wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein (Q585V7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Endoplasmic reticulum oxidoreductin, putative
Sequence:
MVVTLVEPTKWANLIEEYPDTLYSSESAKNVENVLSKTSTRRHQKVLFNAAKPFMPKMIHDCIGTSILNSLVKYGTVTTVDGVCKIVFESCEKILRCRCSPENQRIESLGSLLERIVYRYDCLGNYRQNIIEVLKSLRPSQLMGTPVLLLAAARLLIQNRDFASLVLTNSEARTEFFSASLVRTNRGVVSAFCKILLSEDALKDGEMTGLCSAFIFDSFSGLYEPKATLRPMKDITLLLASCGSIDGVRNLGKSLARWPDIHGRAKGDDYAKIVAHILSRLPDTDSGLPLVKAVLHSEEDINDRLRCRKSSHLHLLASIAEKQSYVQVLSEALGTSVEKKLASAVVQYRRVTKPRVVSTKELLSRKLADMRKGSGENDSARNVSKRFREW
Protein: E3 ubiquitin-protein ligase KCMF1 (EC 2.3.2.27) (FGF-induced in gastric cancer) (Potassium channel modulatory factor) (PCMF) (ZZ-type zinc finger-containing protein 1) (Q9P0J7)
Organism: Homo sapiens (Human)
Function: Has intrinsic E3 ubiquitin ligase activity and promotes ubiquitination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:38297121}. Late endosome {ECO:0000269|PubMed:25582440}. Lysosome {ECO:0000269|PubMed:25582440}.
Interaction partners:
- E3 ubiquitin-protein ligase UBR4
- Ubiquitin-conjugating enzyme E2 A
Sequence:
MSRHEGVSCDACLKGNFRGRRYKCLICYDYDLCASCYESGATTTRHTTDHPMQCILTRVDFDLYYGGEAFSVEQPQSFTCPYCGKMGYTETSLQEHVTSEHAETSTEVICPICAALPGGDPNHVTDDFAAHLTLEHRAPRDLDESSGVRHVRRMFHPGRGLGGPRARRSNMHFTSSSTGGLSSSQSSYSPSNREAMDPIAELLSQLSGVRRSAGGQLNSSGPSASQLQQLQMQLQLERQHAQAARQQLETARNATRRTNTSSVTTTITQSTATTNIANTESSQQTLQNSQFLLTRLNDPKMSETERQSMESERADRSLFVQELLLSTLVREESSSSDEDDRGEMADFGAMGCVDIMPLDVALENLNLKESNKGNEPPPPPL
Protein: Auxin-responsive protein SAUR50 (Protein SMALL AUXIN UP-REGULATED RNA 50) (O65695)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Provide a mechanistic link between auxin and plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), and triggers PM H(+)-ATPases activity by promoting phosphorylation of their C-terminal autoinhibitory domain as a result of PP2C-D subfamily of type 2C phosphatases inhibition, thus leading to the acidification of the apoplast and the facilitation of solutes and water uptake to drive cell expansion (By similarity). Triggers plant growth probably by promoting cell elongation (By similarity). Regulates branch angles and bending (By similarity). Effector of hormonal and environmental signals in plant growth (Probable).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FJG1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9FJG1}.
Interaction partners:
- Auxin-responsive protein SAUR65
- AT5g20880/F22D1_50
- Auxin-responsive protein IAA4
- Auxin transporter protein 1
- TBCC domain-containing protein 1
- Auxin-responsive protein SAUR78
Sequence:
MAIMKKTSKLTQTAMLKQILKRCSSLGKKNGGGYDEDCLPLDVPKGHFPVYVGENRSRYIVPISFLTHPEFQSLLQRAEEEFGFDHDMGLTIPCDELVFQTLTSMIR
Protein: Unconventional myosin-VI (Unconventional myosin-6) (A0A8I5Y7N7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, microvillus {ECO:0000256|ARBA:ARBA00004105}. Cell projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004632}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane, clathrin-coated pit {ECO:0000256|ARBA:ARBA00004600}.
Interaction partners:
Sequence:
MEDGKPVWAPHPTDGFQMGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNVKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSDTIKSYQGKSLGTMPPHVFAIADKAFRDMKVLKMSQSIIVSGESGAGKTENTKFVLRYLTESYGTGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKEERNYHIFYRLCAGASEDIREKLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKSPEYVKAGSLKDPLLDDHGDFIRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSAPSLEYCAELLGLDQDDLRVSLTTRVMLTTAGGTKGTVIKVPLKVEQANSARDALAKTVYSHLFDHVVDRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEVKLVGILDILDEENRLPQPSDQHFTSVVHQKHKDHFRLTIPRKSKLAVHRNLRDDEGFIIRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRALFESSTNNNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKYMPEKLARLDPRLFCKALFKALGLNEVDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELVKRVNLWLVCSRWKKVQWCSLSVIKLKNKIKYRAEACIKMQKTIRMWLCKRRHKPRIDGLVKVGTLKKRLDKFNEVVSALKDGKPEVNRQIKDLEISIDALMAKIKSTMMTREQIQKEYDALVKSSEDLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEQRRRKEEEERRMKLEMEVKRKQEEEERKKREDDEKRIQAEVEAQLARQREEESQQQAVLAQECRDRELALRIAQNESELISDEAQGDTALRRYWALGCTLEQMAKEMSDILSRGPAVQATKAAAGTKKHDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNKKRNTETEQRAPKSVTDYAQQNPAAQLPARQQEIEMNRQQRFFRIPFIRPADQYKDPQNKKKGWWYAHFDGPWIARQMELHPDKPPILLVAGKDDMEMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQSAIESRQARPTYATAMLQNLLK
Protein: Secreted protein (Q9TY06)
Organism: Caenorhabditis elegans
Interaction partners:
- Apoptosis regulator ced-9
- Programmed cell death activator egl-1
- Cell death protein 3
- Transcription factor cep-1
Sequence:
MMSYKRDGYFSIVSSCLIFCLHFLPLLSIRTKLSSLFITSLANNACNSNTVEYNIGRKLTVMCDEFDSELMSYKEEKSFVKFLGSGFKTYASIVRRVF
Protein: CAP-Gly domain-containing linker protein 3 (Cytoplasmic linker protein 170-related 59 kDa protein) (CLIP-170-related 59 kDa protein) (CLIPR-59) (B9EHT4)
Organism: Mus musculus (Mouse)
Function: Functions as a cytoplasmic linker protein. Involved in TGN-endosome dynamics. May modulate the cellular compartmentalization of AKT kinase family and promote its cell membrane localization, thereby playing a role in glucose transport in adipocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Note=Localized to Golgi stacks as well as on tubulovesicular elements juxtaposed to Golgi cisternae. {ECO:0000250}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase CYLD
Sequence:
MTKTDPAPMAPPPRGEEEEEEEEDEPVPEAPSPTQERRQKPVVHPSAPAPLPKDYAFTFFDPNDPACQEILFDPKTTIPELFAIVRQWVPQVQHKIDVIGNEILRRGCHVNDRDGLTDMTLLHYACKAGAHGVGDPAAAVRLSQQLLALGADVTLRSRWTNMNALHYAAYFDVPDLVRVLLKGARPRVVNSTCSDFNHGSALHIAASNLCLGAAKCLLEHGANPALRNRKGQVPAEVVPDPMDMSLDKAEAALVAKELRTLLEEAVPLSCTLPKVTLPNYDNVPGNLMLSALGLRLGDRVLLDGQKTGTLRFCGTTEFASGQWVGVELDEPEGKNDGSVGGVRYFICPPKQGLFASVSKVSKAVDAPPSSVTSTPRTPRMDFSRVTGKGRREHKGKKKSPSSPSLGSLQQREGAKAEVGDQVLVAGQKQGIVRFYGKTDFAPGYWYGIELDQPTGKHDGSVFGVRYFTCAPRHGVFAPASRIQRIGGSTDPPGDSVGAKKVHQVTMTQPKRTFTTVRTPKDIASENSISRLLFCCWFPWMLRAEMQS
Protein: DNA ligase (EC 6.5.1.1) (A0A0C4DGV9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRLILPQLERERMAYGIKETMLAKLYIELLNLPRDGKDALKLLNYRTPTGTHGDAGDFAMIAYFVLKPRCLQKGSLTIQQVNDLLDSIASNNSAKRKDLIKKSLLQLITQSSALEQKWLIRMIIKDLKLGVSQQTIFSVFHNDAAELHNVTTDLEKVCRQLHDPSVGLSDISITLFSAFKPMLAAIADIEHIEKDMKHQSFYIETKLDGERMQMHKDGDVYKYFSRNGYNYTDQFGASPTEGSLTPFIHNAFKADIQICILDGEMMAYNPNTQTFMQKGTKFDIKRMVEDSDLQTCYCVFDVLMVNNKKLGHETLRKRYEILSSIFTPIPGRIEIVQKTQAHTKNEVIDALNEAIDKREEGIMVKQPLSIYKPDKRGEGWLKIKPEYVSGLMDELDILIVGGYWGKGSRGGMMSHFLCAVAEKPPPGEKPSVFHTLSRVGSGCTMKELYDLGLKLAKYWKPFHRKAPPSSILCGTEKPEVYIEPCNSVIVQIKAAEIVPSDMYKTGCTLRFPRIEKIRDDKEWHECMTLDDLEQLRGKASGKLASKHLYIGGDDEPQEKKRKAAPKMKKVIGIIEHLKAPNLTNVNKISNIFEDVEFCVMSGTDSQPKPDLENRIAEFGGYIVQNPGPDTYCVIAGSENIRVKNIILSNKHDVVKPAWLLECFKTKSFVPWQPRFMIHMCPSTKEHFAREYDCYGDSYFIDTDLNQLKEVFSGIKNSNEQTPEEMASLIADLEYRYSWDCSPLSMFRRHTVYLDSYAVINDLSTKNEGTRLAIKALELRFHGAKVVSCLAEGVSHVIIGEDHSRVADFKAFRRTFKRKFKILKESWVTDSIDKCELQEENQYLI
Protein: Flavin-dependent halogenase armH3 (EC 1.14.19.-) (A0A0U2JT80)
Organism: Armillaria mellea (Honey mushroom) (Agaricus melleus)
Function: Flavin-dependent halogenase involved in the biosynthesis of melleolides, a range of antifungal and phytotoxic polyketide derivatives composed of an orsellinic acid (OA) moiety esterified to various sesquiterpene alcohols. The halogenase catalyzes the transfer of a single chlorine atom to the melleolide backbone, resulting in a 6'-chloromelleolide product. The enzyme acts on free substrate and does not depend on carrier-protein-dependent acceptor molecules.
Interaction partners:
Sequence:
MEAQVPLSTDILVIGGGPAGSYAAAVLAREGFKVVLLEKDVFPRYHIGESMLPSCRPFLRFIDFEEKMKNYGFFPKPGAALKLNQDKREGYTDFTANGPDNAAWNVVRSEFDDLLLRHAAELGVHVYEGVQVEKIHFSPDESTRPVSLAWSKGDGTQGDVSFNWLVDASGRNGIMSTRYLKNRTFNKSLKNVAVWGYWTGAGRYAPGTKRENAPWFEALTDETGWAWFIPLHNGATSVGVVLAEDESKRKKAQHRAESNGKSLSEVQHDCYMADLQRAPGLIQLLGSEAKFEGKLMSAGDYSYHASEYAGSHFRIAGDAGAFIDPFFSSGIHLALTGGLSAASTIAASIRGNCTEEEACAFHSSKVETAYTRFLFVVLGIYKQIRAQETAVLYEAEEDNFDRAIDSLRPVIQGCADADENLTEAELQSTLDFCRSVLAPNQQQNNLRTPVDTGAADVKAKHAPSETDAQNPLQSMDDCKRNFGTEVINGFYVKMEQGMLGLVCA
Protein: Stannin (AG8_1) (O75324)
Organism: Homo sapiens (Human)
Function: Plays a role in the toxic effects of organotins. Plays a role in endosomal maturation.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:15269288, ECO:0000269|PubMed:16246365}; Single-pass membrane protein {ECO:0000269|PubMed:16246365}.
Interaction partners:
Sequence:
MSIMDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLMTPNGPEVHG
Protein: Succinate dehydrogenase subunit 5, mitochondrial (Q0JDA2)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Succinate dehydrogenase subunit 7
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Succinate dehydrogenase subunit 4
- Succinate dehydrogenase subunit 8A
- Succinate dehydrogenase subunit 6
- Succinate dehydrogenase subunit 3-2
- Succinate dehydrogenase subunit 3-1
- Succinate dehydrogenase subunit 8B
Sequence:
MAAALRSSCAAARRLLRISPAALSTLTAASSRPAAVAPLARPIAAAAVSGGNNAFSWNLRRLFSSNEKHLPAISDPEVESAFKDLMAASWTGLPDSLVIEAKKAASKATDDKAGKEALLNVFRAAEACEEFGGVLVTLRMALDDLCGITGENVGPLPGYIEDAVKSAYKRYMKYLESFGPEENYLRKKVENELGTKMIHLKMRCSGVGSEWGKITLIGTSGISGSYVELRA
Protein: Lariat debranching enzyme (EC 3.1.4.-) (Intron debranching enzyme) (RNA lariat debranching enzyme) (C4M1P9)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Function: Cleaves the 2'-5' phosphodiester linkage at the branch point of excised lariat intron RNA and converts them into linear molecules that can be subsequently degraded, thereby facilitating ribonucleotide turnover.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:30023353}. Note=In trophozoites, appears to localize to the cytoplasmic side of the nucleus concentrating on the basal region. {ECO:0000269|PubMed:30023353}.
Interaction partners:
- RNA helicase
- Cwf19-like C-terminal domain-containing protein
- RNA helicase
Sequence:
MATEQIQHIAIVGCVHGKYREMYRQLSEYEKSTGKEISFVICTGDMQTLRYEADLVYLKVPPKYKQMGDFHLYYEGKEKAPYLTLFIGGNHESSNVLLHLYNGGFVCFNMYYLGVCSCININGLRIVGVSGIYKSFDEKKPYTYPPSPNDVVSLFHTRNYVIQMLSNLSQSSQIDISLSHDWPQGIVMKGNYKQLYRFQPGFKKDGASLGSPINKVILNTLKPKYWISGHMHCEYHAEEGPTHFIALGKIGYKNAISYLDLPLKQKTDLEYDKDWVCNLIMTWPAFSNKAQFPDLSYSISELLSKRTKELDKKIIELWEKYIGLKIIYDSDTFDIQFTSRRFYIEKIYNELNIN
Protein: Clathrin light chain (CLC) (P17891)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi. The yeast light chain is important for cell growth. The light chain may help to properly orient the assembly/ disassembly of the clathrin coats.
Subcellular location: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and vesicles.
Interaction partners:
- Clathrin heavy chain
- Protein SLA2
- Epsin-3
- Epsin-5
- EH domain-containing and endocytosis protein 1
- AP-1 complex subunit beta-1
- AP-1 complex subunit mu-1-I
- AP-2 complex subunit alpha
- Actin cytoskeleton-regulatory complex protein PAN1
- AP-2 complex subunit sigma
Sequence:
MSEKFPPLEDQNIDFTPNDKKDDDTDFLKREAEILGDEFKTEQDDILETEASPAKDDDEIRDFEEQFPDINSANGAVSSDQNGSATVSSGNDNGEADDDFSTFEGANQSTESVKEDRSEVVDQWKQRRAVEIHEKDLKDEELKKELQDEAIKHIDDFYDSYNKKKEQQLEDAAKEAEAFLKKRDEFFGQDNTTWDRALQLINQDDADIIGGRDRSKLKEILLRLKGNAKAPGA
Protein: Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) (SAICAR synthetase) (P9WHN1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Phosphoribosylamine--glycine ligase
- Adenylosuccinate lyase
- N5-carboxyaminoimidazole ribonucleotide mutase
- Bifunctional purine biosynthesis protein PurH
- Phosphoribosylglycinamide formyltransferase
- N5-carboxyaminoimidazole ribonucleotide synthase
- Phosphoribosylformylglycinamidine cyclo-ligase
- Phosphoribosylformylglycinamidine synthase subunit PurL
- Amidophosphoribosyltransferase
- Phosphoribosylformylglycinamidine synthase subunit PurQ
Sequence:
MRPALSDYQHVASGKVREIYRVDDEHLLLVASDRISAYDYVLDSTIPDKGRVLTAMSAFFFGLVDAPNHLAGPPDDPRIPDEVLGRALVVRRLEMLPVECVARGYLTGSGLLDYQATGKVCGIALPPGLVEASRFATPLFTPATKAALGDHDENISFDRVVEMVGALRANQLRDRTLQTYVQAADHALTRGIIIADTKFEFGIDRHGNLLLADEIFTPDSSRYWPADDYRAGVVQTSFDKQFVRSWLTGSESGWDRGSDRPPPPLPEHIVEATRARYINAYERISELKFDDWIGPGA
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 (Complex I-B8) (CI-B8) (NADH-ubiquinone oxidoreductase B8 subunit) (Q02370)
Organism: Bos taurus (Bovine)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:10852722, ECO:0000305|PubMed:18721790}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
Sequence:
MAAAAAIRGVRGKLGLREIRIHLCQRSPGSQGVRDFIEKRYVELKKANPDLPILIRECSDVQPKLWARYAFGQEKNVSLNNFSADQVTRALENVLSSKA
Protein: Adipogenesis regulatory factor (Adipogenesis factor rich in obesity) (Adipose most abundant gene transcript 2 protein) (Adipose-specific protein 2) (apM-2) (Q15847)
Organism: Homo sapiens (Human)
Function: Plays a role in fat cell development; promotes adipogenic differentiation and stimulates transcription initiation of master adipogenesis factors like PPARG and CEBPA at early stages of preadipocyte differentiation. Its overexpression confers resistance to the anticancer chemotherapeutic drug cisplatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:23239344}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma
Sequence:
MASKGLQDLKQQVEGTAQEAVSAAGAAAQQVVDQATEAGQKAMDQLAKTTQETIDKTANQASDTFSGIGKKFGLLK
Protein: Transcriptional activator RocR (Arginine utilization regulatory protein RocR) (P38022)
Organism: Bacillus subtilis (strain 168)
Function: Positive regulator of arginine catabolism. Controls the transcription of the two operons rocABC and rocDEF and probably acts by binding to the corresponding upstream activating sequences.
Interaction partners:
- RNA polymerase sigma-54 factor
- Catabolic NAD-specific glutamate dehydrogenase RocG
- Ornithine aminotransferase
- Sporulation initiation phosphotransferase F
- Uncharacterized EAL-domain containing protein YkuI
- Arginase
- Protein RocB
- Amino-acid permease RocC
- 1-pyrroline-5-carboxylate dehydrogenase
Sequence:
MVKDSEFLTLVFQSILDEIDVGLHVVDEHGNTIVYNNKMMQIEDMEKHDVLNKNLMDVFMFSKQQDSTLVQALQEGKTIKNVKQSYFNNKGQEITTINHTYPIVQDGKIRGAVEIAKDVTKLERLIRENMNKKGSTTYTFDSILGTSPAIQDVIENAKRATRTSSSVLLAGETGTGKELFAQSIHNGSDRSGGPFISQNCAALPDSLVESILFGTKKGAFTGAVDQPGLFEQAHGGTLLLDEINSLNLSLQAKLLRALQERKIRRIGSTKDTPIDVRIIATMNEDPIDAIAGERMRKDLYYRLSVVTLIIPPLRERKEDILLLASEFIQKNNHLFQMNVEHISDDVKQFFLSYDWPGNIRELEHMIEGAMNFMTDEQTITASHLPYQYRMKIKPADIPEPETPRHQPAADLKEKMESFEKYVIENVLRKHGHNISKAAQELGISRQSLQYRLKKFSHSSNE
Protein: Serine/threonine protein kinase, putative (EC 2.7.1.-) (Q580I6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
TAAAATAKYLNRSDREVRAAIREGRGEAFVAYSIIFDAEQRKILRNGADEILNKETTEMGCTTYGTELTHVPRATERELHLGLLLTQSPVMESLLGNGDVSSNKHAYNGSNFVPASMRETHHGAATAAATPPNPGGVFFIGKRADSYAETSGTLDSSYREDCGSTNPIDEARPGCSRDSKSRLSSGNTERQRVGSVAKSDVIYTREEREFIVKNNVGWRIGLMADLTSSGVMRVVYEVLKRYAMEWKSPTSFELLVRPTAVTFERIYNPLRETSSWDSAEDEGLQHTQQKRADRVLQVVILIHLFRIRESHDDGYILDFSVLKGSVIALDIVRCLFCTLVQKLA
Protein: Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase (EC 3.6.1.13) (EC 3.6.1.16) (EC 3.6.1.53) (ADPRibase-Mn) (CDP-choline phosphohydrolase) (Q7T291)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP-choline and CDP-ethanolamine, but not other non-reducing ADP-sugars or CDP-glucose.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 1
- ADP-sugar pyrophosphatase
- Phosphoglucomutase-2
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate acyltransferase 2
- Glycerol-3-phosphate dehydrogenase 1-like protein
Sequence:
MEDPVFTFGLIADVQYADIEDGENYLRTRRRYYRGSADLLRDAVLQWRRERVQCVVQLGDIIDGHNRRRDASDRALDTVMAELDACSVDVHHVWGNHEFYNFSRPSLLSSRLNSAQRTGTDTGSDLIGDDIYAYEFSPAPNFRFVLLDAYDLSVIGREEESEKHTHSWRILTQHNHNLQDLNLPPVSVGLEQRFVKFNGGFSEQQLQWLDAVLTLSDHKQERVLIFSHLPVHPCAADPICLAWNHEAVLSVLRSHQSVLCFIAGHDHDGGRCTDSSGAQHITLEGVIETPPHSHAFATAYLYEDRMVMKGRGRVEDLTITYS
Protein: Chaplin-H (Q9AD92)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: One of 8 partially redundant surface-active proteins required for efficient formation of aerial mycelium; the short chaplins assemble into a hydrophobic, amyloidal fibrillar surface layer that envelopes and protects aerial hyphae and spores, presumably anchored to the long chaplins. Chaplins have an overlapping function with the surface-active SapB peptide; chaplins are essential on minimal medium while on rich medium both chaplins and SapB are required for efficient aerial hyphae formation. Chaplins are also involved in cell attachment to a hydrophobic surface. Forms amyloid fibrils in vitro probably composed of stacked beta-sheets. A small chaplin extract (ChpD, ChpE, ChpF, ChpG and ChpH) self-assembles into 2 different amyloids; small fibrils at the air-water interface form an amphipathic membrane that resembles spore-surface structures involved in aerial hyphae formation, and hydrophilic fibrils in solution that resemble the fibers that attach cells to a hydrophobic surface. At the air-water interface the hydrophilic surface is in contact with water (probably equivalent to the peptidoglycan layer), while the hydrophobic face is exposed to the air, making the surface of the aerial hyphae hydrophobic. A minimal chaplin strain capable of forming aerial mycelium/hyphae on minimal medium contains ChpC, ChpE and ChpH. The strain also has restored rodlet formation on the hyphae surface. A small chaplin extract applied to a chaplin-deficient strain restores aerial hyphae formation. The small chaplin extract forms an amyloid-like structure similar to that seen on the surface of cells without rodlets (rdlA-rdlB deletions), and is highly surface active, reducing surface tension from 72 to 26 mJ/m(2), which probably allows escape of hyphae from an aqueous environment into air.
Subcellular location: Cell surface {ECO:0000269|PubMed:12832396, ECO:0000269|PubMed:12832397, ECO:0000305|PubMed:17462011}. Secreted, cell wall {ECO:0000269|PubMed:12832396, ECO:0000269|PubMed:12832397, ECO:0000269|PubMed:21526199, ECO:0000269|PubMed:21628577}. Fimbrium {ECO:0000269|PubMed:19682261}.
Interaction partners:
- Rodlin protein RdlA
- Rodlin protein RdlB
- Peptidase
- Chaplin-C
Sequence:
MLKKVVAAAAATGGLVLAGAGMAVADSGAQGAAVHSPGVLSGNVVQVPVHVPVNVCGNTISVIGLLNPAFGNVCINK
Protein: Ethylene-responsive transcription factor ERF086 (Q6J9Q2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity). Involved in the control of cell division patterns during the early lateral root primordium development. Acts downstream of auxin signaling. Regulated by ARF7 and ARF19 in response to auxin. Co-acts with LBD16 and LBD18 to control lateral root development. Involved in the determination of floral meristem identity and suppression of bract growth. Required for proper conversion of secondary inflorescences to flowers. Acts together with NPR5/BOP2 and NPR6/BOP1 to promote expression of LFY and AP1, two central regulators of floral meristem identity.
Subcellular location: Nucleus {ECO:0000269|PubMed:17630277}.
Interaction partners:
- LOB domain-containing protein 16
- LOB domain-containing protein 18
- Translationally controlled tumor protein 2
- Auxin response factor 19
Sequence:
MSTSKTLDHNKPFETSQTQMGFALIHQNTSANTTTTTTTGERRGRRSKQAEPGRFLGVRRRPWGRYAAEIRDPTTKERHWLGTFDTAHEAALAYDRAALSMRGTQARTNFVYTPTDVHTILTNPNLHSLIVSPYNNNQSFLPNSSPQFVIDHHPHYQNYHQPQQPKHTLPQTVLPAASFKTPVRHQSVDIQAFGNSPQNSSSNGSLSSSLDEENNFFFSLTSEEHNKSNNNSGYLDCIVPNHCLKPPPEATTTQNQAGASFTTPVASKASEPYGGFSNSYFEDGEMMMMNHHEFGSCDLSAMITNYGAAAASMSMEDYGMMEPQDLSSSSIAAFGDVVADTTGFYSVF
Protein: Stage IV sporulation protein A (EC 3.6.1.-) (Coat morphogenetic protein SpoIVA) (Q182W3)
Organism: Clostridioides difficile (strain 630) (Peptoclostridium difficile)
Function: ATPase. Has a role at an early stage in the morphogenesis of the spore coat and is required for proper coat localization to the forespore.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P35149}. Note=Localized on spore coat surrounding the forespore. {ECO:0000250|UniProtKB:P35149, ECO:0000269|PubMed:23292781}.
Interaction partners:
- Stage III sporulation protein AA
- Stage III sporulation protein D
- Stage 0 sporulation protein A homolog
- Stage II sporulation protein P
- Pro-sigma
- RNA polymerase sigma factor
- Stage II sporulation protein D
- RNA polymerase sigma factor
- Stage III sporulation protein AD
- Anti-sigma F factor
Sequence:
MNNNIYEDISKRTQGDIYIGVVGPVRTGKSTFIRKFMEKLVIPNIDNEFKKDRTRDEIPQSGSGKTIMTVEPKFVPADGVEIKIKDTVSLKVRMVDCVGYIVEGALGHEEGGKQRLVSTPWSQEAMTFEKAAEIGTKKVIKDHSTIGIVVLTDGSVTGIDRKSYVEPEERVIQELKNLKKPFAVVLNTLSPKSEETSMLRSELEEKYEVPVLPMNVVEMEEEDIEEVMEAVLYDFPLTEIRINLPKWVEGLERNHWIKSSIITTLKQSIIDIGKIRDIEGIIQGFSELEFLEDTGVDNVELGEGVINIDLQTKQDLFYNVLEEKSGFKIEGDYQLLSLITRLSKVKNEYDKIESALIDAKIKGYGVVAPSLEELSLEEPEIMKQGKQYGIKLKANAPSLHIIKADISTEVSPIVGNQNQGEEMIKYLMEVFEEQPADLWESNMFGKSLHDLVKEQLQSKLYTMPEEIRVKMQKTLQKIVNEGSSNIITILL
Protein: Phosphodiesterase (EC 3.1.4.-) (A0A1D8PCV9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- 3'\5'-cyclic-nucleotide phosphodiesterase PDE1
- Adenylate cyclase
- Adenosine kinase
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
- Adenylate kinase
- GTP:AMP phosphotransferase, mitochondrial
- AMP deaminase
- Adenine phosphoribosyltransferase
- cAMP-dependent protein kinase regulatory subunit
Sequence:
MAEVLSLVDLEIPQVTDKYYKFDTFKHLICHLFKKTSTETDSNVPIVIIFPTNNDIPSRKTRSTTTTTTTTTTTNTSKLDNLPFSDKSLLIQFFFTHLNILMIQGENSDEGKLYQEISSAKELLTNRISRVGNWTGTTHFRYCRHENDCGLLNQHSKIAGIIPTMTYILNCNATRSEIATNQLIYLYRLMIEEINFIELLQDASTTRLSQLCYAVGHWSFPAHNLSNDDLVYCVYLMIDYAIKQVEGFDNIPLNELLAFIFIVRDTYKNGNPFHNFRHAVDVLQACFHFLIRLGSLPKFKQFVEDPKLDYTEVHDTHTVLIALQNNSSEEKASLNPIQTLGLLVAALGHDVGHPGTTNDFMIKFSAPTALLYNDRSVLESYHASLFINKVLRICWPDLLTCTIEEKSELTIRSLIISSILATDMGEHNEYVNRLKSFKTHNEILNHDNTVKLISALLIKCADISNVTRPLRVSAQWAMVLSREFAEVELLKSVIKKDIDLDFTKDLTYDHVPHELREILEIQPDIHKGQIFFINLFAENLFNSVSDLLPQLQYTCDIIMENKLFWLERAKK