lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the hydrolysis of sulfoquinovosyl diacylglycerides (SQDG) to sulfoquinovose (SQ), which is then degraded by E.coli through the SQ Embden-Meyerhof-Parnas (SQ-EMP) sulfoglycolysis pathway as a source of carbon and sulfur. Therefore, is likely involved in the utilization of the sulfoquinovose headgroup found in ubiquitous plant sulfolipids. Is also able to hydrolyze simple sulfoquinovosides such as sulfoquinovosyl glycerol (SQGro). In vitro, can use the substrate analog para-nitrophenyl alpha-sulfoquinovoside (PNPSQ), but shows no detectable activity toward 4-nitrophenyl alpha-D-glucopyranoside (PNPGlc). Is a retaining glycoside hydrolase, since it forms the alpha anomer of SQ. Also exhibits some alpha-glucosidase activity against alpha-glucosyl fluoride in vitro, although natural substrates, such as alpha-glucobioses are scarcely hydrolyzed.
Domain:
Structural analysis revealed the molecular coevolution of catalytically important amino acid pairs directly involved in substrate recognition, as well as structurally important pairs distal to the active site.
Sequence:
MDTPRPQLLDFQFHQNNDSFTLHFQQRLILTHSKDNPCLWIGSGIADIDMFRGNFSIKDKLQEKIALTDAIVSQSPDGWLIHFSRGSDISATLNISADDQGRLLLELQNDNLNHNRIWLRLAAQPEDHIYGCGEQFSYFDLRGKPFPLWTSEQGVGRNKQTYVTWQADCKENAGGDYYWTFFPQPTFVSTQKYYCHVDNSCYMNFDFSAPEYHELALWEDKATLRFECADTYISLLEKLTALLGRQPELPDWIYDGVTLGIQGGTEVCQKKLDTMRNAGVKVNGIWAQDWSGIRMTSFGKRVMWNWKWNSENYPQLDSRIKQWNQEGVQFLAYINPYVASDKDLCEEAAQHGYLAKDASGGDYLVEFGEFYGGVVDLTNPEAYAWFKEVIKKNMIELGCGGWMADFGEYLPTDTYLHNGVSAEIMHNAWPALWAKCNYEALEETGKLGEILFFMRAGSTGSQKYSTMMWAGDQNVDWSLDDGLASVVPAALSLAMTGHGLHHSDIGGYTTLFEMKRSKELLLRWCDFSAFTPMMRTHEGNRPGDNWQFDGDAETIAHFARMTTVFTTLKPYLKEAVALNAKSGLPVMRPLFLHYEDDAHTYTLKYQYLLGRDILVAPVHEEGRSDWTLYLPEDNWVHAWTGEAFRGGEVTVNAPIGKPPVFYRADSEWAALFASLKSI
The following text describes a protein:
Function:
Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptidoglycans. Host outer membrane disruption due to local fusion between the inner and outer membrane performed by the spanin complex.
Subcellular Localization:
Host cell outer membrane; Lipid-anchor; Periplasmic side.
Domain:
The proline-rich region is an essential fusion motif involved in host membrane fusion leading to lysis.
Sequence:
MLKLKMMLCVMMLPLVVVGCTSKQSVSQCVKPPPPPAWIMQPPPDWQTPLNGIISPSERG
The following text describes a protein:
Function:
Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules.
Sequence:
MSCGNEFVETLKKIGYPKADILNGEDFDWLFEDVEDESFLKWFCGNVNEQNVLSEKELEAFSDLQRSGKPILEGTALDEVLRTCKTFDLKTCKLDDKEIQILEDEVQTLQKLNNSKIQRRNKYQLMVSETSYRFLALNAKQEEATKKLKQKQGFLNSVNTKLSNELQGLTEEVNNLMIFFRNSNLSERTNPMVFLSQFPLGKYISQEEQSTAALTLYTKKQFFQGMHEVVESSNEDNFQLLDIQTPSICDNEEILRERRLEMARLQMACICVQKQIIYLKTSNLSMKSSIKWAEENLNRLTNEVIDKENLDAEISSLNSEILKLEEQITHIKDKVLPAVVKEYAQLLNMPVVKGDFELQIAKQDYYTARQELVLNELIKQKASFELVQLSYEIELRKHWDTYRQLESLVQQLSQRNTVLCQHLAVLSDIPASEQLTSRTPIDTKDHSTHRLYELLEGDNKKKELFITHEHLEEVAEKLKQDVSVIQDQLAVSTQEHFFFLSKLNNDVDMLCDALYRGGNQLLLCDQELKEHFHQVESQLNELHHLLTDILADVKTKRRILATNKLHQVER
The following text describes a protein:
Function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MYLVYLMFIPMVFLFYHKNFKMWFLVYSFFLLYSILPMFFKTGEIIFCNHFSSWSGDTVNAMLIILSIVVIMLSGIIMMEGNRMNYMMMSFYFSMLFLVLFFGSDDLLNFLVFFELSMLPIFLLIGWWGKGKERMFSNYYFFLYTLVTSLPMFMLILKTMTLGMESMTLYNYYNLKITWFMFLLLVLGFLTKLPIYGLHIWLPKAHVDAPVGGSMVLAGILLKIGGFGMMRCFMLMGEEVKMTYSVFFIMFLGVWGLMFTGVVCLRLTDFKVIVAFSSVSHMSLAVAGLMSYFYWGFKGSYLMFLGHGILSPVLFFFGDMLYKRYHSRHINSMKGLISSSSFMFYLITLFFFAMNFGFPPFMNFFGEIGLFMSLLSFNYLQALFMFGGFLMAGIFMLNMFVMIGQSKKMLFQKMVLLNYEKMTIFFFFLSYIYMSLLFSSII
The following text describes a protein:
Function:
Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Acts as a viroporin that forms an oligomeric ion channel in membranes. Modulates the host DNA repair mechanisms to promote degradation of nuclear viral cDNA in cells that are already productively infected in order to suppress immune sensing and proviral hyper-integration (superinfection). Manipulates PML-NBs and modulates SUMOylation of host BLM protein thereby enhancing its DNA-end processing activity toward viral unintegrated linear DNA. Also inhibits RAD52-mediated homologous repair of viral cDNA, preventing the generation of dead-end circular forms of single copies of the long terminal repeat and permitting sustained nucleolytic attack.
Miscellaneous:
MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K).
Subcellular Localization:
Host membrane; Single-pass type I membrane protein.
Domain:
The N-terminus and transmembrane domains are required for self-oligomerization and proper virion budding, whereas the cytoplasmic domain is required for CD4 degradation. The cytoplasmic domain is composed of 2 amphipathic alpha helix that form a U-shape.
Sequence:
MQPLQILAIVALVVAAIIAIVVWTIVYIEYRKILRQRKIDRLIDRITERAEDSGNESEGDQEELSALVERGHLAPWDVDDL
The following text describes a protein:
Function:
Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with topbp1 by participating in cdk2-mediated loading of cdc45l onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre-initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation.
Subcellular Localization:
Nucleus. Note=Associates with chromatin.
Sequence:
MASQNVVFAIDVDYRPEGTQNTTNAYQDHLKQWILRVLLSLGHRYGLEKVRWGYKFFNSRTVKSATLITRGSDFKELQEKVFSDFEEELHVKFTTEGKSPRSQEKSHKLKPSPACCVQNALKEILLDFQWDRPDLTSPTKVTLRPRRSSRSGRNIPLQDCDMLSVDKNVLFVVSECPRSKAELEDYLSMRREDSRHHKDINEQMLPKGLIDMLMQRNVVLHWADSGVFKADHVAKDYTGIETLMERLGLVGGQVVPMLSPCLPLMDQHPKMNSLLALGVDAFPIDSTNSYLHLSKRMQQQLFPPLGASFSWIADGTKRSCNVTLEPVSYRQRSLRAPVDVLLKGVLQSLDILSLSHSAIETWILQCPDAELGQEAFQHLKQLSTGGHAMLAEVSEGDVVCSAVLSVLSSCTAQITVLQPLLAQEGQLLPADLVSLDTTDISGDLPDVVSSVLSVMYDIMEEDDCSDHEKMPLVPDWANQELKQQSSSRSNGMVEGWFPLSDQSGISCHLMESMRLLHAAPEEKEKGEEYSDTQQEITSSLSEFYQSSTAGSSGSLRSKKRGTQCTPVRQKMKTMSRSLQMLNFARLNVKAQKTQGDSGSAGSGKGTEKGGKKSSGDRTKPGLLHFSSEEELLSHLGLTYQKAVENRTMSVPSQVQDLLSVVKSFLKSNTEASLLNLVQKHVLKSCQSIRQHYGNSSDDESKIRECQLQAVLRLELCKQTEQEDEEVVEQRVEDVADMLRNISRSKDAVYLSRFMQEEVLPLYMNSIPKVLADVYHSLGTQLPEALVAVLPSDFFSDESLAKDSVSVSLSSFSATQSNISSVGDHLEELRNRSAKKRRQSMITRHKSMTEAPQALRQIEMPRKSTRLAKPKLCVPIEKTAVEQPPLPKQPVQEVTKVRRNLFNQVTVSPSKKSKMPRSQSVSAVEGIKKRKRSDVDNDDRHTLLTKKVSETPLHKQVSSRLLHRQRTGRKSGESDVCIIEESPIKPAADLRRSPRIKSLTRRHSSVFYSSSQPRSRNLDRVVSSSQLSHSEGKGKFSVSSVRSPVRLLFGATQSPGRLRHTTVSSLEDQASKGLPLRCSSFENQNKTPQKLRSDALASAVGCRTPQSPRTPNRTVGDNGMALRGSPFQSPAAKSIVVETPMKSPLKGILKTPIKKSLLDCVSPNGAWLRSPGCKTPKKCVTWSPSPRKPVPENQVNVPDSPVFAKRHSPRLVTPGKNSSPEEKIVFKTPDKVPQRKSKTSPEIILRRLEIPVNIDPETCKSITRSGKIRTLSLPYKTSKGSDEFLPQSESGSFPFCNSPLKPNIQKTIQSPIPTHRMCTRSGNTPVKESCSPSSNSQGITGTSPSPRKSLSSAVAKSSPSPSFGPSRSGVGNQNNSSISNVEKHTDDDKIIVQNKANDEKAEEASSSDSQQFDCSEFSITTDDESIDISEAAVVKTQLVGGIKMNIAFSRKPSKSDVFEFEGKQTTSTGTPLTRSYGFRQTPDRRQREAEARLGYSSGKPKISTPRTRRTPACGKQSSPQPLTYEVEMEMQASGLPKLKLRRTDSFNAGDLPSSATKGMTSHLVHRNKTNLKAPQIDSPLVQSSRHPGCISPSLCSRATPAKGTPGKGVQTYICQSITPTHHPTSSQSPLASPLTPSPQSRGWPTPENLNSWPRKKRARIETCGNKEQVIKGVPLLEKTGVIEDPELEGIFRIQGVEELKESLSTPISQRKLGLRSSQVMDHQGSPEGMDWTETMAQMCDAKDSTKTEQFAWMGRKVDTPKVKKQVSASGIFALTQSPLLYKKSAVIKEATQFSGSKSELEISPLCQPRRRRTPSRTYSRKKLLD
The following text describes a protein:
Function:
Key adapter protein that plays an essential role in JNK and NF-kappa-B activation and proinflammatory cytokines production in response to stimulation with TLRs and cytokines. Mechanistically, associates with the catalytic domain of MAP3K7/TAK1 to trigger MAP3K7/TAK1 autophosphorylation leading to its full activation. Similarly, associates with MAPK14 and triggers its autophosphorylation and subsequent activation. In turn, MAPK14 phosphorylates TAB1 and inhibits MAP3K7/TAK1 activation in a feedback control mechanism. Also plays a role in recruiting MAPK14 to the TAK1 complex for the phosphorylation of the TAB2 and TAB3 regulatory subunits.
Subcellular Localization:
Cytoplasm, cytosol. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MQSNQSWTDDLPLCQLCGVGSSPNCVYGPDGKGTQSHPNEDGHFRFSTESCFLYGVFNGFEGSRVASFVCQCLTAELLLGQLSSGDTDADVRRILTQAFDVVEKSYFETIDDALAEKANLQTQLPEGAYVSAQTHNIADRLKTLEQEVTRGATAIVALILKNKLYIANVGTNRALLCKTTSDGQNQVIQIGRAHTTDNEDELTRLAQLGLDPVRLRQTAVISGQSSTRRIGDYKVKFNYTDIDVLSAAKHKPIIAEPEIHGGQSLAGVTGFLLLMSEGLIKALEAAHGPEQVNQEVVAMVAAELAQQGSLEAAAQAVVERVKRLHHDVFVSGRQRAQHCAHHEDMTLLIRVINYTLADGSLTPTQGGRIYPVSVPYSNHQSTSKTSVTLSLVMPAQGTLTNGSSTSSTLEGDTPTAGNQSPSTTLQSTNTHTQSSSSSSGDGSLFRQRSNQAAQPDETGRVPPYVDFTQFFRLWGKDHNDSQTVSAELGPQ
The following text describes a protein:
Function:
May be an activator protein for the gylABX operon.
Sequence:
MARNIQSLERAAAMLRLLAGGERRLGLSDIASSLGLAKGTAHGILRTLQQEGFVEQDDASGRYQLGAELLRLGTTYLDVHELRARALVWTDDLARSSGESVHLGVLHQQGVLIVHHVFRPDDSRQVLEIGAMQPLHSTALGKVLSAYDPVAHSEALEADRKAFTDRTVCEPDSFEHVLDITRARGYAADVEETWEGIASIAAPIHDRRRMPVGAVGITGAVERLCREGELRPELVAAVRDCARAVSRDLGAGRF
The following text describes a protein:
Function:
Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity).
Subcellular Localization:
Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane.
Sequence:
MSMNVTNPNIAKTSMRGLTNFISDLRNSPSKENEEKRVTKEMAHIRKEFKENKNIDGYQRRKYVCKLVYMYMLGYELDFGHMEAVTLLSSTKFSEKQIGYIALGILLNEQHEMLPLIINSFKEDLLARSDYFQSLALAAICNIGGKEVAEFLSPLIQKLLIANTSSPMVKKRCALAILRMNRKHIGLVTPDSWVERLVSVLDEPDFGVLTSLMSLLIELASENPIGWEPAIPKVIHLLKKIIINKEFPKEYVYYHVTCPWLQVKLLKFLRYFPAPDDSQGGKVLGEILTAVFAQSESAKAGTVNHKNSLNAVLFEAINLIIHLDNDPVLLKQTSLLLGRFITVKETNIRYLGLEAMSHFASLSNETSIMIKKYQDTVLLSLKDSDISIRRRALDLLYGMCDKNTCKHIVAELLSYLQTADYAIREELVIKIANLAEKFASNYSWYVDVILQLITTAGDFVSDDIWFRVVKIVTNHEDIQAYAASTVFNALQSRNCHETLIKVGGYILGEFGHLIADNPQSSPLVQFNILHSKFNTCGAPTKALLLSTYAKFVNLFPELTQQTQEVFKQHQSYIDAEIQQRACEYLNLTSLNEDLMQTVLDVIPAFIDAKDNSNTTSNTANNSNMINSQDSKISSGGFNQSPQPSQQQQQQQPPQQQQAQLQQNVSSNGLDLLDPFGLGLGNQQQQQQQPVQQAQPVYQQQQQAESFSPVQSDTVSSFGQQQQQQQGGFSSPTIQASSSPISSGGSDPMQIKILASYKRLCLVSEGVLYEDSMLQVGLKSEYQSGQGRLMLYYGNSSAFPLTNFNVTLNSIAGLTLQPQSIAPVIQPKAQLQQPVTFSCTSEFTESPVITINFLTPGKPITITLRLPIVISKFFEPLRLSSGDFFARWKTISGKPLEIQEIFKSTKPIDIQSYNRVIQEGLNITVLKQVDPNPNNIVASCLFPFGSNGQPINSYIRIETNPQANMCRLTIRSQSATLTNTIKNLLISHLQ
The following text describes a protein:
Function:
Functions as a transcription repressor, probably via its interaction with histone deacetylase complexes. Involved in the functional recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus. Binds DNA, apparently without sequence-specificity, and bends bound double-stranded DNA. Binds phosphoinositol phosphates (phosphoinositol 3-phosphate, phosphoinositol 4-phosphate and phosphoinositol 5-phosphate) via the same basic sequence motif that mediates DNA binding and nuclear import.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MNGFSTEEDSREGPPAAPAAAPGYGQSCCLIEDGERCVRPAGNASFSKRVQKSISQKKLKLDIDKSVRHLYICDFHKNFIQSVRNKRKRKTSDDGGDSPEHDTDIPEVDLFQLQVNTLRRYKRHYKLQTRPGFNKAQLAETVSRHFRNIPVNEKETLAYFIYMVKSNKSRLDQKSEGGKQLE
The following text describes a protein:
Function:
Acts as a ligand for KLRK1.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MGSCSNAPVRAQICPGSLASARRAETAGRVISTEHESVPVEPARSRTCAPAQSPGAPAGSPAPLGPRAPRSPGWGVRRPGKPLPASPSIRRRFVPFGLLVLLYWPRGGASGQATGATSLFCEFSVKPQSSAGRPWCEVRGYVKRNLFLSYNCQSKEITLVGPMRTRMNDTGFRETQKETLNDLMEELQKKVRDIKAEIYPKNGSLDLHGEMKCVRGASRYTSASWQFAFNGQITHLFDSENGKWTVLQPAGRQFQGTLDSDRDVTNFLTKVSNGDCKSWMEYIMNHWDEKLETTVPQSRPQDMAPSGASGSAPSTWIFLLFLYCAILLGIHVGVL
The following text describes a protein:
Function:
Couples NMDA-sensitive glutamate receptor signaling to the nucleus and triggers long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes. Part of the cAMP response element-binding protein (CREB) shut-off signaling pathway. Stimulates outgrowth of olfactory axons and migration of gonadotropin-releasing hormone (GnRH) and luteinizing-hormone-releasing hormone (LHRH) neuronal cells.
Miscellaneous:
MISCELLANEOUS: Transport from dendrites to the nucleus is induced by NMDA receptor activation and results in a rapid stripping of synaptic contacts and a reduction of dendritic complexity (By similarity). KIF5C associates to its 3'-UTR mRNA in granules along dendritic shafts, suggesting that this protein may regulate its dendritic trafficking and local translation at postsynaptic sites.
Subcellular Localization:
Nucleus. Nucleus envelope. Nucleus membrane. Nucleus matrix. Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Cell projection, dendrite. Synapse. Synapse, synaptosome. Postsynaptic density. Membrane. Note=Found on the outside of the luteinizing-hormone-releasing hormone (LHRH) cell membrane and axons projecting from the olfactory pit and epithelium. Associates with transcriptionally active chromatin regions. Detected at the nuclear membranes of CA1 neurons. Cortical cytoskeleton. Localized in proximal apical dendrites. Colocalizes with CABP1 in dendrites and dendritic spines. Myristoylation is a prerequisite for extranuclear localization. Translocates from dendrites to the nucleus during NMDA receptor-dependent long-term potentiation (LTP) induction of synaptic transmission at Schaffer collateral/CA1 synapses of hippocampal primary neurons and in an importin-dependent manner (By similarity).
Sequence:
MGAAASRRRALRSEAMSSVAAKVRAARAFGEYLSQSHPENRNGADHLLADAYSGHDGSPEMQPAPQNKRRLSLVSNGRYEGSISDEAVSGKPAIEGPQPHVYTISREPALLPGSEAEAIELAVVKGRRQRERHPHHHSQPLRASPGSSREDISRPCQSWAGSRQGSKECPGCAQLVPGPSSRAFGLEQPPLPEAPGRHKKLERMYSVDGVSDDVPIRTWFPKENLFSFQTATTTMQAISVFRGYAERKRRKRENDSASVIQRNFRKHLRMVGSRRVKAQTFAERRERSFSRSWSDPTPMKADTSHDSRDSSDLQSSHCTLDEACEDLDWDTEKGLEAMACNTEGFLPPKVMLISSKVPKAEYIPTIIRRDDPSIIPILYDHEHATFEDILEEIEKKLNIYHKGAKIWKMLIFCQGGPGHLYLLKNKVATFAKVEKEEDMIHFWKRLSRLMSKVNPEPNVIHIMGCYILGNPNGEKLFQNLRTLMTPYKVTFESPLELSAQGKQMIETYFDFRLYRLWKSRQHSKLLDFDDVL
The following text describes a protein:
Function:
Acts as a repressor of the nagEBACD operon and acts both as an activator and a repressor for the transcription of the glmSU operon. Genetic interactions among priB, dam, lexA, nagC, polA, rdgB, rdgB, rep and uup link the PriA-PriB replication restart pathway to DNA double-strand break repair.
Sequence:
MTPGGQAQIGNVDLVKQLNSAAVYRLIDQYGPISRIQIAEQSQLAPASVTKITRQLIERGLIKEVDQQASTGGRRAISIVTETRNFHAIGVRLGRHDATITLFDLSSKVLAEEHYPLPERTQQTLEHALLNAIAQFIDSYQRKLRELIAISVILPGLVDPDSGKIHYMPHIQVENWGLVEALEERFKVTCFVGHDIRSLALAEHYFGASQDCEDSILVRVHRGTGAGIISNGRIFIGRNGNVGEIGHIQVEPLGERCHCGNFGCLETIAANAAIEQRVLNLLKQGYQSRVPLDDCTIKTICKAANKGDSLASEVIEYVGRHLGKTIAIAINLFNPQKIVIAGEITEADKVLLPAIESCINTQALKAFRTNLPVVRSELDHRSAIGAFALVKRAMLNGILLQHLLEN
The following text describes a protein:
Function:
Mitochondrial ribosome (mitoribosome) assembly factor. Binds at the interface of the head and body domains of the mitochondrial small ribosomal subunit (mt-SSU), occluding the mRNA channel and preventing compaction of the head domain towards the body. Probable inactive methyltransferase: retains the characteristic folding and ability to bind S-adenosyl-L-methionine, but it probably lost its methyltransferase activity.
Subcellular Localization:
Mitochondrion.
Sequence:
MGNAEKNSSDAPMQGGHLLFPALRQLRQGPHTRSPLRFLSSLHALPAKTRDSQRIEYVDLQETTALYGESGKEDDEIQGRFSGQKLVLSQELEEEDSGTGQELEAGQSSPGAVAVPAELSEAISKAVAGYSTRSLRHLTRQLSEGLHDHSRGWLSDPPKRVNLDTESSRGGLLASWKQASKARFPKYENWKNDEKDRRAPQYSDGQVAAYAAARMPATYAALVHVLEELKWQRPEFVPERVLDFGSGLGSALWAASSVWNTWPKQAVAVEQARGMTQLADVILRGAEDAPPVHRFRSLDALLKGKTGGHQHFDLVIAAYALGEQGTAEERKRVLRKLWARTKSILVIVEAGTPRGFEIVLEAREALIIREDKRVSRQRSSEKDVGAHVVAPCPHDGACPMSGTKQWCHFAQRLQRTGLQRVAKRADAALRAHEDEKFSYVVIQRGPRGSSAHMNVGEGASRPSAEAWATLDAGAASKNEGRGSRELGGRPPDGEERQAVGQPAESSAAQIDTDDTQRKFVGSVHLKRADIAMNGLPEAEPSVVADAESSSEIGAIDNETTEGRETDGVENGKGSRPPARHFPRQWARLISPPRQRHGHVILDLCCPGEERTGNLERWTVSKGLGGELGSKERYSNARKARWGSRWHWDIG
The following text describes a protein:
Function:
Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA.
Subcellular Localization:
Nucleus.
Sequence:
MAALVNYSSSDSDTDVSSNEIENAPSRPKLSLPEEFENKYRSSPRLLDDPVFHQGRKRTFAHVEGAWTTQSFIEVKLTRSLSSQLQQILKSEIAIEERDDGTPKSNDWVPLFFSELGLAKPLHLTLSSMDCLDYESKESFRVQWKQTLSSAHFQPFSIQLGKVLYLVNEQQTRGFLAWRIHFDEHHLKPLCQKINDLNISFGMQPLRPDFIPHISFCWRKTNPKECEAWSSAISLYEVPSKFDNLVSAIEDLLKSNNTNIPVKSVKLSTGGYLDTLELKEPY
The following text describes a protein:
Function:
Catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. Is involved in L-lyxose utilization via xylulose, and may also be involved in the utilization of 2,3-diketo-L-gulonate.
Sequence:
MTQYWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQGKGLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHDYLRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEINHALPPVVGSAEICGEITAQTAALTGLKAGTPVVGGLFDVVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLRDGEAHPYVYGRYVNDGEFIVHEASPTSSGNLEWFTAQWGEISFDEINQAVASLPKAGGDLFFLPFLYGSNAGLEMTSGFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRERFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQRDLRHPVRTLLPDMTAHQLYQKKYQRYQHLIAALQGFHARIKEHTL
The following text describes a protein:
Function:
Catalyzes the desulfonation of aliphatic sulfonates.
Sequence:
MSQSKSNILWFLPTHGDGRYLGTATGGREVNFNYLRQIAQAADQLGYFGVLLPTGRSCEDSWIVASSVAPFTERLRYLVAVRPGLQSPSVAARMTATLDRITNGRLLINVVTGGDPVENKGDGIFLGHDERYEVTREFLNVYSDLLGGKAVNVEGKHIRIEDGKLLFPPVQSPRPPLYFGGSSDAGIDVAVDTVDKYLTWGEPPAQVAEKIARVREVANARGRKLSFGIRLHVIVRETNEEAWSAANELIKHVSDDTIARAQRNFARMDSVGQQRMAQLHGGKRDKLEISPNLWAGVGLVRGGAGTALVGDAQTVAARIKEYQDIGIDTFIMSGYPHLEEAYRFAELVFPLLSLDHGSNVTRLHHNSGPFGETVGNDYRPSRLASQS
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
EKPTLVLDMDKTLIHAHKATASLKLFSGKTLPLQRYLVAKRLGVDTFLNEMSQIYEIVVFTRAVKPYADRILDRLNPAGNLFTHRLYRDSCSPKEVGGRKVVKDFSRLGRDLRHTVIVDDKPESFCLQPSNGIVIRAFKNRKGHKYDELKKISNLLKEIARAEDVRQALEK
The following text describes a protein:
Function:
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MLNVVRAAAVLILVQSIHSTDPNDFLNRKYYSSSVLGLVKLLKMEQEFMVNFSIYANILQEKVDNLNIFLDALKRPNHKTHNEREKFVSNPLNAFGLIRRLNQDWPKLQNYTQKPLGLEQLTAMQDIVSAAPESFDMNEKLKAMHRIETTYDLQPKDIAKGLLQRTEFNYRLLFRDCLALAYHKFEIGEFKRSLLWFQEALKLSTDGSLEIMNRLKEIELKGFATAVAKRSIYLSNQGLTNETIDDMANSQLQDAKLMDLEQLISSELKQWINDDSTTPPTDHNLGCRGLFPKKSNLVCRYNSSTNAFLKLAPLKMEEISRDPYIVMFHEVISDKDIEEMKGEITEMENGWTSLGDPKEIVSRVYWIRKESSFSKRINQRISDMTGFKLEEFPAIQLANFGVGGYFKPHYDFYTDRLKEVDVNNTLGDRIGSIIFYAGEVSQGGQTVFPDLKVAVEPKKGNALFWFNAFDDSTPDPRSLHSVCPVLVGSRWTITKWLHYAPQLFVKPCSPRVHLE
The following text describes a protein:
Function:
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. This sigma factor is responsible for the expression of the levanase operon. The open complex (sigma-54 and core RNA polymerase) serves as the receptor for receipt of the melting signal from the remotely bound activator protein LevR for the expression of the levanase operon. Associates with the RNAP core only in stationary phase cells.
Sequence:
MDMKLQQVQVLKPQLTQELRQAITLLGYHSAELAEYIDELSLENPLIERKETDTPPLSYHKTNKNRMNAQEAGLQLSNPQKTLQDALKQQSLDMNLTNTEKKIFNYLIHSLDSNGYLEEDIEEAARRLSVSAKEAEAVLAKLQSLEPAGIGARSLQECILLQLQRLPNRNEQAEMLVSAHFDAFAQKKWKTLSVETGIPLHTIQDISDDIAALHPRPGLLFARPEQDVYIEPDIFITVKNGHIAAELNTRSFPEIDLHPQYRTLLSSGSCQDTVSYLSAKYQEWRWLSRALRQRKQTITRIINELITRQKDFFLKGRSAMKPLTLREVADCLSLHESTVSRAIKGKTIQTPYGLFEMKLFFSAKAEASGDGDASNYAVKTHLENLINQEDKTKPLSDQKLVDLLYEQHGIQISRRTVAKYRDQMNIPSSAARKRYK
The following text describes a protein:
Function:
Transports CMP-sialic acid from the cytosol into the Golgi apparatus, functioning as an antiporter that exchanges CMP-sialic acid for CMP. Binds both CMP-sialic acid and free CMP, but has higher affinity for free CMP (By similarity). Also able to exchange CMP-sialic acid for AMP and UMP (By similarity). Also mediates the transport of CDP-ribitol (By similarity).
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MAQARENVSLFFKLYCLAVMTLVAAAYTVALRYTRTTAKELYFSTTAVCVTEVIKLLISVGLLAKETGSLGRFKASLSENVLGSPKELMKLSVPSLVYAVQNNMAFLALSNLDAAVYQVTYQLKIPCTALCTVLMLNRTLSKLQWVSVFMLCGGVILVQWKPAQATKVVVEQSPLLGFGAIAIAVLCSGFAGVYFEKVLKSSDTSLWVRNIQMYLSGIVVTLVGTYLSDGAEIKEKGFFYGYTYYVWFVIFLASVGGLYTSVVVKYTDNIMKGFSAAAAIVLSTIASVMLFGLQITLSFAMGALLVCISIYLYGLPRQDTTCIQQEATSKERVIGV
The following text describes a protein:
Function:
The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.
Subcellular Localization:
Secreted.
Domain:
The N- and C-terminal barrels adopt an identical fold despite having only 13% of conserved residues; The N-terminal region may be exposed to the interior of the granule, whereas the C-terminal portion may be embedded in the membrane. During phagocytosis and degranulation, proteases may be released and activated and cleave BPI at the junction of the N- and C-terminal portions of the molecule, providing controlled release of the N-terminal antibacterial fragment when bacteria are ingested.
Sequence:
MTHVLTGIFERGGKEEIMSACSFLLLLSISSLCLNANPGIKVKITEEGLHFGMQVGLEFLKQRLKEAIFEDWHGEDTSGLSGFNYTVSKIRIQHVQFPGKSLFLIPATGMKLLVHDASAIATADWRFSTWLLRSSGKLKVCLTGVSISAAAKVSKDEDGHPKLLLENCHGNVDGIDIQLDDTSRWFYRLLVNLLERPLRNNFNLNLCPIIYSEIERFNAELKQHQNRIQLDAFAVIDYSLVKPPSISLASISVDFKGAVYSALNRTQLSFEPDPFHLPNTRDFMLYIGISEYFFRSASLAYYTSGAFDVSIEKELSAYFRLTTETFNNIIPTIAFYYGVSNPVMMNLTVTAAPVISLHNGRFLLDLSGSMDVLVVQTNFTTNSMFTLNITAKTHINMIIFEKNLIPTLCLDSFDLALAHSTIGFFKASIMKNFMSYILQKGVIPAVNVNLKDGIPLPVLDTMVLVQPTITMYQGYLLISTDAKLKPTNIWKHNHIRTF