lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Type I acyl-CoA thioesterase; 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. MpaH' acts as a peroxisomal acyl-CoA hydrolase that converts MPA-CoA into the final product MPA. 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. 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 (Probable).
Subcellular Localization:
Peroxisome matrix. Note=The mpaH' location in peroxisomes is required for the unique cooperation between biosynthetic and beta-oxidation catabolism machineries to produce final MPA.
Sequence:
MSTEKFTITEHLVPGSHIREYPGSTVNQEDVLKIHVKQYTPKREGPVPDDAITFIATHGVGLPKELYEPLWDELLDQASGFHIRAIWMADVASMNQSGIHNEDKLSMDCSWMDHARDLLLMINHFRDQMPRPLVGIGHSFGGNIITNLAYLHPRLFTTLLLLDPLIQLSPPSLGFGTDAPSAINYTLWRDDVWPSREVAIRANRAIMQGMDPRCLDRMTKHFFRDLPTPLYPDVEAIKALFGTTADSTTTPVTLTTPKYHELVAQIRQNFNARDPKTGRIEVPRDTHADMDPLVAYIPLYRPEPRSTFRRLETLRPSCLWVIAGATFLNIDEIREGVKICGSGIGGSGGVPDGRVREVVLPGFGHLMPFQEVKTVAETCIVWLQQEMDRFRQTERQWKEDRDGKSHLAVEENWYKVLKPIPSGRKKRNDKGKL
The following text describes a protein:
Function:
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC8 binds to ARE-containing RNAs (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus. Nucleus.
Sequence:
MAAGFKTVEPLEYYRRFLKENCRPDGRELGEFRTTTVNVGSIGTADGSALVKLGNTTVICGIKAEFGAPPTDAPDKGYVVPNVDLSPLCSSRFRSGPPGEEAQVASQFIADVIENSQIIQKEDLCISSGKLAWVLYCDLICLNHDGNILDACTFALLAALKNVQLPEVTINEETALAEVNLKKKSCLNIRTHPVATSFAVFDDTLLIVDPTEEEEHLATGTLTVVMDEEGRLCCLHKPGGSGLTGAKLQDCMSRAVTRHKEVKKLMDEVFKSMKPK
The following text describes a protein:
Function:
Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39'. May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MDSPNRDYQAQALGDYLETTPDSIFRINAEDLTRSPVGRFIRRGIQHFFKLTIHLYFTSAPATQPAINPHTDNYHILILQLQGEKHWLVCQVDNAESCEEFTLYPGDVLFLPRRAGHVAWTTNVTSVHATIGFQGVDCGDLVEAAGFTEQDVGLDSTSPCMLLTMDQAKVLHHVVDTTADADLGGPAAIAQLFVEHQSTLRVRRAISKNGCSGLCTCEGPSWAYFGSYGPDCGSDCDGWWGGSCDVDGCHGPDT
The following text describes a protein:
Function:
May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. Required for ciliogenesis (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton. Cell projection, cilium membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite.
Sequence:
MAEEQQEVVPQESGLRKSRVQKVPELPILERRNWLIHLHYVRKDYESCKAVIKEQLQATQGVCEYAVYVQALILRLEGKIQESLELFQTCAVLNPTSSDNLKQVARSLFLLGKHKAAVEVYNEAARLNQKDWEICHNLGVCYLFLKDLSKSKEQLTLALQLHRQDLSAITLGKIQLQEGDIDGAIQTFTQALQLSPENTELLTTLGLLYLQNGLFQKAFEYLGNALTYDPSNYKGILAAGCMMQSHGDYDVALSKYRVAASSVPESSPLWNNIGMCFYGKKKYVAAISCLKRALYLSPFDWRVLYNLGLVHLSMQQYASAFHFLSAAISLHHGNAGLYMLLAVALTYLDDIENAKSSYQQAASLDQTDPLVNLNFAVLLYNQGDKKGALGQYQELERKVSALRETSTEFDPEMVDMAQKLGAALQVGESLVWTRQTKDPKGKQRGAGKGPGAEQAPLGSNQALGRAMSSAAGYSKASGLSSGITISTVSKHPSLPLEPEDPSLTSSTAPDYRRGHS
The following text describes a protein:
Function:
Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Sequence:
MIKLVFRYSPTKTVDGFNELAFGLGDGLPWGRVKKDLQNFKARTEGTIMIMGAKTFQSLPTLLPGRSHIVVCDLARDYPVTKDGDLAHFYITWEQYITYISGGEIQVSSPNAPFETMLDQNSKVSVIGGPALLYAALPYADEVVVSRIVKRHRVNSTVQLDASFLDDISKREMVETHWYKIDEVTTLTESVYK
The following text describes a protein:
Function:
Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. 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.
Subcellular Localization:
Chromosome. Nucleus.
Sequence:
MGKRKEGSPIAPSSQRKKQRQEVDDTYDEEDYVQAGPSASNDYGHNKKQRKEANNSLDTLDYDNSMSLASSQRGSASQSGTGDVGIIESISLRNFMCHSMLGPFRFGPNVNFVIGNNGSGKSAVLTALIVGLGGKAAVTNRGSSIKGFVKEGQTFAEIFITLRNRGQDAYKPDVFGNSITVQQRLTTDGSRTYKLKSATGAVVSNKKEELTAILDHFNIQVDNPVSVLTQEMSKHFLQSKNESDKYKFFMKATQLEQMKEDYSYIMETKSRTHDQVENGSERLRDLRLECIQKEERFKSIASLGEMKEKLEDLKNKMAWALVIEAEKQIKPFIEQIAAEEGRTVKYKQKIDECQGKVNIAEEKFRAKQEELDNITQEAVALKPQGIALKEDAQKKRKSYNESEVLYNRHRMELKRLERDADQLHKRIEELKKSADNASESEKMARQKEIAQIRDRMKALHDKEITTNQQIHQFQQAIEKYKEERIRIGNEERNVKQRLEQHKRQLRELHESKTDRLRRFGQNMPALLAAIDEAYKLGRFRKKPVGPLGACIHLKDQELALAVECCLKGLLFAFCCDNHQDERMLQNIMSREYPRGRRPQIIVNEFRDQVYDVSRRATFHPNHPTVLTALEIDHPVVANCLIDMRGVETILIIKGTDEAREIMQKRAPPRNCREAFTGEGDQVYTNRYYSSDTRRAAILSRDVEAEISHLEKELRNFGGQMAKFQQRLHSVDKDVKENEDILRQYHNSKKQIQIDLRAFSERIAELENVEEQPSIDIATLEGEAEENLNKIELVKQEMELTKENMGNLKLLLTMAESNYEEIKRKISSVSEVAEPVKEDLHRIDQEVENCKRHKKHYVDKLKEHLDRIQKRKEEVAGKEQELEVKISQAKCVCPERIEVSRTARSLDTEITRLREKINSEEVLHGNREEIIKQYHEAKERYQDVEGKVKHLKRFIKLLDDIMAQRYKSYQQFRRCLTFRCKIYFDSLLSQRAYSGKINFDHKNETLSITVQPGEGNKAALSDMRSLSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRISMDMMLSMADSQRFRQFILLTPQNMSSLPSTSLIRILRMKDPERGQTTLPFRPVDQQEEDED
The following text describes a protein:
Function:
Required for the polymorphic O-glycosylation of serine-rich repeat protein PsrP. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in PsrP. Part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins encoded upstream in the same operon (Probable). The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to PsrP (experimentally characterized with truncated PsrP-SSR1 constructs); this subunit alone has weak N-acetylglucosaminyl transferase activity that is 10-fold stimulated by GtfB. The complex requires at least a 25 residue-long peptide for activity; the in vitro assay has only been seen to glycosylate Ser residues. The alpha linkage was shown in L.reuteri.
Miscellaneous:
MISCELLANEOUS: Encoded in RD10, a pathogenicity island with an atypical GC content that is associated with invasive pneumococcal disease. Pathogenicity islands account for greater than half the genomic diversity observed between isolates. The main function of this island seems to be correct synthesis and export of pneumococcal serine-rich repeat protein PsrP (Probable).
Subcellular Localization:
Cytoplasm. Cell membrane; Peripheral membrane protein. Note=Cell membrane association requires GtfB.
Domain:
Has 2 Rossmann-like domains, called R-fold-1 and R-fold-2. R-fold-1 is interrupted by an extended beta-sheet domain that loops out of the structure and is required for recognizing both PsrP substrate and coactivator GtfB. UDP and N-acetyl-D-glucosamine bind between the Rossmann-like folds.
Sequence:
MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKPFSLITASRLAKEKHIDWLVKAVIEAHKELPELTFDIYGSGGEDSLLREIIANHQAEDYIQLKGHAELSQIYSQYEVYLTASTSEGFGLTLMEAIGSGLPLIGFDVPYGNQTFIEDGQNGYLIPSSSDHVEDQIKQAYAAKICQLYQENRLEAMRAYSYQIAEGFLTKEILEKWKKTVEEVLHD
The following text describes a protein:
Function:
Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
Sequence:
MFTGIVETVGVVSAKDVMDTSETGGSGYSITVSDASVVLTDVHIGDSIAINGVCMTVTEFDSERTSFKVGVAPETLRKTNLGEFEVGHKVNLERSMSATTRYGGHVVQGHVDTTVTITRITPDPPNSITYRFHVPACTPSAGESSHLPSTDFLQYIVPKGYVCLDGTSLTVIDVDWSTREFSVMLIAHTLKSVVMPTKSIGDRVNIEVDQVGKYVENMVRGMLMSENNTVLAPMIERAVEKYLSKSHQ
The following text describes a protein:
Function:
Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MSIDWNWGIFLQEAPFGNTTYLGWLWSGFQVTVALSITAWIIAFLVGSIFGILRTVPNRFLSGLGTLYVELFRNVPLIVQFFTWYLVVPELLPEDLGMWFKAELDPNIQFFLSSMICLGLFTAARVCEQVRAAIQSLPRGQKNAALAMGLTLPQAYRYVLLPNAYRVIVPPMTSEMMNLVKNSAIASTIGLVDMAAQAGKLLDYSAHAWESFTAITLAYVLINAVIMLVMSLVERKVRLPGNVGSK
The following text describes a protein:
Function:
An NAD-dependent ADP-ribosyltransferase (ADPRT), it catalyzes the transfer of the ADP-ribosyl moiety of oxidized NAD onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis. It probably uses the eukaryotic prolow-density lipoprotein receptor-related protein 1 (LRP1) to enter mouse cells, although there seems to be at least one other receptor as well. Is active against mouse fibroblasts, Chinese hamster ovary eEF-2, brine shrimp (Artemia spp. nauplii) and upon expression in S.cerevisiae.
Miscellaneous:
MISCELLANEOUS: Exotoxins are often highly strain specific; not encoded in strain ATCC 39315 / El Tor Inabe N16961.
Sequence:
MYLTFYLEKVMKKMLLIAGATVISSMAHPTFAVEDELNIFDECRSPCSLTPEPGKPIQSKLSIPSDVVLDEGVLYYSMTINDEQNDIKDEDKGESIITIGEFATVRATRHYVNQDAPFGVIHLDITTENGTKTYSYNRKEGEFAINWLVPIGEDSPASIKISVDELDQQRNIIEVPKLYSIDLDNQTLEQWKTQGNVSFSVTRPEHNIAISWPSVSYKAAQKEGSRHKRWAHWHTGLALCWLVPMDAIYNYITQQNCTLGDNWFGGSYETVAGTPKVITVKQGIEQKPVEQRIHFSKGNAMSALAAHRVCGVPLETLARSRKPRDLTDDLSCAYQAQNIVSLFVATRILFSHLDSVFTLNLDEQEPEVAERLSDLRRINENNPGMVTQVLTVARQIYNDYVTHHPGLTPEQTSAGAQAADILSLFCPDADKSCVASNNDQANINIESRSGRSYLPENRAVITPQGVTNWTYQELEATHQALTREGYVFVGYHGTNHVAAQTIVNRIAPVPRGNNTENEEKWGGLYVATHAEVAHGYARIKEGTGEYGLPTRAERDARGVMLRVYIPRASLERFYRTNTPLENAEEHITQVIGHSLPLRNEAFTGPESAGGEDETVIGWDMAIHAVAIPSTIPGNAYEELAIDEEAVAKEQSISTKPPYKERKDELK
The following text describes a protein:
Function:
Interferes with host cell cytokinesis, centrosome positioning and Golgi distribution, and contributes to the morphology and stability of the pathogen-containing vacuole. May exert its effects by acting directly or indirectly on host microtubules.
Subcellular Localization:
Host vacuole, host pathogen-containing vacuole, host pathogen-containing vacuole membrane; Multi-pass membrane protein. Host vacuole, host pathogen-containing vacuole, host pathogen-containing vacuole lumen. Secreted. Note=At 12 hours post-infection (pi), detected at the vacuole membrane. At 24 hours pi, detected at the membrane and within the vacuole. At 40 hours pi, located predominantly within the vacuole with low levels in the membrane. Secreted, probably by a type III secretion system (Probable).
Sequence:
MVYFRAHQPRHTPKTFPLEVHHSFSDKHPQIAKAMRITGIALAALSLLAVVACVIAVSAGGAAIPLAVISGIAVMSGLLSAATIICSAKKALAQRKQKQLEESLPLDNATEHVSYLTSDTSYFNQWESLGALNKQLSQIDLTIQAPEKKLLKEVLGSRYDSINHSIEEISDRFTKMLSLLRLREHFYRGEERYAPYLSPPLLNKNRLLTQITSNMIRMLPKSGGVFSLKANTLSHASRTLYTVLKVALSLGVLAGVAALIIFLPPSLPFIAVIGVSSLALGMASFLMIRGIKYLLEHSPLNRKQLAKDIQKTIGPDVLASMVHYQHQLLSHLHETLLDEAITARWSEPFFIEHANLKAKIEDLTKQYDILNAAFNKSLQQDEALRSQLEKRAYLFPIPNNDENAKTKESQLLDSENDSNSEFQEIINKGLEAANKRRADAKSKFYTEDETSDKIFSIWKPTKNLALEDLWRVHEACNEEQQALLLEDYMSYKTSECQAALQKVSQELKAAQKSFAVLEKHALDRSYESSVATMDLARANQETHRLLNILSELQQLAQYLLDNH
The following text describes a protein:
Function:
Component of the ESCRT-I complex, a regulator of vesicular trafficking process.
Subcellular Localization:
Cytoplasm. Endosome. Late endosome membrane; Peripheral membrane protein.
Sequence:
MSKPDLNSLSIKMKQINLLKERFSHTIEVVKDSTFKIPFLNVHLLISLPVNFPNSPPAYFLEILQTHQPVSLPPNYQWTQISNLASVTVHIMEPFIKDSRILETLIEQVKRSQAMQQQQQQQQQQQRNQQAQQQYSPPPPYKDQPINKQPAQQQPQPVQQKPQQQQNGTNKIPMIPTEFPELKSKSVEELEELLKNEDSLNAFIYSYDEVSELSNRKSKLLSENERLTKITDPLPNDINDLSANLMTSKQKLEELKRKQEQLQQKKNSIADKYSQQNLLEILNDSISDLESESDNIVHSFLEGNLELKEFKKQFKEKRSSYHSKCANKDLFFK
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER).
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum.
Sequence:
MDLTTLIDKLNVSSAASAHDQAYSFACQAEKYDPKDLNIQRHKLVALIHLEKFDEAEQVLQDKGTTGLEFEAAYIYYRQGKHAELAKVLETAQKDTRLIHIAAQAAYKEEDFDRAYELTQELLGTGIDELDLLVNESAIVAQQALHRQGVFPLTMTSTAKSSHDFLFNRAIAELSEGRYDSALDLLSQAQVACSEADMPAEEIDTVKIQAAYIHQLKGDTAEAKRILDSVAESGSHLSGLTDLVAANNAVTLSPDITFNPNVALRKLQDHGLGLSSTAKGPTAPNGPAIQAQRKVFALNRLILEGSAGKDTSKLAKKLTRTYPGLVSAQVVAATNGNSDLEDLIETLRKRDPKCTNIGSVLAIAQAYVLTGRLQAAYDALTTYINSLPENLAPYPGLIAATSSIARLMGKKKLALKLIEKANTQWQKNSAPYSASLAYALSLLESNKPSNQKKAKNLLLKLVEKKPRDEIPRIALSGALGTQEVLTREIPDLISGVDVDNLEEVGVIIPQSKKRSAEVSTKTSKKRKTKIPANADPAVTPDPERWLAKRDRSTYKPKKVKGKKVQNTQGGAVDDSLELGSNTAEKTTVVKSKAKGKKKKGKK
The following text describes a protein:
Function:
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Subcellular Localization:
Cytoplasm.
Sequence:
MKFVDEAVIRVEAGDGGSGCVSFRREKYIPDGGPDGGDGGDGGSVYLEADENFNTLIEYRFERFHMAERGENGRGRDCTGHSGKDLILKVPVGTRAIDHDTEEVLGDLTTHGQKLLVAKGGFHGLGNTRFKSSTNRAPRQKTLGTPGEVRSLKLELLLLADVGLLGMPNAGKSTFIRAVSRATPKVADYPFTTLVPNLGVVNPRPGQSYVIADIPGLIEGAAEGAGLGIRFLKHLERCRILLHIIDIEPIDGTDPVDSARAIVGELEKYSPKLASKPRWLVFNKADLLLEDELKEKAERVVKELGWEGEVYTISAYGRDGTKELAAKLWDFIQSLPPEDKDANPEDEVEFKWDNYHQANIDAINEDYDDDFDDDFDDDDYDVEVIYQR
The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MQRQKPKGPGKPGSRFKPGSGTFKGAGGGRKSGDNSQKRPRQEINKSRLAATEAEIQDLKTKYAEIDATAIKKFAQFPLSKKTQKALAESKFVHPTQVQRDSIGPALQGKDVLGAAITGSGKTLAFLIPVLEHLFMNKWSRTDGVGAIIISPTRELAYQIFETLKKVGKHHDFSAGLIIGGKNLKFERTRMDQCNILICTPGRLLQHMDENPLFNTSTMEMLVLDEADRCLDMGFQKTLNSIIENFPPVRQTLLFSATQTNTVQDLARLNLKDPVYVGYGGATPREEPSASTKKTPNTAVLAVPELLQQSYVVLNLEDKITMLWSFIKNHLKQKIIVFVASCKQAKYLYEIFCKLRPGSPLLALYGTLHQDRRIAIYEDFLRKSHVVMFSTDVASRGLDFPAVNWVVQLDCPEDVSQYIHRAGRSARNKTRGECLLVLTPSEEEYMISALKEQLNIDIRCVQIDPKKLFSPRVKIEAFLAQFPELRATAQRAFLSYIKSVFLMRNKRLFNVFSLDLDAFAQSLGLAVTPRVPFLEKFLWRQKQLQQQKEQGDNAKSINPLLSKLTKQQSFGGGDEDEENSDDEDFIKVKRKDHDVEGEPVKLDEEDDTENEAEAPLVVPKREKLVTKASLAKKALKKNLQVNSKLKFDDEGETMADDRSQMKALSARQRTVNQDDDDGGINLVLSKALLTEEDQYDKQRFRELVKKRHKLQREKLRKKAEEAKGSDDEEEQQDDDNADDAGSESDHSVDLSWLPDPDKVYKNKPNASDRNESKSESSDASDDEKADDSDGDDDDVSDDEPAYKKSKLTNKMTLMDTEAIAASLLGS
The following text describes a protein:
Function:
Involved in meristem development. Acts as a negative regulator of the CUC-STM pathway in shoot apical meristem (SAM) neo-formation.
Sequence:
MEITVIASSSIDEGIGSWDLKTGTEQLQFKPCASPAHGLTAVGEKFLASSQLSARNTSGSIFYWSWTKPQAEVKSYPVEPIKALAANNEGTYLVGGGISGDIYLWEVATGKLLKKWHGHYRSVTCLVFSGDDSLLVSGSQDGSIRVWSLIRLFDDFQRQQGNTLYEHNFNEHTMSVTDIVIDYGGCNAVIISSSEDRTCKVWSLSRGKLLKNIIFPSVINALALDPGGCVFYAGARDSKIYIGAINATSEYGTQVLGSVSEKGKAITCLAYCADGNLLISGSEDGVVCVWDPKSLRHVRTLIHAKGSRKGPVNNIQIVRKTIVANSNKTQVSWKSRGALIPPPLEKYERPVEDTMDGIVTVDPPPFSDVPVYSSFLSADLIDEQVKELQQQGSAATEMEMERLKLEYKRSLQMNEQWQKNYENLLQVVMEEEQIGGTN
The following text describes a protein:
Function:
Plays a role in maintaining mitochondrial morphology. May act as a component of the MICOS complex, a large protein complex of the mitochondria (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Lipid-anchor; Intermembrane side.
Sequence:
MGASQSAEQEARPEVVRIDRNEIPEEYKTVGVSSDVVSRVNATRVAGNDGESDRLRQELAREREEKARLREDMAKLSQLQQRKTAGISAAPVSISGNDLEERKKIFDDTVERVQKQFFAYHRENVCQDNENEIVRCLQENPGRVLKCAPLTEAFEKCVGEFRQQVLKGN
The following text describes a protein:
Function:
Catalyzes the dephosphorylation of C5 and C6 carbon sugars in vitro. Catalyzes the dephosphorylation of 3'-AMP and phosphoserine in vitro.
Sequence:
MRIMASHDTPVSPAGILIDLDGTVFRGNELIEGAREAIKTLRRMGKKIVFLSNRGNISRAMCRKKLLGAGIETDVNDIVLSSSVTAAFLKKHYRFSKVWVLGEQGLVDELRLAGVQNASEPKEADWLVISLHETLTYDDLNQAFQAAAGGARIIATNKDRSFPNEDGNAIDVAGMIGAIETSAQAKTELVVGKPSWLMAEAACTAMGLSAHECMIIGDSIESDIAMGKLYGMKSALVLTGSAKQGEQRLYTPDYVLDSIKDVTKLAEEGILI
The following text describes a protein:
Function:
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Miscellaneous:
MISCELLANEOUS: The porphobilinogen subunits are added to the dipyrromethane group.
Sequence:
MKKNIIIGSRGSILALAQANLVKDRLQGNYPNLSFEIKEIVTSGDKDLKSNWENSDISLKSFFTKEIEQELLDGEIDIAVHSMKDMPAVSAKSLICGAIPDREDPRDVLVSKNGLLVTLPQGAKVGTSSLRRAMNLKTVRPDFEIKHLRGNIHTRLKKLETEDYDAIVLAAAGLKRTGLADKITEYLNGEVFPPAPAQGVLYIQCRENDEEIKEILKSIHNEAIAKIVEIEREFSKIFDGGCHTPMGCYSQVNGDKIKFTAVYLDEGKQIRAVVEDDLAKGKEIAYMAAEEIKNKIVK
The following text describes a protein:
Function:
Promotes cell proliferation, G1/S cell cycle progression and induces expression of the cell cycle regulator CCND1. Regulates proliferation induced by pro-inflammatory cytokine response via activation of NFKB1 and PI3K/AKT signaling pathways.
Subcellular Localization:
Cytoplasm. Note=Does not colocalize with TGM1.
Domain:
The EF-hand is necessary for the colony survival activity to protect cells from death induced by exposure to DCA.
Sequence:
MPQLLQNINGIIEAFRRYARTEGNCTALTRGELKRLLEQEFADVIVKPHDPATVDEVLRLLDEDHTGTVEFKEFLVLVFKVAQACFKTLSESAEGACGSQESGSLHSGASQELGEGQRSGTEVGRAGKGQHYEGSSHRQSQQGSRGQNRPGVQTQGQATGSAWVSSYDRQAESQSQERISPQIQLSGQTEQTQKAGEGKRNQTTEMRPERQPQTREQDRAHQTGETVTGSGTQTQAGATQTVEQDSSHQTGRTSKQTQEATNDQNRGTETHGQGRSQTSQAVTGGHAQIQAGTHTQTPTQTVEQDSSHQTGSTSTQTQESTNGQNRGTEIHGQGRSQTSQAVTGGHTQIQAGSHTETVEQDRSQTVSHGGAREQGQTQTQPGSGQRWMQVSNPEAGETVPGGQAQTGASTESGRQEWSSTHPRRCVTEGQGDRQPTVVGEEWVDDHSRETVILRLDQGNLHTSVSSAQGQDAAQSEEKRGITARELYSYLRSTKP
The following text describes a protein:
Function:
Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from the membrane-anchored tetraheme c-type NapC protein and transfers these to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as the terminal electron acceptor.
Subcellular Localization:
Periplasm.
Sequence:
MHWAARQPRPSIKPQGGEFTMKKQLIALLSVFTVLAGIAHAELNNPGGIGGLESLRGATEIEATRAADPMKKYPREQALESDFVYQPPLIPHNIRNYEVSLNANKCLACHSWKNAKEMGATKISVTHFVNREDAVLSDVSPRRYFCLQCHVPQADAKPLVENDFERVDSLR
The following text describes a protein:
Function:
Membrane-bound O-acyltransferase involved in the remodeling of glycosylphosphatidylinositol (GPI) anchors. Acts only on GPI-anchored proteins, but not on free GPI lipids. Also involved in lipid metabolism, having profound effects on sphingolipid-sterol-ordered domains integrity and assembly. Involved in cell integrity and apoptosis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MLRLFRFDVLETSTKDTERPNSKSSRLSSTSGSSHPSSSSRLTVRSAVPEKSAFGSIEFIFYFSVILSILTIACFKIHYVSSPKHPNYKNIEKYLKPGWLFGQKVDSADFQYSAFRENMPILLLVIIVYNFLWRLVKLVFTKNTNDELAIKNNYRLCFSLLFALLVYGTGVIYVLTIALINYLISKSLKNSIFNPLLTWTLDISVVFFKEYFAYCKFSSLHPGLGFLDQYTGILERWYVLFNITMLRLVSFNMDYYWSLKHNSEKLNTLIFDKDREPTTLTFRERVDYSCLDEDYNLKNFLTYIFYAPLYLAGPIISFNNFMSQMKYPTVSTLKYRNLLYAIRFLVCVLTMEFLLHYAYVTAISKDGNWNQYSAVESAMISFIVLFMTWLKLLIPWRLFRLWSLIDDIEPPENIVRCMCNNYSAVGFWRAWHRSFNRWLIRYIYVPLGGSNHSILNLFIIFTFVALWHDISWELFAWGWLIVLFILPERLCCFMSRRTGLTKHPYYRYISGFGAALNIYFMIICNLIGFAVGIDGIKNVLVSFFLTLKGAMSAIAAFIMFFSAVQIMFQIRVNEEEEGINLRC
The following text describes a protein:
Function:
Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Localization:
Cell projection, cilium membrane; Multi-pass membrane protein.
Sequence:
MALITFYQIPKTIKYKSNVCSCATFITVLLFLLTFIPPLIIVLLTENFLNGINTGYERPIVYFNSKLLCYLKTDQHGNYITWSTFPNHQFIEASQLRVPNATSVTTFKMESMGHIGFVVPPHCNNLELIGRLVLLQNVPITFNDTLYEAPVINQSSLSSKTYQVVNVLKHYNRRKVRTQLTNQQAVWRKDADEPNKSTFTVKLIISYDAAFNFYYYQTIWEQLKWFWVVYLAILIPFYWVFGYIRRLIFTNHMVITWVAKGENFRYGTRMKDEGYT