lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved in a terminal step of poly(A)+ mRNA transport through the NPC probably by binding the ATP-dependent RNA helicase DBP5 and GFD1 at the cytoplasmic side of the NPC. These interactions are thought to be important for the dissociation of transport proteins such as the heterogeneous nuclear ribonucleoprotein (hnRNP) NAB2 from exported mRNA.
Miscellaneous:
MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side.
Sequence:
MRFVFDEVFNSDTDSPEFEETCSTTSSTSSQCPTPEPSPAIKLPSFTKVGTKKLVNESVVILDPALENALRDLNLQSKLIPINEPIVAASSIIVPHSTNMPLPRASHSSLLDNAKNSNATAPLLEAIEESFQRKMQNLVLANQKEIQSIRENKRRVEEQRKRKEEEERKRKEAEEKAKREQELLRQKKDEEERKRKEAEAKLAQQKQEEERKKIEEQNEKERQLKKEHEAKLLQQKDKLGKAVTNFDKISKMFWHYKDKIAQIKQDIVLPIKKADVNVRNLLSRHKRKINPKFGQLTNSNQQLFKIQNELTQLINDTKGDSLAYHWILNFIAKAVVHQAETEVRVKPESALPLGKLTLYLLVQFPELQELFMARLVKKCPFVIGFTCEIDTEKGRQNMGWKRNNENKWEDNTSYDERMGGILSLFAIITRLQLPQEFITTTSHPFPIALSWHILARICNTPLNLITNTHFVILGSWWDAAAVQFLQAYGNQASKLLILIGEELTSRMAEKKYVGAARLRILLEAWQNNNMESFPEMSP
The following text describes a protein:
Function:
Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins. Required for secretion of cholera toxin through the outer membrane. This subunit forms the outer membrane channel.
Subcellular Localization:
Cell outer membrane. Note=Most of the protein is in the periplasm which it traverses to contact proteins of the cell inner membrane.
Domain:
The N0, N1, N2 and N3 domains are periplasmic, while the secretin and S domains form a channel that is partially inserted in the outer membrane. The cap gate extends out on the extracellular side of the channel partially closing the channel. The secretin domain forms a double beta-barrel structure; the outer barrel has an outer diameter of about 110 Angstroms while the inner barrel forms the central gate with a small pore in the closed state.
Sequence:
MKYWLKKSSWLLAGSLLSTPLAMANEFSASFKGTDIQEFINIVGRNLEKTIIVDPSVRGKVDVRSFDTLNEEQYYSFFLSVLEVYGFAVVEMDNGVLKVIKSKDAKTSAIPVLSGEERANGDEVITQVVAVKNVSVRELSPLLRQLIDNAGAGNVVHYDPANIILITGRAAVVNRLAEIIRRVDQAGDKEIEVVELNNASAAEMVRIVEALNKTTDAQNTPEFLKPKFVADERTNSILISGDPKVRERLKRLIKQLDVEMAAKGNNRVVYLKYAKAEDLVEVLKGVSENLQAEKGTGQPTTSKRNEVMIAAHADTNSLVLTAPQDIMNAMLEVIGQLDIRRAQVLIEALIVEMAEGDGINLGVQWGSLESGSVIQYGNTGASIGNVMIGLEEAKDTTQTKAVYDTNNNFLRNETTTTKGDYTKLASALSSIQGAAVSIAMGDWTALINAVSNDSSSNILSSPSITVMDNGEASFIVGEEVPVITGSTAGSNNDNPFQTVDRKEVGIKLKVVPQINEGNSVQLNIEQEVSNVLGANGAVDVRFAKRQLNTSVMVQDGQMLVLGGLIDERALESESKVPLLGDIPLLGQLFRSTSSQVEKKNLMVFIKPTIIRDGVTADGITQRKYNYIRAEQLFRAEKGLRLLDDASVPVLPKFGDDRRHSPEIQAFIEQMEAKQ
The following text describes a protein:
Function:
Vesicle-associated membrane protein-associated protein (VAP) implicated in maintaining the cortical endoplasmic reticulum (ER)-plasma membrane (PM) attachment. ER-PM contacts function to modulate the distribution of contractile ring components to ensure robust ring assembly. ER-PM contacts function also in controlling exocytosis and maintenance of cell polarity regulating cell shape. VAPs play an important role in regulating eisosome assembly. VAPs also contribute to ER-phagy by tethering atg8 to the ER membrane, but also by maintaining the ER-plasma membrane contact (Ref.8). Restricts the localization of duc1 away from the site of cell division.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Note=Localizes at the cortical endoplasmic reticulum-plasma membrane contact sites.
Domain:
The MSP domain is required for binding to the FFAT motif of target proteins.
Sequence:
MSVECSGELFFYPPFTTMSKELISVHNPNPEPVIFKVKTTAPKHYCVRPNSGKIEPKSTVNVQVLLQAMKEEPAPDFKCRDKFLIQSMAIGDADTSNVENYHEFWTEMEKQGRSIFDRKIRCVYSTKQPPQSADKQVENTSTSNPPVSVEGSENLASSVGGPTAVGVSLDEAQNDFNGAKDHLSNGVNTVVPDSTFRSTFESAQIPDASVVQTVVTDADNGAASVKDTIVTAESASSKGADVARSKVQDIIDNEIPKPSESPRRSVSSTPPVHPPPPVPQNLSAVNEEFDTKKNDFDSKLPESTPAVEKVSENLGSETRESLQGAKPAAGAHSSDNALEQIKPSYSADPSSSTGASLTESPGIPPNIVIILCLIFFLIGYLFF
The following text describes a protein:
Function:
May play a role in p53/TP53-mediated apoptosis.
Subcellular Localization:
Nucleus.
Sequence:
MQLQQEKKKLLYSLCDVCNIQLHSAAQAQVHYNGKSHLKRVKQLNNGEVPKASASLAPTSLQSLSSSSSQGSSCHSNTLPTLVRTPSLMMQSGLDMKPFMTFPVESSSPVGLFPNFNTMDPVQKAVINHTFGVSIPPKKKQVISCNICQLRFNSDSQAEAHYKGSKHAKKLKAQESPKNKQKSAVAQDSGTKTITSTSTNTTTTTTTTSSCTAVTASCSDQTEKSTEPLAAHKVPASPQAFVPAPVAPAVALVPSPCKTAPVHASPPTEPTGLAVALKNTSKPAALPTAPSEPSVESEEEKAKKLLYCSLCKVAVNSLSQLEAHNTGSKHKTMLEARNGAGPIKAYPRPGSKLKVQATQLNKGSGLQNKTFHCEICDVHVNSEIQLKQHISSRRHKDRVAGKPTKPKYSPYNKQQRSSSSLAAKLALQNDLVKPISPAFLPSPFSTTTVPSISLHPRPNTSIFQTASLPHSFLRAAPGPIRPTTGSILFAPY
The following text describes a protein:
Function:
Probable rhomboid-type serine protease that catalyzes intramembrane proteolysis. May function in the heat-shock response pathway.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein. Note=Might be neither mitochondrial nor chloroplastic.
Sequence:
MENFGEGRRSGGGMLPLLALSAVAEYYRLPWKPPVTASLLAANTLVYLRPAFIDPVIPHISEVWFNPHLIFKHKDLKRLFLSAFYHVNEPHLVYNMMSLLWKGIKLETSMGSSEFASMVFTLIGMSQGVTLLLAKSLLLLFDYDRAYYNEYAVGFSGVLFAMKVVLNSQAEDYSSVYGILVPTKYAAWAELILVQMFVPNASFLGHLGGILAGIIYLKLKGSYSGSDPVTMAVRGVSRLVTWPLRFLNGMVRSRRRRITGRGRVGRGQTGIAGPGIWRCQSCTYDNSGWLSACEMCGSGRARGNGWSLNQGPALSSSNDLPLDELRRRRVERFS
The following text describes a protein:
Function:
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
Sequence:
MAIKKIISRSNSGIHNATVIDFKKLLTNSKPEKSLLVTLKKHAGRNNQGKITVRHHGGRHKRKYRLIDFKRYHYDNLKATVKSIEYDPNRSCFISLLHYQNGVKTYIISPDGIKVGDQVYSSDHAIDIKLGYCMPLAFIPEGTQVHNIELNPKGGGKIARSAGSYARILGQDETGKYIILQLISGETRKFLKECRATVGVVSNLDHNLVVIGKAGRSRHKGIRPTVRGSAMNPNDHPHGGGEGRSPVGRDAPRTPWGKRHMGVKTRNMKKHSTNLIIRNRKGEQY
The following text describes a protein:
Function:
Probably functions as a cargo-recognition protein that couples cytoplasmic vesicles to the transport machinery. Contributes to retrograde melanosome transport from the cell periphery to the center. Overexpression causes accumulation of late endosomes and/or lysosomes at the microtubule organising center (MTOC) at the center of the cell. Probably binds cholesterol and requires the presence of cholesterol in membranes to function in microtubule-mediated retrograde organelle transport. Binds phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate and phosphatidylinositol 3,5-bisphosphate.
Subcellular Localization:
Apical cell membrane; Peripheral membrane protein. Melanosome membrane; Lipid-anchor. Lysosome membrane; Lipid-anchor. Cytoplasmic vesicle membrane.
Sequence:
MCLKDWLCAFCCLRLGCLEYPKNEKQPLVSGNNNQYKTYAVIDDDERNLWSSPHDLSHTEAVDDRMLQSWIQTRNQLEKDSEEWQKLNYEIYTLRQARREVRARWRRILEDLGFQKEAETLLSVTKQSTISNPKNMKRAMELLVKLSDNTTIFPAGWDLPVRYLYIMDRLICLDAVDDFLNIAQKKYPKTKMDISQ
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates 60S ribosomal protein L42.
Subcellular Localization:
Nucleus.
Sequence:
MVDEFAEATAQFVQWLPKVGIEVAPEVRVEDLRDAGQNRSVVASGAVQEGATLFTIPRSALLNVHTSALRECAAGLPAALEEKIGHWEGLVMCVYYERCVLQERSRWWPCLRLFPAVEEMDNLIYWNAEQRQLLTPSLVGSRIGDESAREMHARVLALAEEWGLSELKEMSWDAFVHIASVIMAYSFDCRLNSDEEDDEEDDDGALDGGTVAADGCIKSIVALAETLNSDTHLANANLTYDRDQLKMIAVKDIKAGEQVYNLYGSYSNAELLRRYGYVEWTGSKYDYGEIELSAIRETISKELAVPDFPFDAVLALLEDKDGWAGELFDYNDIVEESYDCYADGELAPDGAFLVQLLVALAQVPRAALGKGSTLSVRTRKISKKVMQLLESGRITRKAADVLESVIRDRMQAYPPHAAVFDGQKPTDLQAMDPAPRREAMARCVLQCEVKALQKCALAISSNYKIISDDLLMGKLLN
The following text describes a protein:
Function:
Core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. Requires for coordination of the early steps of cytochrome c oxidase assembly with the synthesis of MT-CO1.
Subcellular Localization:
Mitochondrion outer membrane; Single-pass membrane protein.
Sequence:
MPTGKQLADIGYKTFSTSMMLLTVYGGYLCSVRVYHYFQWRRAQRQAAEEQKTSGIM
The following text describes a protein:
Function:
Component of the 60S subunit of the ribosome.
Sequence:
MQLIVRSLDRTVALTASPADSLTSIRQRLLAVYSGHVVDSQRFVFAGRTLDEAKTLGDYSIGESSVLDLVPRLFGGVMEPTLINLAREYNQNMMICRHCYARNPLRATNCRRCRGTNLRKKKLSKYA
The following text describes a protein:
Function:
Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
Sequence:
MEFKPRRVVCWLVITILVALLLWYQTGTQANSTHEHINKGRLSRVSSKVPQDVPLARRKVYDQVETFLIFIGYPRSGHTLVGSLIDAHPNAIIANELDIIGSWLEWNEDHRNKYFLFDQLYKNSHEQTLKGFRSSSVKHRFNYSVRGQWQGRFDRTIKVIGDKKGGGMTARLTNQKQAPILARIKNKIKVKFKFIHVVRNPFDNIATMTTRDKDKTSFKSQGKLNDTDALEQQIFKYFVLAAGNQRLIQRRRKNVLEIHSKDMISKPRDTLRRICKLLDLTCSKQYLYDCASIVYKEPSKTRFRVVWTDKQKQRTLKAMRRFAFLKGYTFDSL
The following text describes a protein:
Function:
Involved in mitotic DNA repair and meiotic recombination. Functions in the recombinational DNA repair pathway. Essential for interhomolog gene conversion (GC), but may have a less important role in intersister GC than spn-A/Rad51. In the presence of DNA, spn-A/Rad51 enhances the ATPase activity of okr/Rad54.
Sequence:
MSRVVLNVDSYEGNDTPSAEIARFVVLYGKASTRKHKIWEGDGLLVCFTDSCLLKSEDERDVICRSSALKGLDQLEDGRIINIGSWSVEIQERIATGPPQKPISAQKPEIQSPMPPMTPGNSENVENRKRGGFSSPFLGIELPKPLSKRSATFVPPLIGSESSSSGGSSSSTIQEKIPPFILNEQDILDRKTTSAVTVDTRFARHLRPHQKSGIQFIFDRLRRGSGKNGGGGGAILADDMGLGKSLQTMAATWALLKGSKTAQQLANSCLIIVPSSLVNNWKAEFDKWWRLMRFPAVIALTANDITTYQSTIKLMPYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKMCSDRPEQLNELIDECMLRRTAADVDLKHLPEKHEYILFCAASPIQKHVHSEICDYMTGDALSLIFFARQLANHPKLLLDNLREKTEKSKAHKHSPLLLAFDGAHMPRGGVKESGKLTALVDMIKCFRLLQECTVIVSNYIETLDMIQQLCEYLNFKVLRLDGKTQVPDRQKLVRTFNDHRDPSNIFLLSTKAGGVGLNLIGASRLVLFDSDWNPANDQQAMARIWRDGQVRPCHIYRLITTGTIEEKMLQRQIKKTGLGCVIDAIEVGDTIATFTDEDLKDIFTFTGSATECNTHDLCECPCDGCGMLENEMDEEDDGDDVVENDAEKIDKSGKIDKIDSDDDEEADDEELEADVTDEVVEDSQEPPEATKPAVAAAGLRTIASLAELSRWRHFSPRHADTWHHFMTNAGLSQVDTDVELTFAFYQESQY
The following text describes a protein:
Function:
Probable anion transporter.
Subcellular Localization:
Plastid, chloroplast membrane; Multi-pass membrane protein.
Sequence:
MASVRSCASVKSAVRSPVSYRSTRAVAAGSGRLRVRSSSLQALAGCASGGGGFGLLGSDDGPRVRRGGREVLATCSASFDGVRPAVVAGAAAQPGSAAFPERAKVVALVATIMLLCNADRVVMSVAVVPLAAQHGWSSSFVGIVQSSFLWGYVFSSMVGGALADRYGGKKVMAGAAALWSLATILTPWAASRSTIMLLAVRALFGLAEGVAFPTMSTFLPKWFPTHERATAVGISMGGFHLGNVISFLATPIIMSHIGLSGTFAFFASLGYLWISVWMMNVESDPLDSHTISKSELQLILAGRAGSKVQGSNKFPSLRELFSRTEFLAVTLANVVNNWGYFVLLSWMPVYFKTVYNVNLKQAAWFSAIPWAVMAMSGYVAGASADFLIKSGFPIGLVRKIMQSIGFMGPCVALLCLRFAQTPSVAAVLMTIALSLSSFSQAGYFCNIQDIAPKYAGSLHGMTNGIGTVAAIVSTIGTGYFVQWLGSFQAFLTLTAALYFSATVFYNVYATGDLIFD
The following text describes a protein:
Function:
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Sequence:
MSSGSAFGDFGPLTERRKAEKARQVRKRIMIAVGTIAIILIVCGIVVTLNGKQKEEKDGSSSKKGSNGNSDGGGGEDGGGDLKAVKKTITMMCKQVDYQGVCEESLTRCAKANESSPLGVLRLAVRVIGEALTEAFDRAELILTNDLLVKGAIADCKEFFGYAKEELNRTLAGMDANDSITKQAYQLSIWLSAVITHQETCIDGFPDGEFKDKVKLSFLKGKELTSNALAFIEKAATFLAGLKLPQRRLLVEEEGAAPRRAEPALGEDGIPEWVPESERRVLKGGGFKAEVKPNVVVAKDGSGQFKTINEALIAMPKKYDGRYVIQLKAGVYDESVTITSQMPNVTLTGDGSKTTIITGKKNFVDGITTFKSATFTAQGDGFMAIGVGFENTAGAAKHQAVALLVLADKSIFLNCKMDGFQDTLYAHSKAQFYRNCDISGTIDFIFGDAAAVFQNCVITLRRPLDNQQNIVTAHGRADAREATGFVLQKCQIIGEPALTAPGRPPIRNYLARPWRECSRTIFMESDLPALIDKAGYLPWNGEFGLKTLYYAEYGNTGPGADTVGRVNWVGYKKVISKDEANKFTLGNFIHPQPWIDPTGTPVKYDFFG
The following text describes a protein:
Function:
Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
Sequence:
MHTYMTHPSKKIIGSISNELADKKILLAVTGSVAIYKSLDLARSLMRNGAEVSVIISKDAAKLISPEMFKWATGNNVVTKLTGDLEHVSLAEDNDVMIVAPSTANTMVKIAYGIADTPITATALNFVGMKKPLIIVPSMHLQMYISPQVADAADRLKRIGVEVIEPEIVGDLAHYPKLEYLTSRITSYVLRGKDLSGFNILATAGPTREYLDSVRFISNPSSGTMGISIANEAYFRGAKVRVICGPISSKIEPYVKDIVYVETTEEMLNEVVKSIENGKFNVVILAGAPADYKFKNKSDTKIDSHTEIPKVELERTPKISEYIRKYNVLLVGFSAETVNSDEELIEKAKIKMRRHGFDLIVANNVRRKDIGFSSEYNEVIVIDKNGDVRKIPKNFKTVIARKILDIVKEQLRR
The following text describes a protein:
Function:
Regulates membrane-cell wall junctions and localized cell wall deposition. Required for establishment of the Casparian strip membrane domain (CSD) and the subsequent formation of Casparian strips, a cell wall modification of the root endodermis that determines an apoplastic barrier between the intraorganismal apoplasm and the extraorganismal apoplasm and prevents lateral diffusion.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MAKARRFVVLALRIATAAAAGVAAIVMATSHKTTTVFGVQVQAKFQYTPSFVFFVAANVVACAYSLLAILVPPASPAARHVLVADAVLGMVLTGAGAAAAAISALGKNGNSHAGWQPICGLVPTFCDHVTGALACGFVAVVLHLLVVLHSIYTMNS
The following text describes a protein:
Function:
Highly specific for ethanolamine phosphorylation. May be a rate-controlling step in phosphatidylethanolamine biosynthesis (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MMAKTKGSYEVFHYTVTKDKVNKGLCDIARYFVPEYRNSKDEDLTIQKLNGGITNVLYLVEDKNIEQKYRYLPVVIRLYGYKSEEIIDRKNELIIQTEADQNGLGAKFYGLFDNGCIYGFIKGEPLAYEDISKPTMQTCIAKEIAQWHSIEMPTRKNPSLWPTIKKWAALAPDVYPVPEKNEYYQSINVKKMIEEGKMLEQRLAQLNSPIVFCHNDLLSGNIIYDPSQNCASFIDFEYANYNFRGLELGNHFNEYAGFGPDYSLYPNKESQIHFLTDYHRSLFKTEPTQDELEKLYIESNQFSLASHLYWGFWAIVQAMNSQIDFDYLEYGKARFDRYYETRDQFLNLN
The following text describes a protein:
Function:
Antitoxin component of a type II toxin-antitoxin (TA) system.
Sequence:
MADHNTAPDTLPADDTWTLANAKARLSQVIDRAQTGPQIITRHGKPNAVIVSAEEWARKTARKGTLAEFLLASPLRGADLALERMHDAPRDEMP
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular Localization:
Nucleus.
Sequence:
MAVLLETTLGDLVVDLYTEERPRACLNFLKLCKIKYYNYCLIHSVQRDFIVQTGDPQGTGRGGESIFCKLYGDQARFFEAEKVPRIKHKKKGTVSMVNNGSDQHGSQFLITTGENLDYLDGVHTVFGEITEGMDVLNKINEAFVDKDFVPYQDIRINHTVILDDPFDDPTGLTIPDSSPEPTKEQLDSGRIGADEEIDDFKGRSVDEVEEILAEKEAKTQAILLEMVGDLPDADIRPPENVLFVCKLNPVTTDEDLEIIFSRFGPIKSCEVIRDWKTSESLCYAFIEFEKEEDCEKAYFKMDNVLIDDRRIHVDFSQSVAKIKWKGKGGKYTKEDFKEYEKDRDKTSKLGLKEKAKAKQDSKYDLVLDNEELEPKISHRHSDKKKKKHHHSDDSDEGQKRSKKSKDPDRRHKEESSRERRKNDKREKRRSRSHSRNRDNRYKKSKDKHHEDSWEREHEERRKSRSPKKSKDKDKSKYR
The following text describes a protein:
Function:
May be required for cellular fusion during osteoclastogenesis.
Subcellular Localization:
Membrane.
Sequence:
MAEPWSGQSLQALPATVLGALGALGSEFLREWEAQDMRVTLFKLLLLWLVLSLLGIQLAWGFYGSTVTGLYHRPGLGNQNGSTSDGSTHFPSWETGANEPLKTHRE
The following text describes a protein:
Function:
Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin (By similarity). Gamma chain of the formate dehydrogenase (FDH) that catalyzes the reversible two-electron oxidation of formate to carbon dioxide. The gamma subunit of formate dehydrogenase forms a c-type heme.
Miscellaneous:
MISCELLANEOUS: The second heme binding site has an unusual CXXXXCH motif.
Subcellular Localization:
Periplasm.
Sequence:
MRYLVISLFAVSLLMAGSALVGNAADAAKAPKKAIELKHGTSKRMHVMFNHTTHKDIACEQCHHDSPAPDKPYASCTDNDCHATPGPRERDTMSMFVAYHAKDTDRSCYGCHKKMAAQHPEFTGCRPCHMSQQARKEAAASEKK
The following text describes a protein:
Function:
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MEERETTKQKTKTKKQKRARSGFWTWVVASVAFRLALVYLPRNLRLSTRPEVASPLTSIRRLGEGYWLKQSVMSPYAGSMYHGSPLLLLALGPLAVKRAIMAIKDLDALFSSLDPEYYDILMKYLYKGLSTGDRPTCDQCLRIHERLTERAGLGCILLSLADTTNTV
The following text describes a protein:
Function:
SNARE required for protein transport between the ER and the Golgi complex.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Golgi apparatus membrane; Single-pass type IV membrane protein.
Sequence:
MNSIYNHGLKQTQTITKDLTQFEKNLSTSPLSLQGAITTSLTAFRKTIKEYSDLLEKNVNDTSYTKHENRLNKFNQDLNEFTSKFDTLKKQRDIQVQEANKQELLGRRHISTTATAALGSTSSDNPYESSSNPSQQQQQQLQDEQNTMSYREGLYHEKNSLERGSEQLDRILEMGQQAFEDIVEQNEILRKVQTKFEESLITLGVSQGTIRSVERRAKQDKWLFWFCVVVMLVVFYYIVKLFR
The following text describes a protein:
Function:
Putative tyrosine recombinase. Not involved in the cutting and rejoining of the recombining DNA molecules on dif(SL) site.
Subcellular Localization:
Cytoplasm.
Sequence:
MRDRISAFLEEKQGLSVNSKQSYKYDLEQFLDMVGERISETSLKIYQAQLANLKISAQKRKISACNQFLYFLYQKGEVDSFYRLELAKQAEKKTEKPEILYLDSFWQESDHPEGRLLALLILEMGLLPSEILAIKVADINLDFQVLRISKASQQRIVTIPTALLSELEPLMGQTYLFERGEKPYSRQWAFRQLESFVKEKGFPSLSAQVLREQFILRQIENKVDLYEIAKKLGLKTVLTLEKYR
The following text describes a protein:
Function:
Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. Together with the E3 ubiquitin ligase rnf7/rbx2, specifically neddylates cullin-5 (cul5). Does not neddylate cul1, cul2, cul3, cul4a or cul4b.
Sequence:
MLTLASKLKRDDGVKGSRTSSTTSDSTRRVSVRDRLLVKEVAELEANLPCTCKVNFPDPNKLHYFHLTVSPDESYYQGGRFQFEIEVPDAYNMVPPKVKCLTRIWHPNITETGEICLSLLREHSIDGTGWAPTRTLKDVVWGLNSLFTDLLNFDDPLNIEAAEHHLRDKDEYRNKVEDYIKRYAR
The following text describes a protein:
Function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2) (By similarity). Might play a role in regulating synapse structure formation at neuromuscular junctions. Might play a role in maintenance of mitochondrial morphology.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MLRTRLIQAASSAQRAFSTSQKALAAKQMTVRDALNSALDDELARDDRVFILGEEVAQYDGAYKVSRGLWKKYGDKRVIDTPITEMGFAGIAVGAAMAGLRPVCEFMTWNFSMQAIDHIINSAAKTFYMSAGAVNVPIVFRGPNGAASGVAAQHSQCFAAWYAHCPGLKVLSPYDAEDARGLLKSAIRDPDPVVFLENELVYGTAFPVADNVADKDFLVPIGKAKVMRPGKDITLVAHSKAVETSLLAAAELAKKGIEAEVINLRSIRPLDTATIFASVRKTHHLVTVENGWPQHGVGAEICARIMEDQTFFELDAPVWRCAGVDVPMPYAKTLEAHALPRVQDLVEATLKVLGGKVGKAAAANK
The following text describes a protein:
Function:
May play a role in mitochondrial and peroxisomal fission.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Mitochondrion outer membrane; Single-pass type IV membrane protein. Peroxisome.
Sequence:
MVTPQSPTPMFNGLDDDLYSDAKYAHEINDKMRVPKRIKATGEYSNEDLLLSNQNGMISSWNYHDKIDMNVPDRIVVLGHNQHLETRSAPREIQLENSILPKNPSVGLVRVQTPPRIITLTDQHFPSASEESSPIRANGHHLYGNDLDEDADDEEVHATQYVRANGVARMGFQGNDTNSVESDSQLTTGSASKRSQLNQQQHNNLDASMLAHREGTPMGELTPHEEILYLRRQLAKLNRRVLNIEINNEQRTQREKIVYCLGLAYFVLKTIFWLNRN
The following text describes a protein:
Function:
Stabilizes the aggregates of proteoglycan monomers with hyaluronic acid in the extracellular cartilage matrix.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MKSLLLLVLISICWADHLSDNYTLDHDRAIHIQAENGPHLLVEAEQAKVFSHRGGNVTLPCKFYRDPTAFGSGIHKIRIKWTKLTSDYLKEVDVFVSMGYHKKTYGGYQGRVFLKGGSDSDASLVITDLTLEDYGRYKCEVIEGLEDDTAVVALDLQGVVFPYFPRLGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNTVPGVRNYGFWDKDKSRYDVFCFTSNFNGRFYYLIHPTKLTYDEAVQACLNDGAQIAKVGQIFAAWKILGYDRCDAGWLADGSVRYPISRPRRRCSPTESAVRFVGFPDKKHKLYGVYCFRAYN
The following text describes a protein:
Function:
Transpeptidase that catalyzes cross-linking of the peptidoglycan cell wall (Probable). Required for the regulation of cell length. Plays critical roles for the survival of the pathogen inside the host. Required for both bacterial survival and formation of granuloma structures in a guinea pig infection model.
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein.
Domain:
The apo form can adopt multiple conformations. The beta5-alpha11 loop near the active site is a flexible region that can adopt a variety of conformations in the acylated state of PBPA and appears important for acylation.
Sequence:
MNASLRRISVTVMALIVLLLLNATMTQVFTADGLRADPRNQRVLLDEYSRQRGQITAGGQLLAYSVATDGRFRFLRVYPNPEVYAPVTGFYSLRYSSTALERAEDPILNGSDRRLFGRRLADFFTGRDPRGGNVDTTINPRIQQAGWDAMQQGCYGPCKGAVVALEPSTGKILALVSSPSYDPNLLASHNPEVQAQAWQRLGDNPASPLTNRAISETYPPGSTFKVITTAAALAAGATETEQLTAAPTIPLPGSTAQLENYGGAPCGDEPTVSLREAFVKSCNTAFVQLGIRTGADALRSMARAFGLDSPPRPTPLQVAESTVGPIPDSAALGMTSIGQKDVALTPLANAEIAATIANGGITMRPYLVGSLKGPDLANISTTVGYQQRRAVSPQVAAKLTELMVGAEKVAQQKGAIPGVQIASKTGTAEHGTDPRHTPPHAWYIAFAPAQAPKVAVAVLVENGADRLSATGGALAAPIGRAVIEAALQGEP
The following text describes a protein:
Function:
Glucosyltransferase that uses UDP-glucose as the sugar donor to elongate alpha-(1->4)-glucans. Is involved in the biosynthesis of both 6-O-methylglucosyl lipopolysaccharides (MGLP) and glycogen. May also use ADP-glucose as substrate.
Miscellaneous:
MISCELLANEOUS: Attempts to disrupt both the Rv3032 gene and glgA in order to create a mutant simultaneously deficient in both alpha-1,4-glucosyltransferases turned out to be unsuccessful. Thus, M.tuberculosis H37Rv requires a functional copy of at least one of these two genes for growth. Moreover, it is not possible to inactivate Rv3032 in a mutant lacking treS, suggesting the joint essentiality of the different alpha-(1->4)-glucans biosynthesis pathways involving these two genes.
Sequence:
MRILMVSWEYPPVVIGGLGRHVHHLSTALAAAGHDVVVLSRCPSGTDPSTHPSSDEVTEGVRVIAAAQDPHEFTFGNDMMAWTLAMGHAMIRAGLRLKKLGTDRSWRPDVVHAHDWLVAHPAIALAQFYDVPMVSTIHATEAGRHSGWVSGALSRQVHAVESWLVRESDSLITCSASMNDEITELFGPGLAEITVIRNGIDAARWPFAARRPRTGPAELLYVGRLEYEKGVHDAIAALPRLRRTHPGTTLTIAGEGTQQDWLIDQARKHRVLRATRFVGHLDHTELLALLHRADAAVLPSHYEPFGLVALEAAAAGTPLVTSNIGGLGEAVINGQTGVSCAPRDVAGLAAAVRSVLDDPAAAQRRARAARQRLTSDFDWQTVATATAQVYLAAKRGERQPQPRLPIVEHALPDR
The following text describes a protein:
Function:
Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-9-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture. However, its presence in the virus may alter its pathogenicity. May become a target for both the humoral and the cellular branches of the immune system.
Subcellular Localization:
Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein. Note=In infected cells becomes incorporated into the envelope of virions during virus assembly at the endoplasmic reticulum and cis Golgi. However, some may escape incorporation into virions and subsequently migrate to the cell surface (By similarity).
Sequence:
MLRMRVRPPSAIPVFLIFVLLPFVLTSKPITPHYGPGHITSDWCGFGDSRSDCGNQHTPKSLDIPQELCPKFSSRTGSSMFISMHWNNDSDFNAFGYSNCGVEKVFYEGVNFSPYRNYTCYQEGSFGWVSNKVGFYSKLYSMASTSRCIKLINLDPPTNFTNYRNGTCTGNGGTAKMPDNPQLVIFNSVVKVSTQFVLPSSSDGFSCTKHLVPFCYIDGGCFEMSGVCYPFGYYYQSPSFYHAFYTNGTAGLHRYICDYLEMKPGVYNATTFGKFLIYPTKSYCMDTMNYTVPVQAVQSIWSENRQSDDAIGQACKSPYCIFYNKTKPYLAPNGADENHGDEEVRQMMQGLLVNSSCVSPQGSTPLALYSSEMIYTPNYGSCPQYYKLFETSSDENVDVTSSAYFVATWVLLVLVIILIFILISFCLSSY