lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose). PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers. It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated. Poly(ADP-ribose) is synthesized after DNA damage is only present transiently and is rapidly degraded by PARG. Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress. Responsible for the prevalence of mono-ADP-ribosylated proteins in cells, thanks to its ability to degrade poly(ADP-ribose) without cleaving the terminal protein-ribose bond. Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.
Subcellular Localization:
Nucleus. Note=Colocalizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage (By similarity).
Domain:
The PIP-box mediates interaction with PCNA and localization to replication foci.
Sequence:
MSAGPGWEPCTKRPRWGAAGTSAPTASDSRSFPGRQRRVLDPKDAPVQFRVPPSSPACVSGRAGPHRGNATSFVFKQKTITTWMDTKGPKTAESESKENNNTRIDSMMSSVQKDNFYPHKVEKLENVPQLNLDKSPTEKSSQYLNQQQTASVCKWQNEGKHAEQLLASEPPAGTPLPKQLSNANIGQSPHTDDHSDTDHEEDRDNQQFLTPIKLANTKPTVGDGQARSNCKCSGSRQSVKDCTGCQQEEVDVLPESPLSDVGAEDIGTGPKNDNKLTGQESSLGDSPPFEKESEPESPMDVDNSKNSCQDSEADEETSPVFDEQDDRSSQTANKLSSCQAREADGDLRKRYLTKGSEVRLHFQFEGENNAGTSDLNAKPSGNSSSLNVECRSSKQHGKRDSKITDHFMRISKSEDRRKEQCEVRHQRTERKIPKYIPPNLPPEKKWLGTPIEEMRKMPRCGIHLPSLRPSASHTVTVRVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDENGERTAGSRWELIQTALLNKFTRPQNLKDAILKYNVAYSKKWDFTALVDFWDKVLEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSVTMSQEQIASLLANAFFCTFPRRNAKMKSEYSSYPDINFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSLEDFPEWERCEKPLTRLHVTYEGTIEGNGRGMLQVDFANRFVGGGVTGAGLVQEEIRFLINPELIVSRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWARSHEDGSEKDDWQRRCTEIVAIDALHFRRYLDQFVPEKVRRELNKAYCGFLRPGVPSENLSAVATGNWGCGAFGGDARLKALIQILAAAAAERDVVYFTFGDSELMRDIYSMHTFLTERKLDVGKVYKLLLRYYNEECRNCSTPGPDIKLYPFIYHAVESSAETTDMPGQKAGT
The following text describes a protein:
Function:
Regulatory protein of the TOL plasmid xyl operons. XylS activates the xylXYZLTEGFJQKIH operon required for the degradation of toluene, m-xylene and p-xylene.
Subcellular Localization:
Cytoplasm.
Sequence:
MDPLDRLIQLANLQGRLDQRCQLQGSWALEHPQAVPGEATFHIVMAGTCYCEFLDGGRLDLHPGDLILLPRGTPHLLRSDSPAQPCEPTVEHRGSIPLYQLNGPGEALDMLCGSYRYHAGASLFGALPERLLVHMDESTQQPLRALIGLMREEAESTRSGARSIIDALATALFALALRAYLDRQPLGDGLFGLLGDARLGRALRAMLERPEHAWTLEQLAQQAAMSRASFVRAFSALGGTSPWNLLTRIRMEKARGLLRQTQKSLLDIAAETGYQSEAAFSRNFRQAFGESPGRFRRQADSAR
The following text describes a protein:
Function:
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity.
Subcellular Localization:
Nucleus.
Sequence:
MDNTKEKNNFKDALLLRMGLNDNKAGMEGLDKEKINKIIMEATKGSRFYGNELKKEKQVNQRIENMMQQKAQITSQQLRKAQLQVDRFAMELERNRNLNNTIVHVDMDAFYAAVEMRDNPELKEKPIAVGSMSMLATSNYHARRFGVRAAMPGFIAKRLCPQLIIVPPNFDKYRAVSKEVKEILAEYDPNFMAMSLDEAYLNITQHLQERQGWPEDKRRYFIKMGNCRKIGIAPNTMLAKVCSDKNKPNGQYQIVPSRSAVMDFIKDLPIRKVSGIGKVTEKMLLALGIVTCTELYQQRALLSLLFSESSWHYFLHVALGLGSTDLARDGERKSMSVERTFSEINKTEEQYSLCQELCTELAHDLQKEGLKGRTVTIKLKNVDFEVKTRASTVPSAISTAEDIFAVAKELLRTEVTAGSPQPLRLRLMGVRMSTFSNDDDRKHQQRSIIGFLQAGNQGLSPTGCTADRTDKTELVKPLETSRKKSFFDKKRSERIPNCQDPPRCKIAGEQALQASEPSQALKKMSESFKTSENSNDPQTFICPVCFREQEGISLEAFNEHVDACLDGPSTSENSEMPSYSHASSADIGQQAHRAVPLWEKRGHGDGEITSGDGADLTETEDRSPKAASMDAVGNNHSEGEGYPDSQGKSCPLSPANETVSTLSREDSAQPCTDEVVTGRALVCPVCNLEQETSDLTLFNIHVDICLNKGIIQELRNSEVNSVKQPKGSTRSTDRLQKASGKTKRAGRKTKGSTSKRTKPRDPRHTLDGFFK
The following text describes a protein:
Function:
Involved in substrate recognition in ubiquitin-dependent degradation.
Subcellular Localization:
Mitochondrion.
Sequence:
MRVPNEVCFNILSYLEADELRCKSTVCTSWRNFIIPTLWEKVVFQNEAQLNNFFDTLQYSKDVSYYFRYLRKLNCSRVRKFLTDKHLMLMTLATGISRLNLSGCTRISEPLIGKLLYQNLNLVTINFSNIFSLPANILEYISDNCPNLKALNIGNCGLVEDTGMVQIIKRCPYLNRLIIPNCRKLTDVSLQILSEKEDLIELDISGCEGFHNADTLSRLVSRNRGLKELSMDGCTELSHFITFLNLNCELDAMRALSLNNLPDLKDSDIELITCKFSKLNSLFLSKCIGLTDSSLLSLTKLSQSLTTLHLGHCYEITDIGVQCLLKSCKNITYIDFGGCLRLSDIAVSAIAKLPYLQRVGLVKCICLTDLSVILLSGSFSRNLERVHLSYCIGLTAKSVSYLMYNCKTLKHLSVTGINSILCTELRSFSRPIPDGINPSQVPVFCAFTKVEIDLFREFIRNRI
The following text describes a protein:
Function:
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Subcellular Localization:
Cytoplasm.
Domain:
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Sequence:
MKLVLMGLPGAGKGTQAEQIVEKYNIPHISTGDMFRAAMKNNTELGRKAKSFMDNGDLVPDEVTNGIVRERLSEDDAKDGFLLDGFPRTVEQAQELENILSDLGTELDAVINIDVEKDVLMKRLTGRWICRTCGKTYHEIYNPPKVPGKCDLDGGELYQRDDDKKETVEKRLNVNMKQTKPLLDFYSEKGKLHNINGEQEIKDVFVDVEKILASF
The following text describes a protein:
Function:
Catalyzes the synthesis of D-serine from L-serine. Has dehydratase activity towards both L-serine and D-serine.
Sequence:
MSDNLVLPTYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVDIERYAHFLSQ
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:
MKGKFRFSLKRGLLRPSWNKYNIYNIARKQLPALNNRTLYQKKWNAKKETRSYHGPQLREYQLKNAFRPKLEGVISSLDNKLPIPFMNQTYAFLESRLDMSIHRALFASSALQARQLVLHGKVHVNGKPERRAYRQLLPGDLVTVDQKSVMNCVSASSNNTPSIQDGKQTEQVSSKDGENEKKKDNDDDLFEQTSNGKLPSINETISNFVPKPFMSLMAFIPAYLEVCFRTCSFVYVRDPVARPGLTEVPSPFPEDLHALAYTYYIRSRNMRQGAARCQARRLIPQKVRDASFYQGPPELYKKRNVSPKEAFSHRYPVRQGKLTKLV
The following text describes a protein:
Function:
Involved in the production of cutin monomers. Esterifies acyl-group from acyl-ACP to the sn-2 position of glycerol-3-phosphate, a step in cutin biosynthesis. Required for colonization of the root by mycorrhizal fungi, and appropriate hyphopodia and arbuscule formation. Cutin monomers act as plant signals that promote colonization by arbuscular mycorrhizal fungi. This signaling function has been recruited by pathogenic oomycetes to facilitate appressoria formation and their own invasion.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MAIATFPTVEKCTSMRREKDTVVTDLDGTLLRGRSSFAYFALVAFGVGGVLRLLFLLLASPIAGIFYYFISESVGIQVIFFATFVGMRVSDIESVARTVLPKFYLEDLHPESWRVFSSCGERCVLTASPRILVEPFLKDYLGVDIVLGTEIETYKGRATGFVKSPGVLVGNNKADALKSTFGETQPEIGLGDRDTDIPFMALCKESYYVPPKPKVEAVSTSKLPKPIIFQDGLLVQKPTPLMAIFIIVWIPFGFFLACLRISVGLILPVPLHYYAFWVTGIRLIINGISPLHIKKYQDQSGVLFVCCHKTILDSIFLSASLGRPIPVITYSTSRLFEIFSPIKTIRLTQDQALDASIIKQLLKESDLATFPEETTSRGPFLLKFSPSFAELTDELVPVALETNKNKMSMFHGTTTRGWKWIDAFFFLMNPRPTYEITFLNKLPHEFTCKSGKSSHEVASYIQKVIAETLSYECTTLTRKNKYI
The following text describes a protein:
Function:
Probable RNA-binding protein that may play a role in growth regulation.
Sequence:
MAVTKLNPSAAPFHCSRRHLFFAPPPPPPPPMPAYQYHATGACAAAAPPPFPFFATYSCASLPFHGHLYPPCGYQAQMGPAPPGAAFAKGVLAAAPPPPHGRPPHKLMVCKGAPTVTDVKLRAQARAAARVGVAAAVRGWRPAPATAGPPRMLVAAAPCGMLHPAAVARRRGMSKVYKPRKPQRAGRERSPSPSPVFTTRPMSPTPPMQKLKPAHTTVMVRNIPNKLTRSDMVRLLDDHCARENRRRGRGGEPRAEYDLVYVRMDFGMCNKERSSNMGYAFVNFTTAEAARGLQRALHGCRWKRSAFDSGKIIDIRAARIQGKDALVRHFGRTTYYECDTDEYLPAVFSPPRDGSTAGAGAPSPPAVKTVGIRVPPRPITLLTHRGNVN
The following text describes a protein:
Function:
May play a role in p53/TP53-mediated apoptosis.
Subcellular Localization:
Nucleus.
Sequence:
MVSWVLKGARRVGRPGIPLMPRLRVEPGDSVSPDPEKPLASAPFLHGSQPLRRSFGSACHTTTLPALVRTPTLMMQPSLDIKPFMSFPVDSSSAVGLFPNFNTKRRGLFGTNKFFQMDPVQKAVINHTFGVSIPPKKKQVISCNVCQLRFNSDSQAEAHYTGSKHAKKVKALEATKNKPKMVPSKDSAKANPSCSVRPGTGDSSDKSEDKGKIKATSSSQPSGSEGGSFFLKSGTTPLTLGAIASPSKSTNGAPGSVAESEEEKAKKLLYCSLCKVAVNSLSQLEAHNTGSKHKTMVEARNGAGPIKSYPRPGSRLKVQNGSKGSGLQNKTFHCEICDVHVNSEIQLKQHISSRRHKDRVAGKPLKPKYSPYNKLQRSPSILAAKLAFQKDLMKPLAPTFLSSPLAAAAVSTALSLPPRPSASLFQAAAIPPALLRPGHGPIRATPTSILFAPY
The following text describes a protein:
Function:
Catalyzes the hydroxylation of nicotinate to 6-hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid, but inactive against other nicotinate analogs.
Sequence:
MNKITINLNLNGEARSIVTEPNKRLLDLLREDFGLTSVKEGCSEGECGACTVIFNGDPVTTCCMLAGQADESTIITLEGVAEDGKPSLLQQCFLEAGAVQCGYCTPGMILTAKALLDKNPDPTDEEITVAMSGNLCRCTGYIKIHAAVRYAVERCAN
The following text describes a protein:
Function:
Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the desaturation of the L-prolyl-[PigG] to yield 1H-pyrrole-2-carbonyl-[PigG].
Sequence:
MDFNLSNSQSDIYESAYRFACDVLDQDAQTRISQKILSTELWKKAAAYGFAHGPVSHQFGGSELGALDTALMIEALGKGSRDIGLSFSLCAHLCACVIPLYRFGSSELKDKYLESLVTGKLIAANAATEPDAGSDIYNMQATAQPCEGGYILNGKKIFITNAPIADVFIIYAKTNPDHGFLGVSAFLIEKGTPGLNVGEVIPKDCLSNCPWSEIVFNDIFIPQSQRIGMEGAGGAIFHDSMIWEKGCLSALFVGGLARLLETTLEYAKARQQFGKAIGQFQSVSNRIIDMKLRLEQCRLMLYRACWKHDQGQDAEADIAMSKLLISEYAVQSGLDAIQTFGGAAMDQELGLVRHLLNMIPSRIFSGTNDIQKEIIARKLGLRGTSS
The following text describes a protein:
Function:
Probable transcription factor involved in the regulation of filamentous growth.
Subcellular Localization:
Nucleus.
Sequence:
MESTLSVSDEKLTNSSTALNNCGDNKESSQVLTTANTTTDNQQVQPKSQHQQSASTEPLSKERTNISLENDLILVDPNQQSKNTVSDSVQDTTGVPSDHGKQQTIGDQIKILISSNPLNIEEYSSHLNRLATILYEENFTSDFLVTLHYKILQLMDELPKFVDLQNPLKSQLYTIIDKNFDILIKLATNYKVMEVSTASIRFLTTVFMNLNYWEVYNLLNKKPVLYHFLNLIEFDLNDCYTRFINDYQRFTYDKITQPTVKSRSRSKVTKKRKVKGDSDFAGSNTATATTSVTTPDANTSHEGKQHRSEAFFSLNPDTSDHDKYVADVISGANVQKRKFRPDVKLEHHRIIKKPQPAADKLSTKSSNYDPDVIHECQLPSAEEPHKLCLRRFSRKYELIRHQETVHSKKKKLFKCFVCVKQNPGVGPRIFTRHDTLAKHIRVNHKISGKEAKAEVAYSKKHAEVVEEGDITVHVGRRKTKVDFELRAHMEKRKSSGDDTNYMETSDLESGEEEVTFNK
The following text describes a protein:
Function:
Mediates influx of magnesium ions. Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
The central ion permeation pathway is formed by the first transmembrane domain from each of the five subunits. Mg(2+) binding strengthens interactions between subunits and leads to the formation of a symmetrical homopentamer surrounding a closed ion permeation pathway. Low Mg(2+) concentrations trigger both a conformation change within each subunit and a loosening of the interactions between subunits. This results in an open ion conduction pathway. In addition, this results in a less symmetrical shape of the whole complex.
Sequence:
MKAHTGKDWFWYQMGPQERSKARDLIHFSHWPQCEKWFENNHHVNFLRVDTTETENEAVFGSIVYDQGLGEEKDHTVFHFYITRQYFFTINFDFSILREIKGKEVVRQMERADNAIEGFLILLGELMNAYLIGVDEFEVKLRKLRWQIKDDNSKSILNRVHLLRHELMIWKNLILSAKKIEMALKETFLPQNEGKKDYQRTQLKIDRGFTYISEFEGELNNLLHSEEVITSHRGNEIVKALTIFTTLFTPITALGALWGMNFSVMPELNWKYGYLFSLLLIVTSTVLIYLYLRKKGWTGDMLQERKKKKKPRKRRTL
The following text describes a protein:
Function:
Implicated as a cell-surface receptor on spermatozoa for 'speract' a chemotactic peptide, and on various other cells as a receptor for atrial natriuretic peptide.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MAHARHLFLFMVAFTITMVIARLDFNPTIINEDRGRTKIHVGLLAEWTTADGDQGTLGFPALGALPLAISLANQDSNILNGFDVQFEWVDTHCDINIGMHAVSDWWKRGFVGVIGPGCGCTYEGRLASALNIPMIDYVCDENPVSDKSIYPTFLRTIPPSIQVVEAIILTLQRYELDQVSVVVENITKYRNIFNTMKDKFDERDYEILHEEYYAGFDPWDYEMDDPFSEIIQRTKETTRIYVFFGDASDLRQFAMTALDEGILDSGDYVILGAVVDLEVRDSQDYHSLDYILDTSEYLNQINPDYARLFKNREYTRSDNDRALEALKSVIIVTGAPVLKTRNWDRFSTFVIDNALDAPFNGELELRAEIDFASVYMFDATMQLLEALDRTHAAGGDIYDGEEVVSTLLNSTYRSKTDTFYQFDENGDGVKPYVLLHLIPIPKGDGGATKDSLGMYPIGTFNRENGQWGFEEALDEDANVLKPVWHNRDEPPLDMPPCGFHGELCTNWALYLGASIPTFLIIFGGLIGFFIYRKRAYEAALDSLVWKVDWSEVQTKATDTNSQGFSMKNMVMSAISVISNAEKQQIFATIGTYRGTVCALHAVHKNHIDLTRAVRTELKIMRDMRHDNICPFIGACIDRPHISILMHYCAKGSLQDILENDDIKLDSMFLSSLIADLVKGIVYLHSSEIKSHGHLKSSNCVVDNRWVLQITDYGLNEFKKGQKQDVDLGDHAKLARQLWTSPEHLRQEGSMPTAGSPQGDIYSFAIILTELYSRQEPFHENEMDLADIIGRVKSGEVPPYRPILNAVNAAAPDCVLSAIRACWPEDPADRPNIMAVRTMLAPLQKGLKPNILDNMIAIMERYTNNLEELVDERTQELQKEKTKTEQLLHRMLPPSIASQLIKGIAVLPETFEMVSIFFSDIVGFTALSAASTPIQVVNLLNDLYTLFDAIISNYDVYKVETIGDAYMLVSGLPLRNGDRHAGQIASTAHHLLESVKGFIVPHKPEVFLKLRIGIHSGSCVAGVVGLTMPRYCLFGDTVNTASRMESNGLALRIHVSPWCKQVLDKLGGYELEDRGLVPMNGKGEIHTFWLLGQDPSYKITKVKPPPQKLTQEAIEIAANRVIPDDV
The following text describes a protein:
Function:
Forms chloride channels.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane.
Sequence:
MDKGATSNHISIGRMLIMWRRSVYKVVYKELIAFLFVFGTISAIYRYALDEHQKKYFEESKAFFQSYIDHLSVPFLLGFYVTTVAGRWWAQYLTIPWPDKLMLTIQSYIAGDGEEVRVLRQGLVRRALLMLILLLRSISLSVRRRYPTFQSLVKEGIMTRKEKQCYESIIPVGNLFWIPATWFVAALNEAVSTGILKNESGAKLIMEEFLEFRANCGALWSYNWVSIPMIYTQVCTLSTYSYFIACLMARQYTGPSLQSLEDIDIALPVGTVMELICYVGLLKVAEQIKNPFGDADEDFDLNFLITRHLRVRYPIFFFN
The following text describes a protein:
Function:
Methylates ribosomal protein L11.
Subcellular Localization:
Cytoplasm.
Sequence:
MDKEWLEVCIYTSSEALEAISGILYNTGVKGVSIEDPKDIEFKRKHPGDWDYFDETLLKVKDTAIVKGYYKEDDKFNEYLDYIKKSVSNLDQFGIDKGEGLVEVHKVNEEDWENNWKKYYKPTKVSNKIVIKPIWENYDKKQEEIIVELDPGMAFGTGTHETTRMCINALEKYIKEDRTVFDIGCGSGILSIAAAKLGAKHVIGVDLDPVAVKSSKENIKYNNLDNIEILEGNLMEVVEGRANIVVANIIADVIIFLTEGVKAFIEKGGYFIASGIINSRKEDVIKKLEETGFIIEEVREEGEWACIVSKIN
The following text describes a protein:
Function:
May act as an E3 ligase mediating SUMO/Smt3 attachment to septins. May be involved in chromosome maintenance.
Miscellaneous:
MISCELLANEOUS: Present with 3170 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MASVMSNNNNNNNNNNASYMFTNPLSNTGGGLINEIKDAINEMEQLKVLELKQICKSLDLSITGKKAVLQDRIKQFLRKSCDIGHIDPWRPKAIKILIAKVRINSSLPKYSTLWETLKTGAFKHPVASGQLPVTALQSTALPPYSQQQALAYSFTSPFYKPIVQIPDANKKLKQSAGRGCTKMKFKVSKSNHDLLKSNKSYKLYLFSGFSIPFIYETVGHEAIDFPYPCELVFNGTKLEDNVKGLKKQNGTGNPANLTPYLKVPTEMNHLDLHYLNIDKEYSISCFIVEVFSPEALLGKILKRPKIIKQATTAYIKRTLNEQDDDDIITTSTVLSLQCPISCTRMKYPAKTDQCKHIQCFDALWFLHSQSQVPTWQCPICQHPIKFDQLKISEFVDNIIQNCNEDVEQVEISVDGSWKPIHNSSAVITDTVNQNHSVKNENQGTVKQEQDYDSRNAFDTNLRNGSNHNEPEIISLDSSDDEAFIPASKSFPTHVNPRNDQLRADIFPSESEGSSDYNPNHTSTPKGSPTMDQDNYQDAFQMRSFLNQGATTNINDTPTNNSSINSFVTATNGDSRIFYNRGPSTPLLPAVLQNLTNQTEAQRNPYGPNYNTTAQDRNLLGIEGDLPPIPPVDPNSEAETELPTRTTSAAHLPPYIHVSTSGHGDDGKIRKRRHSNVSIYIPKNPYATLMKRRPQANHAIMNKTLAQTNDFNTSAQDNSEVVDLTSD
The following text describes a protein:
Function:
Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan.
Subcellular Localization:
Secreted.
Sequence:
MKLFLLLLISALAAAAALPSSFKWSSSGPLVEPKKDGRNIAAIKDPSIVKVDGTYHVFASTATKSGYNLVYFNFKDFSQANQATFHYLDQTPIGSGYRAAPQVFFFKPHNLWYLVFQNGNAAYSTNPNIANPAGWSKPKNFFSSMPSIIAQNKGNGNWVDMWTICDSSNCYLFSSDDNGHLYRSQTSLANFPNGMGNTVIALSDSNKNALFEASNVYHTGNGEYLLLVEAIGSDGQRYFRSWTSNSLTGSWKGLANTEANPFARSNNVAFSGTPWTKSISHGELIRTQTDQTMTISPCKLQYLYQGLSPSAGGDYDLLPWKLGLITQTNSNC
The following text describes a protein:
Function:
Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Sequence:
MAALQYLESLKSSHPELNEWYDSLSDLYQKKLWHQLTLKLEQFIALSVFQAGDALIQFYHNFITDFETKINLLKLAHFAVVVSRQYSEKEAAVSYLEGVIEKLKATKEPRITEPIVYIETQKALFKLEQGDQKECKKVLDDAKTSLDSMTDIDPSVYANFYWVSSQYHKCRQEFSDFYKSALLYLAYTSVEALSDSFKLDLAFDLSLSALLGENIYNFGELLAHPILKSLLGTNVEWLYHILQAFNHGDLVQYQELCRVHHASLIAQPALVENEKKLLEKINILCLIEIIFSRPAEDRTIPLTVIAERTKLSIEDVEHLLMKSLSVHLIEGIIDQVNGTVYISWAQPRVLGIPQIKSLRDQLDSWVDKVHTTLLSVEAETPDLVAA
The following text describes a protein:
Function:
Microtubule-associated protein with the capacity to bundle and stabilize microtubules. May associate with chromosomes and promote the organization of mitotic spindle microtubules around them.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Chromosome. Note=Found in the cytoplasm and nucleolus during interphase and redistributes to the mitotic spindle in prometaphase. Localizes to the mitotic spindle and to the chromosomes during anaphase and telophase then disappears from around the chromosomes during cytokinesis.
Domain:
The KEN box is required for the FZR1-dependent degradation of this protein subsequent to ubiquitination.
Sequence:
MTVPSAEELDSFKYSDLQNLAKRLGLRANMKADKLLKALKAHLNPETRKENKNQDENQFSTDETEIHVSSEEQAETESGGHVTKTRRRRRKKHKTIHGIPTSQTLLQDHLEMKGTDSSNFQNQENQENQDPRDTAEVPSLPEQRPEDGNAASSGEGEVNDIKDSKKPLEKRSLCTDEFSKLGNNKRTSATTPNFKKLHEARFKKMESIDEYIMRKKKHLKEHSSLNELKLDKKGIVTPVPPRGRLSVPCTPARQQCPQGHSATKMNVRFSAATKDNEHKCSLTKTPARKSPHVTAPGSASKGQAVFRTPKSKATERTSIAVITPFKLMTEATQTPSSSKKPVFDLKASLSRPLNYKPHKGKLKPWGQAKENNSLNERVSRVTFHRKTYKQPHLQTREERWKRQEQERKEKKEKLLEARRNLGVTKAQ
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:
MILKRPHLGKFLERMAKLFDVVAFTSRAQRRAETILDVLDPAKEFFSRRLYLDSCKKGGKVKDLAVLERPLNRVIIVDDTSSKCVLNPDNLVLVSRFKRHNLSTDRGLLDLIPFLEELSKEEVEDVRPVIH
The following text describes a protein:
Function:
Counteracts the antiviral effects of host IFN-alpha/beta and key IFN-inducible proteins involved in viral RNA degradation suxh as host OAS1. Acts as a soluble IFN-alpha receptor and thus inhibits the interaction between host IFN-alpha and its receptor.
Sequence:
MAVFGSFCLIFLVLRSVATIEDYCSLNTYSTNGTYMQFTKEPNVDEFAIAGKFKGLHCCAKGYRSIEWYKDGKPYPWPLMVSQLILYPESANQTVYTQSVTEADAGNYTCLLRNDSVVHSHTIQLKVFEKIPDDPKITYVSKDHQVPLGQQLRLFCEAFAGRVDLPDAHNEVVWRKSGHNGTLDDEPRVRQEKISREDGQTFGTYLIIDSVRREDFGEYVCKISKPGKSIEQRVFVDEKIEVEYLNPNPVPVAKLLLCLSAIIFLCLAVVILNLQYGLPLRVRFKDTFGVVEESDGKTNDVLLLYSSKDSELALGTLLPILESRYNYKCVHRELPSSINYWFGELQNDALKSRRIVTLLSPPVVSDNWTSAAIYQAIKQLQALGSKLTIITLKELPRCENETKNSHGETLTILLRTINVVHWERTKEEKFWLNLRLRLPPKRRNERLVDGRSQTQGINSSRLSNDSEESSDLV
The following text describes a protein:
Function:
Adenine nucleotide transporter involved in the uniport of ATP and adenine nucleotide hetero-exchange transport between the cytosol and the peroxisomal lumen. This transport is accompanied by a proton transport from the peroxisomal lumen to the cytosol. Transport of ATP into the peroxisome is required for beta-oxidation of medium-chain fatty acids. Required for growth on medium-chain fatty acids, pH gradient formation in peroxisomes and for normal peroxisome proliferation.
Miscellaneous:
MISCELLANEOUS: Present with 2250 molecules/cell in log phase SD medium.
Subcellular Localization:
Peroxisome membrane; Multi-pass membrane protein.
Sequence:
MLTLESALTGAVASAMANIAVYPLDLSKTIIQSQVSPSSSEDSNEGKVLPNRRYKNVVDCMINIFKEKGILGLYQGMTVTTVATFVQNFVYFFWYTFIRKSYMKHKLLGLQSLKNRDGPITPSTIEELVLGVAAASISQLFTSPMAVVATRQQTVHSAESAKFTNVIKDIYRENNGDITAFWKGLRTGLALTINPSITYASFQRLKEVFFHDHSNDAGSLSAVQNFILGVLSKMISTLVTQPLIVAKAMLQSAGSKFTTFQEALLYLYKNEGLKSLWKGVLPQLTKGVIVQGLLFAFRGELTKSLKRLIFLYSSFFLKHNGQRKLAST
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the tom40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of tom40 with the receptor tom22 and small TOM proteins. Can associate with the SAM(core) complex as well as the mdm12-mmm1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the tom40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Sequence:
MLDFMDYIQLAFAEATNWNCDNSYSSLTATAQSLLDFSTPERLRVHLSSLATPHFATSYTLGTVGLIDGSVSYLYSTVPLNNTPSRSALIPLRKLARGYRQVQPPVAPVEDCGWQSCLGGLGSSESKPSGNDDSQPSPGRKATLLNATLHLPPPTILNALFLRRMSPTMQLSLAVCSTRGAPLSNSAPQASLLGQLSHDTGKYSNEYLFSTDNSLFGWRGLWNFGPDPRHPKENSSPQLSLLSAGAEAYYSPVSSLIGMSTGLRFSTLPAATEMPSSSSSASSTTTTSNHDTPISTFPYTLTLVLTPLTGSLSTTYSLRASPNLAFSSRFGFNVYSWESEMVAGCELWRKRRKPSPPPVDDDGLEWARRKMRMADTPAFAPVEPPTTHNRDEENESVLKIRVDQSWNVRLLWEGRVKELLVSAGVGLGPSSFSSPSRAANSTPAGGGQSVGGGISGRSYWHGVGVSISYSS
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:
MNVTASLSRRPLGCLKAGLCQSLIRGYATAVAASTTQSTGALPDHNFFRIADKHTKKTRTAFAVFTPPKSPTTLPPSSVVTKSKAFKIANSKLPPLMTKPPSDPMPLLTQQQIARMDPTGARTALFSKARHAARVGDVLMVTHRRGGEPFAGVCLAIRRSGIDTAILLRNHLGKVGVEMWYKIYNKNVAGIEIIKRRAKRARRAKLMYMRQPKHDMGSVEQYVFAWKKMRKVLSSKGLTGGVGGGGGKQKGQESKKKN