lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
Subcellular Localization:
Cytoplasm.
Sequence:
MLCEKCNEKNVCMMRPSNKEKLCKECFIESFEEDVHDTILKKRMFEDNDKICIAVSGGKDSSVLAHVLVNLKKKYNYNWELFLLAIDEGIKGYRDDSLKVVYKLEKLYNLPLKILKFENLFSYTMDDVVKFIGKKNNCTVCGVFRRQSFEKGALLFNATKLVTGHNADDLAETILMNMCRGDIDKLAKNINDLSNADHMNKKYNCTGDSQNGIKNLENVQNGPEQVRQKKYKNYENVDNNDNNDNNDNYDNNDNYDDIILNDIMSERLNEKCSCINNNLNNDGGKKNKEMQKCEQDYEEKYNNDNNNNNDNNNDNNNDNNNDNNNNNNNDNNNNNNNNNSNNNNNNNSFFLPRLKPLMWCYEKEIVLYAFHLKLDYFSTECTYSPNSFRGNLRCFIKDIELINAQFILNIIHSAEFFYFNSINQKTLNVCIKCGAYTSNKICKACLIIDGLNNYTDNSFLYSNKKKAKKKISIHFDNKKVEG
The following text describes a protein:
Function:
Ribosome biogenesis factor that coordinates hyperactive transcription and ribogenesis. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I. Essential for stem cell pluripotency and embryonic development. In the nucleoplasm, recruited by promoter-associated/nascent transcripts and transcription to active promoters where it facilitates releases of elongation factor P-TEFb and paused RNA polymerase II to allow transcription elongation and maintain high-level expression of its targets genes (By similarity).
Subcellular Localization:
Nucleus, nucleolus. Nucleus, nucleolus fibrillar center. Nucleus, nucleoplasm.
Domain:
N-terminal domain is required for nucleoplasm location and C-terminal domain for nucleolus location.
Sequence:
MAAGGGGSCDPLAPAGVPCAFSPHSQAYFALASTDGHLRVWETANNRLHQEYVPSAHLSGTCTCLAWAPARLQAKESPQRKKRKSEAVGMSNQTDLLALGTAVGSILLYSTVKGELHSKLISGGHDNRVNCIQWHQDSGCLYSCSDDKHIVEWNVQTCKVKCKWKGDNSSVSSLCISPDGKMLLSAGRTIKLWVLETKEVYRHFTGHATPVSSLMFTTIRPPNESQPFDGITGLYFLSGAVHDRLLNVWQVRSENKEKSAVMSFTVTDEPVYIDLTLSENKEEPVKLAVVCRDGQVHLFEHILNGYCKKPLTSNCTIQIATPGKGKKSTPKPIPILAAGFCSDKMSLLLVYGSWFQPTIERVALNSREPHMCLVRDISNCWAPKVETAITKVRTPVMNSEAKVLVPGIPGHHAAIKPAPPQTEQVESKRKSGGNEVSIEERLGAMDIDTHKKGKEDLQTNSFPVLLTQGLESNDFEMLNKVLQTRNVNLIKKTVLRMPLHTIIPLLQELTKRLQGHPNSAVLMVQWLKCVLTVHASYLSTLPDLVPQLGTLYQLMESRVKTFQKLSHLHGKLILLITQVTASEKTKGATSPGQKAKLVYEEESSEEESDDEIADKDSEDNWDEDEEESESEKDEDVEEEDEDAEGKDEENGEDRDTASEKELNGDSDLDPENESEEE
The following text describes a protein:
Function:
Structural component of the gap junctions.
Subcellular Localization:
Cell junction, gap junction. Cell membrane; Multi-pass membrane protein.
Sequence:
MFYMLVAPLHRAVKINRIVLDNQIFRLHYKATSLLLLMFSILVTSAQYFGDPIDCINHDSVPANVIRTFCWIHSTFNIPAAFNATVGVDGVPHPGIQKYTPDEHRRYYGYYQWVCMVLFLQAGCFYVPRYLWKCYEQGLIRSLVQDLDCPIKESTDVCQKTEAIARYMRNHLDMHHKYFFVYVTSEVLNFVNVVGQILLTDAFLGNMFTTFGTDVLKHHEIDPDQRNDPMVWAFPRMTKCSFHLFGSSGDVMKHDALCLLAQNIINEKIYIFLWFWWVILAFLTGVELGYRVITIALPKVRELILRYRARMADRRMLESVSKRVSTSDWFVLYMLCKNMNPVHYRAFINELAKSMEDDEYGKRLLGSDTSNTSTV
The following text describes a protein:
Function:
Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MMSISLLFLFYPSVLLFFGFGCRYASSFVCPGICRCSSNTIRCNNITEKSVPMSERGPRLVLKHLTMSTIASHTFDGLRRVQHIEIGQSVALETIETLAFNNLLDLNEIFIKNTRSLVHIARRTFNNLPKLRYLSISNTGITVFPDMTSIHSLEPWNQNFVLDICDNLYLLSIPVNAFVGMTTEYTAMNLFNNGIREIQDYAFNGTKINKLVLKNNRNLRVIHREAFKGAVGPRILDVSSTAIETLPSHGLNSVVELVARTAYGLKRLPPFRGLGNLQKAHLTYNSHCCALLTWDTHRDSPINAAQHNGSRPTYCDDSQSEKFPAGMVDSSDTSLLVEIHGTNKDVEDESYGGVDFQYPELGLYCQTRPTLQCTPEADAFNPCEDIAGFSFLRVAIWFINILAIIGNLTVLLIFFTSRCKLTVPRFLMCHLAFADFCIGVYLLMIAAVDLHTRGHYSEHAIDWQTGAGCSAAGFLSVFGGELSVYTLSTITLERWHTITHALQLEKRLGLAQAAGIMAGGWLICLGMAMLPLVGVSSYSRVSMCLPMDVKTPLAQAFILLLLFFNVGAFLVVCVCYVLIYLAVRNPQFPSRSADAKIAKRMAVLIFTDLLCMAPISFFAISAAFKVPLITVTNSKILLVLFFPINSCANPFLYAIFTKAFRKDVYLLLSNMGCCENKANMYRMKAYCSENLVKSSSGNKGTLICTTQMMDPLPLQSQQLKDDGDLGTI
The following text describes a protein:
Function:
Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MSFNFGRRLYTSIWDTAHPLLVRELRNSRMTFFFESPSTGNWFRRFLFNTHARKISSLPPRTRHITKRFASGSFFMLGISPSPCAVEAGTSCAISPEKFVSQSHLLDRKFVCASLYTWKRGLHTTKDDDGLKSEQSNELLTNDSNTSPSPSRETADSDTRSGTMKSQEEHIEGFTSRHIMNRLPHMSHLHRPTKEELLAAANGFWSRLKVRFKWFSIRSVRPFNFDEITALFSWVLLGHVVWIVLGTTTFFSLLIIAINTVLAQETLAGWVGNYLTKSSGVKVVFESAIVPKWKDGVITFKNVFVSRRPGQGTGHVSKGSSKTAAAVAAAAALSGSSSPEPFSDQQSIPDEEDTNYTQFDLSIETVNVTLSFTKWINGKGLLRDVEVKGIRGVVDRRSVHWSDDHLDPKSYRHEHHPGDFEIDSFKMSDVLVTVYQPGNFRPFSVSIFSCDLPQLRKQWLLYDFMSANMMTGSFDNSLFTIHPRQSHSFASAEMDNKIEADGKPSTWKKHSRIRIDGLNIDHLNRGVQGPFSWIYEGTVDIVADIMFPAENDESLAQVMAGLYDRLEATVISNQYQEPDSRRQPGMDGTASSDDKRFLVTDLRLQLNNVRAVVPLFNRDLSYINNALIRPIVAYINSRRTFIPIHCRLVKRLADFDGSWTTFDSGLMDDLSAAVYDAFARDVVDEQARKRRFKKVGFWSLQLAAQAIFMGMAGNIA
The following text describes a protein:
Function:
Can convert androstan-3-alpha,17-beta-diol (3-alpha-diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione.
Subcellular Localization:
Endoplasmic reticulum. Lipid droplet. Note=Redistributed from the endoplasmic reticulum to lipids droplets in the cell upon induction of lipids droplet formation.
Sequence:
MKYLLDLILLLPLLIVFCIESFIKRLIPKKKKSVAGEIVLITGAGHGIGRLTAYEFAKLNTKLVLWDINKNGIEETAAKCRKLGAQVHPFVVDCSQREEIYSAVRKVKEEVGDVSILVNNAGVVYTADLFATQDPQIEKTFEVNVLAHFWTTKAFLPAMMKNNHGHVVTVASAAGHTVVPFLLAYCSSKFAAVGFHRALTDELAALGCTGVRTSCLCPNFINTGFIKNPSTNLGPTLEPEEVVEHLMHGILTNQKMIFVPGSIALLTVLERVFPERFLDVLKRRINVKFDAVVGYKDK
The following text describes a protein:
Function:
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Sequence:
MQEMVKDFFGRPLQDLRISVIDRCNFRCTYCMPAEIFGSDYAFLKDEFLLTFDEIERLAKLFVNIGVRKIRITGGEPLLRKDLTKLIARLVKIDGLIDIGLTTNAVHLTKQAKALKEAGLHRVNVSLDAIDDDIFKNINGRNINTKPVIKGIIAAKEAGLEVKVNMVVKKGMNDHQVLPMAAYFKEQGITLRFIEFMDVGSTNGWNFDQVVTKRELIEMIHKMDPLEPAEAHYFGEVAKRYRYVGTNVEVGFITSVSESFCVSCTRARISADGKFYTCLFATEGLDVRELLRGNLSDEELLSVIQDVWMNRKDRYSDERTEESAKNRPKIEMSYIGG
The following text describes a protein:
Function:
Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex.
Subcellular Localization:
Cytoplasm. Nucleus. Nucleus membrane. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus.
Sequence:
MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE
The following text describes a protein:
Function:
Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate.
Miscellaneous:
MISCELLANEOUS: [Isoform 1]: Main product.
Subcellular Localization:
Cytoplasm.
Sequence:
MEHVTMAVTSSSPGPAPLSLLSNNDDFIAPFNINTKFPSAIVPPRTSSNQPISVAIPSNRISSAGLAATQQAQTRKRKASVAQISLPSMLPTSFSPYTMAPQPPQPPPNPDRFATEDFFSPSRRTWSEEKEKVLTGPYDYLNGHPGKDIRSQMVKAFDAWLDVPSESLEVITKVISMLHTASLLVDDVEDNSVLRRGFPVAHSIFGIPQTINTSNYVYFYALQELQKLKNPKAVSIFSEELLNLHRGQGMDLFWRDTLTCPTEDDYLEMVSNKTGGLFRLGIKLMQAESRSPVDCVPLVNIIGLIFQIADDYHNLWNREYTANKGMCEDLTEGKFSFPVIHSIRSNPSNMQLLNILKQKTGDEEVKRYAVAYMESTGSFEYTRKVIKVLVDRARQMTEDIDDGRGKSGGIHKILDRIMLHQEENVAQKNGKKE
The following text describes a protein:
Function:
Participates in the inductive signaling pathway downstream of let-60 Ras and the RAF/MAP kinase cascade to regulate specification and differentiation of many cell types. Positively regulates the fate of vulval precursor cells. Required for induction of the P12 and excretory duct cell fates. In males, it is also required for proper formation of spicules. Does not function in the signaling pathway that promotes exit from pachytene (By similarity).
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MHIAVDNLTISVPKIDKPTKAALDYVELLRESFSAKKRQKFSKASLAIRPSDFPDLSNQQLCDILVRVAYNGSHIDEDFRKHVLDLVEDQSLTWNQVLLSVIRTQSDQLYMKSQLCELITEMIRFVQIKSFHDPKHADSLISVILPTFVFLTKLILELLSDEDEMETIQIEYETKFPPYHKPLQALNTLIHDNLCGPLLAMYRSSEEVTRQLVLCSEAFSKLERPDESSVGLLDLILEKHQDNCKPTKYEYTPDGLAAYDLKNPSVRILVPIFACFRCHETSKQMAETVQIFVDIMRVSGDDVVFDLLHAAILLKCEESNNLLHLSKQHRLDFRWQSTTFFYKKLPQIIEHLVSFGKVTAEDVQKGMERALNDLTMLFDVADISWQNASFLTVLNALEPLIGSEAANPLRHRRREYMRKTASLTALADSDEKLIENTDIDRLLNAVKQVMNLQFGQNEEFYQEFIRKVNGDDCEDFDAVMSILISEGRLLEVGKAFAMKSKLAQYPSELSLDERIKKFDETFLLLTRIIVKFPGLSIGLLVNGGPGEISIADSIFYRWSMWYVKRVPRKDKSEEKSEEELEAMRIQAKVLIEEINKEVGIEEEIEEEEEDIEPEVVKEMKESGTEKEKEEEEEDGNKETKNETANDEEMPGDEQKTEEKMDTSETPAEPPIQQQSTPEDPPKVEEPAERINQEKPEEKPKEPLEPTWNEMNCALPRISRKKARRYLGLLKQGNPFWSTDNNSLNIGAILAALPSMGKLLIEEHNEEKHRVDRKSAEEHMANIIHALESMPCLFVCLVQWVDCAPASPARTLLAKTMKNALEKRVSSSSASIADDTNLPKWRFILSTCNEMIHELTDRVPVFPDITCTAFSAARRLCPFVTRDEIPDSTKLKHAWYYMCQQSWTSPHALRLLEHANIHSEYNTWIHLYITKIVGGGCGEIMKDQVDMIFGMLMMDDLNVIIRMHEIMMDFWLSEEAGNLQLDGRFDPLSMTAVIRLMANVMLISEWTLDRLINDGPPLVEFDFTSAMTPEPEDPLRREKWVFLLRQMLDRTVNRLFKILRQGVLCTVVNTIVRLIKAIAGSADCKAKRLLIKRIPPEIVFQLAYIEPQCADYALMNAYCDPKNEEHTRTKIRFLCALRRSHIL
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Involved in UBTF-activated transcription, presumably at a step following PIC formation.
Miscellaneous:
MISCELLANEOUS: It is in an antisense orientation to and overlaps the gene of the DNA repair enzyme ERCC1. This gene overlap is conserved in human, suggesting an important biological function.
Subcellular Localization:
Nucleus, nucleolus. Note=Accumulates in the nucleolus of exponentially growing cells.
Sequence:
MAGTQACSATRFSCPPHFTEMSPDSEPSRFSLEALTGPDTELWLIQAPADFAPQCLNGRRVPLSGSKTVKGKLDGKKHRYRVFTSSPQAREATLLASSSEAGGRLTCAPAPSGSLRIMEGPQEYLLSRVPLQLIPTSLPPQIPAGLRPRFSAFGGSPPVTGPGSASALRSPTSGKRKSTRKGTDASSDTQEAVNRHGAMEVKTALGNLGVSVKKRKRYFMQEEMEAKTMEPVAELPVPSATSSKKRKKSKGTETSQVEHTEPVAQTEPPEGTFLFPTKKRKRQKEADGTEEVDGIVADSQPQVIVEAQEETILLSPTKKRRKEKRQNLGMEAEMGPPGVLMVTEHSEHGLQAEVALVSPKKTKKKKGKRVGETEAALPDDFEPQGALAPSKKKERGARL
The following text describes a protein:
Function:
Galactose-specific lectin that displays calcium-dependent activity. Binds to the surface of hemocytes and enhances hemocyte encapsulation and melanization. This is likely by interacting with carbohydrates on the surface of the hemocytes. Also displays agglutination activity against the Gram-negative bacterium E.coli.
Subcellular Localization:
Secreted.
Sequence:
MMVKLLLLFLVCWSALPLESSPLGNRYNLEIGEKQYYISLAKTNWFEASNHCRQNGGFLLNLESREELELLSPHLHPAYSYWLSINDLGERGVYVSEATGLEAPFLNWSAGEPDNSSGYDRCVELWLSTTSFQMNDLPCYSSVAFICQLN
The following text describes a protein:
Function:
Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Requires SYCP1 in order to be incorporated into the central element. May have a role in the synaptonemal complex assembly, stabilization and recombination.
Subcellular Localization:
Nucleus. Chromosome. Note=Associates with chromatin. In prophase I stage of meiosis, localizes in the transverse central elements of the central region between lateral elements of the synaptonemal complexes. Found only where the chromosome cores are synapsed. Colocalizes with SYCE1 in the central elements.
Sequence:
MERHGVAAPPVELKDQEPPAIVESGEHRQSENHEETPGSVAPSASCQLPGPFSSLDSSIETLKKKAQELIENINESRQKDHALMTNFRDSLKMKVSDLTEKLEERMYQVYSHHSKIIQERLQEFTQKMAKINHLEMELKQVCQTVETVYKDLCVQSEVPTCEEQNYKDGEC
The following text describes a protein:
Function:
Protein O-fucosyltransferase that specifically catalyzes O-fucosylation of serine or threonine residues in EMI domains of target proteins, such as MMRN1, MMRN2 and EMID1. Attaches fucose through an O-glycosidic linkage. O-fucosylation of EMI domain-containing proteins may be required for facilitating protein folding and secretion. May also show alpha-(1,3)-fucosyltransferase activity toward the innermost N-acetyl glucosamine (GlcNAc) residue in biantennary N-glycan acceptors. However, this was tested with a library of synthetic substrates and this activity is unsure in vivo. May be involved in biosynthesis of Lewis X-carrying biantennary N-glycans that regulate neuron stem cell self-renewal during brain development.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MVRVRRKKLWASCLCITVASFLLVSFQVVSELGKFERLKIENSNLKDGKQKPEEATKHLHPFLKKGLYQSKRRGSKADSYPIMLWWSPLTGETGRLGHCGADTCFFTINRSYQHHHLTKAFLFYGTDFSIDSLPLPRKVHHDWALFHEESPKNNYKLFHEPVITLFNHTATFSRHSHLPLTTQYLEGVDALKSLRYMVPLHTKNSLRQRLAPLVYVQSDCDPPSDRDSYVRELMTHIQVDSYGECLRNRDLPPQLKNPASMDDDGFYRILAQYKFILAFENAVCDDYITEKFWRPLKLGVVPVYFGSPSITDWLPSNKSAVLVTGFSHPRELASFIKQLDNDDREYEAYLEWKLKGEVSNHRLLTALKERKWGVQDITQDNYIDAFECMVCNKVWENIRLREKGFLPKRWNAEVTHLSCPKPQAFAFPVPALQWTSLREMWIPSFEQSKKEARALRQLVEKNQNFTAQEFWALVFKD
The following text describes a protein:
Function:
Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
Subcellular Localization:
Cytoplasm.
Sequence:
MATLILTNTPTKAHNYANVAYCSFNDSPNFLVSGSYVLIGDATVNEIPRGHIGLNDVQRRNAKAFNGDSVSVSRFLPPPENFNLALLSVELELANKDGKDELVDAILFSKHIREYFLSHVMTTGQRVLLKYNEIGYIFTVNQVAVQGKEKTNRIERGMISADTHIIYEAPLSSGIQIFNQREPTNISKDKESGLVDLERCRLNGFINCGSRHDHTYRRIRLLTEKVKVSEGSPLVTCLLEGPRGSGKTAMAATIGIESDFPYVKIISDETMIELSEPAKCAQIVKIFEDAYKSPLSIIILDDVERLLEYVVTGPRFSDLIYRTFLVLLKRLPPKGKKLLVIGTTSGVKFLDSVGIRDAFALTYNVPTLKKEDAKKVLQRLNVFSSQDLDSAAEALNDMPLKKLYLAIEMAADGEKGEEKINILHFRDILRDMVQN
The following text describes a protein:
Function:
NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers.
Sequence:
MMTLRQVEVIRAVMVTGTIGGAAKLLNVSAPGISRLVKYTERSLGIRFFQRQNGRYFPTPEAENIFEQINGVYKKVDDLSEIISKIGRGGLSELRIGSVPSISQVMVPRAIERVRRRYPDLGIDINILKLEEAIDYLLLGRGECVAMSYRLEHSGLDFLPLASGELYCIVPPGHELAGRKQVSAAEITRYPLIGIDPNDPYGRIMAGIFSRNRLDYNITIRARFGTTVCALVKAGLGIAVIDQFTVAHGGYPGIELLKITEPTRFDTYIAVKRGAPLSLHVEYFIESLRAEMRAVEPSRGNGRAAPARGRKK
The following text describes a protein:
Function:
Involved in the biosynthesis of pipecolate (Pip), a metabolite that orchestrates defense amplification, positive regulation of salicylic acid (SA) biosynthesis, and priming to guarantee effective local resistance induction and the establishment of systemic acquired resistance (SAR). Converts delta-(1)-piperideine-2-carboxylate (P2C) to Pip. Mediates reduction of P2C and biosynthesis of Pip in systemic tissue and contributes to SAR establishment. Does not possess ornithine cyclodeaminase activity in vitro.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MAALPVFIPAESFPSILSHETLINHFRTNLPKHSSTITSPVRQNYTVSSPSSLLLMPSWSSSSSLPYMGVKLVTYFPHNSSQNLPGIHGSYTLFSSTTGQTLATMDGTVLTLYRTSSVSGLGSKILARDDSQVLIMVGSGALAPHLIKSHLAAKPSLRRVIIWNRTPQRAQELAETLSKDPQHKEISFDSHDSLDQIIPLGDIISCATNSTVPLVKGEFLKPGTHLDLVGSFSHEMKECDDNAIQRGSVFVDNDTAMIEAGELAGAFERGVIKREDICGNLVELIKGDKEGRKSSTDITVFKSVGSGTVDLLTAQLVHETYLSRC
The following text describes a protein:
Function:
May be involved in the transport of sterols.
Sequence:
MNSFCGSQHRTKPVPARISDQPTSTSSSSDHHHPMAPPATSPVFRFRSLSSCAHNRPSPLSSSFTATTVKRSTSVRFTRQHTATRNEVMLKDIVGSGISGILYKWVNYGRGWRPRWFVLHDGVLSYYNIHGPDKLVLNHEVEAEAMVIGEESLRRINSHRHCPSRNHKPVSEIHLMVCSVRENRSDERRFSVCTGTKKRLHLRAESKEDRATWVKAMMAVKDLFPRLSNAEAMSPVASVLVSTERLRDRLLMEGVSETAIRESEEIMKSEFSQLQKHIVALKQQQSLLMDTLRHLEAEKVDLENTLIEDRRQSKDETDPYLSTQKKYSEGSGDDSSEEHYRNNHSEDEDDAFYDTCDDILSTGSDHPRSCHDSECEEIIPNGDEKSPTGSVGFNHPHIKRRKNLPDPVEKESSVSLWSIIKDNIGKDLTKVCLPVYFNEPLSSLQKCFEDLEYSYLLDQAYEWGKMGDNLKRVLHVAAFAVSGYASTNGRSCKPFNPLLGETYEAEYQDKGIRFISEKVSHHPMIVACHCEGKGWKFWGDSNLKSKFWGRSIQLDPVGLLTVEFDDGEVFHWSKVTTSIYNLILGKVYCVHYGTMRVEGNRDYLCKIKFKEQSIIDRNPHQIHGVVEDKKGRTVATLFGTWDESLHYVIGGNSGKGKGSSYVSSKPHVLWKRSPTPEYQTRYNLTQFAITLNEITPGLKEKLPPTDSRLRPDQRCLENGQHEMANSEKLRLEQSQRQARKVQEKGWKPRWFAKEKGSNSYRYVGGYWEAREKGNWESCPDIFGQVSTDTDFNPTS
The following text describes a protein:
Function:
Exopeptidase that catalyzes the removal of dipeptide units (NH2-P2-P1-) from the free amino termini of oligopeptides and small proteins. Peptide digestion is sequential and substrate recognition is non-specific, with the exception that Pro is not suitable as a P1 residue. Removes many residues of bioactive oligopeptides such as angiotensin I and neuromedin N and also cleaves oxidized insulin B chain. Able to hydrolyze an X-Pro bond, an imido bond. No endopeptidase activity. May play a physiological role in feeding.
Domain:
The chymotrypsin fold (25-276 and 574-722) is the catalytic domain and the alpha-helical domain (277-573) is the regulatory domain necessary for exopeptidase activity.
Sequence:
MRPNLLAAAIAVPLSLLAAQIAQAGEGMWVPQQLPEIAGPLKKAGLKLSPQQISDLTGDPMGAVVALGGCTASFVSPNGLVVTNHHCAYGAIQLNSTAENNLIKNGFNAPTTADEVSAGPNARVFVLDEITDVTKDAKAAIAAAGDDALARTKALEAFEKKLIADCEAEAGFRCRLYSFSGGNTYRLFKNLEIKDVRLAYAPPGSVGKFGGDIDNWMWPRHTGDFAFYRAYVGKDGKPAAFSKDNVPYQPKHWLKFADQPLGAGDFVMVAGYPGSTNRYALAAEFDNTAQWTYPTIARHYKNQIAMVEAAGKQNADIQVKYAATMAGWNNTSKNYDGQLEGFKRIDAAGQKLREEAAVLGWLKGQGAKGQPALDAHAKLLDLLEQSKATRDRDLTLALFNNTAMLGSATQLYRLSIEREKPNAERESGYQERDLPAIEGGLKQLERRYVAAMDRQLQEYWLNEYIKLPADQRVAAVDAWLGGNDAAAVKRALDRLAGTKLGSTEERLKWFAADRKAFEASNDPAIQYAVAVMPTLLKLEQERKTRAGENLAARPVYLQALADYKKSQGEFVYPDANLSLRITFGNVMGYAPKDGMEYTPFTTLEGVVAKETGQDPFDSPKALLDAVAAKRYGGLEDKRIGSVPVNYLSDLDITGGNSGSPVLDAHGKLVGLAFDGNWESVSSNWVFDPKMTRMIAVDGRYLRWIMQEVYPAPQLLKEMNVGK
The following text describes a protein:
Function:
Catalyzes the pyridoxal 5'-phosphate-dependent transamination of both 3-hydroxykynurenine and L-kynurenine to xanthurenic acid and kynurenic acid, respectively, preferentially using the alpha-ketoacid pyruvate, glyoxylate or oxaloacetate as the amino group acceptor. The affinity and catalytic efficiency for 3-hydroxykynurenine is higher than for L-kynurenine. Involved in the detoxification of cytotoxic metabolite 3-hydroxykynurenine generated by the hydroxylation of L-kynurenine, an intermediate in the tryptophan catabolism pathway. Also catalyzes, although with a lesser efficiency, the transamination of alanine with glyoxylate as an amino group acceptor. May play a role in the detoxification of glyoxylate, a toxic plant metabolite from the diet (Probable).
Subcellular Localization:
Peroxisome.
Sequence:
MKFTPPPSSLRGPLVIPDKIMMGPGPSNCSKRVLAALNNTCLSNFHDELFQVIDEVKDGLRYIFQTENRTTMCITGSAHTGMEALLCNLLEEGDIVLIANNGIWAERAINMATRYGADVRVLGGPADKPFSMTDFKKAIEQHRPKCLFVVHGDSSSGLLQPLEGLGKICHDYDCLLLVDAVASLCGVPFYMDKWEIDGVYTGSQKVLGAPPGITPISISPKALEVIRSRKTPSKVFYWDLLILGNYWGCYDEQKRYHHTVPSNLIFALREAIAQIAEEGLEPVIRRRQECAEQMYRGLQAMGLEIFVKDPEYRLPTVTCIMIPKGVNWWKVSEYAMNNFSLEIQGGFGPTMGIAWRAGIMGESSTLQRVNFYLYAFKESLKATHPDYVFEKKNGQTNGTK
The following text describes a protein:
Function:
Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Required for marginal zone (MZ) B-cell development, is associated with early bone marrow B-cell development, MZ B-cell formation, MZ B-cell number and marginal metallophilic macrophages morphology (By similarity). Facilitates filopodia formation through the activation of CDC42.
Miscellaneous:
MISCELLANEOUS: 'Zizim' means 'spike' in Hebrew.
Domain:
The DOCKER domain is necessary for the GEF activity. The DOCKER domain mediates interaction with activated CDC42 in conjunction with residues 66-126.
Sequence:
MAEVRKFTKRLSKPGTAAELRQSVSEAVRGSVVLEKAKVVEPLDYENVIAQRKTQIYSDPLRDLLMFPMEDISISVIGRQRRTVQSTVPEDAEKRAQSLFVKECIKTYSTDWHVVNYKYEDFSGDFRMLPCKSLRPEKIPNHVFEIDEDCEKDEDSSSLCSQKGGVIKQGWLHKANVNSTITVTMKVFKRRYFYLTQLPDGSYILNSYKDEKNSKESKGCIYLDACIDVVQCPKMRRHAFELKMLDKYSHYLAAETEQEMEEWLITLKKIIQINTDSLVQEKKETVETAQDDETSSQGKAENIMASLERSMHPELMKYGRETEQLNKLSRGDGRQNLFSFDSEVQRLDFSGIEPDIKPFEEKCNKRFLVNCHDLTFNILGQIGDNAKGPPTNVEPFFINLALFDVKNNCKISADFHVDLNPPSVREMLWGSSTQLASDGSPKGSSPESYIHGIAESQLRYIQQGIFSVTNPHPEIFLVARIEKVLQGNITHCAEPYIKNSDPVKTAQKVHRTAKQVCSRLGQYRMPFAWAARPIFKDTQGSLDLDGRFSPLYKQDSSKLSSEDILKLLSEYKKPEKTKLQIIPGQLNITVECVPVDLSNCITSSYVPLKPFEKNCQNITVEVEEFVPEMTKYCYPFTIYKNHLYVYPLQLKYDSQKTFAKARNIAVCVEFRDSDESDASALKCIYGKPAGSVFTTNAYAVVSHHNQNPEFYDEIKIELPIHLHQKHHLLFTFYHVSCEINTKGTTKKQDTVETPVGFAWVPLLKDGRIITFEQQLPVSANLPPGYLNLNDAESRRQCNVDIKWVDGAKPLLKIKSHLESTIYTQDLHVHKFFHHCQLIQSGSKEVPGELIKYLKCLHAMEIQVMIQFLPVILMQLFRVLTNMTHEDDVPINCTMVLLHIVSKCHEEGLDSYLRSFIKYSFRPEKPSAPQAQLIHETLATTMIAILKQSADFLSINKLLKYSWFFFEIIAKSMATYLLEENKIKLPRGQRFPETYHHVLHSLLLAIIPHVTIRYAEIPDESRNVNYSLASFLKRCLTLMDRGFIFNLINDYISGFSPKDPKVLAEYKFEFLQTICNHEHYIPLNLPMAFAKPKLQRVQDSNLEYSLSDEYCKHHFLVGLLLRETSIALQDNYEIRYTAISVIKNLLIKHAFDTRYQHKNQQAKIAQLYLPFVGLLLENIQRLAGRDTLYSCAAMPNSASRDEFPCGFTSPANRGSLSTDKDTAYGSFQNGHGIKREDSRGSLIPEGATGFPDQGNTGENTRQSSTRSSVSQYNRLDQYEIRSLLMCYLYIVKMISEDTLLTYWNKVSPQELINILILLEVCLFHFRYMGKRNIARVHDAWLSKHFGIDRKSQTMPALRNRSGVMQARLQHLSSLESSFTLNHSSTTTEADIFHQALLEGNTATEVSLTVLDTISFFTQCFKTQLLNNDGHNPLMKKVFDIHLAFLKNGQSEVSLKHVFASLRAFISKFPSAFFKGRVNMCAAFCYEVLKCCTSKISSTRNEASALLYLLMRNNFEYTKRKTFLRTHLQIIIAVSQLIADVALSGGSRFQESLFIINNFANSDRPMKATAFPAEVKDLTKRIRTVLMATAQMKEHEKDPEMLIDLQYSLAKSYASTPELRKTWLDSMAKIHVKNGDFSEAAMCYVHVAALVAEFLHRKKLFPNGCSAFKKITPNIDEEGAMKEDAGMMDVHYSEEVLLELLEQCVDGLWKAERYEIISEISKLIVPIYEKRREFEKLTQVYRTLHGAYTKILEVMHTKKRLLGTFFRVAFYGQSFFEEEDGKEYIYKEPKLTGLSEISLRLVKLYGEKFGTENVKIIQDSDKVNAKELDPKYAHIQVTYVKPYFDDKELTERKTEFERNHNISRFVFEAPYTLSGKKQGCIEEQCKRRTILTTSNSFPYVKKRIPINCEQQINLKPIDVATDEIKDKTAELQKLCSSTDVDMIQLQLKLQGCVSVQVNAGPLAYARAFLNDSQASKYPPKKVSELKDMFRKFIQACSIALELNERLIKEDQVEYHEGLKSNFRDMVKELSDIIHEQILQEDTMHSPWMSNTLHVFCAISGTSSDRGYGSPRYAEV