKDGLHLQYAVSFLLSNWLIGNFSFITPRFLPKSLTPGPSISSINSDYRRRSLLPYNVVWKSFIIGTYIAMGFYHFLDQFVAPPSKYPDLWVLLNCAVGFICFSIFWLWSYYKIFTSGSKSMKDL
The following text describes a protein:
Function:
Required for normal levels of the cell wall 1,6-beta-glucan. Involved in a protein folding machinery chaperoning proteins acting in various physiological processes including cell wall synthesis and lysis of autophagic bodies.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MLMYTILIPSLLYIALTIASSELLNSIQGTWQSQSERVITGPTFFDPQKELLEEPKLPGISYSFKNGYWESAQYIVMGNNRNHQCPQAMLIWQHGKYNLKRGKLVLIPNRNDGRQLISDPCLDNGKSEYKRFHNGETLEVDIRFDGYFGNWKLVLVDYLTGKKKQPMWLTSRNATMLPTGTITSTKRKYVKKE
The following text describes a protein:
Function:
Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Note=Localized in the septal membrane. Localization depnds on FtsZ.
Sequence:
MSISSILLSLFFILNILLAIIVIFKERRDASASWAWLLVLFFIPVLGFILYLLFGHNLRRKHLFQWEDRKKIGIERLLKHQLEDLETKQFQFNNRATFDNKDLIYMLIMNNHAVFTEDNSVDVITDGRDKFQRLLSDISKAKDHIHLQYYIYKGDELGKKLRDALIQKAKEGVQVRVLYDELGSRTLRKKFFKELREAGGHVEVFFPSKLRPINLRLNYRNHRKLVIIDGMTGYVGGFNVGDEYLGLNPKFGYWRDTHIRLQGTAVHAIQTRFILDWNQASHHHTLTYIPNHFPDYGPKGNVGMQIVTSGPDSEWEQIKNGYIKMISNAKRSILIQTPYFIPDASLLDALRIACLSGIDVNIMIPNKPDHAFVYWATLSYIGDLLKAGATVYIYDNGFIHAKTIVVDDEIASVGTANIDVRSFRLNFEVNAFIYDITIAKKLVSTFKEDLLVSRKFTYEEYLQRPLWIRIKESVSRLLSPIL
The following text describes a protein:
Function:
Catalyzes the conversion of lactate to pyruvate.
Subcellular Localization:
Cytoplasm.
Sequence:
MKDHQKIILVGDGAVGSSYAFACVNLSIGQEFGIIDIDKDRTIGDAMDLSHAVPFSTPKKIYSANYSDCHDADLVVVTAGTAQKPGETRLDLVNRNIKIMKGIVDEVMASGFDGIFLIASNPVDILTYATWKFSGLPKERVIGSGTSLDTARFRMSIADYLKVDARNVHGYILGEHGDTEFPAWSHTTVGGLPITEWISEDEQGAMDTIFVSVRDAAYEIINKKGATFYGVAAALARITKAILNNENAILPLSVYLDGHYGMNDIYIGAPAVVNRQGVRHIVEMNLNDKEKEQMKNSADTLKKVLDDAMKQID
The following text describes a protein:
Function:
Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1.
Subcellular Localization:
Cytoplasm.
Sequence:
MQSNAENPRKRFTATSPNGNRQNVSVDTSSNVAGPSRPRIANAVPAEILDDPALNQAIKSILPSNYNFEIHKTIHHIRKASASCVALQMPEGLTLWATGIADIVERFTDATTVIMGDVTYGACCVDDYTAMALGCDMLVHYGHSCLVPVDQTAIKTLYVFVEISIDPAHLAATIRANFPNDRHDFRAKILGGSQSAAGKRSEVDESAGRAQIQIGEQASVASGAPPSTLTHLALVGTVQFINAINGLREALRQQQHRLADGQIVSTESPVDRLMLTAGTASSAPVQHITQAAKWKAWSSGEYKVTVPQVKPLSPGEVLGCTSPKLDKDEIDAIVYIGDGRFHLESIMIANPRIPAFRYDPYTKRFVRELYDHAEMRRMRGEAVRLAQDSVGGLDLDPETSIVKKNKAVVVDAEKDRVTASGWGVLLGTLGRQGSLRVLESLSASLSEHVPPIPHVPILLSELSPQKLGLFGEHLAAFIQSSCPRLSIDWGSAFAKPLLSPYEAAVSVKKVKGWQEDVQGLGMSRTPAKQQQDGNGNGSDAVPAEDKHLPLDGDYPMDFYSDTSLGPWTPRHGMAPAKKPVGAKSNLALLRSLRSKRAKASSTPTSAATA
The following text describes a protein:
Function:
Glycosyltransferase involved in the xylosylation of xylan, the major hemicellulose (non-cellulosic component) of primary and secondary walls of angiosperms. Possesses beta-1,2-xylosyltransferase activity, transferring xylose from UDP-xylose to the xylan backbone. Catalyzes the addition of 2-O-xylosyl side chains to the xylan backbone.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MKAAVRSKKSKGSFCHPPLLLLIVAIQFLVIYSPTLDQYMVMLTTGKPGFPSMLIDGRRSFKQVDEFIPEPHLRCDFRDNRSDVCEMEGAIRILGRTSEVFLVAPSLASISGGGGGVNATGVDANATRWKIQPYTRKGESRVMPGITEVTVRLVTADEAPPCDEWHDVPAIVYSNGGYCGNYYHDFNDNIIPLFITSRHLAGEVQLLVTQKQRWWFGKYREIVEGLTKYEPVDLDAEQRVRCYRRATVGLHSHKDLSIDPRRAPNNYSMVDFKRFLMWRYALPREHAIRMEEEDKSKKPRLLVINRRSRRRFVNLDEIVAAAEGVGFEVAAAELDAHIPAAASAVNSYDAMVAVHGSGLTNLVFLPMNAVVIQVVPLGRMEGLAMDEYGVPPRDMNMRYLQYNITAEESTLSEVYPRAHPVFLDPLPIHKQSWSLVKDIYLGQQDVRLDVRRFRPVLLKALHLLR
The following text describes a protein:
Function:
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Possesses a clear preference for long-chain acyl-CoA substrates rather than acyl-ACP primers. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall. In vitro, when AcpM (the natural partner) is used as the carrier, malonate incorporation increases with acyl chain length to reach an apparent maximum with primers ranging in length from C:14-CoA to C:20-CoA. However, the initial acylation step shows preference for dodecanoyl-CoA, suggesting a role for AcpM in determining the specificity of the mtFabH reaction. Shows only very weak activity with acetyl-CoA.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Subcellular Localization:
Cytoplasm.
Domain:
The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH; Exists in an 'open' form that permits binding of the long chain acyl-coenzyme A substrate and release of the corresponding 3-ketoacyl ACP product. Catalysis and intermediate steps in the process are proposed to occur in a 'closed' form of the enzyme.
Sequence:
MTEIATTSGARSVGLLSVGAYRPERVVTNDEICQHIDSSDEWIYTRTGIKTRRFAADDESAASMATEACRRALSNAGLSAADIDGVIVTTNTHFLQTPPAAPMVAASLGAKGILGFDLSAGCAGFGYALGAAADMIRGGGAATMLVVGTEKLSPTIDMYDRGNCFIFADGAAAVVVGETPFQGIGPTVAGSDGEQADAIRQDIDWITFAQNPSGPRPFVRLEGPAVFRWAAFKMGDVGRRAMDAAGVRPDQIDVFVPHQANSRINELLVKNLQLRPDAVVANDIEHTGNTSAASIPLAMAELLTTGAAKPGDLALLIGYGAGLSYAAQVVRMPKG
The following text describes a protein:
Function:
May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Subcellular Localization:
Endoplasmic reticulum. Golgi apparatus, cis-Golgi network.
Sequence:
MSSSAHTSTSAAQLGDAAFDNNVKMSAEFLALTYGALVQQMVEELTQEDAVEQVNQQLYNMGHRIGARLIEEYSVRSGAAPCRTFSQAAEGVALVGLRMFLGVSAEVAQVKDAADTFAISFQDNPLALFVELPDGPLREYLWYSNLLCGVITGALSLVGLQTEARFSRDRLRGDSKNEIILHFKGRERETFQVERN
The following text describes a protein:
Function:
Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Responsible for energy coupling to the transport system.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein.
Sequence:
MPKGYKQKEKIEVVQETVKTKKILEVVDINGHAFENISFTVHAGEVVGVAGIIGSGRTELAEAIFGLKTIKSGSILLGGKSIDTCSLHKRLDEGLVYVPEDRARNGIFSIASVKENIAAASLYQNNRFFINKEKESALVNSFIEQFRIVVQDMNKELASLSGGNQQKVVLAKYLACNPKIIILDEPTRGIDAKARLEVYETIKKMKREGLAILLISSDVEEIVQLVNRVYVMRNGRFVSHMEKEQLSVNEVTRLAYGGVAE
The following text describes a protein:
Function:
Regulator of mitophagy.
Sequence:
MNLLSQFMKPKNKFSIENLRYLHNTLKKNQIITAQNKNLIVESLRQIAEVMIWGDQHDNLFFDFFLEKNIMGFFIQFLAQKTSTEVTIQLLQTLSILVENLRNENSIYFLLSNNYINEIIIHKFDFSSEEVLDYFVSLLKALSLKLDKSTVNFFFNHVEKDFPLYTEAIKFVNHKETMIRIAIRTLTLNIFKVENKEMREYIINSTAVPYFSNIVWFIRRNCMSLSKVLEKSNHDSSYQLKDYMDELTDQFYYLHDIFNLGFESMNIVLAEQFIQYLIYPVFIGSLIDPLKNPDLEDRITPTLALYLLAHVFNIFSFKPLLDTISSALLTATQSQAQLFTSATTAPPPLSTIASNRRHYNSFRRFSSFPNLESLEAMKNDGITSISDTDGRIGASGRLLNNTSTDEDSPPNSGFKPSNSVQSTSSSPSTPKKYQQQFSRLFGSSRKPLPTTPSSSPKPSTTSSITTSTTTTTPTTTITTTTTTTTTTITPSSSPSKQNLSSSIESTNSLNNNNNNNNNNTTANNDNLESTQPKEDNLPTITVLNLNSPNENSTKDDNNNNNNNNNNNNNNNNNNNNNTTPTPSTPTRKRFKFNRNEFKESLLHLIGSDRETFGIVIMLYSFLKNQHIDKRILEKGGMLPYRLALLEGLLSPETNNNNSNNNHHHHHHHHHHHSKTTVTSPNNQQQQQQVSHSTGGIKGQKNSKMSASLPINIGHNRSRSESHAKSLLFNPNLYDTVTLEERSLFKTPSPGSSSLFGELEIETNKTDEGGDEKDEYDDGDDESSVNIRIKSSKHNSINSSVDSTIDLSKNNNNNNNNNNNNENNNNDNNNENNNVNNNNNINNNNNEESEEEEFVPVPESSQKDFTRRLINALFMVLVNSNQFRLVTLQMTLLILKELVYSSDSSSKLTETQALLLEQAYITVTDNLKECLSGPLSEVFLEIFEEELRSYKQIIFESLMEDVSLILPIPQKPVSRLSLSHRLPSGELERTQKAVQQFLVLRELKFTLLRKKDTMLPLKQPPTPMVKEKYLFNLETGVVESSYDIIEYHHFEKVSGPTPPPPSGTPRKRFTHYGVLFHNLLLAVDPPPSISSSSSSSASTSGSGTPNSSIGGTGGGGGGGMGSGTGGTSSPNPSNIIGGTNNKGIYGTIVHIAPLQRLEIETSHRDPSILRVTSHPTTWNVEMVFDDSTQCSKAKQMLERVRDDVRATKMRQIYALLGEKDPDDDSVPPQLNYGNMVERNPTNSDHDSNTTLNNEHNLLSSNNNGEFSTSMSNTPPSRVITPIDTSNSHPLANILGSDDNISFVNNNNNNSNNNNTKKTTSTVNTPISTPHKLKKGNRGSSSNSSLNDSILPTLEDHLRKTVSPKVDMFNTSFFDDTLDLKELISTDELNNGNNNNNNEDNNENPFSNIKRNSNEVKVGQPVQQEIEKEKEKENIIGEDVEKETSIEQKEIKKDENDNNNIVEKEEEEIKDDNIKEEIKQDDSNNKEINNDNSTTNNKEDEEEEIKKDNKDEENIVNIEHINEKEVQEQQTEEQVEEIIKESVDIKVESDNN
The following text describes a protein:
Function:
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), hence rate-limiting enzyme in the synthesis of FAD. Essential for TNF-induced reactive oxygen species (ROS) production. Through its interaction with both TNFRSF1A and CYBA, physically and functionally couples TNFRSF1A to NADPH oxidase. TNF-activation of RFK may enhance the incorporation of FAD in NADPH oxidase, a critical step for the assembly and activation of NADPH oxidase.
Sequence:
MTGILAKLPAYVKGTVVKGFGRGSKELGIPTANFSENVMESLAGDTGNGIYFGLAAVDDSPVHKMVMSIGWNPYYKNTKKTMEVHVIHDFENDFYGSELRVIVLGHIRPEKDFSSLDQLIAEIHNDIRIAKSRLEEPTFKAYYEDPFLTKNSTNK
The following text describes a protein:
Function:
Component of the TRAPP I and TRAPP II complexes. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II seems to play a role in intra-Golgi transport. Has a role late in meiosis following DNA replication (By similarity).
Subcellular Localization:
Golgi apparatus, cis-Golgi network.
Sequence:
MESNLSAKGIFQHASANASGELFQEPVTEDLEKVMQSKGLYSMEELCSIIQEAYAPRVSVLCSRDADEFAMRKGYPKGFWELLYPFGDRIRGKVNRRGMNGEMLTLENLNLHFVPIDALESHLSEASFPSLRSVLCERYPGLVSPEPPSDYSFGVHYKNVERWAWTLAHEGNYQMPLPVYVRQLLTGIPITPFETFSHPVAHLVVVTSHNPSPFESLRSLINSIPYLSLPAFVFNDINYLFVYVHDEDQHDLELSMAIFDTMKQTFGDCGYFLRLHSQKATLDYEHTVPFPTSSWLSAEERLHLLSNTDTEIRLLFESDNESLRRLSSHIAFNGIVSYLDKCVRAWDDQYASPRRGITGKLLFASRKYLSSSNASTNSNYFPSSNAYRPFSPEAYLRKLADYSFMLRDYSHANQIYEIASRQYENDGACLYSAASLEMIVITEHILHLKMPYMSLTNTLRINEYMQSAMLNYLNKSFNSYYHAARCFLLLGQFLSCLPAPKVDDAANWNAGLLYSKRLGPVGRAMIFQQTHTLFKSLSYLKTESTDPFSNKRTRKAALWCVLTADAWLRCRIPFRAKPFVEEAKLFYGKIDWKDLKECVAALDEVEVSKQPASNIPSS
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular Localization:
Membrane; Peripheral membrane protein.
Sequence:
MRINPTTSGPRVSTLEKKNLGRIAQIIGPILDVAFPPGKMPNIYNALVVKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGELVDNLGPVDTRTTSPIHRSAPAFIQLDTKFSIFETGIQVVDLLAPYRLGGKIELLGLAGWKDCFLPSLVLDRSDRVFIIWSKRIRTFACRYQKPMPYHLAILHTALGLLITN
The following text describes a protein:
Function:
Plays a role in the regulation of phosphate uptake.
Subcellular Localization:
Cytoplasm.
Sequence:
MEKATIIKEIESLKEKLLRMGSIVEKMLHKTLDSIKTRDLDLAQEVIETDKLVDDYNWNIENQCIKILSLHQPVAKELRIIASTMKIIKDLERIGDYSVDIAKFASSLLKYSFEIPLADIISLATLVEKMVKDIIRAYSEPNLDQLEDLSSYYNFVYLKYQEISNELLEEIYKNPILTQQIVQLIMISRYLERIADHATNIIELIYYIETGERKELHK
The following text describes a protein:
Function:
Leucine-rich repeat protein that likely mediates protein interactions, possibly in the context of signal transduction.
Sequence:
MERILKSARESGSLNLSNRSLREVPGEVYNNLDTGSQDDKWWEGVDLQKLILAHNNLEVLREDLRNLSSLVVLNISHNQIYSLPAAIGDLPLLKSLDISFNQINTVPEEIGLAAALVKVDFSNNCLTELPASLAGCLNLSELKASNNKISRIPDELAGCSKLSKLDLEGNKLEMLSENMFSSWTILTELNAAKNILTTIPASIGALSKLIRLDLHQNKITLIPSSIKGCSSLAEFYMGNNLLLSIPADIGMLSKLGTLDLHSNQLKEYPVGACKLKLSFLDLSNNTLSGLPPELGTMTTLRKLLLSGNPMRTLRSSLVSGPTSTLLKYLRSRLSSDEEASGSGRTPTKDDQVAAARRLSLSSKELNLSGLGVTSVPPAAWETSDVVKLDLSKNSIEDLPNELTLCSSLQALVLSNNKIKKWPGMVVSSLPSLSSLKLDNNPLAEISSTDLEVLSKLEVLDLSGNASSLTKPSALSSLPQLQELYLRRVKLHEFPIGLLGLKLLRILDLSQNYLTTIPEGIKEFTALIELNLSDNNITALPAELGLLEPNLQVLKLDGNPLRSIRRTVLDRGTKAVLQYLKDKLPSH
The following text describes a protein:
Function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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 (By similarity).
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MFRSLLKRTTFLNQLNKSNGFNRNYFKQSTLTRSDALSRHVETEDNNEHTPFDFTQENLVKVEKILAKYPKQYRQSALIPLLDLAQRQNGGWISLRAMDKVAHICGIAPMTAYEVASFYTMFNRTKIGENFVQVCTTTPCMLRGSGEIIKTCKSHLGIQVGETTPDNKFTLVEVECLGACVNAPMMCINDDFYEDLTSASTINLLDQIKNNKPTKIGPQTHRKAAEGPQGKTTLLEPPVGPTCRDDL
The following text describes a protein:
Function:
May be involved in MAP kinase activation, epithelial sodium channel (ENaC) down-regulation and cell cycling.
Sequence:
MGTPASVVSEPPPWRAPPEVRGRKQAAANIFQDAELLQIQGLFQRSGDQLAEERAQIVWECAGDHRVAEALKRLRRKRPPRQKPLGPSVHHCSRLRTAEPCAPQSRATETASSEQHVNSRRASARIRRNWRKPGPTSYLHQIRH
The following text describes a protein:
Function:
Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Does not exhibit calcium-activated chloride channel (CaCC) activity (By similarity).
Miscellaneous:
MISCELLANEOUS: The term 'anoctamin' was coined because these channels are anion selective and have eight (OCT) transmembrane segments. There is some dissatisfaction in the field with the Ano nomenclature because it is not certain that all the members of this family are anion channels or have the 8-transmembrane topology.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Note=Shows an intracellular localization.
Sequence:
METSSSGITNGRTRVFHPVAKDVNILFDELEAVNSPCKDDDSLLHPGNLTSTSDDASRLEAGGETVPEKNKLNGLYFRDGKCRIDYILVYRKSNPQMEKREVFERNIRAEGLQMEKESSLINSDIIFVKLHAPWEVLGRYAEQMNVRMPFRRKIYYLPRRYKFMSRIDKQISRFRRWLPKKPMRLDKETLPDLEENDCYTAPFSQQRIHHFIIHNKDTFFNNATRSRIVHHILQRIKYEEGKNKIGLNRLLTNGSYEAAFPLHEGSYRSKNSIRTHGAVNHRHLLYECWASWGVWYKYQPLDLVRRYFGEKIGLYFAWLGWYTGMLFPAAFIGLFVFLYGVITLDHCQVSKEVCQATDIIMCPVCDKYCPFMRLSDSCVYAKVTHLFDNGATVFFAVFMAVWATVFLEFWKRRRAVIAYDWDLIDWEEEEEEIRPQFEAKYSKKERMNPISGKPEPYQAFADKCSRLIVSASGIFFMICVVIAAVFGIVIYRVVTVSTFAAFKWALIRNNSQVATTGTAVCINFCIIMLLNVLYEKVALLLTNLEQPRTESEWENSFTLKMFLFQFVNLNSSTFYIAFFLGRFTGHPGAYLRLINRWRLEECHPSGCLIDLCMQMGIIMVLKQTWNNFMELGYPLIQNWWTRRKVRQEHGPERKISFPQWEKDYNLQPMNAYGLFDEYLEMILQFGFTTIFVAAFPLAPLLALLNNIIEIRLDAYKFVTQWRRPLASRAKDIGIWYGILEGIGILSVITNAFVIAITSDFIPRLVYAYKYGPCAGQGEAGQKCMVGYVNASLSVFRISDFENRSEPESDGSEFSGTPLKYCRYRDYRDPPHSLVPYGYTLQFWHVLAARLAFIIVFEHLVFCIKHLISYLIPDLPKDLRDRMRREKYLIQEMMYEAELERLQKERKERKKNGKAHHNEWP
The following text describes a protein:
Function:
Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSVGEVQVIQAWLRSEWHIQVPPAWLDACVNWIKEEADRASIPQSQLNQRVLEQWLLTDLRDLAHPVLPERISEAQKTVLSNRCCVQMDSLLDVSQPAYNQLQRIRGTDCSNDQVSAVTQETQRPWEAKPTRMLMLQLTDGVQNLEGMEYRPIPALNANLPPGTKLQLVGPIAVRLGVLLLKAENIKVLGGEVEQLLEIHSQSRVLCGTLGLPEETHPQQEPDGLVASVADSGYSSLASEASLRHPQSQPLPQISRQDDWDMDEIPDDDFRSIPDHFDDLPQNNNPLEDVPEDFDDIPLDELDNVMCPIDVEVSAGTLEDPERNKHDSSLLNGSKPEEVSFPSRSRLGNTYQSRTLNKVPNTSLASCSTSTLDSSACKETPMYLCSLQAGCWPPKSPQVFRLQAFIVTLVGNLRISGGVWKLGATISDGSGYLDVDLSDNMLSELIGFSAAETRVLRKDLARRGEVDSGIQHCQRELVDMCCMMSVQVDLTGRGVVLSASPISDRECSEMQKRVKEARR
The following text describes a protein:
Function:
Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
Sequence:
MTTQSGCYESVTDFYANKDVFLTGGTGFLGKVLIEKLLRSCPDIGRIFVLMRNKRGKSIETRVTELAACPLFDRLKEENKSALNKVVPVFGDITQLRLGMYEEDIQRLSNVSVAFHLAASVRFDDPLRDAIKTNICSTQELFEMLKATTPQLRAVVHVSTAYSNPENRYVEEKLYPPKFDWKKLVQAVDRYEPETLDALMQKLSQNSPNTYTYTKGLAEQVCNDYSTELPLAIVRPSVVLFTIAEPMSGWVDNFNGPTGMLVSAGLGITRTAYLRPKNRINIIPVDVVVKTIILAAWKRGTIERACGPKHLPIYNSAVTYEQSLEYQEMLDRGKEYLYAVPFSRMLWVPRGYPTDWKTLYYFKLIFTMLLPSFLLDLLIRMFGHKPFLMKLQSRIYGSEVSLRYFVRNEWEFETKQTDNLPSLLDEKDRNTFGWYMPRKLTGKYLENAYPTIRRYLMKDPDETIPYAKRKLARMILADRIISIIVCCLTLVAMYRRMFAESL
The following text describes a protein:
Function:
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Subcellular Localization:
Nucleus.
Sequence:
MPEGPSLFKWCTMTKQFLGRKTTRICGSSKTVDKKKWSGASLEDVRVYGKRLFLHLVHKRVSTAESESEDSDEESVWIRCHFLMWGSVRVNEFNCKSSKTNKFPEPRLIFYFSKEEFLVFYGGSFQEMNHPPEDESRRDILSDGFNRSRAEDCILGDLPISFILLDQKKFAGLGNIIKDEVLFSTGTHPMQLGCQLSRAKATVIVEKVVTFTKRWLAWKMEEKPSSKFGDWTEIYKKAMCPKGHETTKSMFGPTGMERITYWCPKCQAMNDHDDPLSDRRVWTDTSDQDTETVEGPSVKGISQTIPNSEHQMVTADNANMTESFAADQKVPRRAILTVKELKQEGTPANSNQELEFKEDFLMMQESQSSPKSEQTSLGTPHHLSEMKDTSLPTLSLETELINFGTGHVGNKNLPPPLIEEPRQRLPSTKKIKLESEATCIFDLKEEEPAFTSPSSSSSCIVNSICVPDQQYHDEDSTRISVSISTIQELMRSRVRIKVKKIDVSSKD
The following text describes a protein:
Function:
Converts cob(I)alamin to adenosylcobalamin (adenosylcob(III)alamin), a coenzyme for methylmalonyl-CoA mutase, therefore participates in the final step of the vitamin B12 conversion. Generates adenosylcobalamin (AdoCbl) and directly delivers the cofactor to MUT in a transfer that is stimulated by ATP-binding to MMAB and gated by MMAA.
Sequence:
MSDSEEEYRSKLYTKTGDKGTSALFNGERRPKNDAFFHSLGAIDELSATLGIALEHCIIEKNGLESYLEKLIVVMLDIGACVATPLDNSKDSQINKTKFDDNRIKVIESWIDKVDSELPPLKCFIIPYRVGLASAHLHLARTVCRRAEREMVGLSRHSFIPESVSIFINRLSDFLFAAARYAAMKNGAKEDLWRGVTSEFS