wanglab/gogpt-training-data huggingface dataset:
Protein: GTPase Der (Double era-like domain protein) (GTP-binding protein EngA) (P0A6P5)
Organism: Escherichia coli (strain K12)
Function: GTPase that plays an essential role in the late steps of ribosome biogenesis. GTPase point mutations (but not a deletion mutant) are suppressed by mild overexpression of RelA, probably due to increased levels of the stringent response mediator (p)ppGpp. 50S subunits assembled in the absence of Der are defective and unable to assemble into 70S ribosomes. GTPase activity is stimulated by YihI. Overexpression rescues an rrmJ deletion, stabilizing the 70S ribosome. Der and RrmJ are likely to share a mechanism to stabilize 50S ribosomal subunits at a very late stage of 50S subunit maturation possibly by interacting with 23S rRNA or 23S rRNA/r-protein complex.
Interaction partners:
- Cytidylate kinase
- GTPase ObgE/CgtA
- Der GTPase-activating protein YihI
- Probable GTP-binding protein EngB
- Glycerol-3-phosphate dehydrogenase [NAD
- GTPase HflX
- DNA primase
- Ribosome-binding ATPase YchF
- Large ribosomal subunit assembly factor BipA
- Ribosomal RNA large subunit methyltransferase E
Sequence:
MVPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEIEGREFICIDTGGIDGTEDGVETRMAEQSLLAIEEADVVLFMVDARAGLMPADEAIAKHLRSREKPTFLVANKTDGLDPDQAVVDFYSLGLGEIYPIAASHGRGVLSLLEHVLLPWMEDLAPQEEVDEDAEYWAQFEAEENGEEEEEDDFDPQSLPIKLAIVGRPNVGKSTLTNRILGEERVVVYDMPGTTRDSIYIPMERDGREYVLIDTAGVRKRGKITDAVEKFSVIKTLQAIEDANVVMLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGLSQEVKEQVKETLDFRLGFIDFARVHFISALHGSGVGNLFESVREAYDSSTRRVGTSMLTRIMTMAVEDHQPPLVRGRRVKLKYAHAGGYNPPIVVIHGNQVKDLPDSYKRYLMNYFRKSLDVMGSPIRIQFKEGENPYANKRNTLTPTQMRKRKRLMKHIKKNK
Protein: Cyclin-dependent kinase-like 1 (EC 2.7.11.22) (Q6AXJ9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Si:ch73-162j3.4.
- Transmembrane protein 218
- PDZ domain containing 4
Sequence:
MEKYEKISKIGEGSYGVVFKCRNKDTGQIVAIKKFVESEDDPIIKKIALREIRMLKQLKHPNLVNLMEVFRRKRKLHLVFEYCDHTVLNELDRYPRGVPEHMVKSIIWQTLQAVNFCHKQNCIHRDVKPENILITKHQVIKLCDFGFARILTGPCDYYTDCVATRWYRAPELLVGDTQYGPPVDVWAVGCVFAELLSGAPLWPGKSDVDQLYLIRKTLGELIPRHQQVFSTNQFFSGVCVPEPQEMEPLELKYPNLSYQALSLMKGCLRMDPAERLSCEQLLEQPYFDSLREESESVTRELDRKKRTRQPRKHLPPGYLPQLASSTVFPAVENRRNYNNLRKFNYHLPNI
Protein: Tegument protein UL51 homolog (P0CK49)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Plays several roles during the time course of infection, including egress of virus particles from the perinuclear space and secondary envelopment of cytoplasmic capsids that bud into specific trans-Golgi network (TGN)-derived membranes.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:30901892, ECO:0000269|PubMed:33106493}. Virion {ECO:0000269|PubMed:15534216, ECO:0000269|PubMed:30901892}. Host Golgi apparatus {ECO:0000269|PubMed:33106493}. Note=Probably part of the virion tugument. {ECO:0000269|PubMed:15534216}.
Interaction partners:
Sequence:
MAFYLPDWSCCGLWLFGRPRNRYSQLPEEPETFECPDRWRAEIDLGLPPGVQVGDLLRNEQTMGSLRQVYLLAVQANSITDHLKRFDAVRVPESCRGVVEAQVAKLEAVRSVIWNTMISLAVSGIEMDENGLKALLDKQAGDSLALMEMEKVATALKMDETGAWAQEISAVVSSVTAPSASAPFINSAFEPEVPTPVLAPPPVVRQPEHSGPTELALT
Protein: Arginine metabolism regulation protein I (Arginine-requiring protein 80) (P07249)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: With ARG81, ARG82 and MCM1, coordinates the expression of arginine anabolic and catabolic genes in response to arginine.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:3311884}.
Interaction partners:
- Inositol polyphosphate multikinase
- Arginine metabolism regulation protein II
- Pheromone receptor transcription factor
- Protein ARG5,6
Sequence:
MTSNSDGSSTSPVEKPITGDVETNEPTKPIRRLSTPSPEQDQEGDFDEEDDDDKFSVSTSTPTPTITKTKDSSDTSTVTRRKQPIRYIENKTRRHVTFSKRRHGIMKKAYELSVLTGANILLLILANSGLVYTFTTPKLEPVVREDEGKSLIRACINASDTPDATDTSPAQEQSPAN
Protein: DNA-directed RNA polymerase subunit alpha (RNAP subunit alpha) (EC 2.7.7.6) (RNA polymerase subunit alpha) (Transcriptase subunit alpha) (O51455)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Interaction partners:
- Large ribosomal subunit protein uL6
- DNA-directed RNA polymerase, omega subunit
- DNA-directed RNA polymerase subunit beta'
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS2
- Transcription termination/antitermination protein NusA
Sequence:
MLVEKFLKDFTIPEKIEFLKSQGDGSYGKFTIYPFERGFGITIGNTLRRVLLSSIEGYAITAMRVQSNNKDSSSKVVSSEFDLIPGVSEDTLEIIANIKNIHLKLGEGEQRKTISFSVSGKDTNVLKASHFERDGVEVFNKDLVIATLSHDVNLDLEFQINYGRGYVSSEQNSKYLEEVNVIALDSIFSPIEKVSYSVEDTRVGQRSDYDKLVMEIWTTGVISAKDAIKKAASIVREFLFPLVDFEDNVNTSFEKSKSESSNLLDMSIEKLNLSVRSLNCLAKENVRTLGELISKNAEELSKARNFGKKSLEEIIEKLGSYRLYLGMSKEDALSVLSKNVKISE
Protein: 3-oxoacyl-[acyl-carrier-protein] synthase homolog (EC 2.3.1.41) (Beta-ketoacyl-ACP synthase homolog) (P39525)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Possibly involved in the synthesis of a specialized molecule, probably related to a fatty acid, which is essential for mitochondrial respiration. Is essential for oxygen uptake and the presence of cytochromes A and B.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase, mitochondrial
- Acyl carrier protein, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] reductase
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Fatty acid synthase subunit alpha reductase
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Acetyl-CoA carboxylase, mitochondrial
- Fatty acid elongase 1
- Fatty acid elongase 3
- Fatty acid elongase 2
Sequence:
MSRRVVITGLGCVTPLGRSLSESWGNLLSSKNGLTPITSLPNYNEDYKLREKSIPSTITVGKIPENFQNENSAINKLLFTSQDERRTSSFIKLALRTTYEALHNAGLLNPNDITINTSLCNLDHFGCLIGSGIGSIQDIYQTSLQFHNDNKRINPYFVPKILTNMAAGNVSIKFNLRGLSHSVSTACATGNNSIGDAFNFIRLGMQDICVAGASETSLHPLSLAGFIRAKSITTNGISRPFDTQRSGFVLGEGCGMIVMESLEHAQKRNANIISELVGYGLSSDACHITSPPADGNGAKRAIEMALKMARLEPTDVDYVNAHATSTLLGDKAECLAVASALLPGRSKSKPLYISSNKGAIGHLLGAAGAVESIFTICSLKDDKMPHTLNLDNVLTLENNEADKLHFIRDKPIVGANPKYALCNSFGFGGVNTSLLFKKWEGS
Protein: 4-hydroxybenzoate polyprenyltransferase, putative (EC 2.5.1.39) (C6KSS3)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Phosphatidate cytidylyltransferase
- Octaprenyl pyrophosphate synthase
- FAD-dependent monooxygenase, putative
- Alkyl transferase
- PAP2-like protein, putative
- Bifunctional farnesyl/geranylgeranyl diphosphate synthase
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- Ubiquinone biosynthesis O-methyltransferase, putative
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Uroporphyrinogen decarboxylase
Sequence:
MQKPYLQHFFKNLKKYEKKQTSFYILPNNKRIKNEEPICGYYNYCTFKRIKLRSHNNINNTHYNICNNNNNNKEEEEGERERYFLFNKKHFTCKAYKIKGNVFNISYEPYNIYDDNKFLNYKNNLKLYEHKMITLQRCYYSEYIDKHTKNKNKELYDPIKNLQKYKHNNDHNDDNNNNNNNNNNKDDIYNSKMCLQNKLRDMLIFNIKNYIILSRLHIPAGIYLLFYSSLYGYFLTYDMNNLLINNNILNMNEIQHILKNIGLFLFGSINTRITGCIINDLLDKNFDKEVERTKNRPIANKNISVHKAIIYACIHGTLSLLTLFQFNSSTIYTGLYSTFFIFTYPLFKRLTYYAQVYLSLTFNLGYFISASININLINNIIPIIVGFLPLSFLTIIYDTIYAHQDKKDDIRLKLKSLAIKWDKNTLKYSKVLSLNMLLFLYLSSYLFDMHFSYYIFSTFNIMYLYYILDKVSLNDKQKCMTFFKKSKNVLFFMVLATILSKASQVVCKNEENNKKKKGNIS
Protein: ToMV resistance protein Tm-1(GCR237) (Disease resistance protein Tm-1) (Protein p80(GCR237)) (A7M6E7)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Inhibitor of viral RNA replication which confers resistance to some tobamoviruses including tomato mosaic virus (ToMV) (e.g. isolate L), tobacco mosaic virus (TMV), tobacco mild green mosaic virus (TMGMV) and pepper mild mottle virus (PMMoV), but not to resistance-breaking isolates of ToMV (e.g. LT1, SL-1 and ToMV1-2) and tomato brown rugose fruit virus (ToBRFV). Prevents tobamoviruses RNA replication by affecting the association of tobamoviruses replication proteins (large and small subunits) with host membrane-associated proteins (e.g. TOM1, TOM2A and ARL8), thus inhibiting the replication complex formation on the membranes and avoiding viral negative-strand RNA synthesis. Inhibits triphosphatase activity of ToMV replication proteins.
Interaction partners:
- ToMV susceptible protein tm-2
- ToMV resistance protein Tm-2
- Agamous-like MADS-box protein AGL9 homolog
- ToMV resistance protein Tm-2
- X intrinsic protein
Sequence:
MATAQSNSPRVFCIGTADTKFDELRFLSEHVRSSLNSFSNKSSFKVGVTVVDVSTSWKETNSCADFDFVPSKDVLSCHTLGEETMGTFADIRGLAIAIMSKALETFLSIANDEQNLAGVIGLGGSGGTSLLSSAFRSLPIGIPKVIISTVASGQTESYIGTSDLVLFPSVVDICGINNVSKVVLSNAGAAFAGMVIGRLESSKEHSITNGKFTVGVTMFGVTTPCVNAVKERLVKEGYETLVFHATGVGGRAMEDLVRGGFIQGVLDITTTEVADYVVGGVMACDSSRFDAILEKKIPLVLSVGALDMVNFGPKTTIPPEFQQRKIHEHNEQVSLMRTTVGENKKFAAFIAEKLNKASSSVCVCLPEKGVSALDAPGKDFYDPEATSCLTRELQMLLENNERCQVKVLPYHINDAEFANALVDSFLEISPKSRHVECQPAESKSIQDIQNDNAVLEKYPSCNGKNFSRLNDFPNAKPETLQKRTVILQKLKDQISKGKPIIGAGAGTGISAKFEEAGGVDLIVLYNSGRFRMAGRGSLAGLLPFADANAIVLEMANEVLPVVKEVAVLAGVCATDPFRRMDNFLKQLESVGFCGVQNFPTVGLFDGNFRQNLEETGMGYGLEVEMIAAAHRMGLLTTPYAFCPDEAVAMAEAGADIIVAHMGLTTSGSIGAKTAVSLEESVTCVQAIADATHRIYPDAIVLCHGGPISSPEEAAYVLKRTTGVHGFYGASSMERLPVEQAITATVQQYKSISME
Protein: Endoribonuclease toxin ChpB (EC 3.1.-.-) (Toxin ChpB) (mRNA interferase ChpB) (P33647)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type II toxin-antitoxin (TA) system. ChpB is a sequence-specific mRNA and (weak) tmRNA endoribonuclease that inhibits protein synthesis and induces bacterial stasis. Cleavage is independent of the ribosome. Cleavage occurs at ACY sequences where Y is not C. The endoribonuclease activity is not as strong as that of MazF. The endoribonuclease activity (a toxin) is inhibited by its labile cognate antitoxin ChpS. Toxicity results when the levels of ChpS decrease in the cell, leading to mRNA degradation. Both ChpS and ChpB probably bind to the promoter region of the chpS-chpB operon to autoregulate their synthesis.
Interaction partners:
- Antitoxin ChpS
- Antitoxin MazE
- mRNA interferase toxin YafQ
- Antitoxin DinJ
- mRNA interferase toxin RelE
- Toxin YoeB
- Antitoxin YefM
- mRNA interferase toxin MqsR
- mRNA interferase toxin HigB
- Ribonuclease toxin YhaV
Sequence:
MVKKSEFERGDIVLVGFDPASGHEQQGAGRPALVLSVQAFNQLGMTLVAPITQGGNFARYAGFSVPLHCEEGDVHGVVLVNQVRMMDLHARLAKRIGLAADEVVEEALLRLQAVVE
Protein: Protocadherin 15a CD3 isoform (Protocadherin-15a isoform X1) (Protocadherin-related 15a) (A0A1V0D7A1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MRRRWWRLDCLGSAIALFVIISQISAQNTEDWHYEECKLSRSGPPATIVTIDEESPNGTILVENMQINGRARDPDRTISLTLLDNYDYWVILDPALQRLFLNSTGRVLDRDPPSSITTIVVQIQCTNELVGTVILHEVRIVVRDRNDNTPRFQQPRYYVSVNELTPVGTTIFTGFSGNNGATDIDDGPNGQIEYAIQYNPNDPMSNRTVRIAGTLSGNIVLAERLNYEERTRYLIIVQANDRAPYPGTRRTATTTLTLDVLDGDDLGPMFLPCVLVNNTQDCNPVTYRVAIPELTDPNKLNPLNVTPPIRAIDQDRNIQPPSDRPGILYFILVGTPSTYPEFFTLNRSTAELRLLKSVDRELYQRFSLVIKAEQDNGHPLPAYSKLEIEILDENNQAPYFQQSSYRGFVSESSSVGTTISASANLTAPLAIIALDNDIEETKDPQLKITLNEYTSIFTITTSGITRFLTLLKPVDREIQTNYTLTLVATDGVQQSRPVTVDILVIDANDNTPTFAQVSYSVEIFTNMLPGETVLQLMAQDADAGLNGLITYAILAGDHGDFIINNRTGRITLAPGVMLTVGRSYALTVRAADNAPDTERRSSITTVYIEVLPPNNQSPPRFPLQTYNLEISEAMRIGAILLNLQATDRELDPITYRIETGDPQEVFNLSRTIGLLLLAKPLDRETIDQYRLIVTASDGHPGGISTATVSIVITDVNDNDPTFDLTLPRNLTVREEEANVFVGQVRATDPDGGLNGQVRYRLLSFASLFSINSTGSIFTAVPLDRETRSRYDLIVEASDGAVDPRRTTITLLVEVLDINDNSPVFSQPVYTVNVPENTPAGSIILRLTAVDADLVSNVTYRIKTEAALQLFAVNRLTGVISVLQALDFESLAAGNSTYTFEVEALDHGGVLPPGTATVSVRITDMNDFSPVFRQALYKGLVAPNAEKGTVITTVLAEDQDPPGTPASKVRYRVDQELSPYSGSIFDVETDTGLVITKVNLNEQPTTVFKLVVMAYDDGEPVKTNRTTVEITVLQPSRIPIFTEEEYRFSPVSENAPIGTPVGLILAAATNTTVVYSIVSGNEGGVFTVNKSTGIIYTNKSLDYENVTSYVLRVQADSLTVILANLRAPSKTNTAKVFINVQDENDHPPVFSRQVYIGGVTEDTKTFTTVLKIVATDVDTGNYSKMAYRLIIPPTTEGQDSFVIEPYTGVIKSAIMFRNMRRSYFKFQVVATDDYGKGLTSKADVVVSVVNALDMQVVVSNVPPTVVEENKEQLISILERYVQDQIPGAKVIVESIGPRRHGEGYELEDYSKSDLQVYAIDPLTNRAISRQELFKFLDGKILDINKEFQPYLGEGGRILEIRSPDIVATVKKAAQAVGYTEGALLALAIIIILCCIPAILIVMVTYKQFKERQAECAKTARIQMALPAGKSTGGGGGGGGGGGGGGGAQTNLYEELGDGGIRRGMGRQQQLLRPSLLRPEALSMESGIDPGQDYYTQDYYGYDQGFDPYPPYGSRRRLITPMYDEYGEAFMEDEGYYYGGPEVDKKKRIKLILDREHDATSTGEDSGPDIQRNRIPNVSSHSNINGSVYLAQNGTIIRTRRPPYANNLKLGSPTRLGKQFKKLDKLGVTHEEHLPLNGTEDNGPTIGTTTAHSYMTDHNLNSKECSVKGPNCIGPKSNIDKARLEQESSVDNGEVKESVESPCEQTLSDEEELWMGPWNSLHIPMTKL
Protein: Aspartate--tRNA ligase, cytoplasmic 1 (EC 6.1.1.12) (Aspartyl-tRNA synthetase 1) (AspRS 1) (Q75JQ1)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Probable methionine--tRNA ligase, cytoplasmic
- Glutamyl-tRNA
- proline--tRNA ligase
- Aspartate--tRNA ligase, mitochondrial
- Aspartate--tRNA ligase, cytoplasmic 2
- Probable glutamate--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
- Probable isoleucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- arginine--tRNA ligase
Sequence:
MSETTPVPVGEAGEKSATALKKEQKKLEKEKKIAEAKAKKAAEKSAASGNSGEQKNEKKQEQVEENNSNWGELPMNQSKEKITREWTDVSQLTESLVGKSVLIRARLSTSRLQGANLCFVQLRDGLYTVQAVVAKGGSNSKSMVQFVGQVPKESIVDVQATVVSTSVPIESCTQKSVELQVSSFFIVSKSTLLPLQIEDLSRAQPLLDKQEDDLKQLEQLLQNTNLNEQEKTDLEKKKSECIKFVNVSQEKRLDNRALDLRVPAHQSIFRLQSGVCTLFREQLLGEGFIEIHSPKIISAASESGASVFKLNYFNTHAYLAQSPQLYKQMAICADFNKVFEIGPVFRAENSNTHRHLTEFVGLDLEMTFKDHYHEALDTLDRLMTSIFRGLETRFAKEIESVNTQYPFEPFKFTYPSPRFTFDEAAAMLAELNDPDYIVKDNDFNTRQEKRLGKIIKEKFGVDFFIVDKFHVEVRPFYTMPDPNNPQWANAYDLFMRGEEICSGAQRIHDPELLEKSAKSHGVVIEDIQGYIDSFKYGCSQHAGGGVGLERVVMLYLGLGNIRKASFCPRDPTRLTP
Protein: Glutathione S-transferase (Q383M0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTYRVLGSPYALLFHQHVAYLRLKRLPFKVYCRTFATTLFYAWVFRARNSFCTVAPNGKSYLQLWQLVSAVERSGIRQSKSFPSCGKATVAEEENDIQFVIDRHKHPNIHMVNWVIVLYSSWWLAKTGAMYRWVEGDGIDTIEGYLRYFFLVPGVGAARAIAGSFKQAIQKVTSVTGVSKETAPYMKEHFFRLCDALEVHFQEQTKRGDGSLQVSFLLGTPHPTLADVAFGSVFSANFLMDDPPASVIAQKYPHLNCYLEAVTGWKGGVFVGDDGAAGAGGVVARGMKEGDTDECSTYLDVVPDSLFPVLKLVEEVLPFMLSQCEAFHAYMVGDGVRGLKKERLEGPWEGCSGYLLSQITGIKSLMIIDNGVYTVAARAQDLEVALLAAREVVGNDDEDGGGGGGGNGNDSVISTNSEECRGETAHVFSRCAEDAAKQSGCPGGTFSAVEEVQPNTREGSGVVPSIASVVDVTHEGHSNDHTDSDGADFHRVFTSASGRSRSVLLHPRHSGQVAQSMMDSCLFRLRDILRKMHHPHYTLSSVFHGRKMFVAVIPECEVIESRKRKGNTSTIVV
Protein: Protein MC160 (Q98326)
Organism: Molluscum contagiosum virus subtype 1 (MOCV) (MCVI)
Function: Plays a role in inhibition of host innate immune response. Reduces TNF-alpha-mediated NF-kappa-B activation. Interferes with IKK kinase activity and reduces the phosphorylation of both components CHUK/IKKA and IKBKB/IKKB.
Interaction partners:
Sequence:
MAHEPIPFSFLRNLLAELDASEHEVLRFLCRDVAPASKTAEDALRALQRRRLLTLSSMAELLCALRRFDVLKVRFGMTRECAGRLLGHGFLSQYRLQVAAINNMVGSEDLRVMCLCAGKLLPPSCTPRCLVDLVSALEDAGAISPQDVSVLVTLLHAVCRYDLSVALSAVAHGHMTVGVGTPVQDEPMDVLEVDDAEPMEATPACDEIGVVKLAGAASAGAPLADGAFAACTSAGKGEDLATSDLTDSEPEDSVFAVADPVYADVDLSMFVRANATADSSMFVNADAGADSSLVNADAGADSSLVNADAGADSSLVNAVADANSSLMRTTSACTDSEPEDSAGPSCAGMALSMFGRAKSVSSLLLRTKASY
Protein: Fumarate reductase 2 (FRDS2) (EC 1.3.1.6) (NADH-dependent fumarate reductase) (Osmotic sensitivity protein 1) (Soluble fumarate reductase, mitochondrial isozyme) (P21375)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Irreversibly catalyzes the reduction of fumarate to succinate. Together with the second isozyme of soluble fumarate reductase (FRD1), essential for anaerobic growth. Involved in maintaining redox balance during oxygen deficiency conditions. Reduction of fumarate is the main source of succinate during fermentation, and under anaerobic conditions, the formation of succinate is strictly required for the reoxidation of FADH(2).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9587404}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b subunit
- Mitochondrial inner membrane protein SHH3
- 2-oxoglutarate dehydrogenase, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate dehydrogenase assembly factor 2, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Fumarate reductase 1
- Bud site selection protein 22
Sequence:
MIRSVRRVFIYVSIFVLIIVLKRTLSGTDQTSMKQPVVVIGSGLAGLTTSNRLISKYRIPVVLLDKAASIGGNSIKASSGINGAHTDTQQNLKVMDTPELFLKDTLHSAKGRGVPSLMDKLTKESKSAIRWLQTEFDLKLDLLAQLGGHSVPRTHRSSGKLPPGFEIVQALSKKLKDISSKDSNLVQIMLNSEVVDIELDNQGHVTGVVYMDENGNRKIMKSHHVVFCSGGFGYSKEMLKEYSPNLIHLPTTNGKQTTGDGQKILSKLGAELIDMDQVQVHPTGFIDPNDRENNWKFLAAEALRGLGGILLHPTTGRRFTNELSTRDTVTMEIQSKCPKNDNRALLVMSDKVYENYTNNINFYMSKNLIKKVSINDLIRQYDLQTTASELVTELKSYSDVNTKDTFDRPLIINAFDKDISTESTVYVGEVTPVVHFTMGGVKINEKSQVIKKNSESVLSNGIFAAGEVSGGVHGANRLGGSSLLECVVFGKTAADNIAKLY
Protein: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) (O53419)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable enoyl-CoA hydratase EchA8
- Probable 3-hydroxyisobutyrate dehydrogenase
- Probable acyl-CoA dehydrogenase FadE32
- Probable acyl-CoA dehydrogenase FadE25
- Acyl-CoA dehydrogenase FadE34
- Acyl-CoA dehydrogenase IpdE2
- 17-hydroxy-3-oxo-4-pregnene-20-carboxyl-CoA lyase
- Probable fatty-acid-CoA ligase FadD36
- Steroid 3-ketoacyl-CoA thiolase
- Conserved protein
Sequence:
MTGESHEVLTNVEGGVGFVTLNRPKAINSLNQTMVDLLATVLMSWEHEDAVHAVVLSGAGERGLCAGGDVVAVYHSARKDGVEARRFWRHEYLLNALIGRFAKPYVALMDGIVMGGGVGVSAHANTRVVTDTSKVAMPEVGIGFIPDVGGVYLLSRAPGALGLHAALTGAPFSGADAIALGFADHFVPHGDLDAFTQKIVTGGVESALAAHAVEPPPSTLAAQRDWIDECYAGDSVADIVAALRKQGGEPAVNASDLIASRSPIALSVTLQAVRRAAKLDTLEDVLIQDYRVSSASLRSHDLVEGIRAQLIDKDRNPNWSPATLDAITAADIEAYFEPVDDDLSF
Protein: Spectrin beta chain (F1QQE5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Spectrin alpha, non-erythrocytic 1.
- Protein 4.1
Sequence:
MATMTSTTDYDNAEITQQYSRINTRFELSDEELDNDNSSARLFERSRIKALADEREAVQKKTFTKWVNSILARVSCRISDLYLDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLILGLIWTIILRFQIQDIIVETGQADQTGRQETRSAKDALLLWCQMKTAGYPNINITNFTTSWKDGMAFNALIHKHRPDLVDYGNLKRSNPTHNLQQAFNVAEKKLGVTKLLDPEDVFTENPDEKSIITYVVAFYHYFSKMKALAVEGKRIGKVLDQAIETEKMIEKYETLSSDLLTWIEQTIVVLNNRKLANSLTGVQQQLQAFNSYRTVEKPPKFQEKGNLEVLLFTIQSRMRANNQKVYTPKEGALVSDINKAWERLEKAEYDRERVLRDELIRQEKLEQMARRFDRKAAMRETWLMENQRLVSQDNFGYDLPAVEAAKKKHDAIETDIAAYEERVQALVALSKELESERYHDAKRIDARKDNILRLWDYLQELLKARRGRLDKNLTLQRIFQEMLHIISWMDEMKGRLLSPDFGKHLLEVEDLLQKHSLVEADIAVQAERVKSANAAALKFANGDSYKPCDPQVIRDRVQHLDLCYQELCALAAQRKARLEQSRRLWNFLWEIAELESWIREREQIFSSLDYGKDLTSVLILQSKHSVFEDELAARRDNLKQVMDEGESMIQIKHLGSPKVQQRMNDVQRQWQQLEELAAFRKQNLQDTQRFFQFQGDADDLKAWLVDAMRQMSSDDVGHDEYTTQRLLKKHRDLRDEAAKNGATIDALSKQANALPEELRNTPDIQGRLNDIRDMYIELLTLSDLRQKKLDDTMALYTIFSETDACELWMGQKETWLVGLETPENLEDLEIVQNRLSILAQEMGNMQTRVDNVNKAAKQLEDSRHPQTKQVKDCQIRLNKRWEAFKAMVEDKKHRVDSALSLHNYDLDCDETESWIKEKTRVIESTQDLGNDLAAVITIQRKLFGMERDLAAIQDKLDSLRDEAQKLVKEHPENASDILARQEELDAAWDTLKRTLKDREDSLGEVSKLQTFLQDMDDFQAWLFKSQKAVASEDMPDGLPEAEQLLNLHDALRHDMDGHEEDYHRVKDTGAAVIQGQEDDPQYQQLEQRLEGLDKGWGELHKMWDSRKNFLDQGLGFQQFMRDAKQADAILNNQEYTLAHVDKPDTLDGAEKALKKHEDFVTTMDANKEKILSTLETGQRLVDSENLYSGKVKDKMSSIEERNKKNQDKAKEVSGKLKDNRELQHFLQNTQDLTLWINEKMLTAQDTSYDEARNLHSKWQKHQAFMAELASNKDWLHNIDKEGQELMESKPEFEPIVKDRLAKLHELWDKLESTTQEKARLLFDANRSELFDQSLADLKKWLAELQQQLQGDVEEEVKDLTSANILLKKHQITENQVRDRARELEELQEAVEQHGSLREDQPELEIEQQNLQRDFQKLLTPLSQRKGKLEAAKAVHQFFRDLADEILWVNERLPMAMSDDHGNNLQTVQLLLKKNQSLQKEIDGHQPRIDEVLERGRRMAAAAEGSPEEERMSEEMKKLQVVWAQLQEEMAKRRERLYGSNEAQQYYNDADDSEAWIGEQELYMIADEMAKDEQSAMIMLKRHLVLKQTVDDYAYSIQQLADRAQKMLAEEHPDGEAIIRRQGQVDKQYAGLKELAEDRKKKLDHTYHHFLLSREVEDLEQWIAERDVVASSQEMGQDLDHVTILRDKFREFARETGTVGQERVDTVNRIIDELIEGGHSESATLAEWKDGVNESWADLLELIDTRAQLLTSSYDLLKYFYDGKELVGHIEEKKNELPEDLGEDFSKAESFHRMHAAFERDISSLGKQVKQFQETAARLHAQYAGDQATAIQATEKEVVEAWKGLLDACAGRRKQLEETADKFRFFTMVRDLMAWMESILQQIETQEKPRDVSSVELLMKYHQGIRAEIETRGPKFNQCVQLGQALLERKHKDSAEIKEKLMQLVEKRKEMMLKWDDRWDWLRLLLEVCQFARDASVAEAWLIAQEPYVASKDVGQTVDEVEKLLKRHEAFEKSTATWEERFSALERLTTLELLEIRKQQQEIQQYRQEAEKESRREDTGFAEESSQLYPTEEQSLSGLGVIEPSSGGVDGTAGESTVPLISEMQESVSLELDPSTSIQVTKETEKAASLPTESTQVQPVLMEGTLARKHELEGPNKKAPNRSWNNLYCVLKPGHLSIYKDAKSFSHSVTFHGEEPLTLTNSSCEILTNYKKKKQVFKLRLGDGSEYLFQCKDEEELQNWTQAIEQAAQVQIEEPVAGPSGVKALSLPPPSSTTLEVPSTKKDKEKRFSLFAKKK
Protein: Amino acid transporter AVT1I (AtAvt1I) (F4J1Q9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEEDNQEIQRDNVGSSSFFKTCFNALNALSGIGILSVPYSLARGGWLSLSLLLLLAVTAFYTSLLITKCMNADRNIKTYPDIGERAFGRPGRIIVSVFMHLELYLVTTGFLILEGDNLHNLFPGFTIEMIGLRLNGKQAFMATVAFVIMPTLWWDNLSVLSYVSMSGVLATTVTLGSISWIGAFDGIGFHQKGKLINWSGIPTALSLYAFCYGAHPVLPTLYSSMKSKHQFNNVLLICFILCTIGYTSMAVLGYLMYGSQTLSQITLNLPIHKTSSKVAIYTTLVNPVAKYALMITPTVNTIKDWFPSRYSKKAYLHLLISTFFIISSVVIAETLPFFGYMMSLVGALLSVTVSILLPCLCYLKIFGNYKKIGCETIMLFGMVVMSVFVGVIGTYIALRDIIGSV
Protein: Alpha-1,2-mannosyltransferase MNN23 (EC 2.4.1.-) (Q5AP90)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Alpha-1,2-mannosyltransferase required for cell wall integrity. Responsible for addition of the first alpha-1,2-linked mannose to form the branches on the mannan backbone of oligosaccharides. Addition of alpha-1,2-mannose is required for stabilization of the alpha-1,6-mannose backbone and hence regulates mannan fibril length; and is important for both immune recognition and virulence.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Alpha-1,6-mannosyltransferase
- Glutamyl-tRNA
- Alpha-1,6-mannosyltransferase
Sequence:
MSINFLSIPRNRFKAIGVLSVTCILIYVILHSSIITTDFDVSDYGDKFIPSIIFDDNNDNGENLKDPQPELDNDKGNGETDTTTSNSMTTAHTFWKGIFDTFDKYKMDLGQDPENAVSYVDKLKQKQGPLNKEVLLSKAIVSSELMKHLKEKHSGVVEDLPSVMPGSVYNKGSKGVVIIGGGKFSWLAYLALVQLRNVGSKLPVEIVMPSRADYEKELEFCENTLPEMQASCVVLPDVLGEAVMKNRKFASYQFKALALVVTSFEHILLLDSDNMIVSNPDEIFESKLYHQYGMITWPDYWKRTISPLFYDVAEIEVNENKRVRYNRFPLYNAPNVRSNIYTDQEREEVPFHDLQGSIAELSTESGQLIINKHTHGKTILLALYYNFYGPNLFYKLFSLGEQGEGDKDTFVAAAVVTRQDYYQVKSFIKTFGYADSDDKFQGVSMGQRNPLIDRKHYEDHVLALLEKDSFKSSSIADQIEQMKKFENEDFDQHNSIPLFTVHCNYPKLDPKLYMSRDDLYDEKEKKLKYRLYGNLKYTKEVVKDGETGTEASTDKVQIDFELQQWQHMQDILCLKKIYFTHFIDNDMNELCQFIENQVAWLSKSQN
Protein: Tumor necrosis factor receptor superfamily member EDAR (Anhidrotic ectodysplasin receptor 1) (Downless) (Ectodermal dysplasia receptor) (Ectodysplasin-A receptor) (Q9R187)
Organism: Mus musculus (Mouse)
Function: Receptor for EDA isoform TAA, but not for EDA isoform TA-2 (By similarity). May mediate the activation of NF-kappa-B and JNK. May promote caspase-independent cell death.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Ectodysplasin-A
- Ectodysplasin-A receptor-associated adapter protein
- Protein unc-119 homolog A
- Bone morphogenetic protein 4
Sequence:
MAHVGDCKWMSWLPVLVVSLMCSAKAEDSNCGENEYHNQTTGLCQQCPPCRPGEEPYMSCGYGTKDDDYGCVPCPAEKFSKGGYQICRRHKDCEGFFRATVLTPGDMENDAECGPCLPGYYMLENRPRNIYGMVCYSCLLAPPNTKECVGATSGVSAHSSSTSGGSTLSPFQHAHKELSGQGHLATALIIAMSTIFIMAIAIVLIIMFYIMKTKPSAPACCSSPPGKSAEAPANTHEEKKEAPDSVVTFPENGEFQKLTATPTKTPKSENDASSENEQLLSRSVDSDEEPAPDKQGSPELCLLSLVHLAREKSVTSNKSAGIQSRRKKILDVYANVCGVVEGLSPTELPFDCLEKTSRMLSSTYNSEKAVVKTWRHLAESFGLKRDEIGGMTDGMQLFDRISTAGYSIPELLTKLVQIERLDAVESLCADILEWAGVVPPASPPPAAS