wanglab/gogpt-training-data huggingface dataset:
Protein: Transcriptional regulator (Q7MD38)
Organism: Vibrio vulnificus (strain YJ016)
Interaction partners:
Sequence:
MGSPKNLLVRLRSNMEPFSKKLRVVADYILENAHDVQFQTITDLARNTQTSEATVVRLCRDMGYKGYSDFRMALAVDLSQTESRQQNHIEGDICDVSAQSAVDSLQDTAKLIDRKSLARIVERVHQAEFIGCIGVGASSIVGRYLAYRLIRIGKKAIMFEDTHLAAMSASRSSQGDLWFAVSSSGSTKEVIHAAGLAYKRDIPVVSLTNINHSPLSSLSTEMLVAARPEGPLTGGAFASKVGALLLVDVLVNSLLESYPEYKDSVQETAEVVIPLMAN
Protein: 5-OH-xanthotoxin synthase (EC 1.14.14.-) (Cytochrome P450 CYP71AZ1) (D2CGS0)
Organism: Ammi majus (Bishop's weed)
Function: Involved in the biosynthesis of coumarins and furanocoumarins (FCs), natural products required for defense responses against attacks by predators with potential medical and agroindustrial usages such as anticoagulant, rodenticide and artificial vanilla substitutes. Catalyzes the conversion of xanthotoxin into 5-hydroxyxanthotoxin.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:Q6QNI4}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MQMDAVVILLILAFPIASVYVLFYHKKRVDGLSEPPGPPGLPFIGNFYQLYKAPCIHEYLCTLSKRYGSLMTLRMGSVPILVVSSPKMAKEVLKTQDLAYCSRPMMTGMQKLSYNGLDVAFSPYSEHWRQVRKFCTLELFTQKRAQIDFRHVHEQEVSRMIARLSETAAASKDVNAFECFSNLATSIISRVAFGKRHDEDGIGKERLQRMLSELDTMLSVYFVSDFFPMFGWIDSLTGMRARLDRTFKEMDMFYEELIDDHLKPDRPESLTEDIIDVMLKNKGCSSSSLTKDTMKAILLNVFNGGTGTSASLLVWAMTALMRNRGVMKKVQEEIRSVIGKKGNVDEDDIQNLPYLRAVVKETMRLYPTGALLIPRKTIESSIIGEDKDHMYMIKPKTLVYVSMWAIGRDPEIWKNPMKFVPERFLERHDINYQGQQFEYIPFGAGRRICPGIHLGLTTVELALANLLYTFNWEPPVGTRFEDINDETVNGITLQKKNALYIRPKTYMFS
Protein: Metabotropic glutamate receptor 5 (mGluR5) (P41594)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system and generates a calcium-activated chloride current. Plays an important role in the regulation of synaptic plasticity and the modulation of the neural network activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25042998, ECO:0000269|PubMed:7908515}; Multi-pass membrane protein {ECO:0000269|PubMed:25042998, ECO:0000269|PubMed:7908515}.
Interaction partners:
- Homer protein homolog 1
- Guanine nucleotide-binding protein G
- Metabotropic glutamate receptor 1
- Adenosine receptor A2a
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Homer protein homolog 2
- Major prion protein
- Muscarinic acetylcholine receptor M1
- Muscarinic acetylcholine receptor M5
- SH3 and multiple ankyrin repeat domains protein 1
Sequence:
MVLLLILSVLLLKEDVRGSAQSSERRVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRDSLISSEEEEGLVRCVDGSSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPETNHRNPWFQEFWQHRFQCRLEGFPQENSKYNKTCNSSLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLCDAMKPIDGRKLLESLMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDDEVWSKKSNIIRSVCSEPCEKGQIKVIRKGEVSCCWTCTPCKENEYVFDEYTCKACQLGSWPTDDLTGCDLIPVQYLRWGDPEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCMFVPKVYIILAKPERNVRSAFTTSTVVRMHVGDGKSSSAASRSSSLVNLWKRRGSSGETLRYKDRRLAQHKSEIECFTPKGSMGNGGRATMSSSNGKSVTWAQNEKSSRGQHLWQRLSIHINKKENPNQTAVIKPFPKSTESRGLGAGAGAGGSAGGVGATGGAGCAGAGPGGPESPDAGPKALYDVAEAEEHFPAPARPRSPSPISTLSHRAGSASRTDDDVPSLHSEPVARSSSSQGSLMEQISSVVTRFTANISELNSMMLSTAAPSPGVGAPLCSSYLIPKEIQLPTTMTTFAEIQPLPAIEVTGGAQPAAGAQAAGDAARESPAAGPEAAAAKPDLEELVALTPPSPFRDSVDSGSTTPNSPVSESALCIPSSPKYDTLIIRDYTQSSSSL
Protein: Alanine aminotransferase 1 (ALT1) (EC 2.6.1.2) (Glutamate pyruvate transaminase 1) (GPT 1) (Glutamic--alanine transaminase 1) (Glutamic--pyruvic transaminase 1) (Q8QZR5)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- Putative aspartate aminotransferase, cytoplasmic 2
- Alanine--glyoxylate aminotransferase
- Glutamate dehydrogenase 1, mitochondrial
- N-acetylglutamate synthase, mitochondrial
- Alanine aminotransferase 2
- Isocitrate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
Sequence:
MASQRNDRIQASRNGLKGKVLTLDTMNPCVRRVEYAVRGPIVQRALELEQELRQGVKKPFTEVIRANIGDAQAMGQRPITFFRQVLALCVYPNLLSSPDFPEDAKRRAERILQACGGHSLGAYSISSGIQPIREDVAQYIERRDGGIPADPNNIFLSTGASDAIVTMLKLLVAGEGRARTGVLIPIPQYPLYSAALAELDAVQVDYYLDEERAWALDIAELRRALCQARDRCCPRVLCVINPGNPTGQVQTRECIEAVIRFAFEEGLFLMADEVYQDNVYAEGSQFHSFKKVLTEMGPPYATQQELASFHSVSKGYMGECGFRGGYVEVVNMDAEVQKQMAKLMSVRLCPPVPGQALMGMVVSPPTPSEPSFKQFQAERQEVLAELAAKAKLTEQVFNEAPGIRCNPVQGAMYSFPQIQLPLKAVQRAQDLGLAPDMFFCLCLLEETGICVVPGSGFGQQEGTYHFRMTILPPMEKLRVLLEKLRHFHAKFTHEYS
Protein: Periplasmic serine endoprotease DegP (EC 3.4.21.107) (Heat shock protein DegP) (Protease Do) (P0C0V0)
Organism: Escherichia coli (strain K12)
Function: DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolytic activity is essential for the survival of cells at elevated temperatures. It can degrade IciA, Ada, casein, globin and PapA. DegP shares specificity with DegQ. DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:9083020}; Peripheral membrane protein {ECO:0000269|PubMed:9083020}; Cytoplasmic side {ECO:0000269|PubMed:9083020}.
Interaction partners:
- Outer membrane porin C
- Outer membrane protein A
- FKBP-type peptidyl-prolyl cis-trans isomerase FkpA
- Outer membrane porin F
- Chaperone SurA
- Chaperone protein Skp
- Outer membrane protein assembly factor BamA
- Thiol:disulfide interchange protein DsbA
- Chaperone protein DnaK
- Anti-sigma-E factor RseA
Sequence:
MKKTTLALSALALSLGLALSPLSATAAETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ
Protein: Corolla, isoform A (LD15362p) (Q9VX37)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI02132p
- Uncharacterized protein
- Corona
Sequence:
MEKYPLVKEFMGQNWPKDTKMAQLEKELKKRKELIVEEQIVGPRLEQVLFDLTLVKQCALVVEDNGAGMAQANTMIQDCMFQITRIEELLEMAGLQDILYYTVHRKEQEFQRKIKLQEDLAEQENQQNTILESRSIVQEFRKEQALKKEADKELASVDDQLDQSDREWTITLRSMTDKLNKKIVSVLQMGKLINELKEELQKRNLIKTGVTKGAEPSLAGVPSASTISPFQSASDFLNNFIFKNIRPDDNKSMTSVNREITTKKLETPLRSILIKCKEVESVAISNSPTKQVRFSPYPEISHIEEEKFEKTDWLSPSEEAGVPNAELEEDSDEMEATDEDFEEISEEEFEMALKDEGFEQEVKVEKSEEVLHLEQDRYDEKSGSEVEESVSDDKESGGEASGEEEPADAAKQVKIGENPKTDEQLSNEISDKPQIIRVDTLSPFKNISSWASDDIPSTSKGTLNRFTATQFMNYGSNRDENEAPPCKRLKLEEEEFPMSQPMPDYFKHPSSTFNNFDDQSLRFSSPHNNFDDDYLLNFSDDNDVTPTAASAYIL
Protein: ATP synthase subunit alpha (EC 7.1.2.2) (ATP synthase F1 sector subunit alpha) (F-ATPase subunit alpha) (Q72E02)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
Interaction partners:
- ATP synthase epsilon chain
- ATP synthase subunit a
- ATP synthase subunit beta
- ATP synthase subunit b
- ATP synthase F0, B' subunit, putative
- ATP synthase subunit delta
- ATP synthase subunit c
- ATP synthase gamma chain
- WbqC-like family protein
- Succinate--CoA ligase subunit alpha
Sequence:
MQIKAEEISKIIEEQIQSYEQRVEMSETGTVLYVGDGIARVHGVQNAMAMELLEFPGGLMGMVLNLEEDNVGVALLGDDTQIKEGDPVKRTGKIFSVPVGDAVMGRVLNPLGQPIDGLGPLDAKEFRPVELKAPGIIARKSVHEPMPTGIKAIDAMTPIGRGQRELVIGDRQTGKTAVCIDAILAQKNTDIHCFYVAIGQKKATVALVADTLRKYGAMEYTTIISATASEPAPLQFISAYSGCTMAEFYRNNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKVNDSLGAGSLTALPIIETQAGDVSAYIPTNVISITDGQVYLEPNLFNAGIRPAINVGLSVSRVGGAAQIKAMKQVAGTMRLDLAQYRELAAFAQFGSDLDKATKAKLDRGARLVELLKQPQYEPMPTEEQVASMYAATRGLMDDVAVADIRKFETAMLDYLRSGKADILNDIKTKKALDQDIENRLKAAIAEFKKGYQA
Protein: Isomerase prhC (EC 5.-.-.-) (Paraherquonin biosynthesis cluster protein C) (A0A1E1FFL1)
Organism: Penicillium brasilianum
Function: Isomerase; part of the gene cluster that mediates the biosynthesis of paraherquonin, a meroterpenoid with a unique, highly congested hexacyclic molecular architecture. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase prhL (By similarity). Synthesis of DMOA is followed by farnesylation by the prenyltransferase prhE, methylesterification by the methyl-transferase prhM, epoxidation of the prenyl chain by the flavin-dependent monooxygenase prhF, and cyclization of the farnesyl moiety by the terpene cyclase prhH, to yield the tetracyclic intermediate, protoaustinoid A (By similarity). The short chain dehydrogenase prhI then oxidizes the C-3 alcohol group of the terpene cyclase product to transform protoaustinoid A into protoaustinoid B. The FAD-binding monooxygenase prhJ catalyzes the oxidation of protoaustinoid B into preaustinoid A which is further oxidized into preaustinoid A1 by FAD-binding monooxygenase phrK. Finally, prhA leads to berkeleydione via the berkeleyone B intermediate. PrhA is a multifunctional dioxygenase that first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione. Berkeleydione serves as the key intermediate for the biosynthesis of paraherquonin as well as many other meroterpenoids (Probable). The cytochrome P450 monooxygenases prhB, prhD, and prhN, as well as the isomerase prhC, are probably involved in the late stage of paraherquonin biosynthesis, after the production of berkeleydione (Probable). Especially prhC might be a multifunctional enzyme that catalyzes the D-ring expansion via intramolecular methoxy rearrangement, as well as the hydrolysis of the expanded D-ring (Probable).
Interaction partners:
Sequence:
MASNSTREKLIALAHKFCSIISSGDMEAVLALRTESCLTYQCCPSFSTRPLNNQETREYFEEWKHIGWNSKFWIIDEGTMVVDEAAKKIAFRAACSADTIGGPYENENLVILQATDDCALVDGIWEFFDAVRKQDLMNRLAAKQAAKGLDSWCANTHSGDDKGVPANNESKVAA
Protein: Antitoxin VapB30 (P9WJ35)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin VapC30.
Interaction partners:
- Ribonuclease VapC30
- Ribonuclease VapC42
- Ribonuclease VapC28
- Ribonuclease VapC36
- Putative ribonuclease VapC34
- Antitoxin VapB2
- Antitoxin VapB15
- Putative antitoxin VapB5
- Ribonuclease VapC5
- Ribonuclease VapC2
Sequence:
MALSIKHPEADRLARALAARTGETLTEAVVTALRERLARETGRARVVPLRDELAAIRHRCAALPVVDNRSAEAILGYDERGLPA
Protein: Protein RecA (Recombinase A) (P78014)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
Interaction partners:
- DNA topoisomerase 1
- Probable DNA helicase II homolog
- Beta sliding clamp
- Uncharacterized ATP-dependent helicase MPN_020
- Holliday junction branch migration complex subunit RuvA
- 5'-3' exonuclease
- Uncharacterized protein MG360 homolog
- Holliday junction branch migration complex subunit RuvB
- Probable DNA helicase MPN_340
- DNA-directed RNA polymerase subunit beta
Sequence:
MVQKEMINKKISQDNSFIQNNNLADFDFLDAKKNSEIKTVSTGSLHLDEALGTGGLPLGRIVELYGNESSGKTTVALHAVASFQKAGKVACYIDAEGALDLSYAKAIGIDLGKLLVAHPKHGENAFALMESLIKTNKVALIVVDSVAALIPKQELEGNMDDQTIGLHARMMSKGLRRVQSLLPESDTCLLFINQLREKPGVMFGNGEVTTGGRALKFYASMRMEAKRSELLKDRFGNYVGIKSKLTVSKNKVARPFGVAFLEIMFNRGIVYEHEVIELALKHNVVVRSDNAYSFKSQNIAIGKEKLFSVLAEKPELFEQIKQLTIKQIHSPPPPAS
Protein: Transmembrane protein 138 (Q9NPI0)
Organism: Homo sapiens (Human)
Function: Required for ciliogenesis.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:22282472}; Multi-pass membrane protein {ECO:0000269|PubMed:22282472}. Cell projection, cilium {ECO:0000269|PubMed:22282472}. Note=Localizes to vesicles en route to the base of cilium.
Interaction partners:
- Transmembrane protein 216
- Transmembrane protein 237
- Transmembrane protein 231
- Nephrocystin-1
- Tectonic-3
- Ciliogenesis and planar polarity effector 1
- Tectonic-like complex member MKS1
Sequence:
MLQTSNYSLVLSLQFLLLSYDLFVNSFSELLQKTPVIQLVLFIIQDIAVLFNIIIIFLMFFNTFVFQAGLVNLLFHKFKGTIILTAVYFALSISLHVWVMNLRWKNSNSFIWTDGLQMLFVFQRLAAVLYCYFYKRTAVRLGDPHFYQDSLWLRKEFMQVRR
Protein: Spectrin alpha, non-erythrocytic 1 (A0A0D9SGF6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MDPSGVKVLETAEDIQERRQQVLDRYHRFKELSTLRRQKLEDSYRFQFFQRDAEELEKWIQEKLQIASDENYKDPTNLQGKLQKHQAFEAEVQANSGAIVKLDETGNLMISEGHFASETIRTRLMELHRQWELLLEKMREKGIKLLQAQKLVQYLRECEDVMDWINDKEAIVTSEELGQDLEHVEVLQKKFEEFQTDMAAHEERVNEVNQFAAKLIQEQHPEEELIKTKQDEVNAAWQRLKGLALQRQGKLFGAAEVQRFNRDVDETISWIKEKEQLMASDDFGRDLASVQALLRKHEGLERDLAALEDKVKALCAEADRLQQSHPLSATQIQVKREELITNWEQIRTLAAERHARLNDSYRLQRFLADFRDLTSWVTEMKALINADELASDVAGAEALLDRHQEHKGEIDAHEDSFKSADESGQALLAAGHYASDEVREKLTVLSEERAALLELWELRRQQYEQCMDLQLFYRDTEQVDNWMSKQEAFLLNEDLGDSLDSVEALLKKHEDFEKSLSAQEEKITALDEFATKLIQNNHYAMEDVATRRDALLSRRNALHERAMRRRAQLADSFHLQQFFRDSDELKSWVNEKMKTATDEAYKDPSNLQGKVQKHQAFEAELSANQSRIDALEKAGQKLIDVNHYAKDEVAARMNEVISLWKKLLEATELKGIKLREANQQQQFNRNVEDIELWLYEVEGHLASDDYGKDLTNVQNLQKKHALLEADVAAHQDRIDGITIQARQFQDAGHFDAENIKKKQEALVARYEALKEPMVARKQKLADSLRLQQLFRDVEDEETWIREKEPIAASTNRGKDLIGVQNLLKKHQALQAEIAGHEPRIKAVTQKGNAMVEEGHFAAEDVKAKLHELNQKWEALKAKASQRRQDLEDSLQAQQYFADANEAESWMREKEPIVGSTDYGKDEDSAEALLKKHEALMSDLSAYGSSIQALREQAQSCRQQVAPTDDETGKELVLALYDYQEKSPREVTMKKGDILTLLNSTNKDWWKVEVNDRQGFVPAAYVKKLDPAQSASRENLLEEQGSIALRQEQIDNQTRITKEAGSVSLRMKQVEELYHSLLELGEKRKGMLEKSCKKFMLFREANELQQWINEKEAALTSEEVGADLEQVEVLQKKFDDFQKDLKANESRLKDINKVAEDLESEGLMAEEVQAVQQQEVYGMMPRDETDSKTASPWKSARLMVHTVATFNSIKELNERWRSLQQLAEERSQLLGSAHEVQRFHRDADETKEWIEEKNQALNTDNYGHDLASVQALQRKHEGFERDLAALGDKVNSLGETAERLIQSHPESAEDLQEKCTELNQAWSSLGKRADQRKAKLGDSHDLQRFLSDFRDLMSWINGIRGLVSSDELAKDVTGAEALLERHQEHRTEIDARAGTFQAFEQFGQQLLAHGHYASPEIKQKLDILDQERADLEKAWVQRRMMLDQCLELQLFHRDCEQAENWMAAREAFLNTEDKGDSLDSVEALIKKHEDFDKAINVQEEKIAALQAFADQLIAAGHYAKGDISSRRNEVLDRWRRLKAQMIEKRSKLGESQTLQQFSRDVDEIEAWISEKLQTASDESYKDPTNIQLSKLLSKHQKHQAFEAELHANADRIRGVIDMGNSLIERGACAGSEDAVKARLAALADQWQFLVQKSAEKSQKLKEANKQQNFNTGIKDFDFWLSEVEALLASEDYGKDLASVNNLLKKHQLLEADISAHEDRLKDLNSQADSLMTSSAFDTSQVKDKRDTINGRFQKIKSMAASRRAKLNESHRLHQFFRDMDDEESWIKEKKLLVGSEDYGRDLTGVQNLRKKHKRLEAELAAHEPAIQGVLDTGKKLSDDNTIGKEEIQQRLAQFVEHWKELKQLAAARGQRLEESLEYQQFVANVEEEEAWINEKMTLVASEDYGDTLAAIQGLLKKHEAFETDFTVHKDRVNDVCTNGQDLIKKNNHHEENISSKMKGLNGKVSDLEKAAAQRKAKLDENSAFLQFNWKADVVESWIGEKENSLKTDDYGRDLSSVQTLLTKQETFDAGLQAFQQEGIANITALKDQLLAAKHVQSKAIEARHASLMKRWSQLLANSAARKKKLLEAQSHFRKVEDLFLTFAKKASAFNSWFENAEEDLTDPVRCNSLEEIKALREAHDAFRSSLSSAQADFNQLAELDRQIKSFRVASNPYTWFTMEALEETWRNLQKIIKERELELQKEQRRQEENDKLRQEFAQHANAFHQWIQETRTYLLDGIAYRRVIRVYQYEVGDDLSGRSCMVEESGTLESQLEATKRKHQEIRAMRSQLKKIEDLGAAMEEALILDNKYTEHSTVGLAQQWDQLDQLGMRMQHNLEQQIQARNTTGVTEEALKEFSMMFKHFDKDKSGRLNHQEFKSCLRSLGYDLPMVEEGEPDPEFEAILDTVDPNRDGHVSLQEYMAFMISRETENVKSSEEIESAFRALSSEGKPYVTKEELYQNLTREQADYCVSHMKPYVDGKGRELPTAFDYVEFTRSLFVN
Protein: sn-2 acyl-lipid omega-3 desaturase (ferredoxin), chloroplastic (EC 1.14.19.35) (Omega-3 fatty acid desaturase 7, chloroplastic) (HaFAD7) (Q56VS4)
Organism: Helianthus annuus (Common sunflower)
Function: Chloroplast omega-3 fatty acid desaturase introduces the third double bond in the biosynthesis of 18:3, and probably also 16:3 fatty acids, important constituents of plant membranes. It is thought to use ferredoxin as an electron donor and to act on fatty acids esterified to galactolipids, sulfolipids and phosphatidylglycerol.
Subcellular location: Plastid, chloroplast membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAGLVLSGCAIKPFSQSLPIPTKRFITNPSNINLLHPKDPIFSPNFHGFSRWAVKVSAPLRIPSIDQQDLDLDLERERISSLDVQEEEIFDAGAPPPFKLADIRAAIPKRCWVKDPWRSMSYVVRDVAIVLGLAAAAAHLNNWLVWPLYWAAQGTMFWALFVLGHDCGHGSFSNNAKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPLTEKTFKSLDWITRTLRFTLPFPMLAYPFYLWNRSPGKSGSHFDPSSDLFVPAEQKDVITSTICWTTMLALLFGLNFVVGPVQMLKLYGIPYLINVMWLDFVTYLHHHGHEDKLPWYRGKEWSYLRGGLTTIDRDYGWINNIHHDIGTHVIHHLFPQIPHYHLIEATEAAKPVLGKYYREPKKSSPIPFHLLGELVRSLKKDHYVSDTGDVLYYQTDDKLSKEK
Protein: Guanine deaminase (Guanase) (EC 3.5.4.3) (Guanine aminohydrolase) (Q57X48)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- Inosine-adenosine-guanosine-nucleoside hydrolase
- Nucleoside hydrolase, putative
- Hypoxanthine phosphoribosyltransferase
- Hypoxanthine phosphoribosyltransferase
- Adenylosuccinate synthetase
- Dihydroorotate dehydrogenase
- Adenylosuccinate lyase
- GMP synthase
Sequence:
METAVPVRYFLGTLIEAPARDTLIFAPRSLVCVGADGCITAVLQPNDIKNESGVSGGGGSGCGGKSDNETYEQTLKEARRSGALTVLKDHQYLLPGLIDLHVHAPQWPQLGKALDRPLEIWLHEYTFPLEAKYADLDFAATSYNSLVSTLLAHGTTTAVYFATIHVDASLLLARVCLEKGQRAVVGRVAMDLASQCPAYYRDASPQESIERSEIFIQAVRKLPGNDNSSPLVLPAVVPRFIPTSSDEALQGLGRLVAKYGCHVQSHVSESDWEHHHVLERCGKPDAFALDDAGLLTRRTVLAHGNFLSDADMKLLCSRGSAVAHCPLSNFYFSGAVFPLRRALDFGLRVGLGTDISGGPSPAIWDAARDALMAARALESGVDPTTSKEERGGRRHANPEQSKAEDSNGKKGENPRVGGSAAESRDSTSCRINSVEAFWLATTRGGEALDLKVGRLAAGFHFDAVVVDVSVPTGGVHIFQGLDGPRDIFDKIVYGASAANVVQTYVAGRLVHGRVEL
Protein: Voltage-dependent L-type calcium channel subunit beta-2 (CAB2) (Calcium channel voltage-dependent subunit beta 2) (P54288)
Organism: Oryctolagus cuniculus (Rabbit)
Function: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.
Subcellular location: Cell membrane, sarcolemma {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent N-type calcium channel subunit alpha-1B
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Voltage-dependent L-type calcium channel subunit alpha
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent L-type calcium channel subunit beta-3
- Voltage-dependent L-type calcium channel subunit beta-1
- Calcium voltage-gated channel auxiliary subunit alpha2delta 2
Sequence:
MNQASGLDLLKISYGKGARRKNRFKGSDGSTSSDTTSNSFVRQGSADSYTSRPSDSDVSLEEDREAVRREAERQAQAQLEKAKTKPVAFAVRTNVSYSAAHEDDVPVPGMAISFEAKDFLHVKEKFNNDWWIGRLVKEGCEIGFIPSPVKLENMRLQHEQRAKQGKFYSSKSGGNSSSSLGDIVPSSRKSTPPSSAIDIDATGLDAEENDIPANHRSPKPSANSVTSPHSKEKRMPFFKKTEHTPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFEGRISITRVTADISLAKRSVLNNPSKHAIIERSNTRSSLAEVQSEIERIFELARTLQLVVLDADTINHPAQLSKTSLAPIVVYVKISSPKVLQRLIKSRGKSQAKHLNVQMVAADKLAQCPPELFDVILDENQLEDACEHLADYLEAYWKATHPPSSNLPNPLLSRTLATSALPVSPTLASNSQGSQGDQRTDRSAPARSASQAEEEPCLEPAKKSQHRSSSSAPHHNHRSGTSRGLSRQETFDSETQESRDSAYVEPKEDYSHEHVDHYAPHRDHNHRDETHRSSDHRHRETRHRSRDMDREQDHNECNKQRSRHKSKDRYCDKDGEVISKKRNEAGEWNRDVYIRQ
Protein: Pituitary homeobox 2 (Homeobox protein PITX2) (Paired-like homeodomain transcription factor 2) (xPtx2) (Q9PWR3)
Organism: Xenopus laevis (African clawed frog)
Function: May play an important role in development and maintenance of anterior structures and mediate left-right asymmetry. Could play a role at the interface of lateral plate signaling and heart and gut morphogenesis.
Subcellular location: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:P97474}.
Interaction partners:
Sequence:
MNSMKEPLHLDHLAGSRVAAASSHHHHHHHHQHQTVTLVSMASSLGQRSGECKSRLEVHTISDTSSPDTADKDKSHQTKNEDSSTDDPSKKKRQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERNQQAELCKNGFGPQFNGLMQPYDDMYPSYSYNNWAAKGLTSASLSTKSFPFFNSMNVNPLSSQSMFSSPNSISSMSMSSGMVPSAVTGVPGSGLNSLNNLNNLSNPSLNTAVPTSACPYAPPTPPYVYRDTCNSSLASLRLKAKQHSSFGYATVQTPGSNLSACQYAVDRPV
Protein: ATP-dependent 6-phosphofructokinase, platelet type (ATP-PFK) (PFK-P) (EC 2.7.1.11) (6-phosphofructokinase type C) (Phosphofructo-1-kinase isozyme C) (PFK-C) (Phosphohexokinase) (P47860)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
Interaction partners:
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase A
- Fructose-bisphosphate aldolase B
- Fructose-1,6-bisphosphatase 1
- Fructose-1,6-bisphosphatase isozyme 2
- Fructose-bisphosphate aldolase C
- Transaldolase
- ATP-dependent 6-phosphofructokinase, muscle type
- Hexokinase-2
- ATP-dependent 6-phosphofructokinase, liver type
Sequence:
MSDQDSSTSSTSFPKYLEHLSGDGKAIGVLTSGGDAQGMNAAVRAVVRMGIYTGAKVYFIYEGYQGMVDGGSNIVEAKWECVSSILQVGGTIIGSARCQAFRSREGRLKAACNLVRLGITNLCVIGGDGSLTGANLFRKEWSGLLEELAKNGEIDSDTVKKHAYLNVVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLPESPPEEGWEEEMCLKLSENRARKKRLNIIIVSEGAIDTQNKPITSEKIKELVVTNLGFDTRVTILGHVQRGGTPSAFDRILASRMGVEAVLALLEATPETPACVVSLRGNQAVRLPLMECVQMTQDVQKAMDERRFDEAVKLRGRSFEGNLNTYKRLAIKEPDDKIPKSNCNVAIINVGAPAAGMNAAVRSAVRVGIAEGHKMFAIYDGFDGLANGQIKEIGWGDVGGWTGQGGSILGTKRTLPGKYLEKIAEQMHSKNINALLIIGGFEAYLGLLELAAARNKHEAFCVPMVMVPATVSNNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGADAAYIFEEQFDIRDLQSNVMHLTEKMKTSIQRGLVLRNENCSVNYTTDFIYQLYSEEGKGVFDCRKNVLGHMQQGGAPSPFDRNFGTKISAKAMEWISAKLKGSHGTGKKFVSDDSICVLGIQKRDLLFKPVAELRKATDFEHRIPKQQWWLKLRPIMKILAKYEASYDMSDVGKLEPVHNHGELSAI
Protein: Major capsid protein 2 (MCP2) (Major capsid protein VP2) (A0A6M3VWZ7)
Organism: Pyrobaculum filamentous virus 2 (PFV2)
Function: Self-assembles to form a helical, filamentous nucleocapsid (Probable). Together with capsid protein 2, wraps arounds the DNA and maintains it in an A-form (Probable). Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by positively charged residues (Probable). This certainly protects the viral DNA under conditions such as the extreme desiccation of its host (Probable).
Subcellular location: Virion {ECO:0000269|PubMed:32368353}.
Interaction partners:
Sequence:
MSVEVYRQKIEKGGYSAAYEATRRYEREEIEVLSWSSRWESAWSKFGEAVKALGKIEGAPRALVIAKVQEALAYMSKPLPNMKLAMAAAVQAVRACEQLPGMNRERCLDAVAGALGVAKDWIRREMTGGGGGGGGGGGGGGGAVV