lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pab1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by xrn1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
Subcellular Localization:
Cytoplasm.
Domain:
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex; The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with pan3.
Sequence:
MEADWNELLRIPLPPPNPHGLPTVATTIAFDDVSELLWAGNEYGRITSFYGPELQRYTSVRAHPVAEGPVRQILFHERGVISISSRSVHMITRRGLTQWHITHDEITDLRCMSFTAQTNKIIVAGCQKAMFTIDIDKGTIVDKLRTEHNYVLMKRSRYLCAATDTGSVNALSLTDFSVVKSWKAHGAAVNDMDARGDLLVTCGFSIRQTGSPIVDPLANVYDLKTLSPLPPIPFHAGAAYVRMHPKLQTTSFVASQSGQLQVVDLMNPNAFKLRQATVSFMLGIEISPSGEALAINDAECFIQLWGSPAKIHFNEMSKEVEFADVTPRPPQVDWSPEIPLNVIGMPYYHERLLSAWPSHLLFEVGSPPAPIDPSIVPYLRSGEMGQYAANPKKTRRYQVENTRALASTEPTLIAPKFLSEKAREQSKKADDPVGDTAASLAGARISGESEDDPLLKYSNVEIKYSRFGVDDFDFRFYNQTCFSGLETHIANSFTNSLLQLLKFIPLIRNIALHHAATSCIAESCLLCEMGYLFDMLEKANGQNCQATNLLKTFSSFREASNLGLLEENLTNKSLSSAIQAVNRFFLGQIAQDYRRIAPNSEELDMRLATIASESIRCMFCQNEIVRPGNTLVNELMYPAIDMKQARRNHTLRFSNILRASIEREAQNRGWCHICRRYQQSVMRKTAHRMPHVLMLNAAINSPACRRLWTIPGWLPEEIGIVLEGGQVLCFEGEDLRMRIQGQMPGLIIYDLVGLVAEINIPEHQKAHLVSFINVSVSSRERETRSKWHLFNDFLVTEVDKEEALRFNQSWKSPCVLAFQVRDARHMVDDTWKNFLDTTLLFRDWSLNNGRPVESRVMLSDEEKPTPGTPVALDTEFVDLEKAEINVKADGSQEIVRPSKSGLARVSVLRGSGEREGVPFIDDYISVKEPIVDYVTQYSGIKPGDLDPRTSPHNIVPLKVAYKKLWLLLNLGCVFVGHGLASDFRKVNIQVPKKQTVDTQYLFFHPSKNRRLSLRYLAWAVFKEYIQEEPADSNQGHDSIEDARMALRLWKKFQEYEDAGIVGQILEEIFREGSKLGFRPPPRNGVTTVLSRPGTAVTMQNNSGRNTPSTPDVGAAASAPTTPRQAFRRSIALTPSNGTFSGPGSGEFFTGSPLK
The following text describes a protein:
Function:
With SPAC4D7.04c, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MYDDIFFYLALWVIQSVYGAWDWAKNWVFWTCSYLLNFLYHHHCSRDLIRRDTKKLKKKPKHIAVIIECVEDGGIEGLIHDACELSAWCVCSNIRELTIYERKGFLKQSPEAVEKAIYSHLPFYLGGDKCTVHVTNPCSPDEKNQNDCVDLKVHLIAKEDGRDAIIDLTRGLADLCTKKVISSTQVTLELIDKELKESVIPEPDLLIIFAPLLKLQGFPPWQLRLCEIFHDPILYTTNYLTFFKALVHYSNAEMRLGH
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
KRPGVDKFLATLAQYYEIVIFTPSPEGLAIPVLDSLDSKGFAMHRLHREATHYHNGVHCKDLSWLNRPLRKIVALDDDPDALQFQPENLIRVKPYDDPNDRDDNTLERITPLLIEI
The following text describes a protein:
Function:
VP4 self-assembles to form, together with capsid protein VP10, an icosahedral caspid of 87 nm in diameter, with a T=43 symmetry and composed of 420 hexamers and 12 pentamers. VP4 proteins arrange into hexons, while VP10 proteins form the pentameric densities located at the 5-fold axes in the virion. The stoichiometry of VP4:VP10 is 42:1.
Subcellular Localization:
Virion.
Sequence:
MSESVTQQVFNFAVTKSQPFGGYVYSTNLTASTSSAVTSTQLTPLNLSITLGQITLSGNSLVIPATQIWYLTDAYVSVPDYTNITNGAEADGVILIYKDGVKLMLTTPLISSMSISNPARTHLAQAVKYSPQSILTMYFNPTKPATASTSYPNTVYFTVVVVDFSYAQNPARAVVSANAVM
The following text describes a protein:
Function:
Transcription factor that plays a key role in the humoral immune response as part of the peptidoglycan recognition protein (IMD) signaling pathway. Rel-p68 subunit translocates to the nucleus where it binds to the promoter of the Cecropin A1 gene and probably other antimicrobial peptide genes. I-kappa-B kinase complex (IKKbeta and key) and PGRP-LC are essential signaling components in transmitting the lipopolysaccharide (LPS) signal leading to cact degradation for NF-kappa-B (rel) activation. Part of a Toll-related receptor pathway that functions in the apoptosis of unfit cells during cell competition. Also part of some antiviral immunity: activated downstream of Sting signaling, which detects double-stranded RNA (dsRNA) from viruses, and promotes expression of antiviral effector genes. May be part of a NF-kappa-B and Tollo signaling cascade that regulates development of the peripheral nervous system. Possibly post-transcriptionally regulates the neuron-specific genes sc and ase, by promoting the rapid turnover of their transcripts in the wing imaginal disk.
Subcellular Localization:
[Nuclear factor NF-kappa-B p68 subunit]: Nucleus; [Nuclear factor NF-kappa-B p110 subunit]: Cytoplasm; [Nuclear factor NF-kappa-B p49 subunit]: Cytoplasm.
Sequence:
MNMNQYYDLDNGKNVMFMNDASSTSGYSSSTSPNSTNRSFSPAHSPKTMELQTDFANLNLPGGNSPHQPPMANSPYQNQLLNNGGICQLGATNLINSTGVSFGVANVTSFGNMYMDHQYFVPAPATVPPSQNFGYHQNGLASDGDIKHVPQLRIVEQPVEKFRFRYKSEMHGTHGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFQTNLDSPHSHQLVVRKDDRDVCDPHDLHVSKERGYVAQFINMGIIHTAKKYIFEELCKKKQDRLVFQMNRRELSHKQLQELHQETEREAKDMNLNQVRLCFEAFKIEDNGAWVPLAPPVYSNAINNRKSAQTGELRIVRLSKPTGGVMGNDELILLVEKVSKKNIKVRFFEEDEDGETVWEAYAKFRESDVHHQYAIVCQTPPYKDKDVDREVNVYIELIRPSDDERSFPALPFRYKPRSVIVSRKRRRTGSSANSSSSGTESSNNSLDLPKTLGLAQPPNGLPNLSQHDQTISEEFGREKHLNEFIASEDFRKLIEHNSSDLEKICQLDMGELQHDGHNRAEVPSHRNRTIKCLDDLFEIYKQDRISPIKISHHKVEKWFIEHALNNYNRDTLLHEVISHKKDKLKLAIQTIQVMNYFNLKDVVNSTLNADGDSALHVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVKEEHLSCVESFLNGVPTVQLDLSLTNDDGLTPLHMAIRQNKYDVAKKLISYDRTSISVANTMDGNNALHMAVLEQSVELLVLILDAQNENLTDILQAQNAAGHTPLELAERKANDRVVQLLKNVYPEKGELAMTWIPCKVKEEIDSSSDESSDAGQLEIKSEEMDIETKDEDSVELDLSSGPRRQKDESSRDTEMDNNKLQLLLKNKFIYDRLCSLLNQPLGHGSDPQDRKWMQLARQTHLKQFAFIWLGAEDLLDHVKRKGASVEFSTFARALQAVDPQAYALLVNPT
The following text describes a protein:
Function:
Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MDNIVTQKTNKSECLNKNVHLDPFLILAKSAKGAALKSLIEQVLEAPGVYVFGELLELQCIQQLVNSEHNKHLKLLELFTYGTFQDYVNQAYGLPPLTPLMKKKLHQLTVVALSAKSKYVSYESLMKELHLNNIRDLEDLLISAIYANIIQGRLDQQNSRLEVEWAMGRDVRTEDMDSIINTLNNWCSSCETILGSIETQTASANAFLSEDAIRRAKIDTEVENIMSTIKKTSSHEMDLATSDTRLSSSHPAPSSGIEVKPKKSKVKGLRGSGMKLWSSKNTS
The following text describes a protein:
Function:
May regulate the intracellular trafficking of ran.
Sequence:
MSETFEKRQLYGGAIEIDIPRRFIDVTSYRHIPDHQELFSDEKSDQSVIIELNEFQDHISNANAIKHHYEVLVEDAGISTDKSVILNFRELTQAEMPNFDASIPKYVLLAQQKIAKFNETAENTINIYMALVRLEKSKTDLLITFNEAIALAPTSSSVAVVQNLTPSNDQSKSEQLFLTMLKSFKIKDYSLFVHN
The following text describes a protein:
Function:
Inhibitor of protein-phosphatase 1.
Sequence:
MAASTASHRPIKGILKNKSSTTSSVVASAEQPGRSVDEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPSTPYHSMVGDDEDALSDSETTEALTPDILAKKLAAAEGSEPKCRLHEQESSGDEDSDLSPEEQGKKKRQFEMKRKLHYNEGLNIKLARQLISKDLHEDEEDEEMSETATGESVNMEASNEGSTTSDQLQDTSQSS
The following text describes a protein:
Function:
Required for processing of 5.8S rRNA (short form) at site A3 and for 5' and 3' processing of pre-tRNA.
Miscellaneous:
MISCELLANEOUS: Present with 846 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSGSLSRGNGGKKVLNKNQLLKRNRIRNARSIRAEAVAASSTKTGTPSDLSESGSKLNVDQFISSRQFEVKQLQLAMHNSKAASSTRIFQALPRKLRRRTASHNVRRIPKRMRNRALREMRKSDQQDVLKGSSASSRKAHGLNAKQLYKARMSIKLLRLASKSTSMKLSMPPEVTSSNCHVRQKIKTLKRMIKESSTANPNIKLLNNRMGSYDCTGVNELAPIPKGRVKYTKRQKHFAWLPTHIWNAKRSHMMKRWGYQMVWAPTQKCFKLTHRLGGDTCSSDGALCMDSSYIGTIIVKDKSNDSEGDFLKSIIGKLTAERANLRKYREGQVLFQGLIYSFNEENGEDSTKPLGPCDVFWVQKDTAIIRLHPSIYTQVFNILLQHKEKLTVQDCRYSLASVTLKGAKALESLASCLRSTEYSKSFEQFKMVSMITDHNALPQRCTFAFEAIDPRHLAAPKKLNDSQRKTVNSDDILSLHENYPQDEINAVFNELCDPESRTQSYNNQNTLKEISARRYKLLTATPNSINKTTVPFKESDDPSIPLVIIRRLKTRDWIVVLPWFWLLPLWHLLNRIPRMYHIGLRQFQQIQYENKQLYFPDDYPFTQLGYIENSFYKKEASKTKWDRKPMGKRINFEKIKDIHNTKLPAYSGEIGDFFSSDWRFLQILRNGIDYLQRNDKTLELMDSKKTGQFNAQGVRDINCVNDVLEFCKDYEAKTKAMSLSIEENIPVALCKNRKCQFRTPDSISVNSSSFSLTFFPRCIIAVSCTLLERGHPKDNARIYQVPEKDLEHWLQLAKGVYRPNGRKDHDLKIPLPEVHDLIGFITSGTYHLNCGNGMGIGFIDHHAAIRQPTRYVLIRNVGTNTYRLGEWSKISV
The following text describes a protein:
Function:
D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Sequence:
MYVLVLSLGDPVSRTFLELHPMPLVETRGDIEVRKYGEIPAVVYKGEPTEFYREDILASLGKYAIFISRHEMSNPRPLFTVHTPGSWPDVSVANPRLASALFRALCKHAYEPFECAFEATHHAPNTSLVSATFIEVGSTEAEWRDKRAVGVLAQALEEALTKEFEGPTPTMAIGDLHYVTISDSVLRGEFDLGHVVPKYINITTNIVENILKKHTISIKKTIIFRKNIKNPIRTEIIELLRAKGIEVTLKG
The following text describes a protein:
Function:
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Localization:
Cytoplasm.
Domain:
The PRC barrel domain binds ribosomal protein uS19.
Sequence:
MIKKEEVYKIGLFNKPHGIHGELQFTFTDDIFDRVDCDYLICLLDGIFVPFFIEEYRFRSDSTALVKLEGIDTAERARMFTNVEVYFPVKHAEEAEDGELSWNFFVGFRMEDVRHGELGEVVEVDTATVNTLFVVEQEDGEELLVPAQEEFIVEINQEKKLITVELPEGLLNLEDLEED
The following text describes a protein:
Function:
Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.
Sequence:
MKSPFFFLSALALTLRDSSPSFATAFRLAVTRCARQGIHAPSSSSSSSSRCLVASASALAGPSEELLDLFNRQVTQEFTASQVYLSASIWFDQNDWEGMAAYMLAESAEEREHGLGFVDFANKRNIPIELQAVPAPVSCAEWSSPEDVWQSILELEQANTRSLLNLAEAASTCHDFAVMAFLNPFHLQQVNEEDKIGSILAKVTDENRTPGLLRSLDVVSFLGPCLFRSV
The following text describes a protein:
Function:
Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
Sequence:
MACPHQVSIDVIRSKSLQEIITEKTNAANIENEDDPFYLVDISDVINKYKTLFFKVFFITHIFLTAMKSNPDFQIAATLCGLGTGLDVASAGEIETAVAVGLKDEDVIYSNTCKGISHLKVAAKENLTQMTFDSEVELHRIKRLYPSARLVLRLLVDDSHSELKLGVKAGASFSRVPHLLKVAKELGLNVIGTSFHVGSECGSPDAYAKAIEKSRRVFDIAKGLGMKFNLLDIGGGYPGQINELFTNISRIINKALDIHFPSDSGVRIISEPGQYFSCSSSILVANIISKRIRFEDDDTQIEGYPSDKENMEITYHINEGVIGAFISKLIINLLYIPKKLIKSNEKCYRSSMWGPTCTPVDQILSDYNLPEMEVGEWVYYEIFKCVTRSENVC
The following text describes a protein:
Function:
Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT) (By similarity).
Sequence:
MPQQNYLDELTPGFTPLLAIKEASRCLLCHDAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEKLCQRGCTRSGIDKPIDIARLQRFITDFEQQTAMQIYQPGSKTRGKVAIIGAGPAGLQASVTLTHLGYDVTIYEKQPQPGGWLRHGIPAFRLPQSVLDQEIARIVEMGVNIKCNCDVGGSLSLAQLKAEYRAVLMTVGMSCGSDLPLFEQASHVEIAVDFLQRARQADGDISVPRSALIIGGGDVAMDVASTLKILGCPSVTCVAREELAEFPASEKEFTSTQALGVSIIDGFTPVAVSGNKVTFHHVRHSGELTLEAENIILAVGQHARLDNFAEIKAQHNIIDTHNYQTDDPAIFAAGDIVKGDKTVVYAVKTGKEAAQAIHHYLEEACSC
The following text describes a protein:
Function:
May play a role in photosystem I and II biogenesis.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.
Sequence:
METATLVAISISGLLVSFTGYALYTAFGQPSQQLRDPFEEHGD
The following text describes a protein:
Function:
Integral membrane transporter that imports quinic acid to be catabolized as a carbon source.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MGDDLEASKSSLDRKEFPSAEHVEGTTVGIVRAVDPHQLESLPYGPSGFKGIFSSKYVFGAAFLASMGGFSMGYDMGVISIINSMDKFHAAYPRAESAFGKGFMTGMLLLGAFVGCIFMPYLADRISRKWALTAMVIVFNFGAILQTAATNYDMLVAGRFIGGIGVGTLAMGAPLYISEVSPPHMRGTLLVLESISITLGVVVAFYITYGTRHMATEACFRLPFGLQMVTATILGAGIHFFPYSPRWLALVNRQDDCMSSLCKLRGLTSSDERVQLEYQQIIAEINFQRAVLAKKHPGASGTKLEVLSWMNLFTRKLWKRTAVGVGVAFFQQFSGINAFIYYAPTLFESLGQTAETSLILSGVFNVLQLIAAIVCFLVIEKVGRRPLAIFGGFGTAVAYIIIAVLSGLYSTSWASHSAAGWGCVAMAFIFILIYGVTYSPLGWALPSEVFSTTSRSKGVALATCTIWLSDFIVGVVTPSMLADIGYRTYIFFAVMCSLAGIWAFFLVPETGGKSLEEIDELFGDSSAREEWELAQEAIMTGSTK
The following text describes a protein:
Function:
Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.
Sequence:
MFLINGHKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFWPQLEQEMKTLAAEQQNGVLKVVISRGSGGRGYSTLNSGPATRILSVTAYPAHYDRLRNEGITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVMPVCACGDVSFSSATLYEYLAPLCERPN
The following text describes a protein:
Function:
Binds to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulates their kinase activity. During insulin stimulation, it also binds to IRS-1.
Sequence:
MYNTVWNMDRDDADWREVMMPYSTELIFYIEMDPPALPPKPPKPMTPSSTNEVKDSSGVALQDAEWYWGDISREEVNDKLRDMPDGTFLVRDASTKMQGDYTLTLRKGGNNKLIKIYHRDGKYGFSDPLTFNSVVELINHYRHESLAQYNPKLDVKLMYPVSRYQQDQLVKEDSIDAVGKKLQEYHAQYQEKSKEYDRLYEEYTRTSQEIQMKRTAIEAFNETIKIFEEQCHTQERYSKEYIERFRREGNEKEIERIMMNYEKLKSRLGEIHESKMRLEQDLKKQALDNREIDKKMNSIKPDLIQLRKIRDQYLVWLNHKGVRQKRLNDWLGIQNENRDDTYFVNEEDENLPHYDEKTWFVGDLNRTQAEDLLRGKPDGAFLIRESSKKGCYACSVVADGEVKHCVIYSTPRGYGFAEPYNLYGTLKELVLHYQQTSLVQHNDSLNVRLAYPVYAQMPALGR
The following text describes a protein:
Function:
Plays a role in the cell cycle. Involved in cytokinesis. Component of the cell division ring. In the absence of profilin, caps the barbed end of actin filaments, thus preventing subunit addition and dissociation. In the presence of profilin, nucleates actin filaments that grow rapidly from their barbed ends.
Subcellular Localization:
Nucleus. Note=Nuclear, and septum.
Sequence:
MRNSSKGQDPNFSYDSILSTPTPSARRTIGPRAPKSKTTYHKPPSSIESVSTLIQPNKSQSVTSPYVKQFTFSSKEYNSHNKHALQNSQLPLPKTPEKSTVHRPKANKVEVTDLPSSSSVEHLHTSKHLKGPRLPKNIIKSSEDVQIAPVTPPVHSRSFDPLPKPPVPSVPVSKTKRRTKHKLAPVVEVPEITNEVSPKFTSTNDEQVYRLRSIRAGSPNSVCSFQFEIPSTRPPSLDQLIHLFNDFLRHPVFDFDENAIEMLQSCTPDEKWCFIRSNFAGFDDPSFQIPELAAVHRPVSWFVIQLWNKTISNLQLITLSSLLSTQSDRWISLFLELQGLRALHNLLTYFNSSAVVQPQQAEVPRCMLTLLKKKPTLVTSNSYIFQAITVTLISPNLLPRKVAADLLTWVLSLKEPLVVSILETGFKEINAEYEKEVPLFFGWIKSFKDIILEKELARTPPSSPARNSASSSPSNIAFLEYCTSTMEFINQLIVACEELEQGFDLDILDSLRESGIHEVIQLLRNFPDQQLEKQLNIYESEEERRTISQTTHEDVDSFMSNESSILSSFNEFASNEVGRLLESTIQNILLAKGTEKQKVKLIKVFNSLLQRILLNSKVSNESFEDSLQASLNMLTERFYSDDTARNALKEAKASRAMAEKMVIERDAMAAQVNLGAEDLIAKLNKEVEDQKDVILSQKRTNETLKTEIDALQKSHVTQIQRSEVELRELYLLINSDSFQGSTNSKERIIEYLLDKLDLRKKEIAAESTLWSNDGIDDKLRDLREQMSRQSSQPSTVSTILQIPDKKFHRPFPRHLHRYVGRSASESLTSEKDESIKSMKGIDDFANLEIPGKGIESNVVIKDISNQTHEINSVENKAETVSNNSKITNFDIPNDATSLPTIITHPTPPPPPPLPVKTSLNTFSHPDSVNIVANDTSVAGVMPAFPPPPPPPPPLVSAAGGKFVSPAVSNNISKDDLHKTTGLTRRPTRRLKQMHWEKLNSGLEFTFWTGPSDEANKILETLHTSGVLDELDESFAMKEAKTLVKKTCARTDYMSSELQKLFGIHFHKLSHKNPNEIIRMILHCDDSMNECVEFLSSDKVLNQPKLKADLEPYRIDWANGGDLVNSEKDASELSRWDYLYVRLIVDLGGYWNQRMNALKVKNIIETNYENLVRQTKLIGRAALELRDSKVFKGLLYLILYLGNYMNDYVRQAKGFAIGSLQRLPLIKNANNTKSLLHILDITIRKHFPQFDNFSPELSTVTEAAKLNIEAIEQECSELIRGCQNLQIDCDSGALSDPTVFHPDDKILSVILPWLMEGTKKMDFLKEHLRTMNTTLNNAMRYFGEQPNDPNSKNLFFKRVDSFIIDYSKARSDNLKSEEEEASQHRRLNLVNNHKEHVLERAMSENNKMDNEAMDGFLDKLRNVKLESHHKPRNRSAITMGKEHLIEAPNTSTKSSPAKNELFVPKRSSVKSDLAKVRPRYPKGSESTDGLSDALNITPTKKGEVSSKAKKGYNYEKRRSGRQVSDSYVLNKNSKNKSNKGRSASYTFSDPSSLEDSNRQKPFNGEKFRRFSSKSRRGSQNRDSKKTGKARKDKGINNNQTSPQNKPSKESLKSDTISNEKKVFPQKASKVNLLTPTISNGTRASKHANEKENTFPRGVENNLVAPMIPNNTELNEDTSAVSRNLENATNDLKETFPTTTTISTARAKPGNNDINTILRRNNSRGRRRMLQQMSPLKSNKFSGTNDLNFQQATKPDGSNKSSYMERLEKLKQNSERHLQSVGGKKVYSSEETPVNKILVSPSVSILDHNRILSQSTPIKSPQRAQEMLAGLLSGKLAPKENEK
The following text describes a protein:
Function:
The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating dsDNA into templates for DNA synthesis. An ATP-dependent 5'-3' DNA helicase that prefers 5'-tailed substrates (have a 5' single-stranded (ss)DNA tail). ATP, GTP and UTP are equally active for helicase activity in vitro, while dATP and CTP are less active. Its DNA-dependent ATPase activity is stimulated by ssDNA. Binds ss- but not double-stranded (ds)DNA. Rescues a temperature-sensitive E.coli dnaB mutation in vivo.
Domain:
Within each hexamer the N-terminal domains (NTD) form a ring, as do the ATPase domains; the 2 rings stack. The HPI (Helicobacter pylori insertion) forms a helix-turn-helix that protrudes from the ATPase domain; one side is positively charged while the other is negatively charged. The HPI inserts form a collar on the exterior of the ATPase domains. In the dodecamer (which has 4 layers) the homohexameric rings stack via their NTD rings.
Sequence:
MDHLKHLQQLQNIERIVLSGIVLANHKIEEVHSVLEPSDFYYPPNGLFFEIALKLHEEDCPIDENFIRQKMPKDKQIKEEDLVAIFAASPIDNIEAYVEEIKNASIKRKLFGLANTIREQALESAQKSSDILGAVEREVYALLNGSTIEGFRNIKEVLESAMDLITENQRKGSLEVTGIPTGFVQLDNYTSGFNKGSLVIIGARPSMGKTSLMMNMVLSALNDDRGVAVFSLEMSAEQLALRALSDLTSINMHDLESGRLDDDQWENLAKCFDHLSQKKLFFYDKSYVRIEQIRLQLRKLKSQHKELGIAFIDYLQLMSGSKATKERHEQIAEISRELKTLARELEIPIIALVQLNRSLENRDDKRPILSDIKDSGGIEQDADIVLFLYRGYIYQMRAEDNKIDKLKKEGKIEEAQELYLKVNEERRIHKQNGSIEEAEIIVAKNRNGATGTVYTRFNAPFTRYEDMPIDSHLEEGQETKVDYDIVTT
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.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MATKSAASVVDWSKIYTGLGLDKQTLTSLQSFRARHSTALNKNSALKATAPSIDLSHYKSVLKDQQAVQLAEKVLGEFKPVNYDVSKWNGVVEAFEGKAVAAAKETVSKISTEEASLQATLSNIKDARPFEDLTVDEVAKARPEIAKAVETMLKKGKWSVPGYREKFGDLSLM
The following text describes a protein:
Function:
PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side.
Sequence:
MAAIASTAITTVAIASPSSVAVSRPRAAASLAISGFQGQKLASVCNGGRVTMAQAGAVPDGVADRKPDAKEAPKGFTPPTLNADTPAPIFGGSTGGLLRKAQVEEFYVITWESPKEQIFEMPTGGAAIMRSGPNLLKLARKEQCLALGARLRTKFKIQYQFYRVFPNGEVQYLHPKDGVYPEKVNAGRSPVGVNNRSIGKNANPAELKFAHKQAYDL
The following text describes a protein:
Function:
Inhibits ADP- (IC(50)=66 nM) and collagen-induced (IC(50)=100 nM) aggregation of human platelets. In vitro, inhibits adhesion of endothelial cells to vitronectin, type-I collagen and, to a lower degree, fibronectin and laminin.
Miscellaneous:
MISCELLANEOUS: The disintegrin belongs to the medium disintegrin subfamily.
Subcellular Localization:
Secreted.
Sequence:
EAGEECDCGAPANPCCDAATCKLRPGAQCAEGLCCDQCRFMKEGTVCHRARGDDVDDYCNGISAGCPRNPFH
The following text describes a protein:
Function:
Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MCRSLLDELVDCTRQHTVTIGFACSEPNKKVQDCLKQYSTEQWKDKFREDELRLKKEFLIANGRWPSQYQTSGHIVE
The following text describes a protein:
Function:
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Subcellular Localization:
Cytoplasm.
Sequence:
MSYQDLKECKIITAFITPFHEDGSINFDAIPALIEHLLDHHTDGILLAGTTAESPTLTHDEELELFAAVQKIVNGRVPLIAGVGTNDTRDSIEFVKEVAEFGGFAAGLAIVPYYNKPSQEGMYQHFKAIADASDLPIIIYNIPGRVVVELTPETMLRLADHPNIIGVKECTSLANMAYLIEHKPEEFLVYTGEDGDAFHAMNLGADGVISVASHTNGDEMHEMFIAIAESDVKKAAAIQRKFIPKVNALFSYPSPAPVKAVLNYMGFEAGPTRLPLVPAPEEDAKRIIKVVVDGDYEATKATVTGVLRPDY
The following text describes a protein:
Function:
Electrogenic proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides. Transports neutral and monovalently charged peptides with a proton to peptide stoichiometry of 1:1 or 2:1 (By similarity). Primarily responsible for the absorption of dietary di- and tripeptides from the small intestinal lumen (By similarity). Mediates transepithelial transport of muramyl and N-formylated bacterial dipeptides contributing to recognition of pathogenic bacteria by the mucosal immune system (By similarity).
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein. Note=Localized to the apical membrane of enterocytes.
Domain:
The extracellular domain (ECD) region specifically binds trypsin.
Sequence:
MGMSKSYGCFGYPLSIFFIVVNEFCERFSYYGMRALLILYFRRFIGWDDNLSTAIYHTFVALCYLTPILGALIADSWLGKFKTIVSLSIVYTIGQAVTAVSSINDLTDYNKDGTPDNLSVHVALSMIGLALIALGTGGIKPCVSAFGGDQFEEGQEKQRNRFFSIFYLAINAGSLISTIVTPMLRVHECGIYSQKACYPLAFGVPAALMAVSLIVFVIGSGMYKKFQPQGNVMGKVVKCIGFALKNRFRHRSKQFPKREHWLDWAKEKYDERLISQIKMVTKVMFLYIPLPMFWALFDQQGSRWTLQATAMSGKIGLLEVQPDQMQTVNAILIVVMVPIMDAVVYPLIAKCGFNFTSLKRMTVGMFLASMAFVMAAIVQLEIDKTLPVFPKQNEVQIKVLNIGNGAMNVSFPGAVVTVSQMSQSDGFMTFDVDKLTSINISSTGSPVIPVTYNFEQGHRHTLLVWAPNNYRVVKDGLNQKPEKGENGIRFINSLNESLNITMGDKVYVNVTSHNASEYQFFSLGTKNITISSTQQISQNCTKVLQSSNLEFGSAYTYVIGTQSTGCPELHMFEDISPNTVNMALQIPQYFLITCGEVVFSVTGLEFSYSQAPSNMKSVLQAGWLLTVAVGNIIVLIVAGAGQFSEQWAEYILFAALLLVVCVIFAIMARFYTYVNPAEIEAQFDDDEKKNLEKMNVYSTVTPVSQTQM
The following text describes a protein:
Function:
Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, resulting in the formation of carboxyl biotin. When associated with the beta1 subunit AccD1, is involved in branched amino-acid catabolism with methylcrotonyl coenzyme A as the substrate.
Sequence:
MGITRVLVANRGEIARRVFATCRRLGLGTVAVYTDPDAAAPHVAEADARVRLPQTTDYLNAEAIIAAAQAAGADAVHPGYGFLSENAEFAAAVQEAGLTWVGPPVDAVRAMGSKIESKKLMAAAGVPVLEELDPDAVTTAQLPVLVKASAGGGGRGMRVVHELSALPAEVEAARREAQSAFGDPTVFCERYLPTGHHVEVQVMADTHGTVWAVGERECSIQRRHQKIIEEAPSPLVERVPGMRAKLFDAARLAASAIGYTGAGTVEFLADDSPGREGEFYFLEMNTRLQVEHPVTEETTGLDLVELQLMIADCGRLDTEPPPAQGYSIEARLYAEDPAHGWQPQAGVMHTIEVPGVRAQFDSLGQRTGIRLDSGIVDGSTVSIHYDPMLAKVVSYGATRRQAALVLADALVRARLHGLRTNRELLVNVLRHPAFLDGATDTGFFDTHGMAELSTPLADTATLRLSAIAAALADAEHNRASAGVFSSIPSGWRNLASGYQVKTYRDDADTEHRVEYRFTRTGLALPGDPVVQLVSADVDQVVLAQDGVAHGFTVARHGPDVYVDSARGPVHLVALSRFPEPSSAVEQGSLVAPMPGNVIRIGAEVGDTVTAGQPLIWLEAMKMEHTIAAPADGVLTHVSVNTGQQVEVGAILARVEAPQNGPAEGDSP