lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit recognizes the wild-type Chi sequence, and when added to isolated RecB increases its ATP-dependent helicase processivity. Unlike the case in E.coli, suppresses RecA-dependent homologous recombination, is instead required for single-strand annealing pathway repair of DSB.
Miscellaneous:
MISCELLANEOUS: In the RecBCD complex, RecB has a slow 3'-5' helicase, an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-3' helicase activity, while RecC stimulates the ATPase and processivity of the RecB helicase and contributes to recognition of the Chi site.
Sequence:
MALHLHRAERTDLLADGLGALLADPQPDPFAQELVLVAARGVERWLSQRLSLVLGCGPGRADGVCAGIAFRNPQSLIAEITGTLDDDPWSPEALAWPLLAVIDASLDEPWCRTLASHLGHFATTDAEAELRRGRRYSVARRLAGLFASYARQRPGLLAAWLDGDLGELPGDLAWQPPLWRALVTTVGADPPHVRHDKTIARLRDGPADLPARLSLFGHTRLACTDVQLLDALAVHHDLHLWLPHPSDELWRALAGFQGADGLLPRRQDTSRRAAQHPLLETLGRDVRELQRALPAARATDEFLGATTKPDTLLGWLQADIAGNAPRPAGRSLSDADRSVQVHACHGPARQIDVLREVLLGLLEDDPTLQPRDIVVMCPDIDTYAPLIVAGFGLGEVAGDCHPAHRLRVRLADRALTQTNPLLSVAAELLTIAETRATASQLLNLAQAAPVRAKFGFADDDLDTITTWVRESNIRWGFDPTHRRRYGLDTVVHNTWRFGLDRILTGVAMSEDSQAWLDTALPLDDVGSNRVELAGRLAEFVERLHHVVGGLSGARPLVAWLDALATGIDLLTACNDGWQRAQVQREFADVLARAGSRAAPLLRLPDVRALLDAQLAGRPTRANFRTGTLTVCTMVPMRSVPHRVVCLVGLDDGVFPRLSHPDGDDVLAREPMTGERDIRSEDRQLLLDAIGAATQTLVITYTGADERTGQPRPPAVPLAELLDALDQTTSAPVRERILVTHPLQPFDRKNVTPGALLGAKPFTFDPAALAAAQAAAGKRCPPTAFISGRLPAPPAADVTLADLLDFFKDPVKGFFRALDYTLPWDVDTVEDSIPVQVDALAEWTVGERMLRDMLRGLHPDDAAHSEWRRGTLPPGRLGVRRAKEIRNRARDLAAAALAHRDGHGQAHDVDVDLGDGRRLSGTVTPVFGGRTVSVTYSKLAPKHVLPAWIGLVTLAAQEPGREWSALCIGRSKTRNHIARRLFVPPPDPVAVLRELVLLYDAGRREPLPLPLKTSCAWAQARRDGQDPYPPARECWQTNRFRPGDDDAPAHVRAWGPRAPFEVLLGKPRAGEEVAGEETRLGALAARLWLPLLAAEGSV
The following text describes a protein:
Function:
Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
Sequence:
MELPLGRCDDSRTWDDDSDPESETDPDAQAKAYVARVLSPPKSGLAFSRPSQLSTPAASPSASEPRAASRVSAVSEPGLLSLPPELLLEICSYLDARLVLHVLSRVCHALRDLVSDHVTWRLRALRRVRAPYPVVEEKNFDWPAACIALEQHLSRWAEDGRWVEYFCLAEGHVASVDSVLLLQGGSLCLSGSRDRNVNLWDLRQLGTESNQVLIKTLGTKRNSTHEGWVWSLAAQDHRVCSGSWDSTVKLWDMAADGQQFGEIKASSAVLCLSYLPDILVTGTYDKKVTIYDPRAGPALLKHQQLHSRPVLTLLADDRHIISGSEDHTLVVVDRRANSVLQRLQLDSYLLCMSYQEPQLWAGDNQGLLHVFANRNGCFQLIRSFDVGHSFPITGIQYSVGALYTTSTDKTIRVHVPTDPPRTICTRRHDNGLNRVCAEGNLVVAGSGDLSLEVWRLQA
The following text describes a protein:
Function:
Virulence effector that plays a role in hijacking the host vesicular trafficking by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). Acts as a phosphocholine hydrolase by mediating the hydrolysis of phosphocholine to Ser residues of host RAB1 (RAB1A, RAB1B or RAB1C). Dephosphocholination of target proteins restores accessibility to GTPase effector LepB. Can act on both GDP-bound and GTP-bound Rab proteins.
Subcellular Localization:
Secreted. Host cytoplasm. Note=Translocated into the host cell via the type IV secretion system (T4SS).
Sequence:
MKLRYIINENKLVFTSCNMRDKIITGKKIIFSQSVAKDQTKNLSSFLSERFYSVNQSHNHSIIIGSSLSHQENDIEHDTILDTSGVLVTTDTNGIVNGARVAITDGLGGGNGDQEEDDEIYRVSHSSCENFLNCDQNIDTTLSLITQPKASDKKQTAPKTLQHTEASMAAFIYQNHPGKGYIGEFANIGDGLIIILDKRFKIKHMVSACHIYRGFGTWTPPSLQALATTANKDALLVRQTLKLAEGDIIISMTDGVWGELKTSLIAQTNDRRDIGVDKEYFKTLFDELTDAPYPSSFDIARIITQRAMSRSLERRKTLIKLINEIEQQHFHEKSVKTINEVLEYFIKTGHVETAQTLKAILFEDGLSDGITYFENIEIPLEMVMHDLKSRTVGDCSTINVTRIPYHLDELIRGFINYPEKHQILAPLFKARVKSEADLEEAFHRLSLEMVQPEIECPISETHFERAFKKETLDKTQAVLTHYFRISTGLDSKKNYQERLNDLSAYLSKESSLEKNDIKLLLSMLDSEIKPKTGVFQTLFGENQNKLYKAFHKKIELQLLDSEIENKNELK
The following text describes a protein:
Function:
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. Plays a central role in positioning the mitotic spindle at the bud neck during cell division. Targets cytoplasmic dynein to microtubule plus ends, thereby promoting dynein-mediated microtubule sliding along the bud cortex and consequently the movement of the mitotic spindle to the bud neck. Following plus end binding, dynein may be offloaded to the cortex by NUM1. Required for viability in the absence of the kinesin-related microtubule-dependent motor protein CIN8.
Subcellular Localization:
Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle pole. Nucleus. Note=Localizes to the plus ends of cytoplasmic microtubules.
Domain:
Dimerization mediated by the LisH domain may be required to activate dynein.
Sequence:
MTNWQQQLPLTDTQKNELDKSVLRYLNWNYKQTVRHEHAQDYESVRHAIVTLSGFLLQESVDRQEFISNNDTSNESMVDIDELLLPKKWNSIVRLQKKIIELEQNTETLVSQIKDLNTQVSELAQFKPTTSNGTSAHNVLKWIPRNLPSCLINVESSVTSVKLHPNLPIVFVATDHGKLYAFDLFNYTIPLASLQSHTKAITSMDVLFTNYTNSSKKNYLVIVTASKDLQIHVFKWVSEECKFQQIRSLLGHEHIVSAVKIWQKNNDVHIASCSRDQTVKIWDFHNGWSLKTFQPHSQWVRSIDVLGDYIISGSHDTTLRLTHWPSGNGLSVGTGHEFPIEKVKFIHFIEDSPEIRFRTPSTDRYKNWGMQYCVSASRDRTIKIWEIPLPTLMAHRAPIPNPTDSNFRCVLTLKGHLSWVRDISIRGQYLFSCADDKSVRCWDLNTGQCLHVWEKLHTGFVNCLDLDVDFDSNVTPRQMMVTGGLDCKSNVFMR
The following text describes a protein:
Function:
Cyclin-dependent protein kinase (CDK) inhibitor that functions as a repressor of mitosis in the endoreduplication cell cycle. Inhibits the kinase activity of CYCD3-1/CDKA-1, CYCD2-1/CDKA-1 and CYCB1-1/CDKB1-1 complexes in a dose dependent manner. Cooperates with SMR1 and SMR2 to promote endoreplication during leaf development. Required for normal trichome endoreplicating cell cycles. Positive regulator of effector-triggered immunity (ETI).
Miscellaneous:
MISCELLANEOUS: Plants over-expressing SIM are dwarf with serrated leaves containing enlarged cells with increased levels of nuclear DNA.
Subcellular Localization:
Nucleus.
Sequence:
MDLDLIQDLPILNFPPAIKIRANTNRDDDGGGCTTPTSSDHKIPPTTATTPPPPPQKPRPPSTPSSLGIRSCKRKLMTSLSKYEIIVNKDEIERFFSSVYNQTMASSTTTAITVAKRRRSFRSCSRR
The following text describes a protein:
Function:
Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass type II membrane protein; Intermembrane side. Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MSLPDISRRRSPVPQEDWPLTPNALRPSPFPNPVLQALYSLSRVLLFPTYWSLDQLLGCWAPSVRSKSLGWFKVLAGSGVLLPLVVVGLPLALVGLALWLPLQVWRRPFCYQPPPACWVWPQPWHPPAERRRCFVFLTANLCLLPHGLAHFNNLSHSLQRAEAVGAALLDSLQSSQYRVSECSQPPPRVPGGELKATLPMGLDFVCLQEVFDLRAARRLVRVLVPNLGPVIYDVGTFGLMAGPYIKVLGSGLLLASRYPLLRATFRCFPNARREDAMASKGLLSVQAQLGIVDGHPIVGYLHCTHLHAPVEDGHIRCKQLTLLLEWVEEFEAENRQSDEAVAFSVLLGDLNFDNCSQDHAKEQGHKLFSCFQDPCRLGVCQEQPWALGTILNSSMLRHSIACSPEMLRRALRQEKGRRLYLSGPLHGSYPAQSWKGRRLDYITYRRVPGSRLSPEAEQVTFSTAFAGLTDHLAMGLKLQVVCS
The following text describes a protein:
Function:
Acts as an anion channel mediating the transport of chloride, bromide, iodide, nitrate, sulfate, gluconate, thiocyanate, oxalate and bicarbonate ions (By similarity). Its permeability towards bicarbonate is weak and increases when pH is above 7 (By similarity). Mediates thiocyanate transport in retinal pigment epithelium cells (By similarity). Mediates iodide transport in the thyroid gland, playing an important role in the synthesis of thyroid hormones and the maintenance of thyroid function (By similarity).
Subcellular Localization:
Basolateral cell membrane; Multi-pass membrane protein. Recycling endosome membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Lateral cell membrane; Multi-pass membrane protein. Note=Expressed in the cytoplasm in recycling endosomes of medullary collecting duct cells and in acid-secreting gastric parietal cells. Targeted to the basolateral membrane in hypertonicity and potassium depletion.
Sequence:
LFSFKELNEQFKRKIKVVLPVDLVLIIAASFACYCTNMENTYGLEVVGHIPRGIPPPRAPPMNILSAVITEAFGVALVGYAASLALAQGSAKKFKYSVDDNQEFLAHGLSNVISSFLFCIPSAAAMGR
The following text describes a protein:
Function:
Involved in protein trafficking. May serve as a receptor for ARFRP1 (By similarity).
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MAGQFRSYVWDPLLILSQIVLMQTVYYGSLGLWLALVDGLVHSSPSLDQVFDAEILGFSTPPGRLSTMSFVLNALTCALGLLYFIRRGKQCLDFTVTVHFFHLLGCWLYSSRFPSALTWWLVQAVCIALMAVIGEYLCMRSELKEIPLNSAPKSSV
The following text describes a protein:
Function:
Transcriptional activator of promoters containing ATF/CREB sites. Can independently stimulate transcription through ATF/CREB sites. Important for a variety of biological functions including growth on non-optimal carbon sources. Regulates the expression of COS8. Has efficient silencing blocking activities.
Subcellular Localization:
Nucleus.
Sequence:
MDYKHNFATSPDSFLDGRQNPLLYTDFLSSNKELIYKQPSGPGLVDSAYNFHHQNSLHDRSVQENLGPMFQPFGVDISHLPITNPPIFQSSLPAFDQPVYKRRISISNGQISQLGEDLETVENLYNCQPPILSSKAQQNPNPQQVANPSAAIYPSFSSNELQNVPQPHEQATVIPEAAPQTGSKNIYAAMTPYDSNIKLNIPAVAATCDIPSATPSIPSGDSTMNQAYINMQLRLQAQMQTKAWKNAQLNVHPCTPASNSSVSSSSSCQNINDHNIENQSVHSSISHGVNHHTVNNSCQNAELNISSSLPYESKCPDVNLTHANSKPQYKDATSALKNNINSEKDVHTAPFSSMHTTATFQIKQEARPQKIENNTAGLKDGAKAWKRARLLERNRIAASKCRQRKKMSQLQLQREFDQISKENTMMKKKIENYEKLVQKMKKISRLHMQECTINGGNNSYQSLQNKDSDVNGFLKMIEEMIRSSSLYDE
The following text describes a protein:
Function:
G protein-coupled receptor activated by the neuropeptides vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating polypeptide (ADCYAP1/PACAP). Binds VIP and both PACAP27 and PACAP38 bioactive peptides with the following order of ligand affinity VIP = PACAP27 > PACAP38. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors. Activates cAMP-dependent pathway.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSWGDWRRLKPRAPPRGRLHPGTFRRPQPTAGGGGGGGAGGGKKRHALSRSPARLHRLPRRGNAKRRGWQGGFLEEVALEVDVESVLGWGRGGGWGWETASRRLEGEPSRKDAAGWGLETPEGAGPGAEGLQGGQATNLQWEEECYHLRMIEEQHKKCLEEAQLENNTAGCSKMWDNLTCWPATPPGQVVVLACPLIFNFFSPIRGRNVSRSCTNEGWTHLEPGPYPFACGLDDKTSDVDQQQQSMFYSSVKTGYTIGYSLSLATLLVATSILSLFRKLHCTRNYIHMHLFISFILRAASVFIKDLTLFNSEELDYCTKGSVSCKAAMVFFQYCVMANFFWLLVEGLYLHTLLAVSFFSERKYFWGYILIGWGVPSTFTMVWTIIMIRFEDYGCWDTINSSLWWIIKAPILTSILVNFILFIRIIRILVQKLRSPNVGKSDSSPYSRLAKSTLLLIPLFGVHYIMFAFFPSNFKAEVKMVFELIVGSFQGFVVAILYCFLNGEVQAELRRKWRRWHLQGILGSDAKYQHPSGGSNGATCSTQVSMLTRVSPGARRSSSFQAEVSLV
The following text describes a protein:
Function:
Channel protein that facilitates the transport of water, glycerol and hydrogen peroxide across membrane of cell or organelles guaranteeing intracellular homeostasis in several organes like liver, kidney and brain. In situation of stress, participates in endoplasmic reticulum (ER) homeostasis by regulating redox homeostasis through the transport of hydrogen peroxide across the endoplasmic reticulum membrane thereby regulating the oxidative stress through the NADPH oxidase 2 pathway. Plays a role by maintaining an environment suitable for translation or protein foldings in the ER lumen namely by participating in the PKD1 glycosylation processing resulting in regulation of PKD1 membrane trafficking thereby preventing the accumulation of unfolding protein in ER. Plays a role in the proximal tubule function by regulating its endosomal acidification. May play a role in postnatal kidney development.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSPLLGLLPELQDSCTSLGLMLSVVLLMGLARVVARQQLHRPVAHAFVLEFLATFQLCCCTHELQLLSEQHPAHPTWTLTLVYFFSLVHGLTLVGTSSNPCGVMMQMMLGGMSPETGAVRLLAQLVSALCSRYCTSALWSLGLTQYHVSERSFACKNPIQVDLLKAVITEAVCSFLFHSALLHFQEVRTKLRIHLLAALITFLVYAGGSLTGAVFNPALALSLHFMCFDEAFPQFFIVYWLAPSLGILLMILMFSFFLPWLHNNHTINKKE
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.
Sequence:
MNRIARISARIPARIPAHLRQASTASTASTVISTAEEKKPPLKEKKVDWKTDLLKILETEHKQKKRKLWKMRVDQQAMADIFRFTLKDDVQSLVRLTENQLRSRHSPETVPVCFLVLHKKMEKILKKVEAIESPDSLSIFIGIADLYRSIKRNETNTTYLMALLLLSSLRKWKDQRSYEERSSKTIADLFDSMEQKMRQLAKGVNVEEREMEVFLNSDDHKAIQNEVEMLRSFSVPVPRKKEGARYSEELEDLIGPLQTNCHQEEYRNNPFQVDGMEKGKYKTLFEEHLKTESTMWIQVKNTVGEAAEKNGKSGEELITEWDWRKRISDGLRKLDPNDTHPLVSTCLELLPREKLVEILYFTVVAACSQGQNLIGATQFQYDVLDPILKELGNAFKKELGFNETEIWKRVFDSYINYFLDSGVSRQNTHREWWSKACKQQNLAPNFKFQMGNLDAETRNEVCNVIVDVLFNSCLFPVESKDGKNFSPFEVIFPHLSMSPFNKKFAVTWTRSFSYRSISIEEESKLSTDCRLSLSRMLSINSKLMAMFDKNPFDFIVFSTFNLPMTVPPRPWIDRGTGGPLYTAGQDIIRNMFEFKSVRLNDEMRQRIQSPAQGRPVFDALNQLGSTPWVINESMLDTLKTVFGQSGCKESEPLLEKLGIPMRHDTFDVPDFVREFGNVKKEDVDVEKFRRYAKKKAEAVKMRNESNSLWCWMQYRVVLADHFRGQTLFFPHNMDFRGRVYPLSPYLSHMGDDVNRCILKFAKSQPLGSHGFDWLKLHCVNLTGTMKRASVADRMVEAERLIPSILDSARNPLNGEKWWMSSDEPWQTLAACVEIENAMKYGSDVASFPSQLPVHQDGSCNGLQHYAALGRDNEGGVQVNLTQCETPNDVYSDVAQRVEQKRKQDEESNGEDRDVALKLREALPQNVPRKVIKQTVMTTVYGVTMYGAVLQIKRQLKAMDIPGEDAAIFARYLARKTFASLNDAFTSSMALKDWFRLIAKGASDLMKTVEWVTPLGLPVVQPYCRLLERKSKLVLVPIPMKQVDAFPPNFVHSLDSTHMMLTSLNCANRGITFAAVHDCFWTHANSVDEMNQICRQQFVSLHSQPIVEQCSEWFKTTYLTPRIQKILPPSEVDRFADIFTVKVKQGELDIEKVKDSVYFFS
The following text describes a protein:
Function:
Phosphorylates yap-1 which may negatively regulate yap-1 nuclear localization. Plays an essential role in larval development. Regulates growth, the formation of gut granules, lifespan and cell and body sizes probably in synergy with the TGF-beta sma/mab pathway. Does not appear to regulate apoptosis and proliferation. In addition, may synergize with the TGF-beta daf-7 dauer pathway to regulate entry into the dauer stage. Maintains the cellular integrity of intestinal cells by regulating the localization of apical actin and junctional proteins.
Subcellular Localization:
Cytoplasm. Apical cell membrane. Note=In epithelial cells, localized near the plasma membrane. In intestinal cells, localized in the subapical membrane region. Membrane localization starts in the late embryo.
Sequence:
MRPAAPGTTPNGASSDIRHQRGVAPIPFGSTNSAIDAHHNSEIRVGRHRAKLDEIRESLKAYEHEAGLLSSHVALGSLATPSSSSVSHSDITNDNAEVMNFSSSSSNAAATTTTVSSAAVSNSNSFRTEGGGHKMRITPMPQRHLMMDTGANETVFRSGKEMIRNGNPSTTISSTPSTTTEESIRIHPAGYRYDMPTPAYHMNNNAPQYSPGYSRPPPPAYDSSPVNTRMTPVATDNYRTHLHMKVHPVVKAPPPNPTMLNHNKNMAPPPPPPAKSTISIETMSEERKADNIQRLYHTSMDKKTASSVVSINVASPHTTKVNVGDSPLPSKSFIIGPRYTADVDRKNFVNYKDELRPDPRLIPSTSDANHEDFRPILFKPRNLEITMKSRAQPPPPQYNQPSEPPPKRVSSPIDRTLLEPYIKNTRRVQPCKPNMLRFYMEQHVERLLQQYKEREKRMKQLEKEMVSAQLPDIMRNKMLGLLQQKESKYTRLRRQKMSKSHFTVISHIGVGAFGKVSLVRKNDTRKVYAMKSLEKADVIMKQQAAHVKAERDILAEADSPWIVRLFFSFQDDACLYFIMEYVPGGDMMTLLIQKGIFEEDLARFYIAELACAIEYVHNVGFIHRDLKPDNILIDQHGHIKLTDFGLCTGLRWTHDRRYYGPENDHHRVDSFSLPPEVAAIDKSVKVLNVRQQTRRITAHSLVGTGNYMAPEVIAKTGHNQSCDWWSTGVILYEMVFGRVPFHDDTPGGTQHRIKNWRNFLDFTYCGNLSKECLMMIQQLICDASSRLGSHGKDVAERTAQVKNHPWFRGIDWVNLRKLRADYIYIPRVTHDEDTSNFETFQDNDRADKPNVRGLHNPAFYEFTYRHFFDTDSVGCPSLRPSRRRSLRPLLENGTFNESVSEEDSSSHI
The following text describes a protein:
Function:
Transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA4, GATA5 and GATA6. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. Also required in gonadal differentiation, possibly be regulating expression of SRY. Probably acts a corepressor of NR2F2.
Subcellular Localization:
Nucleus.
Sequence:
MSRRKQSKPRQIKRPLEDAIEEEEEECPSEETDIISKGDFPLEESFSTEFGPENLSCEEVEYFCNKGDDEGVQETAESDGDTQSEKPGQPAVETDDWDGPGELEVFQRDGERKIQSRQQLPVGTTWGPFAGKMDLNNNSLKTKAQVPMVLTAGPKWLLDVTWQGVEDNKNNCIVYSKGGQLWCTTTKAISEGEELIAFVVDFDSRLQAASQMTLTEGMYPARLLDSIQLLPQQAAMASILPTAIVNKDIFPCKSCGIWYRSERNLQAHLMYYCSGRQREAAPVSEENEDTAPQISSLCPFPQCTKSFSNARALEMHLNSHSGVKMEEFLPPGASLKCTVCSYTADSVINFHQHLFSHLTQAAFRCNHCHFGFQTQRELLQHQELHVPGSKLPRESDMEHSPSGTEDSLQPATDLLTRSELPQSQKAMQTKDASSDTELDKCEKKTQLFLTNQRPEIQPTTNKQSFSYTKIKSEPSSPRLASSPVQPNIGPSFPVGPFLSQFAFPQDITMVPQASEILAKMSELVHRRLRHGSSSYPPVIYSPLMPKGATCFECNITFNNLDNYLVHKKHYCSSRWQQMAKSPEFPGVSEKMQEAVSPNTGQPSINLLNPAAHSADPENPLLQTPCINSSAVLDLIGPNGKGHDKDFSTQAKKLSTPNSNDDKINGKPVDVKNPSVPLVDGESDPNKTTCEACNITFSRHETYMVHKQYYCATRHDPPLKRSASNKVPAMQRTMRTRKRRKMYEMCLPEQDQRPQLVQQRFLDVANLSNPCTSTQEATEGLGECYHPRCELFPGIVSKHLETSLAMNKCVPVSKCDTAHSSVSCLEMDVPIDLSKKCLSQSERTTASPKRLLDYHECTVCKISFNKVENYLAHKQNFCPVTAHQRNDLAPLDSKVFPNPESERSSPDVSYERSIIKCEKNGNLKQPSPNGNLFSSHLATLQGLKVFSEAAQLIATKEENKHLFLPQCLYPGAIKKAKGADQLSPYYGIKPSDYISGSLVIHNADVEQSTNAENESPKSQASSNGCAVPKKDSLPLLPKNRGMVIVNGGLKQEERPAANPQQENIAQNPQREDGHKSPSWVSENPLTTNENVSPGIPSAEDQLSSIAKSVNGSTQAPTSGKYCRLCDIQFNNLSNFITHKKFYCSSHAAEHVK
The following text describes a protein:
Function:
Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins.
Subcellular Localization:
Secreted.
Sequence:
MHRWSSWRLGAPLFALLATLIVVPLGSAFTDPYDILHHVGTTSFLPEYYQPDTDEICIRNGIRNVACSADNFRLVKLDSVTRANLHQLIAQKQNEPSMMQLAVYVMLVDLERNMHHGWQVGQSTAQQARATINDQVQMHLGLAVSQSDMDPSIDGPGAAKRLGAPPVTAQEESCYKRWLQRNKFATADVDTALNELYVRHVTITQDKKRWDIQSTTGCTENTLLKRDTGDRVDAVVDDDMNVYHPVLGTHNQDPWAKWREFDARHEFLPSGEFGHRKRSIQRRENCVGGHRHRKRGGRAEQQGADASVPLASGVDYAINMPSAPTPGGVGAGVVGDAGLGGSRISSQPHGFAAQVTGGGSTAAVVPKDVNELVQLLSDAQPRVIHLDKVYDLRTTEGICTNCRGCIPDSYVKCPDKGQLAIDNGQGWCKDKRATAVTYDKAGLTPITVSSNKSVIGITSNAAIRGKGLRIAHHQNVILHNFRIDEINPQYIWGGDGITLYDTDLIWIDRITFAHIGRQFIVTGYESAGRVTISNCLFDGATKWSATCDGSHYWTVLGYGSGDKVTFSSNVMSNCSGRSPRIASPDANGQQPAVWHIVNTIFDHNTGHSLDMGPGVSALIEGNVFNDVAQTSLHEATPGKAFAPSDQPVCNQCKGPLGRNCQPNAYKNANPVPSTSNPADVLKDVAKEKVSGAMSPRQVIESVSKSAGAAGAAAVIGASSPDASPGASGDAKLSYAAALSAPQQPPSAGQGKAAAVSPDIKKQQEEEQNKKQQEQEQNKKQQEEEQNKKQQEQEQNKKHDQQKQREKKQQEDEKKQQQQKPPSPPAPPSPPSPK
The following text describes a protein:
Function:
Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Required for heme utilization and virulence.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein; Periplasmic side.
Sequence:
MQQTKRSLLGLLISLIAHGIVIGFILWNWNEPSDSANSAQGDISTSISMELLQGMVLEEPAPEPEDVQKEPEPEPEPGNVQKEPEPEKQEIVEDPTIKPEPKKIKEPEKEKPKPKGKPKGKPKNKPKKEVKPQKKPINKELPKGDENIDSSANVNDKASTTSAANSNAQVAGSGTDTSEIAAYRSAIRREIESHKRYPTRAKIMRKQGKVSVSFNVGADGSLSGAKVTKSSGDESLDKAALDAINVSRSVGTRPAGFPSSLSVQISFTLQ
The following text describes a protein:
Function:
Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Early endosome. Membrane; Multi-pass membrane protein.
Sequence:
MGFSADNLKGFVLALLSSGFIGASFIIKKKGLRRAAAASGVRAGVGGYSYLFEPLWWAGMITMIVGEVANFVAYAFAPAVLVTPLGALSIIVSAVLAHFILKERLHKLGILGCVMCIAGSVVIVIHAPQEHLITSVQEIWSLATQTAFLLYVASVIVLVFVLVFHFAPRYGNTNVLVFTGICSLMGSLSVMSVKAIGTSLKLTFEGNNQLVYPETWFFMLVVVTCVVTQMNYLNKALDTFNTAIVSPIYYVMFTTLTILASVIMFKDWDGQSGGSIVSEICGFIVVLSGTILLHVTKDSDRSSSFRGNYAPLSPSLSARLYSGNGELLKHGDEDASTSEEICLKRQELY
The following text describes a protein:
Function:
Part of the multicomponent anthranilate dioxygenase, that converts anthranilate to catechol. This protein seems to be a 2Fe-2S ferredoxin.
Sequence:
MTEATLAEWHPLGAIDEFTEDEPAARVAGQKPIAVFRIGDELFAMHDLCSHGHARLSEGYVEDGCVECPLHQGLIDIRTGAPKCAPITEPVRVYPIRIVDGQVEVNVG
The following text describes a protein:
Function:
Catalytic subunit of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine.
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum. Membrane; Single-pass membrane protein.
Sequence:
MAQADFVSPTSIDVSEKKEVEFHKKVDHVENPPLSTESAKLEAEEVAAEKLNSEHLLENEFAPITDPTHRRVSKNPDGAELFQFEDEPSYYYVVATYLTYLVLIIIGHVRDFFGKRFHKDDYKYLKDNDGYAPLYNHFDNFYVRRLQHRINDCFSRPTMGVPGRVIRLMNRYSTDSNSTFKLTGDTSLALNVSSYNYLGFAQSHGPCATKVEEAMQKYGLSTCSSNAICGTYGLHKEVEELTANFVGKPAALVFSQGFSTNATVFSTLMCPGSLIISDELNHTSIRFGARLSGANIRVYKHNDMTDLERVLREVISQGQPRTHRPYSKILVVIEGLYSMEGNFCDLPKVVELKNRYKFYLFIDEAHSIGAIGPRGGGICDYFGISTDHVDILMGTFTKSFGAAGGYISATPNIINKLRVTNPGYVYAESMSPAVLAQIKSSFLEIMDNSPTSAGLERIERLAFNSRYIRLGLKRLGFIIFGNDDSPVVPLLLYNPGKINAFSHEMLKRGIAVVVVGYPACPLLTSRVRFCFSASHNKADMDYFLRACDEVGEKLQLKFSTGAAGEDVGKTNVEKMKKNQGWFKPPRWKIEDVLKHGVHDALTQ
The following text describes a protein:
Function:
DNA polymerase II participates in chromosomal DNA replication.
Subcellular Localization:
Nucleus.
Sequence:
KLGWLLNLRSCTLPDPLEGKNEVSGLELYFLEQDGKAFKTRIIYQPYFYVRPEANRSQDVIAYCLRKFEGLVAKAERVFREDLDMADHLNGKKALYVKLSFATVTDLMTVKRELTPLVARNQERLQARQAYEMQGQAREQVTEDDLIFGVDTDGMKGAGTDESESALLELREYDVPYPMRVDQIYMISYMIDRQGYLIVNREFVSEDIQDFEYTPKEAYPGPFIVFNEENEEQLLKRFFEHILDEKPHIFVTYNGDFFDWPFIDARAQIHGINMGREIGISLDERSGEYRGRCSVHMDAFCWVKRDSYLPQGSQGLKAVTKYKLGYDPVEVDAEDMVALARDEPLKMASYSVSDAVATFYLYDKYVHLFVFSLCTIIPLGSEDVLRKGSGTLCEALLMVEAFEGNIVCPNKQSSAHEEKFYKGHLVESETYVGGHVECLESGVFRADFLYDFQLVPSAFQQLIDNIDRDLRFSLEIEMDVPLDRVANYNEVKRDIVDRLVALRERPNRKEQPLIYHLDVAAMYPNIILTNRLQPCAIVNEADCAACAYNTECGRAAIKQKDASCQREMDWVWRGDFYPATRPEYYSIKTQIEYENFSVDKPGGAANADPGKKNINASLPFAQLPTDKQELLLKQRFKSYCSSVYKKTKVTEEQKRSATVCMRENPFYVNTVRAFRDRRYEYKGLTKVWKKKVSQAAESKDLLATIDAQNKCLVYDSLQLAHKCILNSFYGYVMRKGARWHSMEMAGIVTHTGSNIITGARELVEQIGRPLELDTDGIWAILPKSFPETFSFKLKDGGSRSISYPCVMLNADVHAKFTNPQYHELDPATGKYNTHKECSILFEVDGPYKAMVLPASTEEGKLLKKRYAVFNFDHSLAELKGFELKRRGELQLIKAFQSQVFECFLDGDSLEECYASVAKCANRWLDVIDTRGKSMDDEELMALITENKSMSGKLDEYEGQKSTSITTARRLGEFLGEEMVKDKGLTCKMIIVSRPYGEKVTERAIPTAIFATEDAVKRHFLKKWLKDPHLQDFDIRSILDWDYYRTRFASTVQKIISLPAAFQNVRNPVPRIELPDWMRKQVREKNAKHQQGNMKQFFKAAAKGADNGDYVAQLIDMEDLMKGTPPSRPKPPQHRKRGNKTSDENDTSSSTIEEIDDDDMEGVPAANVKLGEVPFTDWLKNRKKKWKSMLGKRRQEREERMRSFGGAAKGNGVGMENFVFDAGSALQREYWQIVEVQQEQGGLFTCWVLTAHSQMLQRITLKMPRVFYITCEEADQEDLLLQLPGARRVSRIVPHYSSKPQSVLEVMLSERQYQQYHKEISQILGDPHVKGVYELQVSALTRAVCALGCVAKVVNPHLSSTNQEYELSDLQFQSTAQASYLMEPQRSLMANREASSPPNSLMRRVLLYFAQQKKRAILGLVVLKEEDDDVSADSLGSAISEGDAHVWYVDPFSNVKSRGSDLKQFFDQLLQESQEEGGPTIVVAQTCIPSSKRLREKIQGLHSFPIAMLPWNEEDTLFPALTWRKLMGEKMLTRCFEMTQYYSDVLDCARYAHLPVGNFTGDHSIAILDTLYSRILTKHKHLWWHSPTSLPDLGGKEQEQQFQQLFSQSLLGSAQQSAPKKGEMISQHRVDTSVVVCEKGSFIDVCVELELDGLAVNAILVASQIHSIEGLGVAHQMEIDFDGNADGEPDTKAESSGAAVAEGDAEESCHEAFRLLRLMVTTLFKDFLASRNKFADHVLQQFYRWLCSPNSLSFDPALHAMVKRLMEKLFLQLLAEFRRLGSQIVYADFSKIIVCTKKKSVRDAQTYLNFILQTVLSNELFQVLNFTPKKYFSNLFFMDAENYGCILLKNVVPEGEQEEENDHDSEGSGEKKPLEIVSHWNIANYLPRGVDEYFLILVGQFIRRRAEFQLRELQRLLKGGDAKHDVAEDPDEQPLDDDEKQLTPLAKYSQRLVSSYFSDKMLRLVPEILTYNMDRDSFPVFAGSHLAMESPALELVKFVCAVFKLEPNVEAQVGKMRRTLLKLLRTSEFGDEAQFRNPSLSFTVQDVICLCCNLCRSVDLCRDPQLFKGSASRSDEDDEGQENAEDAETASAWHCPRCFALYDKTAFEMRLVEMVQAQSVAYQLQDLYCRKCHLPAEHKMREYCPCSGTYALMPGVRESLLETLRLLRRIAQQHNFEWLLETVQRL
The following text describes a protein:
Function:
Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).
Sequence:
MPQSHLSNGDPRPPPGDKLRLYSMRFCPYAERPRLVLAAKGVDYECININLKNKPDWYLAEPNPRGLVPMIEMPDGRLLPESLLCCGGGVPMGGYSLGKMYPGMVYPGGSVPRGGVPRAEVYPMGEYLDELFPQNPMYPSDAFEKNRQRLLIDRFGKVTSSFYQMLMRDMDEDALKGQTETLNKELSLYENELKNKTFFAGEKPGMADFMLWPFFERFCLLEGKYEISAKSFPALTKWISSMHQDPAVKDVEFSPALLRRNFVDSVHKGIPEAALYE