lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Substrate and inhibitor of the cyclin-dependent protein kinase CDC28. Its activity could be important for faithful segregation of chromosomes to daughter cells. It acts in response to a signal from a post-start checkpoint.
Miscellaneous:
MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MTPSTPPRSRGTRYLAQPSGNTSSSALMQGQKTPQKPSQNLVPVTPSTTKSFKNAPLLAPPNSNMGMTSPFNGLTSPQRSPFPKSSVKRTLFQFESHDNGTVREEQEPLGRVNRILFPTQQNVDIDAAEEEEEGEVLLPPSRPTSARQLHLSLERDEFDQTHRKKIIKDVPGTPSDKVITFELAKNWNNNSPKNDARSQESEDEEDIIINPVRVGKNPFASDELVTQEIRNERKRAMLRENPDIEDVITYVNKKGEVVEKRRLTDEEKRRFKPKALFQSRDQEH
The following text describes a protein:
Function:
Binds to the long stretches of ssDNA of the viral DNA replication intermediates created during the protein-primed mechanism of replication of the viral genome and attaches the viral DNA to the membrane of the infected cells. Required for the redistribution of replicating viral DNA from the initial replication site to membrane-associated sites surrounding the nucleoid. Required for the second pull step of DNA ejection.
Subcellular Localization:
Host cell membrane; Single-pass membrane protein.
Sequence:
MEAILMIGVLALCVIFLLSGRNNKKKQEARELEDYLEDLNKRVVQRTQILSELNEVISNRSIDKTVNLSACEVAVLDLYEQSNIRIPSDIIEDLVNQRLQSEQEVLNYIETQRTYWKLENQKKLYRGSLK
The following text describes a protein:
Function:
Plays an essential role in the initiation and regulation of chromosomal replication. ATP-DnaA binds to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex once per cell cycle. Binds the DnaA box (a 9 base pair repeat at the origin) and separates the double-stranded (ds)DNA. Forms a right-handed helical filament on oriC DNA; dsDNA binds to the exterior of the filament while single-stranded (ss)DNA is stabiized in the filament's interior. The ATP-DnaA-oriC complex binds and stabilizes one strand of the AT-rich DNA unwinding element (DUE), permitting loading of DNA polymerase. After initiation quickly degrades to an ADP-DnaA complex that is not apt for DNA replication. Binds acidic phospholipids.
Subcellular Localization:
Cytoplasm.
Domain:
Domain I is involved in oligomerization and binding regulators, domain II is flexibile and of varying length in different bacteria, domain III forms the AAA+ region, while domain IV binds dsDNA.
Sequence:
MRAWEEFLLLQEKEIGVDTVNKWLRSLKVLCFDACNLYLEAKDSFQVTWFEEHIRHKVKASLINNNGKPIRVRVTSLDKSTPFKETQIQQEKTAYFTMKYGDIDPNMSFANFLVTPENDLPVRILQEFAKVSEQGKGFPFNPIYLFGPESSGKTHLMQAAVGGLREAGVKTLYVTSELFTEHLVSAIRSGEMQRFRAFYRNVEALFIEDIEVLSGKGATQEEFFHTFNSLHTEGKLIVISSTFAPGDLKAMEERLISRFEWGISIPVSPLIREGLKSFLERRTEKLNIRIEETALDFLIQALSSHVKSLLHALTTLAKRVAYKKLSHQMLYQGDIEALLHDVLQAAESIRLTPSGIVRATAQYYGVSPESVLGRSQSREYVLPRQVAMFLCRQKLSLSYVKIGEVFSRDHSTVISSIRAISQKLEEDDRECDVSRAIQELTKRLSSAYQSLDFIED
The following text describes a protein:
Function:
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
Subcellular Localization:
Cytoplasm.
Sequence:
MTNTQFYITNFLNHIKLQKGDSSHTLRAYKNDLEEFFNFAKVEPEKVEPIVIRGFISEQILKGKSKTTVARKLSTLRSFFSYLYSEGFIKINPARVVSSVKIKRALPKFLTVDDAFKLVEAPSEDKFTVQRDKAILELFYSSGIRVSELCGLNLEDLDLKEGLIKVRGKGKKERIVPVGQKAKEALKKYLAIRQILRIKKKLSLDETPLFINNRGQRISDRQVRRIVEKYAKFIGVLEKIGPHTLRHTFASHLLMEGADLRVIQELLGHASLSTTQIYTHVDLKHLIEVYDKSHPLSKEDE
The following text describes a protein:
Function:
Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MFVEHNLIKNIKIFTLAFTLTVVLIQLSRFISPLAIIHSSYIFLAWMPLCVMLSILFIFGWRGVVPVLCGMFCTNLWNFHLSFLQTAVMLGSQTFVVLCACAILRWQLGTRWRYGLTSRYVWQRLFWLGLVTPIGIKCSMYLVGSFFDFPLKISTFFGDADAIFTVVDLLSLFTAVLIYNMLFYYLTRMIVSPHFAQILWRRDIAPSLGKEKRAFTLSWLAALSVLLLLLCTPYENDFIAGYLVPVFFIIFTLGVGKLRYPFLNLTWAVSTLCLLNYNQNFLQGVETEYSLAFILAVLISFSVCLLYMVRIYHRSEWLNRRWHLQALTDPLTLLPNFRALEQAPEQEAGKSFCCLRIDNLEFMSRHYGLMMRVHCIRSICRTLLPLMQENEKLYQLPGSELLLVLSGPETEGRLQHMVNILNSRQIHWNNTGLDMGYGAAWGRFDGNQETLQPLLGQLSWLAEQSCAHHHVLALDSREEMVSGQTTKQVLLLNTIRTALDQGDLLLYAQPIRNKEGEGYDEILARLKYDGGIMTPDKFLPLIAQFNLSARFDLQVLESLLKWLATHPCDKKGPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQLHKFGFRIAIDDFGTGYANYERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYLIGRPQPLAD
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. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Subcellular Localization:
Nucleus.
Sequence:
MSRGAPGGRGGGGWRGGRGGGRGGGNMGMGLDIPEGLVITYQEIPLYPAFDLPPFKEPTELENQMFDIYSKFIETMKSSPFFLEKPVVKKDLERYSDKYIAAKPISRMLHRTATDLTFFPEELHSVKDTTKKMAMPKLVSKDLDLKHLETLELAEAAQSKKEGGDAIGVNEDETLPEDEEYDEDIEEDDNDYLIDYYEDDLDVLGGDGSEGGDYDY
The following text describes a protein:
Function:
Transcription factor that binds to target promoter sequences and activates transcription upon il6st/gp130 stimulation. Mediates ventralization of embryos, at least in part via inhibition of smad2 signaling. Required for hairy2 to induce dll1/delta1 and promote neural crest cell proliferation and differentiation. Involved in TGFbeta-mediated mesoderm induction in early embryos, acting downstream of map3k7/tak1 and nlk.2.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAFAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEEGRLLQTAAAAAQQGGPASHPNAAVVTEKQQMLEQHLQDVRKKVQDLEQKMKVVENLQDDFDFNYKTLKSQSDLSELNGNNQSVTRQKMQQLEQMLTALDQLRRTIISDLASLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQIRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTNKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGITFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHQEPTDPGTAPYLKTKFICVTPTTCSSTLDLPMSPRTLDSLMQFPGEGADSSAGNQFETLTFDMELTSECASSPM
The following text describes a protein:
Function:
Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Sequence:
MEDAGEHLRCNDNVNDEERLPLEFMIGNSTSTAELQPPPPFLVKTYKVVEDPTTDGVISWNEYGTGFVVWQPAEFARDLLPTLFKHCNFSSFVRQLNTYGFRKVTTIRWEFSNEMFRKGQRELMSNIRRRKSQHWSHNKSNHQVVPTTTMVNQEGHQRIGIDHHHEDQQSSATSSSFVYTALLDENKCLKNENELLSCELGKTKKKCKQLMELVERYRGEDEDATDESDDEEDEGLKLFGVKLE
The following text describes a protein:
Function:
Reversible hydration of carbon dioxide.
Sequence:
MHIVCMKDGLSPDSAAKQEDGYAVLGFFINAKDDQDTSEAWTTLTSFLPNIKEVDQMVNADQNISINGLIGNVDLSKYYRYMGSLTTPQCSEAVVWTLFHEPIPVNSTLIQMFPLMTSFVDIYRPTQDLNGRQVYTSASSVPSHSWCYEGHLCDYAPSNWSFLPEAKCGGEQQSPINIDTQSTTEDESLGAFTFLNFDDKHVIESITNTGHSVQCNINGSVEVSGGGLPHVYTVLQFHFHWGSVASHGSEHLLDSKSFPMEMHIVCIRKDLNMSEALAHSDGLAVLGFFIEAPQTSKSGSHSSSTSDSSGTTTPPTSSTSDMEAWTKLTNYLDQIQTVNSQVPFSDEISIDDLLGNVDRHSYFRYNGSLTTPQCNEAVVWTVFKESIKVNQNLMTRFPESTGYENIYRPQQEQHSRTILSTKVSAGSSPQVKTARLFYPLLVFVWALLY
The following text describes a protein:
Function:
No chitinase activity. Essential for normal plant growth and development. Regulates cell expansion extent and differentiation at least in roots and hypocotyls. Prevents lignin accumulation in the pith. May modulate ethylene-mediated regulation during development. Probably required to establish thermotolerance acclimation. Plays a role for controlled anisotropic cell expansion in the regulation of waving during root gravitropism and thigmotropism. Involved in the root system architecture adaptation to multiple environmental conditions such as nitrate. Contributes to salt tolerance and possibly to drought by preventing the overaccumulation of sodium ions.
Subcellular Localization:
Secreted.
Sequence:
MVTIRSGSIVILVLLAVSFLALVANGEDKTIKVKKVRGNKVCTQGWECSWWSKYCCNQTISDYFQVYQFEQLFSKRNTPIAHAVGFWDYQSFITAAALFEPLGFGTTGGKLMGQKEMAAFLGHVASKTSCGYGVATGGPLAWGLCYNREMSPMQSYCDESWKFKYPCSPGAEYYGRGALPIYWNFNYGAAGEALKADLLNHPEYIEQNATLAFQAAIWRWMTPIKRAQPSAHDIFVGNWKPTKNDTLSKRGPTFGSTMNVLYGEYTCGQGSIDPMNNIISHYLYFLDLMGIGREDAGPNDELSCAEQKPFNPSTVPSSSSS
The following text describes a protein:
Function:
Endonuclease of the viral base excision repair system that catalyzes DNA cleavage reaction at the apurinic or apyrimidinic sites (AP sites). Cleaves phosphodiester bonds on the 5' side of AP sites. In addition to endonuclease activity, the AP endonuclease has a proofreading 3'-5' exonuclease activity that is considerably more efficient in the elimination of a mismatch than in that of a correctly paired base. Displays 3'-phosphatase and 3'-repair diesterase activities. The single nucleotide gaps generated by the AP endonuclease are filled by the viral repair DNA polymerase X and the DNA ligase (Probable).
Miscellaneous:
MISCELLANEOUS: Consistent with its intracellular location, ASFV encodes its own replicative DNA polymerase and three base excision repair enzymes: a class II AP endonuclease, the repair polymerase Pol X, and an ATP-dependent DNA ligase.
Subcellular Localization:
Host nucleus. Host cytoplasm. Virion. Note=The early enzyme is localized in the nucleus and the cytoplasm, while the late protein is found only in the cytoplasm. Found in association with viral nucleoid.
Sequence:
MFGAFVSHRLWSDSGCTTTCITNSIANYVAFGEQIGFPFKSAQVFIAGPRKAVINIQEDDKVELLKMIVKHNLWVVAHGTYLDVPWSRRSAFVTHFIQQELLICKEVGIKGLVLHLGAVEPELIVEGLKKIKPVEGVVIYLETPHNKHHTYKYSTMEQIKELFLRIRNTRLKQIGLCIDTAHIWSSGVNISSYNDAGQWLRSLENIHSVIPPSHIMFHLNDAATECGSGIDRHASLFEGMIWKSYSHKIKKSGLYCFVEYITRHQCPAILERNLGSSMQLQTALTAEFTTLKSLLK
The following text describes a protein:
Function:
Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code.
Subcellular Localization:
Nucleus.
Domain:
The JmjC domain mediates the demethylation activity.
Sequence:
MSTAVETGSSPAKSNSNNSSSGGNNNNGNGNLSPNAKGVQRRQLRERKQRKLYLEEWSLGDEDGEGTRGFSVAEKLESSKFAQAGMVREMRGCDLTVAFLQQHGFNIPLLFRDKAGLGLRMPDPQEFTVNDVRLCVGSRRLLDVMDVNTQKNLQMTMKEWQQYYDSPQKDRLLNVISLEFSHTRLDRFVQSPEIVRQIDWVDVVWPKQLKDAQREGTNLLGGMMYPKVQKYCLMSVKNCYTDFHIDFGGTSVWYHILRGSKVFWLIPPTDRNLQLYEKWVLSGKQADIFFGDTVEKCARVYLTAGNTFFIPTGWIHAVYTPTQSLVFGGNFLHSFGIVKQLKTASVEDSTKVPQKFRYPFFTEMLWYVLARYVHTLLGHSHLEGEASLSEDEMAARPHTHLTHHELFGLKEIVMYLYDLPPQKKNVPSLVLDPVALIKDVRSLVERHCKDQQDLAITGVSVLKSPPGSQPPFLLYDRTRVKQEIKQEIARKNAEVIREQQQLEAGRAREAESDTSQSTGVGSVIGMGAGVEYSNGVMKKEQLENGSGVTVGGHGSQPEATFALPTDTLKYRPPKKMHLATALVAAAASSSSGGGGPVAGVGGSAVVGSSHSPTGGGVGPVTGAGGAISVIATSSSYIEGGQVGGILNMDNCHSPEGGGAKLSPNLTGTGQPRRRRTRCKNCAACQRSDCGTCPFCMDMVKFGGPGRAKQTCMMRQCLSPMLPVTAQCVYCHLDGWRQTPVSPQTKQLASADGPSALMECSVCYEIAHPDCALSQLDGTEDAADAKGIVNEDLPNSWECPSCCRSGKNYDYKPRHFRARQKSSEVRRVSVSHGQGGAEGHADGNTLLPPPVGQYNDFVFTSESEMESGTVSGHMTHWKHGMKRHHQLEVKTERNNSCDTPSPGISPNAIGGDSKVGKRRKSDDGTSVSSSMHESNDAPCGSSAEGAGGAGNANVSTNQWSGSGGGGGSRKKNSIRSQLAQQMLNSSTRVLKKPQYVVRPASGTGSSSSSGNGGSASATNGISNGSNQSGANSCGAGNGERGTNNGGLSGSNGLGNQHYSSSQNLALDPTVLKIIFRYLPQDTLVTCCSVCKVWSNAAVDPDLWKKMNCSEHKMSASLLTAIVRRQPEHLILDWTQIAKRQLAWLVARLPALKNLSLQNCPIQAVLALHTCLCPPLQTLDLSFVRGLNDAAIRDILSPPKDSRPGLSDSKTRLRDLKVMKLAGTDISDVAVRYITQSLPYLRHLDLSSCQRITDAGVAQIGTSTTATARLTELNLSACRLVSENALEHLAKCEGLIWLDLRHVPQVSTQSVIRFASNSKHDLCVRDIKLVERRRRNSTTANRSWHHD
The following text describes a protein:
Function:
Deubiquitinating enzyme that may play a role in the ubiquitin-dependent regulation of different cellular processes.
Sequence:
MEGSEDEEAEAGGPLQQLVKRQRREKRELQAKIQGMKNAVPKNDKKRRKQLAEEVAKLEAELEQKHKEELKQLKEAMPEQNKIDSIADGVANFELEGREQQIQHPRISKAQKRREKKAALEKEREERIAEAEIENLTGARHLESQKLASLLAARHLEIKQIPSDGHCMYRAIEDQLKDHHNSWTVATLRNQTAKYIHSHFDDFLPFLTNPNTGDMYSKEEFEKYCDDIANTAAWGGQLELRALSHILQTPIEVVQMDSPSIIVGEEYSGKPIILVYMRHAYGLGEHYNSVKLLTDATTENGS
The following text describes a protein:
Function:
Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia and flagellar axoneme. Forms filamentous polymers in the walls of ciliary and flagellar microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, flagellum axoneme.
Sequence:
MIQRPRQKFVEPEWKHANQKLYACSEVERSRAEKLVDDVEVVISETRKLTANVQRDVNRKLEQRVNDMEHWETEINFHLDRVKVQIDSLEATAGRLNKAREAMKEPIHINDACIAAREQRKGIELVHDEAEKELLKEEEVLRGVVLLYNRTDEQLQEQLRLARKMRYQLEKDIQNRSEAVNIDRENIELKNHQFNIQLNNLSQFAARRPTSVDEWESLTNDRINQSNQIVKNCTDLQSLVSGILKQTSEDMASQKKLTDEALSRRIYDVRNAKDKLEEHLAKLRQQITETEINMEKLLKAIEEKKPAKLLAAKRLENRCQRASIELCNDAVQYKLMEESMMIEQSVEKLEQAYEKAKFCLKNLRQKEVDLEEEIALKVMTLAIDASEVECMRKSLLIREY
The following text describes a protein:
Function:
Involved in the tethering and targeting of pkc-3 to modulate the intracellular distribution of the kinase. The complex formed with pkc-3 complexes are likely to be involved in assembly, maintenance, and/or regulation of protein complexes that execute asymmetric and/or polarized cell functions.
Miscellaneous:
MISCELLANEOUS: [Isoform b]: Produced by alternative splicing; MISCELLANEOUS: [Isoform c]: Produced by alternative initiation at Met-45 of isoform a.
Subcellular Localization:
Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Note=Expressed at the inner surface of the plasma membrane at the cell periphery (which includes a region corresponding to plasma membrane and/or actin cortical cytoskeleton) in early embryos. Tightly associated with organelles and/or cytoskeletal structures with some diffuse expression in the cytoplasm. Differentially routed to lateral junctions between polarized cells.
Domain:
The PID domain (phosphotyrosine interaction domain) of isoform a and isoform c is capable of binding residues 212-224 of pkc-3.
Sequence:
MSASQGNVFTRGLSRISRRKKKTKSIQNSLVSEQQPSFDAAIVPMPIPNDKSSIFSKGMDRLRRSLRLPKKRRDRSHDRHLSPDVTGGSKTEQWQPDEGAVRTGTCCFNVKYLGSVEVYESRGMQVCEGALKSLKASRRKPVKAVLYVSGDGLRVVDQGNSRGLLVDQTIEKVSFCAPDRQTDKGFAYICRDGASRRWMCHGFLATKETGERLSHAVGCAFSICLEKKKRRDEETAQVNVQSAQESTSSTPPKDIFHPNWEDNTSEGTSTQNPSNSRSNLAYQSFRKHVSIEDRYLDPQSVIINEVPASNHMDEIRRISKPRPTGNPALFLRQGSLRAPPDMPSSSDQFKRNMSLRTVSNNPTERSPEKKSFGTQLYNEPIYEGDEDPLGLGITPPVVTKTSGSLSNNGLDGINLNWKSIPAPVHQMQQHNANGDFVAAWPQNTIEKPTVGPLDKLQKQFEDIKLISISSGENTPTTRSKADEWLDDVLRVSMSMSPTSPSSDPPSTSSYSVLPKSGPPPAHAPPPLPVRQAVSNGSPSIYQQQLQQANSTRNSPAGINWNSSPNPMKISQPPAKPVDPFDVQWSRLAVNNTH
The following text describes a protein:
Function:
Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MATPGPDELLKSHHILAKRREIRKREMEGVVVFADENSILRTELFDEVQKVKSVGAMPVGVLGEDEGTNEMFLQAPPGCLPLTAGCYASSPVIASGEPEFAPAPFCRCPSDPRPPPPPSPSIRSLLPRAGLKGNRKGEKSERREREREGGGRRERRYDTWDPYVSGSHNSM
The following text describes a protein:
Function:
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton. Nucleus matrix. Note=Throughout the cytoplasm (but not on the cytoplasmic cables) and major component of the cortical actin cytoskeleton.
Sequence:
MSRSGVAVADESIQAFNDLKLGMKYKFVLFSLNDAKTEIVVKETSSDPSYDAFLEKLPENDCLYAVYDFEYQISESEGKRSKIVFFTWSPDTASVRPKMVYASSKDALKRALNGVAIEIQGTDFSEVSYEAVLEKVSRGAGSH
The following text describes a protein:
Function:
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Sequence:
MLTLESLKLDMGKVKEIISGFIRGMVAGSRAEGIVLGISGGVDSAVLTKLCVDALGSERVFGLILPDTRVTPEEDIKDAIDLAESLKIKYWRRDIDDIIDSYERSEFYVHDHKLALGNLRARVRMSLLYYVANSRNLLVAGSGDRSEILIGYFTKYGDGGADLLPIGDLYKTQVRWMAEWLGLPERIARKPSSPRLWEGQMAEKELGIPYERIDLILHGLFDLRIDIDSLREEFGSDVDRVMEMHSRSAHKRTMPPIARVRI
The following text describes a protein:
Function:
Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking.
Subcellular Localization:
Preautophagosomal structure membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9-containing vesicles, thereby enabling growth into autophagosomes.
Sequence:
MDRDSPFADPDRSDPLPAPSNTLKASIFAQSRIVHPSTSVYNQFGRHRHDDIGQESFHEGIQPSVASLANLQGSYTAKSIHPHHSAIGLRNSSYDDHGDDADEQDPEDLLSDEELGLIAGDARNPSASLSYASNRSRKRRTNPSDPRSRASAVGGLSAKQKALWMWANVDNLDAFLQEVYAYYVGRGAICIALSRSLNLLTVAFVICFSTFLFGCIDYSSIRHDGQLSDVIVGHCVAGFSPFATLVVVLLLAAFGWQAVQFVLGLSRLRAMHRFYEQLLGIPDADVQSIPWHEVVNRLSALRDQHPTTSLSSADEMELGQRTSSSLRRSHPQPLDAHDVANRIMRQENYLIALFNENILDLSVPGLRSRSPSLTRSLEWNLHFCLLGFLFDSNGQVRHAFLSERYRADLIEGLRRRFLFMAVVNAIFAPFIVLYLLLYSFFRYFEEYHKDPSNLGSRQYTQYARWKFREFNELPHLFRRRCRTSYVAASKYMDQFPKEKTAIVARFVAFVAGSFTAVLLLASVMDPDVFVHFNITPQRNVLFYIGVFGAILAVARGMIPDEHVVFEPEAMLREVIEQTHYLPQDWKGRFHSAQVHQAFGQLYTLKIYIFLQELLSVVTTPFVLWLSLPACAPDLIDFLRKYTVHVDGLGHVCSFAVFDFARQPTASTMGGAAAKGIHRQQQQQQQQQQQSGGSGRTRAPRNGMSQAKMEQSILGFRANHPDWDPAAHASTASIQRVDDDAGATTLQYGHGDGRSTSDAPTGVGAGAKVKDLIDHIYRGSGGAAGASRW
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:
MARPALVLDLDDCLISKNAKVTDFVAGGYDIGMRPGLIPFLESMAAIYDLYVFSCSAEFYCSGIVDNINKRLSSGRILYYCCRDNCKSYRDPSIDKVVSLKDIRSVPMVDGDCKRTVWLDDDEYYWLFQPNNGFVVPRYDGEDEEDRVLEGFVPLLTALAKLDDFAPAIEGLRTGECKLVDGELKFGEIDGEIVLEGLRRFYVREWFINAMPRQRVYNIKKLEDPEFKKQVMGVKHNGGLESESEGKCVISEASWEALKGVIKAECQQIRLEMEYKENKGKKEVLEAKAEESLKALIGVEECLHSGVYSKDYLQSAKSIIQKRPIIQKRPIYMNFDV
The following text describes a protein:
Function:
Required for the polymorphic O-glycosylation of the serine-rich repeat protein Srr2. A stabilizing protein that is part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat proteins, probably Srr2 in this organism. The GtfA-GtfB (Gtf1-Gtf2 in this bacteria) complex adds GlcNAc from UDP-GlcNAc to Srr2 substrate, attaching the first sugar residue. Stabilizes the glycosylation activity of GtfA in vivo. Upon expression in a gtfB deletion mutant of S.parasanguis, GtfB confers incorrect glycosylation and partial complementation of a biofilm formation defect, while GtfA/GtfB restores correct expression of serine-rich repeat protein Fap1 and completely restores a biofilm formation defect in a S.parasanguis double gtfA-gtfB deletion.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MIILFDFFDKKSKDLYYSLITSGLHGNAVVINDDGFLPQNINSPYSFFCNMEGKNGNPLYFNQVPLPDLWEIKGNNIEAEIWDFSIKRAKIFYQEPKYKRQVKNIDWFDNNKKVRYTDHYNRFGWCFARTHFDKNQNVTTKSYFDKDGKEVIVENFRTGVIILNWLNKDYFFDNRVAFLNFYFSLMGWNLSRIWYNSLSTPFFVSYRMTYPGEDILFWQEDIEDTIPANMRVLLESTNTRTQKVIVQKKNTYHKIKSMLPKEQQEKIGYLGFIYPNKKNNKGRKDIFILTNSDQIEHLEVLVHHLSDYHFHIAAYTEMSFKLMSFSQEQNVTLYPNISRTDLDNLFEICDIYFDINHGNEVDDVIRRAFEYNHLIFAFDNTCHNRELVLDSNIISHTTCEQLINLMKNLSGSIMYLLEQQREQTSNETKERYKEILGGYGNA
The following text describes a protein:
Function:
Key component of the ribosome quality control system (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes and their subsequent degradation. RqcH recruits Ala-charged tRNA, and with RqcP directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal alanine extensions (Ala tail). The Ala tail promotes nascent chain degradation. RqcP is associated with the translocation-like movement of the peptidyl-tRNA from the A-site into the P-site. RqcH, RqcP and charged tRNA(Ala) are necessary and sufficient to add an Ala tail to a model stalled nascent peptide; does not add Val.
Miscellaneous:
MISCELLANEOUS: Activity of this protein is best tested in a clpP or ssrA deletion mutant; ssrA (tmRNA) encodes the SsrA tag added to nascent proteins in stalled ribosomes by trans-translation, which targets the nascent protein for degradation.
Sequence:
MRLDKFLKVSRLIKRRTLAKEVADQGRISINGNQAKASSDVKPGDELTVRFGQKLVTVQVNELKDTTKKEEAANMYTILKEEKLGE
The following text describes a protein:
Function:
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein.
Sequence:
MHSRPVFLRALRLRQQPLPARRFLPPQSLRPLSSTARLLDESKKSEQQSQKKKSTNDEPITPRSPWAVFTQVLKEEIEKNKGWQDNVKQLQGDVDKFADSAAMKRAKDVYEKTRLTNLIKNNPRIQSAVGDLQKAGISVHDAVQHALADSEVLKAISAATNRFVSAASSATAPIRDTKAYKLMAESLEEAFEDESGVGSRYGGYEEKEARRKKREMRAKKAGRAAIKRVEENPEAGEALVLSDKPESVSRLAFIKESPTYQRMMENYYESDSPFVSAIRTIGTKVGSLFEENETAQVIRAMKALDPNFRMDRWTGELREYIVPEVVDAYLSADRESLKAWCGEATFNVLWATMGQFIKQGLVSDSKILDIKHVDIAHGKMLENNIPVFVITFATQEQLLFRSAKTGKVVVGSEDDVEQCRYAMVITRLESELENELTGGWKVVEMARRGARGGL
The following text describes a protein:
Function:
Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA.
Sequence:
MRGGEQVDREFDVSKARVLEQLQLCLDNSKKGALDAPIEALLNFINELDDYVTTSSCSGRIALFCEQQDARKRTGTWLLASHDVVTVEAAAAAYQDERIRDSQGPVMFKFEPFVLHVQCRTLERARDFLKTALDCGLRLWMASLCMCAPCISNSGLVLGKKFMVAVRTTLKLESPVAYDGQRLVDEAYIACLVQMANDMFAENLQRIARFETGVRAMVARQAEQATRALEREHARQARKHSQMAVAPAAKPTSTPAEAEEPILSLDF
The following text describes a protein:
Function:
Probable aminotransferase.
Sequence:
MPRIRKPPSRSLPEPSAALANTTTRNLWLHFARHGAGIQHPVIVRGDGVTIFDDRGKSYLDALSGLFVVQVGYGRAELAEAAARQAGTLGYFPLWGYATPPAIELAERLARYAPGDLNRVFFTSGGTEAVETAWKVAKQYFKLTGKPGKQKVISRSIAYHGTTQGALAITGLPLFKAPFEPLTPGGFRVPNTNFYRAPLHTDLKEFGRWAADRIAEAIEFEGPDTVAAVFLEPVQNAGGCIPAPPGYFERVREICDRYDVLLVSDEVICAFGRIGSMFACEDLGYVPDMITCAKGLTSGYSPLGAMIASDRLFEPFNDGETMFAHGYTFGGHPVSAAVGLANLDIFEREGLSDHVKRNSPALRATLEKLYDLPIVGDIRGEGYFFGIELVKDQATKQTFTDDERARLLGQVSAALFEAGLYCRTDDRGDPVVQVAPPLISGQPEFDTIETILRSVLTDTGRKYLHL