lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA.
Miscellaneous:
MISCELLANEOUS: In the RecBCD complex, RecB has a slow 3'-5' helicase, an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-3' helicase activity, while RecC stimulates the ATPase and processivity of the RecB helicase and contributes to recognition of the Chi site.
Domain:
The N-terminal DNA-binding domain is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function. This domain interacts with RecC; The C-terminal domain has nuclease activity and interacts with RecD. It interacts with RecA, facilitating its loading onto ssDNA.
Sequence:
MAETIPLNPITLPLNQISLIEASAGTGKTYTIGSLYLRLLLKAGENNFSRPLNVEEILVVTFTEMATEELKKKIRERITDAINKLTAFAKTQDKSAFKNDEFLTALCDNLNIFEAIHRLKLAEQNMDLAAIYTIHGFCRRMLMQYAFHSGIHFNLELIKDQSDLLVRFANEFWREHFYPLDFESANFIATELVSPANVLSLLKADLGKDLQVEIENKQALSVPIQIFLPQYLGGYQKALNELKAFWLESADEISAIITNELVKDYPKDQLKSLNRKKYQVKRLGDWINKINQWSNNPRDYQINTTLKDYFLQSSIEKNCEESTDKNKDKKPATPFYSPIFADLEKRVNALMTPDLLSKLTLYHYRQGLQQKLLDYKLNHQEKSFDDLLRLLCEALQDAQGDELAEMIRFQYPFAMIDEFQDTDSQQYAIFSKIYRDNPEKNTGFIMIGDPKQAIYRFRGADIFTYLKASDEAQSRFELTKNYRSEKHLVDGVNALFDFPQSPFIYQNIKFTAVDSRDDHLRFYLNGKVEPAYRFYLTESDKVNKTEMAKICAISIQHWLKSAAENQAVFQNEDTYKTLQAANIAVLVRDKNEAALVKNELQKLGIASVYLSDQNSVFDSNVAKELAWVLKACLNVAERPILNAIATALFGLNAADIHQIQQNEADWQRWADSFAQYQQTWQRQGILAMLHQILLEQGISERLLSQATGERDLTDFLHLAEILQQAATLHESEAALLSWFEKQIQGEARQEAQIRLESERQLVKIVTIHKSKGLEYDLVWLPFLAAPSKDPSKKYINIYYSKERDETLWDIENRNLNALCEETFAEELRLLYVALTRAKYQMAFALPAQFDKKWNALHYVLSQGEIGKEINLSDSKDTETLLQTFKEKMQDNVEICTKPNLEALPTLSINTKNDDFKASEFTGNIEQDWRITSFTSIEQAHRRQNYFTESAGKKHAVFDDAKDYDSQNAIEISTALLNENESNILDLPRGKQVGTALHRHFENCYFSDLANTEEIDKLRQSLQLDETFTESLQNWLQQISHTPLSNEIGIALADLANKDCIKEMPFYLAIREHFDVEAFNHTLKAHHHLPSESLQFEQIQGMVRGSIDLVFRHNGKYYLVDYKSNFLGSTLADYNQEALKKEMLHSHYDWQYLIYTLALHRYLQSVVPHYDYARDFGGVFYLFLRGMNGEPQSGVFYDRPSVELITELDGVF
The following text describes a protein:
Function:
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Subcellular Localization:
Cytoplasm.
Sequence:
MNESSEANDLAIRRQIIDETKCVVVKVGTRVLTTSDGKLDLERVDRLAEQLCRIADTGRQTIMVSSGAVGAGVAKLGLPQRPTDLKSLQAIAAIGQADLIGAYEKSLQKRGRHAAQVLLTRNDLRRRSGYLHVRNALNGIDELGAIAVVNENDSVAVSELKTTFGDNDRLAAQVAGLFNDVMLILLTDVSALYDGHPDEKDSQPIHMVHDVDDGVMALVDDQVSTVSKGGMGGKLRASKLANSHGHPTIIGSGTEEFVLDRIFAGDAVGTLFVPPKRSLKGRRRWIGSSANVAGTLFLDQGAVDAIQKHGRSLLAIGIQRVEGTFAHGNVVRLVGPNGEEFGRGLSNYRSHEVARIAGKPSEQIEWILGHRPYENVIHRNNLVLRIVPE
The following text describes a protein:
Function:
Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
Sequence:
MANAAFNTMNAIKKKVHTMKTLKDSAGDEVELLEQKLLEYKAIGEKNEEELMNLNKRIFQIQNDQGITQQQLSDALEKYNTINKNLSQAEAEMLNLSKRVRSIEEEYETVENKLIQTTTKWEQASKAFEESQRGIKVLEARIYTDEERIAQIETELEVIILFGEDADRKYEETARKLAITEVDLSRSESRVQIAEARGMELEEEYKVVSNNMKSLEIFQIEAQARFENYEMIVTSLTHQLQETESRAASAERMVTFLQKEIDKIEDELAAEKDKFRLVANELDFTFTELTAF
The following text describes a protein:
Function:
Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MVLVSKGDFIWIEPGKAEGSIPIGARVIDQDHGRLKVIDDLGNEQWLSADRRVRLMHPTSVQGVEDMCQLGDFHESAILRNLFIRYREKLIYAYTGSILIAVNPYMDIAIYTADEIRMYKRKRIGELPPHIFAIADNAYTNMRREKKNQSVIISGESGAGKTESTKLVLQFLATISGQHSWIEQQVLEANPVLEAFGNAKTIRNDNSSRFGKYIDVHFNESGSIEGAKIEQYLLEKSRIVTQSENERNYHIFYCLLAGLSKEEKMELELGTAADYYYLIQGKTLTAEGRDDAADLAEIRSAMRVLMINEQEIGSIFKLLAALLHIGNIRFRQNTTDNMESVDVADPSTLVRIAKLLNLHEQNLLDAITTKSLVTREERVISRLNGQQAIDARDALAKAIYGKLFIHIVRRVNDAIYKPSQSIRTSIGILDIFGFENFESNSFEQLCINFANETLQQFFVQHVFKMEQKEYDEENINWRHIKFVDNQATVDLIAQRPMNILSLIDEESIFPKGTDKTMLLKLHSTHGRNELYLQPKSELQRAFGVTHFAGSVFYNTRGFLEKNRDSFSGDLSALISSSKMPFLARLFDDLEYDTSSRKKVTVGNQFRRSLEQLMTQLTQTHPFFIRCIKPNELKRALVMDRDLVLRQLRYSGMMETIKIRRSGYPIRHDYYPFVFRYRVLVSSIRGPANRIDLHDAAKKICHKVLGPNADYQLGKTKVFLKDKHDLVLEQEYYRILKDKAVIIQKNVRRWLVRKDFEKQRQAAVTIQTAWRGYDQRKRYRQIISGFSRLQAVLRSRQLVSHYQSLRKTIIQFQAVCRGTLLRRQVGEMRRRGEKAPLTEVSSTASVISDSHEEELVSHLFDFLPSDGKDSGNENDSTDSSRRGSYSRLHPSPVMPPTNIPRVDSFIDEDLSKFQFGKYAATFFQAQATATHIKKPIKTALLTHTEPSAQLAALASWTTILRFMGDLSDVKPGSTNGSEIYDKTPVMSRLYATLGKKFSTRDVEEALLSSEYGGNKTLKKGMGKKLISMTLKRKGKIGGSDTSSISSDSAYSGFNAMLENKPMTSLDKLHYIIGLGILREDLRDEIYCQLCKQLSNNPSKLSAARGWILLSLCVGCFAPSERFIKYLFCFIRERGPAGTGYSTYIEDRLRRTQVNGTRHQPPSYVELQANKSQKPVVLAVTFMDGSVKTLCADSATTASELCKQLAEKVGLTNSFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEQGRQERNAPWRLFFRKEIFSPWHDPKDDAVSTNLIYQQVIRGIKYGEYRCDKDEELAAICAQQYYIDEGTMDVNKLENNLASYLPDFEMAGKDMALEKWTQTIMHQYRKKFTGRLPSQIEVKEDVVSIAKTKWPLLFSRFYEALKFAGPPLPKNEVIIAVNWTGVYVVDDREHVMLEFSFPEISTAYYGKGKRSTTDTCTIRSVVGDEYTFQSPNADDITNLIVLFLEGLKKRSRYLVAIKAQKGDEKNNFLDFEKGDLLILVNEFTGNTLLTESVVKGENSRTCLFGLIRAENVYVLPTLVKPSKNTLQIFPKDMDMSLDLFNNNKQVTVIDYNAEPYTLENFAEDNFNSQVKRVGSQISLMTLRKKESQIESWRFSRDHIEHPLLKKLNGRDDACRGAVEIFAAIMKYMGDEPSKRSRLGTHLTDHIFKLPISMEALRDELYCQLVKQLTLNPSIMSEEKGWELLWMATGLFAPSAALAKEISHFLKSRPHPIALDCQNRMQKLAKGGSRKYPPHLVEVEAIQHKTTQIFHKVFFPDKTDEAIEVDSATRARDFCHKIGYRLGLKSSDGFSLFVKIKDKVLAVPETEFFFDYVRSLSDWVHTNHAMQKDSTMIPINYQVYFMRKLWFNFVPGADSQADIIFHYHQESQKYLLGYHKTTKNDVIELAALILRAMTKEGKNAPLAQIPQLLDDIVPKDSLKMCSASEWRKTISNAYARVEHLKPDQAKIEFLKYICRWPTFGSAFFPVSQYSDLSLPDRLLLAINQTGVNIYHLESKNLLVQYPFNVICNWTSGNTYFNMTVGNMLKGNEGKKLLLDTTVGYKMDDLLTSYISLLISNQTNQPSKHREVAL
The following text describes a protein:
Function:
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Sequence:
MNAVVVLNKPKGFTSQDTVTKVKKILKVKKAGHAGTLDPMATGILIVCINEATKITPFLMELEKEYVFKAKFGISTDTYDAEGKIVRVVEDFKLEREQVESILEEFTGEIMQIPPMYSAVKVGGKPLHELARKGVEIERKPKKVIIHSIKIESFEPPFVTFRVVCSKGTYVRSLCHDIGEKLRIGAHIVELTRTRIGEFRVEESIELEELKSLISNNLDSSAFSFQPKKGIFSIDQALYFLPSVTMQDYIIPRFLNGNPVKIPSGIVPAGWVKVKDTRGKILGIGYGNGVIIKPERIIWEEV
The following text describes a protein:
Function:
Probably part of an ABC transporter complex. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLFAALRDMQWRKRRLVITIISTGLIFGMTLVLTGLANGFRVEARHTVDSMGVDVFVVRSGAAGPFLGSIPFPDVDLARVAAEPGVMAAAPLGSVGTIMKEGTSTRNVTVFGAPEHGPGMPRVSEGRSPSKPDEVAASSTMGRHLGDTVEVGARRLRVVGIVPNSTALAKIPNVFLTTEGLQKLAYNGQPNITSIGIIGMPRQLPEGYQTFDRVGAVNDLVRPLKVAVNSISIVAVLLWIVAVLIVGSVVYLSALERLRDFAVFKAIGTPTRSIMAGLALQALVIALLAAVVGVVLAQVLAPLFPMIVAVPVGAYLALPVAAIVIGLFASVAGLKRVVTVDPAQAFGGP
The following text describes a protein:
Function:
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis, transfering GlcNAc-1-P from cytosolic UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol embedded in the cytoplasmic leaflet of the endoplasmic reticulum membrane.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MYSSIWTVLAILALSASLIFNPADQPLLSSVGFSLIAYLVTYNLIPALGPAFIKVGFSGRDLSKKDRPEIPETMGAVCAIVYLFCMFLFIPFVFYQYLAKTIGGGVVVGYDSLSEGLVKGRILSAFPHEKLAEYLSAILCLQSMFILGVADDLFDIRWRNKFFLPAIAAIPLLIVYYVDFGITAVMVPVVLRPYFGDIVDLGALYYMYMAAVAIFCPNSINIYAGVNGLEVGQSVMIGVCILLNDFIYLVQPNHPAEESHLFSVYLLLPFLAVSIALLRHNWCPAKCFVGDTYCYFAGMVFAVVGILGHFSKTLLLFFVPQIFNFLYSVPQLFKIVDCPRHRLPKFNPETGLLEPSRTYFDKKKPGKLGQIMIYVLEKLHLLKVWRDEKGVVISISNMTLINLVLVYVGPLREDHLAAVLLGIQFASGLAAIALRHSVAAMIFGRDNI
The following text describes a protein:
Function:
Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery, forms H3K4me1, H3K4me2 and H3K4me3 methylation marks at active chromatin sites where transcription and DNA repair take place (By similarity). Responsible for H3K4me3 enriched promoters and transcriptional programming of inner mass stem cells and neuron progenitors during embryogenesis. Required for H3K4me1 mark at stalled replication forks. Mediates FANCD2-dependent nucleosome remodeling and RAD51 nucleofilaments stabilization at reversed forks, protecting them from nucleolytic degradation. Does not methylate 'Lys-4' of histone H3 if the neighboring 'Lys-9' residue is already methylated (By similarity). Has RNA binding activity towards transcripts involved in RNA processing and the DNA damage response (By similarity).
Subcellular Localization:
Nucleus. Nucleus speckle. Chromosome. Cytoplasm. Note=Localizes to a largely non-overlapping set of euchromatic nuclear speckles with SETD1B, suggesting that SETD1A and SETD1B each bind to a unique set of target genes (By similarity). Predominantly nuclear (By similarity).
Sequence:
MDQEGGGDGQKAPSFQWRNYKLIVDPALDPALRRPSQKVYRYDGVHFSVSDSKYTPVEDLQDPRCHVRSKARDFSLPVPKFKLDEFYIGQIPLKEVTFARLNDNVRETFLKDMCRKYGEVEEVEILLHPRTRKHLGLARVLFTSTRGAKETVKNLHLTSVMGNIIHAQLDIKGQQRMKYYELIVNGSYTPQTVPTGGKALSEKFQGSGAAAETTEARRRSSSDTAAYPAGTTVGGTPGNGTPCSQDTNFSSSRQDTPSSFGQFTPQSSQGTPYTSRGSTPYSQDSAYSSSTTSTSFKPRRSENSYQDSFSRRHFSTSSAPATTATATSATAAATAASSSSSSSSSSSSSSSSSSSASQFRGSDSSYPAYYESWNRYQRHTSYPPRRATREDPSGASFAENTAERFPPSYTSYLAPEPNRSTDQDYRPPASEAPPPEPPEPGGGGGGSGGGGGGGGGGGGGAPSPEREEARTPPRPASPARSGSPAPETTNESVPFAQHSSLDSRIEMLLKEQRSKFSFLASDTEEEEENSSAGPGARDAGAEVPSGAGHGPCTPPPAPANFEDVAPTGSGEPGAARESPKANGQNQASPCSSGEDMEISDDDRGGSPPPAPTPPQQPPPPPPPPPPPPPPYLASLPLGYPPHQPAYLLPPRPDGPPPPEYPPPPPPPPPHIYDFVNSLELMDRLGAQWGGMPMSFQMQTQMLTRLHQLRQGKGLTAASAGPPGGAFGEAFLPFPPPQEAAYGLPYALYTQGQEGRGSYSREAYHLPLPMAAEPLPSSSVSGEEARLPHREEAEIAESKVLPSAGTVGRVLATLVQEMKSIMQRDLNRKMVENVAFGAFDQWWESKEEKAKPFQNAAKQQAKEEDKEKMKLKEPGMLSLVDWAKSGGITGIEAFAFGSGLRGALRLPSFKVKRKEPSEISEASEEKRPRPSTPAEEDEDDPEREKEAGEPGRPGTKPPKRDEERGKTQGKHRKSFTLDSEGEEASQESSSEKDEDDDDEDEEDEEQEEAVDATKKEAEASDGEDEDSDSSSQCSLYADSDGENGSTSDSESGSSSSSSSSSSSSSSSSSSESSSEEEEQSAVIPSASPPREVPEPLPAPDEKPETDGLVDSPVMPLSEKETLPTQPAGPAEEPPPSVPQPPAEPPAGPPDAAPRLDERPSSPIPLLPPPKKRRKTVSFSAAEEAPVPEPSTAAPLQAKSSGPVSRKVPRVVERTIRNLPLDHASLVKSWPEEVARGGRNRAGGRVRSTEEEEATESGTEVDLAVLADLALTPARRGLATLPTGDDSEATETSDEAERPSPLLSHILLEHNYALAIKPPPTTPAPRPLEPAPALAALFSSPADEVLEAPEVVVAEAEEPKQQLQQQHPEQEGEEEEEDEEEESESSESSSSSSSDEEGAIRRRSLRSHTRRRRPPLPPPPPPPPSFEPRSEFEQMTILYDIWNSGLDLEDMSYLRLTYERLLQQTSGADWLNDTHWVQHTITNLSTPKRKRRPQDGPREHQTGSARSEGYYPISKKEKDKYLDVCPVSARQLEGGDTQGTNRVLSERRSEQRRLLSAIGTSAIMDSDLLKLNQLKFRKKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQMVADMREKRYVQEGIGSSYLFRVDHDTIIDATKCGNLARFINHCCTPNCYAKVITIESQKKIVIYSKQPIGVDEEITYDYKFPLEDNKIPCLCGTESCRGSLN
The following text describes a protein:
Function:
NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers.
Sequence:
MRFHSPAIQYFHAVRRTGSIRAAARVLNVASSAVSRQILKLEQEVGSPLFERTARGLTLTTVGEMLARHVMNVLQDLDRFRSDVASLSGNWRGTVSIACIESLTESVLPDLIASHRGRARRVSFTTEVKGSSDVLEALSRGEADIGIAMALRHPPDLRQVALKRFRLGAVVSREHPLARRKTVTLEQCLAFPVINALPELSIYHLLQPLIAQLSETPEPAIQANSIDLMRELAARGVGVAFQTQLGIGRLSRESQLVFLPLDNAGSPVWSDLGIYVRAERTLPAYTESFLQELVRELGERERRENAAYPQTA
The following text describes a protein:
Function:
May play a role in chromatin regulation of male germ cells.
Subcellular Localization:
Nucleus. Note=Present in nuclei of spermatids during chromatin condensation.
Sequence:
MVPLGYNNKYFGYVQDCQQQATDNSPIHYYTGDKQNQSYSQSMCKEQSQNTVTVSPASFNKKAQSTQGSYNRAMKSSSSLYSTCSTTPSKDSLLKNSSYPSWKSLDSSLSHHKSETTSLTSFTSTSSLEPSKISSRSRLLLPKTQTSSSIDLCWKSPSLESNQRVSTSSSTSVQHHEAPSLNIIWTTPSLESNQSEHDSQLCKSKSQKDSSLDRLWSSLLESSQKALSSPSFTNRLQRNSFPPTSSSLEFSRVARNSPLPDCSKPLKIPVSNSNNNVFSLPLSPAKSRKSTPSPHSFLPSRRLSTCQPKPKIVARCDPSTRAINTAVCHPKVQNTASLSDKQRPRQLPSIHPKPNPSGQRVSSPKPCIKNKIASVPCSRLPNKSSVERSVKTEPENEISWALDYSHPCIIKGGSVPVDVVNKIINSISKSTIQKDLSRQILFRRMRGKPNPRPGPRLSSTYSVCLECASAIKSQCNHLSGKRDPRCATLFVIPTPESSTDGKVDVKIILILSLPEKPSSTCFQLPMKDSKSENNLEALDDNLDVLEKITQFFPASESDFIQGLKTKRKCLAVSSESKDLSQEPQSIDWLLYVKNSNGIQLETQVQGPSSSSSSSCSSVSSSSSASSIGRPSPPTPWVDPTPVPVSGYVLAKVRSYHRLPPGTSWLEFIRGSSSDTIKLRQSPPVKAKPVRSHNSKCLKKGKRETSALLRYFQTKFQNEKS
The following text describes a protein:
Function:
Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific mRNA endoribonuclease that inhibits translation elongation and induces bacterial stasis. Cleavage occurs between the second and third residue of the Lys codon followed by a G or A (5'AAA(G/A)3'), is reading-frame dependent and occurs within the 5' end of most mRNAs. Ribosome-binding confers the sequence specificity and reading frame-dependence. When overexpressed in liquid media YafQ partially inhibits protein synthesis, with a reduction in growth rate and colony growth rate. This effect is counteracted by coexpression with cognate antitoxin DinJ. YafQ and DinJ together bind their own promoter, and repress its expression; Cell death governed by the MazE-MazF and DinJ-YafQ TA systems seems to play a role in biofilm formation.
Sequence:
MIQRDIEYSGQYSKDVKLAQKRHKDMNKLKYLMTLLINNTLPLPAVYKDHPLQGSWKGYRDAHVEPDWILIYKLTDKLLRFERTGTHAALFG
The following text describes a protein:
Function:
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
Sequence:
MLCGSRSSESVMAVQSLYRKWRSQTFAELVGQEHVVQTLRNAIAEDRVGHAYLFTGPRGVGKTTMARLLAKAVNCLNPDPTARPCGVCEMCAAIAEGRAVDVIEMDAASHTSVEDAREIIERVQFRPAEARMKVYIIDETHMLSTAAFNALLKTLEEPPDHALFILATTEVHKVPATILSRCQRFTFVRHSVSAMAAHLRRIAAAEGIVLADGVPEAIARAATGSMRDALGILEQLASFVEGPITLPQVQSLLGMTAAAEVDALITALVNHDLTAALRAVHGVANQGADVRQFTRDLVERLRAVMVLKATGDRTLLDLSDDEVALLGQWVQQADMAALVHWVKLFSNLDAQLRTTPYGQLPLEVAVVEALLVPPPVAQPASSSASRSASLAGRTPTSRPSAAVPAIVPQTEPVRAPAHPEPVPPSVVAPPPPPVPEPVSASGSEVPSDVTPVSDPPPPPPEAWAATRQMRPPADPAVARAADADMSVLEQLEAIWEDFKRDVRPRSPTVQALLNSARPYDVEGNTIVLLVTSSFHKERLEEPKNRSLLEDLLRRRLGKTYAVRCTIEEKSVEPTDLRGKIREARKDELVRAALNIFDAHIVDIEPLDPE
The following text describes a protein:
Function:
Calcium-binding protein. May play a role in cellular signaling events.
Subcellular Localization:
Cytoplasm.
Sequence:
MDAVDATMEKLRAQCLSRGASGIQGLARFFRQLDRDGSRSLDADEFRQGLAKLGLVLDQAEAEGVCRKWDRNGSGTLDLEEFLRALRPPMSQAREAVIAAAFAKLDRSGDGVVTVDDLRGVYSGRAHPKVRSGEWTEDEVLRRFLDNFDSSEKDGQVTLAEFQDYYSGVSASMNTDEEFVAMMTSAWQL
The following text describes a protein:
Function:
Activates insulin and somatostatin gene transcription. Key regulator of islet peptide hormone expression but also responsible for the development of the pancreas, most probably by determining maturation and differentiation of common pancreatic precursor cells in the developing gut. As part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells is involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element. Binds the DNA sequence 5'-CC[CT]TAATGGG-3'.
Subcellular Localization:
Nucleus.
Sequence:
MGFMDKIYLTPKDMCILSTLLRCQPKITRGSKSTVSLQHLLESPTFAQSSFLRFTKTPRKCGSAVGFPRSPVNSRILLSVAHPWRAQSSLKINTPPLLLRXKIMGAXKNEMXGXTARGLPEAGGGGARRLRTAYTNTQLLELEKEFHFNKYLCRPRRVEIAALLDLTERQVKVWFQNRRMKHKRQTQHREPPDGEPACPGALEDTGDPVKEPAVSPGGPSASRAAWEACSHPPEVVPGALIAADPRPLSGGLKGAGAPSLAATARGGRAGPGHCQKCLPGAPDSLPSDLTSSRATPVSAIRRPLP
The following text describes a protein:
Function:
Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNSFFGTPAASWCLLESDVSSAPDKEAGRERRALSVQQRGGPAWSGSLEWSRQSAGDRRRLGLSRQTAKSSWSRSRDRTCCCRRAWWILVPAADRARRERFIMNEKWDTNSSENWHPIWNVNDTKHHLYSDINITYVNYYLHQPQVAAIFIISYFLIFFLCMMGNTVVCFIVMRNKHMHTVTNLFILNLAISDLLVGIFCMPITLLDNIIAGWPFGNTMCKISGLVQGISVAASVFTLVAIAVDRFQCVVYPFKPKLTIKTAFVIIMIIWVLAITIMSPSAVMLHVQEEKYYRVRLNSQNKTSPVYWCREDWPNQEMRKIYTTVLFANIYLAPLSLIVIMYGRIGISLFRAAVPHTGRKNQEQWHVVSRKKQKIIKMLLIVALLFILSWLPLWTLMMLSDYADLSPNELQIINIYIYPFAHWLAFGNSSVNPIIYGFFNENFRRGFQEAFQLQLCQKRAKPMEAYALKAKSHVLINTSNQLVQESTFQNPHGETLLYRKSAEKPQQELVMEELKETTNSSEI
The following text describes a protein:
Function:
Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.
Sequence:
MVSFKDIQEAHVRVSPYTHYTPVLTNQAIDQLATESLFGPATSASPSPRPRIRLAFKAEHLQRVGAFKYRGATNSVLVHLGAAKAQHDASASKSTKFSPGKLVVVTHSSGNHAAALACAAKSAGCVAAVVMPNNAPKPKKEAVAGYGARITFCEPTLEARESTAEAVMQDYEKQGYIVRFVHPYDEPLVIAGQGTMALELLDQAAQLEEWATCSHAADRIPSNARPLHGTRNVAPSGPKAESVWRKRDMSEAALDIIIAPVGGGGMLSGVATAIKGADDRIVVIGAEPDLVDDAFHSYQTGSVQQPPQPPKTICDGLLTSLSPLTLEHIRNHVDGIVTAREENVLKALQLHWTRQKQFVEPSAAVGLATVLQGFNQAAEQAGGALTDSTNRSLWGLRDWVHHLADQKRQKGETQPEIRIGIIWSGGNMEVGKVVAKFEEYGL
The following text describes a protein:
Function:
Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Recruited to DNA lesions in order to initiate the DNA repair by homologous recombination. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, also involved in the regulation of DNA damage response mechanism. Required for cell growth and meiotic recombination (By similarity).
Subcellular Localization:
Nucleus. Note=Localizes to nuclear DNA repair foci in response to DNA double strand breaks.
Sequence:
MDGQTRYLDELVGALRAERAQGRAGGYAGEFPPREGGGRARRVARTVVAKLADAEVADAAFWRACEALDLVFTGRPMVLAEALDEEAGVLWAVRSCWRVAAVHFGRRERGWALRRASSRWVRLCADLYGQRWRARVGAELDRELCAGEAAVRAVLGGGQEAGEHMRALRALCVAAEWAVSREFWFVTGGAERVGLRLQRLARLARYIGDAVELPLAEYEEVQVRLLGVSVQAYLEPDRPGLGELRFALEQLQYFVRGKHLRREFAAWSRLLLRLYVRCRSDRAALLLVREVLVLDAAELPEAATDAQRSLQLVRYDLERQFAADHALRWDPALRAKLLAAGTPPVILEPFTSNRQLEKLRLRVLCDFQVGDSALLVHQFSAAGVPLGADPVALYTHLDEGIARAFGRQDTEAQVRYLSLVRKLACLESRKPSPGFDCDLCDHTNLWLPRESIDPSRPEAASDSLAFKLLVGYYLREQLESSGEALVIGILITLRSIFTHFQPPKLVENHYGDMVDEHGCIQLFRMAFMSLNRHVRILSVLLIPYWNLSRSYNADEQQTALIIKFLQRNPDPHITETYLMAWTQLTLSTSGELFDSLLLKLIDIFNSSNFVEHVVMASQLKFIARVLNKTAYQLLSPILPILLKQIGKNLGEKKLSLERLLNLLEYSAKTVIENFQRYIVPYALTQYKGDALTEIAKIMCQNNEPSMVSEQKKRLLDRNSRQIFAVALVKHGLFSLETIETLFINNDPTFDRSYVAGFLPDYKTLAEVLKLFKPVEKVDSPMNDNERAVLSSLRFLFLTNFSVDKHRGSKFKNVTEWTQEKEAVFQKKLKDNILGIFQVFSSDMHDIEGKTTYFEKLRVISGISFLIKYASKECIISALAQVSICLQTGLEIPEMRYNTLRCWLHLVKYLSEEELSTVIDVLICFILQKWDEFSGKIQQAAIDILDALILEKQTLLTNSRPYIVLAFLNKSELHIFENHGFFARTASKLLKNTNWVSVFVSNLKSHNIYVIKQTLQDIRLFLEKKQDAGIDIKLISKDGKNISELLGALLDTSHKYRNSDLIICETCALCISMIGVLDVTKHELQRCNVYDNDICDFNNPTQTTKFLINIINERLVPSFWQSENPTKQLFVALVIQESLKYCGLSASSWDVTKPDLYPNESKLWNRFNDISKTTLYPLLSSLYLAQSWKEYVPLSYPSFKVKDGYSTWIKNLSLDLLKTATESSHPLHVFSSLIREDDGTLSDYLLPYIIMDIIIKAESGTKYFDYLQNVIKDFEYIFNYTLYDLNHYQIDGLKMCYDSIFRVFEYCKKWVNQFRQNYSKQHGTFTIREEKYTRMLNRAGKFADIIPSHVLAQKSLETNSFERSALYLEQSYREKSSNGLQDDKLLPYLQTTYAEINDIDAVVGVLKVFCSNNLTSRIEELQYSDNWKMAQDCFDALGDSLLNEQGGVENSVPTSRMLKLMYDHQLYDQTLKKLELNIPSKKRQLPLNLDEFYNMGIETASLSGNITELKIWIRRIEQLETLTDPSILLHYNLAKSLLAVLEGKTDMIETHSKYCYRLIGSHFTTPSHSTTLLKRRNLFIKLHGIRDNSILSKCSTDIQFNRSVRNLAVRFKNVGSDFEPNFYLLSMRKSHNLMRSEEFVKQDLADTYFKMAQLARENDRLDIASDCLMHALKLEHTEAELEYAEILWKQGEKELALKTVAEIHQKRKGIKTLKDRDRAKVLLKYTEWLDLSNNATSVQISHQYKEVIGLDKDWDEPYYSFGLYYSRLLEKKRADGFVTTGSLEYKAITYFLSAFEKNTVKVREALPKVITFWLDTASRSVESGSSEGEYHFKRYTKEICKCIDVAIQNCPTHIWYTVLTQLLSRLLHKHTDSATLIMNILLKLTLEYPSIMLWYITVLLNSQENKRVHAGKQIMDAIKKRMPDKSSLISSAISLVQAMTRVCIKDVKNMSSRSGKSLQNDFKFDINLAPSEMVVPVNINLANLSPSYADTSGKHGSSKRVTINCFTPHYKVYSSLKKPKKINIIGSDGELYGIMCKKEDVRQDNQYMQFANMMVFLLGKDSESRRRSLNITTYAILSLREDCGLIEIVPNVDTIRSILMAKYDSMKIKYTLSVLYEKWKSVSEEQRLGFYKSCTDTFPPVLYQWFLETFPNPIRWYNARNAFVRSYAVMAMVGHILGLGDRHLENILLDLQTGKVLHVDFDCLFEKGKTLPVPEIVPFRLTQNIQDAFGVTGTEGTFKKSSEVTVRVMRNNELALVNIIETIMYDRNMDHSIQNALRVLRNKVRGIDPRDDLPLSVPGQVDTVVQQASSDENLAQMYIGWLPFW
The following text describes a protein:
Function:
NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Activates SHMT2 by mediating its desuccinylation. Modulates ketogenesis through the desuccinylation and activation of HMGCS2. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX.
Subcellular Localization:
Mitochondrion. Cytoplasm, cytosol. Nucleus. Note=Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus.
Domain:
In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-102 and Arg-105) that bind to malonylated and succinylated substrates and define the specificity.
Sequence:
MRPLPVAPGRLFSQLCCGPKPSASPQSKICLTMARPSSNMADFRKCFANAKHIVIISGAGVSAESGVPTFRGTGGYWRKWQAQHLATPLAFAHNPSQVWEFYHYRREVMRNKEPNPGHLAIAQCEARLRDQGRRVVVITQNIDELHRKAGTKNLLEIHGTLFKTRCTSCGNVAENYKSPICPALLGKGAPEPDTQESRIPVHKLPRCEEAGCGGLLRPHVVWFGENLDPAILKEVDRELARCDLCLVVGTSSVVYPAAMFAPQVASRGVPVAEFNMETTPATNRFRFHFPGPCGVTLPEALAPHETERIS