wanglab/gogpt-training-data huggingface dataset:
Protein: DNA-directed RNA polymerase III subunit RPC1 (RNA polymerase III subunit C1) (EC 2.7.7.6) (DNA-directed RNA polymerase III largest subunit) (RNA polymerase III subunit C160) (P08968)
Organism: Trypanosoma brucei brucei
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MLKGSSSTSFLLPQQFVEPLPHAPVEISALHYGLLSRNDVHRLSVLPCRRVVGDVKEYGVNDARLGVCDRLSICETCGLNSIECVGHPGHIDLEAPVFHLGFFTTVLRICRTICKRCSHVLLDDTEIDYYKRRLSSSSLEPLQRTMLIKTIQTDAYKTRVCLKCGGLNGVVRRVRPMRLVHEKYHVEPRRGEGPRENPGGFFDAELRTACAYNKVVGECREFVHDFLDPVRVRQLFLAVPPGEVILLGLAPGVSPTDLLMTTLLVPPVPVRPRGCAGTTTVRDDDLTAQYNDILVSTDTMQDGSLDATRYTETWEMLQMRAARLLDSSLPGFPPNVRTSDLKSYAQRLKSKHGRFRCNLSGKRVDYSGRSVISPDPNLDVDELAVPLHVARVLTYPQRVFKANHELMRRLVRNGPHVHPGATTVYLAQEGSKKSLKNERDRHRLAARLAVGDIVERHVMNGDLVLFNRQPSLHRVSMMAHRARVLPFRTFRFNECCCAPYNADFDGDEMNVHFVQTEKARAEALQLMSTARNIISAKNGEPIIACTQDFLAAAYLVTSRDVFFDRGEFSQMVSHWLGPVTQFRLPIPAILKPVELWTGKQLFELIVRPSPEVDVLLSFEAPTKFYTRKGKHDCAEEGYVAFLDSCFISGRLDKKLLGGGAKDGLFARLHTIAGGGYTARVMSRIAQFTSRYLTNYGFSLGLGDVAPTPELNKQKAAVLARSVEVCDGLIKSAKTGRMIPLPGLTVKQSLEARLNTELSKVRDECGTAAVQTLSIHNNTPLIMVQSGSKGSALNIAQMMACVGQQTVSGKRILDAFQDRSLPHFHRFEEAPAARGFVANSFYSGLSPTEFFFHTMAGREGLVDTAVKTAETGYIYRRLMKAMENLSVRYDGTVRNTKGDVIQLRFGEDGLDPQLMEGNSGTPLNLEQEWLSVRAAYARWVVGLLAGSKTASDGNAIRDNENYFNEFISMLPTEGPSFVEACLNGDQEALKVCEEQESREDALHNSNGKTNDRESRPRTGRLRRAVLISHLVKVCSRKFKDDIQDFFVKKVREQQRIRNLLNLPNTSRERTEGGGDNSGPIANKRTKKRAPSLKVKDSKEGGRVSELRDLEMLQTELLPLTRGMVTRFIAQCASKYLRKACEPGTPCGAIAAQSVGEPSTQMTLRTFHFAGVASMSITQGVPRLVEVINANRNIATPVVTAPVLLMEGEENHCEIFRKRARFVKAQIERVLLREVVSEIVEVCSDTEFYLRVHLNMSVITKLHLPINAITVRQRILAAAGHTMSPLRMLNEDCIEVFSLDTLAVYPHFQDARWVHFSLRRILGLLPDVVVGGIGGINRAMISSNGTEVLAEGAELRAVMNLWGVDSTRVVCNHVAVVERVLGIEAARRVIVDEIQNILKAYSLSIDVRHVYLLADLMTQRGVVLGITRYGIQKMNFNVLTMASFERTTDHLYNAAATQRVDRDLSVSDSIIVGKPVPLGTTSFDLLLDGSISNDILPPQRCVKRGMGPNFHTAKRHHLVPLAAEGVFRLDLF
Protein: Histone deacetylase (EC 3.5.1.98) (E7FH14)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
Interaction partners:
- Calcium/calmodulin-dependent protein kinase type IV
- Histone deacetylase
- AT-rich interactive domain-containing protein 4A
- AT-rich interactive domain-containing protein 4B
- Histone deacetylase 1
Sequence:
MLLKPTVPGLCAMLQTIYETESCFSSDSTSSRERPVELLPQSRSTSMPSTVDVKTLLPSGMQSPVGGGGDQGGGSGGPVDLRTDPRLSALSAVDPSLREKQLQHELLLLKQQQELQKQLLFAEFQKQHEVLTRQHEVQLQEHLKQQQEILAAKRQQELEQKRKLEQQRHEEMEKQRLEQQLIMLRNKEKGKESAIASTEVKLKLQEFLLSKKEPGPGGLNHSFPQKCWGAHHTSLEQSSPPQSNTPGTPPSYKLPPLLGSYEGKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAIEISVSSMCSSAPGSGPSSPNSSNCAIAENGSSGSVPNIHAEQLRSLHQSLTGDGAPSPLSLYTSPSLPNISLGLPANAHITAPQKLSAQQEAERQTIQSLRQGGALTGKFISTSSLPTCLSTGAPHDPEPPAASNSHSSHSSLLQHVLLLEQARQQSALLAVPMYGQSPLVTGERVSNNMRTVNKLPRHRPLSRTQSAPLPQTPQALQHLVMQQQHQHFLEKQKHYQLNKILSKGTDLPRQPPTHPEETEEELTETAEMQDERGEGPDHVREGLQKDSSGETTPPSERIVPLKGESTESDLEEEDDEDEAVELRECDEDAPYGQYLDQQHVQQLNVFQASLSITGMPHRPLGRAQSSPVTSSLKGTTLNEVPIKHLFTTGLVYDTFMLKHQCMCGNTNIHPEHAGRIQSVWSRLQETGLLGRCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSGAVRMAVGCVIELAFKVAAGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLGVGKILIIDWDIHHGNGTQQAFYNDPNVLYISLHRYDDGNFFPGSGAPEEVGVGPGEGFNVNIAWTGGVEPPMGDVEYLTAFRTVVMPIANEFSPDVVLVSAGFDAVEGHQSPLGGYNVTAKCFGHLTKQLMKLAGGRVVLALEGGHDLTAICDASESCVEALLGDELNPLPLTVLQQKPCPKATASLERVIEIQSKHWTSLQRLAPTVGQSLLDAQRREKDEADTLTAMASLTVDNEQQTTSTETSRSAEEPMEEEPVL
Protein: RNA helicase (EC 3.6.4.13) (Q95SF2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAAASKVSISMGTAMASGAPPPAIVAPPPKPDRRERGGGRDRGDRIDRGERGDDKRAEDLTHKDKEKELEAIRERYLGIIKKKRRVRRLNDRKFVFDWDAGEDTSIDYNNLYKERHHVQFFGRGNVAGIDIKEQKRTQSKFYGDLLEKRRTEAEKEQEKVRLKKMKRKEDKQKWDDRHWSEKENDEMTERDWRIFREDYNVTIKGGRIPNPIRSWNESGFPKEIIDIIDKVGYKEPTPIQRQAIPIGLQNRDIIGVAETGSGKTLAFLIPLLSWIQSLPKIERLEDVDQGPYAIIMAPTRELAQQIEEETTKFGQPLGIRTVVVVGGLSREEQGFRLRLGCEIVIATPGRLIDVLENRYLVLNQCTYIVLDEADRMIDMGFEPDVQKILEYMPVTNLKPDTEEAEDETKLMENFYTKKKYRQTVMFTATMPPAVERLARTYLRRPATVYIGSVGKPTERTEQIVYMMGENDKRKKLMEILSRKIDPPVIIFVNQKKGADVLAKGLEKLGYNSCTLHGGKGQEQREYALAALKSGAKDILVATDVAGRGIDIKDVSLVINYDMAKTIEDYTHRIGRTGRAGKTGCAISFVTKDDSALFYDLKQCVSASPVSTCPPELMNHPEAQHKPGTVVTKKRREEKIFA
Protein: ATP phosphoribosyltransferase (ATP-PRT) (ATP-PRTase) (EC 2.4.2.17) (P00498)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of the enzymatic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Histidine biosynthesis trifunctional protein
- Imidazole glycerol phosphate synthase hisHF
- 1-
- Histidinol-phosphate aminotransferase
- Imidazoleglycerol-phosphate dehydratase
- DNA repair protein RAD16
- Histidine--tRNA ligase, mitochondrial
- eIF-2-alpha kinase GCN2
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 3
Sequence:
MDLVNHLTDRLLFAIPKKGRLYSKSVSILNGADITFHRSQRLDIALSTSLPVALVFLPAADIPTFVGEGKCDLGITGVDQVRESNVDVDLAIDLQFGNCKLQVQVPVNGEYKKPEQLIGKTIVTSFVKLAEKYFADLEGTTVEKMTTRIKFVSGSVEASCALGIGDAIVDLVESGETMRAAGLVDIATVLSTSAYLIESKNPKSDKSLIATIKSRIEGVMTAQRFVSCIYNAPEDKLPELLKVTPGRRAPTISKIDDEGWVAVSSMIERKTKGVVLDELKRLGASDIMVFEISNCRV
Protein: Endo-chitosanase (EC 3.2.1.132) (Q875I9)
Organism: Aspergillus fumigatus (Neosartorya fumigata)
Function: Chitosanase catalyzing the endo-type cleavage of chitosan, the deacylated form of chitin. Chitosanase may be crucial in the degradation of the deacetylated portion of chitin in the fungal cell wall. Chitoolisaccharides produced by the hydrolysis of partially N-acetylated chitosan are known to have many biological activities, including antibacterial activity, immune-enhancing effects, and elicitor activity. The chitosans with higher degrees of deacetylation were shown to be the better substrates. Chitodimer, chitotrimer, and chitotetramer are the major products but monoacetyl chitodimer, monoacetyl chitotrimer, and monoacetyl chitotetramer are also produced.
Subcellular location: Secreted {ECO:0000269|PubMed:16396247, ECO:0000269|PubMed:17651155}.
Interaction partners:
Sequence:
MRLSEILTVALVTGATAYNLPNNLKQIYDKHKGKCSKVLAKGFTNGDASQGKSFSYCGDIPGAIFISSSKGYTNMDIDCDGANNSAGKCANDPSGQGETAFKSDVKKFGISDLDANIHPYVVFGNEDHSPKFKPQSHGMQPLSVMAVVCNGQLHYGIWGDTNGGVSTGEASISLADLCFPNEHLDGNHGHDPNDVLFIGFTSKDAVPGATAKWKAKNAKEFEDSIKSIGDKLVAGLKA
Protein: Arginine deiminase (ADI) (EC 3.5.3.6) (Arginine dihydrolase) (AD) (P9WQ05)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ornithine carbamoyltransferase
- Argininosuccinate lyase
- Argininosuccinate synthase
- Probable amino acid decarboxylase
- Polyamine aminopropyltransferase
- Phosphate acetyltransferase
- L-glutamate gamma-semialdehyde dehydrogenase
Sequence:
MGVELGSNSEVGALRVVILHRPGAELRRLTPRNTDQLLFDGLPWVSRAQDEHDEFAELLASRGAEVLLLSDLLTEALHHSGAARMQGIAAAVDAPRLGLPLAQELSAYLRSLDPGRLAHVLTAGMTFNELPSDTRTDVSLVLRMHHGGDFVIEPLPNLVFTRDSSIWIGPRVVIPSLALRARVREASLTDLIYAHHPRFTGVRRAYESRTAPVEGGDVLLLAPGVVAVGVGERTTPAGAEALARSLFDDDLAHTVLAVPIAQQRAQMHLDTVCTMVDTDTMVMYANVVDTLEAFTIQRTPDGVTIGDAAPFAEAAAKAMGIDKLRVIHTGMDPVVAEREQWDDGNNTLALAPGVVVAYERNVQTNARLQDAGIEVLTIAGSELGTGRGGPRCMSCPAARDPL
Protein: Beta-glucuronidase (EC 3.2.1.31) (Q9V9T9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD24679p
- Esterase P
- Beta-glucuronidase
- GH07829p
- Carboxylic ester hydrolase
- Esterase-6
- SD03412p
- SD21168p
- Inositol oxygenase
Sequence:
MKSHWMPVTCLLLGSLQVLLAYTENDFLVNANRKELTDSPLFEYDNVRKPTPTKGLLYPRDSETREVRSLDGMWQLVRSDPYDPLQGIREKWFMDALRKTGREIISMPVPASYNDITTDNLRDHVGTVWYERTFFVPRSWKTMQRTWLRFSSVHYSAVVWINGRNATSHSIGHLPFESEISGLLSFGGDNRITVMCDNRLSNRTIPQGSVYKVATDDGTVPIQSYTFDFFNYAGIHRSVHLYTTPLLHISDLEVTTQLTKEGLGRIDYRVWLDASKEGLQIQPIQLRVQLRDKDGHVAAQQINKAVYHGTLLVPNATPWWPYLMHSDPGYLYNLQFELFVASNEKELESLQDTYRLPVGIRSLSWDNDSLLLNGKPLYLRGFGRHEDSDIRGKGLDNALLARDFNLLKWTGANAYRTSHYPYSEESMQFADQHGIMIIDECPAVNIDIFEPQLLENHMSSLEQLIHRDRNHPSVVAWSVANEPRSNKQGALKYFEFLVNYVREIAHGRPLTAAINANSSSCHLAQFLDIVGFNRYNSWYQNSGRTDMILNLLTIEAQSWRDRFGKPVIQFEYGGDTMEGMHSLPAFIWSEEYQVELFSRHFKAFDELRGRGWFIGEFVWNFADFRTAQTITRVGGNKKGVFTRNRQPKEVAHILRRRYFALAKELDMFGLPEDLTVYISKHIHNEL
Protein: Transcription factor MYB96 (Myb-related protein 96) (AtMYB96) (Q24JK1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator involved in the activation of cuticular wax biosynthesis under drought stress. Binds directly to DNA consensus sequences found in the promoters of genes encoding very-long-chain fatty acid-condensing enzymes involved in cuticular wax biosynthesis. Functions together with MYB94 in the activation of cuticular wax biosynthesis. Involved in drought stress response through abscisic acid (ABA) signaling. Mediates ABA signals that enhance plant resistance to drought by reducing stomatal opening. Mediates ABA-auxin cross-talk to regulate lateral root growth under drought stress conditions. Involved in the regulation of ABA biosynthesis and ABA-dependent seed dormancy state. Binds to the promoters of NCED2 and NCED6, which are enzymes catalyzing the first step of ABA biosynthesis. Regulates seed germination by controlling the expression of ABI4, a repressor of lipid breakdown during seed germination. Binds to the promoter of LTP3 and transactivates LTP3 gene in response to drought stress and freezing. Involved in cold stress response. Binds directly to the promoters of heptahelical protein (HHP) genes in response to cold stress. HHPs modulate the expression of SCRM/ICE1, SCRM2/ICE2 and CAMTA3, which are upstream regulators of cold-responsive C-repeat-binding factors (CBFs). Involved in defense responses against the bacterial pathogen Pseudomonas syringae. May act as a molecular link that mediates cross-talks between ABA and salicylate. Involved in a crosstalk between the circadian clock and ABA signaling. Binds directly to the promoter of APRR1/TOC1 to activate its expression. Promotes ABA signaling. Recruits the histone deacetylase HDA15 to the promoters of a subset of Rho GTPase (ROP) genes, which repress ABA signaling at the early stages of signal transduction. HDA15 represses ROP expression by removing acetyl groups of histone H3 and H4 from the cognate regions, particularly in the presence of ABA.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:19625633}.
Interaction partners:
- Histone deacetylase 15
- Non-specific lipid-transfer protein 3
- Ethylene-responsive transcription factor WIN1
- 3-ketoacyl-CoA synthase 6
- Protein ECERIFERUM 2
- Very-long-chain aldehyde decarbonylase CER1
- 3-ketoacyl-CoA synthase 1
- E3 ubiquitin-protein ligase MIEL1
- Very-long-chain 3-oxoacyl-CoA reductase 1
- Fatty acyl-CoA reductase 3
Sequence:
MGRPPCCEKIGVKKGPWTPEEDIILVSYIQEHGPGNWRSVPTHTGLRRCSKSCRLRWTNYLRPGIKRGNFTEHEEKTIVHLQALLGNRWAAIASYLPERTDNDIKNYWNTHLKKKLKKINESGEEDNDGVSSSNTSSQKNHQSTNKGQWERRLQTDINMAKQALCEALSLDKPSSTLSSSSSLPTPVITQQNIRNFSSALLDRCYDPSSSSSSTTTTTTSNTTNPYPSGVYASSAENIARLLQDFMKDTPKALTLSSSSPVSETGPLTAAVSEEGGEGFEQSFFSFNSMDETQNLTQETSFFHDQVIKPEITMDQDHGLISQGSLSLFEKWLFDEQSHEMVGMALAGQEGMF
Protein: NUF2 component of NDC80 kinetochore complex (B1AQT4)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
METLSFPRYNVAEIVIHIRNKILTGADGKNLTKNDLYPNPKPEVLHMIYMRALQIVYGIRLEHFYMMPVNSEVMYPHLMEGFLPFSNLVTHLDSFLPICRVNDFETADILCPKAKRTSRFLSGIINFIHFREACRETYMEFLWQYKSSADKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNQDFHQKT
Protein: Serine (or cysteine) proteinase inhibitor, clade A, member 3C (A0A0G2JSK1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAFIAALGLLMAGICPAVLCDGILGRDTLPHEDQGKGRQLHSLTLASINTDFTLSLYKKLALRNPDKNVVFSPLSISAALAILSLGAKDSTMEEILEGLKFNLTEITEEEIHQGFGHLLQRLSQPEDQAEINTGSALFIDKEQPILSEFQEKTRALYQAEAFVADFKQCNEAKKFINDYVSNQTQGKIAELFSDLDERTSMVLVNYLLFKGKWKVPFNPNDTFESEFYLDEKRSVKVPMMKIKDLTTPYVRDEELSCSVLELKYTGNASALFILPDQGKMQQVESSLQPETLKKWKDSLRPRIISELRMPKFSISTDYNLEEVLPELGIRKIFSQQADLSRITGTKNLHVSQVVHKAVLDVDETGTEGAAATAVTAALKSLPQTVPLLNFNRPFMLVITDNNGQSVFFMGKVTNPM
Protein: Ion transport domain-containing protein (G5EDR9)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ion_trans domain-containing protein
- GTL-1
- Protein ced-11
- Transient receptor potential channel
Sequence:
MGTKNSKIADGAAQVEQTMARTMSENKVIYKMVDMHGGGILIKLARKCKELNSFVLLDAYLDQEVRKYMYNGGKGKLMPVAELVKARNKERNAKLGAFSRKKGKGKSGPNILDEFDQGQAEMAGDLKKALKLLDGGGKGGKSESKYREMVWSVDERGSMGENLLAICLLQGSALHNLIARRLINFFPKLINDICVSEEYYGLSPLHLAIVNQDAQFTSLLLRLGADLNQRCYGAFFCADDQKASRTDSLEHEFVELTKNTNYTGSMYFGEYPLSFAICMGQHDLFRMLLAKKANLSAQDTNGNTALHLCVIHDKMDMLDAVLEAGGNIRLANKQNLTALTLAARLAKKTMFNKILQLECEKVWTYGSSQCVAYPLTKIDTIDETTGEMNDTSALSLVVYGESIQHLELMDGLIEQILDEKWKAYGRALWLRSLLGFIFFYCCFVCAYMLRPSSATTEHLTRGRINDDGETESTNSTNYLQWHAIDTQCHLMYYSAWPWYHGWFRLGCEIMTIIVMLFQILLDFGDIRRIGFQKWFNFLKAFPAKLMFKGAFLFIIISIPCRLACSFHEFFLTIDNTMAIISILLVTQHFLYYMRAIPFVGPFVLMVYTIIATDLVRFAMIYSIFLVGFSQSFYLIFTSCERDSTAIKKIDPMGSEFNNIMENPVDALLRTFIMTIGEFSVLYREMSACDNFWMKWIGKLIFVIFETFVSILQFNLLIAMMTRTYETIFLTRKEWKRQWAQVILMLEMGLSPASRKMHLLRYTRPTGINKRVRSYVVVSKGEGERTEKNELAAREAKEEQKREERRQLLKKKQREHEVKAKALAMMSAKLHIEVKKRRILRQQTVDANSKM
Protein: Late embryogenis abundant protein 2 (Q9SRX6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25005920}. Nucleus {ECO:0000269|PubMed:25005920}.
Interaction partners:
- Late embryogenesis abundant protein 6
- Glutamate racemase
- At2g44060
- Probable desiccation-related protein LEA14
- Desiccation-related protein At2g46140
- 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal
- Late embryogenesis abundant protein 31
- Late embryogenesis abundant protein 32
- Late embryogenesis abundant protein 7
- Late embryogenesis abundant
Sequence:
MARSLANAKIQSVFGSEKLSNAVFRRGFAAAAKTALDGSVSTAEMKKRAGEASSEKAPWVPDPKTGYYRPETVSEEIDPAELRAILLNNKQ
Protein: Serine/threonine-protein kinase Nek5 (EC 2.7.11.1) (Never in mitosis A-related kinase 5) (NimA-related protein kinase 5) (Q7TSC3)
Organism: Mus musculus (Mouse)
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q6P3R8}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q6P3R8}.
Interaction partners:
Sequence:
MDNFHLIKIIGEGTFGKVYLAKDKSESSHCVIKEISLTKEKEASKNEVILLARMEHPNIVTFFSSFQENGRLFIVMEYCDGGDLMQRIQRQRGVMFSEDQILCWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAKLGDFGTARTLNDSMELAQTCAGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFESNNFHHLVLKICQGRVAPISPHFSRDLQSLIPQLFRVSPQDRPSVTSLLKRPFLETLIARSLYPEVCSRRIQSHAHMENMAIGPTACWRVSPWSAAYLQRKFEAQQYKLKVERQLGLRPSSVEPHPNEGEKLQSHWEETKFQELQYRKNKMKDQEYWKQLEEIRQQYHNDMKEIKKKMGRELKRVVKFEISLDKCISEEDTVQENEAVDKLNATLSFEDGTKFQEHRCKEEHEDYTDRAFEELCGPEAEGFFQDVIAAENRRQWDAGAPHTLLRIMAMADVTSTCPTMPDDGQVIVMEGSVENGKQWWLDVPGTPCALAAECACSGSLSASKGETVMIKPQLPKEDQEKVEIATGIMVDDEQLEPGSDEDDIKFEESEDELRSEIIESLEKLAASTEEAEQAPSSSKNAEEPGEKEKTNLPVKKLQ
Protein: Putative antitoxin VapB5 (P9WF19)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probable antitoxin component of a type II toxin-antitoxin (TA) system. The cognate toxin is VapC5.
Interaction partners:
- Ribonuclease VapC5
- Ribonuclease VapC8
- Ribonuclease VapC4
- Antitoxin VapB2
- Ribonuclease VapC2
- Antitoxin VapB30
- Ribonuclease VapC15
- Ribonuclease VapC47
- Antitoxin VapB15
Sequence:
MSEVASRELRNDTAGVLRRVRAGEDVTITVSGRPVAVLTPVRPRRRRWLSKTEFLSRLRGAQADPGLRNDLAVLAGDTTEDLGPIR
Protein: Actin-depolymerizing factor 7 (ADF-7) (AtADF7) (Q67ZM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers. Binds monomeric actin (G-actin) with a marked preference for the ADP-loaded form and inhibits the rate of nucleotide exchange on G-actin. Required for pollen tube growth. Promotes turnover of longitudinal actin cables by severing actin filaments in pollen tubes.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21632657, ECO:0000269|PubMed:24058157}. Note=In germinating pollen grains and elongating pollen tubes, associates with the subapical actin fringe (PubMed:21632657). Associates with actin cables in the shanks of pollen tubes (PubMed:24058157). {ECO:0000269|PubMed:21632657, ECO:0000269|PubMed:24058157}.
Interaction partners:
- Profilin-5
- Profilin-4
- Profilin-2
- Profilin-1
- Profilin-3
- Cyclase-associated protein 1
- Villin-5
- Fimbrin-5
- Villin-1
- Protein phosphatase EYA
Sequence:
MANAASGMAVEDECKLKFLELKSKRNYRFIIFRIDGQQVVVEKLGNPDETYDDFTASLPANECRYAVFDFDFITDENCQKSKIFFIAWSPDSSRVRMKMVYASSKDRFKRELDGIQVELQATDPSEMSFDIIKSRAL
Protein: L-rhamnonate dehydratase (RhamD) (EC 4.2.1.90) (P77215)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-L-rhamnonate (KDR). Can also dehydrate L-lyxonate, L-mannonate and D-gulonate, although less efficiently, but not 2-keto-4-hydroxyheptane-1,7-dioate.
Interaction partners:
- 2-keto-3-deoxy-L-rhamnonate aldolase
- Inner membrane transport protein RhmT
- Uncharacterized HTH-type transcriptional regulator RhmR
- L-rhamnose mutarotase
- Glucarate dehydratase
- HTH-type transcriptional activator RhaR
- L-rhamnose isomerase
Sequence:
MTLPKIKQVRAWFTGGATAEKGAGGGDYHDQGANHWIDDHIATPMSKYRDYEQSRQSFGINVLGTLVVEVEAENGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLSATLYYSGSGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYATGARPDLAKEMGFIGGKMPTHWGPHDGDAGIRKDAAMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKRNAPVGMMVTSGEHHGTLQSFRTLSETGIDIMQPDVGWCGGLTTLVEIAAIAKSRGQLVVPHGSSVYSHHAVITFTNTPFSEFLMTSPDCSTMRPQFDPILLNEPVPVNGRIHKSVLDKPGFGVELNRDCNLKRPYSH
Protein: Golgi SNAP receptor complex member 1 (Golgi SNARE protein 1) (Protein transport protein GOS1) (P38736)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. Rescues alpha-factor maturation defects.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16107716, ECO:0000269|PubMed:16699523, ECO:0000269|PubMed:9755865}; Single-pass type IV membrane protein {ECO:0000269|PubMed:16107716, ECO:0000269|PubMed:16699523, ECO:0000269|PubMed:9755865}. Note=Punctate localization pattern. Localization affected by loss of SVP26, a membrane protein, and is shifted to the ER.
Interaction partners:
- Vacuolar v-SNARE NYV1
- Protein transport protein BOS1
- Synaptobrevin homolog YKT6
- Protein transport protein BET1
- Protein SLY1
- Protein transport protein SFT1
- Syntaxin PEP12
- Integral membrane protein SED5
- Protein transport protein SEC22
- ER-derived vesicles protein ERV29
Sequence:
MSSQPSFVTIRGKAISLETQTESLLSKYSTFAQTTSSEQTGQEKKIDKQLEGILGQRQDVIDSLTQICDSNPAISASKLSQLHRHKEILQDHWKSFRNIRSSIQQERNRLNLLFSVKNDIANSTTDAPAPIGDADEYIQNETRRIDQSNNVVDRLISQAWETRSQFHSQSNVLNTANNKVLQTLQRIPGVNQLIMKINTRRKKNAFVLATITTLCILFLFFTW
Protein: m7GpppX diphosphatase (EC 3.6.1.59) (Decapping scavenger enzyme) (Heat shock-like protein) (Protein DCS-1) (Scavenger mRNA-decapping enzyme DcpS) (G5EFS4)
Organism: Caenorhabditis elegans
Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs of the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 2 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to m(7)GMP and m3(2,2,7)GMP, respectively. May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by dcs-1 to m7GMP. Binds to m7GpppG and strongly to m7GDP.
Subcellular location: Nucleus.
Interaction partners:
- 5'-3' exoribonuclease 1
- 5'-3' exoribonuclease 2 homolog
- RNA-binding protein pno-1
Sequence:
MKRIADEELVREERAEESTQKWLQDAKFQEILGADSSHKSLFVLLSHPDGSQGILLANKSPFSEEKSDIEKLLATAQLQEISRNDIFGSYNIEIDPKLNLLKSQLIYPINDRLIAKYRQEEKFVIRETPELYETVTRPYIEKYQLNLNWVYNCLEKRSEVDKIVFEDPDNENGFVLLQDIKWDGKTLENLYVLAICHRHGLKSVRDLTGDDLEMLYNMRDKSLEAINQKYGLKTDQIKCYFHYQPSFYHLHVHFINLKYDAPASTTMSAILLDDVINNLELNPEHYKKSTLTFTRKNGDKLMEMFREALKN
Protein: Protein MICRORCHIDIA 7 (AtMORC7) (EC 3.6.-.-) (Protein CRT1-homolog 3) (CRT1-h3) (F4JRS4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits ATPase activity. Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair. Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing. Together with MORC4, acts to suppress a wide set of non-methylated protein-coding genes, especially involved in pathogen response. Positive regulators of defense against the oomycete Hyaloperonospora arabidopsidis (Hpa).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:27171361}. Note=Accumulates in discrete nuclear bodies adjacent to chromocenters. {ECO:0000269|PubMed:27171361}.
Interaction partners:
- Disease resistance protein RRS1
- Putative nuclear RNA export factor SDE5
- Protein LURP1
- Protein SAWADEE HOMEODOMAIN HOMOLOG 1
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Sequence:
MDNSIHVKREIQLPSTSPAGFPGRESVTVVDLCSSDDDSDIGEVAGGLEKVGNNFVGLKRGRDTFGGSSEVDRNNVKKVTTLAELGVGLPEGFGQSNPPESLTHPIPANPCNVFRPVPPPPPPPYAGTSGKIGGCKQFWKAGDYEGAAGDNWDLSSGGFDHVRVHPKFLHSNATSHKWALGAFAELLDNALDEVASGATYVKVDMLENNKGGNRMLLIEDNGGGMDPEKMRQCMSLGYSAKSKLANTIGQYGNGFKTSTMRLGADVIVFSRCPGKDGKSSTQSIGLLSYTFLRSTGKEDIVVPMLDYERRDPEWSKIIRSSTRDWDKNVETIIQWSPFSSEEDLLHQFDLMKDRGTRIIIYNLWEDDQGMLELDFDADPYDIQLRGVNREERNIKMASQFPNSRHFLTYKHSLRSYVSILYLRIPPGFRIILRGIDVEHHSVVNDMMQTEQITYRPQSESYGVVTNMSAIVIIGFVKDAKHHVDVQGFNVYHKNRLIKPFWRIWNATGSDGRGVIGVLEANFVEPAHDKQGFERTTVLARLESRLVQMQKTYWSTNCHKIGYAPRRREKSAYGYDNRDSSPENDREGPSSIKTPTPASDKFYSSSYPNHNGDNGVSGKDGARLQEELRREKERRKALEVEVQLSRQKIEEMKKEQENLIEIFSEERDRRDGEEEVLRNKLEEASNTIDDLLNKIKKMEGSKVPSWRH