lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components. Required for recruitment of telomeres to PML nuclear bodies. SUMO protein-ligase activity is required for the prevention of DNA damage-induced apoptosis by facilitating DNA repair. Required for sister chromatid cohesion during prometaphase and mitotic progression (By similarity).
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MSGRSAPVVSFSSVDNSLSSLKNCQGYLHTGMDITVSVALDLLETGCESTEVDAMESVMLEYSAMERDLKQYIHAVEETVQKLRREQMEQVPDLQSLVQEKYATIQKKNDDEDLKKNDRFVQFKDQLREMRKQMGEKEEGDAAFENVDEDIAVLPSQQNLTCPITQMEMTNPVKNKVCGHTYEKEAIERMIQDRHQKKKRVKCPKVGCVHSDMQISDLVPDTALKRTIDILNKQKGRH
The following text describes a protein:
Function:
Involved in the uptake of ammonia (Probable). Implicated in aging.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MNTLQNLTLKMDRQPTIRMKPDKQLDCSLSQDDGVWMMASSFIIFTMTAGFGLLESGRVSSKDEVNCMVKNVFDVIFGGLAYWMFGYGLTFGDSKHQLGRYVGFGDFFFDPERVSDDDSTDEKGISYSLFIFQMSFATTTSTIVSAGMSERIHLKSHCFISFFITLVHSVAGHWVWDQEGVFRMMGVVDSAGCSAVHLVGGVSGLVATLYLKPRRNRFAKNGIRTVSDPTKAILGFLMIWWGWLAFNTSSNYAVTHGQWTEGMRSAVGTILASAGGGVVTVIITRLSTKKIQMDMLIDGMLASLVASTGGCLYFTPWQATLVGAIGSSLALAAYPVTEWLKIDDPVGVFPVHVVGSIWGMIAPAIFVYRRPMNFGPPECDFQTSDEINGLLYGGGFYLLFLQSFVILVIGTYSAICAFIILFLIHHSPVGLRVDKYTEELGADLIEHGLAGFNVMTYTIEKKLDTKTLSAVLMIIVRWRAKAKLGAQRRKKIHDSGSVAPQQAESVEMNVIHRRH
The following text describes a protein:
Function:
Catalyzes the hydrolytic deamination of cytosine to uracil or 5-methylcytosine to thymine. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSPVEGSPAKPEDYPHFMSVAHEQALKSLSEGGIPIGAALVHLPTSRIISRGHNNRVQLSSNVRHGEMDCLENLGRVPEGLLSECAMFTTLSPCIMCSATCILYKIRTVVLAENENFLGGEQLLRDNGANVINLDSEEIKNMMKNWINSPRGKVWNEDIGEVTGS
The following text describes a protein:
Function:
Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Essential for postembryonic development, especially during the formation of the shoot apical meristem (SAM).
Subcellular Localization:
Cytoplasm, P-body. Note=The localization to P-body is VCS-dependent.
Sequence:
MSGLHRSSSSSKNIGNCLPSKELLDDLCSRFVLNVPEEDQQSFERILFLVEYAYWYYEDNAVENDPKLKSLSLKEFTSLLFNSCDVLRPYVTHIDDIFKDFTSYKCRVPVTGAIILDETYERCLLVKGWKGSSWSFPRGKKSKDEEDHACAIREVLEETGFDVSKLLKREEYIEFVFRQQRVRLYIVAGVTEDTVFAPLTKKEISEITWHRLDHLQPASNEVITHGVSGLKLYMVAPFLSSLKSWILKHPSPVARRPNKPLKALCVWNARTSVGGNGTATVESQNRKSELRTTTMESNSRKPELKRTTMESHSTKPELRKGTMESHNTTATVESHNTKPVVDHSQDIKPGGSFINFKFNQSVILQALESGNSA
The following text describes a protein:
Function:
Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences; Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.
Sequence:
MHGRLKVKTTEEQQEAKRKEREKKLKLYTAGTQKVFEKRKKNEFDGEILEVCAQLLSANPDVYTLWNVRKETFQVLAETKTPDEMQELYDKELGFIENCLRVNPKSYGAWYHRCWVLDHTPKPDWKQELKLCTLYLEYDERNFHCWDYRRFVVAKSDVAPSDELEFTSNKISTNFSNYSSWHYRSKLLPVLHPDQEKKGRLKEDILIQGIVLVPRLVSACFKWLLKTMIDQIDACIVRKKDILIQGIVLVPRLVCACSKWLLKTMIDQIDTCIVRKKDILIQGIVLVPHLVSVCTKFCTPIASSLMAATFFICALPGEKPLGIQAVYANSALNQVMVIFSQSVNLLQQPAEVSISGSVMDGTWRNSRGSQYHSIMWIYTVSSDALRQEGERTLQVKLREDVCRSCHLDEGATECWSKDKQDASSLFTAELSDEKTEFLTTELESCQQLRELEPDNKWCLLTVILLMRALDPLKLEAEMLGCFTTILSQDTYRANYFKDLRSKFIMENAIMRYLQESSKVTESQVKQATFDASGKELTTLHHLHHLSSVHCMDLSNNDLLALNDVDLLFCVSDLKADSNKLQDISHLSGLPCLETLSLENNNISSLSQLEPLAACPNLRRLDLSGNSVCDLDLFGSKVRELLPQLTSLNKELL
The following text describes a protein:
Function:
Beta-1,3-xylosidase that hydrolyzes beta-1,3-xylooligosaccharides to D-xylose.
Sequence:
MTTTIQNPILKGFNPDPSIVRVGDDYYIATSTFEWFPGIQLHHSRDLINWRLVGHALTRTSQLNMMGMDNSEGVYAPALTYSDGTFWLCFSNVHSCRGGNWMATPSYVVTADSIEGPWSEPVPIGNYGFDPSLFHDDDGKKYMLNMIWGGRAKTNFFGGIIMQEFDADEGKLVGAPKTVFEGTELGCTEGPQLLKKDDYYYLITAEGGTERNHAVTVCRSKHIWGPYEVHPENPILTSRFQEHAELSRAGHGFLVETQTGEWYMSHLCGRRIPNPEGYQFMPKYDNGFSILGRESALQKAHWQDDWPYIATGKTPVVEVEAPNLPLHPWPESPARDEFIDPTLSLISTLREPVSEKWLSLSERPGFLRLKGRHYLYSRYEQSMVARRFQAHNATVETKLEFKPNTPYEMAGLCAYYARNGHYFLKMTANDLGERVLQVVGNINDVYGEYSNDVVIGDADTVYMRLELKTQWYQYSYSLDGVDWYEIGPALNSTPLSDEGGPDIFRFTGSFAALFVADITGQKRHADFDYFEYLEH
The following text describes a protein:
Function:
Catalyzes the covalent attachment of ubiquitin to other proteins.
Sequence:
MHGRAYLLLHRDFCDLKENNYKGITAKPVSEDMMEWEVEIEGLQNSVWQGLVFQLTIHFTSEYNYAPPVVKFITIPFHPNVDPHTGQPCIDFLDNPEKWNTNYTLSSILLALQVMLSNPVLENPVNLEAARILVKDESLYRTILRLFNRPLQMKDDSQELPKDPRKCIRPIKTTSFSDYYQTWSRIATSKATEYYRTPLLKVPNFIGQYYKWKKMDLQHQKEWNLKYSVIKCWLARKRMPHEVTHSMEEIKLCPTLIPTTDEIFLESPTAINSITDIYETEEEGWKSDTSLYENDTDEPREEEVEDLISWTNTLNTNTSED
The following text describes a protein:
Function:
Alkylsulfatase that cleaves the widely used detergent sodium dodecyl sulfate (SDS).
Miscellaneous:
MISCELLANEOUS: E.coli BL21 cells were shown to not grow on minimal medium agarose plates containing 0.1% SDS, indicating that the SDS was toxic to the bacteria cells. However, overexpression of YjcS in these cells rescued the cells.
Subcellular Localization:
Periplasm.
Domain:
Contains three distinct domains: an N-terminal catalytic domain that contains a binuclear Zn(2+) cluster, a central dimerization domain and a C-terminal sterol carrier protein type 2 (SCP-2)-like fold domain. Although separated by the dimerization domain in terms of sequence, the N-terminal and C-terminal domains are spatially directly adjacent.
Sequence:
MNNSRLFRLSRIVIALTAASGMMVNTANAKEEAKAATQYTQQVNQNYAKSLPFSDRQDFDDAQRGFIAPLLDEGILRDANGKVYYRADDYKFDINAAAPETVNPSLWRQSQINGISGLFKVTDKMYQVRGQDISNITFVEGEKGIIVIDPLVTPPAAKAALDLYFQHRPQKPIVAVIYTHSHTDHYGGVKGIISEADVKSGKVQVIAPAGFMDEAISENVLAGNIMSRRALYSYGLLLPHNAQGNVGNGLGVTLATGDPSIIAPTKTIVRTGEKMIIDGLEFDFLMTPGSEAPAEMHFYIPALKALCTAENATHTLHNFYTLRGAKTRDTSKWTEYLNETLDMWGNDAEVLFMPHTWPVWGNKHINDYIGKYRDTIKYIHDQTLHLANQGYTMNEIGDMIKLPPALANNWASRGYYGSVSHNARAVYNFYLGYYDGNPANLHPYGQVEMGKRYVQALGGSARVINLAQEANKQGDYRWSAELLKQVIAANPGDQVAKNLQANNFEQLGYQAESATWRGFYLTGAKELREGVHKFSHGTTGSPDTIRGMSVEMLFDFMAVRLDSAKAAGKNISLNFNMSNGDNLNLTLNDSVLNYRKTLQPQADASFYISREDLHAVLTGQAKMADLVKAKKAKIIGNGAKLEEIIACLDNFDLWVNIVTPN
The following text describes a protein:
Function:
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Sequence:
MGKLDKKQLIESLKEMTIVEIDEIIKAVEEAFGVTATPIVAAGAAGATQEAASEVSVKVTGYADNAKLAVLKLYREITGVGLMEAKTAVEKLPCVVKQDIKPEEAEELKKRFVEVGATVEVK
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MVWSPKDVYDLTLPILPAWKYFGLPAYKIIKTPNFKSLTHNNSKLNYIMVIISTTAYLYYFKVGDKNTNSFEKHMTMYRLVASFVNYMGAVIFCHKHKNKFLSNIEKCALLQQRLNKLGKKEHSFNKMAKILLTIYTTKLSSMIVVTVNDIVKISTSESHSTVKLGWYCNFITEMFLFYFLIVLRSLYSQLLNCTKFKESAQQVKELGKIHKDLNKLAMEVNETFGELMLLRFSGDFIYLIVGLSSNAVLNAEYETVLDFVWTFTVYVLWIPMALGFIALTVWYFEDILHHDARINENLTNLIEATKQVHLFIFDNQINRLKFTMCGFVDISLNSFHLMISAIVTYVVYLIQFKSMSK
The following text describes a protein:
Function:
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II.
Subcellular Localization:
Nucleus. Chromosome.
Sequence:
MKELFQKRLSAFYNNWIFNKKDLWGNSDVVVIHTQQQEKDYLWGYSVSSQFYLWLIGEQLDDTTTIFTSSAIYFLCSRKNYSKIRSLCCSATVVNKIPVSVQLKANNDDGLVLIDATIRNERAIRNKKLFAHRFDDDGSCPFVLGYVLGEFPRSKLFWNCFNELETGRFKAIDVRCGVSKIMCTVDKPVFGVDKAISVADMPVFGVGVSGKEVAPKHVYRPPVNASKEKGVLKGKGEGSLWGGHVDQLFMEAMENRSVLLEKEESIPELTFEPMELRKKGSDLGSQYELKRFLWGDKGKGGLSRVNENPVSTTKMTENVSALMGDLNLSCSPSSGKQDKLRLANIGGGQQFKFGGNRLDVGKEENSKAGNRNVDQVFKSGASTLDAKEGKLEEIKENDDAVFKFGSSKLDGKDSRSKEVNRDGDQLVKLGEGKKDGDQLFKMGEVKKDGDQQFKIGGKRGRSLQPQMMEEKKGAKDLKLLAERLTAFYSSWRTYKEEQWGKADVLVITTQSKGPLESLSHPVSSSFLVWLLGDEFPETTAVFTDTGIEFLCTKDSFFRLRAIGIRMTMVAKVTVSVQLKKRGELCSDWLRKTLCQVNAAPRSGVNCPLVVGCISWESTEIGVLSHSKMFEVAYVDQSLINLFEQGSFEFAAQHSTLPKQFQMLSLETSTGAKTASALSLSEVAKMKSMDDNSYVSHTPEEEKLLEKKGDTSSSLPTDATVDNAGQVERSKLADKMLLLDIKEEGDMDTSITEDGAEEKLQVKECGEQSTPTTEGGMDHSIQPTDVTDAASENSLPDDKNGRPGKKSAGSDHEDDDWTLIEMECEGQEAEVAERVSWKRWFMDKTVKSFGLKDEVSDEAPSKRTKA
The following text describes a protein:
Function:
Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN).
Sequence:
MDSVEKGAATSVSNPRGRPSRGRPPKLQRNSRGGQGRGVEKPPHLAALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSSTSLDAIIEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGVREVTEPLNLNPAKRPRRQDWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQRVLRYGYFGKEKLKEIKPLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERACSKQTLSSLKLDCKMEVSVSDKLAVVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEHIFLLMEKVNNSCQK
The following text describes a protein:
Function:
Serine protease inhibitor that functions in the melanization-mediated immune response. By preventing the activation of phenoloxidases through the inhibiting of serine proteases CLIPB9, CLIPB10 and CLIPB4, negatively regulates melanization in the hemolymph. By preventing melanization, has a detrimental role during P.berghei parasite mediated-infection and invasion of the mosquito midgut.
Subcellular Localization:
Secreted. Note=Secreted into the hemolymph.
Sequence:
MNKLNFVILCLAALLVFDATAQQDVHGPFQGQRQNEFDLMFVKEIFKNHNSNVVLSPFSVKILLTLIYEASDTSFGNAVSNTKRELSSVIQNDNIDHTRSYYKQLLESAQQDNKDYDLNIATNFFVDDFIEVINKYQQIANTHYHAMLEKVSYSNPTQTAATINNWVSEHTNGRLREIVTPDSLEGAVITLVNVIYFKGLWTYPFPEVANNVKPFYGTRGKPTNAQYMEQNGQFYYDNSADLGAQILRLPYRGNKLAMYFILPNPDNTVNQVLDRINSASLHQALWYMEENEVNVTLPKFKFDFSEQLNEPLQQVGIREIFSQNASLPLLARGRGARDEVRVSRIFQKAGITINELGSEAYAATEIQLVNKFGGDGVQIFNANRPFIFFIEDETLGTMLFAGKIENPVF
The following text describes a protein:
Function:
Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin- and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter (By similarity).
Subcellular Localization:
Nucleus. Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane. Cell projection, lamellipodium. Cell projection, ruffle. Note=Nucleocytoplasmic shuttling protein; shuttles between nucleus and cytoplasm in an integrin-dependent manner; probably sequestered in the cytosol by ITGB1. Its localization is dependent on the stage of cell spreading on fibronectin; cytoplasmic in case of round cells, corresponding to the initial step of cell spreading, or nuclear in case of well spread cells. Colocalizes with ROCK1 and NME2 at beta-1 integrin engagement sites. Together with ITGB1 and NME2 is recruited to beta-1 integrin-rich peripheral ruffles and lamellipodia during initial cell spreading on fibronectin and/or collagen (By similarity).
Sequence:
MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGKSLEGPLDLINYIDVAQQDGKLPFVPLEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGSGKSLLALKTTDANNQEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP
The following text describes a protein:
Function:
Involved in the regulation of gamete interactions during the double fertilization and to prevent multiple-pollen tube attraction; mediates the redistribution of the gamete fusogen HAP2/GCS1 to the cell surface after secretion upon sperm arrival.
Subcellular Localization:
Cytoplasmic vesicle. Secreted.
Sequence:
MASAANGVVFFLTLTSLILSSYSAGRETPIQPPTNSDEPGWGPLGINGSGPLDCLTALYKIKSCTKEILEYFATGAIDISPPCCEAISVITHKCWPSFLGTLGFSQDQTYILRGYCDAVAAAAYTTTRSGSVPIPVVGPSNGPVSSPNGPIQSPLGQPASSPAN
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the tom40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of tom40 with the receptor tom22 and small TOM proteins. Can associate with the SAM(core) complex as well as the mdm12-mmm1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the tom40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Sequence:
MMSFNDYIFYEYLKKTNWNIHNLYCNLTQTADNILNFEIPSGVSCQLSSLTSSNFASGCKISAMPILNGSMSYVYTNVNLENLNRNITYNLQHFYEGYKHVDVPFVHYVNEFQDKKLPLRPTLLYGRMHLPSQHLDAIFATRLSPWLLFFIQGVNEIEDGVGDNLCFNWQYDTGKRCLEFVYESSGAMLGVRGLWNLNYRELNTKINMENKAPSNMRWSLGFETYYGVLTKCAGASLGMRLHSGPSHPYAPFILTCTLNPIVGHITSTFSTAEPRTKAFSAQYDFNIYSYESQLKLGIELWRSKQEMSQSTNDPTANSMSSLLKGTCSTSGDVSISWQARIRNFLLTIGTEAQLTKIDPLFFGVHFEYSK
The following text describes a protein:
Function:
Plays a role in antagonizing the chemotaxis of multiple leukocyte subsets induced by CC and CXC chemokines. Displaces the interaction between CXCL12 and CXCR4 and thereby inactivates the antiviral activity of host CXCL12.
Sequence:
MRGGDVFASVVLMLLLALPRPGVSLARRKCCLNPTNRPIPNPLLQDLSRVDYQAIGHDCGREAFRVTLQDGRQGCVSVGNKSLLDWLRGHKDLCPQIWSGCESL
The following text describes a protein:
Function:
Catalyzes the 2-beta-hydroxylation of gibberellins (GA) precursors, rendering them unable to be converted to active GAs. Hydroxylates the C20-GA GA12 and GA53, but is not active on C19-GAs, like GA1, GA4, GA9 and GA20.
Sequence:
MDPPFNEIYNNLLYNQITKKDNDVSEIPFSFSVTAVVEEVELPVIDVSRLIDGAEEEREKCKEAIARASREWGFFQVINHGISMDVLEKMRQEQIRVFREPFDKKSKSEKFSAGSYRWGTPSATSIRQLSWSEAFHVPMTDISDNKDFTTLSSTMEKFASESEALAYMLAEVLAEKSGQNSSFFKENCVRNTCYLRMNRYPPCPKPSEVYGLMPHTDSDFLTILYQDQVGGLQLIKDNRWIAVKPNPKALIINIGDLFQAWSNGMYKSVEHRVMTNPKVERFSTAYFMCPSYDAVIECSSDRPAYRNFSFREFRQQVQEDVKKFGFKVGLPRFLNHVY
The following text describes a protein:
Function:
Required for O(2)-independent ubiquinone (coenzyme Q) biosynthesis. Together with UbiU, is essential for the C6-hydroxylation reaction in the oxygen-independent ubiquinone biosynthesis pathway.
Sequence:
MKYSLGPVLWYWPKETLEEFYQQAATSSADVIYLGEAVCSKRRATKVGDWLEMAKSLAGSGKQIVLSTLALVQASSELGELKRYVENGEFLIEASDLGVVNMCAERKLPFVAGHALNCYNAVTLKILLKQGMMRWCMPVELSRDWLVNLLNQCDELGIRNQFEVEVLSYGHLPLAYSARCFTARSEDRPKDECETCCIKYPNGRNVLSQENQQVFVLNGIQTMSGYVYNLGNELASMQGLVDVVRLSPQGTDTFAMLDAFRANENGAAPLPLTANSDCNGYWRRLAGLELQA
The following text describes a protein:
Function:
Vesicle trafficking protein that functions in the secretory pathway.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MTVIDILTRVDAICQKYDKYDVDKLNGANVAGDDPFARLYASVDADINQCVDKAETAKQEKNRAAVVALNAEIRRTKAKLLEEDLPKLQRLAVKKVKGLTREEIATRSDLVAALPDRIQSIPDGSSTATKKNGSWGASGSRTGGAIKFDSTADGNFDDEYFKGTEESNQFRREYEMRRMKQDEGLDVIGEGLETLKNMASDMNEELDRQVPLMDEMDDKVDRANADLKNTNVRLKETVLQLRSSRNFCIDIILLCVILGIAAYLYNVLKK
The following text describes a protein:
Function:
Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. Controls phosphorylation and abundance of PDS1 to prevent anaphase entry. Also helps prevent mitotic exit.
Miscellaneous:
MISCELLANEOUS: Present with 2530 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSLSQVSPLPHIKDVVLGDTVGQGAFACVKNAHLQMDPSIILAVKFIHVPTCKKMGLSDKDITKEVVLQSKCSKHPNVLRLIDCNVSKEYMWIILEMADGGDLFDKIEPDVGVDSDVAQFYFQQLVSAINYLHVECGVAHRDIKPENILLDKNGNLKLADFGLASQFRRKDGTLRVSMDQRGSPPYMAPEVLYSEEGYYADRTDIWSIGILLFVLLTGQTPWELPSLENEDFVFFIENDGNLNWGPWSKIEFTHLNLLRKILQPDPNKRVTLKALKLHPWVLRRASFSGDDGLCNDPELLAKKLFSHLKVSLSNENYLKFTQDTNSNNRYISTQPIGNELAELEHDSMHFQTVSNTQRAFTSYDSNTNYNSGTGMTQEAKWTQFISYDIAALQFHSDENDCNELVKRHLQFNPNKLTKFYTLQPMDVLLPILEKALNLSQIRVKPDLFANFERLCELLGYDNVFPLIINIKTKSNGGYQLCGSISIIKIEEELKSVGFERKTGDPLEWRRLFKKISTICRDIILIPN
The following text describes a protein:
Function:
O-methyltransferase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893. MpaG methylates farnesyl-DHMP-3C (FDHMP-3C) to yield MFDHMP-3C. The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. MpaG and mpaB can also switch the order in which they act and, in this case, the conversion of FDHMP to MFDHMP-3C can take place via 5-O-methyl-FDHMP (MFDHMP). After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA. MpaH can also hydrolyze DMMPA-CoA to release demethylmycophenolic acid (DMMPA) that is further converted to MPA by mpaG (Probable).
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MSAASPASIIQELASAAKQYENNESGAREALIAQSRALIASLEVPSEFIQHTFWSQPALSAIVRLATDVNLFQYLKDAQEEGLSAEALASKTGMDVSLFARLARHLVAMNVITSRNGVFYGTALSNGLAAENYQQSIRFCHDVSRPSFGAFPSFFKGNGYKTPALGTTDGPFQSAHKVDISFPQWLVGNPPYLQYFNSYMSAYRAGKPNWCDNGFYPVADRLLNGFDASVSDVLLVDVGGGRGHDIATFGSQFSPLPGRLVLQDREQVINSIPADESRQFEATTHDIFTTQPVKNARAYYMHSVPHGFGDEDAVKIMANLVPALAKGYSRVLLNEIVVDEESPVMSATNMDLIMLAHMGAKERTEADWRSILTRAGLKVVNIYSYPGVAESLIEAELA
The following text describes a protein:
Function:
Involved in a F420-dependent anti-oxidant mechanism that protects M.tuberculosis against oxidative stress and bactericidal agents. Catalyzes the F420H(2)-dependent two-electron reduction of quinones to dihydroquinones, thereby preventing the formation of cytotoxic semiquinones obtained by the one-electron reduction pathway. In vitro, catalyzes the reduction of menadione to menadiol; since menaquinone is the sole quinone electron carrier in the respiratory chain in M.tuberculosis, the physiological electron acceptor for Fqr-mediated F420H(2) oxidation is therefore likely to be the endogenous menaquinone found in the membrane fraction of M.tuberculosis.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Sequence:
MPLSGEYAPSPLDWSREQADTYMKSGGTEGTQLQGKPVILLTTVGAKTGKLRKTPLMRVEHDGQYAIVASLGGAPKNPVWYHNVVKNPRVELQDGTVTGDYDAREVFGDEKAIWWQRAVAVWPDYASYQTKTDRQIPVFVLTPVRAGG
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MKYINQFMKISKGFLVPSSTIGLNSKTYHYKFPLLSFVREFSNGSYLRESAQNPANLGSQKGSDIFSMLANQKDDSNRQQKEERVKERPRSRISFKKQETMDPSYTLQSMVLRSSLKKVGALCRQIAHKPFYHALLQMKMSDKKISKYIATALVSARENAVREAGLDESTLYVDQIWVGKAKYLKKLITMGRGGRAIERSPRVRVTVVLRDERALLRDLQRRQQRLERKKVWTPLPNRPIYLKSNFFTC