lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Subcellular Localization:
Cytoplasm.
Sequence:
MAERFDRIWHNARLATMRADRPDLGEIEHGLIAARGGHIVYAGAAADFPADADAIKRIDCAGRWITPGLVDCHTHLVYGGNRAHEFELRLKGASYEEIARAGGGIVSTVAATRKASEAELVASALPRLDALIGEGATTVEIKSGYGLDAETEMRQLAAARSLGRQRPVAIRTSFLGAHALPPEADGDKDRYIDLVCKEMLPAVAKAGLADAVDTFMEGIAFSAGQTARVFETARGLGLPVKLHADQLSNLGGAALAAKFSALSADHLEHTDEAGAAAMAKAGTVAVLLPGAFYFIRETQKPPVESFRKHGVHMALASDCNPGSSPLTSLLLAMNMGATLFRMTVAECLAGVTREGAHALGVLDETGTLEAGKWCDLAIWDIERPAELVYRIGFNPLHRRVWRGQ
The following text describes a protein:
Function:
Involved in degradation of glycine betaine. Part of a Rieske-type oxygenase system that catalyzes the conversion of glycine betaine (GB) to dimethylglycine (DMG) (Probable). This subunit is the terminal oxygenase component of the system (Probable). Required for growth on choline and GB, but not for growth on DMG.
Sequence:
MDVTSTLSLGDPLEPARKATADMLRSRDHSFSLPQPFYCDQRLFEIDMQEIFHKEWLIAGMTCEIPAKGNFLTLQIGKNPVLVIRGAEGQVHAFHNVCRHRGSRLCVSEKGKVAKLVCPYHQWTYELDGRLLFAGTEMGADFDMKEYGLKPIQVKTAGGYIFISLAENPPAIDDFLATLEHYMEPYDMENAKVAVQTTIREAANWKLVIENNRECYHCNGSHPELLKTLLEWDDVTDPRASQAFKDQVAACTSAWDAEKIPYAHASFGLRNRIVRMPLLDGTVSMTMDGKQGSKKLMGRIKNPDLGSMRILHLPHSWNHCMGDHLIVFTVWPISAQETLVTTKWLVHKDAVEGVDYDVARLREVWDATNDQDRRLAEENQRGINSDAYQPGPYSKTYEFGVINFLDWYSERMLNNLGEESAHVRKVAGS
The following text describes a protein:
Function:
Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
Sequence:
MTAPTFPMHVSVAQARELFAALLPAPPVVTLPLRKALGCTLGADLTALVSHPSATESALDGIACREADTLTASAGAPVALRVVGESRAGEPFAGEVGPGECVRIYTGAPLPPGTDAICPVEQLREGEGTSAVERGTVELLRPARPGDVRPEGGDFHAGETVMSAGLRLTPARLALAAALGHAQVPVRRWRVALLSTGDEVVAPGQPLAPGQVYDSNRVGLAALLTEAGYEVLDLGHAPDSPAALRERLGAAGGADLLLTSGGVSMGRYDFMRDLLLGEGEITFWKVKMRPGGPALCGRWGGLPVFGLPGNPVSSLVVFQVIVRPVLTGEPLPTRQVTAATPFASLADKTAFWRGVLSGDEVRDYPRQGSGVLRSLSDADALVVVPEGQNIAAGERVEVVLL
The following text describes a protein:
Function:
Mediates the Na(+)-independent high affinity transport of organic anions such as the thyroid hormones L-thyroxine (T4), L-thyroxine sulfate (T4S), and 3,3',5'-triiodo-L-thyronine (reverse T3, rT3) at the plasma membrane. Regulates T4 levels in different brain regions by transporting T4, and also by serving as an export pump for T4S, which is a source of T4 after hydrolysis by local sulfatases. Increases the access of these substrates to the intracellular sites where they are metabolized by the deiodinases. Other potential substrates, such as triiodothyronine (T3), 17-beta-glucuronosyl estradiol (17beta-estradiol 17-O-(beta-D-glucuronate)), estrone-3-sulfate (E1S) and sulfobromophthalein (BSP) are transported with much lower efficiency. Transports T4 and E1S in a pH-insensitive manner. Facilitates the transport of thyroid hormones across the blood-brain barrier and into glia and neuronal cells in the brain.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Note=Expressed in both luminal and abluminal membranes of brain capillary endothelial cells. Localized to the apical membrane and basal surfaces of choroid plexus.
Sequence:
MDTSSKENIQLFCKTSVQPVGRPSFKTEYPSSEEKQPCCGELKVFLCALSFVYFAKALAEGYLKSTITQIERRFDIPSSLVGVIDGSFEIGNLLVITFVSYFGAKLHRPKIIGAGCVIMGVGTLLIAMPQFFMEQYKYERYSPSSNSTLSISPCLLESSSQLPVSVMEKSKSKISNECEVDTSSSMWIYVFLGNLLRGIGETPIQPLGIAYLDDFASEDNAAFYIGCVQTVAIIGPIFGFLLGSLCAKLYVDIGFVNLDHITITPKDPQWVGAWWLGYLIAGIISLLAAVPFWYLPKSLPRSQSREDSNSSSEKSKFIIDDHTDYQTPQGENAKIMEMARDFLPSLKNLFGNPVYFLYLCTSTVQFNSLFGMVTYKPKYIEQQYGQSSSRANFVIGLINIPAVALGIFSGGIVMKKFRISVCGAAKLYLGSSVFGYLLFLSLFALGCENSDVAGLTVSYQGTKPVSYHERALFSDCNSRCKCSETKWEPMCGENGITYVSACLAGCQTSNRSGKNIIFYNCTCVGIAASKSGNSSGIVGRCQKDNGCPQMFLYFLVISVITSYTLSLGGIPGYILLLRCIKPQLKSFALGIYTLAIRVLAGIPAPVYFGVLIDTSCLKWGFKRCGSRGSCRLYDSNVFRHIYLGLTVILGTVSILLSIAVLFILKKNYVSKHRSFITKRERTMVSTRFQKENYTTSDHLLQPNYWPGKETQL
The following text describes a protein:
Function:
Involved in a special stress-induced plastid-to-vacuole protein trafficking pathway. Interacts with ATG8F in plastid bodies to subsequently enable their delivery to the vacuole by an autophagic pathway. Interacts with the plastid proteins APE1 and PSBS/NPQ4 and may recruit them as cargo into plastid bodies that may be recognized by the autophagy machinery for degradation in the vacuole. Involved in the alleviation of damage caused by salt stress during plant development, probably through its involvement in plastid-to-vacuole and ER-to-vacuole trafficking. Plays a role in seed germination in response to exogenous abscisic acid (ABA) treatment.
Miscellaneous:
MISCELLANEOUS: Plants over-expressing ATI1 display increased ability of seed germination in presence of exogenous abscisic acid (ABA). Plants silencing ATI1 and ATI2 display decreased ability of seed germination in presence of exogenous ABA.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Membrane; Single-pass membrane protein. Plastid, chloroplast membrane. Note=Under favorable growth conditions, partially associated with the endoplasmic reticulum (ER) membrane network. Upon exposure to carbon starvation, mainly associated with newly identified spherical compartments that dynamically move along the ER network and reach the lytic vacuole. Under carbon starvation, salt stress and during senescence, localized to novel plastid-associated bodies that are transported to vesicles. These plastid bodises are morphologically distinct from the ER-associated bodies.
Sequence:
MANNEEHPPRGNEWEVVSLTSSAYAAAPGPYNVESRDVRKYDAYYGAETSRDLYMSEHFVFPPSEHENLPIDESLFVAEQRKDGRDLMLEGQGLSDQFHYEAGNNQQSIYGESALGSSRHMESFGSESAVYEHGLVDAEGNLDLHSDGEGEKDVKKSTHNLPCEAWWKRRAISMYSRTREANAIWSLFFAAAVTGLVVLGQRWQQERWQVLQLKWQSSISSEKLGRVLEPLSRLKDVIVRSNPQASLVRSGSSSEV
The following text describes a protein:
Function:
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Localization:
Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MSLLKEIQANAAVAWSPVKRRAELLALGSKGDGGVGFENNGGEFKLVSMDLSDPDRGMLTLGSVKTASRFTSLAWRDVPRHHDTCPYGIIAGGMADGSVSLWNPALLLDREPGTDAPASCEIGRITRHKGAVNALQFNPHEDSAHLLASGGSDGEVYIMSLEKLASPGVFTPGGPTTPQAQANEITSVAWNTQVNYILATGSQNGTVVVWDLKQKKPWCELRDPARGAATAIAWNPNEGLQIATASGDDQHPAVKLWDLRISTSTPLAEFHDHTAGVLSMSWCPNDPGLLLSCGKDNRTLLWDLFSRKTVAEFPSDAPNAPSMGSDQFFGGGLAGQRRWNVQWSPQVPAVASTCSLDGKLQIWGLSGGGNPACRPPKWMRRPAGASFGFGGKLVTIANPQEPAAPNGDNRRLIHMQRVISDTGLVAEAEALDRSLETKDFKGHCEQKIASAATAEERSVWSFMKILFEKDARQHLLLHLGLDAEKINELNAKFNPETAVQNAAAAPLAADPTAQAPGPQVDPVTGALLSDRIDSGLGADDVFSSGFHPNGGDQTAAAMPASPLSDVSALVAALPSALDEDKSKRLDAVPAPVYTEESENTLMQALLVGNFEVAVNCCLAYNQLADALLLASCGGPELWEKTQRAFFAHQQRPVMRVVSAIIKNELNELVEVSDLTEWRETLAILSTYAKSEEFPSLCDKLATRLEAAGDLHSATLCFMCAVNVEKTVNAWCKESEVEARTHGHTFALHRLVEKVSVFAMAVDQPDQSMGPEVAQRFAEYASLMAAEGRLDIAAKYARFPDLSCAILKDRIYNAYPMQGYQPPPFPFDLVQVQSQAQIQQQQQQQQQQQQQQQQQQQRQAPAQQQRGYGTKPAYGATRNQYGAPAAPTPVPVPTPMPTPGAFGAQGAGYPPQQHAPVPTPAFPGHSGGYQPAPQQSAYPGAPGLPPQPQQAGGYPSQQQGYPGQSAPSPYSANPAPTPFQGQSAAPAFPGQPQQQQVPPQQPGYGRPQQPGFPGQQPPQPGFPSGPPSSSGSRSHPQMYSGPPSTGGTPHMPSPGYGGAPRPGTGFAPPAATPASPSIPQGTGVNPLTAAMGSSRITKPSVDMSSHQRDGFVSSVGNKELTLKYGNATTASLSPVANAAPKAGGFPPNVVPGSTENVGPQDMPIVNAFNDLVSQLQGLPLTMMEQKQLQEIQKGKEIMFTKLNIGELSPEVVSRLHEMVACFGQRDFGSAQTIYVALTASDWAHHKDWLRGLKSLIHISMKLLCARRRQAMLFLPLEEDSLLFRLCLYYEAEALVECKFDEEQVGGFPVSFVAAIGICEGVETGIVVEN
The following text describes a protein:
Function:
T-box transcription factor that plays an essential role in the determination of the fate of axial stem cells: neural vs mesodermal. Acts in part by down-regulating, a specific enhancer (N1) of SOX2, to inhibit neural development. Seems to play also an essential role in left/right axis determination and acts through effects on Notch signaling around the node as well as through an effect on the morphology and motility of the nodal cilia.
Subcellular Localization:
Nucleus.
Sequence:
MYHPRELYPSLGAGYRLGPAQPGADSSFPPGLAEGYRYPDLDTPKLDCFLSGMEAAPRTLAAHPPLPLLPPAMGTEPAPSAPEALHSLPGVSLSLENRELWKEFSSVGTEMIITKAGRRMFPACRVSVTGLDPEARYLFLLDVVPVDGARYRWQGRRWEPSGKAEPRLPDRVYIHPDSPATGAHWMRQPVSFHRVKLTNSTLDPHGHLILHSMHKYQPRIHLVRAAQLCSQHWGGMASFRFPETTFISVTAYQNPRITQLKIAANPFAKGFRENGRNCKRERDARVKRKLRGPEPAATEAYGSGGGPCDSTLGGDIHESDPEQASAPGEVTTALAPPCGGPSAEAYLMHPAAFHGAPSHLPTRSPSFPEAPDSGRSGPYSAAFLELPPGPGGSGYPAAPPAAPFAPHFLQGGPFPLPYPGPGGYLDVGSKPMY
The following text describes a protein:
Function:
Acts as a regulator of centriole duplication through a direct interaction with STIL, a key factor involved in the early steps of centriole formation. The CEP85-STIL protein complex acts as a modulator of PLK4-driven cytoskeletal rearrangements and directional cell motility. Acts as a negative regulator of NEK2 to maintain the centrosome integrity in interphase. Suppresses centrosome disjunction by inhibiting NEK2 kinase activity.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Nucleus, nucleolus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cell cortex. Note=Localizes to centrosomes and nucleolus in interphase. Upon entry into mitosis, relocates from nucleolus and accumulates at spindle poles. Associated with the pericentriolar material. Localizes to centrosomes at a low level in G1 phase and a slightly increased level in S phase, with gradually elevated levels during G2 phase. The levels at centrosomes further increase at G2/M, reaching a peak at spindle poles at early mitotic stages and remain high until the end of anaphase. Localizes at the leading edge.
Sequence:
MAMQEKYPTEGISHVTSPSSDVIQKGSSLGTEWQTPVISEPFRSRFSRCSSVADSGDTAIGTSCSDIAEDFCSSSGSPPFQPIKSHVTIPTAHVMPSTLGTSPAKPNSTPVGPSSSKLPLSGLAESVGMTRNGDLGAMKHSPGLSRDLMYFSGATGENGIEQSWFPAVGHERQEEARKFDIPSMESTLNQSAMMETLYSDPHHRVRFHNPRTSTSKELYRVLPEAKKAPGSGAVFERNGPHSNSSGVLPLGLQPAPGLSKPLPSQVWQPSPDTWHPREQSCELSTCRQQLELIRLQMEQMQLQNGAICHHPAAFGPSLPILEPAQWISILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALELHQELASCLQDLQAVCSIVTQRAQGHDPNLSLLLGIHSAQHPETQLDLQKPDVIKRKLEEVQQLRRDIEDLRTTMSDRYAQDMGENCVTQ
The following text describes a protein:
Function:
Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Promotes histone H3 trimethylation at 'Lys-9' (H3K9me3). Binds to trimethylated lysine residues in histones, and possibly also other proteins. Regulator of cellular lifespan by maintaining the repression of CDKN2A, but not by inducing telomerase activity.
Miscellaneous:
MISCELLANEOUS: The human orthologuous proteins of Drosophila Polycomb group protein Pc, CBX2, CBX4, CBX6, CBX7 and CBX8, show distinct nuclear localizations, contribute differently to transcriptional repression, and appear to be part of distinct PRC1-like protein complexes.
Subcellular Localization:
Nucleus.
Sequence:
MELSAIGEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVMAYEEKEERDRASGYRKRGPKPKRLLLQRLYSMDLRSSHKAKGKEKLCFSLTCPLGSGSPEGVVKAGAPELVDKGPLVPTLPFPLRKPRKAHKYLRLSRKKFPPRGPNLESHSHRRELFLQEPPAPDVLQAAGEWEPAAQPPEEEADADLAEGPPPWTPALPSSEVTVTDITANSITVTFREAQAAEGFFRDRSGKF
The following text describes a protein:
Function:
Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
Sequence:
MKPMSYWDYIKVEELLALQGGANGDETQVGNDEALFIVVHQVYELWFKLILRELTFARDLLRQDTVPGHQIALGVRSLRRAIAVFEQANQHFRVMETMTARDFLDFRERLMPASGFQSAQLREIEILLGLEDNERIAVCQGGSFKDALKLPNGALSSAAYRVEAREAHGQSLKHCLYAWLSRIPIDGSNEPAAVKRFLRDYIGSVRAESQRRLQTAIDRQLAPAEVERLRARYQADDVGAETFLLAEEDPQADAMTREKRRAVRAAMLFVESYRELPQLAWPRELLESILELEQSMLIWRQRHARMVERIIGRRVGTGGSSGVDYLDQTALRYRVFTDLWTVRSLLLRKSSVPPIRQGASYAFAEEALV
The following text describes a protein:
Function:
Has an integral role during the infection of macrophages in the mammalian host.
Subcellular Localization:
Membrane.
Sequence:
MCRTLLGIAVAFALVCCVVGPGAAQGHPERADSEEPRCGFDELEAHTIGTRVSGISRVELPTGELVVAAAATGALQPIRIAVFTDDISNSSQHCTASGQSRPNFRGSRVTCSAAEVLTRAKKRVLLELLIPSAVQLHQERLNVQRVNGNIVVDSSIQKDRVCGQFSIREEHMKTGVKDADFVLYMSAAPTSGSVIAWALKCQNFDNGRPSVGVVNISPKYIAADPKTVRVIAHEVLHALGFSRSVFQERNMLAMASFRSKGPSPVICSEKVVAKAQQHYGCKTQAFMELEDTGDIDDASSHWKRRNAKDELMAGFSGVGIYSALTIAAMEDTGYYQGNYAKAEPMAYGHDAGCKLSSDQCVTNSTSQIPGMFCDAPDAPWSCTSDRLGVGRCILTSHKSNLPTYFQYFSDPRLGGPDPLMDFCPVVEVAEGTMCAATTNALKGSVYGVMSRCVDTPVGFSMDDSAVRQHGICVEVQCDSTKYYIKANGASAFCDCPPGSTYNLSTLSPSFSKGYLVCPSYESVCAIKINASLYEEYSGFLTDHSVAGVLTSVKAVVAVLLVVLFMV
The following text describes a protein:
Function:
Controls the expression of genes used for utilizing diverse lipids as energy sources.
Sequence:
MSSANTNTSSAPDAPPRAVMKVAVLAESELGSEAQRERRKRILDATMAIASKGGYEAVQMRAVADRADVAVGTLYRYFPSKVHLLVSALGREFSRIDAKTDRSAVAGATPFQRLNFMVGKLNRAMQRNPLLTEAMTRAYVFADASAASEVDQVEKLIDSMFARAMANGEPTEDQYHIARVISDVWLSNLLAWLTRRASATDVSKRLDLAVRLLIGDQDSA
The following text describes a protein:
Function:
Part of the nuclear pore complex. Has a critical role in nucleocytoplasmic transport. May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex.
Subcellular Localization:
Nucleus, nuclear pore complex.
Sequence:
MGDEMDVLVPEREMKDFQFRALKKVRIFDSPDELPKERSNLLAVSNKYGLVFAGGASGIRIFCTKNLLIQNQPGKDPNKIVDDVEGTLIPMKFPVHHLALSCDNLTLSVCMMSSEFGSLIAFFDVRTFWNEAKQQKRPFAHHKLVKDAGGMVIDMKWNPTVPSMAAVCLADGSISVLEVTDAVKVWASCPSSGAVTSVCWSPKGKQLAVGKQNGTVVQYLPSLQEKKVIPCPPFYEADNPVRVLDVLWIGTYVFTIVYAAGDGTLETPPEVVLAVLPKKEEKRPEMFVNFMEPCYGSCTERQHHYFLNYIEEWDLVLAASAASTEVSILARQSDQTTWESWLLEDSSRAELPVTDKSDDSLPVGVAIDYTSQVEIPIGDEKTLPPAPVLMLLSTDGVLCPFYMINQNPGVRCLMRIPEPLPVEGERQPRSPGSTTTTATSSQSSLKPETSPALASAPVPPLSLVSSTPSSSSSLPPATGSAATFTFASSTLKSGSSLPGDPPPYPFASDSTKPAPGSALTGAAGFSFAPPTSKAPVPSAAPMATTASSSFSFGATSFKPTLESTPVANASIPHVGPKQPFPPAASAVSVNLSEKFAAVEASTPVSNAQSSPSVLALSTASKSAPGGPVSHCAPLSASTSPTSVKSSTSTSAAGVRSAQSGPVASMVQKSARITPSSTKPTSTQGRSPQPATAGEKQVHQWKESDPIMAGIREEIAHFQKEMEELKSRTSKACFQVGTPEEMKLLRKESDDLHTFLLEIKETTESLHGDISTLKTTLLEGFVGVEEAREQNERNRDSGYLHLLYKRPLDPKSEAQLQEIRRLHQYVKFAVQDVNDVLDLEWDRHLEQKKKQKRLLVPERETLFNTLANNREIINQQRKRLNHLVDSLQQLRLYNQTSQWSILGDTSPPHGNTQSFDSDLESLRNVLMKTTLESHTKSLPKGPAKLSPVKQAQLRNFLAKRKTPPIRSTAPASLSRSAFLSQRYFEDLDEVSSTSSISQSLENEDSQSLDQDEEVPPAPVSRHAPVVRTSSIQPSLLTQASPFAKPHPPLNASLSLMGALTPAPASKIVPQGADSTMLATKTVKHGAPGPSVTISAPQAAAAAALRRQMANQPPAVSTSLTESTLKNVPQVVNVQELKSGTQTPTAVIGSSVPHSAAKVIHQVLATVGTNQAKQGPLINYLKPQPPPGPAGASGNTKIDTSVTTTPSAAGSFNKPFSFTSGTSFNFGAMTSATVPPPTFTASQVTAPPAKESSQHDAFSFGGSAKPLFENVPEGPLTSGAVQAASAAGTAFSSSGGETPNNKPAAGATVAPSPATSKPEAPPSKLGEHLFQSSVAGETLGSFSGLRVGQADDSPKATGKAPAVNLAGAQPAKTSSVPSGFSFGSAPQLGKHAETPVTSVATPGPASLSVSPSASGSTGGLFGNVQFAGVGSSGGLNLGGASPSGNKPTFSFGIQQTGGAAPQPTPSPAPLPTSTSTLSFGNLLSLASTPALASASGKSETESKLPSSPEKPSDGEAPGPEPPLPGQQQSAQPAQPDAGREEPTPSQPALGDSGTPTSSSASAVPATEAGPGAPALADAKTEAAPPPVSTSPAPERSATTAGAAASPPAPTAEAPEASSSSGAVSPSAQSPAVETSASAATSSGPTVFSQASGANPPGSAFGQPAGDTTAAPPAVPAFDQPAATAASSVFGQVVVSTTATTTASTQATGSGFGSPAFGTAAAGGFGQSAFGQTPAFGQPASGSASGFSFTQNAFGSAPAFGQPAASAPASSSGNVFGASSSTSSASSFSFGQTSANSGGGLFGQSNPPTFGQGAGFGQGGSVFGGSAAATTAASSSGFSFCQASGFGSSNTGSVFGQAASTGGTVFGQSSSSTGGLFGSGNTGRGGGFFSGLGGKPSQDAANKNPFSSASGAFGSTTTSNSSNLFGNSGAKTFGFGSSSFGEQKPTGTFSSGGGSVAAQGFGFSSPSKTGGFGAAPVFGSPPTFGGSPGFGGVPAFGSAPAFTSPLGSTGGKVFGEGTEAASAGGFGFGSSSNTTSFGTLASQNAPTFGSLSQQTPGFGTQNSGFTSFGTSGTGFGFGSSNSSAPGFGGWRS
The following text describes a protein:
Function:
Replicates viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'-5' direction (By similarity). Non-processive DNA polymerase that achieves processivity by binding to host thioredoxin (TrxA). This interaction increases the rate of dNTP incorporation to yield a processivity of approximately 800 nucleotides (nt) per binding event. Interacts with DNA helicase gp4 to coordinate nucleotide polymerization with unwinding of the DNA. The leading strand is synthesized continuously while synthesis of the lagging strand requires the synthesis of oligoribonucleotides by the primase domain of gp4.
Sequence:
MIVSDIEANALLESVTKFHCGVIYDYSTAEYVSYRPSDFGAYLDALEAEVARGGLIVFHNGHKYDVPALTKLAKLQLNREFHLPRENCIDTLVLSRLIHSNLKDTDMGLLRSGKLPGKRFGSHALEAWGYRLGEMKGEYKDDFKRMLEEQGEEYVDGMEWWNFNEEMMDYNVQDVVVTKALLEKLLSDKHYFPPEIDFTDVGYTTFWSESLEAVDIEHRAAWLLAKQERNGFPFDTKAIEELYVELAARRSELLRKLTETFGSWYQPKGGTEMFCHPRTGKPLPKYPRIKTPKVGGIFKKPKNKAQREGREPCELDTREYVAGAPYTPVEHVVFNPSSRDHIQKKLQEAGWVPTKYTDKGAPVVDDEVLEGVRVDDPEKQAAIDLIKEYLMIQKRIGQSAEGDKAWLRYVAEDGKIHGSVNPNGAVTGRATHAFPNLAQIPGVRSPYGEQCRAAFGAEHHLDGITGKPWVQAGIDASGLELRCLAHFMARFDNGEYAHEILNGDIHTKNQIAAELPTRDNAKTFIYGFLYGAGDEKIGQIVGAGKERGKELKKKFLENTPAIAALRESIQQTLVESSQWVAGEQQVKWKRRWIKGLDGRKVHVRSPHAALNTLLQSAGALICKLWIIKTEEMLVEKGLKHGWDGDFAYMAWVHDEIQVGCRTEEIAQVVIETAQEAMRWVGDHWNFRCLLDTEGKMGPNWAICH
The following text describes a protein:
Function:
Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cell projection, cilium. Cytoplasm. Golgi apparatus.
Sequence:
MGLLKKRSSSGSTQPMVRSVSPDIELSTVMDTELVAKAYGKRDTEGKKPRTRRYNPFHRAFDSSDMETSYQKFFVRRRLETLPVMIAFSFFFDVVVLIIYYLDRAIPSRVIAISIMAICAVTNLILFSLSRYRLISDWSLTRVMPYLIWSLVCAQSFVDLGLYYQPLMPSDGAGWQVFFIFASFTMLPVPLGAMILLSTFAITVHCLMVGLLSLANKEYMAEQIGANILLYLCAIILGCVCYLVSDKQHRMAFLETNESLKTKLTIQEQAAQQEGLLLSVLPKHVADAMVMDVGKKNTGQFNRIYIRRHENVSILFADIVGFTAMSGKMTAQELVKTLNALFANFDKLAEKNNQLRIKILGDCYYCICGVPEQRIDHAVCSVQMGLDMVVAIAAVRKSTQSGVDMRVGIHTGAVLAGVMGQKRWQFDVWSTDVVLANNMESGGVPGRVHISQTTFDCLNGEFDVEPGEGDTRSDSIKQAGIKTYLIKIVKNQNKPLSTGGLDLNGHLDSVEDTDGPAMESVPENFDKIKKDEMEKENQFKDKNKTVSFEPEVEEREEQKDENQKLDEAIAERESNTKLGEKMYFLLLRFKDKAMESRFQQGKDRMSAAGISSALVVVFFVFLVQLLMLPRTAISIATFCVCFVVLSIITYVSLAPSFKKSYPSILIKLATFVERTPWARIMCATFIIALVSVTDIADVLTCVDESSDNVTNLSPRDLRCLNPHYFNYMLLLVMAVITTMFQITHIVKFLLTIIITAFYCILMNVIKPILYNRPDDFLEDSMPSTDHNEVASRIANTVQLVVVAAALIYFNSHLEVTSRLLFYWKTEAKEQKEEVGRMRVKNENLVLNIMPEHVAKHFLGSKKSEEELYAQSYTESGVMFASMPNFSDFYSEDAINNQGTECLRFLNEIISDFDDLLNEPRFKSILKIKTINSTYMAASGVFPNPEEIHYRDDMERWQHLADLVDLAFSMRNTLDTINAQSFNNFMLKIGINHGPILAGVIGATKPHYDIWGNTVNVSSRMESTGQPGKIQVVEACMNILKRYGFKFEKRGLVKVKGKGELMTYYLIGKDETVRNDMDNSIPNMVVAS
The following text describes a protein:
Function:
Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side.
Sequence:
MRSRSGSGVRLDRILFMVEQTICSHQNPITALFANQKDFPGHAWVRDNVYIAQALWALYRAYMKCADFDEDLTKAKELGFTCVKMMQSILECLMRQADKLEQFKKYQRPLDALHSKYAVATKGTVCGDADWGHLQMDAISLYLLTLAQITASGLQVVRNFDEVAFIQNLVYYIETGYRTPDYGVWERGDKTNQGIRELNASSIGMVKAALQALNDVGDLFVDGSRGSVVHVLPDEIEQCSAVLSSMLPRESFSKETDAALLGIISYPAFCVEDPELVAQTRETITHRLLGKYGCRRFMRDGYKTVLEDGSRLYYNKSELQQFEDIECEWPIFLCYLILDAMYSKDDEAVEAYWQQLESVLVLSDKGFRLVPELYVVLREHVSAEKAHPSTQPRVPGGATPFLWAQSLYVIICLLYEGFLLPAELDPLSRRLSVYEKRPPCEVQVTVLAESADVQRELRAHDIHVQRVDEIDPVFTILPASALGHLLEKIGESKKLNLSGRPLDRPIGLLSTSRLYQIGNKFVIFTPQFMDSRRSHLMYDIRILTDEWSSELQYIYASWNSVSISGRPLVVLVITQGMLSTEGLSHFSNIHLNRHMKSTVIGAIKKINTGYLSGARVVMKDLSDFFRTTAVSKMEFRDKKAEEMLRSVAAEKVQFTLLTEDATEAKSEKMASPRGPRTLKRGESVKDRSAYSLIHKASMRHRSIALDSNDADLIQLRLAYKSRPRDLHEMDSPRQSPPLGQKPLGLVKEHSSGELRQQLLKTTRRGAENETAHRDLKTEQIMEMKADDLLDLLNETTVLEEQISIVHCLWMKFGPDYDTELGCQHITVRMLMEEVHTKACEAREWALVRLTAGLLKKQLEELSKAVTHLLVRQKQITVGMASKKEEVITCPKTNEELEKIMNRAYGDDANSFTLAQEIIVYLGSLVRTEPKLFLEMFRLRIGLIIQVLASELARLRNLSGTEAAETLLTVSPFELKSMIFSLLSGRLLEEYAEDGFHYGDTIRETRTGIGSFRRQIEERKSLRKSTRSVGGLDIPKEEDEEDEADEDDFQFGIWLRHRRIDGALNRVPNGFYAILWDTVHKMPHGVKINDTILHWGLTQEMTRKEIKFALEVEEALNRIAEPEYRELVVETLWLLGRLEKLVLLEQPNIPRDRPLDVDHILHVANQIFVNHNKQLETLVLECCASSNPNNTKCDGARSICKHFYDSAPAGEYGTSHYIIRALMQLYS
The following text describes a protein:
Function:
Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.
Subcellular Localization:
Mitochondrion matrix.
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 GTP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP hydrolysis.
Sequence:
MSMLVRPRAIPRIAPILAPQRPSKRFNSSSTASTSSPVSHVASAVADTAHSLADKFREAARFINSPSYDGVEEKGLRMLVFGKPGSGKGTLSSRLVKEYDISFVSTGDVLRKEIAAKSEVGRKAEAVVASGGLVSDELMLEIVKAELDRLKGKSWIIDGFPRTLHQGELIDTVLNQENRPLNMVVHLNVPDSVIMARIAARWVHLPSGRVYNTTYSAPKVPGKDDVTGEPLTKRPDDTPETFSKRLQAYYESTAPLLKYFEETYPESLHSISGSSSDELWPQLVELIEPFNLRRRQTPAEKGRVDAEKVRKQADDLRDSREVDVPGEGKKVVAR
The following text describes a protein:
Function:
Positive regulator of RNAII and RNAIII in a cell density-dependent manner. It can contribute to the expression of virulence genes controlled by agr. May also regulate target genes via an agr-independent pathway.
Subcellular Localization:
Cytoplasm.
Sequence:
MDYQTFEKVNKFINVEAYIFFLTQELKQQYKLSLKELLILAYFYYKNEHSISLKEIIGDILYKQSDVVKNIKSLSKKGFINKSRNEADERRIFVSVTPIQRKKIACVINELDKIIKGFNKERDYIKYQWAPKYSKEFFILFMNIMYSKDFLKYRFNLTFLDLSILYVISSRKNEILNLKDLFESIRFMYPQIVRSVNRLNNKGMLIKERSLADERIVLIKINKIQYNTIKSIFTDTSKILKPRKFFF
The following text describes a protein:
Function:
Involved in anther lipids biosynthesis and is required for tapetum degradation and pollen wall formation. Required for the formation of Ubisch bodies and microspores. Possesses lipase activity in vitro toward two synthetic substrates, p-nitrophenyl acetate (pNPA) and p-nitrophenyl butyrate (pNPB).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MATTLTPTQRYAAGALLALALRQAQIHQSVLLGAHHHHDDDDEEQGRTSTSSGGGGGSSSSSSNSGAGADADLWTHDSHGLLRPVFRFLEIDPKAWSGLEETAASSEAKHHIGAFLRIIFEEDGESSSDRSVQELALAKGVDVMVMSLGNDSEVGNTIKGGDQDALPSSSGTDKSPGESSHDDQLGINKLTLDDIPANNHRKMALLFALLSACVADKPVSQEEEDRKSTRFRKGYDARHRVALRLLSTWLDVKWIKMEAIEVMVACSAMAAAKEQEQSQESASPKSKWEKWKRGGIIGAAALTGGALLAITGGLAAPAIAAGFGALAPTLGTLVPVIGASGFAAMATAAGSVAGSVAVAASFGAAGAGLTGSKMARRIGSVKEFEFKPIGENHNQGRLAVGILISGFAFDEDDFCRPWEGWQDNLERYILQWESKHIIAVSTAIQDWLTSRLAMELMKQGAMRTVLSGLLAAFAWPATLLAATDFIDSKWSVAIDRSDKAGKMLAEVLLKGLQGNRPVTLIGFSLGARVIFKCLQELALSSDNEGLVERVVLLGAPVSVKGERWEAARKMVAGRFVNVYSTDDWILGVTFRASLLTQGLAGIQAIDVPGVENVDVTELVDGHSSYLSAAQQILEHLELNTYYPVFVPLSAANEETDGTVAQ
The following text describes a protein:
Function:
Endoplasmic reticulum (ER)-resident protein that confers cellular protection as an anti-apoptotic protein by limiting multiple stress-inducing pathways surrounding the endoplasmic reticulum and mitochondria. Inhibits the activities of the key sensor for the endoplasmic reticulum unfolded protein response IRE1alpha/ERN1 both directly and by blocking BAX/BAK binding. Modulates ER calcium homeostasis by acting as a calcium-leak channel. Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MLGSFVTLKPTAEAGEWRLCPTDASIMNIFDRKINFDALLKFSHITPSTQQHLKKVYASFALCMFVAAAGAYVHVVTRFIQAGLLSALGSLGLMIWLMATPHSHETEQKRLGLLAGFAFLTGVGLGPALDLCIAINPSILPTAFMGTAMIFTCFTLSALYARRRSYLFLGGILMSAMSLMVLSSLGNLFFGSIWLFQANLYVGLVVMCGFVLFDTQLIIEKAENGDKDYIWHCVDLFLDFVTLFRKLMMILAMNEKDKKKEKK