lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular Localization:
Cell projection, growth cone. Cytoplasm, perinuclear region.
Sequence:
MKEFDDFNFSVEKYTKDLTRECVGGSDLQQRKKEIEAYNETTAATLKQTCKKNYMEFIQTAKEISRNLESEMYQLSHILIEQRNILATMTDGKTSSHLKAESLEAESTTATEDLENSHATRAVKEMVQGFNGNLEGKTFLNEGALIELDSNDYRPIQRVFFFLFNDVLIVCKVKHDKRLDFLTEYDPKKIAVINIKDLDGVKNAINIITPDGSKIYQSITAAGKTEWIEKLEEAFRFDQQKKPKKGQAPQPPTRAKQQSKASTPEKETTPQSPGQPKSLEDETPEWLSTASEEIQTLVAQRHFEDAQELIKRTQDFLRNENRKKLPLADAIETKVKQQELKLINVLLKELSNSHNRNLQIALRAAKRPLKILVEMGRYRQASATLLKVCAVSLRVAQREARRNNADISELFFCDLTQVACDFLTAFEKQPACVSALVVWCNAELQYFASQLIKHYLTKGTSLESVAKCVERVRKPSTKLTEIGLDISYHLEGLLRTTLESLIEESKERLLDSVGRTEESWQPYNLQTKSNLKRLLLELDVLGIDVRAQATGDTWINLTQSTVVFIRHFLQLTEYCGCLAKCETLLQSLELLLKELFIAQHSLKPPSDMAVDPNFVMKNKIFLVDNLLPIAIDKFRQISGRQCEGLRELHTKMSRQQGAPVPRQRSVYTTDVF
The following text describes a protein:
Function:
Involved in sperm motility. Its absence is associated with genetic background dependent male infertility. Infertility may be due to reduced sperm motility in the female reproductive tract and inability to penetrate the oocyte zona pellucida (By similarity).
Subcellular Localization:
Cytoplasm. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side. Note=Becomes associated with the spermatid mitochondrion capsule at step 16 of spermatogenesis.
Sequence:
MCDQTKHSKCCPAKGNQCCPPQQNQCCQSKGNQCCPPKQNQCCQPKGSQCCPPKHNHCCQPKPPCCIQARCCGLETKPEVSPLNMESEPNSPQTQDKGCQTQQQPHSPQNESRPSK
The following text describes a protein:
Function:
DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability.
Subcellular Localization:
Nucleus.
Sequence:
MEAVLRHLNNILELLAVSRTDRVREWDRPTTQRAFKWAEYCEQLHSRYQSNPTVRSSLESGLTDTNRRLKETFPSYSPVEFSELAQCQHKLIVYLLRNPSSPHFIIEMLFPDQNSPSQELLAAQNSLVTRKSAFSLLCCTVNRTSSYYGLQTEPEVRGKLLGKLLNSILARPGNEEHAKCLLDSVRCNSAGKVDGFYDVIAGALLCSSDESQRFIITWLKESDGGLNTFCSVISPEVCAVISRQSPEFRKLYWGALKQWASCLEYDVIESVWVTSEGAGSFDVLADRLRDLINSGESLKEETETALKALTLQDGDFSVKGVSVWTDLTLQLKL
The following text describes a protein:
Function:
Uptake of allantoin into the cell. Allantoin uptake is not dependent on sodium, and PucI is likely to be a proton-coupled symporter. Shows highest recognition for binding of allantoin, good recognition for binding of hydantoin, L-5-benzylhydantoin and 5-hydroxyhydantoin, and to a lesser extent for a range of nucleobases and nucleosides.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MKLKESQQQSNRLSNEDLVPLGQEKRTWKAMNFASIWMGCIHNIPTYATVGGLIAIGLSPWQVLAIIITASLILFGALALNGHAGTKYGLPFPVIIRASYGIYGANIPALLRAFTAIMWLGIQTFAGSTALNILLLNMWPGWGEIGGEWNILGIHLSGLLSFVFFWAIHLLVLHHGMESIKRFEVWAGPLVYLVFGGMVWWAVDIAGGLGPIYSQPGKFHTFSETFWPFAAGVTGIIGIWATLILNIPDFTRFAETQKEQIKGQFYGLPGTFALFAFASITVTSGSQVAFGEPIWDVVDILARFDNPYVIVLSVITLCIATISVNVAANIVSPAYDIANALPKYINFKRGSFITALLALFTVPWKLMESATSVYAFLGLIGGMLGPVAGVMMADYFIIRKRELSVDDLYSETGRYVYWKGYNYRAFAATMLGALISLIGMYVPVLKSLYDISWFVGVLISFLFYIVLMRVHPPASLAIETVEHAQVRQAE
The following text describes a protein:
Function:
Involved in the biosynthesis of the polyketide antibiotic aureothin. Catalyzes the oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA), an unusual polyketide synthase starter unit. Reaction mechanism involves the generation of a peroxodiiron(III/III) intermediate, which effects the initial oxidation of p-aminobenzoate to p-hydroxylaminobenzoate (Ar-NHOH). Ar-NHOH is then probably directly converted to the fully oxidized p-nitrobenzoate via a four-electron N-oxidation, bypassing the formation of a nitroso compound.
Sequence:
MREEQPHLATTWAARGWVEEEGIGSATLGRLVRAWPRRAAVVNKADILDEWADYDTLVPDYPLEIVPFAEHPLFLAAEPHQRQRVLTGMWIGYNERVIATEQLIAEPAFDLVMHGVFPGSDDPLIRKSVQQAIVDESFHTYMHMLAIDRTRELRKISERPPQPELVTYRRLRRVLADMPEQWERDIAVLVWGAVAETCINALLALLARDATIQPMHSLITTLHLRDETAHGSIVVEVVRELYARMNEQQRRALVRCLPIALEAFAEQDLSALLLELNAAGIRGAEEIVGDLRSTAGGTRLVRDFSGARKMVEQLGLDDAVDFDFPERPDWSPHTPR
The following text describes a protein:
Function:
A tubulin-like GTPase that forms filaments, which are required for positioning viral DNA and capsids in the middle of the host cell for optimal replication. The motor component of a partition system which pushes phage DNA (encased by protein gp105) to the center of the bacterial host cell. Also required for movement of phage capsids to the vicinity of the viral DNA and rotation of the encased viral DNA at midcell. Forms filaments during the lytic phase, which position phage DNA at the center of the bacterial host cell. Filaments have a three-stranded intertwined achitecture and form a spindle-like cytoskeleton within the infected cell. Has GTPase activity. Filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling, and switch from growing in a polar manner to catastrophic depolymerization, i.e. they display dynamic instability, like tubulin. In infected host cells the filament ends close to the cell pole are relatively stable, while the other end near the phage DNA is highly dynamic. Both capsid movement and DNA rotation probably require treadmilling (Probable).
Subcellular Localization:
Host cytoplasm. Note=In infected host cells forms a spindle-like structure emanating from each cell pole.
Domain:
Consists of two domains: a nucleotide-binding N-terminus that hydrolyzes GTP and a C-terminus domain necessary for polymerization. The domains are bridged by a long, central helix. Interactions between the C-terminus and the following monomer drive polymerization.
Sequence:
MPVKVCLIFAGGTGMNVATKLVDLGEAVHCFDTCDKNVVDVHRSVNVTLTKGTRGAGGNRKVILPLVRPQIPALMDTIPEADFYIVCYSLGGGSGSVLGPLITGQLADRKASFVSFVVGAMESTDNLGNDIDTMKTLEAIAVNKHLPIVVNYVPNTQGRSYESINDEIAEKIRKVVLLVNQNHGRLDVHDVANWVRFTDKHNYLIPQVCELHIETTRKDAENVPEAISQLSLYLDPSKEVAFGTPIYRKVGIMKVDDLDVTDDQIHFVINSVGVVEIMKTITDSKLEMTRQQSKFTQRNPIIDADDNVDEDGMVV
The following text describes a protein:
Function:
Catalyzes the efflux of L-methionine, L-leucine, L-isoleucine and L-valine. Activity is dependent on electrochemical potential.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MSGLKQELGLAQGIGLLSTSLLGTGVFAVPALAALVAGNNSLWAWPVLIILVFPIAIVFAILGRHYPSAGGVAHFVGMAFGSRLERVTGWLFLSVIPVGLPAALQIAAGFGQAMFGWHSWQLLLAELGTLALVWYIGTRGASSSANLQTVIAGLIVALIVAIWWAGDIKPANIPFPAPGNIELTGLFAALSVMFWCFVGLEAFAHLASEFKNPERDFPRALMIGLLLAGLVYWGCTVVVLHFDAYGEKMAAAASLPKIVVQLFGVGALWIACVIGYLACFASLNIYIQSFARLVWSQAQHNPDHYLARLSSRHIPNNALNAVLGCCVVSTLVIHALEINLDALIIYANGIFIMIYLLCMLAGCKLLQGRYRLLAVVGGLLCVLLLAMVGWKSLYALIMLAGLWLLLPKRKTPENGITT
The following text describes a protein:
Function:
Putative odorant or sperm cell receptor.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
PLKLVSNLSSSVVITSQLLSEPVYYMVSDFVLLGLSSSQELQLFFFVFFSVLYVVIVLGNLLIILMVTLDNTLHSLMYFLLGNLSFVDICQASFATPKMIVDFLSEHKTISFSGCIAQIFFIHLFTAGEMVLLVSIAYDRYVAICKPLHYVIIKSQRTCIVLVMISWAVGLVHTLSQLSFTMNLPFCGPNVVDSFFLILFFGPCIFIYVWPFTTYPVDKVLAIFYTIFTPILNPIIYTLRNRDMKTAMRKIMMYYLRPKKISEMPLVLRNSL
The following text describes a protein:
Function:
Cysteine protease effector that inhibits host cell autophagy by targeting lipid-conjugated ATG8 family proteins on pre-autophagosomal structures. Specifically hydrolyzes the amide bond between the C-terminal glycine residue and an adjacent aromatic residue in ATG8 proteins conjugated to phosphatidylethanolamine (PE), producing an ATG8 protein that cannot be reconjugated by host ATG7 and ATG3. Mechanistically, Ravz interacts with ATG8 proteins conjugated to PE via its LIR motifs, extracts them from the membrane of autophagosomes and integrates the PE part into its own lipid-binding site. It then removes the lipid component of the ATG8 protein. Also able to mediate delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) during non-canonical autophagy. Inhibits host ubiquitin recruitment to bacteria-containing vacuoles, suggesting that it is able to mediate delipidation of other proteins in addition to ATG8 proteins. It is however not involved in the exclusion of autophagy adapters from bacteria-containing vacuoles decorated with ubiquitin.
Subcellular Localization:
Secreted. Host cytoplasmic vesicle membrane. Note=Translocated into the host cell via the type IV secretion system (T4SS) (Probable). In host cells, localizes to mature autophagosome membranes.
Domain:
The LIR motifs (LC3-interacting regions) are required for the interaction with ATG8 family proteins. The LIR motifs 1 and 2 at the N-terminus bind one ATG8 protein and the LIR motif 3 at the C-terminus binds another ATG8 protein. Among ATG8 proteins, the LIR motif 3 has preference for host GABARAP (GABARAP GABARAPL1, GABARAPL2) compared to LC3 (MAP1LC3A, MAP1LC3B, MAP1LC3C); The membrane targeting (MT) region binds phosphatidylinositol 3-monophosphate (PI3P). The MT region, together with the alpha-3 helix promote localization to high-curvature membranes, intimating localization to highly curved domains in autophagosome intermediate membranes. The alpha-3 helix is involved in extraction of the phosphatidylethanolamine (PE) moiety and docking of the acyl chains into the lipid-binding site.
Sequence:
MKGKLTGKDKLIVDEFEELGEQESDIDEFDLLEGDEKLPGDSELDKTTSIYPPETSWEVNKGMNSSRLHKLYSLFFDKSSAFYLGDDVSVLEDKPLTGAYGFQSKKNDQQIFLFRPDSDYVAGYHVDAKSDAGWVNDKLDRRLSEISEFCSKATQPATFILPFVEMPTDITKGVQHQVLLTISYDPKSKQLTPTVYDSIGRDTYSESLSSYFKGKYRTTCDEILTQSIEKAIKSTDFTLGKFTRAAYNHQNRLTEGNCGSYTFRTIKEVISSSAQGTEVKIPGSGYITSNSYLTSQHVQDIESCIKYRNLGVVDIESALTEGKTLPVQLSEFIVALEDYGKLRSQQSEKSMLNFIGYSKTAKLTAVELLIGILNDIKGKNEISESQYDKLVKEVDCLMDSSLGKLVQFHLKNLGAESLQKLVLPCVKFDDTIDDFVTIEKDELFDVPDITGEELASKKGIEQGALDKEALLKQKQIKTDLLDLREEDKTGLKKPLHGGIKVK
The following text describes a protein:
Function:
Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins.
Subcellular Localization:
Nucleus.
Sequence:
MSTPAQQLNEFIESPKVIKEGYEIIDQLMKNNYNVNSLVTDLGDTLPSEDERIRFRATSLLTYCLIKYPIKEESKDVFVDYLASRLVDAVCLEPILTALLQLVTKKPSDEIINEIAMAYSCMRTQLYTKEVRILVYQFYKVFINYYQATEVIDTCVQLIELERDPECLKEVFDLIKLVSQKNEIDADSAPLLFDCASAYFPILYPPKGDEALRIDLTNKILDAFVSAPIYAQFALPFLLDKLDADLSSIKLEALKAIYFCIQRFELKYVYAYFTHIWESIEQNISTVGVVEVNEFAFAIASYFCSLDDFHSKNLMESIKMFCLRMMSETDEIIINFVNGLLEELTKKSEKFFKVFVPVFIQCFHDQLQDADDRPKEQFERELFIVRLIYQRIIEGMPLLDCVKGQVAWDLHRLATPLHPCFVSLLDIDVSLALLNLLGEQRMVPFQNAIELSENKCHDAIPILQRLYEKEEDVMISLLPANKIITNLELVSGIALHSPKLFEQLLKLIPTLQSNEYVPVFQSILSDALPFNCLDVYVNHCIPVFIVITNGVLSPLFNTLMNRLSRLHSILSSKKISELTEGVLSQLKEHSRLLLILPSLLQFYQPENLIVYLNEVQEVDKDTIAIYSLLISKLTNIIPHVLEQNKEYFNGYKTIQELDSHESNKQATPIFIEELCRMNNKAIECLKEMIVFDSINKKNELHWKEELFNLVYERFIESHQVTTVEESHIMILLFSLLPTEKLLTYESTVLKIFNIICVPTSHLNEIDSVVVLLFNILPTVSQYPMSLIESELDSIITKLFNVLYINGTTIKYRCDIIDLLTRIRVVYGIDAIRPYQKNVIKKLLVPLDDNKRLVRRSAAICRNIWETTA
The following text describes a protein:
Function:
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular Localization:
Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
Sequence:
MEDKYILLSAVETFKSRLEELLMQSAKVQKQTMLRKELASSMNDMASTVQEALNKKKSS
The following text describes a protein:
Function:
Required for 60S pre-ribosomal subunits export to the cytoplasm.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVRRRTAAVLPNNLPHLQNLVKRDPKLYREEFLQQWNHYQTAREVFLVNPGEDDDEFANLIGFLAQTCNHYHDVTKNFPAELAQLLQENHEQLHPDVAEKIVQSLVLLKNKTVISSFTLLKWFFSLLNSNVNTSKALRKNLYEQISTTIRNENKKSRNEKLNKVVQTALFTMVENAGTVTSKVADYTNKKKEYTVGEMMGVWAVRLVQDLWRRKIWSGDARAVEIMKTAALSPNTKVMLAGIHFFLGVDSLDAEDDSDEDEGPDLKKLLHQSNINKKSKSREAQMQKARASLKRKERLKNAPPINVNFPALQLLHDPQGFADDLYERQLSGNKRKLPLEHKLVVLQLLSRLVGSHRLIVLGLYSYMMKYMTPHQRDVTQILACAAQASHEFVPPDTLEPLIRKIADEFVTSGVASEVVCAGINGIREICARAPFAMTPELLQDLTEYKSSKDKGVMMASRGLLSLYRDIAPEMLKRKDRGKLASMEFKERKPLRYGEDLHTVEGIQGLDLLEKYKAENGEEENEDDWKAWEAIDDSSSDSDSEGWININSDDEISISDSGDDDGEEGNSKKLQTEKPEVGSQEPVDLANSIAVRTILTPADLKKLEELREKEGVERLVNGPKRLPKTNDVIDAIDIEGPRKKQKADREARLASVMEGREGREKYASKRSGFMPTSLSNKRKQRNKNFMMMKHKAKNKKSRSLHEKQRILRAHVERERKQI
The following text describes a protein:
Function:
An essential component of the GATOR subcomplex GATOR2 which functions as an activator of the amino acid-sensing branch of the mTORC1 signaling pathway. The two GATOR subcomplexes, GATOR1 and GATOR2, regulate the mTORC1 pathway in order to mediate metabolic homeostasis, female gametogenesis and the response to amino acid limitation and complete starvation. GATOR2 activates the mTORC1 signaling pathway through the inhibition of the GATOR1 subcomplex, controlling the switch to cell proliferation and growth under nutrient replete conditions and during female oocyte development. GATOR2 probably acts as an E3 ubiquitin-protein ligase toward GATOR1 (By similarity). In the presence of abundant amino acids, the GATOR2 complex mediates ubiquitination of components of the GATOR1 complex, leading to GATOR1 inactivation (By similarity). This GATOR2 component is required for activating mTORC1 and promoting cell growth in both germline and somatic cells. In addition to its role in regulation of the mTORC1 complex, functions independently of mTORC1 to promote the acidification of lysosomes and facilitates autophagic flux.
Subcellular Localization:
Lysosome. Cytoplasmic vesicle, autophagosome. Note=Localizes to lysosomes and autolysosomes under fed and starved conditions. In female egg chambers, localizes primarily to autophagosomes and autolysosomes during amino-acid starvation.
Sequence:
MPDSVEDTSTISLRICLEGHANALALNKDNNQIALAGRSLLKVYSINSNGFTESCNMRGKNQNLSYSANDVAWSTLDSNLLATAATNGVVSVWDLSKFGRQKQLLVYNEHERTAHTVTFHSSEPNILISGSQDGTIKCFDIRSDKSINTYFCNSESVRDVKFSPHTQNIFSAVSENGTVQLWDMRKWDKCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWNMDGRPGLEHTIHTIAVVGRVKWRPERTYHIASCALVVDYSVHVWDIRRPYIPFASFNEHTNVTTGIAWQGSDSHCLLSISKDSTIYKHAFKDATRPALKANAQGASLGRFGDISFANKIKEYEPKTSGASNTKSSSFIRRKTNVAGSIQFHLDHSKMYKFMVNDTFSGYPLSESVSRPTQEHESFIGCARELVISGKKLSELCEHNAEVSKKYGKHNATTLWNFIKLFYGSNHFEPPFEHRSSFSNQKNPMNSRRATQVASDWPQQRTELGQDLNGNTPETAHEIDVANVDDDTLGSSGVEHPPTSSVILSETQIISEITFDNFELLRNGFIYVGPTECPKALAFPALHHDVQAARPQLDLKASDHEKSPPPHVPTVLKVSHVPPIPMWEPHKFVSDALMLMNDVGDVQTALTVLIALGEARKLLPIDDALVEHWFYTYVDQLHRYELWNEACEVINRSWLRSVQQLNQHSTAMHTNCGECGRPMGGKVGWYCDKCKSMQSAKCCVCGLIVRGVYAWCQGCSHGGHIEHLQKYFAKHSKCPKCGHLCAYS
The following text describes a protein:
Function:
Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein. Melanosome.
Sequence:
MYFSVTSLQESEAYEDAFHPFGGEPLSYTRFSLARQVDGDNSHVEMKLAADEEENVDSNMRGNQTSIAKPKRLNGYVCYGIIAVIVFFLIGFMIGYLGYCRRVESQDCGKEAGTQPSCPEETETFESEEQLPGVPRIFWADLKSTLSGKLDAVDFARAIKMLNENSYVPREAGSEKDTSLAFFIENQLQDCKLGKVWHDEHFIKIQVKGSSQNSVSIVSTSGNGSQAYPVESPEGYVAYSKAATVTGKLVHANFGTKQDFEDLNMPVNGSLVIVRAGKISFAEKVANAESLNAIGVLIYMDYSKYPIVNANLPVFGHAHLGTGDPYTPGFPSFNHTQFPPSQSSGLPNIPVQTITRAGAEKLFQNMEGDCPRIWGTDSSCKLVSSQDKNVKLSVNNVLKEIRILNVFGVIKGFEEPDRYVIVGAQRDAWGPGAAKSSVGTSLLLTLARILSDMVLKGQFKPSRSIVFASWSGGDFGAVGATEWLEGYLSSLHLKAFTYINLDKAVVGTTNFKVSASPLLYSLIEKIMKDVKHPLNGLSLYRDSNWISKVQKLSLDNAAFPFLAYSGIPAVSFCFCEDTDYPYLGTPMDTYETLNREVPQLNRVARAAAEVAGQLVIKLTHGVELNLNYEMYNDEILRFVKEMNLFRADIRDMGLNMQWLYSARGDFFRATSRLTTDYKNAEKTDRSVMREINDRIMKVEYHLLSPYVSPREFPFRHIFWGSGSHTLSALLEHLKLRKKNNGAFNQTLLENQLALATWTIQGAANALSGDIWDIDNEF
The following text describes a protein:
Function:
Plays a role in determining ER morphology.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation.
Sequence:
MSSFLGLFKRSDPSANYEKELQVLQTKLAETEKRLLSRRLRLRRTKGLFTLYSLVVYIVYVGIVVAKNQLSRDQLLSGNRLTLGVLLGPPAIYIVRYVIQAVLGRFVSFDEDRIKYLRQQQEGKLEELKQKTGFYSTKAIVDRYEPKKKEVKKPAQQQANKQNAPTNRRQGVPPPTANVPRNLPPTANVPAVPVVPAPGPGPNVPAAVPAIPKPVPVSEKEVLAAKQSLDNAGVSVAPVSTGPYQRQWFDRVLDLLVGEDESAAQNRQALICSKCHNHNGLAPFGKTAAEIRYKCPNCGEWNGNLVPTEAVELVEEVKEENENEKEEAEEEEGDAVVPSEVKELVSEMVSEVPEVSMAN
The following text describes a protein:
Function:
GPI-anchored cell wall protein involved in stabilizing the cell wall. Not implicated in virulence, heme uptake and biofilm formation.
Subcellular Localization:
Secreted, cell wall. Cell membrane; Lipid-anchor, GPI-anchor. Note=Found anchored in the cell membrane as well as a covalently-linked GPI-modified cell wall protein (GPI-CWP).
Domain:
The CFEM domain is involved in heme-binding and contains 8 cysteines and is found in proteins from several pathogenic fungi, including both human and plant pathogens (By similarity). The CFEM domain adopts a novel helical-basket fold that consists of six alpha-helices, and is uniquely stabilized by four disulfide bonds formed by its 8 signature cysteines (By similarity).
Sequence:
MKASVSLLLLSAASMASAAMSVSQCAQMCLSNMKAKAGELGCSAGDDKCLCSQANYGYGIRDCTTEACPDDDAIAVLSSALSSCPSDSAAVTATGAGGSSSGSGSGSDSGSGSGSGSGSGSGSGSGSGSSSGSGSGSGSGSGSGSGSNSGSGSASSTATGTATGTATGTATGTATGTATGSENSTTGGAGAGAGAGASSTGTNASGTGATTSGANPSNTGATTTDTTLTTTTTSSENGSSTGNSSSETGAGSGSSTATGSGSGSGAGSASTTAPNSSSTGNVAPRGAVVGSGAVGALALAALIIL
The following text describes a protein:
Function:
Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, probably via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Note=Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus (By similarity).
Domain:
Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Motifs 1 and 2 are essential for the association with nuclear receptors, and constitute the RID domain (Receptor-interacting domain) (By similarity).
Sequence:
IIRRCIQRFFSLNDGQSWSQKRHYQEAYIHGHAETPVYRFSLADGTIVSAQTKSKLFRNPVTNDRHGFVSTHFLQREQNGCRPNPILQDKGIRPPAAGCGMSLSPSQSVQMLGSRTYGVADPSNTGQMAGARYGASSSVASLTPGQSLQSPSSYQSNSYGLNMSSPPHGSPGLGPNQQNIMISPRNRGSPKMASHQFSPAAGVHSPMGSSGNTGSHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNINQPSKASSQDSKSPLGLYCEQNPVESSVCPSNSRDPPVTKENKENSGEASETPRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDSNCKDSSISVTSPSGVSSSTSGAVSSTSNMHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSTASGGEGSVXQEQLSPXKKENNALLRYLLDRDDPSDVLAKELQPQADGGDSKLSQCSCXTNPSSGQEKDPKIKTEEVSGDLDNLDAILGDLTSSDFYNSPTNGSHPGAKQQMFAGPSSLGLRSPQPVQSVRPPYNRALSLDSPVSVGSVPPVKNVSAFPVLPKQPILAGNPRMMDSQENYGANMGGPNRNVPVNPTSSSGDWGLANSRASRMEPLASSPLGRAGGDYSAALPRPALGSSGPTLPLRSNRLPGARPTLMLQMRAGEVPMGMGVSPYSPAVPSNQPGSWPEGMLSMEQGPHGAQNRPLLRNSLDELLGPPSNPEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVSQGQALESKQDVFQGQEAAVMMDQKAALYGQTYPAQGPPLQGGFHLQGQSPSLNSMMSQISQQGSFPLQGLHPRASMVRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALEMKMESPTGAAVMRPMLQSQQAFFNAQMAAQQKRELMNHHLQQQRMAMMMSQPQPQAFSPPPNVTASPSMDGVLAGSAMPQAPPQQFPYATNYGMGQPPEPAFGRGSSPPSAMMSSRMGPSQNAMVQHPQTAPMYQSSEMKGWPSGNLARNGSFPQQQFAPQANPAAYNMVHMNSSGSHLGQMTMTPMPMSGMPMGPDQKYC
The following text describes a protein:
Function:
GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence.
Subcellular Localization:
Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor.
Sequence:
MHLFKRIALTLWLIISSTLAVVITEDRVDRGTISVNLGEVTVNSGASWSIINNAVTAFAGKINVQSGGGLYISSTSPLLALQVTLTSLLDSITNDGVISLDSRASLTASNYNLIGLSFTNNGEMYLAASGVLPSTMDLTAASWTNNGLIVAYQNQRSSGVLNLGTPLGAITNNGQICLYNQVYQQQTRIEGSGCITANKNSAIYISNAVLPVATTQNFYLQDSKSSMIVQAVSSTQTFNVYGFGNGNKIGITLPAVGIPPNPAYSYDVDTGILTVRAGLLSQKFNIGLGYYSLFFSVVTDNGAGLPSTILGSISYSGPVPSRNLPASCKIACKPVPTAPGTNPTEYTTTITTTNSAGNPLTETGVVDISTDSNGSWFTTTSIFPTTSQSSSSETVASSSQPDSSSTEPSAFPSSTGDSSAEPSITSDYSSSELSVVPSSASESASESSAEPSSASESASESGSESVASETSASESASEQSSTSESVSSEFASSDSSSEPSSASESSVESSSASEFVVPSSATETSVSESASESSAEPSSASESVASESAVSETSASESAAPSSASETSVSESAASSSASESFASESSVESSAVPSSASEFSTSESVASETPASETPASETPASESASEQSSTSESSAEISSASESSAEPSSAKSAISESASEFSAAPSSASQSSASQSSTNESSSQQSSAESSSTGTSSVSASAATSEYTATWTTTNSDGSVSTESGIISQSGSSFTTITTFVPDATSEYTTTWTTTNSDGSVSTESGIVSQSGSSFTTITTFAPDATSEYTTTWTTTNSDGSVSTESGVVSQSGTSLTTITTFAPDVTSEYTTTWTTTNSDGSVSTESGIVSQSGSSFTTITTFEPPVVCKRDDVNCGSSIGLSTPYYGNSSQPLSSTKMTDTSATQTVDSSLSSITDATTTQSVNSLETPVPTSGSGNGSNNGSDNGSNNGSNNGSNNGSGSGNGSNNGSNNGSGSGNGFNNGSDNGSNNGSGNASNNGSASGSGSDNGSDNGSDNGSDNGSNNGSNTDNGSNSGSDSGNGIDNGSGNGSSDGSDNGTTNGSGSGGESNNGSGNGSDNGSSPDNGSNNGSNNGSNNGSGDGIGTGSNSDTDNGSGNGSNNGSGSVNGSANGSGNGSNNGSNSGSNSDNGSNNSSGNGSSSDLGSVSGTGNGSNEGSSNESGANNGSNNGAGALPAATLSVVPSPSADSGSTSSASAMVIPNTNGSGKLLNGKVLTLSVLSSMVVVFL
The following text describes a protein:
Function:
Mitochondrial methyltransferase which suppresses respiratory defects caused by OXA1 mutations when overexpressed.
Miscellaneous:
MISCELLANEOUS: Present with 504 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MIVFRRFPTCLLHHIRQPASRSLLLESQRRSLSFTSYKYNSSHIDDDKSKKKLKNVFQMNSNRVIRKQKTKEELAKERFEEQLRSPNRFVRWGAIARSEKFSKGMTKYMIGAYVIFLIYGLFFTKKLFAKDKELERLLKKQEEGNANEYEALRIKELKGKLRRRDELKLEEYKKMQEEGIENFDDIRVQNFDQNKLNEQILPARDTTNFYQEKANEYDKAINMEERVIFLGKRRKWLMKHCQGDVLEVSCGTGRNIKYLDMSRINSITFLDSSENMMEITHKKFREKFPKYKKVAFVVGKAENLVDLAEKGKPSLENEKENQVKYDTIVEAFGLCSHEDPVKALNNFGKLLKPDGRIILLEHGRGQYDFINKILDNRAERRLNTWGCRWNLDLGEVLDDSDLELVEEKRTHLGTTWCIVAKRKGDVKKKDELGFVEKYLQSSIRKRMESFEKKDDMASKKELEPVPPVSKS
The following text describes a protein:
Function:
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Sequence:
MTGPRVRTVTAAALRAQPLPAPGGDKEQRGRVLIVGGSARVPGAVMLAGEAALRAGAGKLQLATAASVAPGMALAMPEALVLGLGENGQGEIVRGHRALDAAMSACDAAVIGPGMASTNTTAALVKRAIDQAVCTLVLDAGALSPRLRAPLGRPFVLTPHAGEMAALAGDDKAAVEAAPADYALAFAKKMRSVVIVKGADSFVAGPDGALWVHRGGVPGLGTSGSGDTLAGLIAGFAARGCDALTAALWGVFVHATAGKQLAKRIGTVGFLAREIPPEVPGILDRLPRG
The following text describes a protein:
Function:
May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MLWFAVHVLLWLELALCLLCCIPGARWRRAIRWFIDLPFVHVTTKGLPYLVVILMALLVQSIYIQVNARQHGEEARVMAGQSTTITLYEANMYRAQRNTYMAAIALLGMLMLREIIQCVTPPRPHPPTHIHFWAQLKSKVLTCMSVPLLHRTASFVRRCVEYEDEIARLKSEMEWSDGAVQDEKHFSEARKQAAAEKLHSAKEDIKASAKHAAREVKQAVDQLQSDKKQD