wanglab/gogpt-training-data huggingface dataset:
Protein: Adenosine deaminase (EC 3.5.4.4) (S-methyl-5'-thioadenosine deaminase) (EC 3.5.4.31) (Q8IJA9)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalyzes the hydrolytic deamination of adenosine to produce inosine. Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI). Plays an essential role in the purine salvage pathway which allows the parasite to use host cell purines for the synthesis of nucleic acids (Probable).
Interaction partners:
- Hypoxanthine phosphoribosyltransferase
- IMP-specific 5'-nucleotidase 1
- Lysine decarboxylase-like protein, putative
- Inosine-5'-monophosphate dehydrogenase
- Adenylosuccinate synthetase
- Bifunctional dihydrofolate reductase-thymidylate synthase
- GMP synthase
- Haloacid dehalogenase-like hydrolase, putative
Sequence:
MNCKNMDTSYEIINYLTKDELDIDLSCMDKKERYKIWKRLPKCELHCHLDVCFSVDFFLNVIRKYNIQPNMSDEEIIDYYLFSKPGKSLDEFVEKALRLTDIYIDYTVVEDLAKHAVFNKYKEGVVLMEFRYSPSFMSFKHNLDKDLIHEAIVKGLNEAVALLEYKIQVGLLCTGDGGLSHERMKEAAEFCIKHKKDFVGYDHAGHEVDLKPFKDIFDNIREEGISLSVHAGEDVSIPNLNSLYTAINLLHVKRIGHGIRVSESQELIDLVKEKDILLEVCPISNVLLNNVKSMDTHPIRMLYDAGVKVSVNSDDPGMFLTNITDNYEELYTHLNFTLADFMKMNLWAVQKSFVDPDIKNKIISKYF
Protein: Zinc finger protein 549 (Q6P9A3)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger protein 773
Sequence:
MAEAALVITPQIPMVTEEFVKPSQGHVTFEDIAVYFSQEEWGLLDEAQRCLYHDVMLENFSLMASVGCLHGIEAEEAPSEQTLSAQGVSQARTPKLGPSIPNAHSCEMCILVMKDILYLSEHQGTLPWQKPYTSVASGKWFSFGSNLQQHQNQDSGEKHIRKEESSALLLNSCKIPLSDNLFPCKDVEKDFPTILGLLQHQTTHSRQEYAHRSRETFQQRRYKCEQVFNEKVHVTEHQRVHTGEKAYKRREYGKSLNSKYLFVEHQRTHNAEKPYVCNICGKSFLHKQTLVGHQQRIHTRERSYVCIECGKSLSSKYSLVEHQRTHNGEKPYVCNVCGKSFRHKQTFVGHQQRIHTGERPYVCMECGKSFIHSYDRIRHQRVHTGEGAYQCSECGKSFIYKQSLLDHHRIHTGERPYECKECGKAFIHKKRLLEHQRIHTGEKPYVCIICGKSFIRSSDYMRHQRIHTGERAYECSDCGKAFISKQTLLKHHKIHTRERPYECSECGKGFYLEVKLLQHQRIHTREQLCECNECGKVFSHQKRLLEHQKVHTGEKPCECSECGKCFRHRTSLIQHQKVHSGERPYNCTACEKAFIYKNKLVEHQRIHTGEKPYECGKCGKAFNKRYSLVRHQKVHITEEP
Protein: Actin-depolymerizing factor 3 (ADF-3) (AtADF3) (Q9ZSK4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q39250}.
Interaction partners:
- Profilin-2
- Profilin-1
- Profilin-5
- Profilin-4
- Profilin-3
- Cyclase-associated protein 1
- Villin-5
- Protein phosphatase EYA
- Villin-1
- Uncharacterized protein
Sequence:
MANAASGMAVHDDCKLKFMELKTKRTHRFIIYKIEELQKQVIVEKIGEPGQTHEDLAASLPADECRYAIFDFDFVSSEGVPRSRIFFVAWSPDTARVRSKMIYASSKDRFKRELDGIQVELQATDPTEMDLDVFKSRAN
Protein: Cyclopropane mycolic acid synthase MmaA2 (CMAS) (EC 2.1.1.79) (Cyclopropane-fatty-acyl-phospholipid synthase) (CFA synthase) (Mycolic acid methyltransferase) (MA-MT) (S-adenosylmethionine-dependent methyltransferase) (AdoMet-MT) (SAM-MT) (A5U029)
Organism: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Function: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence.
Interaction partners:
Sequence:
MVNDLTPHFEDVQAHYDLSDDFFRLFLDPTQTYSCAHFEREDMTLEEAQIAKIDLALGKLGLQPGMTLLDIGCGWGATMRRAIAQYDVNVVGLTLSKNQAAHVQKSFDEMDTPRDRRVLLAGWEQFNEPVDRIVSIGAFEHFGHDRHADFFARAHKILPPDGVLLLHTITGLTRQQMVDHGLPLTLWLARFLKFIATEIFPGGQPPTIEMVEEQSAKTGFTLTRRQSLQPHYARTLDLWAEALQEHKSEAIAIQSEEVYERYMKYLTGCAKLFRVGYIDVNQFTLAK
Protein: Development-specific protein LVN1.2 (P15262)
Organism: Lytechinus variegatus (Green sea urchin) (Echinus variegatus)
Interaction partners:
Sequence:
MSTVAWDFAERRLGLNLDILYPNGTAYNFRVIQDYTTGTQFTIFERYRFCAKQKAPMPEPENCIPGNTSVRFRGFLGAGKDRIDYDLYTMKLTKEETGNLEGEGTFSVVRGTEYDIPLSNSFIGTYFDGETPYAQVSNGGYYNIEIGIDDPKRWFDVPDYCPKELTDLTMIPKHIPKWTWIRLPAPRLF
Protein: Cytochrome P450 7B1 (24-hydroxycholesterol 7-alpha-hydroxylase) (EC 1.14.14.26) (25/26-hydroxycholesterol 7-alpha-hydroxylase) (EC 1.14.14.29) (3-hydroxysteroid 7-alpha hydroxylase) (Hippocampal transcript 1 protein) (HCT-1) (Oxysterol 7-alpha-hydroxylase) (Q60991)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase involved in the metabolism of endogenous oxysterols and steroid hormones, including neurosteroids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon hydrogen bonds of steroids with a preference for 7-alpha position. Usually metabolizes steroids carrying a hydroxy group at position 3, functioning as a 3-hydroxy steroid 7-alpha hydroxylase. Hydroxylates oxysterols, including 25-hydroxycholesterol and (25R)-cholest-5-ene-3beta,26-diol toward 7-alpha hydroxy derivatives, which may be transported to the liver and converted to bile acids. Via its product 7-alpha,25-dihydroxycholesterol, a ligand for the chemotactic G protein-coupled receptor GPR183/EBI2, regulates B cell migration in germinal centers of lymphoid organs, thus guiding efficient maturation of plasma B cells and overall antigen-specific humoral immune response. 7-alpha hydroxylates neurosteroids, including 3beta-hydroxyandrost-5-en-17-one (dehydroepiandrosterone) and pregnenolone, both involved in hippocampus-associated memory and learning. Metabolizes androstanoids toward 6- or 7-alpha hydroxy derivatives (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O75881}; Multi-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000250|UniProtKB:O75881}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cholesterol 25-hydroxylase
- 3 beta-hydroxysteroid dehydrogenase type 7
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
- Sterol 26-hydroxylase, mitochondrial
- NADPH-dependent 3-keto-steroid reductase Hsd3b4
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 3
- Cholesterol side-chain cleavage enzyme, mitochondrial
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 6
Sequence:
MQGATTLDAASPGPLALLGLLFAATLLLSALFLLTRRTRRPREPPLIKGWLPYLGMALKFFKDPLTFLKTLQRQHGDTFTVFLVGKYITFVLNPFQYQYVTKNPKQLSFQKFSSRLSAKAFSVKKLLTDDDLNEDVHRAYLLLQGKPLDALLETMIQEVKELFESQLLKITDWNTERIFAFCGSLVFEITFATLYGKILAGNKKQIISELRDDFFKFDDMFPYLVSDIPIQLLRNEESMQKKIIKCLTSEKVAQMQGQSKIVQERQDLLKRYYRHDDPEIGAHHLGFLWASLANTIPAMFWAMYYILRHPEAMEALRDEIDSFLQSTGQKKGPGISVHFTREQLDSLVCLESTILEVLRLCSYSSIIREVQEDMNLSLESKSFSLRKGDFVALFPPLIHNDPEIFDAPKEFRFDRFIEDGKKKSTFFKGGKKLKTYVMPFGLGTSKCPGRYFAVNEMKLLLIMLLTYFDLEIIDRKPIGLNHSRMFLGIQHPDSAVSFRYKAKSWRS
Protein: WD repeat and SOCS box-containing protein 2 (WSB-2) (CS box-containing WD protein) (Q9NYS7)
Organism: Homo sapiens (Human)
Function: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- RING-box protein 2
- Cullin-5
Sequence:
MEAGEEPLLLAELKPGRPHQFDWKSSCETWSVAFSPDGSWFAWSQGHCIVKLIPWPLEEQFIPKGFEAKSRSSKNETKGRGSPKEKTLDCGQIVWGLAFSPWPSPPSRKLWARHHPQVPDVSCLVLATGLNDGQIKIWEVQTGLLLLNLSGHQDVVRDLSFTPSGSLILVSASRDKTLRIWDLNKHGKQIQVLSGHLQWVYCCSISPDCSMLCSAAGEKSVFLWSMRSYTLIRKLEGHQSSVVSCDFSPDSALLVTASYDTNVIMWDPYTGERLRSLHHTQVDPAMDDSDVHISSLRSVCFSPEGLYLATVADDRLLRIWALELKTPIAFAPMTNGLCCTFFPHGGVIATGTRDGHVQFWTAPRVLSSLKHLCRKALRSFLTTYQVLALPIPKKMKEFLTYRTF
Protein: Condensin-2 complex subunit D3 (Non-SMC condensin II complex subunit D3) (Q6ZQK0)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis. May promote the resolution of double-strand DNA catenanes (intertwines) between sister chromatids. Condensin-mediated compaction likely increases tension in catenated sister chromatids, providing directionality for type II topoisomerase-mediated strand exchanges toward chromatid decatenation. Specifically required for decatenation of centromeric ultrafine DNA bridges during anaphase. Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Condensin-2 complex subunit G2
- Condensin-2 complex subunit H2
- Structural maintenance of chromosomes protein 2
- Structural maintenance of chromosomes protein 4
- Condensin complex subunit 2
- Non-SMC condensin I complex, subunit G
- Condensin complex subunit 1
- Microcephalin
- Structural maintenance of chromosomes protein 3
Sequence:
MALQDLGENLQPWCPLGLSLEWVKTVWDLDFTEIEPLDPSIVGEILETGRDAFTKLYGSLFPFATDESGSLESIWTFFTENDISSNTLVALFCHFVQEAHKKSASAQYREYGLHAAGLYFLLLEIPGIVVNQVFHPVMFDKCIQILKRSWPQESNLTQKRKKDHSKSSKDNYRKSRKRGKPPRKEDYQVDELSREEEEEEEEIYFSGRDLCQIRDAIFNLLKNFLRLLPKFSLKEKPQSIQTCIEVFVALTSFEPIPHKFLISQARNLNEVKHISELAYYGLYLLCSPVHGEENKVIGSIFHQMLNVILMLEVGEGSRCAPLAITSQVINCRNQAVQFVSSLVDELQASVYPVLGTLLQHICAKVVDKAEYRTYAAQSLVQLLTKLPSEEYATFIAWLYKYSRSSKIPHRVFTLDVALALLTLPERELDDTVSLEHQKFLKHKFFVQEIIFDRCLDKAPTVRSKALSSFAHCLELSSSNTSESILEIFINSNLVPGIQNLSNTVLNPSPVLTSRNGYSAQSRTHNNDEQTLPGERCFMTMLRKRIKDEKINVRKSALQVLMSILKHCDILSMEQDLLILQDHCRDPAISVRKQALQSLTELVMAQPTCVPVQKAWLMGVIPVVMDCESTVQEKALECLDQLLLQNIKHHKKFHSADRSQVLAWSLLALLTIENQDLRRYLNKAFHIWSKKDKFSSTFINSVISHTDTERSAPAWMLLSKITCSSPKLDYTKIIESWERLSREQSPNSNTLGYMLCVIGHIAKHLPKGTRDKITGVIKAKLNGFQWSPELISSSVDALQKLCRASAKTVLEEQGLLKQVCGDVLATCEQHLSNILLKEDGTGNMDEGLVVKCIFTLGDIAQLCPAIVEKRVFLLIQSILASSAHSDHLPSSQGTTDALDSQPPFQPRSSAMPSVIRAHAIITLGKLCLQHEDLAKKSIPALVRELEVSEDVAVRNNVIIVICDLCIRYTVMVDNYIPNISVCLKDSDPFIRKQTLVLLTNLLQEEYVKWKGSLFFRFVSTLVDSHPDIASLGEFCLAHLLLKRNPTMFFQHFIECIFHFNSYEKHGQYNKFSQSERGKQLFLLKGKTNKEKRMRIYKFLLEHFTDEQRFNVTSKICLNILACFTDGILPMDMEASELLSDTFDILNSKEIKLLAMRAQTSKDLLEEDDVALANVVMQEAQMKIISQVQKRNFIENIIPIIISLKTVLEKNKIPALRELMNYLREVMQDYRDEINDFFAVDKQLASELEYDMKKYNEQLAQEQALTEHANATKGPEDSDRVPSAQVAPDLEAVPALAAAPMAAAAAAAPMAAAAAAAGQDNADVPPTQSRPSAPRSNFTPTLPPISENGPLKIMSSTRPMSLSTIAILNSVKKAVASKNRTRSLGALPFNVETGSPENPSSHESSLSLEKESDRTVNHVTKRAISTPENSISDVTFAAGVSYIGTPATFFTKEKHEAQEQGSDILCLSLLDKRPPQSPQWNVKSPARSHGSTRSSRRSLRKAPLKTAN
Protein: Uncharacterized protein At1g15400 (Q9XI29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Mitogen-activated protein kinase kinase kinase YODA
- Protein BREAKING OF ASYMMETRY IN THE STOMATAL LINEAGE
Sequence:
MEGLQRSTISFRRQGSSGIVFDDRLIAELNKSGNNEQKDESQRDEQPKPMSESSEQVKPIDEKDKLRPIKTGGGAPGGIERSRSNGGGAQRHHRTTGRVSPAVDPPSPRISSCGCCSAFGKNPPGKKVNPRKRPPKRRSRRRIVTKKR
Protein: Maternal gene required for meiosis, isoform D (Maternal gene required for meiosis, isoform E) (M9PJM9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGSEHYCLRWNNYQSNLLGVFSQLLQDGSLVDVTLVCSEGTSIRAHKVVLSACSSYFQSLFLEHPEGHLIVILKDVRFAELQTLVEFMYKGEVNVQYCQLSALLKTAESLKVKGLAEMTNQNTTLREPEREPDRLRPQGGGGSGGSAHKAADSPAAALDATAATQAATATATATAAAATSTSTSATSAAATAAATAATSASTTATAAAGSSNTTTTTAATTTATCATAATSTAATSSSSSVTSAAAAAAAAASASGVAHSEEATSSSSSTGGQKREASDRSSPTPAKRSSRMHPADKVDVAEDREQEQNQADELLSEELLGRNLKDEEDDDVDELDENEETKLRGRDEDDDDEDEEEDTPMPLDLYQRPNVEPKSAAAATAAQQGGSNSLSGSSNACHTNSSSNSNNNNNNNNNSSSNNNNNTSSGKTSASSNGGTASSGGTADSVVAVDDDDDDDDGGHHHQRQVMDDRLEQDVDEEDLDDDVVVVGPATAMARGIAQRLAHQNLQRLHHTHHHAQHQHSQHHHPHSQHHHTPHHQQHHTHSDDEDAMPVIAKSEILDDDYDDEMDLEDDDEADNSSNDLGLNMKMGSGGAGGGGGVDLSTGSTLIPSPLITLPSSSAAAAAAAAAAMESQRSTPAMSAAQAAGAGASDLSIGGCGGRPASRSSRDGGGNDGGRGGASSSSLLSPGTVANLLPVQSVPLSLKKEIDCSEDDNSSHSRHMQQRSASAGGGLGGDLDYRASHESETSESPHQQQQPPPHAVGVGAGGGSAAAAAAAAAALLHQQQQQQPPHSPPPPPLHMFPCIYCRSAFPNQSKLTRHLLTHSLKTLEYREPTTTALLHSHLLGDLNMAAAGLPSPFAFQMNAAAMAATSGSDTQEQVAALAAAFGIDMEAALSLASTGCTFQSLTASCLEASSGGGSGGGGQGSLSRSATSAGNGGGLMLGSGSGSGSGAAAATGGSGSSGCGGGGGTATSGSLSPSTSAAAAAAAAAQSQSAALLGAASSDPNSVVMCDRPFKCEFCGKAFKLRHHMKDHCRVHTGERPFRCNMCGKTFSRSTILKAHEKTHFPKYVRKFLSPSSPVDTKDELPQ
Protein: Ras-related protein Rab-23 (EC 3.6.5.2) (Q9ULC3)
Organism: Homo sapiens (Human)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Together with SUFU, prevents nuclear import of GLI1, and thereby inhibits GLI1 transcription factor activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P35288}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000250|UniProtKB:P35288}. Cytoplasm {ECO:0000269|PubMed:22365972}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:22452336}. Endosome membrane {ECO:0000250, ECO:0000250|UniProtKB:P35288}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis. {ECO:0000269|PubMed:21255211}.
Interaction partners:
- Transcriptional activator GLI3
- Protein smoothened
- Zinc finger protein GLI2
- Suppressor of fused homolog
- Radial spoke head 14 homolog
- Tetratricopeptide repeat protein 21B
- Tubby-related protein 3
- Tectonic-1
- Sonic hedgehog protein
- EVI5-like protein
Sequence:
MLEEDMEVAIKMVVVGNGAVGKSSMIQRYCKGIFTKDYKKTIGVDFLERQIQVNDEDVRLMLWDTAGQEEFDAITKAYYRGAQACVLVFSTTDRESFEAVSSWREKVVAEVGDIPTVLVQNKIDLLDDSCIKNEEAEALAKRLKLRFYRTSVKEDLNVNEVFKYLAEKYLQKLKQQIAEDPELTHSSSNKIGVFNTSGGSHSGQNSGTLNGGDVINLRPNKQRTKKNRNPFSSCSIP
Protein: Histocompatibility antigen 60 (O77968)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAKGATSKSNHCLILSLFILLSYLGTILADGTDSLSCELTFNYRNLHGQCSVNGKTLLDFGDKKHEENATKMCADLSQNLREISEEMWKLQSGNDTLNVTTQSQYNQGKFIDGFWAINTDEQHSIYFYPLNMTWRESHSDNSSAMEQWKNKNLEKDMRNFLITYFSHCLNKSSSHFREMPKSTLKVPDTTQRTNATQIHPTVNNFRHNSDNQGLSVTWIVIICIGGLVSFMAFMVFAWCMLKKK
Protein: AT4G37550 protein (Acetamidase/Formamidase family protein) (B9DFI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAPLSPRVVVKVDLKKKPWQQDQPLHNRWHPEIPPVAEVKAGEFFRVEMIDAMGGVIKDNDSASDIKNLVLTTTHHLSGPIRVVDEEGVAAKAGDLLAVEICNLGPLPGDEWGFTGSFDRENGGGFLTDHFPCATKAIWYFEGIYAYSPQIPGVRFPGLTHPGVIGTAPSNELLRIWNDRERQLEESGVESLTLCEVVHQRPLACLPTTKGCLLGNIEEGTPEWERIANEAARTIPGRENGGNCDIKNLSRGSKIYLPVFVEGANLSTGDMHFSQGDGEISFCGAIEMSGFLELKCEIIRNGMQEYLTPMGPTPLHVNPIFEIGPVEPRFSEWLVFEGISVDESGKQHYLDATVAYKRAVLNAIDYLFKFGYSKEQVYLLLSCCPCEGRLSGIVDSPNAVATLAIPTAIFDQDIRPKNRKVPVGPRVVRKPDVLKSTYDGKLPITKNPSSSS
Protein: Probable acetyl-CoA acetyltransferase (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) [Cleaved into: Probable acetyl-CoA acetyltransferase, propeptide removed] (P9WG69)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable fatty oxidation protein FadB
- 3-hydroxybutyryl-CoA dehydrogenase
- Probable 3-hydroxybutyryl-CoA dehydrogenase FadB3
- Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit B
- Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit A
- Acetyl-coenzyme A synthetase
- Malate synthase G
- Putative acyltransferase Rv0859
- 2-isopropylmalate synthase
- Steroid 3-ketoacyl-CoA thiolase FadA6
Sequence:
MTTSVIVAGARTPIGKLMGSLKDFSASELGAIAIKGALEKANVPASLVEYVIMGQVLTAGAGQMPARQAAVAAGIGWDVPALTINKMCLSGIDAIALADQLIRAREFDVVVAGGQESMTKAPHLLMNSRSGYKYGDVTVLDHMAYDGLHDVFTDQPMGALTEQRNDVDMFTRSEQDEYAAASHQKAAAAWKDGVFADEVIPVNIPQRTGDPLQFTEDEGIRANTTAAALAGLKPAFRGDGTITAGSASQISDGAAAVVVMNQEKAQELGLTWLAEIGAHGVVAGPDSTLQSQPANAINKALDREGISVDQLDVVEINEAFAAVALASIRELGLNPQIVNVNGGAIAVGHPLGMSGTRITLHAALQLARRGSGVGVAALCGAGGQGDALILRAG
Protein: Pleiotropic ABC efflux transporter of multiple drugs CDR1 (Pleiotropic drug resistance protein CDR1) (Q6FK23)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Pleiotropic ABC efflux transporter that transports and confers resistance to structurally and functionally unrelated compounds including rhodamine 6G, Nile red, caspofungin, cycloheximide, or azoles such as fluconazole, itraconazole, ketoconazole, posaconazole, voriconazole, and isavuconazole. Chlorbromuron, itraconazole, yohimbine, ketoconazole, miconazole, clotrimazole, DE-11, tamoxifen, quinidine, verapamil can compete for rhodamine 6G's binding site(s) while compounds such as propanil, chloramphenicol, benomyl, voriconazole, tritylimidazole, ketoconazole, miconazole, tamoxifen, gefitinib shared binding site(s) with fluconazole. Nile red mediated efflux appears to be relatively more specific since only five compounds such as ZW3-12, rhodamine 123, miconazole, clotrimazole, and itraconazole can inhibit its accumulation. Does not use as substrates 4-nitroquinoline 1-oxide (4-NQO) and disulfiram. Does not play a role in the azole resistance in mature biofilms.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12244114, ECO:0000269|PubMed:21134356}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pleiotropic ABC efflux transporter of multiple drugs PDH1
- Transcription factor PDR1
- Lanosterol 14-alpha demethylase
- Candida glabrata strain CBS138 chromosome G complete sequence
Sequence:
MSLASDKKDADVASTTTTAQDDDNLSTYHGFDHHVQDQVRQLARTLTQQSSLHQKKEHTLPEEGINPIFTNTEADDYNPRLDPTSDEFSSAEWVQNMSNISNSDPDYYKPYSLGCYWKDLVATGESADIEYQANFLNGPYKGLKTVYNTVVPSTASSKDKNFKILKSMEGAVNPGELLVVLGRPGSGCTTLLKSISSNTHGFNIAKESTISYSGMTPNDIRKHFRGEVVYNAEADIHLPHLTVYQTLLTVARLKTPQNRLKGIDRETYARHLTEVAMATFGLSHTRNTKVGNDLVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLDSATALEFIRALKVQASISNAAATVAIYQCSQDAYDLFDKVCVLYDGYQIYFGPAGKAKEYFQKMGYVSPERQTTADFLTAVTSPSERIINQDYINRGIFVPQTPKEMWEYWRASEDHADLIKEIDSKLSDNYDANLAEIKDAHVARQSKRARPSSPYTVSYGMQIKYLLIRNFWRIKQSSGVTLFMVIGNSSMAFILGSMFYKVMKHNTTSTFYFRGAAMFFAVLFNAFSSLLEIFSLFEARPITEKHRTYSLYHPSADAFASILSEVPAKLITAVCFNIIYYFLVNFRRNGGVFFFYFLINIVAVFAMSHLFRCVGSVSKTLSAAMVPASMLLLGLSMYSGFAIPRTKILGWSKWIWYINPLAYLFESLMINEFHDRKFPCSQYIPSGSVYNNVPADSRICSSVGAIRGNDYVLGDDFLRESYSYLHKHKWRGFGIGLAYVIFFLVLYLILCEYNEGAKQKGEILVFPQNIVRRMKKERKLKNVSSDNDVEIGDVSDISDKKILADSSDESEESGANIGLSQSEAIFHWRNLCYDVQIKKETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGEVSVDGKQRDDSFARSIGYCQQQDLHLKTSTVRESLRFSAYLRQPADVSIEEKNQYVEDVIKILEMEQYADAVVGVPGEGLNVEQRKRLTIGVELAAKPKLLVFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFLQRGGKTVYFGDLGDGCKTMIDYFESHGSHKCPPDANPAEWMLEVVGAAPGSHANQDYHEVWRNSDEYQKVQEELEWMSNELPKKNTNNSETVHKEFATGVLYQCKLVSLRLFQQYWRSPDYLWSKFFLTIFNNIFIGFTFFKADRSLQGLQNQMLAVFMFTVIFNPLLQQYLPSFVQQRDLYEARERPSRTFSWKAFIVSQILVEIPWNILAGTVAFVIYYYAIGFYSNASVAHQLHERGALFWLFSCAFYVYIGSLALFCISFNQVAEAAANMASLMFTLSLSFCGVLVTPNGMPRFWIFMYRVSPLTYLIDGMLSTGVANVAIKCSNYELLRFSPAANLTCGEYLGPYLQTVKTGYIVDPSATDTCELCPYSHTNDFLSSVSSKYSRRWRNWGIFICYIAFNYIAGIFLYWLARVPKKSGKLAKK
Protein: Cysteine proteinase 1 (EhCP1) (EC 3.4.22.-) (Q01957)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Function: Cysteine protease which degrades matrix proteins such as collagen, laminin and fibronectin and thus is involved in the destruction of human tissue. Can abolish adhesion. May play an important role in pathogenicity.
Subcellular location: Lysosome {ECO:0000269|PubMed:21440496}.
Interaction partners:
Sequence:
MFTFILMFYIGYGIDFNTWVANNNKHFTAVESLRRRAIFNMNARIVAENNRKETFKLSVDGPFAAMTNEEYNSLLKLKRSGEEKGEVRYLNIQAPKAVDWRKKGKVTPIRDQGNCGSCYTFGSIAALEGRLLIEKGGDSETLDLSEEHMVQCTREDGNNGCNGGLGSNVYNYIMENGIAKESDYPYTGSDSTCRSDVKAFAKIKSYNRVARNNEVELKAAISQGLVDVSIDASSVQFQLYKSGAYTDKQCKNNYFALNHEVCAVGYGVVDGKECWIVRNSWGTGWGEKGYINMVIEGNTCGVATDPLYPTGVEYL
Protein: Seminal vesicle secretory protein 4 (Androgen-dependent protein) (ADP) (Seminal vesicle protein 2) (Seminal vesicle secretory protein IV) (SVS IV) (SVS protein S) (P02783)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Seminal vesicle secretory protein 2
- Seminal vesicle secretory protein 6
- Seminal vesicle secretory protein 5
- Prostate and testis expressed 4
- Seminal vesicle secretory protein 3A
- Seminal vesicle secretory protein 3B
- Amine oxidase
Sequence:
MKSTSLFLCSLLLLLVTGAIGRKTKEKYSQSEEVVSESFASGPSSGSSDDELVRDKPYGPKVSGGSFGEEASEEISSRRSKHISRSSGGSNMEGESSYAKKKRSRFAQDVLN
Protein: Adenosylhomocysteinase 2 (AdoHcyase 2) (EC 3.13.2.1) (S-adenosyl-L-homocysteine hydrolase 1) (SAH hydrolase 2) (Q9LK36)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic
- Homocysteine S-methyltransferase 3
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 1
- Cystathionine beta-lyase, chloroplastic
- Cystathionine gamma-synthase 1, chloroplastic
- Probable cystathionine gamma-synthase 2
- Cysteine synthase, chloroplastic/chromoplastic
Sequence:
MALLVEKTSSGREYKVKDMSQADFGRLEIELAEVEMPGLVSCVTEFGPSQPLKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQDHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGPGGGPDLIVDDGGDATLLIHEGVKAEEIFAKNGTFPDPTSTDNPEFQIVLSIIKDGLQVDPKKYHKMKERLVGVSEETTTGVKRLYQMQETGALLFPAINVNDSVTKSKFDNLYGCRHSLPDGLMRATDVMIAGKVAVICGYGDVGKGCAAAMKTAGARVIVTEIDPICALQALMEGLQVLTLEDVVSEADIFCTTTGNKDIIMVDHMRKMKNNAIVCNIGHFDNEIDMLGLETYPGVKRITIKPQTDRWVFPDTNSGIIVLAEGRLMNLGCATGHPSFVMSCSFTNQVIAQLELWNEKSSGKYEKKVYVLPKHLDEKVAALHLGKLGARLTKLTKDQSDYVSIPVEGPYKPVHYRY
Protein: 3-oxoacyl-[acyl-carrier-protein] synthase 1 (EC 2.3.1.41) (3-oxoacyl-[acyl-carrier-protein] synthase I) (Beta-ketoacyl-ACP synthase I) (Q9I3B2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- Enoyl-[acyl-carrier-protein] reductase FabI
- Enoyl-[acyl-carrier-protein] reductase
- 3-oxoacyl-[acyl-carrier-protein] reductase FabG
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- Beta-ketoacyl-[acyl-carrier-protein] synthase FabY
- 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase
Sequence:
MRRVVITGLGIVSCLGNDKDTVSANLRAGRPGIRFNPSYAEMGLRSHVSGSVDLNLEELIDRKVFRFMGDAAAYAYLAMEQAIKDSGLTPEQISNPRTGLIAGSGGASTLNQMEAIDTLREKGVKRIGPYRVTRTMGSTVSACLATPFQIKGVNYSISSACATSAHCIGQAMEQIQLGKQDVVFAGGGEEEHWSQSCLFDAMGALSTQYNETPEKASRAYDAKRDGFVIAGGGGMVVVEGLEHALKRGAKIYAEIVGYGATSDGYDMVAPSGEGAIRCMQQALATVDAPIDYLNTHGTSTPVGDVAEIRGVREVFGDKAPAISSTKSLSGHSLGAAGVHEAIYCLLMMEGGFIAGSANIDELDPEVADLPILRETRENAKLDTVMSNSFGFGGTNATLVLKRWQG