lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes; Regulates also the sphingolipid metabolism.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MPVCIECGDPVPTLYLDYGKGNIKLVHCETCQTFADKYLEYDFVIVFIDMLLHKRPVYRHLIFNRLEYSSIGYNSGLVKLGILLVLFEVYMKWFRLDRMNRAVAPDNVALHMQYIYMLGVCTMETVCFHLGVRLAVSVLFPGRLVLKNYNELSMSLILSSFGKILLIVMVIWDYGQFEPSILVNLLVFTSNIEALAVFLKTSIPITGIVIGCGIACKLAVQYCIQLQDPHIELSFI
The following text describes a protein:
Function:
Transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MVQEEIMRRGPWTEEEDVQLLFYVKLFGDRRWDFLAKVSGLKRTGKSCRLRWVNYLNPDLKHGKMTPQEERLVLELHSKWGNRWSRIARKIPGRTDNEIKNYWRTHMRKKAQEQRKKSSISPSSSSSSSSITHEENERNFYDTGGIKLLQVEGEKKSSDQEQHGKSMKVYSMDEIWKDIELLEENEEKMNKPIMGSISPLWDYSLDSLWKDFDWSSFR
The following text describes a protein:
Function:
Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non-neural tissues.
Subcellular Localization:
Endoplasmic reticulum lumen. Nucleus membrane; Peripheral membrane protein. Cell projection, growth cone. Cytoplasmic vesicle membrane. Cytoplasmic vesicle, secretory vesicle. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Cytoplasm, cytoskeleton. Note=Upon oxidative stress, redistributes to protusions from the cell surface (By similarity). Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus membrane is mediated by the interaction with TOR1AIP2.
Sequence:
MKLGRAVLGLLLLAPSVVQAVEPISLGLALAGVLTGYIYPRLYCLFAECCGQKRSLSREALQKDLDDNLFGQHLAKKIILNAVFGFINNPKPKKPLTLSLHGWTGTGKNFVSKIIAENIYEGGLNSDYVHLFVATLHFPHASNITLYKDQLQLWIRGNVSACARSIFIFDEMDKMHAGLIDAIKPFLDYYDLVDGVSYQKAMFIFLSNAGAERITDVALDFWRSGKQREDIKLKDIEHALSVSVFNNKNSGFWHSSLIDRNLIDYFVPFLPLEYKHLKMCIRVEMQSRGYEIDEDIVSRVAEEMTFFPKEERVFSDKGCKTVFTKLDYYYDD
The following text describes a protein:
Function:
Catalyzes the transfer of acetyl from acetyl-CoA to the N-hydroxylysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed conditions.
Subcellular Localization:
Cytoplasm. Cell membrane.
Sequence:
MSGPNIVHSGYGLRCEKLDKPLNLGWGLDNSAVLHWPGELPTGWLCDALDQIFIAAPQLSAVVLPWSEWCEEPQALTLFGQVQSDIIHRSAFWQLPLWLSSPANRASGEMVFDAEREIYFPQRPPRPQGEVYRRYDPRIRRMLSFRIADPVSDAERFTRWMNDPRVEYFWEQSGSLEVQIAYLERQLTSKHAFPLIGCFDDRPVSNIEIYWAAEDRIGRHYSWQPFDRGLHLLVGEQQWRGAHYVQSWLRGVTHYLLLNEPRTQRTVLEPRTDNQRLFRHLEPAGYRTIKEFDFPHKRSRMVMADRHHFFTEVGL
The following text describes a protein:
Function:
In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity.
Sequence:
MFMSAKSPLLLLVDGHSLAFRAYYAFGLSKKGPLRTTAGIPTSVCFGFLNSLMQVMESQKPAAIAIAFDRREPTFRHEADGAYKSNRQETPEDFAEDLSYLQQLLEALNLQTITYAGYEADDILGTLACQGSDAGYQVKILSGDRDLFQLVSPEKNISVLYLTRNPFSSNTGYDELDWQGVVDKMGVTPAQIVDFKALCGDKSDCIPGINGIGEKTAIKLLAEYETLEKVYENLAQIKGALKTRLDNGKDDAMHSQMLARIVVDVPLPVTWEDLQLTGFSTDRLVPLLEKLELRTFIDKIQAFHRNFSDNQSPVPMGNEADNGEPKKTVKAKKSKEKVNPDDSQQLSLFDGVPVVNQEDGLITIQLPKQIQPQIITTIAQLEALVEELKKHTDADFPVAWDTETDSLDPLVANLVGIGCAWGQEPNQVAYIPLKHHQGEQLSLGIIKDLLGEILGNAIYPKVLQNAKFDRRVLAHHGIELGGVVLDTMLASYVLQPEETHNLTDLCRRYNLGLVALSYKDLGLKKDQTIADLPLETAGQYCGLDCYATYLLASKLQKELDQYPELKEILKEIEQPLEKILAAMEDRGIRIDCDYLQTLSQQLAENLLTIETAAYEAAGESFNLSSPKQLGTILFDKLGLDRKKSRKTKTGYSTDHATLEKLQGDHPIIDAILEHRTLAKLKSTYVDALPELVNGQTQRIHTDFNQAVTSTGRLSSSNPNLQNIPIRSDFSRQIRRAFLPQKDWLLVSADYSQIELRILAHLSQEPVLLQAYGDRQDVHGVTAKLLFGKEDITPAERNLGKTINFGVIYGMGAQRFARETGISAVEGREFIDRYHRTYAQVFDYLETMKLEAIAKGYVTTIVGRRRYFNFVTEALRQLRGKTVTELDLVDVKMNYNDAQLLRSAANAPIQGSSADIIKIAMVKLAKLLESYQTRMLLQVHDELIFEMPPEEWEELAPLIQNTMEQALTLSVPLVVEMHRGSNWMEAK
The following text describes a protein:
Function:
Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MSVIVFRYLCKEILGTLLATTLILLIIFMTNQFVHYLNDAAAGKITVKAVMEIMSLQVPLLLGYLLPLGLFLGGLLALGRMAVDHEMVILTACGVSRAQIVGMLIVLATFIGVIVAWLMLSVEPKMQWYRVKILKDAVATASLEKIVPGRFQLLSSNGQVFYAGGVNDHHQKMLNVFLAQSETAGGKQRWDLVSADQAGEYSTAKGENFILFKNGFRYVGIPGELKYDVMKFGEYGIRLTSPAMDITERVDAMPTSKLWHLHSKDLKAAAELQWRIAMPLSVWLFALLIVPLSEANPRKGKFAQMLPAVLIYIGYANFMFLGRTWIEDGVISQYLGLWWILGLLLLLAIGLLFFQSRWWRQFRGSRRIACRS
The following text describes a protein:
Function:
Promotes the onset of gluconate uptake upon glucose starvation.
Sequence:
MTEPGNLQPTFVGFIGTTVDALLLFEACRQNYTHFVDRRPQDRERERLIRSGSVFVFDEVQSGIKRWTDGIAWSPSRVIGNFLVYRQLCKKNSVSDRKRSSKSRSDSDEEEVSAFTVSVPVDVDVASHVNISSPSAPSLSDNLFPGSSFSASSQQNPSSPGSNDIKSEFAAVKNEYVLSPTSPTTSAAFPSSFSSLPLVSSKPTGTPFVPKSPPSSSPSTTNVSNASTSSAPINPRAPQTRRESISSTSSIHYCSSSSLSYLHDTERALVGSLTDSYGFKKSGLIKKTISLMIDGRLHHLISYYTPEDVLNGKLQTPSSFNLFQQLTISKDLLEYKSFRIPPLVEAAESEKISQLSTLEKRTLPSFPYNPFFSSSTAEIDPYHFQGLTLSTSPISGVESSSLSSAISRNQSNLSSFQQQQQFSALQSISNNALNENIEQPPIKMAARHSYPNFLQTLPQYMNDVYNPSGLAFNPVNPNANNSFVNLNLIQFTSPSQALFDYGEGPYVDQKSQYLQPKQPSSNTDSIDQSSYNMSLAASKQFLTSDTQPDVNENYSFISNSIPKNLSTSWNQNMGYHVTNSNSELASQNPLYAQQAVSMESMGNAIQSSAYSAMSTPHGGHYDHYAATAKGKNPLAAENHASGGRLPKVPIPPLSNMRRGSVPIIPSSASLPMRTSGNRFCHYSSLNGNHNRISARTNPYPINNQTMLFTEPLSKERGSLS
The following text describes a protein:
Function:
Part of a three-gene cluster containing FLC, UFC and DFC, which is coordinately regulated in response to vernalization. Also regulated by FLX. SOSEKI proteins (SOK1-5) locally interpret global polarity cues and can influence cell division orientation to coordinate cell polarization relative to body axes, probably by guiding ANGUSTIFOLIA (AN) polarized localization.
Miscellaneous:
MISCELLANEOUS: 'Soseki' means cornerstone in Japanese.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=SOSEKI proteins integrate apical-basal and radial organismal axes to localize to polar cell edges, pointing towards the epidermis, mainly to inner basal edges.
Domain:
The DIX-like oligomerization domain is required for polymerization, edge localization and biological activity.
Sequence:
MEAVRCRRGRENNKSPERIIRSLNHHQHDEELEEEVKTKKPIFRRVQVVYYLTRNGHLEHPHFIEVISPVNQPLRLRDVMNRLTILRGKCMTSQYAWSCKRSYRNGFVWNDLAENDVIYPSDCAEYVLKGSEITDKFQEVHVNRPLSGSIQEAPKSRLLRSKLKPQNRTASFDDAELYVGEEEEEEDGEYELYEEKTSYTSSTTPQSRCSRGVSTETMESTEQKPNLTKTEQDLQVRSDSSDLTRSNPVVKPRRHEVSTRVEDGDPVEPGSGRGSMWLQMISCGHIATKYYAPSVMNPRQKEENLRKGVLCKNIVKKTVVDDEREMIRFMSENPRFGNPQAEEKEYFSGSIVESVSQERVTAEPSLRRSNSFNEERSKIVEMAKETKKKEERSMAKVKCIPRTCLMSSSKQIKK
The following text describes a protein:
Function:
Required for efficient repair of photodamaged PSII, but not tightly associated with the complex.
Subcellular Localization:
Plastid, chloroplast thylakoid lumen.
Sequence:
MASLKLSPSSPISISKVGVIPSSKKGLSFLVKAEHHSSSSSSHLQDKCQRRLIVTFGVVAPWISLLSRAPLSFAAESKKGFLAVSDNKDAYAFLYPFGWQEVVIEGQDKVYKDVIEPLESVSVNLVPTSKQTIKEFGPPKQIAETLIKKVLAPPNQKTTLIDASEHDVDGKTYYQFEFTVQARNYTRHALGTITVFNGNFYTLTTGANERRWEKMKDRLHTVVDSFKITV
The following text describes a protein:
Function:
Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake.
Subcellular Localization:
Secreted.
Sequence:
MNWAFFIGTESKMKLWDVLATCLLLLSSVATRPLYQSTHPAKRTYFPSSSHPASLSVEDEEPLFQRKERKLKDISMEDQYDAAGFYPEQFEDVMDFIEATISRLRRSSEPAIGSRGRREQKQRKAANTGGRREEGRGHGVKRKSRGRGGGRGSKGGRGDKGKEGIYVQSRGCLLKEVHLNVTDLGLGYQTKEELIFRYCSGPCAEAETNYDKILNNLTHNKKLDKDTPSRTCCRPIAFDDDLSFLDDNVVYHTLKKHSARKCGCV
The following text describes a protein:
Function:
DNA binding protein that function as transcriptional activator. Is essential for normal postnatal growth and nursing. Is an essential factor for neuronal neuropeptide Y and agouti-related peptide function and locomotory behavior in the control of energy balance.
Subcellular Localization:
Nucleus.
Sequence:
MNLNFTSPLHPASSQRPTSFFIEDILLHKPKPLREVAPDHFASSLASRVPLLDYGYPLMPTPTLLAPHPHHPLHKGDHHHPYFLTTSGVPVPALFPHPQHTELPGKHCRRRKARTVFSDSQLSGLEKRFEIQRYLSTPERVELATALSLSETQVKTWFQNRRMKHKKQLRKSQDEPKAPDGPESPEGSPRGAEAAPAEARLGLPAGPFVLTEPEDEVDIGDEGELGSGPHVL
The following text describes a protein:
Function:
Deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids. Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-tRNA(Tyr). By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. In contrast to DTD1, deacylates L-Ala mischarged on tRNA(Thr)(G4.U69) by alanine-tRNA ligase AARS. Can deacylate L-Ala due to a relaxed specificity for substrate chirality caused by the trans conformation of the Gly-Pro motif in the active site. Also hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly) in vitro, although in vivo EEF1A1/EF-Tu may protect cognate achiral glycyl-tRNA(Gly) from DTD2-mediated deacetylation.
Subcellular Localization:
Cytoplasm.
Domain:
A Gly-transPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of most L-amino acids except L-Ala. The trans conformation of the motif is maintained by Arg-151.
Sequence:
MADGGRVAQARALLQQCLHARLQVRPADGDAAAQWVEIRRGLVIYVCFFKGADTDLLPKMVNTLLNVKLSETETGKHVSILDLPGDVLIIPQATLGGRVKGRSMQYHSNSGKEEGSELYSQFVSLCEKAVANNTKSVEAGVAVAHGTYGNRQVLKLDTNGPYTHLIEF
The following text describes a protein:
Function:
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Subcellular Localization:
Cytoplasm.
Domain:
The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of eif3d into the full eukaryotic translation initiation factor 3 (eIF-3) complex.
Sequence:
MSETINTAAQFPSFEKPTVQFNERGWGPCELPDTFKDVPYQPFSKNDRLGKICDWTSTSNNDKKYQNKYASSFGTGNQYSYYHEEDETTFHLVDTARVQKPPHQRGRFRNMRGRGGRGRNPRGGLNNHHHHGMTTLNGKNVKARDTRRGMGKKFGHRGPPPKMRESSVAVRADWASIEEMDFPRLIKLSLPNIKDGVDIATCGTLEYYDKTYDRINVKNEKPLQKIDRIVHTVTTTDDPVIRRLSKTVGNVFATDAILATIMCSTRSNYSWDIVIEKVGDKPPTDDDSSCNSPRNLAIEATFINHNFSQQVLKTGDQEAKFKFEEPNPFISEDEDIQVASVGYRYKKWELGSDIVLVARCEHDGVLQTPSGEPQFMSIKALNEWDSKLANGVEWRQKLDTQRGAVLANELRNNACKLAKWTVQAVLAGSDQLKLGYVSRINPRDHSRHVILGTQQFKPHEFATQINLSMDNAWGVLRCIIDLVMKQKDGKYLIMKDPNKPIIRLYDIPDNTFDSDDSDDGEGDDGEGFQQVYNYANNSNKI
The following text describes a protein:
Function:
With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Synthesizes long-chain polyprenols, mostly of C95 and C100 chain length. Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator.
Miscellaneous:
MISCELLANEOUS: NUS1 seems to exist in two topological orientations, a minor glycosylated species with its C-terminus oriented towards the lumen regulating NPC2 stability, and a major fraction oriented with its C-terminus directed towards the cytosol where it regulates cis-IPTase activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Colocalizes with Nogo-B during VEGF and wound healing angiogenesis.
Domain:
Contains the RXG motif, which is important for substrate binding and prenyltransferase activity. The catalytic site at NUS1-DHDDS interface accomodates both the allylic and the homoallylic IPP substrates to the S1 and S2 pockets respectively. The beta-phosphate groups of IPP substrates form hydrogen bonds with the RXG motif of NUS1 and four conserved residues of DHDDS ('Arg-85', 'Arg-205', 'Arg-211' and 'Ser-213'), while the allylic isopentenyl group is pointed toward the hydrophobic tunnel of the S1 pocket where the product elongation occurs.
Sequence:
MTGLYELVWRVLHALLCLHRTLTSWLRVRFGTWNWIWRRCCRAASAAVLAPLGFTLRKPPAVGRNRRHHRHPRGGSCLAAAHHRMRWRADGRSLEKLPVHMGLVITEVEQEPSFSDIASLVVWCMAVGISYISVYDHQGIFKRNNSRLMDEILKQQQELLGLDCSKYSPEFANSNDKDDQVLNCHLAVKVLSPEDGKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKFGPVDSTLGFLPWHIRLTEIVSLPSHLNISYEDFFSALRQYAACEQRLGK
The following text describes a protein:
Function:
Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MADSSSSLLPLCERISHKSYILRIVDLTILVLLFSLLWYRILHMCENNTIWLVAFLCESCFSFMWLIITCIKWSPAEDKPYPNRLDERVHDLPSVDMFVPTADPVREPPIIVVNTVLSLLAVNYPANKLACYVSDDGCSPLTYFSLKEASKFVKIWAPFCKKYNVRVRAPFRYFLNPLVATDDSVFSKDWKMMKREYVKLCRKVEDATGDSHWLDADDDFEAFSNTKPNDHSTIVKVVWENKGGVGDEKEVPHLVYISREKRPNYLHHYKTGAMNFLLRVSGLMTNAPYMLNVDCDMYANEPDVVRQAMCVFLQNSKNSNHCAFVQFPQNFYDSYTNELVVLQHYMKRGVAGIQGPIYIGSGCFHTRRVMYGLSSDDLEDDGSLSSVASREFLSEDSLVRKYGSSKELVKSVVDALQRKSNPQKSLANLVEAAQEVGHCHYEYQTSWGNLGWLYDSVAEDTNTSIGIHLRGWTSSFISPDPPAFLGSTPSVGPEAIVQHRRWATGSIEVLFNKQSPLIGFRRKIKFRQRLAYFWVLMCIRSIPELVYCLLPAYCLLNNSALFPKGPCLGIIVTLVGMHCLYTLWQFMILGFSVKSWYVSQSLWRIIATSSWLFSIQDIILKLLGISKIGFIVAKKNMPETRSGYESKSKPSQGEDDGLKLELGKFEFDSSCHFIPGTFIMLVNLAALAGFLVRLQRSSYSHGGGGGSALAETCGCAMIVMLFFPFLKGLFEHGKYGIPLSTLSKAAFLTVLFASYHL
The following text describes a protein:
Function:
Extracellular aminopeptidase that allows assimilation of proteinaceous substrates.
Subcellular Localization:
Secreted.
Sequence:
MRFLPCIATLAATASALAIGDHIRSDDQYVLELGPGETKVVTEAEKWALRAEGKRFFDITGRTSSLELASNKKQKLAVTYPDSVQHNETVQNLINSLDKKNFETVLQPFSEFHNRYYKSDNGKKSSEWLQGKIQEIISASGAKGVTVEPFKHFFPQSSLIAKIPGKSDKTIVLGAHQDSINLNSPSEGRAPSADDDGSGVVTILEAFRVLLTDEKVAAGEAPNTVEFHFYAGEEGGLLGSQDIFEQYLQKSRDVKAMLQQDMTGYTKGTTDAGKPESIGIITDNVDENLTKFLKIIVDAYCTIPTVDSKCGYGCSDHASATKYGYPAAFAFESAFGDDSPYIHSADDTIETVNFDHVLQHGRLTLGFAYELAFADSL
The following text describes a protein:
Function:
Putative transcription factor, weakly pro-apoptotic when overexpressed (By similarity). Tumor suppressor. Required for early embryonic stem cell development; [Isoform 2]: Displaces isoform 4 at the onset of differentiation, required for repression of stemness genes.
Miscellaneous:
MISCELLANEOUS: Defects in DIDO1 may be a cause of myeloid neoplasms.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Note=Translocates to the nucleus after pro-apoptotic stimuli (By similarity). Translocates to the mitotic spindle upon loss of interaction with H3K4me3 during early mitosis.
Domain:
The PHD-type zinc finger forms an aromatic cage around H3K4me3.
Sequence:
MDDKGDPSNEEAPKAIKPTSKEFRKTWGFRRTTIAKREGAGDAEADPLEPPPPQQQLGLSLRRSGRQPKRTERVEQFLTIARRRGRRSMPVSLEDSGEPTSCPATDAETASEGSVESASETRSGPQSASTAVKERPASSEKVKGGDDHDDTSDSDSDGLTLKELQNRLRRKREQEPTERPLKGIQSRLRKKRREEGPAETVGSEASDTVEGVLPSKQEPENDQGVVSQAGKDDRESKLEGKAAQDIKDEEPGDLGRPKPECEGYDPNALYCICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLERNGEDYICPNCTILQVQDETHSETADQQEAKWRPGDADGTDCTSIGTIEQKSSEDQGIKGRIEKAANPSGKKKLKIFQPVIEAPGASKCIGPGCCHVAQPDSVYCSNDCILKHAAATMKFLSSGKEQKPKPKEKMKMKPEKPSLPKCGAQAGIKISSVHKRPAPEKKETTVKKAVVVPARSEALGKEAACESSTPSWASDHNYNAVKPEKTAAPSPSLLYKSTKEDRRSEEKAAAMAASKKTAPPGSAVGKQPAPRNLVPKKSSFANVAAATPAIKKPPSGFKGTIPKRPWLSATPSSGASAARQAGPAPAAATAASKKFPGSAALVGAVRKPVVPSVPMASPAPGRLGAMSAAPSQPNSQIRQNIRRSLKEILWKRVNDSDDLIMTENEVGKIALHIEKEMFNLFQVTDNRYKSKYRSIMFNLKDPKNQGLFHRVLREEISLAKLVRLKPEELVSKELSTWKERPARSVMESRTKLHNESKKTAPRQEAIPDLEDSPPVSDSEEQQESARAVPEKSTAPLLDVFSSMLKDTTSQHRAHLFDLNCKICTGQVPSAEDEPAPKKQKLSASVKKEDLKSKHDSSAPDPAPDSADEVMPEAVPEVASEPGLESASHPNVDRTYFPGPPGDGHPEPSPLEDLSPCPASCGSGVVTTVTVSGRDPRTAPSSSCTAVASAASRPDSTHMVEARQDVPKPVLTSVMVPKSILAKPSSSPDPRYLSVPPSPNISTSESRSPPEGDTTLFLSRLSTIWKGFINMQSVAKFVTKAYPVSGCFDYLSEDLPDTIHIGGRIAPKTVWDYVGKLKSSVSKELCLIRFHPATEEEEVAYISLYSYFSSRGRFGVVANNNRHVKDLYLIPLSAQDPVPSKLLPFEGPGLESPRPNIILGLVICQKIKRPANSGELDKMDEKRTRLQPEEADVPAYPKVATVPQSEKKPSKYPLCSADAAVSTTPPGSPPPPPPLPEPPVLKVLSSLKPAAPSPATAATTAAAASTAASSTASSASKTASPLEHILQTLFGKKKSFDPSAREPPGSTAGLPQEPKTTAEDGVPAPPLLDPIVQQFGQFSKDKALEEEEDDRPYDPEEEYDPERAFDTQLVERGRRHEVERAPEAAAAEREEVAYDPEDETILEEAKVTVDDLPNRMCADVRRNSVERPAEPVAGAATPSLVEQQKMLEELNKQIEEQKRQLEEQEEALRQQRAAVGVSMAHFSVSDALMSPPPKSSLPKAELFQQEQQSADKPASLPPASQASNHRDPRQARRLATETGEGEGEPLSRLSARGAQGALPERDASRGGLVGQAPMPVPEEKEPASSPWASGEKPPAGSEQDGWKAEPGEGTRPATVGDSSARPARRVLLPTPPCGALQPGFPLQHDGERDPFTCPGFASQDKALGSAQYEDPRNLHSAGRSSSPAGETEGDREPQARPGEGTAPLPPPGQKVGGSQPPFQGQREPGPHALGMSGLHGPNFPGPRGPAPPFPEENIASNDGPRGPPPARFGAQKGPIPSLFSGQHGPPPYGDSRGPSPSYLGGPRGVAPSQFEERKDPHGEKREFQDAPYNEVTGAPAQFEGTEQAPFLGSRGGAPFQFGGQRRPLLSQLKGPRGGPPPSQFGGQRGPPPGHFVGPRGPHPSQFETARGPHPNQFEGPRGQAPNFMPGPRGIQPQQFEDQRVHSPPRFTNQRAPAPLQFGGLRGSAPFSEKNEQTPSRFHFQGQAPQVMKPGPRPLLELPSHPPQHRKDRWEEAGPPSALSSSAPGQGPEADGQWASADFREGKGHEYRNQTFEGRQRERFDVGPKEKPLEEPDAQGRASEDRRRERERGRNWSRERDWDRPREWDRHRDKDSSRDWDRNRERSANRDREREADRGKEWDRSRERSRNRERERDRRRDRDRSRSRERDRDKARDRERGRDRKDRSKSKESARDPKPEASRASDAGTASQA
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MFSIDSCLKTRPLTFRIARLGMNFTTCSAARSYVGKKEIIVPKNIQFDLEGEQLQITGPHGTLNMRFPNYLNLSKTNDILKVGMDANIEKQATKKQRAMWGTTRAILANNVKGVTMYWQSIIKLVGIGYRTSLNDGNIHLKIGYANDILVSIPTDVQVENPTPTSLVLRGIDRQKVTQFAAKIRSFKKPEPYKGKGIYVDGEKPQLKAKRSIS
The following text describes a protein:
Function:
Functions as a zinc transporter.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSGGDDFGNNSFSNSIGGGLNSKFSRYAKNGSQQLVLMLFGAKGIRSWVTIMLFYLLQSLSVINVSFYMLLFSTIQSLITEKPWNLLSQLRPSQIKKIIYYSLFNLFIVLTWNCSVKYIGPLGTILASDYSYSTYPIIFGTLLQGNFLSTDMSRASIMLIFGYLLIPFFGGSKLQIHGYSASQVFMIGIFSLLIHNILVMVKKTAVKGWSNSHRNKLSSLGSLVATIVLFVLKMFESWSPSNHPVYIDYNQVSYYQLLQLVIVSVILLSFNQLTEDVSEQQLGFLVLSKASLTSTLLFGFIIAIFIGFYDFFSPILILSFVLIITAIHILYSKSNNVDQQSQVTFKTPIDGSSSIKTFNSSHENKAGYYLEIAKDVIRQIIEKPVSRRIFTFLIINLMFMFVEMAYGIWTNSLGLITDACHMLFDATALFIALVAEVISQWKQNDTYSYGYGRVQVLSGFVNGIFLIFIAVTILMESIERLLEPPEINTDKLLLVSVLGFLVNLVGIFSFHGDHGHSHGGGGGHTHGHSHGGEKKKSHDDHGHSHGGSSHAEEPKKKRSVNIDGVFLHLLADTLGSVGVIVSSLIIQIWGYTLADPICSLCISILIFLSVLPLIKGTAKTLLQCTPDSINSDIHQITQKILGTPGVTGLLNYHFWSHYDEMNIATLKIQVDSNADNEKIKKSISKFLKHDYSVHKTLIEFVNFSNLLNNSSNNNNNNEYNYNNNESIDNHSLPHEPQFHHNHHGHSHNH
The following text describes a protein:
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.
Miscellaneous:
MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried out by the same active site and suggest a common mechanism for both reactions.
Domain:
The Walker A ATP-binding motif also binds Pi and PPi.
Sequence:
MPKVRTKDLIEQFQLELISGEEGIHRPIDTSDLSRPGIEMAGFFTYYPADRVQLLGKTELTFFDTLTSEQKQERMKALCTEETPCIIVTRNQDVPDELLQASRESGMPLLRSSQTTTRLSSRLTNYLEGKLAPTTAVHGVLVDIYGVGVLITGQSGVGKSETALELVKRGHRLVADDSVEIRQEDEDMLVGSSPDLIEHLLEIRGLGIINVMTLFGAGAVRNYKRITLVINLEIWDQKKNYDRLGLDEEKMKIIDTELTKITLPVRPGRNLAVIIEVAAMNFRLKRMGVNAAQQFSERLMSAIELGNQE
The following text describes a protein:
Function:
Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably responsible for energy coupling to the transport system.
Sequence:
MLKVDNLGFGYSGIPIFEGVSFRVKKGSLCGLFGPNGSGKTTLFKCCMSFLKYDNGSICIDGCDVKRKKIGELAKLVAYVPQEHKPPFPYLVKEVVLMGRTPHMGGIFGVSEDDKSKVMEALEMLEISHIADKPYNQLSGGQRQLVLIARAMAQETPLMLLDEPTSALDFCNQIRIWNILKKISAKGTTILACSHDPNHISWFCDDVIVMYGGGLVAKGNPKSVVSEELLSTIFSDICSVGYMDRLMMVYPKNIQAECPITTINNDLL
The following text describes a protein:
Function:
Reversible hydration of carbon dioxide.
Sequence:
MGIQLLDKYQLQPLSLDSVPWRRQPGQQVLWIGCSDSGCDELESSGLPADEIFEYRSLGNMMVDDLSCKATLGYALDSLKIRNIVICGHYGCHIASGEVNAGLQKPWSSVLDTLRSTHRRTLDSLTGTERDRALVELNVLEQVHSLRQSAEAAEALQKQQLNIWGMVYDKATKRGYQLIEA