lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. RNA-decapping enzyme although it does not bind the RNA cap. May contribute to gene regulation in multiple RNA pathways including monomethylguanosine- and trimethylguanosine-capped RNAs. In oocytes, may play a role in the response to stress induced by heat shock, osmotic stress and anoxia. Required for the developmental axon guidance and regrowth of PLM touch receptor neurons. Early in embryogenesis, plays a role in ciliary shape formation in sensory neurons. Promotes survival at high temperatures.
Subcellular Localization:
Cytoplasmic granule. Cytoplasm, perinuclear region. Note=Localizes to perinuclear puncta in pachytene-stage germ cells. Diffusely localized to cytoplasmic puncta in maturing oocytes.
Sequence:
MEISTENWCKKPKNRSIFSKNISFQKQNKSTEEPPSSVQKLLASLQQAQNKSDLSEQPSTSKPKKNEKRKKAVAQAPASAPAPGPEEKKKQPKRASVGARMQQQAENARISQTKRPRQVSTSKGSSRNTTAPEQQNYQQQQQQYKGPRIPTDILDELEFRFISNMVECEINDNIRVCFHLELAHWYYIDHMVEDDKISGCPNVGSRDFNFQMCQHCRVLRKYAHRADEVLAKFREYKSTVPTYGAILVDPEMDHVVLVQSYFAKGKNWGFPKGKINQAEPPRDAAIRETFEETGFDFGIYSEKEKKFQRFINDGMVRLYLVKNVPKDFNFQPQTRKEIRKIEWFKIDDLPTDKTDELPAYLQGNKFYMVMPFVKDIQIYVQKEKEKLRRRKAEAVQSTPSSSIFSQLFPAQPPPPVPEDATPTRPMYKRLTSEELFSAFKNPPAGEVARPTLPDMSPAVNGLDTLAVLGICTPLKPGASLNEFSGAPQNCPMISEEAGSPADPSAEIGFAMPMDLKQPVVTSDHPWQHHKISDSSAPPQTLESHQGWLDTQLVNTIMHSPNHPLPPTSNSPATPTAVLGHLIGKPIQPQAILPQAATPTALGSAEKPKSSRISLSDNSAFKAISSTQKQSIPKATAAPPSTEKTRSASLSGSSQVVGKPARNLFNSVVSPVSSGIQSIQGDGGAWEDVWFREQLAATTTAGTSISSLAASNQELAMINREETPIEDPYFKQQAYQKAQKAQSLIPACSQWTNSIKLDIDYVVGPLSFWMQQFSTKSPVSGTGPQLP
The following text describes a protein:
Function:
Deubiquitinating enzyme that acts as an inhibitor of mitophagy probably by counteracting the action of park. Possibly functions by hydrolyzing ubiquitin attached by park on target proteins, thereby reducing park's ability to drive mitophagy.
Sequence:
MLYAACGGTQRGISFNDLLCGLVLITRGTQAEKTKFLWNLYCNDAGTFIIKSDYVRNVNLAPFESVSLFAQSERVNFEQFQDWIIKHRNATVLSKWLLSDNCVSLTSELETPTFYQSLAGVTHLEEKDIGDLEKEFWRLKNTSQNGQIDLQFLGPLISPPIPKNALAGLFNAFDENRDGHIDFKELCCGVSAACRGPGVERTRFCFKIFDVDRDGVLSHDETLQMINVLLLVAKENQESQQYKDLTKQLVISDLLEFGQRRSPDGTPSKLTRDNVSLTAEDFMLWTVQCDLRLMQPLLDLIFELCHIVFGLWPQCKHMENDIVRGWLRREERRPYRVGQFWYLITHDWWLSWMQYTQHTTHTCDYCKRTASQRTAVDEALVCDESFNTHSLEQHDSYSLGSGTGSASGSGSASSGISAGRHCGPVRPGPIDNSNLITANPFRNVRTLTGEGGHLKRDTPLVQNHDFELVPKSLWKALNRWYGDNLPLPRQVIQPPNSDVELELYPLNLRILLHQAQPSQTGVGGGTQLGSWGSTVSGGYGVLASGGGYAAIAVSSVLQPPKRYLAYTAAFSRLATVRQVGEFLCEQLRLKSEDIRLWHVPQLDNGAILLEEDAMCLKELLIRDNDQLLLEIRNKDLTWPEELGSLATAQCGQGAGTPGDRRRLTRSSIMSVHAPGATGLHNLGNTCFMNAALQVLFNTQPLAQYFQREMHRFEVNAANKLGTKGQLAMRYAELLKEVWTATTRSVAPLKLRFCVNKYAPQFAGGGQHDSQELLEWLLDALHEDLNRVMEKPYSELKDSNGRPDKIVAAEAWSQHHARNQSIIIDLFYGQLKSKVSCLGCGHESVRFDPFSLLSLPLPVENYIYFEVLVILLDGSVPIKYGFRLNSDCKYSHLKHKLSTMCSLPPNLMLVCELWNSQIRQVLNDDEKLRTQSAKELYVYQLPEQSMRTRSNSGLSMHIEQGLKDIQRSSALITSAQDSLSSLSTLQTSSHRASSRVLCNGHVSGLDVEGEAEVGTDVSQCNSNSNYNPIVSTYSGNGSGDNQVHELLPDEAGKVSRCFGKRECMPHSLFCFKESLILSSSPENTFMHGAAAQQKRVSSAKLLHTESNTSSMSYTNHSGENSMESSLTEPIPLADLEPVSSRNGSGGEDCSYRTSPNDSSGLSTGHTLGASLDVDEQAEEGNAEDHDQPDQITTSQPETSSGVYSRRSSQPPHKAGKYLVAVHRKITRHDSYFLSYHKTRPSLFGVPLLIPNSEGGTHKDLYCAVWLQVSRLLSPLPATTEQANHAADCDDSLGYDFPFTLRAVKADGLTCAICPWSSFCRGCEIRCNNDYVLQGALPPINAAASNTSTPKMNAKFPSLPNLEAKRTPEYTASLSYTPTTKYFEDFTIAIDWDPTALHLRYQSTLERLWVDHETIAISRREQVEPVDLNHCLRAFTSEEKLEQWYHCSHCKGKKPATKKLQIWKLPPILIVHLKRFNCVNGKWVKSQKVVHFPFDDFDPTPYLASVPQETILRHKELLELKNDAEMTMATNEVVSELDEIDAPSKEVKEELPNQTGSTKATASPPPTGNILRQSKTKNAVRRQRLISTSLTKTPIVDGEFEDYHQHRLKPDVDQFDPRYRLYAVVSHSGMLNGGHYISYASNATGSWYCYNDSSCREISQKPVIDPSAAYLLFYERKGLDYEPYLPNIEGRTLPNTASVPLEVDETEGELKKLCSIS
The following text describes a protein:
Function:
Growth suppressor that facilitates the entry of the cell into cell cycle arrest. Functionally similar to the retinoblastoma protein it binds to and represses the activity of cell-cycle-promoting proteins such as SV40 large T antigen, adenovirus E1A, and the transcription factor E2F. Necdin also interacts with p53 and works in an additive manner to inhibit cell growth. Also functions as a transcription factor and directly binds to specific guanosine-rich DNA sequences.
Subcellular Localization:
Nucleus.
Sequence:
MSEQSKDLSDPNFAAEAPSSEVHSSPGVPEGVPPSETLAEPQSPPLGPTAAPQAAQPPQAPSDEDDPKALQQAAEEGRAHQAPSAAQPGPAPPAPAQLVQKAHELMWYVLVKDQKKMIIWFPDMVKDVIGSYKKWCRSILRRTSLILARVFGLHLRLTSLHTMEFALVKALEPEELDRVALSNRMPMTGLLLMILSLIYVKGRGARESAVWNVLRILGLRPWKKHSTFGDVRKLITEEFVQQNYLKYQRVPYVEPPEYEFFWGSRASREITKLQIMEFLARVFKKDPQAWPSRYREALEEARALREANPAAHCPRSSVSED
The following text describes a protein:
Function:
Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC.
Miscellaneous:
MISCELLANEOUS: The catalytically active amino acid residue K274 of E.coli enzyme is missing and corresponds to A283 in B.subtilis. It is postulated that the enzymatic mechanism for the PABA biosynthesis in B.subtilis proceeds without covalent intermediate. First, ammonia is added at C2 of chorismate with concomitant loss of the C4 hydroxy group, yielding 2-amino-2-deoxyisochorismate (ADIC). The second step is the addition of a second molecule ammonia to C4 of ADIC with concomitant loss of the C2 amino group, yielding ADC. Both steps are catalyzed by ADCS.
Sequence:
MAQRRPAGKKIPFQKDSFLQQFEKLAQSRKHHVLLESARGGRYSIAGLDPIATVKGKDGITTIKHGDEMLFKEGDPLRAFHSWFKTLETETNHEFPDFQGGAIGFLSYDYARYIENFKMLSLDDLETPDIYFLVFDDIAVYDHQEESLWLITHVNGSDQETADVKLSELEQMWLTELPAVTSREMKPETAGSFAAPFTEDGFSQAVEKIKQYIASGDVFQVNLSIRQSQSLSVHPYQIYKTLREVNPSPYMAYLETPDFQIICGSPELLVSKKGKLLETRPIAGTRSRGKTNEEDEALANELIHNEKERAEHVMLVDLERNDLGRVSRYGSVRVNEFMAIEKYSHVMHIVSNVQGELQDGYDAVDIIHAVFPGGTITGAPKVRTMEIIEELEPTRRGLYTGSIGWFGYNHDLQFNIVIRTIYATGGQAFMQSGAGVVIDSVPKHEYKESFKKAFAMQRALELSEEETKIR
The following text describes a protein:
Function:
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
Miscellaneous:
MISCELLANEOUS: Spermidine-deficient mutants show a small decrease in growth rate and increased sensibility to superoxide toxicity.
Sequence:
MKKLKLHGFNNLTKSLSFCIYDICYAKTAEERDGYIAYIDELYNANRLTEILSETCSIIGANILNIARQDYEPQGASVTILVSEEPVDPKLIDKTEHPGPLPETVVAHLDKSHICVHTYPESHPEGGLCTFRADIEVSTCGVISPLKALNYLIHQLESDIVTIDYRVRGFTRDINGMKHFIDHEINSIQNFMSDDMKALYDMVDVNVYQENIFHTKMLLKEFDLKHYMFHTKPEDLTDSERQEITAALWKEMREIYYGRNMPAV
The following text describes a protein:
Function:
Nonribosomal peptide synthetase that synthesizes enniatin by coupling three D-hydroxycarboxylic acids and three L-amino acids via amide and ester bonds in an alternating fashion (By similarity). Whereas ESYN1 can accept different amino acids as precursors (L -valine, L-isoleucine or L-leucine), only one species of D-hydroxycarboxylic acid can be found in natural enniatin isolates (D-hydroxyisovaleric acid, D-Hiv) (By similarity). D-Hiv stems from L-valine deanimation by a valine aminotransferase to 2-keto-isovaleric acid (2-Kiv), which becomes subsequently reduced by a keto-isovaleric acid reductase (KivR) to D-Hiv (By similarity). Peptide bond formation and N-methylation of the amino acid occur before three enzyme-bound dipeptidols are condensed to a hexapeptidol (By similarity).
Domain:
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, additional domains required for further modifications are also present (Probable). Enniatin synthetase has the C1-A1-T1-C2-A2-MT-T2a-T2b-C3 domain organization (By similarity). The precursors D-hydroxycarboxylic acids and L-amino acids become activated at the A1 and the A2 domains. N-methylation of the amino acid takes place at the MT-domain. The building blocks are transferred from one module to another by means of T-domains and are ultimately stored at the waiting position T2b. Condensation of the building blocks and final cyclization and release from the enzyme is catalyzed by the C-domains (By similarity).
Sequence:
EFNTGILKASLAYLPLDVRSPVARMKDILSSVSGNTIVIMGTGVEDPGFGLPQLELVRITDTFDETIEDVQNMSRPSATSLAYVVFTSGSTGKPKGVMIEHRAIVRLVKSDNFPNFPSPARMSHVFNAAFDGASWEMFWMLLNGGTVVCIDYLATLDGKELAAVFAKERVNCAFLAPAMLKLYLTDAREALKNLDFLAVGGEKFDPRDAAEAMTLVRGNIANVYGPTEAGMISTCYTIPKDEAFTNGVQLGRSIYNSGAYVMDPNQQLAGLGVMGEHLFGDGVGRGYTKPELNKNRFIDVTIEGKTVRAYGTGDRMRARVGDGLLEFFGRLDNQFKMRGQRIEAGEVESAMLSHKRVLNAAIVLRGGQEEGEQLEMVGFIVADDDDNTEEEETGNQVEGWQDHFESGMYSDISTAVDQSAIGNDFKGWTSMYDGNDIDKGEMQEWLDDAIHTLHNGQVPHHVLEIGTGSGMILFNLNPGLQSYVGLDPSKSAVEFVNRAIESSPKFAGKAKVHVGMATDVNKLGELHPDLVVFNSVVQYFPTPEYLTEVIDGLIAIPSVKRIFLGDIRSYATNRHFLAARAIHTLGTNNNATKDRVRQKVQELEDREEESLVEPAFFTTLKERRPDVVKHVEVIPKNMKATNELIAYRYTAVVHLRDETDEPVYPTEKDSWIDFEEKQMDKKALLDHLRLSKDAMSVAVSNITYAHTAFERRIVESLDEDSKDDAKDTLGGAAWLSAVRSETESRASLTVPELFEIANEAGFRVEVSAARQWSQNGALDAVFHHFPSSNTDRTLIQFPTDNQLRSSLTLANRPLQKLQRRRAALQVRESLQSLVPTYMVPPNIVVLDTMPLNTNGKIDRKELTRRARTLPKQQTAAPVPDFPISDIEITLCEEATEVFGMKVEISDHFFQLGGHSLLATKLISRIQHRLHVRVTVKDVFDSPVFADLAVIIRQGLAMQNPVAEGQDKQGWSSRVAPRTEVEKM
The following text describes a protein:
Function:
Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MGHLPTGIHGARRLLPLLWLFVLFKNATAFHVTVQDDNNIVVSLEASDVISPASVYVVKITGESKNYFFEFEEFNSTLPPPVIFKASYHGLYYIITLVVVNGNVVTKPSRSITVLTKPLPVTSVSIYDYKPSPETGVLFEIHYPEKYNVFTRVNISYWEGKDFRTMLYKDFFKGKTVFNHWLPGMCYSNITFQLVSEATFNKSTLVEYSGVSHEPKQHRTAPYPPQNISVRIVNLNKNNWEEQSGNFPEESFMRSQDTIGKEKLFHFTEEIPEIPSGNISSGWPDFNSSDYETTSQPYWWDSASAAPESEDEFVSVLPMEYENNSTLSETEKSTSGSFSFFPVQMILTWLPPKPPTAFDGFHIHIEREENFTEYLMVDEEAHEFVAELKEPGKYKLSVTTFSSSGSCETRKSQSAKSLSFYISPSGEWIEELTEKPQHVSVHVLSSTTALMSWTSSQENYNSTIVSVVSLTCQKQKESQRLEKQYCTQVNSSKPIIENLVPGAQYQVVIYLRKGPLIGPPSDPVTFAIVPTGIKDLMLYPLGPTAVVLSWTRPYLGVFRKYVVEMFYFNPATMTSEWTTYYEIAATVSLTASVRIANLLPAWYYNFRVTMVTWGDPELSCCDSSTISFITAPVAPEITSVEYFNSLLYISWTYGDDTTDLSHSRMLHWMVVAEGKKKIKKSVTRNVMTAILSLPPGDIYNLSVTACTERGSNTSMLRLVKLEPAPPKSLFAVNKTQTSVTLLWVEEGVADFFEVFCQQVGSSQKTKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSHDSPSVPTFIAVSTMVTEMNPNVVVISVLAILSTLLIGLLLVTLIILRKKHLQMARECGAGTFVNFASLERDGKLPYNWRRSIFAFLTLLPSCLWTDYLLAFYINPWSKNGLKKRKLTNPVQLDDFDAYIKDMAKDSDYKFSLQFEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMISEEEQDDWACRHFRINYADEMQDVMHFNYTAWPDHGVPTANAAESILQFVHMVRQQATKSKSPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQLMWMKKKQQFCISDVIYENVSKS
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:
MATPLDRPLTRGGAFGGCCGSSGDAQGDDAEISLAKTYNTSQGGGWRPPEDKKPRKQKSVVDLLEAVTVKYKTAQDAPILPPRAGNDNKPTLVLDMDETLIAVKFDLYLPGSDYIVPLRLCHLTETGTGMTELYTIAWVRKRPYLEDFLASVAKDWEVIIMTAGIEDYAKPIIAEFDRNKIVSYSLYRDSCSCDKSDGIIYKDLSILGRDVNRTVIVDNTPTCYKKHPENAIPISTWESSSKDRALRSLIPILQELSRAPNIVKALKRMRLNEF
The following text describes a protein:
Function:
Utilizes UDP-glucose as the sugar donor and catalyzes the formation of O-beta-D-glucosyl-cis-zeatin from cis-zeatin. May regulate active versus storage forms of cytokinins and could have an impact on seed growth.
Sequence:
MTIGISWKMDLEIWSVTRDLLRTCKLRQEASAVTCVGLWFLHCHLHITCRSAVQSHRPLSSQHHRTLMGTEKRAMDSVAVVAVPFPAQGHLNQLLHLSLQLASRGLDVHYAAPAQHIRQARARVHGWADEALQSVQFHDLRISGYVSPPPDPTADSPFPSHLMPMFNAYIAGARAPLAALLDTLSGSCRRVVVVHDRINAFASEEAARLPNGEAFGLHCLALSMLLGRMDANHQLLRENGLVFTPVEHCATKEFLECASRARPSKEISPGAGILANTCRALEGDFIDAVAGHLAADGKKLFAVGPLNPLLHASVLEQSKQRHECLNWLDKQPPASVLYVSFGTTSSLRDEQIEELAAALRGSRQRFIWVLRDADRGDIFAEAGESRHEKMLPEFTKDTQGTGLVITGWAPQLEILAHSATAAFMSHCGWNSTMESLSHGQPILAWPMHCDQPWDTELVCNYLKAGILVRPWEKHSEVITAKAIQEVIEEAMLSDKGMAVRQGARVIGDAVRASMVDGGSSRKDLDDFTAYITR
The following text describes a protein:
Function:
Required for gamma-tubulin complex recruitment to the microtubule organizing center (MTOC).
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
Sequence:
MADTSQKPDKATSAAQARQVIDVFHEISTLLNAELDRGTLSICISLIENGVNPEALATVVRELRKDADEVRRQIAQGVVQDGE
The following text describes a protein:
Function:
Confers resistance to late blight (Phytophthora infestans) races carrying the avirulence gene Avr1. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm.
Sequence:
MAIVAISSLMITIQQSMQVTGCNLELFYEKLASLIAVMEKPSSITGDLEALASLELQIVEVAYRAEKEIDSKSIEVVRAKTDTLRGRAFWKLSCFLEQVVENIDSIMKEWMAIRDGCNNMKEYMIVSESSKSFLAKTEMRQGLTFWKRAVGHVDSMMNKWRKKQSICTKSKDVEAQNLTLGSTSRHSLEHENVMVGHENEFEMMQDQLTRGASDLEVVSIVGMGGIGKTTLANKIYTDPFVMSCFDKRAKVTISQDYCVRNVLLRLLSSISGKTHQTYEEQDDGQLADQLQKLLKGPRYLVVIDDIWTTGAWDDIKLCFPDCNCRSRILMTTRNMEVAEYASSGSPPYQMRLMNFDESWSLLYEKVFARGFFPHEFEQLGKQIASKCKGLPLMIVVIAGLLSKIGNRLDRWRSVAENVSSVMNTDLDVQCMRVLALSYYHLPHHLRACFLYFALFPEDKLIFVNELVKLWAAEGFLKVDETKSMEQVAKQSLKDLVDRSLVFIQRVSSFDGKIKACGMHDVIRELCLREARKINFVNVIMDNQNPSEQAKHFSTTRVRISIQSKQSKTVVNRLSMVRNDDSCSIVLSVDDPSSSNMMQALKRFKVLRVLDLASSTLNAFPSCIVELFHLRYLALSVYSSTDDRGIDIPPSIASLQYLQTLILKSPTSLAWKYSRPFILPSEIFKMSQLRHLSLDWNYLKQHESIERSWLLRNLQCLSGWNPLSCTSSIFRLLPNVKKLQIYGIQEGYIRSNKDEVFHSLCYLDQLKELDFKMKKTAIVRPMFPTRLILPSIGTFLKNLKKLAFRGTRLHWKDLEILGKLPKLKALKLGYDACLGTDWEVGEEGFPHLKFLRLKQLYLHKWIASSDHFPCLERLVINRCWSMYSIPQDFVDITTLQLIHVSDSAKSVGNSAKMIQQEIEDNYGSSVETVIRNVEVAEHASSEPSNVSTSEEPLESWRLKMRQGSTTRLLSTYVIELEQYPTGAHIASRMLYTAENSFEDVNSKVVADFGCGCGTLGLAAGLLGAESVIGLDIDAESLEIAYANADELEVLFVYVITFFACKVEKAFKAESFTLVLMDICSLLCFNTFLELFHLQLDMDFIQCDISNLKWRGQIVETVVMNPPFGTRRKGADMDFLSSAMKVASQAVYSLHKTTTREHVKRAALRDYNAISAEVICELRYDVPQLYKFHKKKEVDIAVDLVNKWMEMQYMYTKSKDAEEQNLTFASSTSQHVEAPMVGHENELEMMQDQLARGAGELEVVSVVLMGGIGGVQNLLRIPPSKFNRTFNTSMKVPLRSISSSLVRYHLPSFTSYVPIFLGMFNSSLAIPFSMSVVMLLYLLYT
The following text describes a protein:
Function:
A cytochrome P450 monooxygenase involved in activation of vitamin D precursors. Catalyzes hydroxylation at C-25 of both forms of vitamin D, vitamin D(2) and D(3) (calciol). Can metabolize vitamin D analogs/prodrugs 1alpha-hydroxyvitamin D(2) (doxercalciferol) and 1alpha-hydroxyvitamin D(3) (alfacalcidol) forming 25-hydroxy derivatives. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Sequence:
WGGAWGGGPGACAAGLGAALLLLLFVLGVRQLLKQRRPAGFPPGPSGLPFIGNIYSLAASGELAHVYMRKQSRVYGEIFSLDLGGISAVVLNVRFFADRPCLPLFMKMTKMGGLLNSRYGRGWVDHRKLAVNSFRCFGYGQKSFESKILEETNFFIDAIETYKGRPFDLKQLITNAVSNITNLIIFGERFTYEDTDFQHMIDASVFLYNAFPWIGIIPFGKHQQLFRNAAVVYDFLSRLIEKASINRKPQSPQHFVDAYLNEMDQGKNDPSCTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPTGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRNPEIFYPERFLDSSGYFAKKEALVPFSLGKRHCLGEQLARMEMFLFFTALLQRFHLHFPHGLVPDLKPRLGMTLQPQPYLICAERR
The following text describes a protein:
Function:
Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MKGNTGFSFPHFLGFAIYLSVSRIHKRRRTGEASSVRFPTEAHPNDEAFNPILWPTFYRIYKNKSTESFQSLPYQVSLFSCMLWLYYALIKQDAFLLITINSFGCIVETIYIALFFAYATRDKRIAAMKLFFTINVAFFSLILMITHFAVRSPSLQVSVIGWICVSISVSVFAAPLMIVARVIKTKSVEFMPFTLSFFLTISAVMWFAYGAFLHDICIAIPNVVGFILGMLQMVLYGIYRNSGVKIDTEKKINSSEQQLKTIVVMSQLGVSEVHPVDITVDPLSETVHHEDPSKQKEPSIEDGKCHVGTVARFEYI
The following text describes a protein:
Function:
[Isoform Transglycosylase P7]: Component of the phage ejection machinery which acts as an exolysin. Muralytic protein involved in host peptidoglycan digestion necessary for viral DNA entry into the host cell; [Isoform Protein P14]: Does not display any enzymatic activity. Required for DNA injection in the membrane transformation event. Involved in the formation of the membrane tail tube to connect the virus interior with the host cytosol. Essential for viral infectivity.
Subcellular Localization:
[Isoform Transglycosylase P7]: Virion membrane; Single-pass membrane protein. Note=Part of the capsid inner membrane. Approximately 20 copies per virion; [Isoform Protein P14]: Virion membrane; Single-pass membrane protein. Note=Approximately 20 copies per virion.
Sequence:
MSGALQWWETIGAASAQYNLDPRLVAGVVQTESSGNPRTTSGVGAMGLMQLMPATAKSLGVTNAYDPTQNIYGGAALLRENLDRYGDVNTALLAYHGGTNQANWGAKTKSYPGKVMKNINLLFGNSGPVVTPAAGIAPVSGAQEMTAVNISDYTAPDLTGLTMGAGSPDFTGGASGSWGEENIPWYRVDKHVANAAGSAYDAVTDAVSAPVEAAGNYALRGVVIIAAVAIVVVGLYFLFQDEINSAAMKMIPAGKAAGAAAKALA
The following text describes a protein:
Function:
Catalyzes the hydroxylation of urate to 5-hydroxyisourate (HIU). Is likely to be involved in the urate degradation pathway to allantoin. Is slightly more efficient (about 2.6 times) with NADPH than NADH as the electron donor.
Sequence:
MSLAQLEHALQHDLQRLAHGGEPWVRPRVHPAGHVYDVVIVGAGQSGLGAAFALQRERVHNVLVIDENPPGQEGPWVTYARMQTLRTPKQITSIDLGVPTLTFRAWWEAQHGAAGWDALDKIPRGTWMDYLRWYRAALRLPVRNATQLVRIEPDAAPGIHRLHLAMGAPLMARKIILATGIQGGGQWQVPEWITQALPAQRYAHTSGPIDYAALAGKRVGILGGGASAFDNACFALDQGVARAEVFVRRAALPRVNPIRHMEQAGIIPRFAALPDADKYRMMASFFGRNQPPTNDTFQRACAHAGFALHLDAPWLGVEEHNDVVVVRTPQGEHRFDFLAIATGLVTDPRLRPELAALSGRIACWADRYQAPPGQANPVLDAHPYLGPGFELLPRTPDDAAAVDGLFAFNYSALINHGLSAAALSGLKVALPRLARAVADQLFLDDRQAMVEAYLGYDQAEFVGQWPQPTQAVA
The following text describes a protein:
Function:
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. It probably carries the active site for 3'-splice site cleavage.
Sequence:
MSPSALSEPIAISFIAGRYLLFDIDVVTHLRRTYHICGVLTGTIPQIPQQNLFLGLPVELLPEEAKVLVNKKIAYIVEDTPWHKQHFPSIEGSDRKKYLESLRTEALKAKRAADTEARKRTENALAKKALKGGSESLPGTPRKSNESKDSISNEPDSLFDDERPASRASSAASPSTKLWGITPTVSYHSSSSSQNFPSSLDPSVPSSYPLFAHLHSRDYFMTPGLRFGCDYTVYPGDPLRFHSHFIATGYGWNEEIRLLDIVGGGRLGTGVKKGFLIGGENPQKQSVEETDGLYQHKHPFHDETPYDKE
The following text describes a protein:
Function:
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNNKVMDFMTNKFAPKVNKVVKNPWVSAIQDAIMSALPLVFVGSLVTIVSLLKNLFPGMPDFSMISNFSFGMFGLVVAFLIPYYLMEKKGNSSQKLISGATGLVLFLMLLFPTISADGDAVFILSRFGATGMFLSITTGLFVGCVMNFAAKRSFFSEDTPIPDFVVGWFNSLLPITFILIVGWLITVQFNIDFFEVIVAVFSPLASIVQSYPGFVLSVFIPAFLYTFGISGWVMMPAIYPVYMAGLAENSQAVANGASASNIATQETVYALISIGGVGTTLSLSIMMLILSKSLQLKAIGKAVIVPSIFNINEPLFFGAPIAFNPYLMIPTWINAFLVPSIAYFVMSMNLVSIPAQSFLLWYMPYPVTSYLATQDFRGVIACLAIIVITWLVYLPFFKAYDNSLLKQEKLDAVETEKEMVTN
The following text describes a protein:
Function:
Involved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze the reversible cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-deoxygalactonate (KDGal). It is equally active with both D- and L-glyceraldehyde.
Sequence:
MITPLDAHGNIDYNATNILIKYLEGINVDYLFPMGSTGVFPYFTLKERKDFLKFVRENSKKPIMAGVGSSSINEVNELMKFSMDIGIEAAVLMPPYYIKLNQEAIYHYYKEILSSNDMDLLIYNIPQFTNKIDPETVKNLKSEFSSVKGVKDSSADIRGFMEMLSLSDDDFAVFQGQDDLLFTSLELGASGGVCGTTNFSDGIVRLYHEYKNNREMALKIEKNDVIPLMKKLGKYQFPNAYYEYFYKKNNINGGYRPPMYRVGIEI
The following text describes a protein:
Function:
Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Sequence:
MTQVFVALGANLEDPKAQLDNALMALSSLAENQSLKVSPYYHSTPMGEVVQPDYINAVASFETKLTPLALLDALQHIENTQGRVRKERWGPRTLDLDLLLYGDAIIDEPRLKVPHYGMKERSFVLVPLAAIAPDLVLPCKTPLQSLISEKFLAELQLLGNDH
The following text describes a protein:
Function:
G-protein-coupled receptor of lysophosphatidylserine (LysoPS) that plays different roles in immune response. Acts a damage-sensing receptor that triggers tissue repair upon recognition of dying neutrophils. Mechanistically, apoptotic neutrophils release lysophosphatydilserine that are recognized by type 3 innate lymphoid cells (ILC3s) via GPR34, which activates downstream PI3K-AKT and RAS-ERK signaling pathways leading to STAT3 activation and IL-22 production. Plays an important role in microglial function, controlling morphology and phagocytosis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTNTTEALCEVPANEVFIFAYSLVFLVSLVLNCFPLAVHFCSDQRVQSSITVYMNNLIAADFFLCLSLLLRIASYADSTIMMFNIYCSFGATAFYINMYASILFMEFIAINRYLKIVRPLETHTLQTVRTARYISGAIWFVLLAISSIYVILYLSTSWSKTKPEVFICDFQDSSQISAAYTSVHSASFVIFIFILVSLIFLYWKTLQKLREVQLSTQAEFNRQKFRKSKQNMLVLVVIFCVCFVPYHLVRLPYIFIRHLLNDCTSIQALHILKEVTALLAALNVSLDPLIYFFFCKAFRDKVNLISCQNCP
The following text describes a protein:
Function:
Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MTMDGSTPEEKRLKDIKFRQWGSYVGERQWATVREDYSADGDAWSALTFDDSRSRAYRWGEDGLAGVSDRKQFVNVTMALWNGKDPILKEKLFGVTNSQGNHGEDVKEQYYYLDNTPTHSYMKYLYKYPQNEYPYKQLVEENQKRSRLEKEFEITDTDIFKNNEYFDVVMESAKGDAPDELYFRITAYNRSDKAASLHILPHCTLRNIWSWGADEYQEVKKPHVKQIDEYTVEVETQKFGKRYLVFAPSPGFKESDPDVEPQLIFTENETNTKKLYNQDNKSKYVKDAFHEYVVDGKQEVVNPEKQGTKAAAWFTFKDIPAGEYVTIRYKFTNDKSEVDEFELDNIISKRQAEADEFYWHVTPYPISDELRQIQRQGFAGLLWTKQFYYFVHNYWANGDPDTIKPPMNRANGRNKEWKHLYTDEILSLPDKWEYPFFAAWDSAFHCIPFAMIDPRFAWMQLDHLVREWYMHPNGQIPAYEWNFSDVNPPVHAWAAYRVFKIERKMYGVESLDYLESIFQKLLINFTWWVNRKDAEGKNVFEGGFLGLDNIGVFNRSEELPTGGSLEQADSTGWMAFYSLQMLNIALELAKTRPVYENIASKFFEHFIIIADAMTFRGGDGDESTKDALWDDKDKFYYDAIRYSDHHVESLHVRSLVGLIPLYASLTIEPDLLNRYPSFKKRLNWFLVHQKKMSERNIASMETRGVGERMLLSLVSKDRLLAILDRMLNEDEFLSEYGIRSLSKYHKDHPYVKEVNGEKFTVAYLSGESDSGMFGGNSNWRGPIWFPTNFLLVEALQRFYLYYGPDLKVECPKGSGDYLNLAQCAQEIQHRLIRIFLPDEEGDRACNGGVDILNRDPLFKDYVPFYEYFDGDSGRGLGASHQTGWTSLVTKWIHDNAASNRVPRTPQTPKNRRRQSVFLHASEEANDDDEEELQKYVPKCGPMPGTLARRKSGKSLLNLTVNALDLGDEEGSATTKAAVCGQVGEGKSISEEELEKLHKVQSGASIDSNEAAQLDSDLLGQVRAAFKKFKSRTDEDEFEGDEFETRCS