wanglab/gogpt-training-data huggingface dataset:
Protein: Ferritin-like protein (EC 1.16.3.1) (IMEF cargo protein) (A0A0F5HNH9)
Organism: Bacillus thermotolerans (Quasibacillus thermotolerans)
Function: Cargo protein of a type 1 encapsulin nanocompartment. A ferritin-like iron-binding protein probably involved in iron mineralization in the encapsulin nanocompartment. Has ferroxidase activity even when encapsulated, the rate is probably controlled by the rate of Fe flux across the nanocompartment pores. Part of the iron-mineralizing encapsulin-associated Firmicute (IMEF) system. 2 different cargo proteins have been identified (IMEF and Fer); when both are expressed in E.coli with the shell protein only IMEF is detected within the nanocompartment. E.coli expressing all 3 genes stores the largest amount of iron and is protected from Fe/H2O2-induced oxidative stress.
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:31194509, ECO:0000269|PubMed:31282860}.
Interaction partners:
Sequence:
MKEELDAFHQIFTTTKEAIERFMAMLTPVIENAEDDHERLYYHHIYEEEEQRLSRLDVLIPLIEKFQDETDEGLFSPSNNAFNRLLQELNLEKFGLHNFIEHVDLALFSFTDEERQTLLKELRKDAYEGYQYVKEKLAEINARFDHDYADPHAHHDEHRDHLADMPSAGSSHEEVQPVAHKKKGFTVGSLIQ
Protein: Lactotransferrin (B7ZAL5)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRRVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLHQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAARRARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK
Protein: Ada2a-containing complex component 1 (LD21610p) (Q9VM59)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- SAGA-associated factor 29kDa
- Ada2a-containing complex component 2
- Transcriptional adaptor 3, isoform C
- Transcriptional adapter 2A
- Molybdopterin synthase catalytic subunit
- histone acetyltransferase
- Host cell factor
- Ada2a-containing complex component 3, isoform D
- D12
- DNA polymerase epsilon subunit 3
Sequence:
MEIAEISAEDEDVFHFETEHLALRGNQCYTNLLRTLAVLQAQRIRVHQQIEELEATQNIYLENPQHMLDKLRNNEPLIADNYITTTVLPDLPTLSPNDEEGGTNETPTDASSWTQEANKNRDRSNGRSENFNRLWTNEEQSRLEQLLIQYPPEEVEMRRFGKIAKALGNRTAQQVYSRVQKYFQKLHDAGMPVPGRIPKHRRPGLSKPKIKLRKSTFFPAHNISLQMPEDDFTFDDLRIPSPASDMLLMPASKIEPKIESEYMDADLNAESKRKQELCLKLLSAIQDEKREMEDGYEPDLLAAKCAECEEASVTRTQWRCNSCYCYLNLCGDCLASQLIEGRFEHLSHEVVVDQES
Protein: Cell division control protein 48 homolog D (AtCDC48d) (Transitional endoplasmic reticulum ATPase D) (Q9SCN8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably functions in cell division and growth processes. Interacts with certain SNAREs as part of specialized membrane fusion events where vesicles from the same organelle fuse (homotypic fusion) (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:19245862}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000250}. Note=Primarily localized to the nucleus and, during cytokinesis, to the phragmoplast, a site where membrane vesicles are targeted in the deposition of new cell wall materials. {ECO:0000250}.
Interaction partners:
- NPL4-like protein 1
- NPL4-like protein 2
- AT2G21270 protein
- Plant UBX domain-containing protein 6
- Peptide-N
- Probable ubiquitin conjugation factor E4
- Protein OS-9 homolog
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 2
- Plant UBX domain-containing protein 11
- Plant UBX domain-containing protein 5
Sequence:
MANQAESSDSKGTKKDFSTAILEKKKAANRLVVDEAINDDNSVVSLHPDTMEKLQLFRGDTILIKGKKRKDTVCIALADETCDEPKIRMNKVVRSNLRVRLGDVISVHQCPDVKYGNRVHILPLDDTIEGVSGNIFDAYLKPYFLEAYRPVRKGDLFLVRGGMRSIEFKVIETDPAEYCVVAPDTEIFCEGEPIKREDEERLDEVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQCIREKMDVIDLDDEEIDAEILNSMAVSNDHFQTALGNSNPSALRETVVEVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIRENIEKDIEKERKRAESPEAMEEDEEEIAEIKAGHFEESMKYARRSVSDADIRKYQAFAQTLQQSRGFGSEFRFPDAPTGTTGAFPGAAATVGGVDPFATSGGAADDDDLYS
Protein: E3 ubiquitin-protein ligase LNX (EC 2.3.2.27) (Ligand of Numb protein X 1) (Ligand of Numb-binding protein 1) (Numb-binding protein 1) (RING-type E3 ubiquitin transferase LNX) (O70263)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65.
Subcellular location: Cytoplasm.
Interaction partners:
- Protein numb homolog
- Numb-like protein
- Melanoma-associated antigen B18
- Coxsackievirus and adenovirus receptor homolog
- Ubiquitin-conjugating enzyme E2 N
- Ubiquitin-ribosomal protein eS31 fusion protein
- Immunoglobulin superfamily member 5
Sequence:
MNQPDLADDPDPSPEPLCIVCGQNHSPEENHFYTYTEDVDDDLICHICLQALLDPLDTPCGHTYCTLCLTNFLVEKDFCPVDRKPVVLQHCKKSSILVNKLLNKLLVTCPFTEHCTEVLQRCDLQHHFQTSCKGASHYGLTKDRKRRSQDGCPDGCASLMATTLSPEVSAAATISLMTDEPGLDNPAYVSSVEDGEPVANSSDSGRSNRTRARPFERSTMRSRSFKKINRALSALRRTKSGSVVANHVDQGRDNSENTTVPEVFPRLFHLIPDGEITSIKINRADPSESLSIRLVGGSETPLVHIIIQHIYRDGVIARDGRLLPGDIILKVNGMDISNVPHNYAVRLLRQPCQVLRLTVLREQKFRSRSNAHVPDSYGPRDDSFHVILNKSSPEEQLGIKLVRRVDEPGVFIFNVLNGGVADRHGQLEENDRVLAINGHDLRFGSPESAAHLIQASERRVHLVVSRQVRQSSPDIFQEAGWISNGQQSPGPGERNTASKPAATCHEKVVSVWKDPSESLGMTVGGGASHREWDLPIYVISVEPGGVISRDGRIKTGDILLNVNGIELTEVSRTEAVAILKSAPSSVVLKALEVKEQEAQEDCSPAALDSNHNVTPPGDWSPSWVMWLELPQYLCNCKDVILRRNTAGSLGFCIVGGYEEYSGNKPFFIKSIVEGTPAYNDGRIRCGDILLAVNGRSTSGMIHACLARMLKELKGRITLTIASWPGTFL
Protein: Probable zinc transporter 12 (ZRT/IRT-like protein 12) (Q9FIS2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Zinc transporter involved in zinc uptake in roots. Targeted by BZIP23 transcription factor in response to zinc-deficient conditions.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Putative zinc transporter At3g08650
- TPR repeat-containing protein ZIP4
- F-box protein At3g54460
- Basic leucine zipper 19
- rRNA biogenesis protein RRP36
- Basic leucine zipper 23
- Zinc transporter ZTP29
Sequence:
MSRFRKTLVSAFVLCLVIFPLLVSAAEEENQCGGSKGGSAAEKASALKYKIIAFFSILIAGVFGVCLPIFGLKTESNFFMYVKAFAAGVILATGFVHILPDATESLTSSCLGEEPPWGDFPMTGLVAMAASILTMLIESFASGYLNRSRLAKEGKTLPVSTGGEEEHAHTGSAHTHASQGHSHGSLLIPQDDDHIDMRKKIVTQILELGIVVHSVIIGISLGASPSVSTIKPLIAAITFHQLFEGFGLGGCISEAKFRVKKIWVMLMFFALTAPIGIGIGIGVAEIYNENSPMALKVSGFLNATASGILIYMALVDLVAPLFMNQKTQSSMKIQVACSVSLVVGAGLMSLLAIWA
Protein: Geminin (O88513)
Organism: Mus musculus (Mouse)
Function: Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC). It is degraded during the mitotic phase of the cell cycle. Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle. Inhibits histone acetyltransferase activity of KAT7/HBO1 in a CDT1-dependent manner, inhibiting histone H4 acetylation and DNA replication licensing (By similarity). Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O75496}. Nucleus {ECO:0000250|UniProtKB:O75496}. Note=Mainly cytoplasmic but can be relocalized to the nucleus. {ECO:0000250|UniProtKB:O75496}.
Interaction partners:
- DNA replication factor Cdt1
- DNA replication licensing factor MCM6
- Cell division control protein 6 homolog
- Origin recognition complex subunit 6
- Origin recognition complex subunit 4
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM5
- Multicilin
- DNA replication licensing factor MCM4
- Cell division control protein 45 homolog
Sequence:
MNLSMKQKQEGAQENVKNSPVPRRTLKMIQPSADGSLVGRENELPKGLFKRKLWDDQLASQTSSCGPEANENKDVGDLTQEAFDLISKENPSSQYWKEVAEQRRKALYEALKENEKLHKEIEQKDSEIARLRKENKDLAEVAEHVQYMAEVIERLSNEPLDNFESPDSQEFDSEEEAVEYSELEDSGAGTCAEETVSSSTDARPCT
Protein: SET and MYND domain containing, arthropod-specific, member 4, isoform A (Q9VZ41)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- SET and MYND domain containing, class 4, member 1, isoform B
- SET and MYND domain-containing protein 4
- SET and MYND domain containing, class 4, member 3
- RE32936p
Sequence:
MPGRKKNHHKNNNNSRARHQRGGQQSKDKQEQQDKEQSPSPTEEKELPYRVEHSDIYGRYLVANRQLEAGETLIREEPLAIGPCVSGDPVCLGCYHPVSLKADQYRCPGCAWPLCGSTCAGLKHRHGHTETECQLYAERRAVAGELLTERAGPAEVRDLYELVMIVRILLLRQHDPEQFALIARMESHTEERRQNAVLWRHYEEKVVQRLRVTWQLEDLEAEQVHEVCGILDVNCFEIGQNGAKARTLYPSAFLLAHDCTPNTAHTDDPSSFEILLRTSRRVREREALTLSYAYTLQGTLKRRAFMHEGKLFWCCCRRCSDPRELGTDCSALVCATCRTGSVRAVDPLQQTGDWACDRCAHKMGATEVERQLDRINNDLEDIDVHDIPGLENFLLRYRDVLRPNHYLLLSAKYSLCQIYGRTEGYLLPQMSPEDIARKESYCREFLEIVDVLDPGLTRLRGLIMYELHAPVMVLAQSAFQSGQISRQEFQRRLKEVVKLLQVSRDILLMEPEGSTENAMGQAAADALSKMGC
Protein: Formate dehydrogenase-O major subunit (EC 1.17.1.9) (Aerobic formate dehydrogenase major subunit) (FDH-Z subunit alpha) (Formate dehydrogenase-O subunit alpha) (P32176)
Organism: Escherichia coli (strain K12)
Function: Allows to use formate as major electron donor during aerobic respiration. Subunit alpha possibly forms the active site.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Formate dehydrogenase-O iron-sulfur subunit
- Formate dehydrogenase, cytochrome b556
- Protein FdhE
- Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit
- Formate dehydrogenase, nitrate-inducible, cytochrome b556
- Sulfur carrier protein FdhD
- S-formylglutathione hydrolase YeiG
- S-formylglutathione hydrolase FrmB
- Formate dehydrogenase, nitrate-inducible, major subunit
- Formyltetrahydrofolate deformylase
Sequence:
MQVSRRQFFKICAGGMAGTTAAALGFAPSVALAETRQYKLLRTRETRNTCTYCSVGCGLLMYSLGDGAKNAKASIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGSDKWQQISWEEAFDRIAKLMKEDRDANYIAQNAEGVTVNRWLSTGMLCASASSNETGYLTQKFSRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTAAVADYYAPIRSGTDIAFLSGVLLYLLNNEKFNREYTEAYTNASLIVREDYGFEDGLFTGYDAEKRKYDKSSWTYELDENGFAKRDTTLQHPRCVWNLLKQHVSRYTPDVVENICGTPKDAFLKVCEYIAETSAHDKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLLSQSLPGYMTLPSEKQTDLQTYLTANTPKPLLEGQVNYWGNYPKFFVSMMKAFFGDKATAENSWGFDWLPKWDKGYDVLQYFEMMKEGKVNGYICQGFNPVASFPNKNKVIGCLSKLKFLVTIDPLNTETSNFWQNHGELNEVDSSKIQTEVFRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIALTDGEILSGIFLRLRKMYAEQGGANPDQVLNMTWNYAIPHEPSSEEVAMESNGKALADITDPATGAVIVKKGQQLSSFAQLRDDGTTSCGCWIFAGSWTPEGNQMARRDNADPSGLGNTLGWAWAWPLNRRILYNRASADPQGNPWDPKRQLLKWDGTKWTGWDIPDYSAAPPGSGVGPFIMQQEGMGRLFALDKMAEGPFPEHYEPFETPLGTNPLHPNVISNPAARIFKDDAEALGKADKFPYVGTTYRLTEHFHYWTKHALLNAILQPEQFVEIGESLANKLGIAQGDTVKVSSNRGYIKAKAVVTKRIRTLKANGKDIDTIGIPIHWGYEGVAKKGFIANTLTPFVGDANTQTPEFKSFLVNVEKV
Protein: DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) (Q8T307)
Organism: Trypanosoma brucei brucei
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSTKNSVVGSASGSHASTAGETVTSTRSGTSSRHSRQRRQQYDYVKNPSEPMTAMERLKLVRCSIARLRYLGERHRHTSKLDTTGGDRLLSFFEGLRKRVLKLEYNPRVVAKSKVGAPKHLDYIRGHANVLLGEASTIISECEQAMDRSEAVYEGLAYHQLQDTHRELENLVGLLSGAPSDMESAGSLKLLADLVSPHVAEFDAFAEQRVPEFLQELKNEGFLFSSVINDSQQPANAIGLLSVFIVDVAIGVRPGRSARLVIQHALHNLARLKSRVDKADLTLGAEEDSSNNEHHRMQSLEFEVIRGRLREAKEELERIRDKWDHDEGDIFSRAGTGVQSLQSIIDAKRVKESTVIEEAQAIHDRTVYACLPFASPQYCRIRSETYSQPCHVRVGFKFVAKGDGSVSRTKTQLIYNLMPEFLILMRQQGIAPSDHERFATLAPSKYELWLSLGELPEMVLGARCALRGVNQRLDHFRALEEQKEVGGYFVLRGGERILRNLILQRCNVPLNIERERFATVDSFFSPRAVIIRCKRPSGLTVQNYFYYATKGEVIFTFARRVVWNIPALLVLSALNTRHRTSLDIYKLLTIGLTNGRSPHAARVEALLQHHSQMPYSTLDNFLDYLAVVGLMYRRYHESSFIFRFLPQYHTSFATQHDAWYGLFMLRRHMLPHLNTAEATSDLPPTATSREIREWLSAGLQEELAAKFDALIGILRQLLVFNDGATGNQGNDVLAYQEVFTVSQVLIGAFEVSLMKTMGAVTFRMAGQLSPEIFQATMCLAETPVREAANTLEKLNQLLEYSCRNNGPDPLITLNRLLLTGNFALDREEDFYSPQTAGWAVMTEHLNFYRSFEQLMCVHRGKSIAEMRSSDVRRYPCEAYGFICMVHSPDGEDCGVLNHLSISTVLSASPRVGSSQYKILLAFIEEELKNVRNTTSLISCVDQLVGTVPVWLEGRLLGYLSPNEALSASKALTQKKALRSRGVVGVTGIVRRDSISSLNTMEVVYIPPGSKDPMGLYIFYQYGRLMRPVLQIESPSRGGDLPFPVVYLGTWEQSWRDIAAVPSDLFDGFDQLRRKYEFMEQNGFNILSFTSSTIPFFEHNCSPRNLFQCGLSKQTAGTQLQTQAWRRDAKLFRMYYPQRYISRTLPMDYFGLDDVSLGVNAVVAILAYTGYDLDDAMILNSTAKQFGMLNAGVTVAKIVKASGKGDSNDVFVFHNCLPDGQPFTPELDRHGLPKKRAVPNATAYFSFDTDHKYPSLRDSSAVYCCAKRFEYIDPLTNEKTYEYTRHQITKWRHFDKGEDAWVHSVIPLTYDGPDPTSVLVLFRIPRPPVIGDKFSSRHGQKGTLPLDIRSHDLPFSTRDGITPDIIINPHAFPSRMTVGMVLEMMGAKLGCIQGRLCDHSAWSVIDEQPRSAKTIGDALEALGYNRYGREKLIDGITGEEIEAEVLVGISGYQRLRHMVSDKWQARARTDSHTHRAVTKTGQPVKGRKRHGGVRVGEMERDALLSHGVAEVVIDRLLHVSDKTKAFICVECGSMLSIYERHATEYSTWKTCKFCSAGLHETDDTIAFVEIPQVLRLWATELTSVGIRVVLKTSETSL
Protein: Large ribosomal subunit protein eL31A (60S ribosomal protein L31-A) (L34) (YL28) (P0C2H8)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein uS19
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein eL27A
- Large ribosomal subunit protein eL39
- Ribosome biogenesis protein NOP53
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL22A
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL23
Sequence:
MAGLKDVVTREYTINLHKRLHGVSFKKRAPRAVKEIKKFAKLHMGTDDVRLAPELNQAIWKRGVKGVEYRLRLRISRKRNEEEDAKNPLFSYVEPVLVASAKGLQTVVVEEDA
Protein: Brain-derived neurotrophic factor (proBDNF) (K4MQC6)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU364086}.
Interaction partners:
Sequence:
MTILFLTMVISYFSRMKAAPMKEASVRGHGSLAYPGLRTHGTLESLTGPNAGSRGLTSLADTFEHVIEELLDEDQDIQPSEENKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSTSEWVTAAEKKTAVDMSGATVTVLEKVPVPKGQLKQYFYETKCNPKGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDNKKRVGWRFIRIDTSCVCTLTIKRGR
Protein: Tryptophan dimethylallyltransferase (EC 2.5.1.34) (4-dimethylallyltryptophan synthase) (All-trans-hexaprenyl-diphosphate synthase) (L-tryptophan dimethylallyl transferase) (DMATS) (Q50EL0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A. Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus.
Interaction partners:
- 4-dimethylallyltryptophan N-methyltransferase easF
- Tryptophan synthase
- tryptophan synthase
- Chanoclavine-I dehydrogenase easD
- Catalase easC
- FAD-linked oxidoreductase easE
- Festuclavine dehydrogenase easG
- Chanoclavine-I aldehyde reductase easA
Sequence:
MKAANASSAEAYRVLSRAFRFDNEDQKLWWHSTAPMFAKMLETANYTTPCQYQYLITYKECVIPSLGCYPTNSAPRWLSILTRYGTPFELSLNCSNSIVRYTFEPINQHTGTDKDPFNTHAIWESLQHLLPLEKSIDLEWFRHFKHDLTLNSEESAFLAHNDRLVGGTIRTQNKLALDLKDGRFALKTYIYPALKAVVTGKTIHELVFGSVRRLAVREPRILPPLNMLEEYIRSRGSKSTASPRLVSCDLTSPAKSRIKIYLLEQMVSLEAMEDLWTLGGRRRDASTLEGLSLVRELWDLIQLSPGLKSYPAPYLPLGVIPDERLPLMANFTLHQNDPVPEPQVYFTTFGMNDMAVADALTTFFERRGWSEMARTYETTLKSYYPHADHDKLNYLHAYISFSYRDRTPYLSVYLQSFETGDWAVANLSESKVKCQDAACQPTSLPPDLSKTGVYYSGLH
Protein: Calmodulin-2 B (P0DP35)
Organism: Xenopus laevis (African clawed frog)
Function: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases.
Interaction partners:
Sequence:
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
Protein: Protein javelin (M9NE38)
Organism: Drosophila melanogaster (Fruit fly)
Function: Important for normal assembly of actin bundles during bristle formation.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21930794}. Note=Colocalizes with actin filaments. {ECO:0000269|PubMed:21930794}.
Interaction partners:
Sequence:
MGNGYFRTSQTSSSSRQREKRGKDSYSYQHNYVDRVRLEDTTGGHYHNNQHQQTTHDPRCPQLRAAGWRHTHKSVSHLDLATSCHDAAGTGLGRHSQQLHHHHSNQVNQHHHQQQQSHHHLQHANLHSHHPHAQPHWTQCRVGGAGSGNGQLRNARSLDYTQLEREENALDIAEFYWRFDAEAPLDQVDSYAVLPINDNFEPSAATSTAVGSKETTTTVANKANGSATTNATTAAANALLDILGSESCSLRRSRSLAVIREETFSDLQIGSANSSRRRSQLIPRARLVNRGFFRESPRSRHKFQFKQFKKKPPAKLLRLNGKPNQATLVGEQPADQPTADDTQSQRSNSATCDSHQQQQQQQHQPQQQHQQQQHRLSGESRDFDVYYDNLKRLDALALNLSEQLHPWHNDKSDLESLNSDYFKNSLHQNHLDQQQPSSLEFEALEQVAASLLKERPRIYQSRRQQQKRNNHHSNCLQRHLDTGGESCPEHSQSSVFPETTTSNSDDQTDSPSLSEQEYDLTHIEEIYQQGNNGEESYEIISLTTTTRTRFESSEEGEEEQTGEEVVDSLTTPTEPQTSDSESTLRQNHNEQLDKLIAYDSVYLSSEDSSDCTLVGESCESFEQRTFTSCGESGELETRSLLHISIEDTVYEPQAKQHKKATNQEDQPAPLLTTTAKVEAQIFTQVLKVEHTPKPNILAVVEKRKLKQEEVKHQPPELKRQATDSFVVTANKSNLAENQYHSLPDVNIGVSLKVCESIDKELRSSYNQQRQQQRKEAKKEQQVTRAETYDSIRRFGRAHQKARQREYQEREREREKEASAALQEKDKEREREKPKINKEFSAQERQIEVKETTKSQDIIKEKEQVSRKEEAEDDEEEEPLPPPPPPLTEESQQEDTVADVEEEDNLSVSISQPEQPKEAPVIEVANFSKLIERRAQEIRERQEQIKPSFQIIVTDAQNNIIQKEAIQENKETSQRIEPKPSPKTNSNSSSTCNLVQRPLRRSVSSSSGKPLEHRILSTGAPIYKARPVRVLPSSSSDSSFSRGKMSRPQILHVVDGRGGVAGGGAGGTLRRRSSARSIASTISSPGGEVANEYLQKVDAVRCYWNKLAGNEPETLKTEQPAKETQPGIHFQLGGETTTQGTDKSAVGNDFCSMMPHPSIEIVELGEGAQKATIVKAAPEREEDPDEDQDQFDHIRYKVLKSQQLIRNNFLSTRNKKEAQFDGLIQYLQEYSFQELLSNNNVVIVEPVRTKIERPLQVGINSGSTTTPTTVPPPKPPRVVNASASQPRKTRQKQTGGAAAKRHFFYQPVRVNRELYEDELPDPDTVRNVRRFFEQNVLPTPGQGLLVQSQQKFGGSACQLSPKSRRARGYRYLTIDTSYGGAEEQPKGMEMLEEHKAKHWDNASLSSGISSGVLSSPCGEYHHQESPVMACKDVHVQDVVRRHNSNAANAKARAKFASRRTWCMGAGGPGANESLYRQIYENNLGNSEQQENGEHLEEEDDEQDDQYEDDVEQDMCENYYVSNDVLAKIRECGSTVTYYGGRVLDKTATSTAAPSTKTTQPMTGSATRSRIRQIEACNVCLPSERCEHRLQTKQAAAKQQQDSYQGIKFKLVKSNSCSSRLELAGTGEDEVTADSEVVRKMVHHFEANQTTASNDVQVTINSQSQITSTKKEPEEDVPRRQVTVNNHINVLGDTMPQASQEKAENFNGRPEENGYGAVETVPTYESQAMNIRLDATENKNILQTAAATAAANKVCRNKNVDLAYTLVKTTTNSPKGKPIEAPRQKIGKQLREVEENVEKAAVTKATIKLTKGAPSQIIVPVDIHSQASIVAHTAPIPERRLSNASSSNSVVDKTVVRHYVANDKSIYERRKYDEIEFEEFEVYDPSKEPPPQVEEGTDKIPTDAELYDSLDDKM
Protein: Calcium-binding EF hand family protein (Q9FNN0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein F7J8_130
- Leucine-rich repeat protein kinase family protein
- RING-type E3 ubiquitin transferase
- Mitochondrial carrier protein CoAc2
- SNF1-related protein kinase regulatory subunit beta-3
- Glycoside hydrolase family 28 protein/polygalacturonase family protein
- At5g51840
- At2g23910
- Cation/H
- Cellulose synthase-like protein B1
Sequence:
MSKASVILYITVGILVLFLVSYSPKKKGDHDHHHGGHNQHHRLKLRSSFNFKPTRHDPVPFDPLVADMERRREDKEWERQYIEHSHPELVSHSQKETTGGGHEHAPGHESQPEWEEFMDAEDYLNDEEKFNVTDRLILLFPKIDVSPADGFMTESELTEWTMQSSAKEVVHRTQRDLDVHDRNKDGFISFSEYEPPSWVRKSDNNSFGYDMGWWKEEHFNASDANGDGLLNLTEFNDFLHPADTKNPKLLLWLCKEEVRERDSDKDGKISFEEFFHGLFDTVRNYEEDNHNSTHPYHDLPEGPAKQLFSQLDKNDDGYLSDVELLPIISKIHPTEHYYAKQQADYIISQADSDKDRRLTLAEMIEHPYVFYSAIFDEDDTDDDYGFHDEFR
Protein: Myosin-binding protein C, slow-type (Q5U3B1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPEPTKKDDGQPEEDGSTPKKLSIDLPNDSDPESTRGRKDSVWSLGDGQPPEEIDKQTENPPLSTLLIEKPQSGSITVGGDITFIAKVEAKDLLRKPTVKWFKGKWMDLASKTGKHLQLKESFERLSKIHTFEMHIIKAKENYAGNYRCEVTYKDKFDSCSFDLEVKEVPEVSQSIDIRSAFKRSSEGQDDAGELDFSGLLKHRHGREVKQEETPEVDVWEILKNARPDEYEKIAFTYGITDLRGLLKRLKKTKKEEKKSEAFAKRLEPAYQVDKGGKIRLIVDLADPTVELKWYKNGQEIRPTPNNRKFIFEHKGTQRIMVINNCQMSDDAAYSVTAGEEKCTTELFVKELPVNIVKELEPVKTTVNERIELECEVSEEGAKVKWMKNGVEVPTGVRSRYRVKSEGTKHWLIIDDASKDDTGTYSLMATGGTSQAHVQVDLKPLKVLMDLQSVTVLLGQPLKLNCEIYPGNVPGRWYKNGQLVQPNDRISITHKTKNHSLDVESSTIHDAGDYTFVPEGYTQTLSAKVHIIDPPRVHLEALNVQDNTVTIVAGNKLRLEIPISGEPAPRVVWMKGERVILDTGSRVHAETFADHTCLTIDITEREDTGNYKIVLQNEAGEDTASVKVKVVDIPDPPEAPLVTEVGGDWCTMTWEPPRYDGGSPILGYFIERKKKQSSRWMRLNFDLCKETTFEPKKMIEGVPYEVRIFAVNAIGVSKPSEPSKPFIPLAVTSEPTMLVVDDVTDTTVTMKWRPPDTIGAAGLDGYQIEYCIEGTDDWIVANKELTKKTKYTITGLPVEAKILVRVKAINAAGASQPRTTQHSILVKEVIEPPKIRIPRHLKQTYIRKVGEVVNLVVPFVGKPRPKVTWLKEGQPIDPTISIRNSDCDSIMFIRKAERKHSGKYELSVQVENHIDTAMLDIQIVDLPGPPQAVKIEEIWGNNVALDWSPPKDSGNAPITGYTIQKADKKTMEWYTCVEHYHRTCITISDLVVGNEYFFRIYSENMVGLSEDATATKDSALIVKEGLHLKNPEYNDRDFTEPPRFTQPLINTFAIAGYNATLNCSVRANPRPKVVWMKNKITIIDDPRYRMFHNQGVCTLEIRKPSPFDGGVYTCKAVNDLGEAQVDCKLEVKGGFTFFELMKRGVPLHLIDKYMNESKTSESEKKGSD
Protein: NEDD8-activating enzyme E1 regulatory subunit AXL (Protein AXR1-LIKE) (Protein AXR1-LIKE 1) (Q9ZV69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory subunit of the dimeric ECR1-AXL1 E1 enzyme. E1 activates RUB1/NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a RUB1-ECR1 thioester and free AMP. E1 finally transfers RUB1 to the catalytic cysteine of RCE1 (Probable). May function redundantly with AXR1 in the RUB conjugating pathway. Seems not to be functionally equivalent to AXR1 in vivo.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P42744}.
Interaction partners:
- NEDD8-activating enzyme E1 catalytic subunit
- Probable NEDD8-conjugating enzyme Ubc12-like
- NEDD8-conjugating enzyme Ubc12
- NEDD8-like protein RUB3
- F12F1.16 protein
- Ubiquitin-NEDD8-like protein RUB1
- NEDD8-specific protease 1
- Autophagy-related protein 3
- Cullin-1
- Molybdopterin synthase catalytic subunit
Sequence:
MAEPKTKYDRQLRIWGELGQSALETASICLLNCGPTGSEALKNLVIGGIGSITIVDGSKVEIGDLGNNFMVDAKSVGQSRAKTVCGFLQELNDSVKANFVEENPDTLISTDPSFFSQFTLVIATQLVEDSMVKLDRICREANVMLVLARSYGLTGFVRISVKEHTAIETKPDHSLDDLRLNSPWPELKSYVESIDLNVEEPAAHKHIPYVVILVKVAEEWAQHHSGNLPSTREEKNEFKDLVKSKMVSADEENYKEALLAAFKVFAPTGISQEIQDINHDSCAEVGSNSSDFWVMVAALKEFISNEGGGEVPLEGSMPDMISSTEHYINLQKIYHSKAEADFLSMEQRVKSILVKVGQDPSSISKPTIKSFCKNARKLKVCRYRTIEDEFKSPSTTELHKYLADENYSGAIGFYILLRAVDRFAGTYKKFPGQFDGSTDEDASQLKTIALSLLSEMGCDGYELQEELYNEMCRFGAAEIHVVAALIGGITSQEVIKLITKQFVPKRGTFIFNGIDHKSQSLTL