lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG (By similarity). Overexpression reduces biofilm formation. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLSLYEKIKIRLIILFLLAALSFIGLFFIINYQLVSERAVKRADSRFELIQKNVGYFFKDIERSALTLKDSLYLLKNTEEIQRAVILKMEMMPFLDSVGLVLDDNKYYLFSRRANDKIVVYHQEQVNGPLVDESGRVIFADFNPSKRPWSVASDDSNNSWNPAYNCFDRPGKKCISFTLHINGKDHDLLAVDKIHVDLNWRYLNEYLDQISANDEVLFLKQGHEIIAKNQLAREKLIIYNSEGNYNIIDSVDTEYIEKTSAVPNNALFEIYFYYPGGNLLNASDKLFYLPFAFIIIVLLVVYLMTTRVFRRQFSEMTELVNTLAFLPDSTDQIEALKIREGDAKEIISIKNSIAEMKDAEIERSNKLLSLISYDQESGFIKNMAIIESNNNQYLAVGIIKLCGLEAVEAVFGVDERNKIVRKLCQRIAEKYAQCCDIVTFNADLYLLLCRENVQTFTRKIAMVNDFDSSFGYRNLRIHKSAICEPLQGENAWSYAEKLKLAISSIRDHMFSEFIFCDDAKLNEIEENIWIARNIRHAMEIGELFLVYQPIVDINTRAILGAEALCRWVSAERGIISPLKFITIAEDIGFINELGYQIIKTAMGEFRHFSQRASLKDDFLLHINVSPWQLNEPHFHERFTTIMKENGLKANSLCVEITETVIERINEHFYLNIEQLRKQGVRISIDDFGTGLSNLKRFYEINPDSIKVDSQFTGDIFGTAGKIVRIIFDLARYNRIPVIAEGVESEDVARELIKLGCVQAQGYLYQKPMPFSAWDKSGKLVKE
The following text describes a protein:
Function:
Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import (Probable). In addition, binds D-galactose and D-glucose and plays a role in the chemotaxis towards these two sugars by interacting with the Trg chemoreceptor. Chemotaxis requires MglB, but not MglA or MglC.
Subcellular Localization:
Periplasm.
Domain:
The calcium-binding site is structurally similar to that of EF-hand proteins, but is in two parts, with the last calcium ligand provided by Glu-228.
Sequence:
MNKKVLTLSAVMASMLFGAAAHAADTRIGVTIYKYDDNFMSVVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANQGWDLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGAADGTNWKIDNKVVRVPYVGVDKDNLAEFSKK
The following text describes a protein:
Function:
Probable transcription factor that regulates root development and phosphate (Pi) acquisition and homeostasis. Probably acts as a repressor of primary root growth and regulates Pi homeostasis through the control of root architecture.
Miscellaneous:
MISCELLANEOUS: Seeds silencing ZAT6 fail to germinate. Plants overexpressing ZAT6 have retarded growth with smaller primary roots and fewer leaves.
Subcellular Localization:
Nucleus.
Sequence:
MALETLTSPRLSSPMPTLFQDSALGFHGSKGKRSKRSRSEFDRQSLTEDEYIALCLMLLARDGDRNRDLDLPSSSSSPPLLPPLPTPIYKCSVCDKAFSSYQALGGHKASHRKSFSLTQSAGGDELSTSSAITTSGISGGGGGSVKSHVCSICHKSFATGQALGGHKRCHYEGKNGGGVSSSVSNSEDVGSTSHVSSGHRGFDLNIPPIPEFSMVNGDEEVMSPMPAKKLRFDFPEKP
The following text describes a protein:
Function:
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. SWM1 is required for APC/C activity in meiosis.
Sequence:
MSSSSYRDSYFQYRHLPAPHHILYAEWNQDILALPDEVANITMAMKDNTRTDAEEGRAPQDGERNSNVRESAQGKALMTSEQNSNRYWNSFHDEDDWNLFNGMELESNGVVTFAGQAFDHSLNGGTNSRNDGANEPRKETITGSIFDRRITQLAYARNNGWHELALPQSR
The following text describes a protein:
Function:
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane.
Sequence:
MEENKVQKLDRNRSINHLTQLNEEIPKSSHLNGSSEKTSKANSANTNHSTDKSTEIKFQSITEKTLKQSSETILDFSPITQQPMVNFNVSIKGVSCLDYSESIIWMPKFSEVATSASCTPGLECLSQLDQVLIHPIIDKLELLSATIQSKYDIKNKDGQMIFKGIEDISASLIRYSGYDCIAIDLYDCYQTKVLRISRTTSDNLCFATNFYNLNIISPPENIIGGLSHQINTELLKEIIHNGNNVGNITKQTPENGNLVGNVEVNCKFICG
The following text describes a protein:
Function:
Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression. Mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2. Binds H3K9me and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene. Mediates down-regulation of CDH1 expression. Also represses L1 retrotransposons in collaboration with MORC2 and, probably, SETDB1, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression. The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed.
Subcellular Localization:
Nucleus. Chromosome. Note=Detected on heterochromatin. Dissociates from chromatin during interphase and early mitosis. Detected on nucleosomes (By similarity).
Domain:
The chromo domain mediates interaction with methylated 'Lys-9' of histone H3 (H3K9me), with the highest affinity for the trimethylated form (H3K9me3).
Sequence:
MAAAAEEGMSAAALVMSVPDSIGRSPESEGVGAGDEEKDAATKGTVAVGDSEEDGEDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKKLAENKAKAVRKDIQRLSLNNDIFEADSDSDQQSDTKEDISPRKKKKKIKCKEETSPEDLRKKRTKMGKLKDKFKTELESTSEIIGFDVKTKKRIWEVKEELKDSKKPKKDEIKETKELKKANKRAEVRDLKIKIREDVKENRKTKKERYIESPLESESPNDSLILEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPRKFEEPKEIKKLESTNAFLERRAIPKKQRNQDKGISNLELNKLPSPVFAQTLKSSRLSGEEKSLKSPDLAEEEKEKKNEPKGKYQKRYDLDKEEKARKEPKVLKSFKEIRNAFDLFKKTTEEKNDVLENNSKREEISLDSKIMNDNKTKDKCSLKEKRNTRDETDTWAYIAAEGDQEVSDSVCQTDETSDGRQPVLSLGMDLQLEWMKLEDFQKHLDGEDEPFITTNRIPNNLLRDAVKNGDYIAVKVALNSNEEYNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNVLVYELLKSHLETLSRVAEETIRDYFESRLALLEPVFPIACHRLCEGPDFSTDFNYMPPQNMPEGSGVLLFIFHANFLGKDVIARLCGPCSVQAVVLNDKFQLPVFLDSHFVYSFSPVAGPNKLFIRLTEAPFAKVKLLIGAYRVQLQ
The following text describes a protein:
Function:
Essential component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which is required for the sorting of proteins with complicated topology, such as beta-barrel proteins, to the mitochondrial outer membrane after import by the TOM complex.
Miscellaneous:
MISCELLANEOUS: Present with 1470 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion outer membrane.
Sequence:
MVSSFSVPMPVKRIFDTFPLQTYAAQTDKDEAVALEIQRRSYTFTERGGGSSELTVEGTYKLGVYNVFLEANTGAALATDPWCLFVQLALCQKNGLVLPTHSQEQTPSHTCNHEMLVLSRLSNPDEALPILVEGYKKRIIRSTVAISEIMRSRILDDAEQLMYYTLLDTVLYDCWITQIIFCASDAQFMELYSCQKLSGSIVTPLDVENSLLQKLSAKSLKISLTKRNKFQFRHREIVKSMQGVYHNHHNSVNQEQVLNVLFENSKQVLLGLKDMLKSDGQPTYLHLKIASYILCITNVKEPIKLKTFVENECKELVQFAQDTLKNFVQ
The following text describes a protein:
Function:
Endonuclease that can use RNA and single-stranded DNA as substrates. In contradiction with PubMed:23620482, cannot hydrolyze single-stranded DNA and does not cleave mismatches.
Sequence:
MGWSLRMWIVSILVLTQLVNGALCWGDAGHYAVCKIAQSYFEEDTVVAVKKLLPESANGELAAVCSWPDEIKKLPQWRWTSALHFADTPDYKCNYEYSRDCPKDWCVTGAIFNYTNQLMSTSENSQSIVHYNLTEALMFLSHYMGDIHQPLHEGFIGDLGGNKIKVHWYNQETNLHRVWDDMIIESALETYYNSSLPRMIHELQAKLKNGWSNDVPSWESCQLNQTACPNPYASESIDLACKYAYRNATAGTTLGDYYFVSRLPVVEKRLAQGGIRLAGTLNRIFSAKRKLARA
The following text describes a protein:
Function:
Part of an ABC transporter complex that transports riboflavin into the cell.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MQQTLPVTRVSPRVRSLQRFEWPALGLPVTLMLLLVFWQAGVTLSGYPAFILPSPALVAGRFWQALSSGLLWQHTLATLSAALGGFTLALIIALILGYTLAHIRWLEQALAPVLAASQAIPVVAVAPLIILWFGAGLTSKVLVAALITFLPILINTVVAIRSIPRELIEMAYISGANRWQLLRYVEAPLALPVLFGGVRTGLALATTGAVVGEFVAGRVGLGALINIARGLFDTPLIFVALATLALITLTLYVLAGLLERLLVRWEAS
The following text describes a protein:
Function:
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Sequence:
MPEGDTVWQAARRLHDALAGRVLTRSDFRVPRYATVDLTGRTVLDVTPRGKHLLTRVEGGLTVHSHLRMDGSWKVFAPGQRWSGGPAHQIRVILGTADRTAVGYRLPVLDILRTAEEQRAVGHLGPDLLGPDWDPERALDNLRADPPRALGEALLDQRNLAGIGNVYKSELCFLLGVTPWLPVGELPADRAARLPTLAKKLLEANRDRPVRRTTGLRGQDLFVYGRAPRPCLRCGTSVRVADQGDGSRERPTYWCPTCQAGPAPRPGGRTGVRPRR
The following text describes a protein:
Function:
Amino acid transporter importing serine, an essential substrate of the mitochondrial branch of the one-carbon pathway, into mitochondria. Mitochondrial serine is then converted to glycine and formate, which exits to the cytosol where it is used to generate the charged folates that serve as one-carbon donors. May also transport other amino acids including alanine and cysteine.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MECCGRRKEDFAEKQQEAPAGRKGSAAAWIQKTALLNSEFLKMSADIPLNINIKEPRWDQSTFIGRASHFFTVTDPRNILLSDAQLENARKIVHDYRQGIVAPGLTENELWRAKYIYDSAFHPDTGEKMVLIGRMSAQVPMNMTITGCMMTFYRTTPAVVFWQWINQSFNAIVNYTNRSGDAPITVSQLGTAYVSATTGAVATALGLNALTKHVSPLIGRFVPFAAVAAANCINIPLMRQRELKFGIPITDENGNRLGESTKAAQQAITQVVISRILMAAPGMAIPPFIMNTLEKRAFLKRFPWMSAPIQVGLVGFCLVFATPLCCALFPQKSSMSVTRLEPDLQAKIQENSPELERVYFNKGL
The following text describes a protein:
Function:
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Subcellular Localization:
Cytoplasm.
Domain:
The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of eif3d into the full eukaryotic translation initiation factor 3 (eIF-3) complex.
Sequence:
MVFEAFEVGTVPFNSDGWGPPDASDTSSTSVAAANLLPNVPFASFSRSEKLGRVADWTRALSNPSARPHTGSKSDPSAIFDFSAFAVDEGFGLTNSGGNADEDAAFRLVDGKPPPRPKFGPKWRFNQYHNRNQLPQRRDEEVEAKKREAEKDRARRDRLYNNNRNNIHQQRREAAAFKSSVDIQPEWNMLEQIPFSTFSKLSFTVSEPEDLLLCGGLESYDRSFDRITPKADRRLERFKNRSFKVTTSDDLVIRRLAKEDKATVFATDAILAALMCAPRSVYSWDLVIQRVGNKLFFDKRDGSPLDLLSVHETSQEPLPEGKDDINSAHSLGLEAAYINQNFAQQVLVKNGKRETFDEPIPNVNEGEENASIAYRYRRWKLDDSMYLVARCELQSTVDLNNQRSFLTLNALNEFDPKYSGVDWRQKLETQRGAVLANELKNNGNKLAKWTAQALLANADMMKIGFVSRVHPRDHFNHVILSVLGYKPKDFAGQINLNTNNMWGIVKSIVDLCMKLSEGKYVLVKDPSKPQVRIYEVPADAFDNDYVEEPLPEDEQVQPPEENTDAGAETNGVSSTNVAVEDKKSEVEA
The following text describes a protein:
Function:
Growth factor that supports the survival of sensory and sympathetic peripheral neurons in culture and also supports the survival of dopaminergic neurons of the ventral mid-brain. Acts by binding to its coreceptor, GFRA3, leading to autophosphorylation and activation of the RET receptor. Strong attractant of gut hematopoietic cells thus promoting the formation Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue.
Subcellular Localization:
Secreted.
Sequence:
MEWRVEGPKYRSDRFLSAYRSLPAQQVRYKEPGLWSTLTLLSLFAGAIMATPQTWHHNQTLGATSESMGTVSPAPMEEKSREALYLDAWSNWHGENVTIQGSSASELFRAERSPAGATKTRKGSRKAGRGNRSRNCRLHNLRLKVRDLGLGFESDEIVKFKYCSGSCQRARTNYDLTLSNLLQQGHIVPGPHERPSSHPCCRPTKYEDFSFMDVRNVWKTVSQVSAAECGCVG
The following text describes a protein:
Function:
Outer dense fibers are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail. May help to maintain the passive elastic structures and elastic recoil of the sperm tail.
Miscellaneous:
MISCELLANEOUS: 'Shippo' is a Japanese word for tail.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton, flagellum axoneme. Note=Expressed in the cytoplasmic lobe of spermatids.
Sequence:
MAEEVWMGTWRPHRPRGPIMALYSSPGPKYLIPPTTGFVKHTPTKLRAPAYSFRGAPMLLAENCSPGPRYSVNPKILKTGKDLGPAYSILGRYHTKTLLTPGPGDYFPEKSTKYVFDSAPSHSISARTKTFRVDSTPGPAAYMLPVVMGPHTVGKVSQPSFSIKGRSKLGSFSDDLHKTPGPAAYRQTEVQVTKFKAPQYTMAARVEPPGDKTLKPGPGAHSPEKVTLNKPCAPTVTFGIKHSDYMTPLVVDVE
The following text describes a protein:
Function:
Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes TNFRSF1B. Plays a role in the down-regulation of antiviral innate immunity by targeting MAVS for ubiquitin-proteasomal degradation. Also destabilizes TRAF6 by enhancing its 'Lys-48'-linked polyubiquitination.
Subcellular Localization:
Cytoplasm.
Domain:
The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes.
Sequence:
MDFTEAYADTCSTVGLAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSSENYIKMKTFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANVNGSHSMCGWNSLHQASFQENAEIIKLLLRKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLYCNEDSWQLPIHAAAQMGHTKILDLLIPLTNRACDTGLNKVSPVYSAVFGGHEDCLEILLRNGYSPDAQACLVFGFSSPVCMAFQKDCEFFGIVNILLKYGAQINELHLAYCLKYEKFSIFRYFLRKGCSLGPWNHIYEFVNHAIKAQAKYKEWLPHLLVAGFDPLILLCNSWIDSVSIDTLIFTLEFTNWKTLAPAVERMLSARASNAWILQQHIATVPSLTHLCRLEIRSSLKSERLRSDSYISQLPLPRSLHNYLLYEDVLRMYEVPELAAIQDG
The following text describes a protein:
Function:
Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Sequence:
MSTTATSTNELALLDKSVVVSPLVLLSVVDHYNRVAKDSKKRVVGVILGDNSTDTIKVTNSYAIPFEEDEKNPGVWFLDHNFIDSMGEMFKKINAKEKLIGWYHSGPKLKPSDLKINEVFRRYTDNPLLLIVDVQPREVGIPTDAYFAVDDIKNDGSAAEKTFIHVPSLIEAEEAEEIGVEHLLRDIRDQAAGNLSLRVSETHQSLLGLHQKLGEIANYLDKVYQKKLPMNHTILGKLQNVFNLLPNLMQQSGSDLDGGSDSSHALATAFTVKTNDELMIIYISTLVRAIIAFHDLIENKLENKKLNENKAQASVAESSLNSEKKDSIED
The following text describes a protein:
Function:
Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy. Acts by recognizing and binding cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA in the cytosol. Following cGAMP-binding, promotes the formation of autophagosomes, leading to target cytosolic DNA for degradation by the lysosome. Exhibits guanine base-specific ligand recognition. Binds 3'-3'linked cGAMP, 2'-3' linked cGAMP and 3'-3' linked c-di-GMP with much greater affinity as compared to 3'-3' linked c-di-AMP. Lacks the C-terminal tail (CTT) found in mammalian orthologs which is essential for interferon signaling.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MRRAEENNGFGTIPKRRNQHTPFYASIGMIVVIIVAFTSYHITSYGDDRNRAMRQYSFTFSLAYLAFLVGELLRRCCLFAEEYRHIETRYNGSLKKAIQTTFSFGHNNVLFVASLLFFVVFVASNDPNGSSSVIQGNSTAEPHTEMRQTSGWQGLWGQFIISALLTPLVVHLLGLRELSKVEESQLNEKENKNVADGLAWSYYFGYLKFVLPELEKQIEKTSKFRSKEKFVKKMFILIPSNCFWDDKIPGSDYDPQNRITFEGNTEPLEKTRGGVFLRHYKHSVYEIKDGENEPWFCIMEYATPLLTLYDMSVAQPGELSREERDAQVVVFLRKLQDILEGDRACQGKYELVTFSPDRDLADVMLRKLKDSELEIGG
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 C-terminal domain has nuclease activity and interacts with RecD. It interacts with RecA, facilitating its loading onto ssDNA; The N-terminal DNA-binding domain is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function. This domain interacts with RecC.
Sequence:
MSASIQAFDPLTVPISGTNLIEASAGTGKTYGIAALFTRLIVLEQKNVERVLVVTFTKAATAELKTRLRGRLDDVLQVLESKGIAKLGDDTLSDGIAAYCAEHHEGDTFLPELLKQALQKEGRTRLIVRLKAAIGQFDNAAIYTIHGFCQRILRDYAFLCQAPFDVEMTEEDGDRLLIPAQDFWRERVSNDPVLAALALKRKAVPQTVLAQISRYLSRPYLNFRRPQADLKQAQRNAETSWQTICRLLPELEAGFWRIHPDLNGNSYRKNSFGNLFKELAQKSAAGQLPFLDKDTHDRLLKLASDKLEAGLKKGKTPDAAVFAELQKLADFGRDLNALEEAEEATMIRLQLDLIEYLNRSLAEMKKSRRERGFDDLLLDVHTALTDNPHADTLARAVAENWETALIDEFQDTDPLQYEIFQKIFIAQNRPLFLVGDPKQAIYSFRGADIYAYLQAAEDARHRYTLATNYRSHAALIGSIGALFRLKERPFVLENIGYSEVGAARAESRLSPERPAVQVRWLHENDNEKANKDVLRRRAADYCADEIAHALNEAARGRLNFKGCPLQSGDIAVLVRTHNEAVMVSAALKKRQVQSVLLSRESVFASPEAAALSALIGFWLEPRRAGTLRFVLTSSIFGYDAQQLHDFNQNESEILHWAESARTALDNWNKYGIFAAMQQFSQTHGIETRLLSRNNGRSLTNYFQLLELLAAEDAQNRNPAALHKWLGDQISLAENNSGDNRAIRLESDEDLVKIVTMHASKGLQYPLVYCPFAWDAQDTGPSDWQILHQGANRTELLAKAQLSEDEQKQYADEEMAERLRLLYVALTRAEEQLNIYAAYSTNTADNPLAYLIEGSPQDSRETVRRAYACEKDGIAMLKRNWRRVADNAPSGTNFAFTENAPPPAAYRSNAGQTAEFAANSIPERGFRFVRHTSFTALSRHTQTPDGGEEDACPSLDAAETSVPAMPSETPTASDGISIHDFPKGTQAGLCLHEILEDFKFGQAAAGQETLIADKLKKYGFEEIWLPAVAEMAEACRKTPLTGAYDLSDISPECRCPEMGFTLHTEDFSLKRLRDWFARDDIRLPEVCRAAAETLDFHTVNGFLNGFVDMVCQDPDGNICVIDYKSNHLGTDASAYTQQAMDEAVAHHHYYLQALIYAVAAARYFKLRGQPPAAVSVRYLFLRGLDGKGGGVWRWDIDAAALEQIK
The following text describes a protein:
Function:
Part of the yadCKLM-htrE-yadVN fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches.
Miscellaneous:
MISCELLANEOUS: The operon is cryptic under classical laboratory conditions, but is functional when constitutively expressed.
Subcellular Localization:
Periplasm.
Sequence:
MFFNTKHTTALCFVTCMAFSSSSIADIVISGTRVIYKSDQKSVNVRLENKGNNPLLVQSWLDTGDDNAEPGSITVPFTATPPVSRIDAKRGQTIKLMYTASTSLPKDRESVFWFNVLEVPPKPDAEKVANQSLLQLAFRTRIKLFYRPDGLKGNPSEAPLALKWFWSGSEGKASLRVTNPTPYYVSFSSGDLEASGKRYPIDVKMIAPFSDEVMKVNGLNGKANSAKVHFYAINDFGGAIEGNARL
The following text describes a protein:
Function:
Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Increases the apparent Ca(2+)/voltage sensitivity of the KCNMA1 channel. It also modifies KCNMA1 channel kinetics and alters its pharmacological properties. It slows down the activation and the deactivation kinetics of the channel. Acts as a negative regulator of smooth muscle contraction by enhancing the calcium sensitivity to KCNMA1. Its presence is also a requirement for internal binding of the KCNMA1 channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside and for external binding of the agonist hormone 17-beta-estradiol (E2). Increases the binding activity of charybdotoxin (CTX) toxin to KCNMA1 peptide blocker by increasing the CTX association rate and decreasing the dissociation rate.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
CVDEPVSLFWACFLLTFYNPGVIPGWNLTQGVISKRQTSTDILILWFLPWVGQLCIHTPLVLDAYDKTRVPALGLSKGVQAWSPCSEIRTCVHGLPSVWTQKSTCHLIETNIREQEELEGKKVPQYPCLWVNVSAVGRWAVLYHTEDTRDRNQQCSYIPGSLENYQVARADVEKVKAKFHEQQIFYCFSTTRENETTVLYRRLYGPQTLLFSLFWPTFLLTGGLLIIAMVKINQSLSILAAQK
The following text describes a protein:
Function:
Catalytic component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex is involved in the regulation of the mating pheromone response.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Nuclear localization requires the formation of the CSN complex.
Domain:
The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex (By similarity).
Sequence:
MSLSNKTVKELRQLLKERYTVEDELTESIALSSMRFKPSQEPEFHALSQSSLLKTKLKQQSSTDIPSYTHVLISKLSCEKITHYAVRGGNIEIMGILMGFTLKDNIVVMDCFNLPVVGTETRVNAQLESYEYMVQYIDEMYNHNDGGDGRDYKGAKLNVVGWFHSHPGYDCWLSNIDIQTQDLNQRFQDPYVAIVVDPLKSLEDKILRMGAFRTIESKSDDNSATSYYELETIIFDSELNRALFETKLNLHCVIEDDESEQISLNRLIDSMKQYSYLMDSKNVRTRIKLATTSERVSNENKKNIDYQNRSTRSQFCLNTQRGDSTETSSFGSMFSGDNTSDVDMEDRNLTEFDSTDTSLCINGEPSIHVNRVERSSRSTDNFHNSKKRMNSNQERCHDEGNDMLQRNVLETDYARAKNRILASKIKQYERLRFYKDTFTL
The following text describes a protein:
Function:
Required for virulence. Acts both as a protease, which degrades and/or refolds damaged substrate targets, and as a chaperone. Plays an important role in the stress response network mediated through the two-component regulatory system MprAB and SigE signaling networks. May utilize its PDZ domain to recognize and process misfolded proteins at the cell membrane, leading to activation of the MprAB and SigE signaling pathways and subsequent establishment of a positive feedback loop that facilitates bacterial adaptation. Interacts with and potentially cleaves several proteins, including the 35 kDa antigen PspA. Proteolytic cleavage of PspA may help to maintain cell envelope homeostasis in Mycobacterium and regulate specific stress response pathways during periods of extracytoplasmic stress. In vitro, exhibits proteolytic activity against the artificial substrate beta-casein.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein. Secreted, cell wall. Secreted. Note=Traffics from the cytoplasm through the cell membrane to the cell wall where it is autoprocessed and eventually secreted into the culture filtrate protein.
Domain:
Each subunit is composed of an N-terminal cytoplasmic domain, a transmembrane domain, a catalytic serine protease domain, and a single C-terminal PDZ domain. The protease domains form the central core of the trimer and the PDZ domains extend to the periphery. PDZ domain is required for protease activity.
Sequence:
MAKLARVVGLVQEEQPSDMTNHPRYSPPPQQPGTPGYAQGQQQTYSQQFDWRYPPSPPPQPTQYRQPYEALGGTRPGLIPGVIPTMTPPPGMVRQRPRAGMLAIGAVTIAVVSAGIGGAAASLVGFNRAPAGPSGGPVAASAAPSIPAANMPPGSVEQVAAKVVPSVVMLETDLGRQSEEGSGIILSAEGLILTNNHVIAAAAKPPLGSPPPKTTVTFSDGRTAPFTVVGADPTSDIAVVRVQGVSGLTPISLGSSSDLRVGQPVLAIGSPLGLEGTVTTGIVSALNRPVSTTGEAGNQNTVLDAIQTDAAINPGNSGGALVNMNAQLVGVNSAIATLGADSADAQSGSIGLGFAIPVDQAKRIADELISTGKASHASLGVQVTNDKDTLGAKIVEVVAGGAAANAGVPKGVVVTKVDDRPINSADALVAAVRSKAPGATVALTFQDPSGGSRTVQVTLGKAEQ