lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May play a role in ribosome biogenesis.
Subcellular Localization:
Nucleus, nucleolus. Nucleus, nucleoplasm.
Sequence:
MVKRKQGSRAQKRAEETYTEFSSALIDQAEEDRVTSKQDDDLFVLDTDRKDAIGTSARNKAARRAANREKLLAGVTTTSGSDAKRRKYEPSDKDLRQIQKVLQHHGKDGAIALALRGKARMEQKRHAKRMNGMTPKSGKPTYDLWDDAAVASADTTSKKKSKLIAVATGKPSPNGISPVDIVSATKPLPVDPNFEVLSQQPTKALSNKHLKARKHAQLTAKPTLALEVAHPGQSYRPDKEQHQDAIGEALSIEIRRNEAEEYKSKPISSGMSEFTKRFIVGESDSEESSDEEEEDNDDGNVATMGATKLIKKKEKLTRAQRNKQKRVKAEQTALFARKQSKQFNHQINEVHKHSKAVKEEEKLHSVRQSELAQLRDEKKSQPLGKNLWNAVSQVDPLRAPSLPVALTEELEGKSGGKGSLRTVTPKGSLVTDRLESMVARGMVSKKKVDGRRIVQGKRRKKVMGVKGTEYLLI
The following text describes a protein:
Function:
Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate.
Subcellular Localization:
Nucleus.
Sequence:
MQIGLSMSCKSPTVPDPKATEAEPEQGKFLPLKTMLGPRYDDQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTNRFYDRNDIQKEGIKYIKLQCKGHGECPTPENTETFIRVCEHFSEKNPTELIGVHCTHGFNRTGFLICAFLVEKLDWSIEAAVATFAQARPPGIYKGDYLKELFRRYGDEDDAPSPPELPEWCFEDDEEEDDDNGKMGGQESEPGSSSSSFGKRRKEHLKLGAVFLEGVTVKYVTQVTTQPKLGGIQQKCQQFCGWEGSGFPGAQPVSMDKQNIKFLEQKPYKVSWKADGTRYMMLIDGKNEVYMIDRDNSIFHVSNLEFPFRKDLRMHLTNTLLDGEMIVDKVNGQVVPRYLIYDIIKFNGQPVGDCDFNVRLSCIEKEIIFPRHEKMKTGHIDKAQEPFSVRNKPFFDIYASRKLLEGSFAREVSHEVDGLIFQPTGKYKPGRCDDILKWKPPSLNSVDFRLKITRIGGEGLLTQNVGLLYVGNFDRPFAQIKVTKELKQYDNKIIECKFENNSWVFMRQRIDKSFPNAYSTAMAVCNSIQNPVTKEILFEFIDRCMAASQGQTRKHHLDPDTELMPPPPPKRPRTIT
The following text describes a protein:
Function:
Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Plays an important role in chromosome congression and in the recruitment of CENP-O complex (which comprises CENPO, CENPP, CENPQ and CENPU), CENPE and PLK1 to the kinetochores.
Subcellular Localization:
Nucleus. Chromosome, centromere. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex.
Sequence:
MSGKARASRKKPQQVKRSLKQRANKEADLPENEVGNTAKRNRSHAKHLSSKVTGQATYVHLKRVKISSSKRTTWQPLPKDTEEYLQSMMESVILGILFNIKRKEEIQCHLNQLKKRLLQQCATLKVPPRKLNYLKDVSKMLKMEKAQERANEESLASLQEEIDKIVETTESMTESIQSLKNKIQILTSEVEEEEQEVKQVFHIDSNKVLALPELSQKSLKAPILQEEILALIPNQNALLKDLDVLHDSAPVKNVSAFIEEAYKKLDS
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:
MKRPGEPVQRLQPAKKNVNVVSNTNSAHDSQLPAAAVPVSHDDRLSGSSSCSKTIFKVVWGKISTRKHKTWEGDGTLEVSGRSAVLKDEAGKVITTASGLKIDEVTEGIQLVVGSKEVEVLEKCNENQQPRLENSSTVVSSTGGSKICLPVPSIGGFKPPVQVVRDDVEAEARSEASPRIDAVPLVDTTNFSRDSSCRVQNNFKSVFTTREDEQEAVQPLIMKKPSFEHQFQHNAQNEPVVEVQVPLCVTRHLRPHQREGVAFLYECVTGLRMLEPPGCGAILADEMGLGKTLQCIALMYTLLKTGPYGKPLAKRVLIVTPSSLVDNWDREITKWLRSERIFTFIVGPNNKLKRYAQSPHIPILIISYEMLAKQIGELETVKFDLMFCDEGHRLKNSNVKAFGVLNRLECRRRVLLTGTPIQNDLQEFFSLINFVNPGAIGTYQDFKARYETPIVVSQRPGVLPQSIELGIERLNELNAITGRFVLRRTQEVINRYLPDKHEVVVFCHPSALQTQLTRTALSFYDSEKGADNAVSPLQLITILKKICNHPSLVSVQGKGDPESLVHLLAEQLPPWQRMGPTDSAKLGIVEALLEAMLAMQEKIVIVSYYSKTLDMIGGLCDHYNYKYCRLDGSTAGPDRSRIVAAFNNPANDSFILLLSAKAGGAGLNLIGASRLVLYDNDWNPANDLQAMSRVWRDGQRKPVFIYRLLTAYSIEERIFQRQISKTSLSGTVVDQRQNLSNLKLSEEELKDLFSIIDPNAEADCLTHSLLECPCAGIGNAPDRVAELPELCDPLDDLTNEPISRFQLRPTVGGGGKHGKLGTKKHALKMQELMRWEHHRSPVSERVLEQLGLARSADEIVFLFRNIVSAPK
The following text describes a protein:
Function:
May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex.
Sequence:
MAEGSFSVQSESYSVEDMDEGSDEVGEEEMVEGNDYEEFGAFGGYGTLTSFDIHILRAFGSLGPGLRILSNEPWELENPVLAQTLVEALQLDPETLANETAARAANVARAAASNRAARAAAAAARTAFSQVVASHRVATPQVSGEDTQPTTYAAEAQGPTPEPPLASPQTSQMLVTSKMAAPEAPATSAQSQTGSPAQEAATEGPSSACAFSQAPCAREVDANRPSTAFLGQNDVFDFTQPAGVSGMAFPRPKRPAPAQEAATEGPSAASGVPQTGPGREVAATRPKTTKSGKALAKTRWVEPQNVVAAAAAKAKMATSIPEPEGAAAATAQHSAEPWARMGGKRTKKSKHLDDEYESSEEERETPAVPPTWRASQPSLTVRAQLAPRPPMAPRSQIPSRHVLCLPPRNVTLLQERANKLVKYLMIKDYKKIPIKRADMLKDVIREYDEHFPEIIERATYTLEKKFGIHLKEIDKEEHLYILVCTRDSSARLLGKTKDTPRLSLLLVILGVIFMNGNRASEAVLWEALRKMGLRPGVRHPFLGDLRKLITDDFVKQKYLEYKKIPNSNPPEYEFLWGLRARHETSKMRVLRFIAQNQNRDPREWKAHFLEAVDDAFKTMDVDMAEEHARAQMRAQMNIGDEALIGRWSWDDIQVELLTWDEDGDFGDAWARIPFAFWARYHQYILNSNRANRRATWRAGVSSGTNGGASTSVLDGPSTSSTIRTRNAARAGASFFSWIQHR
The following text describes a protein:
Function:
Negatively regulates TGF-beta signaling.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MDRQSSFVSIWLQLELCAMAILLTKGEIRCYCDAPHCVATGYMCKSEANACFTRVLDPLNANSPLTHGCLEAGAADACSSRRAATAADGLSGALVLECCHDDMCNYRGLHDLAHTKDSADGRYQADGNNRNLVTRVQELGSAKEVWFRAAVIAVPIAGGLILVLLIMLALRMLRSENKRLQDQRQQMLSRLHYSFHGHHTKKGHVAKLDLECMVPVTGHENCCLTCDKMRQADPSNEKILSLVHWGMYSGHGKLEFV
The following text describes a protein:
Function:
Component of a complex that catalyzes the oxidation of glycolate to glyoxylate.
Sequence:
MSMEKFEFPIDLAEKCVKCGLCKSVCPTYPFKEEEGAFARGRLALAEMVVKGELPLTKEVVAQWNECAMCRRCEWICPNDVQYKEIMVHAREIQRKETERDFISEAGLKSLEFMQSKPGRVALKIAGILSKPLPKEIKVPLPTGGVKFFPKPYGKPFGIRGKTFRAKNEKMKLLFFTGCMIDVFYGKTGENVIKVLNKLGYTVIVPKDIKCCGAPHLYHGNTEAFEKLKEHNLKEIEKYEYDALVVACPTCGGALKEDYGKDWKVFSFTEIIANEDIEFKGKGEKVTVHVPCHYYTAMKLNPNNFYKALGKVKNAETVKAEKAQSCCGFAGLFSIKNPELSEEIQREKMLDFKKTEADYVVTECPGCVLQLRDGVKKFKNQQEVKHIADYLGERI
The following text describes a protein:
Function:
Plays a role in erythroid cell differentiation.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Mainly nuclear.
Sequence:
MILTKAQYEEIAQCLVSVPPTRQSLRKLKQRFPSQSQATLLSIFSQEYQKHIKRTHAKHHTPEAIESYYQRYLNGVGKNGAAPVLLELANEVDYAPSLMARIILERFLQGHEQTPPSKSVINSMLRDPSQIPDGVLANQVYQCIVNDCCYGPLVDCIKHAIGYEHEVLLRDLLLKKNLSFLDEDQLRAKGYDKTPDFILQVPVAVEGHIIHWIESKASFGDECSHHAYLHGQFWSYWNRFGPGLVIYWYGFIQELDCNRERGILLKASFPTDIVTLCHSTA
The following text describes a protein:
Function:
Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Domain:
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Sequence:
MSTNSRSNSRANFNNEIHDIGTAQNSSMPPTYYDRSLADIFPPHLLKKVVSEVVSTFLLVFVTCGAAGIYGSDKDRISQLGQSVAGGLIVTVMIYAVGHISGAHMNPAVTLAFAVFRHFPWIQVPFYWAAQFTGSICASFVLKAVLHPIAVLGTTTPTGPHWHSLVIEIIVTFNMMFVTLAVATDTRAVGELAGLAVGSAVCITSIFAGAVSGGSMNPARTLGPALASNLYTGLWIYFLGPVLGTLSGAWTYTYIRFEEAPSHKDMSQKLSSFKLRRLQSQSVAVDDDELDHIQV
The following text describes a protein:
Function:
Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Subcellular Localization:
Cytoplasm.
Sequence:
MTIIKQEKTLFFFKNLQNIICNTFSKIDGKSLFKEDMWNTKKGYGRTRILKKGKVFEQVSVNFSHVFGKSLPKSSSNKKRDLENCSYQASGISVVSHPKNPYVPTSHLNIRFFLAKNKKRKTIWWFGGGFDLTPYYGFYQDVIHWHTIAKKICQPFGDDIYFKYKKWCDDYFFIKHRNESRGIGGLFFDDLCLPDFHSAFLFSKSIGKGYIDAYFPIVNLRKSYSWGSRERNFQLYRRGRYVEFNLLLDRGTLFGIQSNGRIESILSSMPPLVKWEYGWHPKPNSPESKLYTDFLPIKDWIDK
The following text describes a protein:
Function:
Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.
Subcellular Localization:
Nucleus.
Sequence:
MSRKLKKTNLFSKDVAPLMYAYGDSPQPLPETVQCVDELVTSYLTDICANAYRCAQTVHRTKIKVEDFKFVLRNDPVNLGRAEELIMMNKVIADARKQFDNSEGKSLKRVNKDEDLEDIPEEDGEDMGGMGPGSELAVEETSKRGRKPKKRKNAKGSV
The following text describes a protein:
Function:
Component of KG oxidoreductase (KOR) that catalyzes the CoA-dependent oxidative decarboxylation of 2-oxoglutarate (alpha-ketoglutarate, KG) to succinyl-CoA. Methyl viologen can act as electron acceptor in vitro; the physiologic electron acceptor is unknown. Is involved in the alternative TCA pathway that functions concurrently with fatty acid beta-oxidation. Since a growing body of evidence indicates that lipids (for example cholesterol and fatty acids) are a predominant growth substrate for M.tuberculosis during infection, flux through KOR likely represents an important step in intermediary metabolism in vivo. KOR-dependent decarboxylation of KG also appears to be an important source of CO(2) in M.tuberculosis metabolism.
Miscellaneous:
MISCELLANEOUS: Is extremely stable under aerobic conditions.
Sequence:
MTRSGDEAQLMTGVTGDLAGTELGLTPSLTKNAGVPTTDQPQKGKDFTSDQEVRWCPGCGDYVILNTIRNFLPELGLRRENIVFISGIGCSSRFPYYLETYGFHSIHGRAPAIATGLALAREDLSVWVVTGDGDALSIGGNHLIHALRRNINVTILLFNNRIYGLTKGQYSPTSEVGKVTKSTPMGSLDHPFNPVSLALGAEATFVGRALDSDRNGLTEVLRAAAQHRGAALVEILQDCPIFNDGSFDALRKEGAEERVIKVRHGEPIVFGANGEYCVVKSGFGLEVAKTADVAIDEIIVHDAQVDDPAYAFALSRLSDQNLDHTVLGIFRHISRPTYDDAARSQVVAARNAAPSGTAALQSLLHGRDTWTVD
The following text describes a protein:
Function:
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2.
Subcellular Localization:
Cytoplasm. Mitochondrion intermembrane space.
Domain:
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation; The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters; The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
Sequence:
MTTTIVLASPNYAANESKFATSLAKFQANSTDASHQRDIHMIDRIAGNLASLTVNAYDRGLLFLDESTTLEEIKAILPKLFAAVHPGAALSVDGVFAKELADAFERESLLAGWMIESKGPFVLRRPAQVEAVPLKLSTKKSAGASVGVKLDFLFKKPEKQNTLSKNDVLKAAQEEEEGEDDLYDEDALVSDEETQLGKDVLAPPSTCSKPGKKKRCKNCTCGQREQDEAEAAAASAAAPKAVKLTDTMEIDFTELLKSKNAVSSCGSCYLGDAFRCSGCPYIGLPAFKPGEQVLISENRDKLSWMADDL
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
DVAIDFSHEEWACLDSAQRDLYKDVMVQNYENLVSVAGLSVTKPYVIMLLEDGKEPWMMEKKLSKAYPFPLSHSVPASVNFGFSALFEHCSEVTEIFELSELCVFWVLHFLSNSPNSTVEAFFKKWENKELSTKKDIYDEDSPQPVTMEKVVKQSYEFSNSNKNLEYTECDTFRSTFHSKPTLSEPQNNSAEGNSHKYDILKKNLSKKSVIKSERINGGKKLLSSNKSGAAFNQSKSLTLPQTCNRQKIYTCSECGKAFGKQSILNRHWRIHTGEKPYECRECGKTFSHGSSLTRHQISHSGEKPYKCIECGKAFSHGSSLTNHQSTHTGEKPYECMNCGKSFSRVSLLIQHLRIHTQEKRYECRICGRAFIHSSSLIHHQKSHTGEKPYECSECGKAFCCSSHLTQHQRIHSMKKKYECNKCLKVFSSFSFLVQHQSIHTEEKPFEV
The following text describes a protein:
Function:
Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes.
Sequence:
MSSISRTVECSFRTATRSTPRIRPTFASSCRCLTRSNNIAADIQSRTFFSLPDLTKIASLVPGQGQEDTSENARAQGVEVDGEVQRYHARKILPYSQAQLYSLVSDVPSYASFIPFCKSSTVLAPSSPGFSSTREWVGWKPEDKPFEVLAELAVGFGGLEERYVSKVVGRPYESVVATASNQTPMFKTLTTSWTFSPASSISPHPSFGNPSSDSSNSRIPNSASPADPTHGPSLLTIDLAFSFLNPLHRIASQAVLPKVAEKMVEAFEERCLKVWGQGKQ
The following text describes a protein:
Function:
Transcription activator that plays a role in the promotion of seed germination by both negatively and positively regulating the abscisic acid (ABA) and phytochrome A (phyA) transduction pathways, respectively.
Subcellular Localization:
Nucleus.
Domain:
The NET domain could serve as an interface to localize different proteins or complexes to chromatin.
Sequence:
MSVHVKEEPVLVPNCDVENTELAVFNGNGESELENFGTCVDEITDRVNQLEQKVVEVEHFYSTKDGAAQTNTSKSNSGGKKIAISQPNNSKGNSAGKEKSKGKHVSSPDLMRQFATMFRQIAQHKWAWPFLEPVDVKGLGLHDYYKVIEKPMDLGTIKKKMESSEYSNVREIYADVRLVFKNAMRYNEEKEDVYVMAESLLEKFEEKWLLIMPKLVEEEKKQVDEEAEKHANKQLTMEAAQAEMARDLSNELYEIDLQLEKLRESVVQRCRKLSTQEKKGLSAALGRLSPEDLSKALKMVSESNPSFPAGAPEVELDIDVQTDVTLWRLKVFVQEALKAANKSSGGTNAQNNNNTGTGEINKNNAKRRREISDAINKASIKRAKKA
The following text describes a protein:
Function:
Cyclic di-GMP effector that influences virulence by regulating flagellar synthesis. Binds bis-(3',5')-cyclic diguanylate (cyclic di-GMP or c-di-GMP), an important bacterial second messenger that controls a wide range of cellular processes. YajQ influences Salmonella pathogenicity by inhibiting the flagellar gene transcription, thereby allowing normal expression of the flagellum. Cannot bind GMP.
Domain:
Composed of two domains with a four-stranded antiparallel beta-sheet flanked on one side by two alpha-helices.
Sequence:
MPSFDIVSEVDLQEARNGVDNAVREVESRFDFRGVEATIELNDANKTIKVLSESDFQVNQLLDILRAKLLKRGIEGASLDVPDEFVHSGKTWYVEAKLKQGIESAVQKKIVKLIKDSKLKVQAQIQGEEIRVTGKSRDDLQSVMALVRGGDLGQPFQFKNFRD
The following text describes a protein:
Function:
Disulfide reductase which serves multiple functions in mitochondria, protecting mitochondrial components against thiol-oxidative damage as a thiol-disulfide oxidoreductase, and supporting urea cycle and respiration in mitochondria in a manner independent of active site thiols.
Subcellular Localization:
Mitochondrion.
Sequence:
MRGFIANSLKPHMRSFALRRSFTSSRILRKVNAVESFGDYNTRISADKVTVVDFYADWCGPCKYLKPFLEKLSEQNQKASFIAVNADKFSDIAQKNGVYALPTMVLFRKGQELDRIVGADVKTLSSLLAKYQE
The following text describes a protein:
Function:
Acetyltransferase implicated in the O-acetylation of Nod factors.
Sequence:
MKMSELEKMLKGEHFDGASAEIEALRSQAGRLKLEINQSLDEAERYALQRELFGHLGHKSCVQPPFHCEFGKTIRIGDHTFINMNVVMLDGAPITIGDHVLIGPSTQFYTASHSLDYRRRQAWETICKPIVIEDDVWIGGNVVINQGVTIGARSVVAANSVVNQDVPPDTLVGGTPARILRSLKDPAESMAE
The following text describes a protein:
Function:
Putative site-specific recombinase having a very important role in sporulation. It probably plays a role in the recombination of SpoIIIC and SpoIVCB to form sigma K factor.
Sequence:
MIAIYVRVSTEEQAIKGSSIDSQIEACIKKAGTKDVLKYADEGFSGELLERPALNRLREDASKGLISQVICYDPDRLSRKLMNQLIIDDELRKRNIPLIFVNGEYANSPEGQLFFAMRGAISEFEKAKIKERTSSGRLQKMKKGMIIKDSKLYGYKFVKEKRTLEILEEEAKIIRMIFNYFTDHKSPFFGRVNGIALHLTQMGVKTKKGAKVWHRQVVRQILMNSSYKGEHRQYKYDTEGSYVSKQAGNKSIIKIRPEEEQITVTIPAIVPAEQWDYAQELLGQSKRKHLSISPHNYLLSGLVRCGKCGNTMTGKKRKSHGKDYYVYTCRKNYSGAKDRGCGKEMSENKLNRHVWGEIFKFITNPQKYVSFKEAEQSNHLSDELELIEKEIEKTKKGRKRLLTLISLSDDDDLDIDEIKAQIIELQKKQNQLTEKCNEIQSKMKVLDDTSSSENALKRAIDYFQSIGADNLTLEDKKTIVNFIVKEVTIVDSDTIYIETY
The following text describes a protein:
Function:
Palmitoyl acyltransferase that catalyzes N-terminal palmitoylation of SHH; which is required for SHH signaling. It also catalyzes N-terminal palmitoylation of DHH. Promotes the transfer of palmitoyl-CoA from the cytoplasmic to the luminal side of the endoplasmic reticulum membrane, where SHH palmitoylation occurs. It is an essential factor for proper embryonic development and testicular organogenesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Note=Co-localizes with SHH in the ER and Golgi membrane.
Sequence:
MLPRWELALYLLASLGFHFYSFYEVYKVSREHEEELDQEFELETDTLFGGLKKDATDFEWSFWMEWGKQWLVWLLLGHMVVSQMATLLARKHRPWILMLYGMWACWCVLGTPGVAMVLLHTTISFCVAQFRSQLLTWLCSLLLLSTLRLQGVEEVKRRWYKTENEYYLLQFTLTVRCLYYTSFSLELCWQQLPAASTSYSFPWMLAYVFYYPVLHNGPILSFSEFIKQMQQQEHDSLKASLCVLALGLGRLLCWWWLAELMAHLMYMHAIYSSIPLLETVSCWTLGGLALAQVLFFYVKYLVLFGVPALLMRLDGLTPPALPRCVSTMFSFTGMWRYFDVGLHNFLIRYVYIPVGGSQHGLLGTLFSTAMTFAFVSYWHGGYDYLWCWAALNWLGVTVENGVRRLVETPCIQDSLARYFSPQARRRFHAALASCSTSMLILSNLVFLGGNEVGKTYWNRIFIQGWPWVTLSVLGFLYCYSHVGIAWAQTYATD
The following text describes a protein:
Function:
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Subcellular Localization:
Mitochondrion.
Sequence:
MQAVRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEHGVCTADKDCEDAYRVCQILDIPFHQVSYIKEYWNDVFSDFLNEYEKGRTPNPDIVCNKHIKFSCFFHYAVDNLGADAIATGHYARTSLEDEEVFQQKHIKRPEGLFRNRFEVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIEDNKVLGTHKGWFLYTLGQRANIGGLREPWYVVEKDGVKGNVFVAPRRDHPALYRDLLRTSRVHWITEEPPAALVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAVHALTTGQFAVFYKGDECLGSGKILRLGPSAYTLQKGQHRGGVAIENPSDGPEDGPGLRPLP
The following text describes a protein:
Function:
This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
Miscellaneous:
MISCELLANEOUS: The class C beta-lactamase family has a specific amino-acid numbering system known as SANC, for structural alignment-based numbering of class C beta-lactamases, or else the simpler name structural position. A multiple sequence alignment was used to derive a consensus sequence and then the consensus was numbered taking into account insertions and deletions. This allows use of identical numbers, e.g. for active site residues, despite differences in protein length. UniProt always uses natural numbering of residues, hence there appear to be differences in numbering between this entry and some papers.
Subcellular Localization:
Periplasm.
Sequence:
MMKKSICCALLLTASFSTFAAAKTEQQIADIVNRTITPLMQEQAIPGMAVAIIYEGKPYYFTWGKADIANNHPVTQQTLFELGSVSKTFNGVLGGDRIARGEIKLSDPVTKYWPELTGKQWRGISLLHLATYTAGGLPLQIPGDVTDKAELLRFYQNWQPQWTPGAKRLYANSSIGLFGALAVKSSGMSYEEAMTRRVLQPLKLAHTWITVPQSEQKNYAWGYLEGKPVHVSPGQLDAEAYGVKSSVIDMARWVQANMDASHVQEKTLQQGIELAQSRYWRIGDMYQGLGWEMLNWPLKADSIINGSDSKVALAALPAVEVNPPAPAVKASWVHKTGSTGGFGSYVAFVPEKNLGIVMLANKSYPNPARVEAAWRILEKLQ
The following text describes a protein:
Function:
Component of the cleavage factor Im (CFIm) complex that plays a key role in pre-mRNA 3'-processing. Involved in association with CPSF6 or CPSF7 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. NUDT21/CPSF5 binds to cleavage and polyadenylation RNA substrates. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA. Binds to, but does not hydrolyze mono- and di-adenosine nucleotides. May have a role in mRNA export.
Subcellular Localization:
Nucleus.
Sequence:
MRDIWVNMSNPSPLLPVHLGHITHIPSWTATSKVTQHSDIVLRHRPVCYFASPQRFFLSRLFSAFPQALSLIFRMNYEMGSSADGDRSSSGDSSNHVLDIYPLSCYYFGSKDPLLLKEETLADRILRMKSNYSRYGSRTCVVAVILVELFKHPHLLLLQVKNSFFKLPGGRLRPGESEINGLKRKLSRKLSVNEDGDGSDWEVGECLGMWWRPDFETLLYPYLPPNVKNPKECTKLFLVKLPPSRKFIVPKNLKLLAIPLCQLHENDKTYGPIIAGVPQLLSKFSFNIIDS
The following text describes a protein:
Function:
3'-5' RNA exonuclease that trims the 3' end of oligo(U) and oligo(A) tracts of the pre-U6 small nuclear RNA (snRNA) molecule, leading to the formation of a mature U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate. Participates in the U6 snRNA 3' end processing that prevents U6 snRNA degradation. In addition also removes uridines from the 3' end of U6atac snRNA and possibly the vault RNA VTRNA1-1; Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA.
Subcellular Localization:
Nucleus.
Sequence:
MAGKSSGLGALACYGSSSEEEGPSPSKSLQQQQTGTGELPGPKQQQHKDVVVTLQNSKRKLDNVDERLIPLGKDTKRTRTKDLEKRVQLPSVPTDVLQMFSDQQAIEAKRDNPEEHGGRIRSFPHVAGNWATHVYVSFEPDADFTDGVKHLLGSLEADVQLQQVQDYHISLSRTVPLTFHWIQPFIDSLRDALRHTERFFCTFHGAKVYTNDEKTRSFLGLEVTGGHNHLLQLVLGVDSCLEEFRLQKYYKNPSFHMTVGWCVGDVHEDTQQFNQKLQASLAEAQEEFPSLGGFLVQEIKCKSGNRFFSFPLR
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSLNLSVRDINFIKYLWRYYNFFLITPWHDFDNIVPCNSSICKIFATLLIFIKVYWVSDATFLDKHLLFTQKVNYCITTVTITTLNLLTVVKSSFLADGNKWRTLFNNLRYLDLNLHNKGKTEGSIWKNFYFTFVLRQLFFIMSVVYQIHVWTSKEKISFLRGFWLSPAVDMFYEFQIIELMTSVVKSLESRYADLNENFLQCQDEKFESFVYYHRILGETVDLFNSLFGYQTLLITFHIGSQLVVCLNFSFGFLTPSSFTLQLDLLISNFWVVLVIIVSFVRMVILVDSTVQQAERFLDLLYKMQMVFPQLRKNCFLTKFSKHNIRKFTAAGYFQMRKGIIFSVMANVATYFIIAVQLNESQKTT
The following text describes a protein:
Function:
Required for the maturation of the [FeFe]-hydrogenase HydA (By similarity). Catalyzes the reductive cleavage of S-adenosyl-L-methionine (in vitro), suggesting it may contribute to the biosynthesis of an essential sulfur-containing ligand that binds to the hydrogenase active site [2Fe-2S] cluster.
Sequence:
MTGREILEKLERREFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDEVHIRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFGAKTIVLQSGEDPYYMPDVISDIVKEIKKMGVAVTLSLGEWPREYYEKWKEAGADRYLLRHETANPVLHRKLRPDTSFENRLNCLLTLKELGYETGAGSMVGLPGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANEKKGDFTLTLKMVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVIMPNWTPSPYRQLYQLYPGKICVFEKDTACIPCVMKMIELLGRKPGRDWGGRKRVFETV
The following text describes a protein:
Function:
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Subcellular Localization:
Cytoplasm.
Sequence:
MVVNSDPDWLWRGTAEIFPHNADSNNPQEHLGILTQQDRPLRVKLGIDPTGTDIHLGHSIPFRKLRAFQDAGHTAVVIIGDFTAQIGDPTGKSEVRKQLTADQVKRNAESYLAQLKPILDFDTPGRLEIRYNSEWLSNLDLNKILELLATMTVGQMLAKEGFAERFQKENPIFLHEFLYPLMQGYDSVAVNADVELGGTDQKFNIAVGRDLQRHFGKTPQFGLLLPILLGTDGQQKMSKSLNNYVGLQEDALSMYSKLEKTPDRLLGEYFELLTNLDLAELPENPRECQKLLAKEVTAQFHGVAGAIAAQKTAEDIVTQGKAGNTDSVPEFSLAEITFPVKLAYLLSASGLCPSSSEGRRQIKGGAVRLDGDRLEDVNQEYADPKMLINKVLQMGKKKFIRLIS
The following text describes a protein:
Function:
Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Sequence:
MFVTETDNDALNFRISATKAGYIEDPYVLHFQNRNSLPRPPLINRGTFVRTWSIDALCEEFILRVPGMKQIISLGAGTDTRVFRFLAKYGPSKFVYHEFDFLVNCVKKLRVISRHKDMSDLLGGPDGFKIDARQGTLRSASYNLTSMDINDLAKQPLLEHIRPDLPTILLSECCLCYLSVGGVDAIYQWATSTFPSLMTIIYEPIRSSDPFGAMMVRNLSARGITMPTLSHYDTPDDQKKRMREYGFSFCNALDFYEIEKQWFSQELVKRLNHIEMLDELEEWALLASHYCLVYAISKKCEESIKQNKDLSDHNTKLFPF