lokahq/bioreason-rl huggingface dataset:
Protein: Jupiter microtubule associated homolog 1 (J3KT51)
Organism: Homo sapiens (Human)
Function: Not known
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
InterPro domains:
- IPR033335: Microtubule-associated protein Jupiter (family) [1-101]
Sequence:
MTTTTTFKGVDPNSRNSSRVLRPPGGGSNFSLGFDEPTEQPVRKNKMASNIFGTPEENQASWAKSAGAKSSGGREDLESSGLQRRNSSEASSGDFLDLKVSVTA
Predicted GO terms:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0065007 (biological regulation), GO:0048518 (positive regulation of biological process), GO:0050789 (regulation of biological process), GO:0009893 (positive regulation of metabolic process), GO:0065009 (regulation of molecular function), GO:0019222 (regulation of metabolic process), GO:0050794 (regulation of cellular process), GO:0048522 (positive regulation of cellular process), GO:0050790 (regulation of catalytic activity), GO:0031323 (regulation of cellular metabolic process), GO:0044093 (positive regulation of molecular function), GO:0031325 (positive regulation of cellular metabolic process), GO:0010562 (positive regulation of phosphorus metabolic process), GO:0051338 (regulation of transferase activity), GO:0043085 (positive regulation of catalytic activity), GO:0051174 (regulation of phosphorus metabolic process), GO:0045937 (positive regulation of phosphate metabolic process), GO:0043549 (regulation of kinase activity), GO:0051347 (positive regulation of transferase activity), GO:0019220 (regulation of phosphate metabolic process), GO:0042325 (regulation of phosphorylation), GO:0033674 (positive regulation of kinase activity), GO:0042327 (positive regulation of phosphorylation)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0031975 (envelope), GO:0016020 (membrane), GO:0031974 (membrane-enclosed lumen), GO:0012505 (endomembrane system), GO:0005654 (nucleoplasm), GO:0031090 (organelle membrane), GO:0031967 (organelle envelope), GO:0043233 (organelle lumen), GO:0005635 (nuclear envelope), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0043228 (non-membrane-bounded organelle), GO:0031965 (nuclear membrane), GO:0043231 (intracellular membrane-bounded organelle), GO:0070013 (intracellular organelle lumen), GO:0043232 (intracellular non-membrane-bounded organelle), GO:0031981 (nuclear lumen), GO:0005730 (nucleolus), GO:0005634 (nucleus)
Protein: Ephrin-A3 (EFL-2) (EHK1 ligand) (EHK1-L) (EPH-related receptor tyrosine kinase ligand 3) (LERK-3) (P52797)
Organism: Homo sapiens (Human)
Function: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling (By similarity).
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
InterPro domains:
- IPR031328: Ephrin (family) [13-179]
- IPR001799: Ephrin receptor-binding domain (domain) [30-169]
- IPR008972: Cupredoxin (homologous_superfamily) [28-177]
- IPR034252: Ephrin-A ectodomain (domain) [31-166]
- IPR019765: Ephrin, conserved site (conserved_site) [121-148]
Sequence:
MAAAPLLLLLLLVPVPLLPLLAQGPGGALGNRHAVYWNSSNQHLRREGYTVQVNVNDYLDIYCPHYNSSGVGPGAGPGPGGGAEQYVLYMVSRNGYRTCNASQGFKRWECNRPHAPHSPIKFSEKFQRYSAFSLGYEFHAGHEYYYISTPTHNLHWKCLRMKVFVCCASTSHSGEKPVPTLPQFTMGPNVKINVLEDFEGENPQVPKLEKSISGTSPKREHLPLAVGIAFFLMTFLAS
Predicted GO terms:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding), GO:0005102 (signaling receptor binding), GO:0046875 (ephrin receptor binding)
Biological Process (BP): GO:0008150 (biological process), GO:0009987 (cellular process), GO:0023052 (signaling), GO:0007154 (cell communication), GO:0007267 (cell-cell signaling)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0071944 (cell periphery), GO:0016020 (membrane), GO:0005886 (plasma membrane)
Protein: Tryptase beta-2 (Tryptase-2) (EC 3.4.21.59) (Tryptase II) (P20231)
Organism: Homo sapiens (Human)
Function: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity.
Subcellular location: Secreted. Note=Released from the secretory granules upon mast cell activation.
InterPro domains:
- IPR001314: Peptidase S1A, chymotrypsin family (family) [60-229]
- IPR043504: Peptidase S1, PA clan, chymotrypsin-like fold (homologous_superfamily) [31-267]
- IPR018114: Serine proteases, trypsin family, histidine active site (active_site) [70-75]
- IPR033116: Serine proteases, trypsin family, serine active site (active_site) [218-229]
- IPR009003: Peptidase S1, PA clan (homologous_superfamily) [3-271]
- IPR001254: Serine proteases, trypsin domain (domain) [30-272]
Sequence:
MLNLLLLALPVLASRAYAAPAPGQALQRVGIVGGQEAPRSKWPWQVSLRVRDRYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPKKP
Predicted GO terms:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0003824 (catalytic activity), GO:0140096 (catalytic activity, acting on a protein), GO:0016787 (hydrolase activity), GO:0005515 (protein binding), GO:0017171 (serine hydrolase activity), GO:0042802 (identical protein binding), GO:0008233 (peptidase activity), GO:0008236 (serine-type peptidase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0050896 (response to stimulus), GO:0071840 (cellular component organization or biogenesis), GO:0006950 (response to stress), GO:0071704 (organic substance metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0006952 (defense response), GO:0016043 (cellular component organization), GO:1901564 (organonitrogen compound metabolic process), GO:0019538 (protein metabolic process), GO:0043170 (macromolecule metabolic process), GO:0045229 (external encapsulating structure organization), GO:0006508 (proteolysis), GO:0043062 (extracellular structure organization), GO:0022411 (cellular component disassembly), GO:0022617 (extracellular matrix disassembly), GO:0030198 (extracellular matrix organization)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0032991 (protein-containing complex), GO:1902494 (catalytic complex), GO:0071944 (cell periphery), GO:0005576 (extracellular region), GO:0030312 (external encapsulating structure), GO:0005615 (extracellular space), GO:1905368 (peptidase complex), GO:0031012 (extracellular matrix), GO:0062023 (collagen-containing extracellular matrix)
Protein: Phosphoprotein (Protein P) (P12579)
Organism: Human respiratory syncytial virus
Function: Plays critical roles in regulating RNA replication and transcription through its interactions with multiple proteins. Tethers the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex. Recruits the M2-1 protein, a processivity factor that is required for efficient transcription of viral RNA. Acts as a chaperone for neo-synthesized nucleoprotein by forming an N-P complex that preserves N in a monomeric and RNA-free state and prevents the association of nascent N with host cell RNAs. Recruits the host phosphatase PP1 to inclusion bodies to regulate viral transcription. Together with the nucleoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway.
Subcellular location: Virion {ECO:0000250|UniProtKB:P03421}. Host cytoplasm {ECO:0000250|UniProtKB:P03421}. Note=Localizes in cytoplasmic inclusion bodies. {ECO:0000250|UniProtKB:P03421}.
InterPro domains:
- IPR003487: Phosphoprotein, pneumoviral (family) [72-231]
Sequence:
MEKFAPEFHGEDANNRATKFLESIKGKFTSPKDPKKKDSIISVNSIDIEVTKESPITSNSTIINPTNETDDNAGNKPNYQRKPLVSFKEDPIPSDNPFSKLYKETIETFDNNEEESSYSYEEINDQTNDNITARLDRIDEKLSEILGMLHTLVVASAGPTSARDGIRDAMVGLREEMIEKIRTEALMTNDRLEAMARLRNEESEKMAKDTSDEVSLNPTSEKLNNLLEGNDSDNDLSLEDF
Predicted GO terms:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0016032 (viral process), GO:0019058 (viral life cycle)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0018995 (host cellular component), GO:0033643 (host cell part), GO:0043657 (host cell), GO:0033646 (host intracellular part), GO:0043656 (host intracellular region), GO:0030430 (host cell cytoplasm)
Protein: Large ribosomal subunit protein eL38 (60S ribosomal protein L38) (P49167)
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:14562095, ECO:0000269|PubMed:22096102}.
InterPro domains:
- IPR038464: Large ribosomal subunit protein eL38 superfamily (homologous_superfamily) [1-78]
- IPR002675: Large ribosomal subunit protein eL38 (family) [1-77]
Sequence:
MAREITDIKQFLELTRRADVKTATVKINKKLNKAGKPFRQTKFKVRGSSSLYTLVINDAGKAKKLIQSLPPTLKVNRL
Predicted GO terms:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005198 (structural molecule activity), GO:0003735 (structural constituent of ribosome)
Biological Process (BP): GO:0008150 (biological process), GO:0009987 (cellular process), GO:0071840 (cellular component organization or biogenesis), GO:0044085 (cellular component biogenesis), GO:0022613 (ribonucleoprotein complex biogenesis), GO:0042254 (ribosome biogenesis), GO:0042274 (ribosomal small subunit biogenesis)
Cellular Component (CC): GO:0005575 (cellular component), GO:0032991 (protein-containing complex), GO:0110165 (cellular anatomical entity), GO:1990904 (ribonucleoprotein complex), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005829 (cytosol), GO:0005737 (cytoplasm), GO:0044391 (ribosomal subunit), GO:0043229 (intracellular organelle), GO:0022626 (cytosolic ribosome), GO:0043228 (non-membrane-bounded organelle), GO:0015934 (large ribosomal subunit), GO:0043232 (intracellular non-membrane-bounded organelle), GO:0022625 (cytosolic large ribosomal subunit), GO:0005840 (ribosome)
Protein: Meiotic recombination protein REC114 (Q9CWH4)
Organism: Mus musculus (Mouse)
Function: Required for DNA double-strand breaks (DSBs) formation in unsynapsed regions during meiotic recombination. Probably acts by forming a complex with IHO1 and MEI4, which activates DSBs formation in unsynapsed regions, an essential step to ensure completion of synapsis.
Subcellular location: Chromosome {ECO:0000269|PubMed:30569039}. Note=Located in discrete foci on the axes of meiotic chromosomes. The number of foci is highest at leptonema and decreases at zygonema. {ECO:0000269|PubMed:30569039}.
InterPro domains:
- IPR029168: Meiotic recombination protein REC114-like (family) [1-259]
Sequence:
MSEAGNVASGLGLPGEVSQWSLKRYGRFMLLDNVGSPGPSSEAAAAGSPTWKVFESSEESGSLVLTIVVSGHFFISQGQTLLEGFSLIGSKNWLKIVRRMDCLLFGTTIKNKSRMFRVQFSGESKEEALERCCGCVQTLAQYVTVQEPDSTTQELQQSQGPREAGESQGKDPLQQGPSLTLEQHVCMAAGAGVLQERTSVTHRAQSILAPEKLTLAYEGSSWGTEELGPFLRLCLMDQNFPAFVEEVEKELKKITGLRN
Predicted GO terms:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0009987 (cellular process), GO:0000003 (reproduction), GO:0022414 (reproductive process), GO:0071840 (cellular component organization or biogenesis), GO:1903046 (meiotic cell cycle process), GO:0051321 (meiotic cell cycle), GO:0022402 (cell cycle process), GO:0007049 (cell cycle), GO:0070192 (chromosome organization involved in meiotic cell cycle), GO:0061982 (meiosis I cell cycle process), GO:0016043 (cellular component organization), GO:0045132 (meiotic chromosome segregation), GO:0007059 (chromosome segregation), GO:0140013 (meiotic nuclear division), GO:0045143 (homologous chromosome segregation), GO:0098813 (nuclear chromosome segregation), GO:0007129 (homologous chromosome pairing at meiosis), GO:0006996 (organelle organization), GO:0007127 (meiosis I), GO:0048285 (organelle fission), GO:0051276 (chromosome organization), GO:0000280 (nuclear division)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005737 (cytoplasm), GO:0005622 (intracellular anatomical structure)
Protein: Glutathione peroxidase (Q8I5T2)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Not known
InterPro domains:
- IPR036249: Thioredoxin-like superfamily (homologous_superfamily) [43-204]
- IPR013766: Thioredoxin domain (domain) [38-205]
- IPR000889: Glutathione peroxidase (family) [15-205]
Sequence:
MFFSMFIKFILPISFICYNFGKKFNMFSYFQKIKVSEQELLSSIYDYEVKDLSGSNVSMSKFKNKVLIIFNSASKCGLTKNHVEQFNKLHEKYNARGLEILAFPTSQFLNQEFDNTKDICTFNEKNKIKYNMFSPIEVNGDNTHPLFKYLKKNCDSMHDENGTLKSIGWNFGKFLVDKNGEVVNYFSPKTNPLDLEKIIIQLLQK
Predicted GO terms:
Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016209 (antioxidant activity), GO:0004601 (peroxidase activity), GO:0016491 (oxidoreductase activity), GO:0016684 (oxidoreductase activity, acting on peroxide as acceptor), GO:0004602 (glutathione peroxidase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0050896 (response to stimulus), GO:0006950 (response to stress), GO:0006979 (response to oxidative stress)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005737 (cytoplasm), GO:0012505 (endomembrane system), GO:0005794 (Golgi apparatus), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle)
Protein: Vitamin B6 transporter bsu1 (Amiloride transporter car1) (Changed amiloride resistance protein 1) (Vitamin B6 uptake protein 1) (P33532)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Thiamine-regulated, high affinity import carrier of pyridoxine, pyridoxal and pyridoxamine. Also imports, but does not export, amiloride and so confers sensitivity.
Subcellular location: Membrane {ECO:0000269|PubMed:15701794}; Multi-pass membrane protein {ECO:0000269|PubMed:15701794}. Note=During mitosis, also localizes to the septum.
InterPro domains:
- IPR011701: Major facilitator superfamily (family) [91-464]
- IPR036259: MFS transporter superfamily (homologous_superfamily) [66-500]
- IPR020846: Major facilitator superfamily domain (domain) [83-506]
Sequence:
MASKIASLFSPSETASKDQHENVAEDLELGTASSQSDGIHETNSEYDEKKREESPEVIDISNLISSDHPAHPQNWHWAKRWSIVFMFCLMQIYVIWTSNGFGSIEYSVMAQFNVSAQVATLCLSMNILGSGLGPMFLGPLSDIGGRKPVYFCSIFVYTVFNISCALPRNIVQMIISHFIIGVAGSTALTNVAGGIPDLFPEDTAGVPMSLFVWACAGGAIGAPMATGVDINAKYGWRWLYYINIIVGGFFLIVILIIPETLPIKVITRYENAKGRIVEGIPKNNLKEVLKKCKFVTTMGFRMMLTEPIILSMGLYNFYAYGISYFFLTAIWPVFYDTYKMSEMGASCTYLSGFVASTLLFLYQPIQDWIFRRDKAKNNGVARPEARFTSALFITLLFPAGMFLFAFTCHPPFPWMSPIVGNSMVTVANGHNWMCILNYLTDSYPLLSGSAVAAFTLPSFIGATVFAHVSQIMFNNMSVKWAVATMAFISISIPFIIYTFYFFGQRIRALSSLTGNKALKYLPLENN
Predicted GO terms:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005215 (transporter activity), GO:0022857 (transmembrane transporter activity), GO:0015101 (organic cation transmembrane transporter activity), GO:0015203 (polyamine transmembrane transporter activity)
Biological Process (BP): GO:0008150 (biological process), GO:0009987 (cellular process), GO:0051179 (localization), GO:0051234 (establishment of localization), GO:0055085 (transmembrane transport), GO:0006810 (transport), GO:0071702 (organic substance transport), GO:0071705 (nitrogen compound transport), GO:0015695 (organic cation transport), GO:0015846 (polyamine transport), GO:0015848 (spermidine transport)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005737 (cytoplasm), GO:0012505 (endomembrane system), GO:0043229 (intracellular organelle), GO:0005783 (endoplasmic reticulum), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle)
Protein: ACP24A4 (Q45WF5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Not known
InterPro domains:
- IPR051388: Serine protease inhibitor and venom toxin (family) [15-77]
- IPR002223: Pancreatic trypsin inhibitor Kunitz domain (domain) [23-77]
- IPR020901: Proteinase inhibitor I2, Kunitz, conserved site (conserved_site) [54-72]
- IPR036880: Pancreatic trypsin inhibitor Kunitz domain superfamily (homologous_superfamily) [15-77]
Sequence:
MKLLILLFVFIALASNSLALKNEICGLPAAANGNCLALFSRWSYDAQYNVCFNFIYGGCQGNDNSFESQEECINKCVE
Predicted GO terms:
Molecular Function (MF): GO:0003674 (molecular function), GO:0098772 (molecular function regulator activity), GO:0030234 (enzyme regulator activity), GO:0140678 (molecular function inhibitor activity), GO:0061134 (peptidase regulator activity), GO:0004857 (enzyme inhibitor activity), GO:0061135 (endopeptidase regulator activity), GO:0030414 (peptidase inhibitor activity), GO:0004866 (endopeptidase inhibitor activity), GO:0004867 (serine-type endopeptidase inhibitor activity)
Biological Process (BP): GO:0008150 (biological process), GO:0000003 (reproduction), GO:0019953 (sexual reproduction)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005576 (extracellular region), GO:0005615 (extracellular space)
Protein: Phytochrome-interacting ankyrin-repeat protein 2 [Cleaved into: Protein ANKYRIN REPEAT 6, mitochondrial] (Q9FNP4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes anthocyanin accumulation through interaction with PHYA, especially in response to far-red light, high light and sucrose treatment, probably by triggering A3G2XYLT/UF3GT expression. Required for gametophytes development as well as male-female gamete recognition during fertilization, possibly by regulating mitochondrial gene expression. Represses PHYA-mediated PIF3 phosphorylation.
Subcellular location: [Phytochrome-interacting ankyrin-repeat protein 2]: Cytoplasm {ECO:0000269|PubMed:21395597}. Nucleus {ECO:0000269|PubMed:21123745, ECO:0000269|PubMed:21395597}.; SUBCELLULAR LOCATION: [Protein ANKYRIN REPEAT 6, mitochondrial]: Mitochondrion {ECO:0000269|PubMed:21123745, ECO:0000269|PubMed:29312411}.
InterPro domains:
- IPR036770: Ankyrin repeat-containing domain superfamily (homologous_superfamily) [13-164]
- IPR002110: Ankyrin repeat (repeat) [28-129]
Sequence:
MLQEPSAAFSLRRNSFRRRSPRSNVDDRGWNPLHIKARKGDLKSVKQLLDQGMDVNALAWGPKSKGVSALHLAAEGGHIEVMDLLLERGANIDAKTWGSCGWTPLHAAAKERKREAVKFLVENGAFLADDITDTRFNPPVHYCHGLEWAYEEMKKLNSESSSSSGGDTSSSSDN
Predicted GO terms:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0051179 (localization), GO:0009987 (cellular process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0006725 (cellular aromatic compound metabolic process), GO:0034641 (cellular nitrogen compound metabolic process), GO:1901360 (organic cyclic compound metabolic process), GO:0044260 (cellular macromolecule metabolic process), GO:0006139 (nucleobase-containing compound metabolic process), GO:0043170 (macromolecule metabolic process), GO:0046483 (heterocycle metabolic process), GO:0006259 (DNA metabolic process), GO:0090304 (nucleic acid metabolic process), GO:0006260 (DNA replication), GO:0006261 (DNA-templated DNA replication)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0043229 (intracellular organelle), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle), GO:0005634 (nucleus)