data_small/SwissProtV3/valid_set.jsonl

{"protein": "MALLAEHLLKPLPADKQIETGPFLEAVSHLPPFFDCLGSPVFTPIKADISGNITKIKAVYDTNPAKFRTLQNILEVEKEMYGAEWPKVGATLALMWLKRGLRFIQVFLQSICDGERDENHPNLIRVNATKAYEMALKKYHGWIVQKIFQAALYAAPYKSDFLKALSKGQNVTEEECLEKIRLFLVNYTATIDVIYEMYTQMNAELNYKV", "text": "FUNCTION: Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides. FUNCTION: Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GLTP family."}
{"protein": "MDADDTPPNLQISPTAGPLRSHHNTDGHEPNATAADQQERESTNPTHGCVNHPWANPSTATCMESPERSQQTSLFLLKHGLTRDPIHQRERVDVFPQFNKPPWVFRISKLSRLIVPIFTLNEQLCFSKLQIRDRPRFAGRGTYGRVHIYPSSKIAVKTMDSRVFNRELINAILASEGSIRAGERLGISSIVCLLGFSLQTKQLLFPAYDMDMDEYIVRLSRRLTIPDHIDRKIAHVFLDLAQALTFLNRTCGLTHLDVKCGNIFLNVDNFASLEITTAVIGDYSLVTLNTYSLCTRAIFEVGNPSHPEHVLRVPRDASQMSFRLVLSHGTNQPPEILLDYINGTGLTKYTGTLPQRVGLAIDLYALGQALLEVILLGRLPGQLPISVHRTPHYHYYGHKLSPDLALDTLAYRCVLAPYILPSDIPGDLNYNPFIHAGELNTRISRNSLRRIFQCHAVRYGVTHSKLFEGIRIPASLYPATVVTSLLCHDNSEIRSDHPLLWHDRDWIGST", "text": "FUNCTION: Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and regulation of viral and cellular gene expression. Regulates the nuclear localization of viral envelopment factor proteins 24 and 27, by phosphorylating the protein kinase ORF66, indicating a role in nuclear egress. Disrupts host nuclear lamins, including LMNA and LMNB1. Phosphorylates the viral Fc receptor composed of glycoproteins E (gE) and I (gI) (By similarity). Phosphorylation of glycoprotein E (gE) by UL13 alters its subcellular localization, from the host early endosome to the plasma membrane. Participates in the transcriptional regulation of cellular and viral mRNAs mainly by phosphorylating the viral transcriptional regulator IE63. FUNCTION: Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and regulation of viral and cellular gene expression. Regulates the nuclear localization of viral envelopment factor proteins 24 and 27, by phosphorylating the protein kinase ORF66, indicating a role in nuclear egress. Disrupts host nuclear lamins, including LMNA and LMNB1. Phosphorylates the viral Fc receptor composed of glycoproteins E (gE) and I (gI). Phosphorylation of glycoprotein E (gE) by UL13 alters its subcellular localization, from the host early endosome to the plasma membrane. Participates in the transcriptional regulation of cellular and viral mRNAs mainly by phosphorylating the viral transcriptional regulator IE63 (By similarity). SUBCELLULAR LOCATION: Virion tegument Host nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MANLPILLDYWPSMFGMRARVALREKGVEFEYREEDFSNKSPLLLQSNPIHKKIPVLVHNGKPVCESLNVVQYVDEAWPEKNPFFPSDPYGRAQARFWADFVDKKFTDAQFKVWGKKGEEQEAGKKEFIEAVKILESELGDKPYFGGDSFGYVDISLITFSSWFQAYEKFGNFSIESESPKLIAWAKRCMEKESVSKSLPDSEKIVAYAAEYRKNNL", "text": "FUNCTION: Exhibits glutathione-dependent thiol transferase activities. Can use glutathione (GSH) and 1-chloro-2,4-dinitrobenzene (CDNB) as substrates. Involved in the regulation of far-red light influence on development (PubMed:17220357). Regulator of the interplay between light and JA signaling by increasing JAR1/FIN219 efficiency (PubMed:28223489). Maybe involved in gravitropic signal transduction (Probable). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol. SIMILARITY: Belongs to the GST superfamily. Tau family."}
{"protein": "MAQSKFLREYKLVVVGGGGVGKSCLTIQLIQSHFVDEYDPTIEDSYRKQCVIDDEVALLDVLDTAGQEEYSAMREQYMRTGEGFLLVYSITSRQSFEEITTFQQQILRVKDKDYFPMVVVGNKCDLEGEREVTRQEGEALARSFNCKFIETSAKSRINVDKAFYDIVREIRRYNREMQGYSTGSGGSNAGGPSNKMEVNDSDAEAGCCSKCVLM", "text": "FUNCTION: Modulates the activity of the adenylate cyclase catalytic subunit and therefore affects the biosynthesis of cyclic-AMP (By similarity). Plays a role in both surface attachment and surface recognition of appressoria, a highly specialized infection structure for plant penetration. Regulates appressorium formation by coordinated regulation of cAMP signaling and Pmk1 MAPK pathways (PubMed:24835254). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
{"protein": "MGKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFSSVQYIMTEVNFGWLVRSVHRWSASMMVLMMILHVFRVYLTGGFKNPRELTWITGVILAVLTVSFGVTGYSLPWDQIGYWAVKIVTGVPEAIPVIGSPLVELLRGSVSVGQSTLTRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b family. PetB subfamily."}
{"protein": "MLNIAIAVFIGGGLGSVLRWLISYRLNSLFPHFATGTLVANCIGAFIIAFGIAWFSKAPNIDPIWKIMLTTGFCGGLTTFSTFSVEVVALFNEGRIGWALGTMGANLAGSFLMTAFAFWLLREM", "text": "FUNCTION: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family."}
{"protein": "LAGSKHKEEKADLDPSNPVANWIHARSTRKKRCPYTKYQTLELEKEFLFNMYLTRDRRYEVARVLNLTERQVKIWFQNRRMKMKKMNKEKTDKEQS", "text": "FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Abd-B homeobox family."}
{"protein": "MAHDEQLWLTPRLQKAAALCNQTPAASDTPLWLGVDLGTCDVVSMVVDGNAQPVAVCLDWADVVRDGIVWDFFGAVTLVRRHLDTLEQQLGCRFTHAATSFPPGTDPRISINVLESAGLEVSHVLDEPTAVADLLALDNAGVVDIGGGTTGIAIVKQGKVTYSADEATGGHHISLTLAGNRRIPLEEAEQYKRSNAQEIWPVVKPVYEKMAEIVARHIEGQGIADLWLAGGSCMQPGVEALFRQRFPELQVHLPQHSLFMTPLAIANSGRAKAEGLYAS", "text": "FUNCTION: May protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition, may function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. FUNCTION: May protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition, may functin in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity (Probable). Overexpression of eutJ and eutS in E.coli leads to multiple BMC-like structures; eutS expression alone leads to 1 BMC-like structure per cell (PubMed:27063436). FUNCTION: Expression of the eut operon allows this bacteria to use ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078). EA enhances bacterial survival in macrophages in a concentration- dependent manner, suggesting it is an important nutrient during infection (PubMed:29531136). SIMILARITY: Belongs to the EutJ family."}
{"protein": "MDMRTSFLCVTYVILLTGSACGLQITSTGQTSIEKASGESVKLDCQFTLASDDSGPLDIEWSLQPSDNQKEEKVVIVYSGDRAFEHYYDPLKGRVHFNSPDPKNGDASMNIMGLKATDTGTYQCKIKKVPGIASRKYLLTVMVRPSKPKCSAEGQTYVGKNMVLKCSSVEGTQPMEYIWERTSGNKLLPPLAILDKVTGTMTLKNATGDASGTYRCQAKNRVGTEECVVEVTITQPPNTAGIIAGVIICILLLLILLALILFCCCRARHKKKYEKEIAYEIREDVPPPKSRVSTARSFTSVGSQRSSLGSMSPSNLHEYSKPQYDKIPSEEYDRPPSHAPIPPPSRMAGPNLSRMGAIPVMIPAQNKDGSIV", "text": "FUNCTION: May function as a homophilic cell adhesion molecule and be essential for tight junction integrity. May also be involved in transepithelial migration of leukocytes through adhesive interactions with jaml. The interaction between both receptors may also mediate the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Basolateral cell membrane; Single-pass type I membrane protein Cell junction, tight junction Cell junction, adherens junction."}
{"protein": "MPTKTSQHAFAGSERWVVPRYSSKPGTLIRLGSVLTDPEDLESSLNLDSIPPIPPHLLRDATPEVRMSVQTELSKSDSTLAKAAPALEGILTLGGGVEASRSQGVSSSLNISGTVKATVFRADKSYMDVLLKDKNVISYAKRGLGKPMFVVVGVATAGRVEMKETRHVTRKAGVSGKVGVEVIGEGEVGLERERSDKSCNEVRGEGGLDFAYRVREFGYSRVRGTVKDKGDWTGKVLFAGGKGPVVEKGGEVVPVFKEFKEGEVKLRATGSFDVAAKA", "text": "FUNCTION: [Gasdermin-like protein het-Q1, N-terminal]: Pore-forming protein that causes membrane permeabilization and cell death (PubMed:35135876). Released upon cleavage and maturation by het-Q2 and binds to membrane inner leaflet lipids (PubMed:35135876). Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering cell death (By similarity). FUNCTION: [Gasdermin-like protein het-Q1]: Gasdermin-like protein involved in heterokaryon incompatibility, a process that ensures that during spontaneous vegetative cell fusion, only compatible cells from the same colony survive (non-self-recognition) (PubMed:35135876). In P.anserina, the het-q locus exists as 2 incompatible alleles, het-Q1 (this entry) and het-Q2 (AC P0DW09) (PubMed:35135876). This form constitutes the precursor of the pore-forming protein: during the allorecognition process, it is cleaved by het-Q2, releasing the N- terminal moiety (Gasdermin-like protein het-Q1, N-terminal) that binds to membranes and forms pores, triggering cell death (PubMed:35135876). SUBCELLULAR LOCATION: [Gasdermin-like protein het-Q1, N-terminal]: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the gasdermin family."}
{"protein": "MTHNIHDNISQWMKSNEETPIVMSSRIRLARNLENHVHPLMYATENDGFRVINEVQDALPNFELMRLDQMDQQSKMKMVAKHLISPELIKQPAAAVLVNDDESLSVMINEEDHIRIQAMGTDTTLQALYNQASSIDDELDRSLDISYDEQLGYLTTCPTNIGTGMRASVMLHLPGLSIMKRMTRIAQTINRFGYTIRGIYGEGSQVYGHTYQVSNQLTLGKSELEIIETLTEVVNQIIHEEKQIRQKLDTYNQLETQDRVFRSLGILQNCRMITMEEASYRLSEVKLGIDLNYIELQNFKFNELMVAIQSPFLLDEEDDKSVKEKRADILREHIK", "text": "FUNCTION: Catalyzes the specific phosphorylation of arginine residues in proteins (By similarity). Is required for stress tolerance and virulence in S.aureus. Acts as a modulator of the repressor activity of CtsR upon heavy metal and oxidative stress caused by these metal ions (PubMed:22902728). FUNCTION: Catalyzes the specific phosphorylation of arginine residues in proteins. SIMILARITY: Belongs to the ATP:guanido phosphotransferase family."}
{"protein": "MTDYYEPINIFRQCAISVKKRGQEHGLDVATRRVASWQRSAKLNSPTLRKVSDDYFLTKKVKSDYWQVSDMDLSATAFSSVGNLVMVTSNKDQDNVKLYTYAEDPNSMRQLQTITVPGAPITTATLLPAAEFNPTAYVPDHEQLLLTGHRDGIVNLISTSFTKGESRIVKRYNHRKHLVSMANEVMNIDTKHKDEIEQLLANHKQKSNSARAMPVRSIKPWNGMGFVSLINDSLFVFTLNNTKTPQYLNSFPGIQSFAIQTHSNPYLLGLTGTHFGANNIALLDLKKTLYIPDPVIDKEYRKSSSRSVSSDCTWISSCYLAQALGKEVNIWDVRRTDGKPKAKILPNKGVIEHLSYHYETDTLFSSDDQGNIIAWDLTNLDRLEYCGLVHGLDAVKYNMNLPINDSNYSQCGNVVVNGNNNSACTYRKLARKIEVNQRAGTLFSYCDHELGLHRLFSAPVEISLQLSDTETINYESEEEEVMVHVDKLHDNSHENSSILHSDSTTLHSRDFDSYSDNESANTTDNDNELAYMDTFKRPVPAFLDEKVAAYNNPVLSSSSSTLAYGYF", "text": "FUNCTION: Involved in cell wall metabolism and required for the separation of the mother and daughter cells. SIMILARITY: Belongs to the WD repeat DSE1 family."}
{"protein": "MAKVTANDLLERFQLELLSGEEGIHRSITTSDISRPGIEMAGFFTYYPAKRLQLLGRTELSFYKQLSPVDKEERMSKLCTYDTPGIIISRGLEVPPELLKASEKVGVPVLRSNITTTRLSSMLTNFLESQLAPTTAVHGVLVDIYGIGVLITGSSGVGKSETALDLVRRGHRLVADDSVEIRREHEDTLVGRSPELIQHLLEIRGLGIINVMTLFGAGAVRPFKRIALCVNLELWDQKKVYDRLGLSEDYLRIMNVDIPKLTIPVRPGRNLAVIIEVAAMNFRLKRLGINAAQQFSDRLNDVIEEGEQEF", "text": "FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Also phosphorylates/dephosphorylates the HPr-like catabolite repression protein crh on a specific serine residue. Therefore, by controlling the phosphorylation state of HPr and crh, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion (By similarity). SIMILARITY: Belongs to the HPrK/P family."}
{"protein": "MASIGSQVRKAASSIDPIVTDYAVGYFNHLSGITFDAVQSKQVDLSTEVQFVSDLLIDAGASKAKVKELSESILKQLTTQLKENEAKLELTGDTSKRLLDINVLKSHNSKSDINVSLSMLGVNGDIEHTGRKMETRVDLKKLAKAEQKIAKKVAKRNNKFVKYEASKLINDQKEEDYDSFFLQINPLEFGSSAGKSKDIHIDTFDLYVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSILHVEQELRGDDTKALQSVLDADVWRKQLLSEEAKINERLKEMDVLRQEFEEDSLEVKKLDNEREDLDNHLIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIYQHNERLDYYRGQDFDTFYTTKEERRKNAQREYDNQMVYRKHLQEFIDKYRYNAAKSQEAQSRIKKLEKLPVLEPPEQDKTIDFKFPECDKLSPPIIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRFEGTIYDYRDYILQSADAAGVVKKH", "text": "FUNCTION: Acts as a positive activator of the GCN2 protein kinase activity in response to in response to low amino acid, carbon, or purine availability (PubMed:7621831, PubMed:10733573). Component of the GCN1-GCN20 complex that forms a complex with GCN2 on translating ribosomes; during this process, GCN20 helps GCN1 to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA-binding domain of GCN2, and hence stimulating GCN2 kinase activity (PubMed:7621831, PubMed:9234705, PubMed:10775272, PubMed:15722345). Participates in gene-specific mRNA translation activation, such as the transcriptional activator GCN4, by promoting the GCN2-mediated phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52', and hence allowing GCN4- mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:15722345). SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily."}
{"protein": "MAFSPNVLLGGRVCAAVARSGFATRRVTIPGSTSREPDPDFDWEPEERELQEVESALKRQKKAIRFQKIRRQMEASGAPPRTLTWEAMEQIRYLHREFSESWSVPRLAEGFDVSTDVIRRVLKSKFIPTLEQKLKQDQKVLKKIGLARSIPELPGPGDSSKPLSAGQSVSGSLLIPGDEASSRGHGHSTALKAIELNTQSTNITTRQTERNKGVQGLEEGKDFVPVAAGHPTSTCRGARGIDSDGLPSDKRLEELKAGEAGDQIFSKRVVQRGREFFDSNGNFLYRI", "text": "FUNCTION: Plays an essential role in mitochondrial ribosome biogenesis. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation of core subunits of the oxidative phosphorylation system. SUBCELLULAR LOCATION: Nucleus Secreted Mitochondrion membrane. SIMILARITY: Belongs to the neugrin family."}
{"protein": "MGDDQSLRSTVAENDISANLSFTQGFLLGQLSVVLLIGAFIKFFIFGEAPPPPSRGLSHRASTHRRSNSIYTINPNEGTSRSLREKPSTSNVLRPVPSSATNTRSILRKTYYSAIPTNPSGKHGRHRIHHSSHQPESLDWFNVLIAQTIAQYRQTAYLLKDDPTSSILSSLTAALNNPEKKPSFIDKIAVTDISLGEEFPIFSNCRIIAVDDPNSDGGRLQALLDVDLSDDNLSIAVETSLLLNYPKPCSAILPVALSISVVRFSGTLCISLVPASTPPLHTPSPSPSPPTADGAVNAGTHPTNGSREPTQEAPNAQEESPPKTSPKSNVAFSFLPDYRLDLSVRSLIGSRSRLQDVPKVAQLVEARVHSWFEERVVEPRVQVVGLPDLWPRMGRTGVRTGEDSETGSNAASRSAMSADMGNSLRADDIGREPDGLRFRGLGARPPFDSVSRTSSFNVETGGFRSHSMTREGSGGGMSDDFHMPGTLPGGAAAN", "text": "FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta- barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I 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. SIMILARITY: Belongs to the MMM1 family."}
{"protein": "MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLESGEVVEGHKKPSSDTPTHRLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEINGEYEWETGNVIVETFEKQGIDAAQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQSLLDKHYLRKHGAKAYYGQ", "text": "FUNCTION: Involved in the degradation of L-arabinose. Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5- phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond cleavage analogous to a class II aldolase reaction). SIMILARITY: Belongs to the aldolase class II family. AraD/FucA subfamily."}
{"protein": "MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHRFLVALYDPDRFLCSGILLNEEWVLTAAHCDRRNIRIKLGMHSKTVPNEDEQTRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVSNSEHIAPLSLPSSPPSVGSVCRIMGWGRISPSKETYPDVPHCANINLLDYEVCLAAYPEFGLPATSKTLCAGILEGGKDTCVGDSGGPLICNGQFQGILSWGNDVCGYILQPALYTRVFDHLDWIQSIIAGNTDVTCPP", "text": "FUNCTION: Snake venom serine protease that may act in the hemostasis system of the prey. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
{"protein": "MSTILESLPTGQKVGIAFSGGLDTSAALHWMKLKGAVPYAYTANLGQPDEDDYDAIPKRAIEYGAAGARLIDCRAQLVAEGIAALQSGAFHITTAGVTYFNTTPIGRAVTGTMLVAAMKEDGVNIWGDGSTYKGNDIERFYRYGLLVNPDLKIYKPWLDQTFIDELGGRAEMSEFMNQAGFAYRMSAEKAYSTDSNLLGATHEAKDLESLESGIKIVNPIMGVAFWRDDVKIAAEEVTVRFEAGQPVALNGVEFKDQVELLLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGLALLYIAYERLVTGIHNEDTIEQYRENGRRLGRLLYQGRWFDPQAIMLRETAQRWVARAITGEVKIELRRGNDYSILSTKSPNLTYQPERLSMEKVASTFSPRDRIGQLTMRNLDITDTRDKLRVYAQVGLLTPGESSALPQIKSDSGE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argininosuccinate synthase family. Type 2 subfamily."}
{"protein": "MATVIHNPLKALGDQFYKEAIEHCRSYNSRLCAERSVRLPFLDSQTGVAQNNCYIWMEKRHRGPGLAPGQLYTYPARCWRKKRRLHPPEDPKLRLLEIKPEVELPLKKDGFTSESTTLEALLRGEGVEKKVDAREEESIQEIQRVLENDENVEEGNEEEDLEEDIPKRKNRTRGRARGSAGGRRRHDAASQEDHDKPYVCDICGKRYKNRPGLSYHYAHTHLASEEGDEAQDQETRSPPNHRNENHRPQKGPDGTVIPNNYCDFCLGGSNMNKKSGRPEELVSCADCGRSGHPTCLQFTLNMTEAVKTYKWQCIECKSCILCGTSENDDQLLFCDDCDRGYHMYCLNPPVAEPPEGSWSCHLCWELLKEKASAFGCQA", "text": "FUNCTION: Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron- specific complexes (nBAF). The npBAF complex is essential for the self- renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Specifically binds acetylated lysines on histone 3 and 4 (H3K14ac, H3K9ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac). In the complex, it acts as a tissue-specific anchor between histone acetylations and methylations and chromatin remodeling. It thereby probably plays an essential role in heart and skeletal muscle development. FUNCTION: [Isoform 2]: Acts as a regulator of myogenesis in cooperation with HDGFL2 (PubMed:32459350). Mediates the interaction of HDGFL2 with the BAF complex (PubMed:32459350). HDGFL2-DPF3a activate myogenic genes by increasing chromatin accessibility through recruitment of SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex) to myogenic gene promoters (PubMed:32459350). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the requiem/DPF family."}
{"protein": "MKVLDQSLLWMLLPFFHLIASAAEHEEVAKHAIKLHRGKGATATQRKQWALDSCRRLTGLLRQKNVVLNKLKNAIRAVEKDTSLSGEEKLFQVHTFEIFQKELNESENSIFQAIYGLQRALQGDYRDVVNMKESSKQRLEALREAAIKEETEYVELLAAEKHQVEALKNMQHQNKSLSMLDEILEDVRKAADRLEEEIEEHAFDDNKSVKGVNFEAVLRVEEEEASSKQNMTKREVEDGLGLSMLIDSQNNQYILTKPRDSTIPRADHHFIKDIVTIGMLSLPCGWLCTAIGLPTMFGYIICGVLLGPSGLNSIKSIVQVETLGEFGVFFTLFLVGLEFSPEKLRKVWRISLQGPCYMTLLMIAFGLWWGHLLRIRPTQSVFISTCLSLSSTPLVSRFLVGSARGDKEAGDIDYSTVLLGMLVMQDVQLGLFIAVMPTLIQAGAGASSSVVMEVLRILFLIGQILFSLAAVFLLCLVMKTYLIGPYYRKLHLESKGNKEILVLGVSAFTFLMLTVTELLDVSMELGCFLAGALVSSQGHMVTEEIMTYIEPIRDFLAIIFFASIGLHVFPTFVIYELTVLVFLTLSVVIMKFVLAVLVLSLILPRSSQYIKWIVSAGLAQVSEFSFVLGSRARRAGILSREVYLLILSVTTLSLLLAPVLWKAAITKCVPRPERRSSL", "text": "FUNCTION: Probable Na(+)/H(+) antiporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family."}
{"protein": "MKRVVIAGTSSMVGKTTISTGIMKALSKKNNVQPYKIGPDYIDPTYHTEATKNKSRNLDSFFMDEMQVRSIFKRHSKNKDINVIEGVRGLYEGISPYNDVGSTASVSKTLNAPVILLMDARSLTRSAAAIIKGFKSFDTELNIKGVIFNKIRGEGHLNKLKEAVKYYDNDIEIIGAIPRDDGLSVSQRHLGLVPTPENKQKLLERIDLWGNTVEECLDIEKIVELSDESFDFEVDEKNKEETLWKVEKNNSKIAVAFDESFNFYYWDNFDALEENGAKIKFFSPLNDVEVPDCDTIYLGGGYPELFSEKLSNNKSMIDSIRNFDGKIYGECGGLMYLTNSIDGKEMLKLIDADAVMTPNVQGLSYVKGTFEKDCIIGEKSKEFKAHEFHYSKLININENDFSYRINRGKGIINSMDGITSKDGDIVGGYAHQHCIGNPYFAANLSKT", "text": "FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. SIMILARITY: Belongs to the CobB/CbiA family."}
{"protein": "MHRPNFRPPTPPYPSPGIGGWGGGNNFRGALGGGPRPPSPRDGYGSPHHTPPCGPRARPYGSSQSPRHGGNFSGARFGSPSPGGYPGSYSRSPAGSQHQFGYSPGQQQTYPQGSPRTSTPFGSGRGREKRMSNELESYFKPSMLEDPWAGLEPVSVVDISQQYSNTQTFTGKKGRYFS", "text": "FUNCTION: May play a role in maintenance of cell cycle integrity by regulating mitosis or cytokinesis. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=The subcellular location is regulated during cell cycle. During interphase located in the nucleus. During mitosis located at the centrosome and dispersed in the cytoplasm. During telophase located in the midbody. Colocalizes with PLK1 at the centrosome in M phase."}
{"protein": "MALPIIIDCDPGHDDAIALVLALASPELEVKAITSSAGNQTPEKTLRNVLRMLTLLKRPDIPVAGGAVKPLMRELIIADNVHGESGLNGPALPEPSFAPQSGTAVELMAKTLRESAQPVTIVSTGPQTNVALLLNSHPELHTKIARIVIMGGAMALGNWTPAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHAADIERFRAIGNPISTIVAELLDFFMEYHKDEKWGFVGAPLHDPCTIAWLLKPEIFTTVERWVGVETKGKYTQGMTVVDYYFLTGNKPNATVMVDVDRQGFVDLLAERLQYYA", "text": "FUNCTION: Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. SIMILARITY: Belongs to the IUNH family. RihA subfamily."}
{"protein": "MGSNQDDQAFLFAMQLASASVLPMVLKTAIELDLLETIAKAGPHGSVSSSELVAQLPKVNNPEAPVMIDRICSLLASYSVLTCTLKETADGCAERFYGLAPVCKFLIKNDAGVSLAPLLLMNQDKVLMESWYYLKDPVLDGGIPFNKAYGMSAFEYHGKDQRFNKVFNSGMFNHSTMTMKKIVELYNGFSGLKTLVDVGGGTGASLNMITSKHKSLKGINFDLPHVIADATTYQGIEHVGGDMFESVPKGDAIFMKWILHDWSDAHCLQVLKNCYKSLPENGKVIVAECILPEAPDTTPATQNVIHIDVIMLAHNPGGKERTEKEFEALAKGAGFKGFNKAACALNTWVMEFCK", "text": "FUNCTION: Catalyzes the conversion of caffeic acid to ferulic acid and of 5-hydroxyferulic acid to sinapic acid. The resulting products may subsequently be converted to the corresponding alcohols that are incorporated into lignins. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily."}
{"protein": "MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAAMSLLQQLEAIESTLLEKEADRNSRQKRCNGENVPCGPNHSTCCSGLSCEETFGYGWWYDTPFCVKPSKG", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 06 (ICK-Trit) subfamily."}
{"protein": "MAVGKNKRLSKGKKGIKKRVVDPFSRKDWYDIKAPSFFEVKNVGKTLVNRTAGLKNANDALKGRIVEVSLADLQKDEEHSFRKVKLRVDDVQGKACLTTFNGMSMTSDKLRSLVRKWQTTIEADQTIKTTDGYVCRIFVIGFTRRRYNQIKKTTYAQSSQIRAIRQKMFQVIQNQATGCSMRELVQKLIPEIIGREIEKATGGIFPLQNVFVRKVKILKSPKLDAQKLLEQHGEAQDVGTKVIKDVAPLASV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family."}
{"protein": "MTDTKQLFIEAGQSQLFHNWESLSRKDQEELLSNLEQISSKRSPAKLLEDCQNAIKFSLANSSKDTGVEISPLPPTSYESLIGNSKKENEYWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQDMVKDKKVEIPWYIMTSGPTRAATEAYFQEHNYFGLNKEQITFFNQGTLPAFDLTGKHFLMKDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGIKHVYMYCVDNVLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIATKNEKPCVIEYSEISNELAEAKDKDGLLKLRAGNIVNHYYLVDLLKRDLDQWCENMPYHIAKKKIPAYDSVTGKYTKPTEPNGIKLEQFIFDVFDTVPLNKFGCLEVDRCKEFSPLKNGPGSKNDNPETSRLAYLKLGTSWLEDAGAIVKDGVLVEVSSKLSYAGENLSQFKGKVFDRSGIVLEK", "text": "FUNCTION: UDP-N-acetylglucosamine pyrophosphorylase that utilizes N- acetylglucosamine-1-phosphate as substrate (PubMed:9603950). Together with AGM1, is involved in the production of UDP-N-acetylglucosamine from N-acetylglucosamine-6-phosphate (PubMed:9603950). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UDPGP type 1 family."}
{"protein": "MSFFKKLAASAGIGAAKVDTILEKDAYFPGEEVQGTVHVKGGKIAQDIRYIDLQLSTRYVIVKDDEEHRKYATIHSFRVTGSFTIQPGEEHQFPFTFTLPLDTPITVGKVEVAVVTDLDIQGGIDKSDHDRIFVEAHPWIENVLEAIENLGFRLNEADCEQAPYFQRRLPFVQEFEFVPTSGYYRQMLDELELIFLLDEDGLEIIFEVDRRARGLRGWLEEMYNDGEQLVRVRFSQSELEDTEELEEVLEEILDQYAE", "text": "FUNCTION: Controls the expression of spo0A and is required to pass the morphological stage 0 of sporulation. SIMILARITY: Belongs to the spo0M family."}
{"protein": "MAEDDMVSLLFKLKVEDVTCSDDPEKHMKNASNERKPLIEPVENQLMDIGEEGGSLDYWLLYLYVDCLTMMCCFHRGSLPYNWMQGALLTNLPSYQHDVTLDEVNRGLKSASDFFGYVDPMRSDYFTAFSFPGRVTKLNEQMELTSTKGRCLKFDLYASTQLRFKPGELVRHGECKFAIG", "text": "FUNCTION: Hydrolyzes cytokinin glucosides thus liberating free cytokinins."}
{"protein": "MDVDVEEAALEQVAALLQRPDQLEKLPELKKRADRKKLAVEAMLRTGVQGQLEGIRTAIAHLQTASDDITAISQGVHDIRERLGPFPQLKEKLRELRDANARHGQYAAAMENLKHIFNLQTTLQEIRDALDDEKSGGNLLLAHKHIMDLERARDELLAEVHKMSGTNTEKEQMLLVNFFKGVDSVVAELSKNMWFILGRTLEMVKGNEQGGGPQQVVTCLRIVEREERIDKFYMEARSKNSSAFVPPGRPRNWKEKALRSLEKTVSNRVDGNQLEDRSLNKAWLARYLEVCKNVIMDDLQLAKVAIPCFPPDWQIYDRYVHMYHTSVCRRLREVASEHLEKSELVQLMSWIKFYASEDMLGHPKLRINAQAILQDSPVLSRSTLNQLCDQFVEMSRDDLKLWLKNTVSHETHDWYKNLRPSEDNHGYFYTDLPNTVFGMLKDTVTLAKEVSVEVIPSIINLTIQEFNELAGKYRDAFTAYKTDYFAERSKYQEFTSNIIAIANNLHTCIESTEKYKQQIRLSMEGEQNAAAAMTTPLASGRRTAVRQQQLIENMDALNTKWSNAASVAVNYLREEVITDIAPSLVEIFSKKWLTGSAALETVCMTISDYYHDHKHLRPVTRSTLLMDLQFRIVSEYLKAIETKRVSLNSYEERALAGKRMKADVVRLDNLYAEFATSSDMADQLPLLTSIVAAAGDVISLKDKSLLSLEATSFARKFPNCPAELLSAVIATRDDISGSEARSLASEVLQHVQFHPKDQIFDQLFALRQQENSERLPNLGMANMFKADFMSMLKRDA", "text": "FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. SIMILARITY: Belongs to the SEC6 family."}
{"protein": "MNSETGALRRGWTTGTCASAAARAAFEALLGIEPEDPVPVTLPSGARPTFALARLDRGSGFVRAGIVKDAGDDPDVTHGALVLATLRFGAPATGIVFRAGPGVGIVTKPGLPLPPGEPAINAMPRRMIRTALTEVAEANGVTCDLVVEVGIEDGERIAERTMNRRLGIIGGLSILGTTGVVVPYSCAAWIASIHRGIDVARAEGLTHLAGATGATSEAAIRNLYGLPEQALIDMGDFVGGMLKYIRGHPVARVTIAGGFAKMTKLAQGRLDLHSKREAIDFRWLAELYCSIGGKAESGMSVRTANTALEVLQMAQAEHVPIAPAIARSACRVAAGALARADIALDVAIFDRDGCLIASERC", "text": "FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. SIMILARITY: Belongs to the CbiD family."}
{"protein": "MKSLVLGLLVGSAIASGPLQHVLHAPPDPEPKPEPEPQVVKDPFEELRDTFDRLRNKAGDIWDDVMDNIPNIMSNMRPLTIPAKKFTRRPDSEWTHIVRGADLEALWVDDESGYKHRKIDGKLSQYDLRIKAVDPSDLGIDKVKQYSGYLDDNANDKHLFFWFFESRNDPFGDPVVLWLNGGPGCSSLTGMFFELGPASIDENITANYNPYSWNSNSSIIFLDQPVNVGYSYSSQAVSDTVTAAKDVYALLTLFFTQFRQYSAQDFHIAGESYAGHYIPVFASEILHHNNTNINLQSVLIGNGLTDPLSQYPFYRPMACGDGGYPSVLDSQSCQSMDNALPRCLSMIKSCYDIESTFTCLPASIYCNNALIGPYQKTGRNPYDVRTNCTGNDLCYPQLNYITEYLNKPHVMRSLGVEVDSYESCNMDINRNFLFHGDWMKPYHRLVPSLLARIPVLIYAGDADFICNWLGNKAWTEALEYPGHAKFAEAPMENLTMINSQGKNEVFGEVKSHSNLTFMRIFKAGHMTPFDSPQASLEFANSWLSGEWSEV", "text": "FUNCTION: Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (By similarity). SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the peptidase S10 family."}
{"protein": "MGGALSTDGAEQRASSVEELNQRLAHRFAAKCFEPLELTHLKENFFSRALDQHGIRYWNEEILSEFLGIPDGAGSAAAATSDGSLDAGPVIFRMVSYLGAFPFQNTMAPTVLTFESMVKVVVLLTERYGKVLKRGKKDRMKLLFGSLADVGRRDIITVLKEATEDSLESIGPSDPRSASPSTHNTGFLVDQPVNDEDEEDDDDLAIAALESLDAIEVFKHDQRIDKTVYESKISLTTFRRLLTLLLVTAPLRPLGRVSKFTTGLSKPSLDAVHEQVDSILAALDPGEASDGIGYKSFSKLVSTSLPYLFDPLTPLFEHLLFSKNLDLSRKRDSQTTNGLTSKPVPTPPSTPPLSPPLSPVISTGGFDSCILNPALLSHLSFFVSTNVHIPNIFRNRTHLHPVFSSTEHGESLTSFSHHVMTWQAPSILLVRGAVVSESSEEQLTTIGAYLPQPWKQTSSYSSRRSSEAPDPSTLPCLFELSPVHTVLQGSPSFSSLKSNMPVTHFSTKTGIAIGCMIPPSSRKSFGSDLHPKPAGGGSLLIDSALENATFIVSNGLNGPGVFLPPGISPVLSSTSLTASVPSMSSSNQNFTKSISIYNLEVWGIIPSTSLATQLDGSGSPIEKRDAISLQRAQWDFEAREAERRQAINMKVGGGESDAQTGRALLEMAGIIGDSYYSGHHRH", "text": "FUNCTION: May be involved in a process influencing telomere capping. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RTC5 family."}
{"protein": "MNHQEVADRVLNAIGKNNIQAAAHCATRLRLVIKDESKIDQQALDDDADVKGTFETNGQYQIIIGPGDVDKVYDALIVKTGLKEVTPDDIKAVAAAGQNKNPLMDFLKVLSDIFIPIVPALVAGGLLMALNNVLTAEHLFMAKSVVEVYPGLKGIAEMINAMASAPFTFLPILLGFSATKRFGGNPYLGATMGMIMVLPSLVNGYSVATTMAAGKMVYWNVFGLHVAQAGYQGQVLPVLGVAFILATLEKFFHKHIKGAFDFTFTPMFAIVITGFLTFTIVGPVLRTVSDALTNGLVGLYNSTGWIGMGIFGLLYSAIVITGLHQTFPAIETQLLANVAKTGGSFIFPVASMANIGQGAATLAIFFATKSQKQKALTSSAGVSALLGITEPAIFGVNLKMKFPFVFAAIASGIASAFLGLFHVLSVAMGPASVIGFISIASKSIPAFMLSAVISFVVAFIPTFIYAKRTLGDDRDQVKSPAPTSTVINVNDEIISAPVTGASESLKQVNDQVFSAEIMGKGAAIVPSSDQVVAPADGVITVTYDSHHAYGIKTTAGAEILIHLGLDTVNLNGEHFTTNVQKGDTVHQGDLLGTFDIAALKAANYDPTVMLIVTNTANYANVERLKVTNVQAGEQLVALTAPAASSVAATTV", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in sucrose transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MVHCAGCKRPILDRFLLNVLDRAWHVKCVQCCECKCNLTEKCFSREGKLYCKNDFFRCFGTKCAGCAQGISPSDLVRRARSKVFHLNCFTCMMCNKQLSTGEELYIIDENKFVCKEDYLNNSNTAKENSLHSATTGSDPSLSPDSQDPSQDDAKDSESANVSDKETGSNENDDQNLGAKRRGPRTTIKAKQLETLKAAFAATPKPTRHIREQLAQETGLNMRVIQVWFQNRRSKERRMKQLSALGARRHAFFRSPRRMRPLVDRLEPGELLPNGPFSFYGDYQSEYYGPGANYEFFPQGPPSSQAQTPVELPFGAAGGPPGTPLGALEHPLPGHHPPGEAQRFPDMLAHPAGDSPSPEPTLPGSLHSMSAEVFGPSPPFSSISVNGGANYGNHLSHPPEMNEAAVW", "text": "FUNCTION: Transcriptional factor that defines subclasses of motoneurons that segregate into columns in the spinal cord and select distinct axon pathways. Acts in conjunction with ISL-2. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MADDVSEFLGQNPETAAWLELVHGECESDKLWRYRKEFILRNLSDVCGEAEVPPPPETNHKALDRLLAYSMVWANHVFTGCRYPLPVMEKVLKMAENIKVTDAPTHTTRDELVAKVKKRGISSSNEGVEEEPCKKQKSSDHGERESSYIEDTISDGNVPSTSLNKREARLSAAQRTDVNTEFYDKSSNRRSLPVSNAKSRLNLPEEAGYKHGATQGRKSHSDIRHQTSMKGPAQSSDNALKPTRRFTTEHTKERQPFFNRLYKTVAWKLVSAGGFNANLNHEELLNTCIESLKATLEVSFVPLTDLADLPQNKTSQENTVCELRCKSVYLGMGCGKTMETAKAVASREAVKLFLKKKVVVRICKRKFNGRDVEDLVLVDEEFRPVNLPPAIKNPQEIV", "text": "FUNCTION: May regulate DNA damage response and cell proliferation. SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SIMILARITY: Belongs to the CARF family."}
{"protein": "MAERALEPEAEAEAEAGAGGEAAAEEGAAGRKARGRPRLTESDRARRRLESRKKYDVRRVYLGEAHGPWVDLRRRSGWSDAKLAAYLISLERGQRSGRHGKPWEQVPKKPKRKKRRRRNVNCLKNVVIWYEDHKHRCPYEPHLAELDPTFGLYTTAVWQCEAGHRYFQDLHSPLKPLSDSDPDSDKVGNGLVAGSSDSSSSGSASDSEESPEGQPVKAAAAAAAATPTSPVGSSGLITQEGVHIPFDVHHVESLAEQGTPLCSNPAGNGPEALETVVCVPVPVQVGAGPSALFENVPQEALGEVVASCPMPGMVPGSQVIIIAGPGYDALTAEGIHLNMAAGSGVPGSGLGEEVPCAMMEGVAAYTQTEPEGSQPSTMDATAVAGIETKKEKEDLCLLKKEEKEEPVAPELATTVPESAEPEAEADGEELDGSDMSAIIYEIPKEPEKRRRSKRSRVMDADGLLEMFHCPYEGCSQVYVALSSFQNHVNLVHRKGKTKVCPHPGCGKKFYLSNHLRRHMIIHSGVREFTCETCGKSFKRKNHLEVHRRTHTGETPLQCEICGYQCRQRASLNWHMKKHTAEVQYNFTCDRCGKRFEKLDSVKFHTLKSHPDHKPT", "text": "FUNCTION: Transcriptional repressor. May repress NR5A1, PPARG, NR1H3, NR4A2, ESR1 and NR3C1 transcriptional activity. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MKSSVSWLFFSSIPLFSSLSIVAAEVTLDSSNNSYDGSNGTTFTVFSTTDAAAGTTYSLLSDVSFQNAGALGIPLASGCFLEAGGDLTFQGNQHALKFAFINAGSSAGTVASTSAADKNLLFNDFSRLSIISCPSLLLSPTGQCALKSVGNLSLTGNSQIIFTQNFSSDNGGVINTKNFLLSGTSQFASFSRNQAFTGKQGGVVYATGTITIENSPGIVSFSQNLAKGSGGALYSTDNCSITDNFQVIFDGNSAWEAAQAQGGAICCTTTDKTVTLTGNKNLSFTNNTALTYGGAISGLKVSISAGGPTLFQSNISGSSAGQGGGGAINIASAGELALSATSGDITFNNNQVTNGSTSTRNAINIIDTAKVTSIRAATGQSIYFYDPITNPGTAASTDTLNLNLADANSEIEYGGAIVFSGEKLSPTEKAIAANVTSTIRQPAVLARGDLVLRDGVTVTFKDLTQSPGSRILMDGGTTLSAKEANLSLNGLAVNLSSLDGTNKAALKTEAADKNISLSGTIALIDTEGSFYENHNLKSASTYPLLELTTAGANGTITLGALSTLTLQEPETHYGYQGNWQLSWANATSSKIGSINWTRTGYIPSPERKSNLPLNSLWGNFIDIRSINQLIETKSSGEPFERELWLSGIANFFYRDSMPTRHGFRHISGGYALGITATTPAEDQLTFAFCQLFARDRNHITGKNHGDTYGASLYFHHTEGLFDIANFLWGKATRAPWVLSEISQIIPLSFDAKFSYLHTDNHMKTYYTDNSIIKGSWRNDAFCADLGASLPFVISVPYLLKEVEPFVKVQYIYAHQQDFYERYAEGRAFNKSELINVEIPIGVTFERDSKSEKGTYDLTLMYILDAYRRNPKCQTSLIASDANWMAYGTNLARQGFSVRAANHFQVNPHMEIFGQFAFEVRSSSRNYNTNLGSKFCF", "text": "SUBCELLULAR LOCATION: Secreted, cell wall. Cell outer membrane; Peripheral membrane protein; Extracellular side. SIMILARITY: Belongs to the PMP outer membrane protein family."}
{"protein": "MLPQTALLLLMSLNLVHGVFYTERYQTPTGIKGPPSNTKTQFFIPYAIKGKGVSLRGEQGIPGPPGPAGPRGHPGPSGPPGKPGTGSPGPQGQPGLPGPPGPSATGKPGLPGLPGKQGERGLNGPKGDIGPAGLPGPRGPPGPPGIPGPAGISVPGKPGPQGPTGEPGPRGFPGEKGTSGVPGLNGQKGEMGHCTPCRPGERGLPGPQGPTGPPGPPGVGKRGENGLPGQPGLKGDQGVPGERGAAGPSGPQGPPGEQGPEGIGKPGAPGIPGQPGIPGMKGQPGAPGTAGLPGAPGFGKPGLPGLKGQRGPVGLPGSPGAKGEQGPAGHPGEAGLPGPSGNMGPQGPKGIPGNPGLPGPKGEMGPVGPAGNPGAKGERGSSGLDGKPGYPGEPGLNGPKGNPGLPGPKGDPGIAGSPGLPGPVGPAGAKGVPGHNGEAGPRGVPGIPGTRGPIGPPGIPGFPGSKGDVGTPGPPGPAGIAVKGLNGPTGPPGPPGPRGNAGEPGLPGPPGPPGPPGQVALPEDFVKAGQRPFVSANQGVTGMPVSAFTVILSKAYPAIGTPIPFDKILYNKQQHYDPRTGIFTCKIPGIYYFSYHIHVKGTHAWVGLYKNGTPVMYTYDEYIKGYLDQASGSAVIDLTENDQVWLQLPNAGSNGLYSPEYVHSSFSGFLVAPM", "text": "FUNCTION: Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix."}
{"protein": "MGAYKYMQELWRKKQSDVMRFLLRVRCWQYRQLSALHRAPRATRPDKARRLGYKAKQGYVIYRVRVRRGGRKRPVPKGATYGKPVHHGVNQLKFARSLQSIAEERAGRHCGGLRVLNSYWVGEDSTYKFFEVILIDTFHKAIRRNPDMQWITKAVHKHREMRGLTSAGKKSRGLGKGHKFHLTIGGSRRAAWRRRNTLQLHRYR", "text": "FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL15 family."}
{"protein": "MPVIAGGILAALLLLIVVVLCLYFKIHNALKAAKEPEAVAVKNHNPDKVWWAKNSQAKTIATESCPALQCCEGYRMCASFDSLPPCCCDINEGL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FAM24 family."}
{"protein": "MRVIRPVEHADIAALMQLAGKTGGGLTSLLANEATLAARIERALKTWSGELPKGEQGYVFVLEDSETGEVGGICAIEVAVGLNDPWYNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPEWRKEGNGYLLSKSRFMFMAAFRDKFNEKVVAEMRGVIDEHGYSPFWQSLGKRFFSMDFSRADFLCGTGQKAFIAELMPKHPIYTHFLSEEAQAVIGEVHPQTAPARVVLEKEGFRYRHYIDIFDGGPTLECDIDRVRAIRKSRLVEVAEGQPALGDYPACLVANENYHHFRAALVRADPQTSRLVLTAAQLDALKCRAGDHVRLVRLCAEEKTV", "text": "FUNCTION: Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. SIMILARITY: Belongs to the arginine N-succinyltransferase family."}
{"protein": "MAAGPRTSALLAFALLCLPWTREVGAFPAMPLSSLFANAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKDEAQQRSDVELLRFSLLLIQSWLGPVQFLSRVFTNSLVFGTSDRVYEKLKDLEEGIQALMRELEDGSPRAGQILKQTYDKFDTNLRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFVESSCAF", "text": "FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
{"protein": "MVSQAKQPSNATFKNREKPQEVRKANIIAARAVADAIRTSLGPKGMDKMIKTSRGDIIISNDGHTILKQMAILHPVAKMLVEVSGAQDVEAGDGTTSVVIMTGALLGAAEKLLNKGIHPTIIAESFQRAAERSVEILLNMSTKISLDDKEALVRAASTSLSSKIVSQHSSFLAPLAVDCVLSIASHDSTNVDLNDIRLIKKVGGTIDDTEMVNGVVLTQNAVKTAGGPTRIEKARIGLIQFQISPPKPDTENNIVVNDYRQMDKILKEERAYLLNICKKIKKAKCNVLLIQKSILRDAVNDLALHFLSKLGIMVVRDIERDEVEFLSKSLGCKPISDVELFTEDRLGSADVVEEVESDGSNIVTITGVKTTNKNPTVSVVIRGANNMVLDETERSLHDALCVIRCLVKERALIAGGGAPEIEVSYRLMKEARTMEGVEAFVWQEYAEALEVIPTTLAENAGLNSLNVVTELRLRHENGESNSGISVRRSGTSNTYEDHILQPVLVSTSAIRLASECVKSILRIDDITFSR", "text": "FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCP-1 chaperonin family."}
{"protein": "MAEKPEVLDAVLKETVDLENIPIEEVFENLRCTREGLTATAAQERLSIFGYNKLEEKKESKFLKFLGFMWNPLSWVMEAAAIMAIALANGGGKPPDWQDFVGIITLLIINSTISFIEENNAGNAAAALMARLAPKAKVLRDGKWDEEDASVLVPGDIISIKLGDIIPADARLLEGDPLKIDQSALTGESLPVTKGPGDGVYSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCICSIAVGMIIEIIVMYPIQHRKYRPGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLAQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLTVDKALIEVFAKGIDADTVVLMAARASRIENQDAIDTAIVGMLADPKEARAGIREIHFLPFNPTDKRTALTYLDGEGKMHRVSKGAPEQILNLAHNKSDIERRVHTVIDKFAERGLRSLGVAYQEVPEGRKESAGGPWQFIALLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSSALLGQTKDESIAALPIDELIEKADGFAGVFPEHKYEIVKRLQARKHICGMTGDGVNDAPALKKADIGIAVDDATDAARSASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVLGFMLLALIWKFDFPPFMVLIIAILNDGTIMTISKDRVKPSPLPDSWKLAEIFTTGVVLGGYLAMMTVIFFWAAYKTNFFPRIFGVSTLEKTATDDFRKLASAIYLQVSTISQALIFVTRSRSWSFVERPGLLLVFAFFVAQLVATLIAVYANWSFAAIEGIGWGWAGVIWLYNIVTYIPLDLIKFLIRYALSGKAWDLVLEQRIAFTRKKDFGKELRELQWAHAQRTLHGLQVPDPKIFSETTNFNELNQLAEEAKRRAEIARLRELHTLKGHVESVVKLKGLDIETIQQSYTV", "text": "FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily."}
{"protein": "DVSFSLSGGGTASYEK", "text": "SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily."}
{"protein": "MAQMLLHGTLHATIFEAASLSNPHRASGSAPKFIRKFVEGIEDTVGVGKGATKVYSTIDLEKARVGRTRMITNEPINPRWYESFHIYCAHMASNVIFTVKIDNPIGATNIGRAYLPVQELLNGEEIDRWLDICDNNREPVGESKIHVKLQYFDVSKDRNWARGVRSTKYPGVPYTFFSQRQGCKVTLYQDAHVPDNFIPKIPLADGKNYEPHRCWEDIFDAISNAQHLIYITGWSVYTEITLVRDSNRPKPGGDVTLGELLKKKASEGVRVLMLVWDDRTSVGLLKRDGLMATHDEETENYFHGSDVNCVLCPRNPDDSGSIVQDLSISTMFTHHQKIVVVDHELPNQGSQQRRIVSFVGGLDLCDGRYDTQYHSLFRTLDSTHHDDFHQPNFATASIKKGGPREPWHDIHSRLEGPIAWDVLYNFEQRWRKQGGKDLLLQLRDLSDTIIPPSPVMFPEDRETWNVQLFRSIDGGAAFGFPDTPEEAAKAGLVSGKDQIIDRSIQDAYIHAIRRAKNFIYIENQYFLGSSYAWKPEGIKPEDIGALHLIPKELALKVVSKIEAGERFTVYVVVPMWPEGVPESGSVQAILDWQRRTMEMMYTDITEALQAKGIEANPKDYLTFFCLGNREVKQAGEYQPEEQPEADTDYSRAQEARRFMIYVHTKMMIVDDEYIIIGSANINQRSMDGARDSEIAMGGYQPYHLATRQPARGQIHGFRMALWYEHLGMLDDVFQRPESLECVQKVNRIAEKYWDMYSSDDLQQDLPGHLLSYPIGVASDGVVTELPGMEYFPDTRARVLGAKSDYMPPILTS", "text": "FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes. SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily."}
{"protein": "MIIDRVEVETINSFSKLELFKEIYGLIWILPIFALLLGITIEVLVIVWLEREISASIQQRIGPEYAGPLGLLQAIADGTKLLLKEDILPSRGDIPLFSIGPSIAVISILLSFLVIPLGYRFVLADLSIGVFLWIAISSIAPIGLLMAGYSSNNKYSFLGGLRAAAQSISYEIPLTFCVLAISLLSNSLSTVDIVEAQSKYGFFGWNLWRQPIGFLVFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKYGLFYLVSYLNLLVSSLFVTVLYLGGWNFSIPYISFFGFFQMNKIIGILEMVIGIFITLTKAYLFLFISITIRWTLPRMRMDQLLNLGWKFLLPISLGNLLLTTSFQLVSL", "text": "FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
{"protein": "MALVSIAPLASKSCLHKSLSSSAHELKTICRTIPTLGMSRRGKSATPSMSMSLTTTVSDDGVQRRMGDFHSNLWNDDFIQSLSTSYGEPSYREQAERLIGEVKKMFNSMSSEDGELINPHNDLIQRVWMVDSVERLGIERHFKNEIKSALDYVYSYWSEKGIGCGRESVVADLNSTALGLRTLRLHGYAVSADVLNLFKDQNGQFACSPSQTEEEIRSVLSLYRASLIAFPGEKVMEEAEIFSAKYLEEALQKISVSSLSQEIRDVLEYGWHTYLPRMEARNHIDVFGQDTQNSKSCINTEKLLELAKLEFNIFHSLQKRELEYLVRWWKDSGSPQMTFGRHRHVEYYTLASCIAFEPQHSGFRLGFAKTCHIITILDDMYDTFGTVDELELFTAAMKRWNPSAADCLPEYMKGMYMIVYDTVNEICQEAEKAQGRNTLDYARQAWDEYLDSYMQEAKWIVTGYLPTFAEYYENGKVSSGHRTAALQPILTMDIPFPPHILKEVDFPSKLNDLACAILRLRGDTRCYKADRARGEEASSISCYMKDNPGVTEEDALDHINAMISDVIRGLNWELLNPNSSVPISSKKHVFDISRAFHYEYKYRDGYSVANIETKSLVKRTVIDPVTL", "text": "FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens (PubMed:21385377). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (1S,5S)-beta-pinene (PubMed:21385377). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily."}
{"protein": "MKTLYSLRRFYHVETLFNGTLALAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGIGAFLLVLKALYFGGVYDTWAPGGGDVRKIANLTLSPSLIFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICILGGIWHILTKPFAWARRAFVWSGEAYLSYSLGALSIFGFTACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLNRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLATSHFVLGFFFFIGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light- induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. SUBCELLULAR LOCATION: Plastid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily."}
{"protein": "MAALMESVVGRALKFSSTANFRSIRRGETPTLCIKSFSTIMSPPSKAIVYEEHGSPDSVTRLVNLPPVEVKENDVCVKMIAAPINPSDINRIEGVYPVRPPVPAVGGYEGVGEVYAVGSNVNGFSPGDWVIPSPPSSGTWQTYVVKEESVWHKIDKECPMEYAATITVNPLTALRMLEDFVNLNSGDSVVQNGATSIVGQCVIQLARLRGISTINLIRDRAGSDEAREQLKALGADEVFSESQLNVKNVKSLLGNLPEPALGFNCVGGNAASLVLKYLREGGTMVTYGGMSKKPITVSTTSFIFKDLALRGFWLQSWLSMGKVKECREMIDYLLGLARDGKLKYETELVPFEEFPVALDKALGKLGRQPKQVITF", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily."}
{"protein": "MSTCPFNDVFNSTDSSMINTFLKNVQVLLEAASYIESAERKDGKCEHGYASTFPSIQHSSYQRQRKFRNKKCNNNHYRSTHNELEKNRRAHLRLCLERLKTLIPLGPECSRHTTLGLLNKAKAHIKKLEEADRKSRYQLESLEREQRHLRRRLDLLRDGGGSLEAERIRTDSMGSTPCSERSDRSDSDQEEMEVDVESTEFSHGELDSVSTASTSDLDDHSSLQSTASDEGYSSCSIKLAFSS", "text": "FUNCTION: Transcriptional repressor. MXI1 binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. MXI1 thus antagonizes MYC transcriptional activity by competing for MAX. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSEEVVESSSQEASQVIPQEQEDWADDVVTTMPAQEVTEWPEIKLFGRWACDDISISDISLQDYIAVKEKFARYLPHSAGRYAAKRFRKAQCPIVERLTSGLMMKGRSNGKKLLACRIVKHAFEIIHLLTSENPLQVTVNAIVNSGPREDSTRIGRAGTVRRQAVDVSPLRRVNQAIWLICTGAREAAFRNIKTVAECLADELINAAKGSSNSYAIKKKDELERVAKSNR", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS7 family."}
{"protein": "MISGDTILFALMVVTCVNWARYFTALRTLIYIMREAHPLLYQQVDGGGFFTTHGNMTKQVRLFSYIKSKEYHHHHDEVFTSKCDRVRQLFILSSALLGVTLLSSFIV", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the universal stress protein B family."}
{"protein": "MQRSRGFRSKSRRKMTKVVREGRSNPITNKLQKFEEGDLVHITINPSIQKGQPHPRFHGKTGKITDKKGKAYIVSLTDGNKAKELIIRPDHLKLQTSQ", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family."}
{"protein": "MSLVSISEGVRAGLVLKRHVVCFTGTSNDQGLKSISDLLSHMDNPAVPSPQSCSIDSLPDTETQNGISCYLVPYSGTAEIDYELQNRFALWLHKSTVPVILVLQDNPLMIPYLRHQFWFACGEDMGQWQDSVVAESIVDSVYMHHSIRRYILDLIVHLRMHRLSKPSQGGGAHSRSLSDMTLLCKWIALTSGSSFITPDMVQTACERYFPWHLQLIESSKEDPSVMYGSQEELVDELINRFDTFAIKMAQEYKNPLFKQLCIVQSVMKDIIPAT", "text": "FUNCTION: May be involved in telomere capping. SIMILARITY: Belongs to the MTC2 family."}
{"protein": "MDLMSFKEREISKKDCVELFEDTENFFDILKLADSIRKDIVGDTVTFVKNTNIETTNVCTMGCKFCAFSVSKNSPEAFKLDADEIAKKAVIAKKSGLTEVTIHGGIHPDVDTHFQVETINKVNSATSKLGGIYTHAYSPQEILNGAENAGLSIKEALKMLNEAGLRTIPGTAAEILDDEVRSDICPLKMSTKKWIDIMKTAHKTGIKTTSTIIYGHVEEYKHIVDHLSILKELQEETGGITEFIPMSFLHENTPLYKSGRVTDGASGLYELKLYAIARILFKESIKNIQAPRVKIGTKLSQLILKSGANDLGGTLVEDKVSKAAGSIYEDASVDLMKNAITSIGRIPKERTTLYEIIE", "text": "FUNCTION: Catalyzes the radical-mediated synthesis of 5-amino-5-(4- hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D- ribitylamino)uracil and L-tyrosine. SIMILARITY: Belongs to the radical SAM superfamily. CofH family."}
{"protein": "MKMEQALNITSEIGKLQTVLVKRPGSELENITPEYLESLLFDDIPYLKMMQKEHDFFAKTMKDSNIEVLYLEKLAAEALREANNKESFLTKMIKESNQMDESALYVRDYLMSFDEEEMIRKLMSGLKKSEIPERKKKHLNEMMDEQYPFFLDPLPNLYFTRDPAAVIGNGVTINRMFQPARRRESMFIELILKHHPRFSNQEIPVWSGRGEPFSLEGGDELVLNEETVLVGVSERTDARAVERLAESLFSRSPKIKRVLAVEIPETRSFMHLDTVFTMVNFAQFTIHPAIQNQQGELNIYILEKSENGLEITPRRDFQRVIAEVLDEPEIDFIPCGGEDVIVSAREQWNDGANTLAIAPGEVITYDRNQVSNDLLRSAGIKVHEVISSELSRGRGGPRCMTMPLVRENLK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the arginine deiminase family."}
{"protein": "MNKIESRHQLILSLIMEKKIHTQQELQELLEVNGVSVTQSTLSRDIKMLNLVKVNEDDSSHYVINPIAPTRWEKRLRLYMEDALVMLKPIQHQVVLKTLPGLANSFGSILDAMEIPQIVATVCGDDVCLIICEDVEGAQACFEHLKQFTPPFFFSKL", "text": "FUNCTION: In the presence of arginine, coactivates the transcription of the arcABDC operon, with other regulatory proteins such as ArcR and CcpA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ArgR family."}
{"protein": "MSADEPSPEDEKYLESLRDLLKISQEFDASNAKQNDEPEKTAVEVESAETRTDESEKSIDIPREQQLLPSERVEPLKSMVEPEYVKKVIRQMDTMTAEQLKQALMKIKVSTGGNKKTLRKRVAQYYRKENALLNRKMEPNADKTARFFDYLIAIDFECTCVEIIYDYPHEIIELPAVLIDVREMKIISEFRTYVRPVRNPKLSEFCMQFTKIAQETVDAAPYFREALQRLYTWMRKFNLGQKNSRFAFVTDGPHDMWKFMQFQCLLSNIRMPHMFRSFINIKKTFKEKFNGLIKGNGKSGIENMLERLDLSFVGNKHSGLDDATNIAAIAIQMMKLKIELRINQKCSYKENQRSAARKDEERELEDAANVDLTSVDISRRDFQLWMRRLPLKLSSVTRREFINEEYLDCDSCDDLTDDKNDEAAFQEKMAIREYLENKQTEDFAKIAAERGIFKIGEIKSYQTARPIIEDDDVDVESEEEDYGTEFEMLEVVERMPPVSSTLHTEVDLDAVWERDGGSDSERENLSNAPSLHEFPSSSTSSPHATSEHVTSSSPLHIDDDVDRVLNAPPKNSLASSSNRSSF", "text": "FUNCTION: RNA exonuclease that acts as a negative regulator of RNA interference (RNAi) (PubMed:14961122). Probably acts by degrading the 3'-overhangs of short interfering RNAs (siRNAs) (PubMed:14961122). Component of the ERI/DICER complex which is involved in processing amplified double-stranded RNA (dsRNA) intermediates during small-RNA- mediated gene-silencing or RNA interference (RNAi) (Probable). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MLLLQSILITKIMVIQLILFFEYALASGFEDKNILKEGKMMFDTLLKQFLEIDKVISLLYKDFVDNYIDFKNLEIVKIKKENEIENKLKSLLKSENIDYALVVAPEDEDILYNLTKIIESYPVKNLGCSSEAIKIAGNKYLTYLAIKDAVKTPKTFPPKKYVVKKIDSCGGKFNLFDENFLIQEFIDGENLSVSLIVGKKIHPLSLNRQYIDKRGFVGGEVNINHKLKDKIFNEAIKAVKCINGLNGYVGVDVIVNNDGIYIIEINPRITTTIYGLKTNPSLAELLIKNANNEELKFKVKGEKFTIDK", "text": "FUNCTION: Catalyzes the formation of an amide bond between tyramine and the gamma carboxy group of L-glutamate. The enzyme also accepts phenylethylamine in vitro."}
{"protein": "MQSHIGQWTSTAKGHLSRDENGDEKTDYSRWRLVDRQGRQTWRYLESDEENEKSPQTVPEKYFLGLDTGLPDLPKAETPLQAAQDGVSFLSQLQLSSGQWASECTGPMFILPCVIIAWYVTNTPIPPAYAIEIRRYLFARQRVEDGGWGWHVEARSSAIGTALNYVVLRLLGASKDDHRLIQARKLLHSYGGATYAPGIAKFWLCVLGVMKWECVNPFLPEFWLLPDSDPTAPSKWYIHTRTNFTSLSYIWSKQWSFAGDEVTKQLQTELYPEPYSAIDFAAHRTSLAEVDNNYPKWWLVNLMNWLTVAVYIPYMRKKATVESAEQRVWELIQAEDKNSEFIGLSPISKAANMIACYIHDGKDSESVRSHGETIFQYFWMNGEGMACNLSDGIQVWDTSLAVQAIAAAGGAGNPRFQSTVIKAHEFLEDHQLLDDVQDQEMCCRGHRKGGWPFSTKYQGYMISECTGEGLRSILQLQKTFQLDLKKRIPADRLHNAVDCLLNLQNDTGGFGVYEKRQGSLKLAWLEMGEFSGKTMVTYDYVECTTAVVSALASFSEFYPDYRKEEVQTARTRGLEFIKSSQKPYGGWHGAWGVCFTYAGMFALESLALAGETYSNSEPSRKGCTFLVSKQRDDGGWGESYLSFQKEEYIEHEDAQVVQTAWACLGLMHAEYPDKTPVKRGLKLIMSRQQSKGHWLQEQYEGGVGDGVISYSNYKLYWPVRALAEYVRRFGNEEM", "text": "FUNCTION: Terpene cyclase/mutase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids nectripenoids A and B, as well as cochliquninone D and isocochliquninone E (PubMed:29797385). The pathway probably begins with the HR-PKS ntnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS ntnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of nectripenoids (Probable). The FAD-dependent monooxygenase ntnJ then performs an oxidative decarboxylation at C11 of the ntnH/ntnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation (Probable). The membrane-bound polyprenyl transferase ntnF then introduces a farnesyl group before the FAD- dependent monooxygenase ntnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by ntnA (Probable). The terpene cyclase/mutase ntnI then initiates the sequential tricyclic ring formation through protonation of the terminal epoxide and catalyzes the regioselective and stereoselective 6/6/6-tricyclic ring formation (Probable). The cytochrome P450 monooxygenase ntnM may then hydroxylate C1' (Probable). SIMILARITY: Belongs to the terpene cyclase/mutase family."}
{"protein": "MAKIIVVTSGKGGVGKTTTSASIATGLALRGYKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIQGEATLNQALIKDKNCENLFILPASQTRDKDALTREGVEKVMQELSGKKMGFEYIICDSPAGIEQGALMALYFADEAIVTTNPEVSSVRDSDRILGILQSKSHKAEQGGSVKEHLLITRYSPERVAKGEMLSVQDICDILHIPLLGVIPESQNVLQASNSGEPVIHQDSVAASEAYKDVIARLLGENREMRFLEAEKKSFFKRLFGG", "text": "FUNCTION: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ParA family. MinD subfamily."}
{"protein": "MKGKKTLKRTIAAEESNGTSDVKKTKALPIVTHPSHGTVGGQVLTLGQGDVGQLGLGEDIMERKKPALVTLTEDIVQAAAGGMHTVCLGASGSIYTFGCNDEGALGRDTSEEGSEMQPGKVELAEKVVQVSAGDSHTAALTEDGRVFVFGSFRDNNGVIGLLEPMKKSMVPVQVQINTPVIKIASGNDHLVLLTVDGDLYTSGCGEQGQLGRVPERFTNRGGRKGLERLLVPQCIHLKAKGSGRVHFQDVFCGAYFTFAVSQEGHVYGFGLSNYHQLGTKNTQACYAPQNLTSFKNSTKSWIGFSGGQHHTVCVDSEGKAYSLGRAEYGRLGLGENAEEQSEPTPIPDLPKINSVASGASVSYAVSTDGCVFAWGMGTNLQLGTGEEEDVWSPEQMTGKHLEDREVLSVSSGGQHTVLLVRKRS", "text": "FUNCTION: Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP, and thereby plays an important role in RAN-mediated functions in nuclear import and mitosis. Contributes to the generation of high levels of chromosome-associated, GTP-bound RAN, which is important for mitotic spindle assembly and normal progress through mitosis. Via its role in maintaining high levels of GTP-bound RAN in the nucleus, contributes to the release of cargo proteins from importins after nuclear import (By similarity). Involved in the regulation of onset of chromosome condensation in the S phase (PubMed:2361953). Binds both to the nucleosomes and double-stranded DNA (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Cytoplasm Note=Predominantly nuclear in interphase cells. Binds to mitotic chromosomes."}
{"protein": "MNASSWSLRNLPWFRATLAQWRYALRNTIAMCLALTVAYYLNLDEPYWAMTSAAVVSFPTVGGVISKSLGRIAGSLLGAIAALLLAGHTLNEPWFFLLSMSAWLGFCTWACAHFTNNVAYAFQLAGYTAAIIAFPMVNITEASQLWDIAQARVCEVIVGILCGGMMMMILPSSSDATALLTALKNMHARLLEHASLLWQPETTDAIRAAHEGVIGQILTMNLLRIQAFWSHYRFRQQNARLNALLHQQLRMTSVISSLRRMLLNWPSPPGATREILEQLLTALASSQTDVYTVARIIAPLRPTNVADYRHVAFWQRLRYFCRLYLQSSQELHRLQSGVDDHTRLPRTSGLARHTDNAEAMWSGLRTFCTLMMIGAWSIASQWDAGANALTLAAISCVLYSAVAAPFKSLSLLMRTLVLLSLFSFVVKFGLMVQISDLWQFLLFLFPLLATMQLLKLQMPKFAALWGQLIVFMGSFIAVTNPPVYDFADFLNDNLAKIVGVALAWLAFAILRPGSDARKSRRHIRALRRDFVDQLSRHPTLSESEFESLTYHHVSQLSNSQDALARRWLLRWGVVLLNCSHVVWQLRDWESRSDPLSRVRDNCISLLRGVMSERGVQQKSLAATLEELQRICDSLARHHQPAARELAAIVWRLYCSLSQLEQAPPQGTLAS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the aromatic acid exporter ArAE (TC 2.A.85) family."}
{"protein": "MLHRINPVRFSMQSCQRYFSKLVSPLEQHKSNTFTNRVRIPIEAGQPLHETRPFLIKSGELTPGISALEYYERRIRLAETLPPKSCVILAGNDIQFASGAVFYPFQQENDLFYLSGWNEPNSVMILEKPTDSLSDTIFHMLVPPKDAFAEKWEGFRSGVYGVQEIFNADESASINDLSKYLPKIINRNDFIYFDMLSTSNPSSSNFKHIKSLLDGSGNSNRSLNSIANKTIKPISKRIAEFRKIKSPQELRIMRRAGQISGRSFNQAFAKRFRNERTLDSFLHYKFISGGCDKDAYIPVVATGSNSLCIHYTRNDDVMFDDEMVLVDAAGSLGGYCADISRTWPNSGKFTDAQRDLYEAVLNVQRDCIKLCKASNNYSLHDIHEKSITLMKQELKNLGIDKVSGWNVEKLYPHYIGHNLGLDVHDVPKVSRYEPLKVGQVITIEPGLYIPNEESFPSYFRNVGIRIEDDIAIGEDTYTNLTVEAVKEIDDLENVMQNGLSTKFEEDQVAPL", "text": "FUNCTION: Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome. SUBCELLULAR LOCATION: Nucleus Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Note=Has the same dual localization (mitochondrion and nucleus) as one of its substrate, NFS1. SIMILARITY: Belongs to the peptidase M24B family."}
{"protein": "MLLPDLHPYTILLSIFLVLVAKQLVATIGKSTIQEFVWLVYLKVSSNQSIKTYNSKQHELHETNRQKRAISAQDEYAKWTKLNRQADKLSAELQKLNQEIQQQKSSIDKASNALILVLTTLPIWIARVFYRKTHLFYIRQGIFPKYVEWVLALPFLPNGAVGLTIWMFAVNSVVSNFSFLVSFPFAKRVSKPVRDTKVE", "text": "FUNCTION: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET2, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex cooperates with the HDEL receptor ERD2 to mediate the ATP- dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the WRB/GET1 family."}
{"protein": "MLSRSIGKAAGGLVLGLSVAAAAHAAPLFEPVTVISRASANSEPALGKLLATPSTATVQEVRVDAAATAQPQLEFELLGKRVQAVRSKVEALPDGGSIWYGQFRSPSDRLTAATSSGQDDPGNSLILVRSGDTITGSIRKDGKLYRLRPLGNRHVLVEVDESRMPADHPADYNQLPKIPMADNDHIGIAQASSGTPATIRVLVVATNAAVTAYGGNMQSLVQLAVAESNQGYVNSNVGLTLQLAGYETTNYSESGNFTTDLSRFRGTSDGYMDSIHTSRNTTAADVGVLLINNSAYCGLASGIGSTASTAFAAVYWDCATGYYSFAHEIGHLQSARHDIATDSSTSPYAYGHGYRYEPATGTGWRTIMAYNCTRSCPRLNYWSNPNISYNGIPMGNASTADNQRVLVNTKATIAAFR", "text": "FUNCTION: Metalloprotease, specifically cleaves on the N-terminal side of aspartyl, glutamyl and cysteic acid residues. SIMILARITY: Belongs to the peptidase M72 family."}
{"protein": "MVKAVAVLRGDSKVSGTVTFEQADENSNTTVSWNITGNDPNAERGFHIHQFGDNTNGCTSAGPHFNPFGKTHGAPEDEVRHVGDLGNFKTDAEGNSKGSKTDKLIKLIGAESVLGRTLVVHAGTDDLGRGDSEESKKTGNAGARPACGVIGIAA", "text": "FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family."}
{"protein": "MRNENVAGLLAERASEAGWTDQPAYYAPDVVTHGQIHDGAARLGAVLANRGLCRGDRVLLCMPDSPELVQVLLACLARGILAFLANPELHRDDHAFQERDTQAALVITSGPLCDRFAPSTVVDAADLFSEAARVGPADYEILGGDAAAYATYTSGTTGPPKAAIHRHCDVFAFVEAMCRNALRLTPADIGLSSARMYFAYGLGNSVWFPLATGSSAVVNPLPVGAEVAATLSARFEPSVLYGVPNFFARVVDACSADSFRSVRCVVSAGEALEVGLAERLTEFFGGIPILDGVGSTEVGQTFVSNTVDEWRPGSLGKVLPPYQIRVVAPDGAAAGPGVEGDLWVRGPSIAESYWNWPEPLLTDEGWLDTRDRVCIDDDGWVTYACRADDTEIVGAVNINPREIERLIVEEDAVAEVAVVGVKEATGASTLQAFLVPASAEGIDGSVMRDIHRRLLTRLSAFKVPHRFAVVERLPRTANGKLLRSALRGQTPAKPIWELASAEHRSGAPGQLDDQSASALVSGSREVSLKERLAALQQERHRLVLDAVCGETAKMLGEPDPRSVNRDLAFSELGFDSQMTVELCHRLAAATGLRVPETVGWDYGSISGLAQYLEAELSGADRRVTPQSARSGARALPLIEAQLNKVEELTAAIADGEKPRVAERLRALLGTITEGQEHWGQRIAAASTPDEIFQLIDSEFGES", "text": "FUNCTION: Catalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in a CoA-independent manner by attack of the phosphopantetheine thiol of FadD22. This intermediate primes the biosynthesis of the phenolphthiocerol (PPOL) by presenting the pHBA starter unit for elongation by Pks15/1. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MTSNPLDESMESLTVVPPAASPASRILVVEDEAVIRDMVALVLQQEGFTVDVAADGRTALNYFRSDSPEAGSVTENPDLVVLDLMLPAVNGLDFCRLLRRQGVTVPILMLSAKDTETDRVVGLEIGADDYLTKPFGTRELVARCRALLRRSQNQPAETPAVLRYEGLKLFPEECRVLLDDRELTLSPKEFRLLELFMRHPRRVWSRDQLLEKIWGIDFMGDSKTIDVHIRWLREKIEANPSNPSYLLTVRGFGYRLG", "text": "FUNCTION: Member of the two-component regulatory system SphR/SphS. Response regulator. Involved in inducible production of alkaline phosphatase in response to phosphate limitation as it is directly involved in the regulation of phoA transcription in response to phosphate limitation. Binds to two distinct sites upstream from the phoA promoter."}
{"protein": "MKKVITYGTFDLLHWGHIKLLERAKQLGDYLVVAISTDEFNLQKQKKAYHSYEHRKLILETIRYVDEVIPEKNWEQKKQDIIDHNIDVFVMGDDWEGKFDFLKDQCEVVYLPRTEGISTTKIKEEIAGL", "text": "FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to sn- glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit and the teichoic acid polymer by TagB and TagF. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidylyltransferase family."}
{"protein": "MFRTLTVVPLLALGLSLSACADLGQPTVRADLLDQTGKVTGTATFSPSPIGTRVSIEVSGLKAGPHGLHIHENPNCNPGPDAQGQTIPFGAAGGHFDPGASHNHDGPHARNDQGHGGDLPMITVGEDGKGRLNFDTNRLKMTGPTGVLGRSIVIHADADDYQTNPAGNSGGRERCGVFQAIN", "text": "FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family."}
{"protein": "MAARPLSRMLRRLLRSSARSCSSGAPVTQPCPGESARAASEEVSRRRQFLREHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFDGNKWNFKKMVSYKEMLDTVRQQWPELEKVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAGMFSISQMKNRPMILIELFLMFPNSPPANPSIFSWDPLHVQGLRPRMSFSSQVATLWKGCRVPQTPPLAQQRLGSGSFQRHYTSRADSDANSKCLSPGSWASAAPSGPQLTSEQLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRGDFHRA", "text": "FUNCTION: Isoform MOCS1A and isoform MOCS1B probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP). MOCS1A catalyzes the cyclization of GTP to (8S)- 3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate and MOCS1B catalyzes the subsequent conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'- triphosphate to cPMP. SIMILARITY: In the C-terminal section; belongs to the MoaC family. SIMILARITY: In the N-terminal section; belongs to the radical SAM superfamily. MoaA family."}
{"protein": "MEKYILSIDQGTTSSRAILFNQKGEIAGVAQREFKQYFPQSGWVEHDANEIWTSVLAVMTEVINENDVRADQIAGIGITNQRETTVVWDKHTGRPIYHAIVWQSRQTQSICSELKQQGYEQTFRDKTGLLLDPYFAGTKVKWILDNVEGAREKAENGDLLFGTIDTWLVWKLSGKAAHITDYSNASRTLMFNIHDLEWDDELLELLTVPKNMLPEVKASSEVYGKTIDYHFYGQEVPIAGVAGDQQAALFGQACFERGDVKNTYGTGGFMLMNTGDKAVKSESGLLTTIAYGIDGKVNYALEGSIFVSGSAIQWLRDGLRMINSAPQSESYATRVDSTEGVYVVPAFVGLGTPYWDSEARGAIFGLTRGTEKEHFIRATLESLCYQTRDVMEAMSKDSGIDVQSLRVDGGAVKNNFIMQFQADIVNTSVERPEIQETTALGAAFLAGLAVGFWESKDDIAKNWKLEEKFDPKMDEGEREKLYRGWKKAVEATQVFKTE", "text": "FUNCTION: Key enzsyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate (By similarity). FUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. SIMILARITY: Belongs to the FGGY kinase family."}
{"protein": "MPSFTYLTAALALTSSVVASPVEKRDAFEVKQVAHGLHRKNGPAQIAKTLRKYGKAVPAHIQAAADNNAVVQADANTGSDPAVPSDQYDSSYLSPVTVGTSTVHLDFDTGSADLWVFSDLQAKSSLSGHDYYKTDASKRKSGYTWKISYGDGSGASGQVYTDKVTVGQVTATAQAVEAATSVSAQFSQDVDTDGLLGLAMSSINTVKPQQQTTWFDTVKSQLAKPLFAVTLKYHAAGTYDFGYIDSAKYTGAITYVNADASQGFWGFTASGYSVGTGATVSSSISGILDTGTTLMYVPAATAKAYYAKVSGAKLDSTQGGYVFPCSATLPNFSITVAGVKQTVPGKYINYAPITDGSSTCFGGMQPDTDIGQSIFGDIFLKSKYIVHDMSNGTPRLGFAQQAGVSS", "text": "FUNCTION: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family."}
{"protein": "MEAAGSPAATETGKYIASTQRPDGTWRKQRRVKEGYVPQEEVPVYENKYVKFFKSKPELPPGLSPEATAPVTPSRPEGGEPGLSKTAKRNLKRKEKRRQQQEKGEAEALSRTLDKVSLEETAQLPSAPQGSRAAPTAASDQPDSAATTEKAKKIKNLKKKLRQVEELQQRIQAGEVSQPSKEQLEKLARRRALEEELEDLELGL", "text": "FUNCTION: Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon- exon junction on mRNAs and serves as a positional landmark for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as an EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions. May bind RNA; the relevance of RNA-binding remains unclear in vivo, RNA-binding was detected by PubMed:14968132, while PubMed:19410547 did not detect RNA- binding activity independently of the EJC. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Nucleus, nucleoplasm Note=Shuttles between the nucleus and the cytoplasm (PubMed:14968132). Nuclear export is mediated by XPO1/CRM1 (PubMed:14968132). SIMILARITY: Belongs to the pym family."}
{"protein": "MTVGDHLVARMRAAGISVVCGLPTSRLDSLLVRLSRDAGFQIVLARHEGGAGYLADGFARASGKSAAVFVAGPGATNVISAVANASVNQVPMLILTGEVAVGEFGLHSQQDTSDDGLGLGATFRRFCRCSVSIESIANARSKIDSAFRALASIPRGPVHIALPRDLVDERLPAHQLGTAAAGLGGLRTLAPCGPDVADEVIGRLDRSRAPMLVLGNGCRLDGIGEQIVAFCEKAGLPFATTPNGRGIVAETHPLSLGVLGIFGDGRADEYLFDTPCDLLIAVGVSFGGLVTRSFSPRWRGLKADVVHVDPDPSAVGRFVATSLGITTSGRAFVNALNCGRPPRFCRRVGVRPPAPAALPGTPQARGESIHPLELMHELDRELAPNATICADVGTCISWTFRGIPVRRPGRFFATVDFSPMGCGIAGAIGVALARPEEHVICIAGDGAFLMHGTEISTAVAHGIRVTWAVLNDGQMSASAGPVSGRMDPSPVARIGANDLAAMARALGAEGIRVDTRCELRAGVQKALAATGPCVLDIAIDPEINKPDIGLGR", "text": "FUNCTION: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. SIMILARITY: Belongs to the TPP enzyme family."}
{"protein": "MGLFRGFVFLLVLCLLHQSNTSFIKLNNNGFEDIVIVIDPSVPEDEKIIEQIEDMVTTASTYLFEATEKRFFFKNVSILIPENWKENPQYKRPKHENHKHADVIVAPPTLPGRDEPYTKQFTECGEKGEYIHFTPDLLLGKKQNEYGPPGKLFVHEWAHLRWGVFDEYNEDQPFYRAKSKKIEATRCSAGISGRNRVYKCQGGSCLSRACRIDSTTKLYGKDCQFFPDKVQTEKASIMFMQSIDSVVEFCNEKTHNQEAPSLQNIKCNFRSTWEVISNSEDFKNTIPMVTPPPPPVFSLLKISQRIVCLVLDKSGSMGGKDRLNRMNQAAKHFLLQTVENGSWVGMVHFDSTATIVNKLIQIKSSDERNTLMAGLPTYPLGGTSICSGIKYAFQVIGELHSQLDGSEVLLLTDGEDNTASSCIDEVKQSGAIVHFIALGRAADEAVIEMSKITGGSHFYVSDEAQNNGLIDAFGALTSGNTDLSQKSLQLESKGLTLNSNAWMNDTVIIDSTVGKDTFFLITWNSLPPSISLWDPSGTIMENFTVDATSKMAYLSIPGTAKVGTWAYNLQAKANPETLTITVTSRAANSSVPPITVNAKMNKDVNSFPSPMIVYAEILQGYVPVLGANVTAFIESQNGHTEVLELLDNGAGADSFKNDGVYSRYFTAYTENGRYSLKVRAHGGANTARLKLRPPLNRAAYIPGWVVNGEIEANPPRPEIDEDTQTTLEDFSRTASGGAFVVSQVPSLPLPDQYPPSQITDLDATVHEDKIILTWTAPGDNFDVGKVQRYIIRISASILDLRDSFDDALQVNTTDLSPKEANSKESFAFKPENISEENATHIFIAIKSIDKSNLTSKVSNIAQVTLFIPQANPDDIDPTPTPTPTPTPDKSHNSGVNISTLVLSVIGSVVIVNFILSTTI", "text": "FUNCTION: May be involved in mediating calcium-activated chloride conductance. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Apical cell membrane Secreted Note=The C-terminus 30 kDa form is anchored to the membrane. The N-terminus 110 kDa form is released from the membrane triggered by an unknown stimulus. SIMILARITY: Belongs to the CLCR family."}
{"protein": "MNSTNSTNSTTTATSTNTSTQQVVTSLVSNGTIFGVFVIAFLILRIKLKRIYEPKSSFNLINEEKKPEPLPQGVWQWLKPLLKKSDNFVIQQAGLDGYFFLRYLFIIAIYCAVSMSYIFPILLSINASNGNHESGLNQLAYQNVKHRGRYFAHVFCGWIFFWGFLYIIYRELYFYTSMKQAVLASPRYAKKLSSRTVLFQTVPKQYLSEEEFSKLFDGVKRVWIARGSGSIEAMVKARDNMAIQLEGAETKYLKAALKKIKKLNKKSPQLSVSDNIAEYVPDKKRPHHKINKVAKFFFGKKVDTISYIKEELPKLNQKVKALQEDHENSSPFNSVFVEFESQYQAQVAAQITTYHAPLFMTPVYIGIEPSDVVWFNLRMFWWERLGREVSAVSAIVALVILWAFPVAFVGMISNITSLTNEVKWLKFIYKLPKQLLGLLTSLAPTVALAVLMSFLPKFIRGMAITQGAPSKQNVEYFTQQAYFAFQVIQVFLVTTLSSAATSTVTEIVKEPTKAMDLLASNLPKASNFFMSYVILQGLSISSGALLQIVPLILFYVLGAFLDGTVRKKWNRFCGLSSMQWGTAFPVYTNLAVITFSYSIISPLILLFAAVAFFLLYIAYLYNLTYVYQESPDARGIYYPRALFQTIVGIYIGQICLLGLFAVGKGWGPIVLQVIGICVTVLIHLHLSAAFDHLSKVIPVDTMKPLDGVSDTPSFKNIYKGIESTKVKKNTFGANIDMDGIKELPEFPIKKYHKRSESVTEQQVENSIFSENTFEYQFNPANEANADGHAINAENLIEDVPLLADGDTMKIPPAPWWKRFLKPHIYYSYKAVKSRLPEIYGLVDPDERVNDFDISHAYDYPAVSAQCPELWIPRDPFGFSKLLISDVSGVVEMNDENATIDENLKFTLRDVPPPYNDVKDEANGEANGEFDTASKENNPFADPKYKEEESRSAV", "text": "FUNCTION: Acts as an osmosensitive calcium-permeable cation channel. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family."}
{"protein": "MAAILARKSLSALRSRQLVLAGHTIEGTNGYNRTLLGTRSFATKHSFSTDKDDEEREQLAKELSKDWNSVFERSINTLFLTEMVRGLMLTLKYFFEKKVTINYPFEKGPLSPRFRGEHALRRYATGEERCIACKLCEAICPAQAITIEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKLLENGDRWETEIAENLRSESLYR", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). May donate electrons to ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I 23 kDa subunit family."}
{"protein": "VVSCADITALAARQGLFTSDQDLYTDSRMGQLNVLTGTQGEIR", "text": "FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily."}
{"protein": "MKRYILATAIASLVAAPAMALAAGSNILSVHILDQQTGKPAPGVEVVLEQKKDNGWTQLNTGHTDQDGRIKALWPEKAAAPGDYRVIFKTGQYFESKKLDTFFPEIPVEFHISKTNEHYHVPLLLSQYGYSTYRGS", "text": "FUNCTION: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily."}
{"protein": "MSQILHPDAALVLFSGGQDSATCLAWALDRFARVETIGFDYGQRHLVELDSRAKLLDGLKTLKPEWVAKLGETHTLAIPTLAQVSDTALTRDVAIAMGADGLPNTFVPGRNLIFLTFAAALAYRRGIGAIIGGMCETDYSGYPDCRDATIKALGEAINLGMATQFELHTPLMWLDKAATWGLAQTLGGERLVDLIREHSHTCYLGERGARHDWGFGCGECPACQLRAKGWREFSAQRDARQG", "text": "FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). SIMILARITY: Belongs to the QueC family."}
{"protein": "MSFLKSFPPPGSADGLRLQQPDTEAVLNGKGLGTGTLYIAESRLSWLDGSGLGFSLEYPTISLHAVSRDPNAYPQEHLYVMVNARFGEESKEPFSDEDEDDNDDVEPISEFRFVPSDKSALEAMFTAMCECQALHPDPEDEDSDDYDGEEYDVEAHEQGQGDIPTFYTYEEGLSHLTAEGQATLERLEGMLSQSVSSQYNMAGVRTEDSVRTYEDGMEVETTPTVAGQFEDADVDH", "text": "FUNCTION: Involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins (By similarity). Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre- mRNAs (By similarity). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (By similarity). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (By similarity). Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Cytoplasm, cytoskeleton Note=A small fraction is also associated with the cytoskeleton. SIMILARITY: Belongs to the pICln (TC 1.A.47) family."}
{"protein": "MNVSLFVTCLADIFYPGVGKDTVEVLERHGCNVKFPENQICCGQPAFNSGYHEDTKKAAKHTIETFADADYVVLPSGSCAAMLLEYKELFADDPEWEKRAEELASKTYELTQFLVRVLKVEDIGAVCHKKATYHTSCHMSRLLRETEAPFSLLEQVKGLELAPLANKESCCGFGGTFSVKMPAISEQMVEEKVGHIEATGADLLIGADCGCLMNIGGRIERNGKTIEVKHIAQVLNSKE", "text": "FUNCTION: Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. SIMILARITY: Belongs to the LutA/YkgE family."}
{"protein": "MAAEEAEVVSPLIVDTAPDTSGTAAASLAAAVSAAAAAARTGSQAQVSKAALAAKLMSLSGVFAVHKPKGPTSAELLNRLKEKLLAEAGLPSPEWNKRQKQTLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRYIATGELGKATDTLDSTGKVTEEKPYDKITQEDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKRGETVEARPARPVTVHSISLLKYQPPFFTLDVECGGGFYIRSLVSDIGKELSSCATVLELTRTKQGPFTLAQHALPEDRWTINDIAQSLKRCTSLLPEELTFKKSKSEPSSDQALSCGYITLRETKREDDTVKTL", "text": "FUNCTION: Pseudouridine synthase that catalyzes pseudouridylation of mRNAs and tRNAs. Mediates pseudouridylation of mRNAs with the consensus sequence 5'-GUUCNANNC-3', harboring a stem-loop structure. Constitutes the major pseudouridine synthase acting on mRNAs. Also catalyzes pseudouridylation of some tRNAs, including synthesis of pseudouridine(55) from uracil-55, in the psi GC loop of a subset of tRNAs. Promotes the processing of pri-let-7 microRNAs (pri-miRNAs) independently of its RNA pseudouridylate synthase activity. Acts by binding to the stem-loop structure on pri-let-7, preventing LIN28- binding (LIN28A and/or LIN28B), thereby enhancing the interaction between pri-let-7 and the microprocessor DGCR8, which mediates miRNA maturation. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Note=Catalyzes pseudouridylation of mRNAs in the nucleus. SIMILARITY: Belongs to the pseudouridine synthase TruB family."}
{"protein": "MSDTEKPIKSEEPVDEGVDRVDEEENVEEPAEDVGEAAEEASEAPEEAPAEAATTTEAAPADDDEDDSDLSDLDEDEIKNAAIEDDDDDYNKLSAHRRKVQSSGKKTLKKRATKDSRAADDDEDEIDHSHIDLDPSMARRREIEARIDAAMKPASQRRKKLGEDDIEMMQDERISNLREKMRNAAIADAESNREGQPATHKLQLLPEVKDVLQKHHLADSILDNNLLEAVRIWLEPLPDASLPSYSIQEELFDALVRLPIKSIHLRESGLGKVVTFYRKSKQPQLRIKRIADKLVADWTRPIMGRSDNYREKVVSTRSFDPSTQEIALAVAAKRAQTLKDGTLAEKQAERRRRAHIPSAQPANYRVAPKSEIIPQNRGGSTNDMTFKRLKGKLGVTKTGKKKSGVSIEGRGLNG", "text": "FUNCTION: Transcription factor involved in RNA polymerase II transcription regulation. May function in both SPT15/TBP post- recruitment and recruitment steps of transcription (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the IWS1 family."}
{"protein": "IIGDEINGAITTADNIAGKIGII", "text": "FUNCTION: May act as an antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Frog skin active peptide (FSAP) family. Septenin subfamily."}
{"protein": "MSAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRATRREATPPGTPGAPPPPATAPGPGGATAAPHLLAASILADLRGGPVVATAASTAGGTSPVSSSSAASSPSSGRAPGAAKSHRCPFHGCAKAYYKSSHLKSHLRTHTGERPFACDWPGCDKKFARSDELARHHRTHTGEKRFPCPLCTKRFTRSDHLTKHARRHPGFRPELLRRPGARSVSPSDSLPCSLAGSPTPSPVPSPAPAGL", "text": "FUNCTION: Transcription factor that binds GC and GT boxes in the D1A, D2 and D3 dopamine receptor promoters and displaces Sp1 and Sp3 from these sequences. It modulates dopaminergic transmission in the brain by repressing or activating transcription from several different promoters depending on cellular context. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family."}
{"protein": "MPLASPRQLFLLAFLACVAIMGGALYLEHVVGLEACPLCVVQRIFFILIGLTCLAGAIQGPGLRGRRIYSVLVFLLALGGGATAARQVWLQTVPLDQLPACLPSLDYMMQALPFQEVIRLVLHGTADCAQVSWTLFTLSIPEWSLLAFVAYLGFSIVQFLRRA", "text": "FUNCTION: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein. FUNCTION: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family. SIMILARITY: Belongs to the DsbB family."}
{"protein": "MASVTRAVFGELPSGGGTVEKFQLQSDLLRVDIISWGCTITALEVKDRQGRASDVVLGFAELEGYLQKQPYFGAVIGRVANRIAKGTFKVDGKEYHLAINKEPNSLHGGVRGFDKVLWTPRVLSNGVQFSRISPDGEEGYPGELKVWVTYTLDGGELIVNYRAQASQATPVNLTNHSYFNLAGQASPNINDHEVTIEADTYLPVDETLIPTGEVAPVQGTAFDLRKPVELGKHLQDFHLNGFDHNFCLKGSKEKHFCARVHHAASGRVLEVYTTQPGVQFYTGNFLDGTLKGKNGAVYPKHSGFCLETQNWPDAVNQPRFPPVLLRPGEEYDHTTWFKFSVA", "text": "FUNCTION: Mutarotase that catalyzes the interconversion of beta-D- galactose and alpha-D-galactose during galactose metabolism (PubMed:12753898). Beta-D-galactose is metabolized in the liver into glucose 1-phosphate, the primary metabolic fuel, by the action of four enzymes that constitute the Leloir pathway: GALM, GALK1 (galactokinase), GALT (galactose-1-phosphate uridylyltransferase) and GALE (UDP-galactose-4'-epimerase) (PubMed:30451973). Involved in the maintenance of the equilibrium between the beta- and alpha-anomers of galactose, therefore ensuring a sufficient supply of the alpha-anomer for GALK1 (PubMed:12753898). Also active on D-glucose although shows a preference for galactose over glucose (PubMed:12753898). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldose epimerase family."}
{"protein": "MRIINAEGLILGRLASRVAKMLLEGEEVVIVNAEKAVITGNREVIFSKYKQRTGLRTLTNPRRGPFYPKRSDEIVRRTIRGMLPWKTDRGRKAFKRLKVYVGIPKEFKDKQLETIVEAHVSRLSRPKYVTVGEVAKFLGGKF", "text": "FUNCTION: This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. SIMILARITY: Belongs to the universal ribosomal protein uL13 family."}
{"protein": "MGLFDKLKSLVSDDKKDTGTIEIIAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMVAPVDGTIGKIFETNHAFSIESDSGVELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDTVIEFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (PubMed:3129430, PubMed:17158705). The enzyme II complex composed of PtsG and Crr is involved in glucose transport (PubMed:2657735). The non-phosphorylated EIII-Glc is an inhibitor for uptake of certain sugars such as maltose, melibiose, lactose, and glycerol. Phosphorylated EIII-Glc, however, may be an activator for adenylate cyclase. It is an important regulatory protein for cell metabolism (PubMed:789369). FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MGKGNEDSDLHCSSIQCSTDQPPFQQISFTEKGSDEKKPFKEKGKTAFSHSSEKHIQRQGSEPNPNKENSEETKLKAGNSTAGSEPESSSYRENCRKRKMSSKDSCQDTAGNCPEKECSLSLNKKSRSSTAVHNSEIQETCDAHHRGHSRACTGHSKRHRSRALGVQTPSIRKSLVTSVRAMSEAVYQDLAQVWAQQIHSPLTCEQLTLLTRLRGPLCAQVQTLYSMATQAAYVFPAESWLVPATLPGPGESALDREAHPFPGQEITETVSGSDEAKL", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the FRG2 family."}
{"protein": "MKFVLLFGVLLVTLFSYSSAEMLDDFDQADEDELLSLIEKEEARKDCIPKHHECTNNKHGCCRGHLFKYKCQCTTVVTQSGEETERCFCGTPPRHKAAELVVGFGKKIFG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 03 subfamily."}
{"protein": "MTHAAIDQALADAYRRFTDANPASQRQFEAQARYMPGANSRSVLFYAPFPLTIARGEGAALWDADGHRYADFIAEYTAGVYGHSAPEIRDAVIEAMQGGINLTGHNLLEGRLARLICERFPQIEQLRFTNSGTEANLMALTAALHFTGRRKIVVFSGGYHGGVLGFGARPSPTTVPFDFLVLPYNDAQTARAQIERHGPEIAVVLVEPMQGASGCIPGQPDFLQALRESATQVGALLVFDEVMTSRLAPHGLANKLGIRSDLTTLGKYIGGGMSFGAFGGRADVMALFDPRTGPLAHSGTFNNNVMTMAAGYAGLTKLFTPEAAGALAERGEALRARLNALCANEGVAMQFTGIGSLMNAHFVQGDVRSSEDLAAVDGRLRQLLFFHLLNEDIYSSPRGFVVLSLPLTDADIDRYVAAIGSFIGGHGALLPRAN", "text": "FUNCTION: Aminotransferase that acts exclusively on beta-amino acids and exhibits a broad substrate range in vitro, accepting meta-, para- and, to a lesser extent, ortho-substituted beta-phenylalanine derivatives as amino donors, and 2-oxoglutarate or pyruvate as amino acceptors. Is highly enantioselective toward (S)-beta-phenylalanine (is not active with (R)-beta-phenylalanine) and derivatives with different substituents on the phenyl ring, allowing the kinetic resolution of various racemic beta-amino acids to yield (R)-beta-amino acids with >95% enantiomeric excess (ee). Highly prefers aromatic beta-amino acids over aliphatic beta-amino acids; cannot use beta-alanine or beta- glutamate as substrate. Is likely involved in the beta-phenylalanine degradation pathway that allows V.paradoxus strain CBF3 to use beta- phenylalanine as a sole nitrogen source. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MSEARRDSTSSLQRKKPPWLKLDIPSAAPATAEEPSFLQPLRRQVFLRSVSMPAETAHISSPHYELRRPVLQRQTSITQTIRRGAADWFGVSKESDSTQKWQRKSIRHCSQRYGKLKPQVLRELDLPSQDNVSLTSTETPPPLYVGPCQLGMQKIIDPLARGRAFRVADDTAEGLSAPHTPVTPGAASLCSFSSSRSGFHRLPRRRKRESVAKMSFRAAAALMKGRSVRDGTLRRAQRRSFTPASFLEEDTTDFPDELDTSFFAREGILHEELSTYPDEVFESPSEAALKDWEKAPEQADLTGGALDRSELERSHLMLPLERGWRKQKEGAAAQQPKVRLRQEVVSTAGPRRGQRIAVPVRKLFAREKRPYGLGMVGRLTNRTYRKRIDSFVKRQIEDMDDHRPFFTYWLTFVHSLVTILAVCIYGIAPVGFSQHETVDSVLRNRGVYENVKYVQQENFWIGPSSEALIHLGAKFSPCMRQDPQVHSFIRAAREREKHSACCVRNDRSGCVQTSEEECSSTLAVWVKWPVHPSAPELAGHKRQFGSVCHQDPRVCDEPSSEDPHEWPEDITRWPICTKNSAGNHTNHPHMDCVITGRPCCIGTKGRCEITSREYCDFMRGYFHEEATLCSQVHCMDDVCGLLPFLNPEVPDQFYRLWLSLFLHAGILHCLVSICFQMTVLRDLEKLAGWHRIAIIYLLSGVTGNLASAIFLPYRAEVGPAGSQFGILACLFVELFQSWQILARPWRAFFKLLAVVLFLFTFGLLPWIDNFAHISGFISGLFLSFAFLPYISFGKFDLYRKRCQIIVFQVVFLGLLAGLVVLFYVYPVRCEWCEFLTCIPFTDKFCEKYELDAQLH", "text": "FUNCTION: Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Note=Predominantly localized in the endoplasmic reticulum membrane. SIMILARITY: Belongs to the peptidase S54 family."}
{"protein": "MAAAAASTKIVAVVVAVLLAILEMPSCAVARRHHHDHHDKPGHHDGGFPAVMTVNGFEKGEDGGGPAACDGHYHSDGELIVALSTEWFAGGRRCHRRIRITPSEHGRRGGGGGRRAVEATVVDECDSRRGCKDDVVDSSPAVWRALGLDTDSGEVRVTWSDV", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the kiwellin family."}