lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalytic subunit of the GMPPA-GMPPB mannose-1-phosphate guanylyltransferase complex (By similarity). Catalyzes the formation of GDP-mannose, an essential precursor of glycan moieties of glycoproteins and glycolipids. Can catalyze the reverse reaction in vitro (By similarity). Together with GMPPA regulates GDP-alpha-D-mannose levels.
Domain:
The N-terminal substrate-binding domain adopts a Rossman-like fold and has a binding pocket for GTP or GDP-alpha-D-mannose (By similarity). Substrate binding is coordinated by an Mg(2+) ion (By similarity); The C-terminal domain consists of a series of tandem hexapeptide repeats that adopt a beta-helix conformation (By similarity). The beta-helix forms several protein interaction surfaces involved in assembly of the GMPPA-GMPPB mannose-1-phosphate guanylyltransferase complex (By similarity).
Sequence:
MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPILLHQVEALVKAGVRHVILAVSYMSELLEREMRAQEQRLGIKISLSHEKEPLGTAGPLALARELLTDNQEPFFVLNSDVICDFPFDDMLKFHQQHGREGTIVVTKVEEPSKYGVVVYEGDSGRIHRFVEKPQVFVSNKINAGMYIFSPAMLRRIQLRPTSIEKEIFPVMAEEGQLYAMELQGFWMDIGQPKDFLTGMCMYLQSVRQQAPERLRAGPGFLGNVLVDPTAVIGQNCTIGPNVTIGAGVVLEDGVRVKRCTILKGAHIRSHSWLESCIVGWSSSVGQWVRMENVTVLGEDVIVNDELYINGANVLPHKSITDSVPEPRIIM
The following text describes a protein:
Function:
Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the promoter of specific meiotic and post-meiotic genes, facilitating their activation at the appropriate time. In the post-meiotic phase of spermatogenesis, binds to hyperacetylated histones and participates in their general removal from DNA. Also recognizes and binds a subset of butyrylated histones: able to bind histone H4 butyrylated at 'Lys-8' (H4K8ac), while it is not able to bind H4 butyrylated at 'Lys-5' (H4K5ac). Also acts as a component of the splicing machinery in pachytene spermatocytes and round spermatids and participates in 3'-UTR truncation of specific mRNAs in post-meiotic spermatids. Required for chromocenter organization, a structure comprised of peri-centromeric heterochromatin.
Subcellular Localization:
Nucleus. Note=Detected on chromatin.
Domain:
Bromo domains mediate interaction with histones that have acetylated lysine residues at specific positions. Bromo domain 1 mediates binding with histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively). The bromo domains also recognize and bind a subset of butyrylated histones: able to bind histone H4 butyrylated at 'Lys-8' (H4K8ac), while it is not able to bind H4 butyrylated at 'Lys-5' (H4K5ac).
Sequence:
MSLPSRQMAIVNPPPPEYINAKKTGRLTNQLQFLQRVVLKALWKHSFSWPFQQPVDAAKLKLPDYYTIIETPMDLSTIKKRLENRYYEKASECVGDFNTMFSNCYLYNKPGDDIVVMAQALEKLFMQKLSQMPQEEQIVGGKERMKKDIQQKTAVSSAKEQTPSKSAENVFKRQEIPAGFPDVCLSPLNMAQEAPPTCDSQTVVQITKGVKRRADTTTPTTSSAKASSESPPPLREAKPANAPVKENTVKSVLPDSQQQHRVLKTVKVTEQLKHCSEILKEMLAKKHLPYAWPFYNPVDVDALGLHNYYDIVKNPMDLGTIKGKMDKQEYKDACEFAADVRLMFMNCYKYNPPDHEVVTMARMLQDVFEMHFAKIPDEPVESMRACHLTTNSAKALSRESSSEASSGDCSSEDSEDERVQRLAKLQEQLNAVHQQLQVLSQVPLRKLKKKNEKSKRAPKRKKVNRDENPKKKAKQMKQKEKAKSNQPKKKKPLLKLEEEDNAKPMNYDEKRQLSLDINKLPGDKLGRIVHIIQSREPSLRNSNPDEIEIDFETLKASTLRELEKYVLACLRKRSLKPHAKKVVRSKEELHSEKKLELERRLLDVNNQLNCRKRQTKRPAKVAVSPRPPLPPPPPPPPELASGSRLSDSSSSSSSSGSGSSSSSSSSSGSGSSSSDSSSSDSSDSEPEISPKFTGVKQNDLPSKENTKQIQCSVPDITSAETALVQQSTGPCGAPGKPPQQMPGCQVPHHLQATESTASVQTQPLAGDCKRVLHGPPVVHASAESHTVLELQCHAPVQKDIKIKNADSWKSLGKPVKASSVLKSSDELFNQFRKAAIEKEVKARTQEQIRKHLEHSAKDPKVSQESQREFGSGFTPESSSNKVQGRSHGEEQSEQQQLPSPSETQDISKLWLLKDRNLAREKEQERRRREAMAGTIDMTLQSDIMTMFENNFD
The following text describes a protein:
Function:
Required for normal Golgi function.
Subcellular Localization:
Golgi apparatus membrane; Peripheral membrane protein.
Sequence:
MRSIGAAGAGPSPGLRWRPRSWGGACAPMADGGAEVAAVPPSGAANGLSNGAGGALAQTGNPLSRKLNKILETRLDNDKEMLEALKALSTFFVENSLRTRRNLRGDIERRSLAINEEFVSIFKEVKEELESINEDVQAMSSCCQDMTSRLQAAKEQTQDLIIKTTKLQAESQRLEIRAQVADAFLSKFQLTSDEMGLLRGTREGPITEDFFKALGRVKRIHNDVKVLLRTNQQTAGLEIMEQMALLQETAYERLYRWAQSECRTLTQESCDISPVLTQAMEALQDRPVLYKYTLDEFGTARRSTVVRGFIDALTRGGPGGTPRPIEMHSHDPLRYVGDMLAWLHQATASEKEHLEALLKHVTIQGIEENIQEVVGHITEGVCRPLKVRIEQVIVAEPGAVLLYKISNLLKFYHHTISGIVGNSATTLLTTIEEMHLLSKKIFFNSLSLHASKLMDKVELPPPDLGPSSALNQTLMLLREVLASHDSSVVPLDARQADFVQVLSCVLDPLLQMCTVSASNLGTADMATFMVNSLYMMKTTLALFEFTDRRLEMLQFQIEAHLDTLINEQASYVLTRAGLSYIYNTVQQHKPEQGSLANLPNLDSVALKAAMVQFDRYLSAPDSLLMPQLNFLLSATVKEQIIKQSTELVCRAYGEVYAAVMNPVNEYKDPESILHRSPQQVQTLLS
The following text describes a protein:
Function:
Glycosyltransferase required for the biosynthesis of the tetrasaccharide (GlcA-Gal-Gal-Xyl-)Ser core linker of heparan sulfate and chondroitin sulfate. May be involved in the biosynthesis of the HNK-1 carbohydrate epitope on glycoproteins. Required for embryonic development. Involved in the elongation of the pharyngeal isthmus during the later stages of embryonic development. Involved in vulval epithelium invagination.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
MFPSRLLEKWWLRAFIALVIFFVWQLFYAINRVQSLEEERATLQATIEVLTRKSDGLRTQIFEKERNLVRLNGKVEEIDTQIRDHLSLLPRVNRSTPFIYFITPTHFRAAQRADLTRLSYTLSHVPNLHWIVVEDSDELTPSIAGILKRSKIPNTHLNARTPSDQKMRYDDPNWTLPRGVEQRNRALLWIQNQLSGVKEGVVYFGDDDNTYDLKIFGEMRKVKNAGVWPVGIVGGMFVETPILEKNGSISHFNAVWKPERPFPIDMAAFAVNISLVLSNANALFSFDVPRGYQESTFLENLGIHRYNMEPLAEMCTKVYVWHTRTEKPKLSKESIDRLTKKTGFNSLEAHALGVDN
The following text describes a protein:
Function:
Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MKSLLRQIPQISKVVEIFKKKYPEIYVVKAAREVAEKYRKEIIEGKRKDLNGFLEDVERKIKSLMKPNIKRVINATGVVINTNLGRAPLSKDVINFISEIANGYSNLEYNLEEGKRGSRIAHIEKYLNELTGAESSFVVNNNAGAVFLVLNTLAEGKEVIISRGELVEIGGSFRIPDIMKKSGAILREVGTTNKTKVSDYEGAINQNTALLMKVHKSNFYMEGFVEEVKLEDLVKLGHKYGIPTYYDAGSGLLINLKEFGISVDEPNFRDCISLGIDLVSGSGDKLLGGPQAGIIVGKKNLIEKIKKNPIARALRIDKLTLSGLEMTLKLYFEKRYEDIPVIRMLTQDEKALRQKAKRLEKLLKDIPGLKISVIKDKAKPGGGSLPELELPTYCVAIRHDRLSSQELSRRLRLAEPPIVCRIREDQLLFDMRTVFHEDLKTIKKTLQELLSI
The following text describes a protein:
Function:
Involved in chloroplast protein import across the inner envelope membrane. Also acts as a chloroplast permease regulating the iron transport and homeostasis. Involved in the uptake and sequestration of iron in plastids.
Subcellular Localization:
Plastid, chloroplast inner membrane; Multi-pass membrane protein.
Sequence:
MQSLLLPPASSSGVSAVALRPGFQHSFNHQSLSTRSLPLFNPLLLAPKKKTTISSYQSPPSLSVYGFQIGGSKPSFTPSTVAFSYPTSPSSVPGDNEVDKAKLAQVAKRLEKTSRYFKRLGSIGFWGQLVSTVVAAVILSFSIVVTGKPTSPATFYATASGIAAAFVSVFWSFGYIRLSERLRRTSIDPAKAPPRADVVKGLRSGIMVNILGMGSALLGMQATVGFLVAKALTTSANPFYQGVSQGYSPVLALDVFLVQASANTLLSHFLGLVCSLELLRSVTVPNSESVVVPKVA
The following text describes a protein:
Function:
Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MDFDEELNLCITKGKNVDHSFGGEASSTSPRSMKKMKSPSRPKPYFQSSSSPYSLEAFPFSLDPTLQNQQQQLGSYVPVLEQRQDPTMQGQKQMISFSPQQQQQQQQYMAQYWSDTLNLSPRGRMMMMMSQEAVQPYIATKLYRGVRQRQWGKWVAEIRKPRSRARLWLGTFDTAEEAAMAYDRQAFKLRGHSATLNFPEHFVNKESELHDSNSSDQKEPETPQPSEVNLESKELPVIDVGREEGMAEAWYNAITSGWGPESPLWDDLDSSHQFSSESSSSSPLSCPMRPFF
The following text describes a protein:
Function:
Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.
Sequence:
MTYAVKEIFYTLQGEGANAGRPAVFCRFAGCNLWSGREEDRAQAVCRFCDTDFVGTDGENGGKFKDADALVATIAGLWPAGEAHRFVVCTGGEPMLQLDQPLVDALHAAGFGIAIETNGSLPVLESIDWICVSPKADAPLVVTKGNELKVVIPQDNQRLADYAKLDFEYFLVQPMDGPSRDLNTKLAIDWCKRHPQWRLSMQTHKYLNIP
The following text describes a protein:
Function:
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG. The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG. The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone. The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL. These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin. Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps.
Sequence:
MTHFPVNIASDKQEFDPERWAKTPTTESSVNGENGTAPTSGLPSRHPSTGISVLIVGAGMGGLMTALECWRKGHDVAGILERSEGPVYSGDIIVMQPSAVSIIRHWPDMLHDMKAEQVHAVVSYETHDGRHIYGPTVPSFNDPEHLETRKGPFVAPAQVRRKFYRMLLRQVARCGLRVEYGKTVKSYFEDEKDGKGGVIIATTGEAEVRVADIVVAADGLKSPSEILIAGQHVPPRSSGLSIYRTAFPKDLAMQNELVRKRWSDSPPIWEYWLGPGMYLGVFVGDDIISFGFTPRDDIVEGTATESWEPDTDPETVAQAMLSGAGDWDPAVLALIRSAPKGAIVHWPLLWRDLRREWTSPAGRVVQVGDSAHSFIPTSGNGGSQALEDAITLATCLQLAGSSQRAYLGTKIYNLLRYERVSCAQKMSFVNSQLKTGTDWDAIWKDPAKIRTRFPKWIFQHDPEAYAYEKFGEAFAHLLDGREFVNTNYPPGHEFRAWTVEEVWRNIADGKRVEDLLDGDWS
The following text describes a protein:
Function:
Confers broad-spectrum resistance to pathogens.
Subcellular Localization:
Secreted.
Sequence:
MANSMRLFATMLLLAMLVMAIGPMRIVEARTCESQSHRFKGPCVSEKNCASVCETEGFSGGDCRGLRRRCFCTRPC
The following text describes a protein:
Function:
[ESR1p]: Extracellular signal peptide that regulates cell fate.
Subcellular Localization:
[ESR1p]: Secreted, extracellular space.
Sequence:
MASRMGMVAIVSLFVCALAASTSVNANVWQTDDIPVVNSNMVRHSNMERQQQQGGFIGHRPRLASFNRASNQDGDRKRTVPSGPDHMHHSIPSHTPQHPPVYVQALYEDDRSRTSSGPSKSIGPPPLSDRY
The following text describes a protein:
Function:
Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Subcellular Localization:
Mitochondrion.
Sequence:
MANAWRSAVSCIMGAIKTQTPQPRVFSRGIQTVTLIPGDGIGPEISTAVMKIFEAAKTPIQWEERNVTAIKGPGGRWMIPPEAKESMDKNKIGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVDLVTIRENTEGEYSGIEHVIVDGVVQSIKLITEEASRRIAEYAFEYARNNQRTSVTAVHKANIMRMSDGLFLRKCREVAENFKDVKFTEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLHGHAKKIETACFDTIRDKKVLTKDLGGNSKCSEFTADICRRVQDME
The following text describes a protein:
Function:
May function in protein folding and assembly, and disassembly of protein complexes.
Sequence:
MSFVVGFDFGTKNCTIAVAQKGGVDVIANEVSNRLTPSMVSFGEKERYLGESALTNQLRNIRNTITNIKRFIGQEFKTDTVQEELKHEMFQSYEMDNGFVGYNVTYAGEQCSFSSEAILGMLFGKLKKTTEAFVNNPVRDVVISVPVFWNDYQRRAILNAGSIAGLNIIRLINETTATALSYGIYKEWSETDPTNVLFVDVGDSATSVSAVQYKKGQLKVLGTASNPNIGSRVFDETLVKHFAKEFQTKYKINVFENKKALIRLRQACEKVKKILSSNNEAPVSIDSLMDDKDVKGMIDRATFEELANDDMNTIVEPLQRLLSELQMTPDQFQSIEITGGGTRSTSLQKKLSEVLGRDLSKTINSEESVCRGAALQCAMLSPVFRVRPFAVNDVASYPVSVHFKSVSGVEQKLDLFNLKSAIPTPKPLRISFPVTKAEGFEIVVNSTFGTIATVKVDNIPAFTNKSSIKAKVWLDIHGIFHIDEVKLVEQIPEEETAAPAETPAETPANGEAAKPAEEKKVKVKETSLVFTTSRKGLTNELLKAAIEEEGRMQASDLLAIETAEKKNALESYIYDMRSKLQSSLKEYVTPADAETFMTQLNKQMDWLESEEGEDQTKSVYAGKLEELRRLGNPIQKRKQDLEDYPDAVQTLKNIASYVKNEAMIPGERYDHIEKEEKEKLCKDCDDAVEWIDALVAKQQATPKTQPCIINTTEVLAKKTQLEVTAKMILGKPKPKPVEVPKEEPKDTPMESKDAPAEEPVATKDQKMDDILD
The following text describes a protein:
Function:
Involved in the biosynthesis of the anthracyclines carminomycin, rhodomycin, daunorubicin (daunomycin) and doxorubicin (adriamycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the incorporation of a hydroxyl group at position C-11 of aklavinone, resulting in epsilon-rhodomycinone.
Miscellaneous:
MISCELLANEOUS: S.peucetius subsp. caesius ATCC 27952, a mutant strain derived from S.peucetius ATCC 29050, is the only organism reported to produce doxorubicin in vivo.
Sequence:
MALTKPDVDVLVVGGGLGGLSTALFLARRGARVLLVERHASTSVLPKAAGQNPRTMELFRFGGVADEILATDDIRGAQGDFTIKVVERVGGRVPAQLRESFEELVGATEQCTPMPWALAPQDRVEPVLVAHAAKHGAEIRFATELTSFQAGDDGVTARLRDLGTGAESTVSARYLVAADGPRSAIRESLGITRHGHGTLAHFMGVIFEADLTAVVPPGSTGWYYLQHPDFTGTFGPTDRPNRHTFYVRYDPERGERPEDYTPQRCTELIRLAVDAPGLVPDILDIQAWDMAAYIADRWREGPVLLVGDAAKVTPPTGGMGGNTAIGHGFDVAWKLAAVLRGEAGERLLDSYGADGSLVSRLVVDESLAIYAQRMAPHLLGSVPEERGTAQVVLGFRYRSTAVAAEDDDPEPTEDPRRPSGRPGFRAPHVWIEQDGTRRSTVELFGDCWVLLAAPEGGAWGQAAARAARIWASASTSISSAAMSPPPPAN
The following text describes a protein:
Function:
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Sequence:
MNNMLNEKKNFIRHVLMNSPPGKLYDLVKDINILLGSSVSIQKILEEVLKDYNEKNYNFILTDKNEYVITCKKFKVNHLYFIPKLKALVHVNHLKRTANVLETVKELKYPEQLENYRKECDKKLVDYVQEHYKKWSNLQTINYPEVHIKSPNGLRSEHCSSVYAYNEEDIFYLFFIICCDRSYLKNFHASTWRSSWTAQFFVDNDHVLLSGTIDISLTYFEDANINFKTSKCFEKKVRVNRDVDMFSSNILSAINEYENYILYDLNNFFTNINKNLIKSTRRIIPLSGQKFDWKGKYEDIPKQISNS
The following text describes a protein:
Function:
Inhibits programmed -1 ribosomal frameshifting (-1PRF) of a variety of mRNAs from viruses and cellular genes. Interacts with the -1PRF signal of target mRNA and translating ribosomes and causes premature translation termination at the frameshifting site. May exhibit antiviral activity.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, P-body. Note=Predominantly found in t for dsDNA.
Sequence:
MDGNVQEELELEKSIRRFREKFHGKVTLETAVALMRRFTNNHDQVCKYIILCMDNDTDLDVRNDLRNDPVARNVINKIKSDDQKAKEMPKDKDIKDLAKRMNTLPLTEKNLKMFNDAAENRIPSRDRQFACKECDFVWWRRVPQRKEVSRCHRCRKKFDPVPENKMWGIAEYHCPVCRRMFRGFGQIEVSSPCYVCRNPVLPSCILPPRRNQGPRTRNTHSCLAENCYNRRVPFVAGLQCAHPKSRIMNQLPKVLHPSEPHISTGSTIATCLSQGSLTENDIDDIILDDIKEEEEDEGSDDSDG
The following text describes a protein:
Function:
Iron-sulfur cluster subunit of the adenylylsulfate reductase which catalyzes reversibly the reduction of adenosine 5'-phosphosulfate (APS) to sulfite and AMP during dissimilatory sulfate reduction. The iron-sulfur cluster 2 is thought to accept electrons from a still unknown electron donor and transfer electrons to the iron-sulfur cluster 1 of this protein and then onto the FAD of AprA.
Subcellular Localization:
Cytoplasm.
Domain:
Consists of three sections from the N- to the C-terminus: [4Fe-4S] cluster-binding domain, beta-sheet and C-terminal tail. The beta-sheet and the C-terminal tail interact with AprA to stabilize the AprA/AprB heterodimer.
Sequence:
MPTFVDPSKCDGCKGGEKTACMYICPNDLMILDPEEMKAFNQEPEACWECYSCIKICPQGAITARPYADFAPMGGTCIPLRGSEDIMWTIKFRNGSVKRFKFPIRTTPEGSIKPFEGKPEAGDLENELLFTETALTVPQVALGQKAQIADAETSQCWFDLPCEGGNR
The following text describes a protein:
Function:
Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. The short isoform is a more potent inhibitor of TP53 activity than the long isoform.
Subcellular Localization:
Nucleus.
Domain:
Region I is sufficient for binding TP53 and inhibiting its G1 arrest and apoptosis functions. It also binds TP73. Region II contains most of a central acidic region and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc mediates the heterooligomerization with MDM2.
Sequence:
MTSHSTSAQCSASDSACRISSEQISQVRPKLQLLKILHAAGAQGEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGDLLGCQSFSVKDPSPLYDMLRKNLVTSASINTDAAQTLALAQDHTMDFPSQDRLKHGATEYSNPRKRTEEEDTHTLPTSRHKCRDSRADEDLIEHLSQDETSRLDLDFEEWDVAGLPWWFLGNLRNNCIPKSNGSTDLQTNQDIGTAIVSDTTDDLWFLNETVSEQLGVGIKVEAANSEQTSEVGKTSNKKTVEVGKDDDLEDSRSLSDDTDVELTSEDEWQCTECKKFNSPSKRYCFRCWALRKDWYSDCSKLTHSLSTSNITAIPEKKDNEGIDVPDCRRTISAPVVRPKDGYLKEEKPRFDPCNSVGFLDLAHSSESQEIISSAREQTDIFSEQKAETESMEDFQNVLKPCSLCEKRPRDGNIIHGKTSHLTTCFHCARRLKKSGASCPACKKEIQLVIKVFIA
The following text describes a protein:
Function:
Catalyzes the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (By similarity). Key transducer of G protein-coupled receptor signaling: activated by G(q)/G(11) G alpha proteins downstream of G protein-coupled receptors activation. In neutrophils, participates in a phospholipase C-activating N-formyl peptide-activated GPCR (G protein-coupled receptor) signaling pathway by promoting RASGRP4 activation by DAG, to promote neutrophil functional responses.
Subcellular Localization:
Cytoplasm. Membrane. Nucleus. Note=And particulate fractions.
Sequence:
MAGARPGVHALQLEPPTVVETLRRGSKFIKWDEEASSRNLVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDTRLEEKLMTVVAGPDPVNTTFLNFMAVQDDTVKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLNFNRSESIRPDEFPLEIFERFLNKLCLRPDIDKILLEIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRSSQARLLIEKYETNKQFLERDQMSMEGFSRYLGGEENGILPLEALDLSMDMTQPLSAYFINSSHNTYLTAGQLAGPSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAEAAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLSAGIPLPSPQDLMGRILVKNKKRHRPSTGVPDSSVRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKTSLEPQKSLGEESLSREPNVPMPDRDREDEEEDEEEEETTDPKKPTTDEGTASSEVNATEEMSTLVNYVEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDLPMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIVDGIVANALRVKVISGQFLSDKKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLIYTEASDYIPDDHQDYAEALINPIKHVSLMDQRAKQLAALIGESEAQASTETYQETPCQQPGSQLPSNPTPNPLDASPRWPPGPTTSSTSSSLSSPGQRDDLIASILSEVTPTPLEELRSHKAMVKLRSRQDRDLRELHKKHQRKAVALTRRLLDGLAQARAEGKCRPSPSALGKATNSEDVKEEEEAKQYREFQNRQVQSLLELREAQADVETKRKLEHLRQAHQRLKEVVLDTHTTQFKRLKELNEREKKELQKILDRKRNNSISEAKTREKHKKEVELTEINRRHITESVNSIRRLEEAQKQRHERLVAGQQQVLQQLEEEEPKLLAQLTQECQEQRERLPQEIRRCLLGETAEGLGDGPLVACASNGHAPGSGGHLSSADSESQEENTQL
The following text describes a protein:
Function:
Plays an essential role in heart function and development by regulating the organization and function of the sarcoplasmic reticulum in cardiomyocytes.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein. Note=Localizes to endoplasmic reticulum tubular network. In cardiomyocytes, localizes to the junctional sarcoplasmic reticulum membrane which is closely tethered to the cell membrane and contractile machinery.
Domain:
The short lumenal loops between transmembrane domains 1 and 2 and between transmembrane domains 3 and 4 may impart a wedge-like configuration, thus deforming membranes.
Sequence:
MSAAMRQRFDQFLHQKNCMTDLLAKTEAKTGVNRSFIALGVIGLLALYLVFGYGASLLCNLIGFGYPAYVSIKAIESPNKEDDTQWLTYWVVYGVFSIVEFFSDLFLSWFPFYYMLKCGFLLWCMAPSPANGADLLYKRIIRPFFLKHESQVDNVVNDLKDKAKETADTISKEARKAAVSLLGEEKKST
The following text describes a protein:
Function:
Involved in pre-mRNA splicing. May be involved in endoplasmic reticulum-associated protein degradation (ERAD) and required for growth at low and high temperatures (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSSLMEFQDRNTTNNETEHQKSITDQSSSVPAGVILPPPAIREIIDKSASYVARNGPAFEEKIRQNEQANTKFAFLHANDPYHPYYQHKLTEAREGKLKSHATGLSTQKTSTLARPIQKPIEATIPAPSPYLFSEPLPSISSLDLDVLRLTARYAAVRGSSFLVSLSQKEWNNTQFDFLKPNNALYPYFMRIVQQYTSLIREPISSPEQELRENVRDPYSLLSKIQPRVRWQSHMESQKKKQKEEAEKEKLEYAQIDWNDFVVVEVIQFTKSDEHAKLAKPTNLADLQTATLEQKSAMFTMPDQNYTIEEAPPTAEPWEPISAPKKQEFGVSLPPSLASPEKGGISSTTSVSPAAQASPVLSTTTQPKVQKPVPKAFQPKVPMEISPFSGELVPATELEEHMRLKLLDPRWQEQRKVEESRKSTLNLENVNVAANMKRLVSQRTDLFDVQNGVEISQEEIERRKRAATQSAWGATPTNKRR
The following text describes a protein:
Function:
Involved in the translocation of an unknown substrate across the membrane. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for virulence.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
In Rv1747 the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused. The two FHA domains are required for phosphorylation by PknF.
Sequence:
MPMSQPAAPPVLTVRYEGSERTFAAGHDVVVGRDLRADVRVAHPLISRAHLLLRFDQGRWVAIDNGSLNGLYLNNRRVPVVDIYDAQRVHIGNPDGPALDFEVGRHRGSAGRPPQTTSIRLPNLSAGAWPTDGPPQTGTLGSGQLQQLPPATTRIPAAPPSGPQPRYPTGGQQLWPPSGPQRAPQIYRPPTAAPPPAGARGGTEAGNLATSMMKILRPGRLTGELPPGAVRIGRANDNDIVIPEVLASRHHATLVPTPGGTEIRDNRSINGTFVNGARVDAALLHDGDVVTIGNIDLVFADGTLARREENLLETRVGGLDVRGVTWTIDGDKTLLDGISLTARPGMLTAVIGPSGAGKSTLARLVAGYTHPTDGTVTFEGHNVHAEYASLRSRIGMVPQDDVVHGQLTVKHALMYAAELRLPPDTTKDDRTQVVARVLEELEMSKHIDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDRQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLLAPGGKTAFCGPPTQIGPVMGTTNWADIFSTVADDPDAAKARYLARTGPTPPPPPVEQPAELGDPAHTSLFRQFSTIARRQLRLIVSDRGYFVFLALLPFIMGALSMSVPGDVGFGFPNPMGDAPNEPGQILVLLNVGAVFMGTALTIRDLIGERAIFRREQAVGLSTTAYLIAKVCVYTVLAVVQSAIVTVIVLVGKGGPTQGAVALSKPDLELFVDVAVTCVASAMLGLALSAIAKSNEQIMPLLVVAVMSQLVFSGGMIPVTGRVPLDQMSWVTPARWGFAASAATVDLIKLVPGPLTPKDSHWHHTASAWWFDMAMLVALSVIYVGFVRWKIRLKAC
The following text describes a protein:
Function:
Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.
Sequence:
MRVTKVVKRDGRVVEFDSFRIRRAIEMAMREVGKFDEAILDKVVKYVLDVIDSTFSDERPPHVEEIQDIVELALMKYDLFEVAKAYIVYRKEREKIRKEKMAILGKDYVDDVDKRLSLNAVRLLASRYLQKGPDGRFLEDPKGLFIRIASLVVIPDILYDPLIFDKEGEQEVHPTEYFNPEEWAGKVGLGGGDPENHLAPPFVWNAHHLERMKALYDELNSQGKMRVSWSQFFDMLRDGRFDHHYKDFLEYYRLMVDLKFIPNSPTLFNAGTMLGQLSACFVLPIEDSLESIMRSATEAAMIFKSGGGVGINYSKLRPQGDIVRSTGGQASGPVSFMRIIDVITDVVKQGGRRRGANMGILEIWHPDIMKFIEAKAKPGNLENFNLSVMITEDFWKYYEEGKDYPLINPRNGEVWGSIDPREAFRKIAEMAWRTGDPGVLFADNINRRNILREHLGEIKSTNPCGEEPLYPYESCNLGSMNLYAYIRRENGLVTFDWDEYSRDIRKALRFLDNIIDVNKFPIPEIEKTTKRTRKVGLGLMGLADTLFALRIPYNSEEGFNFMRRAAEYLTYFAMLESVERAKERGSFPLFPESGYVRGEMPVEGFYHPEIWNLDWDYLREQIMRNGIRNAEVTTIAPTGSISMIAEVSSGIEPQFALVFEKRVTVGSFFYVDAEFERQLKENGLYSEKILRDIAENGGSLYGIEAPEGKEDVIERMKRIFLVAYDIPWWDHIRAEAEISRWICAAVSKTINMPNWVSVSDIEKAYLFAHRLGLKGITVYRDGSKSAQVLITPTQRRGEYASFIENETLKMMESLGIELPQLRKAKVEEKTQAQPVFKPPAQPNHVETCPECGSTRLIHKEDCVTCLDCGWSACVVT
The following text describes a protein:
Function:
Cleaves internal linkages in 1,3-beta-glucan.
Miscellaneous:
MISCELLANEOUS: Present with 1420 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MCYSRQAIPPPVPNRPGGTTNRGPPPLPPRANVQPPVCSSENSSKPRENRVAGESLRTPSSSNPLADSQVNSDNIFQSPVLSNLKAPPSVFNKVQHPVPKPNIDDQSVDPLETNKFYTNMLLDDNTQPIWTHPYSIWFSRDPELFGLAANHTLASQRVFDTTTNPPRFYFNPTNIKSFVFKAREFVSSNDIKLEFRDMKHMSMCLLMSLSSSQFIEFPLVQGMGFVTAIYHDLGFELRSAVGFRSLERISVNERYGKYNIQLENNRNWILYLTSPDYSFPQDFQISLLDSNTIISSHKINGLICQLSADSVPSIDMAAGCYPVYCDLSGQTVDEHFTNYRFNYTVAGYSQSGTTLMYALPHHKAAFTPEMQEREIASSLDSTVKGLMTGYLTNSFDMQVQVPQELGFEPVALSLNKKADYSQEKLSKIREAAVQEVQLSDPQQESNIDSMYFSGKILAKYAWILYVTHYILHDENLTKELLSKLTIAMERFISNQQVLPLNYDVSWKGIISSGSSSQDFGNSYYNDHHFHYSYHVITAAIISLVDSDLSGVTNNSWLENNRDWVECLIRDYSGVDNDDPYFPQFRSFDWFNGHSWAKGLFPSGDGKDEESTSEDVNSCYAIKLWGLVTGNSKLTDIANLQLGIMRNVFQSYFLYESNNTVQPKEFIGNKVSGILFENKIDHATYFGMEPQYIHMIHAIPITSASSWVRTPNFVKEEWEEKMQPIIDQVNDGWKGIIMLNMALLDPKFSYDFFSQPDFNRNFLDNGQSLTWSLAYSGAFS
The following text describes a protein:
Function:
Participates in transcription elongation, termination and antitermination.
Sequence:
MSEEKAKWYVVHTYSGYENKVKVNLQKTVDNRNLHHWIFDIQVPMEEQVEVKDGKKKITLKKTFPGYVLVKMLMTDDSWYIVRNTRGVTGFVGPGSKPVPLTEEEVLSMGIKEKQPEVDVEVGENVKVVSGPLEGFPATIQEINVEKGKIKALVNMFGRETPVELDFNQIEKLD