Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A0A1D8PT03 | YCP4_CANAL | MKIAIIQYSTYGHITQLAKAVQKGVADAGYKADIFQVPETLPQEVLDKMHAPAKPTDIPIATNDTLTEYDAFLFGVPTRYGTAPAQFFEFWGATGGLWANGSLAGKPAGVFVSTSGQGGGQETTVRNFLNFLAHHGMPYIPLGYANAFALQSSMEEVHGGSPYGAGTFANVDGSRQPSTLELEIAEKQGEAFVKSATKLVKGSKKTNTTTTSKSAATSDAAGTTSGTAAGTSAATGAATGTSAPKESTKEASSSAKKEATNGTATRTQQSTKAPETAEKSSCSKCIIM | 1.6.5.2 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|PROSITE-ProRule:PRU00088}; | cellular response to oxidative stress [GO:0034599] | eisosome [GO:0032126]; fungal biofilm matrix [GO:0062040]; membrane [GO:0016020]; plasma membrane [GO:0005886] | FMN binding [GO:0010181]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955] | PF03358; | 3.40.50.360; | WrbA family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26325183}; Peripheral membrane protein {ECO:0000269|PubMed:26325183}. | CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2; Evidence={ECO:0000305|PubMed:26325183}; CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+); ... | null | null | null | null | FUNCTION: Flavodoxin-like protein (FLP) that plays a role in cell wall integrity, oxidative stress protection and virulence (PubMed:26087349, PubMed:26325183). FLPs act as NAD(P)H quinone oxidoreductases (PubMed:26325183). Reduces ubiquinone (coenzyme Q), enabling it to serve as an antioxidant in the membrane (PubMed:2... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D8PTL7 | TRK1_CANAL | MLYRVSGFYKRHTRNFTNIDYGYYIRNFIHHIASKIYPYAKVVLPNFRAAHYFYILTLVILGSILVYPVKTCAYIDVLFFTAGASTQAGLNTVNVNDLSLYQQIVLYLLATLATPIFIHGSLLFVRLYYFERHFDNIKERSLMDYRMRKSATLARLGSAPTMSSTRLNTFNNQVLGFQEREAEKGSSSSPQSSSSQTSQPVSTAYNDQGGNDIEHHSEPSDSDDDESGNGPVTFQEKIHFEEPQRPRSQRRHSRTDSGIKFSALPHPRRRKSIDPEDMYRSINMLQEHKKNQEAKSKGIQFLNIGSPVRRKSRSSNIEAF... | null | null | chloride transport [GO:0006821]; intracellular potassium ion homeostasis [GO:0030007]; potassium ion import across plasma membrane [GO:1990573]; response to toxic substance [GO:0009636] | chloride channel complex [GO:0034707]; membrane [GO:0016020]; plasma membrane [GO:0005886] | chloride channel activity [GO:0005254]; chloride transmembrane transporter activity [GO:0015108]; high-affinity potassium ion transmembrane transporter activity [GO:0140107]; potassium ion transmembrane transporter activity [GO:0015079] | PF02386; | null | TrkH potassium transport family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19175416}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:15485849, ECO:0000269|PubMed:19175416, ECO:0000269|PubMed:33069635}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29465; Evidence={ECO:0000269|PubMed:15485849, ECO:0000269|PubMed:19175416, EC... | null | null | null | null | FUNCTION: Potassium transporter that mediates K(+) influx, as well as Cl(-) efflux as a secondary function (PubMed:15485849, PubMed:19175416, PubMed:33069635). TRK1 is the major K(+) uptake transporter that regulates membrane potential and intracellular pH (PubMed:33069635). The TRK1-mediated Cl(-) efflux should serve ... | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
A0A1D9BZF0 | GCNA_MOUSE | MDSGSSSSSSSSGSSSGSCSTSGSGSTSGSSTTSSSSSSSSSSSSSSSSSSKEYMPELPKQRKASCVVIDSESDSDNTSDEKNTTVCEISSGDETSDIDRPGGQKLPLIVIDDDDDGSPDLKNTKQKSDEPQMSVLEKEGVECIGSDSTSPHDVCEIWDVCGSSNQTSSELEPEGEPESEAKGEPESEAKGEPESEAKGEPESEAKGESESEAKGEMETEAKGESESEAKGEMETEAKGESESEAKGEMETEAKGEPESEAKGEMETEAKGEPESEAKGEMETEAKGESESEAKGEMETEAKGESESEAKGEMETEAKGE... | null | null | DNA damage response [GO:0006974]; DNA integrity checkpoint signaling [GO:0031570]; homologous chromosome pairing at meiosis [GO:0007129]; homologous recombination [GO:0035825]; meiotic chromosome condensation [GO:0010032]; protein-DNA covalent cross-linking repair [GO:0106300] | condensed chromosome [GO:0000793]; PML body [GO:0016605] | null | null | null | Serine-aspartate repeat-containing protein (SDr) family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:31839538}. Nucleus, PML body {ECO:0000269|PubMed:31839538}. Nucleus {ECO:0000269|PubMed:27718356}. Note=Co-localizes with SUMO2 at PML bodies in all interphase cells (By similarity). Localizes on condensed chromosomes in spermatocytes in G2 and M during meiotic proph... | null | null | null | null | null | FUNCTION: May play a role in DNA-protein cross-links (DPCs) clearance through a SUMO-dependent recruitment to sites of DPCs, ensuring the genomic stability by protecting germ cells and early embryos from various sources of damage (PubMed:31839538). Can resolve the topoisomerase II (TOP2A) DPCs (PubMed:31839538). {ECO:0... | Mus musculus (Mouse) |
A0A1E1FFL0 | PRHA_PENBI | MAPMIPPRLQRFPATASADEIFAAFQEDGCVVIEGFISPEQVARFSQEVDPAMEKIPVEVTNNGNSNDRTKRFSKCVIASPTFRNEIIESDLMHELCDRVFSKPGEGMGYHFNDNMVIEVQPGAPAQRLHRDQELYPWWNSMGPAGPECVINFFCAVTPFTEENGATRLVPGSHLWPEFTQINERDCPQFGKIETVPAIMQPGDCYLMSGKVIHGAGHNATTTDRRRALALAIIRRELRPMQAFSLSVPMKLAREMSERSQTMFGFRSSVQHCDVDMVHFWGNDGKDIAHHLGLEAPSVHV | 1.14.11.- | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:Q4WAW9}; | paraherquonin biosynthetic process [GO:0140874] | null | dioxygenase activity [GO:0051213]; metal ion binding [GO:0046872] | PF05721; | 2.60.120.620; | PhyH family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + preaustinoid A1 = berkeleyone B + CO2 + H2O + succinate; Xref=Rhea:RHEA:65184, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:69025, ChEBI:CHEBI:69026; Evidence={ECO:0000269|PubMed:27602587, ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48.3 uM for preaustinoid A1 {ECO:0000269|PubMed:29317628}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:27602587, ECO:0000269|PubMed:29317628}. | null | null | FUNCTION: Multifunctional dioxygenase; part of the gene cluster that mediates the biosynthesis of paraherquonin, a meroterpenoid with a unique, highly congested hexacyclic molecular architecture (PubMed:27602587). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide syn... | Penicillium brasilianum |
A0A1E3P8S6 | EAT1_WICAA | MFFTKVLNNQVANGLKQLPVHKRVQMAYDLHIPNKTVNPNLNIRSHEPIVFVHGIFGSKKNYRHDCQKIANVTHTPVYTIDLRNHGQSMHALPFDYETLAQDVTDFCEDHGLKKVNLIGYSLGAKICMLTMLQNPDLVRSGVIIDNSPIEQPHIEIFLTQFIKSMLHVLNSTKIRADDKDWKSKANQAMRRYIPNGGIRDYLLANLINKVPKGYKSPVINYDDGYIHFQNPVRHMTEVAVKNVSAWPTEHVKGLKFEGQVRFLKGTKSAFIDEKGLEAIKEYFPNYSLSELNATHFILNERPQEYVKLICDFIKVNRYKS... | 2.3.1.268; 3.1.1.-; 3.1.2.1 | null | cellular lipid metabolic process [GO:0044255] | mitochondrion [GO:0005739] | acetyl-CoA hydrolase activity [GO:0003986]; carboxylic ester hydrolase activity [GO:0052689]; transferase activity [GO:0016740] | PF00561; | 3.40.50.1820; | AB hydrolase superfamily | null | SUBCELLULAR LOCATION: Mitochondrion. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ethanol = CoA + ethyl acetate; Xref=Rhea:RHEA:55972, ChEBI:CHEBI:16236, ChEBI:CHEBI:27750, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.268; Evidence={ECO:0000269|PubMed:28356220}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289, ChE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.12 mM for acetyl-CoA (for acetyl-CoA hydrolase reaction) {ECO:0000269|PubMed:28356220}; KM=2.43 mM for ethanol (for alcohol acetyltransferase reaction) {ECO:0000269|PubMed:28356220}; | null | null | null | FUNCTION: Alcohol acetyltransferase that catalyzes the synthesis of ethyl acetate from ethanol and acetyl-CoA. Can also function as a thioesterase by hydrolyzing acetyl-CoA in the absence of ethanol, as well as esterase hydrolyzing ethyl acetate. {ECO:0000269|PubMed:28356220}. | Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8) (Yeast) (Hansenula anomala) |
A0A1F4 | EYS_DROME | MSNVHQFDTQTMAESPQIRRDMGRLCATWPSKDSEDGAGTALRAATPLTANGATTTGLSVTLAPKDMQRNHLLKMPTATIEKPTITATIASSSSTSTSTTRKSVTATRSLKLNPNILLPTLRILARGLLLPALILAILVGSSQAGFACLSNPCVFGVCIDGLNSSYSCYCIDGYTGIQCQTNWDECWSSPCQNGGTCVDGVAYYNCTCPEGFSGSNCEENVDECMSNPCQNGGLCRDRTNGYICTCQPGYLGSHCELDVAVCETGTGARCQHGGECIEGPGLEFTCDCPAGWHGRICQEEINECASSPCQNGGVCVDKLA... | null | null | cell morphogenesis [GO:0000902]; rhabdomere development [GO:0042052]; temperature compensation of the circadian clock [GO:0010378] | cell surface [GO:0009986]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; non-motile cilium [GO:0097730] | calcium ion binding [GO:0005509]; extracellular matrix structural constituent [GO:0005201] | PF00008;PF12661;PF02210; | 2.60.120.200;2.10.25.10; | EYS family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:17011488, ECO:0000269|PubMed:17036004}. Note=Secreted by photoreceptor cells, through the stalk membrane into the interrhabdomeral space (IRS). Although secreted, lacks a canonical signal sequence and ... | null | null | null | null | null | FUNCTION: Essential for the formation of matrix-filled interrhabdomeral space: critical for the formation of epithelial lumina in the retina. Acts together with prominin (prom) and the cell adhesion molecule chaoptin (chp) to choreograph the partitioning of rhabdomeres into an open system. {ECO:0000269|PubMed:17011488,... | Drosophila melanogaster (Fruit fly) |
A0A1I9LM04 | CNDD2_ARATH | MAPPFVFPQILRALEEDPEDNHRLFAQNPVDVTSLRPSDLEEFVKGVSFDLSDRELFCVEDQDVFDRVYSLVRSFFSLPPSCKCNLVESLRSNLSVLLPNVDSISRSVQDQEDDVPIIDRITSHRNALKIYTFFLLTVVMNEESHISSVETTKVAARGRKKQIIQSWNWEPQRGRMLNLIANSLEINLSLLFGSSDLDENYLSFIVKNSFTLFENATILKDAETKDALCRIIGASATKYHYIVQSCASIMHLIHKYDFAVVHIADAVARAESKYSDGTLAVTIIRDIGRTDPKAYVKDTAGADNVGRFLVELADRLPKLM... | null | null | cell division [GO:0051301]; chromatin organization [GO:0006325]; meiotic chromosome condensation [GO:0010032]; mitotic cell cycle [GO:0000278]; mitotic chromosome condensation [GO:0007076] | condensed chromosome, centromeric region [GO:0000779]; nucleus [GO:0005634] | histone binding [GO:0042393] | PF12717;PF12922; | 1.25.10.10; | CND1 (condensin subunit 1) family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:25065716}. Nucleus {ECO:0000250|UniProtKB:Q15021}. Note=Associates with the chromosomes throughout meiosis. {ECO:0000269|PubMed:25065716}. | null | null | null | null | null | FUNCTION: Essential protein (PubMed:23929493). Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes (By similarity). The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisome... | Arabidopsis thaliana (Mouse-ear cress) |
A0A1I9LMX5 | PCEP9_ARATH | MKLLSITLTSIVISMVFYQTPITTEARSLRKTNDQDHFKAGFTDDFVPTSPGNSPGVGHKKGNVNVEGFQDDFKPTEGRKLLKTNVQDHFKTGSTDDFAPTSPGHSPGVGHKKGNVNVESSEDDFKHKEGRKLQQTNGQNHFKTGSTDDFAPTSPGNSPGIGHKKGHANVKGFKDDFAPTEEIRLQKMNGQDHFKTGSTDDFAPTTPGNSPGMGHKKGDDFKPTTPGHSPGVGHAVKNDEPKA | null | null | cellular response to nitrogen starvation [GO:0006995]; nitrate import [GO:1902025]; regulation of lateral root development [GO:2000023]; regulation of leaf morphogenesis [GO:1901371]; regulation of root development [GO:2000280]; response to ammonium ion [GO:0060359]; response to auxin [GO:0009733]; response to nitrogen... | apoplast [GO:0048046] | hormone activity [GO:0005179] | null | null | C-terminally encoded plant signaling peptide (CEP) family | PTM: Hydroxylated peptide is more active than non-hydroxylated peptide. {ECO:0000269|PubMed:24179096}.; PTM: The mature small signaling peptide is generated by proteolytic processing of the longer precursor. {ECO:0000269|PubMed:25324386}. | SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.2]: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25324386}. Note=Accumulates in xylem sap under nitrogen (N)-starved conditions. {ECO:0000269|PubMed:25324386}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.3]: Secreted, extracellular space, a... | null | null | null | null | null | FUNCTION: Extracellular signaling peptide that represses primary root growth rate and significantly inhibits lateral root formation. Modulates leaf morphology (PubMed:24179096). Regulates systemic nitrogen (N)-demand signaling. Mediates up-regulation of genes involved in N uptake and assimilation pathways (PubMed:25324... | Arabidopsis thaliana (Mouse-ear cress) |
A0A1I9LN01 | LAF3_ARATH | MTGWYEFPVMIGFVSAAVFLLISVAYLPLLNDLYWSTLKSLTPPAGIVADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWGGELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGTTDELSWKDFQDVYLYADSSKKMMIRTCLFFPITTWSRLLDLK... | 3.5.-.- | null | de-etiolation [GO:0009704]; response to far red light [GO:0010218]; seed germination [GO:0009845] | membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471] | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810] | PF07969; | 3.10.310.70;3.20.20.140;2.30.40.10; | Metallo-dependent hydrolases superfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14645728}. | null | null | null | null | null | FUNCTION: Required for phyA-controlled responses to continuous far-red light (FRc) conditions, including the inhibition of hypocotyl elongation and the regulation of XTH15/XTR7 expression. {ECO:0000269|PubMed:14645728}. | Arabidopsis thaliana (Mouse-ear cress) |
A0A1J1DL12 | RIDA_DERFA | MSPKRIISTPLAPQPIGPYSQAVQVGNTVYLSGQIGMNVRTNEMVTGPIRDEAQQAFTNMKAVVEASGAKMSDVVKVNIFIRNFNDFPAINDVMKEFFQSPFPARSTVGVAELPKNARVEIESIVVIE | 3.5.99.10 | null | organonitrogen compound catabolic process [GO:1901565] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739] | 2-iminobutanoate deaminase activity [GO:0120242]; 2-iminopropanoate deaminase activity [GO:0120243]; deaminase activity [GO:0019239] | PF01042; | 3.30.1330.40; | RutC family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52758}. | CATALYTIC ACTIVITY: Reaction=2-iminobutanoate + H2O = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:39975, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:76545; EC=3.5.99.10; Evidence={ECO:0000305|PubMed:27539850}; CATALYTIC ACTIVITY: Reaction=2-iminopropanoate + H2O = NH4(+) + pyruvate; Xref=Rhea:RHEA:... | null | null | null | null | FUNCTION: Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism (PubMed:27539850). May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediat... | Dermatophagoides farinae (American house dust mite) |
A0A1L3THR9 | CDA_PESTX | MLAPLFAALLAGAATASPIQERQSSVPVGTIITACTVPNTFALTFDDGPFAYTSELLDLLSSNGVKATFFLNGQNWGSIYDYTSVVTRMDAEGHQIGSHTWSHADLATLDAAGITSQMTQLETALTSILGKVPTYMRPPYFSTNALALSTLGGLGYHVINANIDTLDYEHDDDTIGVAFTNFQNGLASGGTVSLMHDVHAQTVHVLVQEAINAIKAKGLTPVTVGTCLGDASANWYKSGGGSGTTPPPATGGPSPDDTCGGSNGYVCQNSQCCSQWGWCGTTSEYCAAGCQAAYGPCT | 3.5.1.41 | COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q6DWK3}; | cell wall organization [GO:0071555]; chitin catabolic process [GO:0006032]; evasion of host immune response [GO:0042783]; polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576] | chitin binding [GO:0008061]; chitin deacetylase activity [GO:0004099]; metal ion binding [GO:0046872] | PF00187;PF01522; | 3.30.60.10;3.20.20.370; | Polysaccharide deacetylase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27901067}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089, ChEBI:CHEBI:57704; EC=3.5.1.41; Evidence={ECO:0000269|PubMed:27901067}; PhysiologicalDirection=le... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:27901067}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:27901067}; | FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine polymers in chitin to form chitosan and acetate (PubMed:27901067). May play a role in evasion of the host immune response; plant chitinases liberate chitin molecules from the fungal cell wall which act as elicitors of the plant immune response, deace... | Pestalotiopsis sp |
A0A1L4BJ46 | HEMI1_HEMLE | MTFLILTILATVTPSLYSHVVQRELRVNFEPLAGQRDSWPVARAAMVTFDARSEKAREFSECRMINSMHELSRELMDSPEHTVKRASKEEMDDLVQRCSGSAEGRSWFIWPDTKWCGPGTDAKNESDLGPLEADKCCRTHDHCDYIGAGETKYGLTNKSFFTKLNCKCEAAFDQCLKESIDRAEGSAKSSMEGLHSFYFNTYSPECYEVKCSRKRDAECTNGIAIWKDSYKS | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:26335363}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:26335363}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium-dependent phospholipase A2 activity [GO:0047498]; metal ion binding [GO:0046872] | PF05826; | 1.20.90.10; | Phospholipase A2 family, Group III subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26335363}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:26335363}; | null | null | null | null | FUNCTION: Scorpion venom phospholipase A2 (PLA2) that shows high hydrolytic activities towards lecithin and acts as an effective blocker of all angiogenesis key steps in vivo and in vitro (PubMed:26335363). It has no effect on apoptosis and does not display hemolytic, inflammatory or neurotoxic effects (PubMed:26335363... | Hemiscorpius lepturus (Scorpion) |
A0A1L4BJ98 | DTPLD_HEMLE | MAHCYYNSKRGCNRVMKTVALVVLISTVMVEESRGDSQEDKKRPIWNIGHMVNAVKQIEEFLDLGANALEADVTFDDNGNPKWTYHGTPCDCFRDCLRWEYVDEYLKRIRELTSPGSSKFRKGFILLMLDLKISKLSDNAKSKAGKEIADMIIKRLWSGSGEKAQLYIVLSFPYVNDIEFVRAFRERVKSKGFASEAEKRIGWDISGNEDLGKIRDAYQKLGITDNVWQSDGITNCLTRSHDRLAEAVCKRDSDKEWPSLKKVYYWTVDKQSSMKEALKVGVDGMITNDPDDLVAVLNEFSGTHRLANINDSPWQKIPRP... | 4.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:28335389}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914}; | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; toxin activity [GO:0090729] | PF13653; | 3.20.20.190; | Arthropod phospholipase D family, Class II subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28335389}. | CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652, ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892; Evidence={ECO:0000305|PubMed:28335389}; CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N... | null | null | null | null | FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) with a high activity (PubMed:28335389). ... | Hemiscorpius lepturus (Scorpion) |
A0A1L4BKS3 | TERL_BPG20 | MKRLRPSDKFFELLGYKPHHVQLAIHRSTAKRRVACLGRQSGKSEAASVEAVFELFARPGSQGWIIAPTYDQAEIIFGRVVEKVERLSEVFPTTEVQLQRRRLRLLVHHYDRPVNAPGAKRVATSEFRGKSADRPDNLRGATLDFVILDEAAMIPFSVWSEAIEPTLSVRDGWALIISTPKGLNWFYEFFLMGWRGGLKEGIPNSGINQTHPDFESFHAASWDVWPERREWYMERRLYIPDLEFRQEYGAEFVSHSNSVFSGLDMLILLPYERRGTRLVVEDYRPDHIYCIGADFGKNQDYSVFSVLDLDTGAIACLERM... | 3.1.21.-; 3.6.4.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:28100693}; Note=Nuclease activity requires 2 Mg(2+) ions per subunit (PubMed:28100693). Also active in the presence of Mn(2+) or Co(2+) but inactive with Ni(2+), Zn(2+) or Ca(2+) (PubMed:28100693). Cu(2+), Cd(2+) and Cs(2+) do not support catal... | chromosome organization [GO:0051276]; viral DNA genome packaging [GO:0019073] | viral terminase, large subunit [GO:0098009] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872] | PF17289;PF03237; | 3.30.420.240;3.40.50.300; | Tequatrovirus large terminase family | null | null | null | null | null | null | null | FUNCTION: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a sma... | Thermus phage G20c (Thermus thermophilus phage G20c) |
A0A1L5YRA2 | TPIS_SCYPA | MANQRKFFVGGNWKMNGDKAAIDGIISFMKGPLNADTEVVVGCPQCYLMYTREHMPANIGVAAQNCYKTAKGAFTGEISPAMIKDCGCEWVILGHSERRNVFGEPDQLISEKVGHALEAGLKVIPCIGEKLEERESNRTEEVVFAQMKALVPNISDWSRVVIAYEPVWAIGTGKTATPEQAQDVHAKLRQWLRDNVSPQVAESTRIIYGGSVSAGNCKELAKTGDIDGFLVGGASLKPDFVTIINARA | 4.2.3.3; 5.3.1.1 | null | gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol catabolic process [GO:0019563]; glycolytic process [GO:0006096]; methylglyoxal biosynthetic process [GO:0019242] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | IgE binding [GO:0019863]; methylglyoxal synthase activity [GO:0008929]; protein homodimerization activity [GO:0042803]; triose-phosphate isomerase activity [GO:0004807] | PF00121; | 3.20.20.70; | Triosephosphate isomerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}; CATALYTIC ACTIVITY: Reaction=dihydroxyacetone phosphate = methylglyoxal + phosph... | null | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}. | null | null | FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. {ECO:0000250|UniProtKB:P00939}.; FUNCTION: It is also responsible for the non-negligible p... | Scylla paramamosain (Mud crab) |
A0A1L6K371 | JUGN4_JUGNI | MAKPILLSISLCLVALVNGCLAQSGGRQQPRFGECKLKRLVALEPSNRIEAEAGVIESWDPNNQQFQCAGVAVVRRTIEPNGLLLPQYSNAPQLLYIVKGRGITGVLFPGCPETFEESQQGQSRIRPSLRSASFQRDRHQKIRHFREGDVIAFPAGVAHWCYNDGDTPVVAVALMDTTNNANQLDQNPRNFYLAGNPDDEFRPQGQQEYEQHRRQQQHQQRHGEPGQQQRGSGNNVFSGFDADFLADAFNVDTETARRLQSENDHRRSIVRVEGRQLQVIRPRWSREEQEREERKERERERESESERRQSRRGGRDDNGL... | null | null | seed maturation [GO:0010431] | extraorganismal space [GO:0043245] | IgE binding [GO:0019863]; nutrient reservoir activity [GO:0045735] | PF00190; | 2.60.120.10; | 11S seed storage protein (globulins) family | PTM: Proteolytically processed from a single precursor to produce an acidic and a basic chain that are linked by a disulfide bond. {ECO:0000269|PubMed:27936684}. | null | null | null | null | null | null | FUNCTION: Seed storage protein. {ECO:0000255|RuleBase:RU003681, ECO:0000305|PubMed:27936684}. | Juglans nigra (Black walnut) (Wallia nigra) |
A0A1L6Z3A0 | TPS8_PSEAD | MSRFTSATHGLNLSIKMPISVSQVPSIRSNTSKYELQKLRSTGRSVLQTRRQLAIINMTKRSEADDNDGVERRKGVFHPNLWDDGFIQSLSTVYHEQASYRERAERLIGEVKAVFDSISMGDGDQFISPSAYDTAWVARVPAIDGSSRPQFPQAIDWILLNQQQDGSWGSQSHLSLTHRLTDTLACVIALASWKIESVQIDEGLDFITRGVEKLQSESVPAEFEIIFAELLNQAKSLQLSLPYEHSCLQSLWRKQEPILANGLMDSVAKRSLSSLEEMQDHRMNTDSDGTMHVESFLSSPAVAARVLMRTGNPICLAYLN... | 4.2.3.180 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:28096378}; | gibberellin biosynthetic process [GO:0009686] | chloroplast [GO:0009507] | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.50.10.160;1.10.600.10;1.50.10.130; | Terpene synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = diphosphate + pseudolaratriene; Xref=Rhea:RHEA:54116, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:138050; EC=4.2.3.180; Evidence={ECO:0000269|PubMed:28096378}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54117; Evidence={ECO:0000269|Pu... | null | PATHWAY: Terpene metabolism. {ECO:0000305}. | null | null | FUNCTION: Converts geranylgeranyl diphosphate to an new 5,7-fused bicyclic diterpene, named pseudolaratriene (PubMed:28096378). Catalyzes the first committed step in pseudolaric acid B (PAB) biosynthesis (PubMed:28096378). PAB exhibits antiproliferative activity by inhibiting microtubule polymerization, and has demonst... | Pseudolarix amabilis (Golden larch) (Pseudolarix kaempferi) |
A0A1L7NQ96 | KET3E_ARTGO | MKIGCHGLVWTGHFDAEGIRYSVQKTREAGFDLVEFPLMDPFSFDVQTAKSALAEHGLAASASLGLSDATDVSSEDPAVVKAGEELLNRAVDVLAELGATDFCGVIYSAMKKYMEPATAAGLANSKAAVGRVADRASDLGINVSLEVVNRYETNVLNTGRQALAYLEELNRPNLGIHLDTYHMNIEESDMFSPILDTAEALRYVHIGESHRGYLGTGSVDFDTFFKALGRIGYDGPVVFESFSSSVVAPDLSRMLGIWRNLWADNEELGAHANAFIRDKLTAIKTIELH | 5.1.3.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27713017}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:27713017, ECO:0000269|PubMed:30279320}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:27713017}; Note=Binds 1 divalent metal cation per subunit. Se... | carbohydrate metabolic process [GO:0005975] | null | manganese ion binding [GO:0030145]; racemase and epimerase activity, acting on carbohydrates and derivatives [GO:0016857] | PF01261; | 3.20.20.150; | Hyi family | null | null | CATALYTIC ACTIVITY: Reaction=L-ribulose = L-xylulose; Xref=Rhea:RHEA:53268, ChEBI:CHEBI:16880, ChEBI:CHEBI:17399; Evidence={ECO:0000269|PubMed:30279320}; CATALYTIC ACTIVITY: Reaction=D-allulose = keto-D-fructose; Xref=Rhea:RHEA:42360, ChEBI:CHEBI:27605, ChEBI:CHEBI:48095; Evidence={ECO:0000269|PubMed:27713017, ECO:0000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31 mM for D-allulose {ECO:0000269|PubMed:27713017}; KM=37.5 mM for D-fructose {ECO:0000269|PubMed:27713017}; Vmax=177 umol/min/mg enzyme for the epimerization of D-allulose {ECO:0000269|PubMed:27713017}; Vmax=78.4 umol/min/mg enzyme for the epimerization of D-fruct... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. Is stable from pH 6.0-11.0. {ECO:0000269|PubMed:27713017}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. Is highly stable at 55 degrees Celsius. {ECO:0000269|PubMed:27713017}; | FUNCTION: Catalyzes the reversible C-3 epimerization of several ketoses. Shows the highest enzymatic activity for the epimerization of L-ribulose to L-xylulose. Is also able to convert D-allulose (also known as D-psicose) to D-fructose and, to a lesser extent, L-tagatose to L-sorbose, D-ribulose to D-xylulose, L-allulo... | Arthrobacter globiformis |
A0A1L8F5J9 | NMDZ1_XENLA | MGTMRLFLLAVLFLFSFARAGCDPKIVNIGAVLSTKKHEQIFREAVNQANKRHFTRKIQLNATSVTHRPNAIQMALSVCEDLISSQVYAILVSHPPAPTDHLTPTPISYTAGFYRIPVIGLTTRMSIYSDKSIHLSFLRTVPPYSHQALVWFEMMRLFNWNHVILIVSDDHEGRAAQKKLETLLEEKESKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAAMLDMTGAGYVWLVGEREISGSALRYAPDGIIGLQLINGKNESAHISDAVAVVAQAIHELFEMENITDPPRGCVGNTNIWKTGPL... | null | null | chemical synaptic transmission [GO:0007268]; regulation of membrane potential [GO:0042391]; response to zinc ion [GO:0010043] | neuron projection [GO:0043005]; NMDA selective glutamate receptor complex [GO:0017146]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211] | metal ion binding [GO:0046872]; NMDA glutamate receptor activity [GO:0004972] | PF01094;PF00060;PF10613;PF00497; | 3.40.50.2300;3.40.190.10; | Glutamate-gated ion channel (TC 1.A.10.1) family, NR1/GRIN1 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19524674, ECO:0000269|PubMed:21677647, ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:26912815, ECO:0000269|PubMed:27135925, ECO:0000269|PubMed:28232581, ECO:0000269|Ref.11}; Multi-pass membrane protein {ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:27062927, E... | null | null | null | null | null | FUNCTION: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, pl... | Xenopus laevis (African clawed frog) |
A0A1L8FDW4 | PEX5_XENLA | MAMRGLIEAECGGSNPLMKLTNHFTQDKALREEGLQHVSWPPGATVVSKPLGEATEDELVSEFLHTRAPSLQSRAPHTFKMDGLLAEMQEIEQSSFRPEPLRAPGVADLALSEQWSAEFLGVEVDPVEEEDWSREFTEQADPHASPSRWAEEYLQQSEEKLWLGESEGAMAEKWTEEYQPEDDLQREAKSLVSQVTDPKLANTQFLQFVKRIGDGELSFSHAPSTPSQTVSQAEQWSEQFVHEQAEQWVDQFAPLEKDFEKAKAAVESDVDFWDKLQEEWEEMAKRDAEAHPWLSDFQDLSSKSIDKGYMFEDNNPFSEV... | null | null | pexophagy [GO:0000425]; protein import into peroxisome matrix, docking [GO:0016560]; protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein import into peroxisome matrix, substrate release [GO:0044721]; protein import into peroxisome matrix, translocation [GO:0016561] | cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778] | peroxisome matrix targeting signal-1 binding [GO:0005052]; protein carrier chaperone [GO:0140597] | PF13432;PF13181; | 1.25.40.10; | Peroxisomal targeting signal receptor family | PTM: Monoubiquitinated at Cys-11 by pex2 during pex5 passage through the retrotranslocation channel (By similarity). Cys-11 monoubiquitination acts as a recognition signal for the pex1-pex6 complex and is required for pex5 extraction and export from peroxisomes (PubMed:35931083). When pex5 recycling is compromised, pol... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:35931083}. Peroxisome matrix {ECO:0000269|PubMed:35931083}. Note=Cycles between the cytosol and the peroxisome matrix (PubMed:35931083). Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the dockin... | null | null | null | null | null | FUNCTION: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) (PubMed:35931083). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing throu... | Xenopus laevis (African clawed frog) |
A0A1L8G2K9 | SPRTN_XENLA | MGDMQMSVVDPTWELLDPNPDIRALFLEFNDTFFWGQLSGVEVKWSARMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVETLLHEMIHALLFVTHNNKDHDSHGPEFCKHMERINGRTGANISVYHNFHDEVDEYRKHWWLCNGPCQKRKPYFGYVKRAMNRAPSSLDPWWADHQRTCGGSFVKVKEPENYPQKRKRKNDPTISEVNSSSHVKGKSNGVDIRTVIPFSGTGYKLFEPNKSDAPLKILNINPTKDKAAVPLLNHTPPSTNINGTFLTNKIGSAKSTPAQSILTKVSVANTKVFINLNGSPIKLPSGS... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040}; | DNA damage response [GO:0006974]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508] | chromatin [GO:0000785]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; polyubiquitin modification-dependent protein binding [GO:0031593]; single-stranded DNA binding [GO:0003697] | PF10263; | 3.30.160.60; | Spartan family | PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000269|PubMed:30595436}. Note=Localizes to sites of UV damage via the PIP-box (By similarity). Recruited to stalled replication forks at sites of replication stress (By similarity). {ECO:0000250|UniProtKB:Q9H040}. | null | null | null | null | null | FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (PubMed:30595436, PubMed:35534579, PubMed:36608669). DPCs are highly toxic DNA lesions that interfere with esse... | Xenopus laevis (African clawed frog) |
A0A1L8GSA2 | TET3A_XENLA | MMETQPTSLPHVLPQDVYEFCDDRKSLGRLRVSEMPAESNGDGGGSKGDGAAVVAKEVPEQSNKKRKRCGVCVPCLRKEPCGACYNCVNRSTSHQICKMRKCEQLKKKRVVPLKGVEAVNKDDSKNQAKEQVPNVKNCSESILVDGPKTDQMEAGPVNHVQEGRLKKECDSTLPSKACEDLANQLLMEANSWLSNTAAPQDPCNKLNWDKPTIPNHTAATNNSNLEDAKNLVAFSAVAEAMSNYGMPASGTPSSVSMQLYEKFNYETNRDSSGHPEGNAPSCPEDLNTLKTALALAKHGVKPPNCNCDGPECPDYLEWLE... | 1.14.11.80 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6N021}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=The zinc ions have a structural role. {ECO:0000250|UniProtKB:Q6N021}; | 5-methylcytosine catabolic process [GO:0006211]; DNA demethylation [GO:0080111]; eye development [GO:0001654]; nervous system development [GO:0007399]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; positive regulation of transcription by RNA polymerase II [GO:0045944] | chromosome [GO:0005694]; nucleus [GO:0005634] | 5-methylcytosine dioxygenase activity [GO:0070579]; methyl-CpG binding [GO:0008327]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF12851;PF02008; | null | TET family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0JP82}. Chromosome {ECO:0000250|UniProtKB:A0JP82}. Note=Detected on chromatin, where it binds to target gene promoters. {ECO:0000250|UniProtKB:A0JP82}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-methyl-2'-deoxycytidine in DNA + O2 = a 5-hydroxymethyl-2'-deoxycytidine in DNA + CO2 + succinate; Xref=Rhea:RHEA:52636, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:13315, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85454, ChEBI:CHEB... | null | null | null | null | FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming during embryonic development. Conversion of 5mC into 5hmC probably constitutes the first step in cytosine demethylation. ... | Xenopus laevis (African clawed frog) |
A0A1L8GVF0 | RA50S_XENLA | MSKIEKMSIQGVRSFGINDKNKQVIQFFTPLTILVGPNGAGKTTIIECLKYMTTGDFPSGSKGNTFVYHPKLAHETDVRAQICLQLKDVNGEPVAVQRSIICRQKGKSTECKTVDCVITRIKHGGPVSLRPKCEEMNKEMISALGVSSAVLNNVIFCHQEDSNWPLSEGKRLKGKFDEIFSITRYSKALETLRDVRMKEDQNVSNYQEEIKYLKENKEKAREIQDNLQSKEKQLTVSKENVKSIESQLEPLKDRLADIQRNLFKVIRLENEIKALESRKRTMEQDNQDLMEKMEKVFQGTDEELNEMYQNQCFVREKERK... | 3.6.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q92878}; Note=Binds 1 zinc ion per homodimer. {ECO:0000250|UniProtKB:Q92878}; | chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA double-strand break processing [GO:0000729]; DNA duplex unwinding [GO:0032508]; DNA strand resection involved in replication fork processing [GO:0110025]; metaphase chromosome alignment [GO:0051310]; R-loop processing [GO:0062176]; telomere mainte... | chromosome, telomeric region [GO:0000781]; condensed nuclear chromosome [GO:0000794]; Mre11 complex [GO:0030870]; site of double-strand break [GO:0035861] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded telomeric DNA binding [GO:0003691]; G-quadruplex DNA binding [GO:0051880]; metal ion binding [GO:0046872]; protein serine/threonine kinase activator activity [GO:0043539]; single-stranded telomeric DNA binding [GO:0043047] | PF13476;PF04423;PF13558; | 3.40.50.300; | SMC family, RAD50 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92878}. Chromosome, telomere {ECO:0000250|UniProtKB:Q92878}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q92878}; | null | null | null | null | FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:19892829, PubMed:23434370). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an ... | Xenopus laevis (African clawed frog) |
A0A1L8GXM0 | RA50L_XENLA | MSKIEKMSIQGVRSFGIEDKNKQVIQFFTPLTVLVGPNGAGKTTIIECLKYITTGDFPPGSKGKTFVHDPKVAHETDVRAQIRLQLKDVNGELVAVQRSMICTQKGKSTEFKTLEGVITRIKHGEKVSLSTKCAEMDKEMISALGVSAAVLNNVIFCHQEDSNWPLSEGRQLKVKFDEIFSATRYIKALETLKKVRTQQAHNVREYQVEIKYLKQNKEKAREIQDNLQSKEKQLAVSKENVKSIESQLEPLKDRLADIQRNLSKVMRLDNEIKALESRKRTMEQDNQDLEEKMEKVFQGTDEELNGMYQNHQRSVREKER... | 3.6.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q92878}; Note=Binds 1 zinc ion per homodimer. {ECO:0000250|UniProtKB:Q92878}; | chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA double-strand break processing [GO:0000729]; DNA duplex unwinding [GO:0032508]; DNA strand resection involved in replication fork processing [GO:0110025]; metaphase chromosome alignment [GO:0051310]; R-loop processing [GO:0062176]; telomere mainte... | chromosome, telomeric region [GO:0000781]; condensed nuclear chromosome [GO:0000794]; Mre11 complex [GO:0030870]; site of double-strand break [GO:0035861] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded telomeric DNA binding [GO:0003691]; G-quadruplex DNA binding [GO:0051880]; metal ion binding [GO:0046872]; protein serine/threonine kinase activator activity [GO:0043539]; single-stranded telomeric DNA binding [GO:0043047] | PF13476;PF04423;PF13558; | 1.10.287.1490;3.40.50.300; | SMC family, RAD50 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92878}. Chromosome, telomere {ECO:0000250|UniProtKB:Q92878}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q92878}; | null | null | null | null | FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:19892829, PubMed:23434370). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an ... | Xenopus laevis (African clawed frog) |
A0A1L8HU22 | NEIL3_XENLA | MEALPPQVLKPLDCMSIYSRHREPENRHNELSTGRCGRGHVIFSSMKALQPQVLKPTGSHANLQQVLYAPAATIITAPASSHNDLSSLTGCSYAGVETLGKELFIYFGLKAMRVHFGMNGSMRINQPMKKGQENGRPIPIAVLEVQLTKDLICFYESTVDVRNASECQEKIRFFEELDVCSSKFSFPRAECEIKKQRTRMLCDILLDQMILPGVGNIIKNEALFDSGLHPGVQAGLLTDEQVSHLVKMTRDFTLLFYKCRKSGSALYKHYKVYKRPNCGQCGTKITVCRLGEHNRMTYFCPKCQKDKPQHVDVSKLPTRN... | 3.2.2.-; 4.2.99.18 | null | base-excision repair [GO:0006284]; interstrand cross-link repair [GO:0036297] | chromosome [GO:0005694]; nucleoplasm [GO:0005654] | class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA N-glycosylase activity [GO:0019104]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; MCM complex binding [GO:1904931]; zinc ion binding [GO:0008270] | PF06831;PF06839; | 1.10.8.50;3.20.190.10;2.30.30.380; | FPG family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TAT5}. Chromosome {ECO:0000269|PubMed:30842657}. Note=Recruited to replication stress sites via interaction with ubiquitinated CMG helicase. {ECO:0000269|PubMed:30842657}. | CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RH... | null | null | null | null | FUNCTION: DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA) (PubMed:30842657). Mediates interstrand cross-link repair in response to replication stress: recruited to replication stress sites via interaction with ub... | Xenopus laevis (African clawed frog) |
A0A1L8HV70 | DCK1_XENLA | MATPPKRICIDVPASPSGNKCKVKRISIEGNIAAGKSTFVNILKKANEEWDVVPEPIARWCNIQSCKDEFEELTTSQKSGGNLLQMMYEKPERWSFTFQSYACLSRIRAQLKALGGKLKEAENPVLFFERSVYSDRYIFASNLYEAECMNETEWTVYQDWHDWMNSQFGADLELDGIIYLRAIPEKCLNRVYTRGREEEQGIPMEYLEKLHYKHETWLHHRTLRTDFEYLQEIPILTLDVNEDFRDNKQKQESLIEKVKEFLSTL | 2.7.1.113; 2.7.1.74; 2.7.1.76 | null | deoxyribonucleoside monophosphate biosynthetic process [GO:0009157]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; deoxyadenosine kinase activity [GO:0004136]; deoxycytidine kinase activity [GO:0004137]; deoxyguanosine kinase activity [GO:0004138] | PF01712; | 3.40.50.300; | DCK/DGK family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27707}. | CATALYTIC ACTIVITY: Reaction=2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a ribonucleoside 5'-diphosphate + dCMP + H(+); Xref=Rhea:RHEA:20061, ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:57566, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=2.7.1.74; Evidence={ECO:0000269|PubMed:27906638}; CATALYTIC ACTIVITY: ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.34 uM for deoxycytidine {ECO:0000269|PubMed:27906638}; KM=527 uM for deoxyguanosine {ECO:0000269|PubMed:27906638}; KM=533 uM for deoxyadenosine {ECO:0000269|PubMed:27906638}; KM=12457 uM for deoxythymidine {ECO:0000269|PubMed:27906638}; KM=15081 uM for deoxyuridi... | null | null | null | FUNCTION: Phosphorylates the deoxyribonucleosides deoxyadenosine, deoxycytidine and deoxyguanosine with highest activity against deoxycytidine followed by deadenosine and deoxyguanosine (PubMed:27906638). Shows only very minor activity against deoxyuridine and deoxythymidine (PubMed:27906638). {ECO:0000269|PubMed:27906... | Xenopus laevis (African clawed frog) |
A0A1P8AQ95 | STMP4_ARATH | MTKNMTKKKMGLMSPNIAAFVLPMLLVLFTISSQVEVVESTGRKLSWAFNGAPIVFTPPSSSCGGSPAAVMASEWMPRRPCRRTRPPGTNIPVSQSP | null | null | response to ethylene [GO:0009723]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414] | apoplast [GO:0048046]; plasma membrane [GO:0005886] | LRR domain binding [GO:0030275]; receptor serine/threonine kinase binding [GO:0033612] | null | null | Serine rich endogenous peptide (SCOOP) phytocytokine family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31001913}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. Note=The precursor of STMP4 accumulates at the plasma membrane and is proteolytically cleaved to release the STMP4 in the apoplasm. {ECO:0000269|PubMed:31001913}. | null | null | null | null | null | FUNCTION: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation... | Arabidopsis thaliana (Mouse-ear cress) |
A0A1P8ASY1 | JHS1_ARATH | MPPRKKPKSSALKSNKQSSANHSSQPSTFGIQQLFLRHIQNSQSTSNSHTSTADPVDQQNVNGLASDTAVLTPQNPLGTSNEKPDESKDMDQQLTEASPKISKNLKRFSPGMLIKQSQDDCGGEITWKISPVNERLRAAAKNIPKMMDLTENSLGVKSSTIRPCSLNKLVQKQCPTSGITSKVEQWLSSPSKKASKRPAFATNRVMERVNPSPDAEFEIVNTSSSGNSPFQTPPSLSCPHNKLPCTVTCSGACGSMGAGQHKKALLELLDQVEDVIAVDDKTTDDVGIVMPQARVKDDIISSVVDCAVDEGPVSLPKMQN... | 3.1.-.-; 3.6.4.12 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P38859}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P38859}; | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; meristem maintenance [GO:0010073]; replication fork reversal [GO:0071932] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | 4 iron, 4 sulfur cluster binding [GO:0051539]; 5'-flap endonuclease activity [GO:0017108]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; single-stranded DNA helicase activity [GO:0017116] | PF13086;PF13087;PF08696; | 3.90.320.10;3.40.50.300; | DNA2/NAM7 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26951435}. Chromosome {ECO:0000250|UniProtKB:P51530}. Note=Localized to nuclear foci in response to DNA damage. {ECO:0000269|PubMed:26951435}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:P51530}; | null | null | null | null | FUNCTION: Essential protein required during embryogenesis (PubMed:15266054). Key enzyme involved in DNA replication and damage repair, shoot apical meristem (SAM) maintenance, and development (PubMed:26951435). Involved in Okazaki fragments processing. Possesses different enzymatic activities, such as single-stranded D... | Arabidopsis thaliana (Mouse-ear cress) |
A0A1P8AUY4 | MDN1_ARATH | MAIDGSFNLKLALETFSVRCPKVAAFPCFTSILSKGGEVVDNEEVIHALGDAFLHPEFTVPLVHCFLPIIRNVVDRVVGLLRLVDDLKSSIDYSDDVSSVLDNAMTEGISVIDFYVRRGQRLELHECACLAFSRALHFNTSLLGSILNYFEKAPPPYERILVKDIVSESRMEATDAYLLCLRVSYRFLVIRPEVFSKLWDWSCYLDSMKRLSECPRQQRHFLEKYRDAVWCGIQILSVVLRCSDRLAGCFGFEEEEALSCLLRWEEFCQDIEIEKAGLYIQLPTYTALKSLQQFNTLVPGINKRQSAGLEADEPQMKIRR... | null | null | abscisic acid-activated signaling pathway [GO:0009738]; embryo sac development [GO:0009553]; regulation of developmental growth [GO:0048638]; ribosomal large subunit export from nucleus [GO:0000055] | chloroplast envelope [GO:0009941]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasmodesma [GO:0009506]; preribosome, large subunit precursor [GO:0030687] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF07728;PF17865;PF17867;PF21108; | 3.40.50.300; | Midasin family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q12019}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q12019}. | null | null | null | null | null | FUNCTION: Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits. Functions at successive maturation steps to remove ribosomal factors at critical transition points, first driving the exit of early pre-60S particles from the nucleolus and then driving late pre-60S particles from the n... | Arabidopsis thaliana (Mouse-ear cress) |
A0A1P8AW69 | KTN81_ARATH | MAKRGYKLQEFVAHSGNVNCLSIGKKTSRLLLTGGDDYKVNLWSIGKTTSPMSLCGHTSPVDSVAFNSEEVLVLAGASSGVIKLWDLEESKMVRAFTGHRSNCSAVEFHPFGEFLASGSSDTNLRVWDTRKKGCIQTYKGHTRGISTIEFSPDGRWVVSGGLDNVVKVWDLTAGKLLHEFKCHEGPIRSLDFHPLEFLLATGSADRTVKFWDLETFELIGTTRPEATGVRAIAFHPDGQTLFCGLDDGLKVYSWEPVICRDGVDMGWSTLGDFCINEGKFIGCSYYRNSVGIWVSDISELEPYGAVSEDKNECMVKRFSV... | null | null | microtubule depolymerization [GO:0007019]; microtubule severing [GO:0051013]; regulation of unidimensional cell growth [GO:0051510] | cytoplasm [GO:0005737]; katanin complex [GO:0008352]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630] | microtubule binding [GO:0008017] | PF13925;PF00400; | 2.130.10.10; | WD repeat KATNB1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:28978669}. Note=Present in dynamic discrete particles specifically localized to microtubule (MT) crossovers and branching nucleation sites. {ECO:0000269|PubMed:28978669}. | null | null | null | null | null | FUNCTION: May participate in a complex which severs microtubules in an ATP-dependent manner (By similarity). Microtubule severing may promote rapid reorganization of cellular microtubule arrays (By similarity). Confers precision to microtubule (MT) severing by specific targeting of KTN1 to MT cleavage sites such as cro... | Arabidopsis thaliana (Mouse-ear cress) |
A0A1R3RGK0 | OTAA_ASPC5 | MTFTSHPQSEPLAIIGLACKYANDINSPLDLYQQVMAARSMHGPMPPSRMDAAFYYHPSSEATGTTYAKGGYFLQSDLNAFDSPFFQLSEIDVLAMDPQQKMLLENVYHALENAGIPLKDAVSSSTSVFVGCSNNDHLALANADLLLALKGKGTGTSPSILANRISWFYDFQGTSQTIDTACSSSLVAFHQGCMDVRAGKSTMSIISGVNLMEHPAPTMYLSSLGVLSPDGRSMSFDARANGYGRGEGLGTVIIKPLTAALRDGNRIRAIVRSTGSNQDGRTPGITVPSPTAQERLIREVYKAADLDPSRTGYVEAHGTG... | 2.3.1.- | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|PROSITE-ProRule:PRU00258}; | fatty acid biosynthetic process [GO:0006633]; methylation [GO:0032259]; ochratoxin A biosynthetic process [GO:1900818] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]; polyketide synthase activity [GO:0016218] | PF00698;PF08240;PF16197;PF00109;PF02801;PF08659;PF08242;PF21089;PF00550;PF14765; | 3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;3.40.50.150; | null | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 9 H(+) + 4 malonyl-CoA + 5 NADPH = 7-methylmellein + 3 CO2 + 5 CoA + 4 H2O + 5 NADP(+); Xref=Rhea:RHEA:72767, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:1925... | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:24699234, ECO:0000269|PubMed:30054361}. | null | null | FUNCTION: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of ochratoxin A (OTA), a mycotoxin composed of a chlorinated type I polyketide dihydroisocoumarin moiety linked to L-phenylalanine, and demonstrated to have nephrotoxic, immunotoxic, genotoxic, neurotoxic, and teratog... | Aspergillus carbonarius (strain ITEM 5010) |
A0A1S3PBB7 | KNG_SALSA | MKLGVRLCVLVVFSLQLWGPGQGQELEPEQVLAFCDDKDVEAAVDLALVKYNQKLPYGNQLALYQILESSKAQNDSCTQYFVEFNSRVTDCPAGGDKVWRDCDYLPTGNKVPRPCKATVHMSETDKKVLAVFCDPVEAPVVAERTTCLGCPREIDVESEDLKDPLTYSITRFNADSDSSHHFILNSVGFATRQVVAGFRYRLMFDMRKSNCSKADHKELNDECHPDPDVELAHCNSTVDVAPWRHETAEANVECAPGPLDNFDVFRRRPPGWSPLRNFNNFAEVKTTQASTASAKEESSEESQERSPSAVTMANPEPALP... | null | null | negative regulation of blood coagulation [GO:0030195]; positive regulation of cytosolic calcium ion concentration [GO:0007204] | blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; vacuole [GO:0005773] | cysteine-type endopeptidase inhibitor activity [GO:0004869] | PF00031; | 3.10.450.10; | null | PTM: N-glycosylated, with sialylated biantennary complex-type glycans. {ECO:0000269|PubMed:11447131}.; PTM: O-glycosylated, sialylated oligosaccharides. {ECO:0000269|PubMed:11447131}.; PTM: Bradykinin is released from kininogen by kallikrein. {ECO:0000250|UniProtKB:P01042}.; PTM: The N-terminus is blocked. {ECO:0000269... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12397376}. Vacuole {ECO:0000269|PubMed:12397376}. | null | null | null | null | null | FUNCTION: Inhibits papain and ficin (cysteine proteinases) but not trypsin (a serine proteinase). {ECO:0000269|PubMed:10583403}. | Salmo salar (Atlantic salmon) |
A0A1S3X835 | MBP2C_TOBAC | MYKPQQQQQLFDLQDNNGAAFDNGGTDPSCWLSHENEISRTDSSLSSSNVDPLLFNDLVQIVPLVQSLIDRKEKSSFTRRGSMTYTKMPSRESLYKKTSEVKGRNAGQSTATKKHRDQNKNVSSSQDGYAENFSTPSSTSSLTEKDREELMTLREKVEDLQKKLLEKDELLKEAEILKNEITATNAELDEMKKDISEKDFLVKTTQVQLSDALVKLADKKAAVEKLEWEAMTSSKKVERLQEDLDLLQGEISSFIQFVHALTGNDSRDSAEECNVIPYPWDQNVEIDKLNERDLQKMEAAREAYIAAVAAAKENPDEASL... | null | null | defense response [GO:0006952]; negative regulation of protein transport [GO:0051224]; plasmodesmata-mediated intercellular transport [GO:0010497]; positive regulation of defense response to virus by host [GO:0002230]; regulation of cytoskeleton organization [GO:0051493]; transport of virus in host, cell to cell [GO:004... | cytoplasm [GO:0005737]; microtubule cytoskeleton [GO:0015630] | microtubule binding [GO:0008017]; RNA binding [GO:0003723] | null | null | Microtubule binding protein 2C family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12913144}. Note=Microtubule-associated (PubMed:12913144). Localized in cytosolic punctae when associated with KN-1 (PubMed:17965274). {ECO:0000269|PubMed:12913144, ECO:0000269|PubMed:17965274}. | null | null | null | null | null | FUNCTION: Prevents homeodomain proteins (e.g. STM) association to plasmodesmata and, consequently, cell-to-cell transport. Binds to RNA. Alters KN1 RNA-binding capacity (PubMed:17965274). Regulates cytoskeleton (e.g. actin) organization that determinates cell shape (By similarity). Interferes with cell-to-cell transpor... | Nicotiana tabacum (Common tobacco) |
A0A1S3XSG2 | DAO1_TOBAC | MATTKQKVTAPSSSTAPCCPSTSILRREATAAVAGVGDGLQNWNNVPSVDDKQKKTASSALASLASTEPLSSNTSTKGIQIMTRAQTCHPLDPLSAAEISVAVATVRAAGETPEVRDGMRFIEVVLLEPDKSVVALADAYFFPPFQSSLMPRTKGGSLIPTKLPPRRARLIVYNKKTNETSIWIVELNEVHAAARGGHHRGKVISSNVVPDVQPPIDAQEYAECEAVVKSYPPFRDAMRRRGIDDLDLVMVDPWCVGYHSEADAPSRRLAKPLVFCRTESDCPMENGYARPVEGIYVLVDVQNMQIIEFEDRKLVPLPPA... | 1.4.3.-; 1.4.3.21 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P46883}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12807}; Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807, ECO:0000250|UniP... | alkaloid metabolic process [GO:0009820]; amine metabolic process [GO:0009308]; nicotine biosynthetic process [GO:0042179]; putrescine catabolic process [GO:0009447] | peroxisome [GO:0005777] | aliphatic amine oxidase activity [GO:0052595]; copper ion binding [GO:0005507]; primary amine oxidase activity [GO:0008131]; putrescine oxidase activity [GO:0050232]; quinone binding [GO:0048038] | PF01179;PF02727;PF02728; | 3.10.450.40;2.70.98.20; | Copper/topaquinone oxidase family | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}. | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24287136}. | CATALYTIC ACTIVITY: Reaction=a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938, ChEBI:CHEBI:228804; EC=1.4.3.21; Evidence={ECO:0000269|PubMed:24287136}; PhysiologicalDirection=left-to-right... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=163 uM for putrescine {ECO:0000269|PubMed:24287136}; KM=478 uM for N-methylputrescine {ECO:0000269|PubMed:24287136}; KM=492 uM for cadaverine {ECO:0000269|PubMed:24287136}; Vmax=561 pmol/sec/mg enzyme with putrescine as substrate {ECO:0000269|PubMed:24287136}; Vmax... | PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:16656744}.; PATHWAY: Amine and polyamine degradation; putrescine degradation. {ECO:0000269|PubMed:24287136}. | null | null | FUNCTION: Involved in putrescine catabolism in peroxisomes (PubMed:24287136). May also be involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide prope... | Nicotiana tabacum (Common tobacco) |
A0A1S3YCW2 | ADC1A_TOBAC | MPALGCCVDAAVSPPPGYSFLWDSSLPAPEIFPSGVPPSTNTAVATTTTTHWSPAHSSALYSIDGWGAPYFTVNSSGDISVKPHGTDTLPHQEIDLLKVVKKASDPKNLGGLGLQFPLVVRFPDILKNRLESLQSVFDYAVQSQGYEAHYQGVYPVKCNQDRFVVEDIVKFGSGFRFGLEAGSKPELLLAMSCLCKGSHEGLLVCNGFKDAEYISLALVARKLMLNTVIVLEQEEELDLVIDISKKMAVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQIVRVVKKLEESGMLDCLQLLHFHIGSQIPSTALLADG... | 4.1.1.19 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P21170}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P11926}; | alkaloid metabolic process [GO:0009820]; arginine catabolic process [GO:0006527]; nicotine biosynthetic process [GO:0042179]; spermidine biosynthetic process [GO:0008295] | chloroplast [GO:0009507] | arginine decarboxylase activity [GO:0008792] | PF02784; | 1.20.58.930;3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family, SpeA subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682, ChEBI:CHEBI:58145; EC=4.1.1.19; Evidence={ECO:0000250|UniProtKB:Q9SI64}; | null | PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:32242247}.; PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. {ECO:0000250|UniProtKB:Q9SI64}. | null | null | FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the... | Nicotiana tabacum (Common tobacco) |
A0A1S3Z5Y0 | SIPK_TOBAC | MDGSGQQTDTMMSDAGAEQPPPAPQPVAGMDNIPATLSYGGRFIQYNIFGNIFEVTAKYKPPILPIGKGAYGIVCSALNSETIENVAIKKIANAFDNKIDAKRTLREIKLLRHMDHENIVAIRDIIPPPQREAFNDVYIAYELMDTDLHQIIRSNQGLSEEHCQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARVTSETDFMTEYVVTRWYRPPELLLNSSDYTAAIDIWSVGCIFTELMDRKPLFPGRDHVHQLRLIMELIGTPSEAEMEFLNENAKRYIRQLPLYRRQSFTEKFPHVHPAAID... | 2.7.12.2 | null | defense response [GO:0006952]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2; Evidence={ECO:0000305|PubMed:9618567}; Physi... | null | null | null | null | FUNCTION: Phosphorylates myelin basic protein (MBP) in vitro (PubMed:9618567). May be involved in disease resistance (Probable). {ECO:0000269|PubMed:9618567, ECO:0000305|PubMed:9618567}. | Nicotiana tabacum (Common tobacco) |
A0A1S4AUX8 | ODC1A_TOBAC | MAGQTIIVSGLNPAAILQSTIGGGASPTAAAAENGTRKVIPLSRDALQDFMLSIITQKLQDEKQPFYVLDLGEVVSLIDQWKSALPNIRPFYAVKCNPEPSFLSILSAMGSNFDCASRAEIEYVLSLGISPDRIVFANPCKPESDIIFAAKVGVNLTTYDSEDEVYKIRKHHPKSELLLRIKPMFDGNARCPMGPKYGALPEEVEPLLRAAQAARLTVSGVSFHIGSGDADSNAYLGAIAAAKEVFETAAKLGMSKMTVLDVGGGFTSGHQFTTAAVAVRSALKQHFDDQPELTIIAEPGRFFAETAFTLATTIIGKRVR... | 4.1.1.17 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P11926}; | alkaloid metabolic process [GO:0009820]; nicotine biosynthetic process [GO:0042179]; polyamine biosynthetic process [GO:0006596]; putrescine biosynthetic process from ornithine [GO:0033387]; response to wounding [GO:0009611]; tyramine biosynthetic process [GO:1901695] | chloroplast [GO:0009507]; cytoplasm [GO:0005737] | ornithine decarboxylase activity [GO:0004586] | PF02784;PF00278; | 3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, ChEBI:CHEBI:326268; EC=4.1.1.17; Evidence={ECO:0000250|UniProtKB:P11926}; | null | PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:32242247}.; PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1. {ECO:0000250|UniProtKB:O22616}. | null | null | FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the... | Nicotiana tabacum (Common tobacco) |
A0A1S4BDC4 | MPO1_TOBAC | MATTKQKVTAPSPSPSSSTASCCPSTSILRREATAAIAVVGDGLQNWTNIPSVDEKQKKTASSALASLPTTEPLSTNTSTKGIQIMTRAQTCHPLDPLSAAEISVAVATVRAAGETPEVRDGMRFIEVVLVEPDKSVVALADAYFFPPFQSSLMPRTKGGSQIPTKLPPRRARLIVYNKKTNETSIWIVELNEVHAAARGGHHRGKVIASNVVPDVQPPIDAQEYAECEAVVKSYPPFRDAMRRRGIDDLDLVMVDPWCVGYHSEADAPSRRLAKPLVFCRTESDCPMENGYARPVEGIYVLVDVQNMQIIEFEDRKLVP... | 1.4.3.-; 1.4.3.21 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P46883}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12807}; Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807, ECO:0000250|UniP... | alkaloid metabolic process [GO:0009820]; amine metabolic process [GO:0009308]; nicotine biosynthetic process [GO:0042179]; response to auxin [GO:0009733]; response to jasmonic acid [GO:0009753] | peroxisome [GO:0005777] | aliphatic amine oxidase activity [GO:0052595]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; methylputrescine oxidase activity [GO:0052599]; primary amine oxidase activity [GO:0008131]; protein homodimerization activity [GO:0042803]; quinone binding [GO:0048038] | PF01179;PF02727;PF02728; | 3.10.450.40;2.70.98.20; | Copper/topaquinone oxidase family | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}. | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24287136}. | CATALYTIC ACTIVITY: Reaction=a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938, ChEBI:CHEBI:228804; EC=1.4.3.21; Evidence={ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012, ECO:0000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=309 uM for putrescine {ECO:0000269|PubMed:24287136}; KM=57 uM for N-methylputrescine {ECO:0000269|PubMed:24287136}; KM=215 uM for cadaverine {ECO:0000269|PubMed:24287136}; KM=0.19 mM for N-methylputrescine {ECO:0000269|PubMed:17174363}; KM=0.76 mM for putrescine {E... | PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:16656744, ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012}. | null | null | FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the... | Nicotiana tabacum (Common tobacco) |
A0A1S4EWW7 | VA1_AEDAE | MASHVIVKFITAAILIGSCYANYCDQSLCRRGPHVACNAPTQFGSACGQEPKFVKMDARMKNLLLKKHNELRAEIACGKHGFPQAARMPTLVWDDELAHIASFNARKCIFAHDKCRNTREFKFAGQNLAITAFAGYNFQAADRAENFTQEWFNEHKDCPKSYVDSYPMSHSGPQIGHFTQMVNDRAWKMGCSMVHYKNGRVIKYYLVCNYSMTNMIEEPIYTRGSAGSKCQTGQNPQYRGLCSPREKVRSESYRG | null | null | multicellular organism reproduction [GO:0032504] | extracellular space [GO:0005615] | null | PF00188; | 3.40.33.10; | CRISP family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31937766}. Host endosome {ECO:0000269|PubMed:31937766}. Host mitochondrion {ECO:0000269|PubMed:31937766}. Note=Delivered into the human immune cells by endocytosis in a RhoA-dependent manner; escapes from host endosomes to mitochondria. {ECO:0000269|PubMed:31937766}. | null | null | null | null | null | FUNCTION: Activates autophagy in human monocytic cells, dendritic cells and macrophages (PubMed:31937766). Does not affect cytokine expression in human monocytic cells (PubMed:31937766). {ECO:0000269|PubMed:31937766}.; FUNCTION: (Microbial infection) Promotes dengue virus type 2 replication in human monocytic cells, de... | Aedes aegypti (Yellowfever mosquito) (Culex aegypti) |
A0A1S4F020 | CBPB1_AEDAE | MIPRIVVVLLSVLAVVTARRSYEGYKVYGIVPESPDEAEILYQIRQSNPDLDFWHLTKQPGDEARVLVAPKDQRSFLIKLIRHGLHYQEVISDVEGTLAPYNEPRTRGMSLDRDVSTSYLRHNEINEYLQTLSQKYPSLVSVEEAGTSYEGRSIKTITINKKPGNAVVFLDAGIHAREWIAPATALYAIEQLVEHSSENQEVLSNLTWVIMPVVNPDGYEFSHETDRFWRKTRKPTGKTCKGTDGNRNFDYHWGEVGASTQACADTFRGETAFSEPETRAVRDAVMKLKGSCKFYLSLHSYGNYILYPWGWTSKLPETWE... | 3.4.17.2 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P15086}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:34658092, ECO:0000269|PubMed:34750241}; | proteolysis [GO:0006508] | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615] | metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270] | PF00246;PF02244; | 3.30.70.340;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:25521592}. | CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal lysine or arginine amino acid.; EC=3.4.17.2; Evidence={ECO:0000269|PubMed:34658092, ECO:0000269|PubMed:34750241}; | null | null | null | null | FUNCTION: Carboxypeptidase that preferentially hydrolyzes arginine and lysine residues at the C-terminus (PubMed:34750241). During infection by dengue virus, may play a role in preventing viral packaging, maturation, and release from the midgut (PubMed:25521592). {ECO:0000269|PubMed:25521592, ECO:0000269|PubMed:3475024... | Aedes aegypti (Yellowfever mosquito) (Culex aegypti) |
A0A1S4GMJ4 | CLC9_ANOGA | MCILTLVERKHLKNMVHVRLLVMMHILIIYSTFGAVRRPINIRVLEGNSCDTPQVIGGKCMNISLCDPAFVHSIAYQEHTPVCQQNAFYRVICCQPFLDFCENSKQFQIMHGIEAEPGMFPHLARLGLKSEEDGIAWTCSANIISERFLLTAAHCNPVNIAGLGCAESMQCDQQNTVKSFISNPKYKTSFKYHDIALVELEQNIRFNKRVLPICPYISKTDLHESEDLVIAGWGATESHFQSPRLMFATVRTVLQNDCKDHYASLLKASPNKKLHQGITDEMYCAQGALVDNVTEYIDACSGDSGGPLQTKQNNNLYLIG... | 3.4.21.- | null | defense response to bacterium [GO:0042742]; defense response to symbiont [GO:0140546]; innate immune response [GO:0045087]; positive regulation of melanization defense response [GO:0035008]; proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, CLIP subfamily | PTM: Secreted as a full-length protein (PubMed:12364791). Following bacterium E.coli infection, proteolytically cleaved into two chains, p12 and p30, which remain covalently linked (PubMed:12364791). {ECO:0000269|PubMed:12364791}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph (PubMed:33045027). Recruited by CLIPA8 to microbial surfaces where it is cleaved into the two chain active form (PubMed:33045027). {ECO:0000269|PubMed:33045027}. | null | null | null | null | null | FUNCTION: Probable serine protease which plays an essential role in the innate immune response against bacteria and protozoa infection by activating the melanization cascade (PubMed:33045027). In the susceptible strain G3, appears to be dispensable for ookinete elimination which occurs by lysis (PubMed:33045027). {ECO:... | Anopheles gambiae (African malaria mosquito) |
A0A1S4H5M5 | CLA28_ANOGA | MKVLLFCIVISLTTLIASGQDIEEELRCPGGYCVSKYLCPNGTFIDDIKHAQTTQLIGLRAGLDIDDFDDCNDYLLVCCQSAPAPTATSTEKPATSDELIEPPPSTNLACGQANEGGLIYDLRNNETLSQYAEYPWVVYILALKKQEANSGDFVCGGTLIHSRLVVTTAHNTDGKTDLVARFGEWDISTTKEPFPQQDIDVAEVIKHPQYVFNPIQNDIALLVLAENVQYAAHIRPICLPQPTDEFVGQRCVSNGWGKERGVYANVMKKLTLPVIGRANCTRMLRYAGLGPFYTLREGFLCAGGEVAVDMCKGDGGSPLA... | null | null | defense response to bacterium [GO:0042742]; innate immune response [GO:0045087]; positive regulation of melanization defense response [GO:0035008]; positive regulation of protein processing [GO:0010954]; proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, CLIP subfamily | PTM: Secreted as a full-length protein (PubMed:31765430, PubMed:33045027). Proteolytically cleaved into two chains which probably remain covalently linked (PubMed:31765430). Cleavage is induced by fungus B.bassiana and Gram-positive or Gram-negative bacteria infection (PubMed:31765430, PubMed:33045027). {ECO:0000269|Pu... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31765430, ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph. {ECO:0000269|PubMed:31765430, ECO:0000269|PubMed:33045027}. | null | null | null | null | null | FUNCTION: Inactive serine protease which plays an essential role in the innate immune response against bacteria, fungi and protozoa infection by activating the melanization cascade (PubMed:31765430, PubMed:33045027). In the melanization cascade, acts downstream of TEP1, SPCLIP1 and CLIPA8 to promote CLIPC9 proteolytic ... | Anopheles gambiae (African malaria mosquito) |
A0A1S4H5S2 | CLA8_ANOGA | MPSWWCCCCLVVLLYAQRMIVPSSAQNDGSDELQECPGGFCSPKYLCPNGTYNEANAQNQEIIMLRFGEEDVCQDYMQVCCSNATSMRYELVTNNEPVEYGCGISNPGGLIYQVEGNRTYAQYGEFPWVVAILEAFYSSNEQQFTYVGGGTLIHPRFVVTAAHIFNKTENLVASFGEWDMNRDENVYPKQNIDIDRTIIVHPEYNSVGLLNDIALAQLKQNVVYDKHIRPICLPNPTDRFDDQLCISTGWGIEALTSAYANVLKRVDLPVIARASCKKLFAETRLGPFFRLHKSVLCAGGEEGADMCDGDGGSGLACPNE... | null | null | defense response to bacterium [GO:0042742]; defense response to symbiont [GO:0140546]; innate immune response [GO:0045087]; positive regulation of melanization defense response [GO:0035008]; positive regulation of protein processing [GO:0010954]; proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252] | PF18322;PF00089; | 2.40.10.10; | Peptidase S1 family, CLIP subfamily | PTM: Secreted as a full-length protein (PubMed:17537726). Proteolytically cleaved into two chains which remain covalently linked (PubMed:17537726). Cleavage is induced by Gram-positive or Gram-negative bacteria infection (PubMed:17537726). {ECO:0000269|PubMed:17537726}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17537726, ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph. {ECO:0000269|PubMed:17537726, ECO:0000269|PubMed:33045027}. | null | null | null | null | null | FUNCTION: Inactive serine protease which plays an essential role in the innate immune response against bacteria, fungi and protozoa infection by activating the melanization cascade (PubMed:16922859, PubMed:17537726, PubMed:23166497, PubMed:33045027). In the melanization cascade, acts downstream of TEP1 and SPCLIP1 to p... | Anopheles gambiae (African malaria mosquito) |
A0A1S4HE51 | CLA30_ANOGA | MAFSLRIGIRTTDSKRCLVLLVLVVLLTVLACLPPSVEGNFPVGKFRRCNNNKGICVSREQCLNGQINTVGHTQIEPRLLNDDDIDECDVYGMQCCNLPSTNVPADSDEEEQEEEEKEKKGGTVTTTTTEEPDDPDWSRQCGQRTDVTERADQDGETNRFEFPWSVALFSKAQFFGKVRKEFLCGGTLIDDYLVLTAARCVNQKDRNTLVVQLGRWNLDAGKESRMQEIAVEELIIHRGYVLSSHLHNVALLVLANGAQLGRAANRVCLPDHSVQFGPDTLCYVVGWSNSPSPNTSNRQLKLRSMVAPVQECTATIRRST... | null | null | antibacterial innate immune response [GO:0140367]; defense response to bacterium [GO:0042742]; defense response to symbiont [GO:0140546]; positive regulation of melanin biosynthetic process [GO:0048023]; positive regulation of melanization defense response [GO:0035008]; positive regulation of protein processing [GO:001... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252] | PF18322;PF00089; | 2.40.10.10; | Peptidase S1 family, CLIP subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph. {ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:33045027}. | null | null | null | null | null | FUNCTION: Probable inactive serine protease which plays an essential role in the innate immune response against bacteria and protozoa infection by activating the melanization cascade (PubMed:24039584, PubMed:33045027). Binds to the surface of parasite P.berghei ookinetes and bacterium E.coli where it promotes the accum... | Anopheles gambiae (African malaria mosquito) |
A0A1S4NYE3 | CDIA_ECOST | MHQPPVRFPYRLLSYLISTIIAGQPLLPAVGAVITPQNGAGMDKAANGVPVVNIATPNGAGISHNRFTDYNVGKEGLILNNATGKLNPTQLGGLIQNNPNLKAGGEAKGIINEVTGGNRSLLQGYTEVAGKAANVMVANPYGITCDGCGFINTPRATLTTGRPVMNADGSLQALEVTEGSITINGAGLDGTRSDAVSIIARATEVNAALHAKDLTVTAGANRVTADGRVSALKGEGDVPKVAVDTGALGGMYARRIHLTSTESGVGVNLGNLYAREGDIILSSSGKLVLKNSLAGGNTTVTGTDVSLSGDNKAGGNLSVT... | 3.1.-.- | COFACTOR: Note=tRNase activity is metal-independent. {ECO:0000269|PubMed:29923643}; | null | extracellular region [GO:0005576] | endonuclease activity [GO:0004519]; toxin activity [GO:0090729] | PF21726;PF13332;PF04829;PF05860; | 2.160.20.10; | CdiA toxin family; Bacterial EndoU family | PTM: The CT domain is cleaved upon binding to receptor Tsx on target cells. {ECO:0000269|PubMed:30388452}. | SUBCELLULAR LOCATION: Secreted {ECO:0000255}. Target cell, target cell cytoplasm {ECO:0000305|PubMed:30388452}. Note=Secreted to the cell surface by CdiB, its two partner secretion pathway (TPS) partner (Probable). Toxin translocation into the target cell depends on the proton motive force of the target cell, but not o... | null | null | null | null | null | FUNCTION: Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring target bacteria in a contact-dependent fashion (target cell counts decrease 1... | Escherichia coli (strain STEC_O31) |
A0A1S5RW73 | KPS_SALDI | MSFATSLPRPTTTGAAGFGLPLATCISLSVSHSFSPKFGICNNTSLRLKSKAGSGCYEGIHRSQLAASTILEGHTPINPEVESEKIRLIERIRLMFRSMDDGEISVSPYDTAWVALVEDIGGSGGPQFPTSLEWISNNQLDDGSWGDRKFVLYDRILNTLACVVALTTWKMHPNKCEKGLRFISDNIEKLADEDEELMPVGFEIALPSLIDLAKRLCIEIPDNSASIKNIYAKRDSKLKRIPMDLMHKKPTSLLFSLEGMEGLNWDKLLDFQSEGSFLSSPSSTAYALHHTKDELCLEYLLKAVKKFNGGVPNAYPVDMF... | 5.5.1.28 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:28204567}; | diterpenoid biosynthetic process [GO:0016102]; gibberellin biosynthetic process [GO:0009686] | chloroplast [GO:0009507] | isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397; | 1.50.10.160;1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsc subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (-)-kolavenyl diphosphate; Xref=Rhea:RHEA:54684, ChEBI:CHEBI:58756, ChEBI:CHEBI:138310; EC=5.5.1.28; Evidence={ECO:0000269|PubMed:27865008, ECO:0000269|PubMed:28204567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54685; Evidence={ECO:000026... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 uM for geranylgeranyl diphosphate {ECO:0000269|PubMed:28204567}; Note=kcat is 0.88 sec(-1) with geranylgeranyl diphosphate as substrate. {ECO:0000269|PubMed:28204567}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:28204567}; | null | FUNCTION: Involved in the biosynthesis of clerodane diterpenoids natural products, including salvinorin A with potent agonistic activity on brain kappa-opioid receptors, thus conferring hallucinogenic properties (PubMed:30468448). Diterpene synthase that catalyzes the formation of (-)-kolavenyl diphosphate from geranyl... | Salvia divinorum (Maria pastora) (Diviner's sage) |
A0A1S6M251 | B4GT5_PIG | MRVRRGLLRLPRRSLLAALFFFSLSSSLLYFVYVAPGIVNTYLFMMQAQGILIRDNMRTIGAQVYEQVVRSAYAKRNSSVNDSDYPLDLNHSETFLQTTTFLPEDFTYFANHTCPERLPSMKGPIDINMSEIGMDTIHELFSKDPAIKLGGHWKPSDCVPRWKVAILIPFRNRHEHLPVLLRHLIPMLQRQRLQFAFYVVEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLVFHDVDHIPENDRNYYGCGQMPRHFATKLDKYMYLLPYNEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGD... | 2.4.1.-; 2.4.1.274 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UBX8}; | carbohydrate metabolic process [GO:0005975]; central nervous system myelination [GO:0022010]; central nervous system neuron axonogenesis [GO:0021955]; ganglioside biosynthetic process via lactosylceramide [GO:0010706]; glycoprotein biosynthetic process [GO:0009101]; glycosylation [GO:0070085]; neuron maturation [GO:004... | Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580] | metal ion binding [GO:0046872]; UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity [GO:0008489] | PF02709;PF13733; | null | Glycosyltransferase 7 family | null | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Golgi apparatus {ECO:0000269|PubMed:29546034}. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}. | CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + UDP-alpha-D-galactose = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31495, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950, ChEBI:CHEBI:22801, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.274; Evidence={ECO:0000... | null | PATHWAY: Protein modification; protein glycosylation.; PATHWAY: Sphingolipid metabolism. | null | null | FUNCTION: Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer) (By similarity). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal ma... | Sus scrofa (Pig) |
A0A1S7LCW6 | MAMP_MAGMO | MKLKGTTIVALGMLVVAIMVLASMIDLPGSDMSATPAPPDTPRGAPIVGGQGQAMGLPVAMQRRRGEQRAPVPALSDANGGFVAPNVQFSEAHWQGMEALPLSIELKRKLKLPLDLEGLLIDETSLNAAVSGLLAGDVLVAINGRKVKTLKKMQKETRRVQMDRRASLTVYRKGRLLTLTLSEEKNLGLAQVETAPMILPGDIMPHPYRGPCTQCHAIGTTGHITPDPDGIVLPPGPIRAGAKMPHRDRGPCAACHAIIQ | 1.-.-.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:24097349}; Note=Binds 2 heme groups via the magnetochrome (MCR) motifs. {ECO:0000269|PubMed:24097349}; | null | plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF18509;PF13180; | 2.30.42.60; | Magnetosome MamP family | PTM: Subject to proteolytic cleavage which requires both MamE and MamO. {ECO:0000250|UniProtKB:Q2W8Q1}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:Q2W8Q1}; Single-pass membrane protein {ECO:0000305|PubMed:24097349}. Note=Not seen in magnetosome membranes. {ECO:0000250|UniProtKB:Q2W8Q1}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 for oxidation of Fe(2+). {ECO:0000269|PubMed:24097349}; | null | FUNCTION: Oxidizes Fe(2+) at alkaline pH; successively forms ferrihydrite (Fe(3+)(2)O(3) 0.5 H(2)O) then magnetite (Fe(3)O(4)) from an Fe(2+) solution. {ECO:0000269|PubMed:24097349}. | Magnetococcus massalia (strain MO-1) |
A0A1U8F5V2 | IFI4E_CAPAN | MATEAPPPVDTTEVPPFTAAETAVKQPHKLERKWTFWFDNQSKPKQGAAWGSSLKKAYTFDTVEEFWSLYDQIFKPSKLTVNADFHLFKAGIEPKWEDPECANGGKWTVTSSRKANLETMWLETLMALVGEQFDDSEDICGVVASVRRSQDKLSLWTKTATNEAAQMGIGRKWKEIIDTEKISYSFHDDSKRERSAKSRYTV | null | null | negative regulation of defense response to virus [GO:0050687]; response to virus [GO:0009615] | eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634] | RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-101-Cys-140 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A445AGS0}. Nucleus {ECO:0000250|UniProtKB:A0A445AGS0}. | null | null | null | null | null | FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiatio... | Capsicum annuum (Capsicum pepper) |
A0A1U8GR65 | IF4E1_CAPAN | MATAEMEKTTTFDEAEKVKLNANEADDEVEEGEIVEETDDTTSYLSKEIATKHPLEHSWTFWFDNPVAKSKQAAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLVVGADLHCFKHKIEPKWEDPVCANGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHEDEICGAVVSVRGKGEKISLWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRNAKNRYTV | null | null | defense response to virus [GO:0051607]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634] | RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-126-Cys-164 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}. | null | null | null | null | null | FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:18182024). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiat... | Capsicum annuum (Capsicum pepper) |
A0A1U8QK63 | PKIC_EMENI | MALEEVPSVSRDLDHSALRALSSASPSSLPSSCSRSTTSLLFQSKGIEFRLSIPDTFLSLVEPHRNAFLASYSTQGNTQSPLELALSFLYFLLDQKVSPLVLSSVLRAFNLEFLGNRSEIHSLIADLTPIPKQRQRWLGIYYRFLEASDDKRAEIPLSSIFQHARTNEFQLMAVFGGQGECSRTCLNEFAELYSSYEPMLRRLVGVIGPCLYNLSTSDEYSSYYRNQPLDLKAWITDENHVPDLGFVASAPVSVPVIGALSLARYCVTCHITGCNPGLMRSMLRTATGHSQGLLAAIVVAVSHSWDSFYQATEEVIELLF... | 1.3.1.9; 2.3.1.38; 2.3.1.39; 2.3.1.86; 3.1.2.14; 4.2.1.59 | null | long-chain fatty acid biosynthetic process [GO:0042759] | fatty acid synthase complex [GO:0005835] | (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity [GO:0004317]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; [acyl-carrier-protein] S-malonyltransferase activity [GO:0004314]; enoyl-[acyl-carrier-protein] reductase (NADH) activity [GO:0004318]; fatty acid synthase activity [GO:000... | PF00698;PF08354;PF13452;PF01575;PF16073; | 1.20.1050.120;1.20.930.70;3.30.1120.100;3.30.70.3320;6.10.60.10;3.20.20.70;3.10.129.10;3.40.366.10; | Fungal fatty acid synthetase subunit beta family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChE... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:22510154}. | null | null | FUNCTION: Fatty acid synthase beta subunit; part of the pki gene cluster that mediates the biosynthesis of 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde (PubMed:22510154). The first step in the pathway is the generation of the decanoyl starter unit by the FAS composed of subunits pkiB and pkiC, which is then tran... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
A0A1U8QLG8 | PBCB_EMENI | MSPPLDSALEPLSEYKETAFPRTEKDPSQYKEHDLVTPEKEIQTGYFSPRGSHSSHGSHDSSASSNISLDDARMSDVNNSPNVFHDDPDTIDEKLSMYWKAANETVIREPYDYIAGIPGKEIRRKLLEAFNHWYKVDEQSCQAIATTVGMAHNASLLIDDIQDSSKLRRGVPCAHEVFGIAQTINSANYVYFLAQNQLFRLRSWPQAISVFNEEMVNLHRGQGMELFWRDNLLPPSMDDYLQMIANKTGGLFRMIVRLLQTSSRQVIDVEQLVDVLGLYFQILDDYKNIREEKMAAQKGFFEDLTEGKFSFPICHAIGEG... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; terpenoid biosynthetic process [GO:0016114]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:22506079}. | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
A0A1U8QNG8 | HXNS_EMENI | MDALLPRSSPQLKFYLNGTPISLTSPHPRWTLLDFIRSQDGLKGTKLGCGEGGCGALSGKHVITIEGLGTVDHPHPLQERIAQLHGSQCGFCTPGIVMSLYAMIRNAYDPVTGKFQLSADDIESKGHLDGNLCRCTGYKPILNAARTFIEDDLGSVPSIVESELVGTEEETESDMGAHSGSGDTGSRSSGSCGRPGGCCKDSPGISSCSSRETDMTTPSLPDSPVLKQYDFIPYTPTTELIYPPGLAKFVPELLCYGDAEQAWVKPRSVQEALEILSQCPSATLVTGASEVQVDVRFKDFRPSVSVFVGDITEMTGISWS... | 1.-.-.- | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:P80457}; Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250|UniProtKB:P80457}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P80457}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0... | null | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; FAD binding [GO:0071949]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; xanthine dehydrogenase activity [GO:0004854] | PF01315;PF03450;PF00941;PF01799;PF02738;PF20256; | 3.10.20.30;3.30.465.10;1.10.150.120;3.90.1170.50;3.30.365.10;3.30.390.50;3.30.43.10; | Xanthine dehydrogenase family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=90.4 uM for hypoxanthine {ECO:0000269|PubMed:363427}; KM=36.15 uM for 2-hydroxypurine {ECO:0000269|PubMed:363427}; KM=524.5 uM for 6,8-dihydroxypurine {ECO:0000269|PubMed:363427}; KM=188.6 uM for nicotinate {ECO:0000269|PubMed:363427}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.4. {ECO:0000269|PubMed:363427}; | null | FUNCTION: Nicotinate hydroxylase, part of the hnx cluster involved in the purine degradation (PubMed:4581274). The nicotinate hydroxylase hnxS accepts nicotinate as a substrate and catalyzes the first step of nicotinate catabolism (PubMed:4581274). HnxS accepts also hypoxanthine, but not xanthine, as a substrate (PubMe... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
A0A1U8QWA2 | ATR12_EMENI | MAIIDTTKDLSALFTQQVRASPNALALEDDKTSYTYAELDKEVEELSRRLRSYGVSRDSLVGVLLPRSAHFVIACLAALRAGGAFLVLELAYPPDLLADVLEDATPAVVVTHRSETGKIKGSVPVISLDEPPVDANGHTVEPGPLPVDDDLDRLAFVSYSSGTTGKPKGIANPHRAPVLSYNLRFGVQDLQPGDRVACNVFFIWEILRPLIRGATVVAVPDDHSYDPAALVDLLASRHITETLMTPTLLATILSRHSDIGARLPELRTLWLNGEVVTTDLARRAIRALPNTRLLNCYSACETHEIACGDIKEIVSDESQY... | 1.1.1.-; 1.2.1.- | null | organonitrogen compound biosynthetic process [GO:1901566]; secondary metabolite biosynthetic process [GO:0044550] | null | oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00106;PF00501;PF07993;PF00550; | 3.30.300.30;1.10.1200.10;3.40.50.12780;3.40.50.720; | NRP synthetase family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.1 mM for glycine betaine {ECO:0000269|PubMed:31061132}; KM=0.24 mM for glycine betaine aldehyde {ECO:0000269|PubMed:31061132}; KM=5.8 mM for N,N-dimethylglycine {ECO:0000269|PubMed:31061132}; KM=90 mM for 3,3,-dimethylbutyraldehyde (for the aldehyde reductase R2 ... | null | null | null | FUNCTION: NRPS-like enzyme with an unusual domain architecture that converts back glycine betaine to choline via a 2-step reduction mechanism, and thereby can be an alternative source of choline (PubMed:31061132). Permits direct reutilization of endogenously stored glycine betaine for on-demand biosynthesis of choline ... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
A0A1V0E492 | TPS1_PIPNI | MACVSDLVAFTQPLIIGAKPLEIVRRSAAFHPNVWGDYFLKLSQDEKKLESMRERAKVLKEKVLKKLSTIEGGERLELIDTLYHLGVAYNFEKEIEEALEKIYKAYDEDATQDNLCTLALRFRLLRQHGWNASSDVFNKFKETKNGNFKESVASDVLGMLSLYEASYVGTKEDKILEEAISFTTRNLSAALPNMEPLLAERVAHSLELPLHKRLQRLEARYFITMYEKNNAHDEMLLEYAKLDYNLLQALHQNEMKELTKWWTKIDLVGKMKFPRDRVTECYFWPLGAFFEPQHSRGRIFATKITQLTSIIDDLYDVYGT... | 4.2.3.104; 4.2.3.57 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | beta-caryophyllene biosynthetic process [GO:1901937]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; sesquiterpene biosynthetic process [GO:0051762] | null | alpha-humulene synthase activity [GO:0080017]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene + diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295; Evidence={ECO:0000269|Pub... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21 uM for (2E,6E)-farnesyl diphosphate {ECO:0000269|PubMed:29248443}; Note=kcat is 0.455 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate. {ECO:0000269|PubMed:29248443}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:29248443}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds that contribute to the characteristic flavors of black pepper (PubMed:29248443). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into beta-caryophyllene and, as a minor compound, into alpha-humulene (PubMed:29248443). {ECO... | Piper nigrum (Black pepper) |
A0A1V0E4A6 | TPS2_PIPNI | MDAVSCAINALSAQAPPKHLGGNNVGRKSVTFPKDIWGDYFLKISPNEEKLDSWRVRAKELKEKVFDILSCAKGAEQVHIIDALYHLGVSYQFEKEIEEALKNMLTTYNDDTSTEDDLYTLALRFRLLRQNGFHASTKALNKFKDAHGSFREDLASDVMGLLSLYEASYAGTVDDLILDEALAFTKIHLKAALPHLDSHLAQRVSHSLELPLHKRIQRLEAREFISLCEKDDSIVIKELLEFAKLDYNILQALHQWELKELTKWWKKLNLVGKMTFARDRMTEIYFYVSGFFFEPQYSRGRIISSKILAICSVVDDEYDV... | 4.2.3.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | cadinene biosynthetic process [GO:1901928]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; sesquiterpene biosynthetic process [GO:0051762] | null | (+)-delta-cadinene synthase activity [GO:0047461]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate; Xref=Rhea:RHEA:56556, ChEBI:CHEBI:33019, ChEBI:CHEBI:140564, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:29248443}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56557; Evidence={ECO:0000269|PubMed:29248443}; CATALYTIC... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18.4 uM for (2E,6E)-farnesyl diphosphate {ECO:0000269|PubMed:29248443}; Note=kcat is 0.694 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate. {ECO:0000269|PubMed:29248443}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:29248443}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds that contribute to the characteristic flavors of black pepper (PubMed:29248443). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into alpha-cadinene, delta-cadinene and delta-cadinol (PubMed:29248443). {ECO:0000269|PubMed:... | Piper nigrum (Black pepper) |
A0A1V0QSA8 | ERIE_HERER | MSAPINGTVEKSYVPGAELWCQEDETAITEPYTYVNSMPGKDVRGRFIEAANHWLHVEPEPLAVICKIVAMLHNASLVIDDIEDNSQLRRGQPVAHKIYGLAQAINSANYVYFLALKEADQLKPYQREGYNSHEIILGALTSVSDFAAQDLLYSVFSDELVNLHRGQGLELVWRDSLRCPTEEQYIDMVNKKTGGLFRLAIKLLTACSSNPSTIDYVPLFNLFGVFFQIRDDLMNLDDNEYEKNKGFAEDLTEGKFSFPVIHGITAQKDNSVLINVLQKRPTTPPLKLHAIHHLRNNTGSFKYTETILNSLETRLRGEID... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | isoprenoid biosynthetic process [GO:0008299]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:31535864}. | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of erinacines, cyathane-xylosides that show unique biological activities, including leishmanicidal activity, stimulating activity for nerve growth-factor synthesis, and agonistic activity toward the kappa opioid rec... | Hericium erinaceus (Lion's mane mushroom) (Hydnum erinaceus) |
A0A1W2P872 | NOVA2_MOUSE | MEPEAPDSRKRPLETPPEVVCTKRSNTGEEGEYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLVQGTAEALNAVHSFIAEKVREIPQAMTKPEVVNILQPQTTMNPDRAKQAKLIVPNSTAGLIIGKGGATVKAVMEQSGAWVQLSQKPEGINLQERVVTVSGEPEQVHKAVSAIVQKVQEDPQSSSCLNISYANVAGPVANSNPTGSPYASPADVLPAAAAASAAAASGLLGPAGLAGVGAFPAALPAFSGTDLLAISTALNTLASYGYNTNSLSLGLNSAAASGVLAAVAAGANPAA... | null | null | central nervous system neuron development [GO:0021954]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of cold-induced thermogenesis [GO:0120163]; neuron differentiation [GO:0030182]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of axon guidance [GO:1902667]; regul... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | mRNA binding [GO:0003729]; RNA binding [GO:0003723]; sequence-specific mRNA binding [GO:1990825] | PF00013; | 3.30.1370.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30638744}. | null | null | null | null | null | FUNCTION: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion. It binds specifically to the sequences 5'-YCAY-3' and regulates splicing in only a subset of regulated exons (PubMed:14615540). Binding to an exonic 5'-YCAY-3' clust... | Mus musculus (Mouse) |
A0A1W5T1U1 | POXE_PENOX | MAPSQAPREPIAIVGSGCRFPGESSSPSKLWELLQAPRDVQTEIPPTRFNPHGFYHPDNLHHGTSNVRHSYLLTEDHRHFDAQFFGIKPAEAHCIDPQQRLLMETVYESLESAGLRLEDLRGSETAVYVGLMCGDYADIVLRDPESFPMYLSTGTARSIMSNRISYFFDWHGPSMTIDTACSSSLVAVHEAVQTLRLGRSRVAVAAGSNLCLSPEPYIAESKLQMLSPTGRSRMWDIQADGYARGDGVAAVVLKTLSAALADGDHIECLIRETSVNQDGRTRGITMPSSEAQTRLIQDTYARAGLDPLKPQERCQYFEAH... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; lactone biosynthetic process [GO:1901336]; methylation [GO:0032259]; organonitrogen compound biosynthetic process [GO:1901566]; polyketide biosynthetic process [GO:0030639]; toxin biosynthetic process [GO:0009403] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:28365998}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety (PubMed:28365998). The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis... | Penicillium oxalicum |
A0A1W6QDI7 | KSL1_ISORU | MSLAFNLRVIPFSGHTIQSRRGLFPVHESPMITTKPFAAVKCSLTTSTDLMGKIKEKFNGKVHTSLPAITTHSADTPSNLCIIDTLQRLGVDRYFQSEIDSILDDTYRLWQLKKEDIFSDITTHAMAFRLLRVKGYQVSSEELAPYADQEHVNLQEIDVPTVIELYRAAQERVTEEDSTLKKLYVWTSTFLKQQLLTDAIPDKKLHEQVDYYLKNYHGILDRMGVRRSLDLYDVGHYKTLKAADGFSNLCNEDFLAFARQDFNISQAQHQKELQQLQRWYSDCRLDTLKFGRDVVRVSNFLTSAMSGDPELSDVRLAFAK... | 4.2.3.131 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q40577}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577}; | gibberellin biosynthetic process [GO:0009686]; miltiradiene biosynthetic process [GO:1901946]; terpenoid biosynthetic process [GO:0016114] | chloroplast [GO:0009507] | magnesium ion binding [GO:0000287]; miltiradiene synthase activity [GO:0062205]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = diphosphate + miltiradiene; Xref=Rhea:RHEA:33983, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635, ChEBI:CHEBI:65037; EC=4.2.3.131; Evidence={ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33984; Evidence={ECO:0... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526}. | null | null | FUNCTION: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities (PubMed:28381502, PubMed:28445526). Catalyzes the conversion of (+)-copalyl diphosphate ((+)-CPP) to m... | Isodon rubescens (Rabdosia rubescens) |
A0A1W7HCY1 | IUTB_VIBVL | MSGHSFFEHLFEHSQHVTPYLHGAIKPRPERCAEHGFIHIEHASSDHIRALYESLKLAHPEAGAAYWLTRTWTLLCWQPLYVAFIAIYSCQGLPKLSSMGQHVQPRFVSGYQFDDDEYRQGSEQELIAHAGKELCALFDYFRQEMSLWTRIRPGFTQHLFADGVFGCLVKLSQFYPTLSGDYFLEQARLWLAACQLPEKLIQSLRYDETSRQLSLVRTSCCLVYKCQGRELCRDCPRHPDNKRE | 1.16.1.10 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:P39405}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P39405}; | cellular response to iron ion starvation [GO:0010106] | cytoplasm [GO:0005737] | 2 iron, 2 sulfur cluster binding [GO:0051537]; ferric-chelate reductase (NADH) activity [GO:0140618]; ferric-chelate reductase (NADPH) activity [GO:0052851]; metal ion binding [GO:0046872] | PF11575; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28150143}. | CATALYTIC ACTIVITY: Reaction=2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH; Xref=Rhea:RHEA:15061, Rhea:RHEA-COMP:11342, Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.16.1.10; Evidence={ECO:0000269|PubMed:32681432}; Phy... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=6.83 nmol/min/mg enzyme with Fe(3+)-aerobactin as substrate and glutathione (GSH) as electron donor (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:32681432}; Vmax=2.32 nmol/min/mg enzyme with Fe(3+)-vulnibactin as substrate and glutathione (GSH) as electr... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 with Fe(3+)-nitrilotriacetic acid (NTA) as electron acceptor. {ECO:0000269|PubMed:32681432}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius with Fe(3+)-nitrilotriacetic acid (NTA) as electron acceptor. {ECO:0000269|PubMed:32681432}; | FUNCTION: Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-aerobactin reductase catalyzing the reduction of Fe(3+)-aerobactin, a citrate-hydroxamate siderophore produced by other bacteria. Catalyzes reduction of Fe(3+)-vul... | Vibrio vulnificus |
A0A1Y2IY60 | LP9_TRAC3 | MFTKLIIAASLAASVAAHATFQELWINGVDQGSSCVRLPQSNSPVTSVSTPDLACNASPHPSDGICQVMPGDEVTVEMHQQPNDRSCATEAIGGDHYGPVLVYMAKVDDATTAVGSSAQWFKVAEIGLPSSNPDYWGTEVLNDNCGHYTFKVPSDIAPGNYLIRAEVIALHVASSIGGAQFYMSCYQVNVGGSGSANPPTVSIPGAYSATDPGILINIYEPLSTYTIPGPTPYATTSPAVANTPYPTTATWNTALQPSTVPTAVPTPGTPGIGKA | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q4WP32}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q4WP32}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497] | PF03443; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:37463979}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:37463979}; | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase (LMPO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 oxidation products (PubMed:37463979). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I)... | Trametes coccinea (strain BRFM310) (Pycnoporus coccineus) |
A0A1Y3DYH2 | ADA_PLAKN | MNILQEPIDFLKKDELKNIDLSQMDKKERYKIWKRIPKCELHCHLDLCFSADFFLSCVRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIRVADIFQDYEMIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKHNLDIELIHQAIVKGIKEVVELLDHKIDVTLLCIGDTGHRAADIKASADFCLKHKADFVGFDHGGHEVDLKPYKEIFDYVKEGGMHLTVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVSESQELIDMVKENNILLEVCPISNVLLKNAKSFDTHPIRKLYDAGVKVSVSSDDPGMFLTNIN... | 3.5.4.31; 3.5.4.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:A5KE01}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:A5KE01}; | adenosine catabolic process [GO:0006154]; hypoxanthine salvage [GO:0043103]; inosine biosynthetic process [GO:0046103]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; purine ribonucleoside salvage [GO:0006166] | cytosol [GO:0005829]; external side of plasma membrane [GO:0009897] | 2'-deoxyadenosine deaminase activity [GO:0046936]; 5'-methylthioadenosine deaminase activity [GO:0090614]; adenosine deaminase activity [GO:0004000]; metal ion binding [GO:0046872] | PF00962; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:19728741}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120 uM for adenosine (at pH 8) {ECO:0000269|PubMed:19728741}; KM=22 uM for 5'-methylthioadenosine (MTA) (at pH 8) {ECO:0000269|PubMed:19728741}; Note=kcat is 6.8 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.51 sec(-1) with 5'-methylthioadenosine... | PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000305|PubMed:19728741}. | null | null | FUNCTION: Catalyzes the hydrolytic deamination of adenosine to produce inosine (PubMed:19728741). Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI) (PubMed:19728741). Plays an essential rol... | Plasmodium knowlesi |
A0A1Z0YU59 | MAMB1_DENAN | RPSFCNLPVKPGPCNGFFSAFYYSQKTNKCHSFTYGGCKGNANRFSTIEKCRRTCVG | null | null | null | extracellular region [GO:0005576] | serine-type endopeptidase inhibitor activity [GO:0004867]; toxin activity [GO:0090729] | PF00014; | 4.10.410.10; | Venom Kunitz-type family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28630289}. | null | null | null | null | null | FUNCTION: Selectively interacts with vasopressin V2 receptor (V2R/AVPR2) and fully inhibits three major signaling pathways of this receptor that are GalphaS protein, the interaction with beta-arrestin and activation of MAP kinase (PubMed:28630289, PubMed:35122240). Inhibits vasopressin binding human V2R in the nanomola... | Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps) |
A0A1Z2R986 | EGLN_DANRE | MKSICCVLVLCLLLCRRSTASESICELKDVSGNSNDWIVLREKPLGCWTDFQTENGTEVHIINLEDNPSVFTVNLLKANKSVVIFTSSSAQSSHAMLFDNPAVSIYVTNKTSLTFIHPTQKPLQILTAPPAGNVSAVLRWAAETFGGVTSVTNARNPKTITFTGVKGSQNSSRCELMPETPTEKPFIHLELNEPIEALKSCYMKHEGEKLHIINIPDGVTIRHVSVHLLSDCNVVLRGPAGTHWIIKNSLRIGILSNNQIHLQSFPLRPRMAISDNPTDIRQKALSYFSSGFISSYSEIRLNVTNVELWITDYSISSAPT... | null | null | angiogenesis [GO:0001525]; blood vessel morphogenesis [GO:0048514]; cell migration [GO:0016477]; cellular response to mechanical stimulus [GO:0071260]; endothelial cell morphogenesis [GO:0001886]; epithelial to mesenchymal transition [GO:0001837]; regulation of transforming growth factor beta receptor signaling pathway... | cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | glycosaminoglycan binding [GO:0005539]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity [GO:0005024]; type II transforming growth factor beta receptor binding [GO:0005114] | PF00100; | 2.60.40.4100; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17813}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis. Required for normal structure and integrity of adult vasculature. Important for endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morph... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A218N034 | WTF4_SCHKA | MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDESTLPPYSEIWKYIKTVSEDSSTGPTETTNPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFFVTIGITCPILLITIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAVGLYNSREKWVVIIWLLWVVICYTLFLRSKFGNLNLNKALICSTCSISAALLLFLLYVRLPFWTLKHMFSGLFQVLGVQSCVVIVTKGLTYLFDKHIDATGYEIEASSLFVIGNFLFFYEMECPGALKRMPKFIRNGIASFLEGIGNIGRAFRGA... | null | null | meiotic drive [GO:0110134]; protein localization to vacuole [GO:0072665] | ascus epiplasm [GO:0072324]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; perinuclear endoplasmic reticulum [GO:0097038]; vacuolar membrane [GO:0005774]; vacuole [GO:0005773] | null | PF03303; | null | WTF family | null | SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane {ECO:0000255, ECO:0000269|PubMed:28631612, ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:32032353, ECO:0000269|PubMed:33108274}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000255, ECO:0000269|PubMed:33108274}; Multi-pass membrane protein {ECO:00... | null | null | null | null | null | FUNCTION: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-s... | Schizosaccharomyces kambucha (Fission yeast) |
A0A248QE08 | FAP_CHLVA | MASITSRASARASCSQANTRAGRVALSGGALLRPARPARSFVPARKQQQGAVRRGGALSARASAVEDIRKVLSDSSSPVAGQKYDYILVGGGTAACVLANRLSADGSKRVLVLEAGPDNTSRDVKIPAAITRLFRSPLDWNLFSELQEQLAERQIYMARGRLLGGSSATNATLYHRGAAGDYDAWGVEGWSSEDVLSWFVQAETNADFGPGAYHGSGGPMRVENPRYTNKQLHTAFFKAAEEVGLTPNSDFNDWSHDHAGYGTFQVMQDKGTRADMYRQYLKPVLGRRNLQVLTGAAVTKVNIDQAAGKAQALGVEFSTD... | 4.1.1.106 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:28860382}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:28860382}; | glycine betaine biosynthetic process from choline [GO:0019285] | chloroplast [GO:0009507]; mitochondrial inner membrane [GO:0005743] | choline dehydrogenase activity [GO:0008812]; flavin adenine dinucleotide binding [GO:0050660]; lyase activity [GO:0016829] | PF05199;PF00732; | 3.50.50.60;3.30.560.10; | GMC oxidoreductase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + H(+) + hnu = a long-chain alkane + CO2; Xref=Rhea:RHEA:18969, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30212, ChEBI:CHEBI:57560, ChEBI:CHEBI:83563; EC=4.1.1.106; Evidence={ECO:0000269|PubMed:28860382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:1... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 (with palmitate as substrate) (PubMed:28860382, PubMed:37000872). Optimum pH is 6.0 (with octanoate as substrate) (PubMed:37000872). {ECO:0000269|PubMed:28860382, ECO:0000269|PubMed:37000872}; | null | FUNCTION: Catalyzes the decarboxylation of free fatty acids to n-alkanes or n-alkenes in response to blue light (PubMed:28860382, PubMed:30106504, PubMed:30673222). Substrate preference is toward fatty acids with C16 or C17 chains (PubMed:28860382, PubMed:30106504, PubMed:30673222). Converts n-octanoic acid (C8 chain) ... | Chlorella variabilis (Green alga) |
A0A250YGJ5 | SIR6_CASCN | MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVRQSSNVVFHTGAGISTASGIPDFRGPHGVWTMEERGLAPKFDTTFENARPTQTHMALVQLERVGLLHFVVSQNVDGLHVRSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKTTGRLCTVAKARGLRACRGELRDTILDWEDALPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGKLVIVNLQPTKHDRHADLRIHGYVDDVMTQLMKHLGLEIPAWDGPRVLEKALPPLPRPPTPKLEPTDKSLAQLNGSVPADSKPEPC... | 2.3.1.-; 2.3.1.286; 2.4.2.- | null | cardiac muscle cell differentiation [GO:0055007]; circadian regulation of gene expression [GO:0032922]; determination of adult lifespan [GO:0008340]; double-strand break repair [GO:0006302]; ketone biosynthetic process [GO:0042181]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of glycolytic ... | chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; damaged DNA binding [GO:0003684]; DNA damage sensor activity [GO:0140612]; metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD+-protein-arginine ADP-ribosyltransferase activity [GO:0106274]; NAD-dependent histone H3K18 deacetylase activity [GO:0097372]; NAD-dependent histo... | PF02146; | 2.20.28.200;3.40.50.1220; | Sirtuin family, Class IV subfamily | PTM: Acetylated at Lys-33. Deacetylation at Lys-33 by SIRT1 promotes homomultimerization and binding to double-strand breaks (DSBs) sites. {ECO:0000250|UniProtKB:Q8N6T7}.; PTM: Phosphorylation at Ser-10 by MAPK8/JNK1 in response to oxidative stress stimulates the mono-ADP-ribosyltransferase activity on PARP1, leading t... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P59941}. Chromosome {ECO:0000250|UniProtKB:Q8N6T7}. Chromosome, telomere {ECO:0000250|UniProtKB:Q8N6T7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P59941}. Note=Predominantly nuclear. Associated with pericentric heterochromatin and telomeric heterochromatin region... | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=... | null | null | null | null | FUNCTION: NAD-dependent protein deacetylase, deacylase and mono-ADP-ribosyltransferase that plays an essential role in DNA damage repair, telomere maintenance, metabolic homeostasis, inflammation, tumorigenesis and aging (By similarity). Displays protein-lysine deacetylase or defatty-acylase (demyristoylase and depalmi... | Castor canadensis (American beaver) |
A0A286QZ36 | RAC1_STIJA | MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGRPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRTKWYPEVSHHCPSTPIILVGTKLDLRDDKETMNKLSERSLRPIAYPQGLQMQKEIHAVKYLECSALTQKGLKTVFDEAIRAVLCPPAKNKSKRSCQLL | null | null | cortical cytoskeleton organization [GO:0030865]; defense response to Gram-negative bacterium [GO:0050829]; engulfment of apoptotic cell [GO:0043652]; establishment or maintenance of cell polarity [GO:0007163]; innate immune response [GO:0045087]; mitotic cytokinesis [GO:0000281]; motor neuron axon guidance [GO:0008045]... | cell projection [GO:0042995]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rho family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63000}; Lipid-anchor {ECO:0000250|UniProtKB:P63000}; Cytoplasmic side {ECO:0000250|UniProtKB:P63000}. | null | null | null | null | null | FUNCTION: Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. {ECO:0000250|UniProtKB:P63000}. | Stichopus japonicus (Sea cucumber) |
A0A286R227 | NIA_ULVPR | MGVRHSASKDYIAGRPLVPGEAPLDKKNSNFSSWKPVTEIDDRDAKCADNWVPRHPDLIRLTGKHPFNSEPPHADVMKEGWLTPVSMHFVRNHGAVPRLEWGSHRITITGLVERPMEITMDDIAKLPAVTVPCLLTCCGNRRKEVNMVKNSQGFSWGPGAVSVNNWTGARLSDVLKLVGVKSQAQGAKYVHFCGPKGELPKGVDGSYGTALTLGHALDPSMDVLIAYKQNGQFLHPDHGFPCRMLIPGWIGGRSVKWLSHLHVSDKDSQNWYHFHDNKVLPPHVDAESAAKQGWWKDPSFILKELNINSTISSPGHDERI... | 1.7.1.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:29371148}; Note=Binds 1 FAD (per monomer/chain). {ECO:0000269|PubMed:29371148}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250|UniProtKB:P49050}; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. {ECO:000... | cellular response to nitrite [GO:0071250]; nitrate assimilation [GO:0042128]; nitrate metabolic process [GO:0042126]; sulfur compound metabolic process [GO:0006790] | mitochondrion [GO:0005739] | FAD binding [GO:0071949]; heme binding [GO:0020037]; molybdenum ion binding [GO:0030151]; molybdopterin cofactor binding [GO:0043546]; nitrate reductase (NADH) activity [GO:0009703]; nitrate reductase activity [GO:0008940]; sulfite oxidase activity [GO:0008482] | PF00173;PF00970;PF03404;PF00175;PF00174; | 2.60.40.650;3.10.120.10;3.40.50.80;3.90.420.10;2.40.30.10; | Nitrate reductase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + nitrite = H(+) + NADH + nitrate; Xref=Rhea:RHEA:17913, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.7.1.1; Evidence={ECO:0000269|PubMed:29371148}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for NADH in the ferricyanide reduction by the FAD-binding domain (at ph 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:29371148}; Vmax=9055 umol/min/mg enzyme in the ferricyanide reduction by the FAD-binding domain (at ph 7.0 and 25 degrees Celsius) {ECO:000... | null | null | null | FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. {ECO:0000305}. | Ulva prolifera (Green seaweed) (Enteromorpha prolifera) |
A0A286Y9D1 | PHF14_DANRE | MDRGSKRRQVKPLADSLLDALDYDSSDDSDFKVGESSGSEGTGNGSDEEGSKESAAGSESDSDAAAASADEEGIDDLETKDLNQEDDEEEKVKESFSEETSSKETGGSSRSRKKGEKSSDMEPNGSATTEENSAEPKKWNLRRNRPMLDFTTMEELNEMDDYDSEDDNDWRPTQGKKKGKASSGKEKEGSGEEDDDDDDGGSDEEDNEDDNDDDDDDDDEGNDDESSSSDSEEEGKKPKKKAGKNTGAFDEEETNDSHSTSHGKGNEDSLLERPQTWSSQRMEHILICCVCLGDNSEDADEIIQCDNCGVTVHEGCYGVD... | null | null | lung alveolus development [GO:0048286]; mesenchymal cell proliferation [GO:0010463]; mesenchymal cell proliferation involved in lung development [GO:0060916]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of mesenchymal cell proliferation [GO:0072201]; negative regulation of mes... | nucleus [GO:0005634] | histone binding [GO:0042393]; histone reader activity [GO:0140566]; zinc ion binding [GO:0008270] | PF00628;PF13831;PF13832; | 2.30.30.1150;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9D4H9}. | null | null | null | null | null | FUNCTION: Histone-binding protein (PubMed:34365506). Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (PubMed:34365506). Represses PDG... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A287B8J2 | DCTN1_PIG | MAQSKRHVYSRTPSGSRMSAEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLRREGTDSNAKTSKLRGPKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAES... | null | null | cell division [GO:0051301]; cytoplasmic microtubule organization [GO:0031122]; establishment of mitotic spindle orientation [GO:0000132]; nuclear migration [GO:0007097] | axon [GO:0030424]; cell cortex [GO:0005938]; cell tip [GO:0051286]; centriole [GO:0005814]; centrosome [GO:0005813]; dynein complex [GO:0030286]; kinetochore [GO:0000776]; microtubule associated complex [GO:0005875]; microtubule plus-end [GO:0035371]; nuclear envelope [GO:0005635]; spindle pole [GO:0000922] | microtubule plus-end binding [GO:0051010] | PF01302;PF12455; | 1.10.287.2610;2.30.30.190; | Dynactin 150 kDa subunit family | PTM: Ubiquitinated by a SCF complex containing FBXL5, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q14203}.; PTM: Phosphorylation by SLK at Thr-145, Thr-146 and Thr-147 targets DCTN1 to the centrosome. It is uncertain if SLK phosphorylates all three threonines or one or two of them. PLK1-mediate... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:... | null | null | null | null | null | FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (PubMed:33734450). Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both d... | Sus scrofa (Pig) |
A0A291NUG3 | STING_PTEPA | MLHSSLHPSIPQPRGRRAKKAAFVLLSVCLVVLWDLGERPEHILQWLMLHLASLQLGLLFKGVCSLVEELRHVHSRYQGSYWKAVRACLGCPIRCGTLLLLSCYFYTPFPNTTHLPFTWTLALLGLSQALSILLDLQDLAPAEVSAVCERRNLNVAQGMAWSFYIGYLRLILPGLPARIHSYNQHHNNLLRGAGSHRLYILFPLDCGVPDDLSMVDPNIRFLHELPLQKADRAGIKSRVYTNSVYELLENGRPVGACVLEYATPLQTLFAMSQDSRAGFSREDRLEQAKLFCKTLEDILADAPECQNNCRLVVYQEPAEG... | null | null | autophagosome assembly [GO:0000045]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of macroautophagy [GO:0016239]; positive regulation of type I interferon production [GO:0032481]; reticulophagy [GO:0061709] | autophagosome membrane [GO:0000421]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; plasma mem... | 2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; proton channel activity [GO:0015252]; signaling adaptor activity [GO:0035591] | PF15009; | 1.20.5.5200;3.40.50.12100; | STING family | PTM: Phosphorylation by TBK1 leads to activation and production of IFN-beta (By similarity). Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-366 in the pLxIS motif (By similarity). The phosphorylated pLxIS moti... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:000... | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q86WV6}; | null | null | null | null | FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes low production of type I interferon (IFN-alpha and IFN-beta) (PubMed:29478775). Compared to other mammals, STING1-dependent type I interferon induction is strongly reduced in bats, suggesting t... | Pteronotus parnellii (Parnell's mustached bat) |
A0A291NUI4 | STING_RHIFE | MPHSSLHPSIPRPRGHRAKKAAFVLLSTCLAALWELGEPADHILRWLVLHLASEQLGLLFKGLCSLAEEIRHVHSRYQGSYWRAFRACLGCPIRCGVLLLLSCYCYTFLPNTAGLPFAWIVALLGLSQALNILLDLQGLAPAVVSTVCEQGNFNVAHGLAWSYYIGYLRLILPGLQARIHTYNQRHNNTVRGTGVHKLYILLPLDCGVPDDLSVADPNIRFLHELPKQSADRAGIKGRVYTNSIYEILENGKPVGTCVLEYATPLQTLFAMSQDSRAGFSREERLEQAKLFCQTLGDILADVPESQYCRLIVYLDAAEGS... | null | null | autophagosome assembly [GO:0000045]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of macroautophagy [GO:0016239]; positive regulation of type I interferon production [GO:0032481]; reticulophagy [GO:0061709] | autophagosome membrane [GO:0000421]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; plasma mem... | 2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; proton channel activity [GO:0015252]; signaling adaptor activity [GO:0035591] | PF15009; | 1.20.5.5200;3.40.50.12100; | STING family | PTM: Phosphorylation by TBK1 leads to activation and production of IFN-beta (By similarity). Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-365 in the pLxIS motif (By similarity). The phosphorylated pLxIS moti... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:000... | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q86WV6}; | null | null | null | null | FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes low production of type I interferon (IFN-alpha and IFN-beta) (PubMed:29478775). Compared to other mammals, STING1-dependent type I interferon induction is strongly reduced in bats, suggesting t... | Rhinolophus ferrumequinum (Greater horseshoe bat) |
A0A291NUI5 | STING_EIDHE | MSHSSLHPSIPWPRGHKAKVAAFVLLIVCLAALWKLGEPSDHLLQWLVLHLASLHLRLLFKRVCCLAEELCHIHPRYQGNYSRAVRACLGCPIRYGAVLLLSCYFYVSLPNTVDLPLTWMLAHLGLSEALNILLGLQSLTPAEISTICEQRNFNVAHGLAWSYYIGYLQLILPGLRARIHTYNQLHSNTLQGVGSHRLYILFPLDCGVLDDLSAADPNIRFLHELPRQSADRAGIKGRVYTNSVYELLEKGKPVGTCVLEYATPLQTLFAMSQDGRAGFSQEDRLEQAKLFCRTLEDILADAPESQKNCRLIVYQEPTEE... | null | null | autophagosome assembly [GO:0000045]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of macroautophagy [GO:0016239]; positive regulation of type I interferon production [GO:0032481]; reticulophagy [GO:0061709] | autophagosome membrane [GO:0000421]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; plasma mem... | 2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; proton channel activity [GO:0015252]; signaling adaptor activity [GO:0035591] | PF15009; | 1.20.5.5200;3.40.50.12100; | STING family | PTM: Phosphorylation by TBK1 leads to activation and production of IFN-beta (By similarity). Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-366 in the pLxIS motif (By similarity). The phosphorylated pLxIS moti... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:000... | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q86WV6}; | null | null | null | null | FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes low production of type I interferon (IFN-alpha and IFN-beta) (PubMed:29478775). Compared to other mammals, STING1-dependent type I interferon induction is strongly reduced in bats, suggesting t... | Eidolon helvum (Straw-colored fruit bat) |
A0A2D0TC04 | PDE_NAJAT | LKQSKQPLESCRNRCNETFSEELSYCSCDNKCTERKACCWDYQDICVLPTQSWSCNKLRCGEKRMANVLCSCSEDCLTKKDCCTDYKSICKRETSWLKDQCASSSASQCPEGFDQSPLILFSMDGFRAEYLETWDTLMPNINKLKTCGTHAKYMRAVYPTKTFVNHYTIVTGLYAETHGIIDNNMYDVKLNQNFSLSGSNMRNAAWWGGQPIWHTASYQGLKAATYFWPGSEVKINGSYPTIYKVYNKSTPFEARVMEVLKWLDLPKAKRPDFSTLYIEEPDTTGHKFGPVSGQVIKSLQMADRTLGMLMEGLKQRNLHN... | 3.6.1.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:W8E7D1}; Note=Binds 2 divalent metal cations per subunit. {ECO:0000269|Ref.1, ECO:0007744|PDB:5GZ4, ECO:0007744|PDB:5GZ5}; | nucleoside triphosphate catabolic process [GO:0009143] | extracellular region [GO:0005576] | ADP phosphatase activity [GO:0043262]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; nucleoside triphosphate diphosphatase activity [GO:0047429]; toxin activity [GO:0090729] | PF01223;PF01663;PF01033; | 4.10.410.20;3.40.720.10;3.40.570.10; | Nucleotide pyrophosphatase/phosphodiesterase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:W8E7D1}. | CATALYTIC ACTIVITY: Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:W8E7D1}; | null | null | null | null | FUNCTION: Hydrolyzes ADP with high activity. Shows weak or no activity on 5'-AMP, 5'-GMP, 3'-AMP, ATP, cAMP, and cGMP. Is devoid of monophosphatase and proteinase activities. Dose-dependently inhibits platelet aggregation induced by ADP and collagen. {ECO:0000250|UniProtKB:W8E7D1}. | Naja atra (Chinese cobra) |
A0A2H1A768 | CDR1_CANAR | MSEKPFVDAPPPEDGVAHQVSPHDNGSLSEEANSINEYTGFGAHQEGEIRELARTFTNMSHDSGHDLSKTNTSQDLLKYLSHMSEVPGVEPFDPEQISEQLNPDSPNFNAKFWVKNMRKLFDSNPDYYKPSKLGLAYRNLRAYGVAADSDYQPTVSNGLWKMAVDYWHDMRKIDESRCFDILKTMDGYFKPGEVTVVLGRPGSGCSTLLKTIACNTYGFHIGEESQISYDGMTPDEIHKHHRGDVVYSAETDVHFPHLSVGDTLEFAAKLRTPQNRGEVSRLEHAKHMASVTMATYGLSHTRNTPVGNDFVRGVSGGERK... | null | null | xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961] | membrane [GO:0016020]; plasma membrane [GO:0005886] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF01061;PF00005;PF14510;PF06422; | 3.40.50.300; | ABC transporter superfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30718246}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + fluconazole(in) + H2O = ADP + fluconazole(out) + H(+) + phosphate; Xref=Rhea:RHEA:61916, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:46081, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:33353950, ECO:0000269|PubMed:36836283}; Physiologica... | null | null | null | null | FUNCTION: Pleiotropic ABC efflux transporter that confers resistance to numerous chemicals including itraconazole, fluconazole, voriconazole and posaconazole. {ECO:0000269|PubMed:30696744, ECO:0000269|PubMed:30718246, ECO:0000269|PubMed:33353950, ECO:0000269|PubMed:35893151, ECO:0000269|PubMed:36836283, ECO:0000269|Pub... | Candida auris (Yeast) |
A0A2H4DGV8 | C7BL6_INUHU | MEPFTTFSLVASSLILLICWALVKANKPAKNLPPGPPKLPIIGNMHQLESQSPHRVLRKLSRKYGPIMHLQLGQVPTVVISTPRLVEEVVKHHDINFADRPTNTTSQIFYYNNQNVAWSSYGNYWRQIKKIVTLELLSVKKVRSFSSIRAEELTRAVKSVEPSVGSTINFRDLTSQTVNNMVSRATLGDVCKERHILLDTMNDILKTFNSFNVVNFFPSLQFLNVITGKKAKWLKIHKQLDHILENILEEHKSKPKGNQDDEDLIDVLLRVKDAGGQELPITNDNVKAITLEMLTAGTSSSSMTIEWAFCELMRHPEVMK... | 1.14.14.168; 1.14.14.170 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | response to jasmonic acid [GO:0009753]; sesquiterpene biosynthetic process [GO:0051762]; terpenoid biosynthetic process [GO:0016114] | membrane [GO:0016020] | germacrene A acid 8beta-hydroxylase activity [GO:0102614]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=germacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--hemoprotein reductase] = 8beta-hydroxygermacra-1(10),4,11(13)-trien-12-oate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:57964, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:1... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:29086444}. | null | null | FUNCTION: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones (PubMed:29086444). Hydroxylates germacrene A acid to 8-beta-hydroxy-germacrene A and 8-alpha-hydroxy-germacrene A acids (PubMed:29086444). Unlike 8-alpha-hydroxy-germacrene A acid with is spontaneously converted into inunolide (12, 8-al... | Inula hupehensis (Inula helianthus-aquatilis subsp. hupehensis) |
A0A2I0BVG8 | CDPK1_PLAFO | MGCSQSSNVKDFKTRRSKFTNGNNYGKSGNNKNSEDLAINPGMYVRKKEGKIGESYFKVRKLGSGAYGEVLLCREKHGHGEKAIKVIKKSQFDKMKYSITNKIECDDKIHEEIYNEISLLKSLDHPNIIKLFDVFEDKKYFYLVTEFYEGGELFEQIINRHKFDECDAANIMKQILSGICYLHKHNIVHRDIKPENILLENKHSLLNIKIVDFGLSSFFSKDNKLRDRLGTAYYIAPEVLRKKYNEKCDVWSCGVILYILLCGYPPFGGQNDQDIIKKVEKGKYYFDFNDWKNISEEAKELIKLMLTYDYNKRITAKEAL... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27923926}; | female gamete generation [GO:0007292]; intracellular signal transduction [GO:0035556]; male gamete generation [GO:0048232]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468] | cytoplasm [GO:0005737]; host cell plasma membrane [GO:0020002]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sperm flagellum [GO:0036126]; symbiont-containing vacuole membrane [GO:0020005] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683] | PF13499;PF00069; | 1.10.238.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily | PTM: Myristoylated. Myristoylation, palmitoylation and the basic cluster motif are required for the localization to the parasitophorous vacuole membrane. {ECO:0000250|UniProtKB:P62344}.; PTM: Palmitoylated. Palmitoylation increases in merozoites in response to low level of extracellular K(+) in the host blood. Myristoy... | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Cell membrane {ECO:0000269|PubMed:29311293}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}; Cytoplasmic side {ECO:0000250|UniProtKB:P62344}. Parasitophorous vacuole membrane {ECO:0000250|UniProtKB:P62344}; Lipid-an... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:27923926}; CATALYTIC... | null | null | null | null | FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (PubMed:27923926). By phosphorylating various proteins, required for microneme secretion and thus merozoite egress from and invasion of host erythrocytes... | Plasmodium falciparum (isolate NF54) |
A0A2I0C265 | PLM9_PLAFO | MFFINFKKIKKKQFPIYLTQHRIITVFLIFIYFINLKDCFHINNSRILSDVDKHRGLYYNIPKCNVCHKCSICTHENGEAQNVIPMVAIPSKRKHIQDINKEREENKYPLHIFEEKDIYNNKDNVVKKEDIYKLRKKKKQKKNCLNFLEKDTMFLSPSHDKETFHINHMNKIKDEKYKQEYEEEKEIYDNTNTSQEKNETNNEQNLNINLINNDKVTLPLQQLEDSQYVGYIQIGTPPQTIRPIFDTGSTNIWIVSTKCKDETCLKVHRYNHKLSSSFKYYEPHTNLDIMFGTGIIQGVIGVETFKIGPFEIKNQSFGLV... | 3.4.23.- | null | entry into host cell by a symbiont-containing vacuole [GO:0085017]; protein processing [GO:0016485] | cytoplasmic vesicle [GO:0031410]; membrane [GO:0016020]; rhoptry [GO:0020008] | aspartic-type endopeptidase activity [GO:0004190] | PF00026; | 2.40.70.10; | Peptidase A1 family | PTM: Autocleaved into a p55 mature form. {ECO:0000250|UniProtKB:Q8ILG2}. | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, rhoptry {ECO:0000269|PubMed:29074774}. Note=In schizonts, localizes to the bulb of rhoptries. {ECO:0000269|PubMed:29074774}. | null | null | null | null | null | FUNCTION: During the asexual blood stage, initiates the proteolytic maturation of several rhoptry proteins and thus, is required for merozoite invasion of host erythrocytes and probably the subsequent development of the ring-stage (PubMed:29074774). Cleaves rhoptry associated protein 1 RAP1 and apical sushi protein ASP... | Plasmodium falciparum (isolate NF54) |
A0A2I2F2I5 | CFOL_ASPCN | MLRSRQATNALRAVGQTRPLRSQTAVAFTQSLNKVPSNRRSEATVATASSTASGAFNSQVRPTPSPTFNQYDSKVQPLTGMSRNVTDESFIGKTGGEIFHDMMLRQGVKHIFGYPGGAILPVFDAIYNSTHFDFILPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNIVTPMQDALLDGTPMVVFCGQVPTTSIGSDAFQEADIVGISRPCTKWNVMVKNIAELPRRINEAFQIATTGRPGPVLVDLPKDVTAGILRRAIPTDAAIPSLPSASIQDAMDLNHKQLEASIARVAKLVNMAKQPVIYAGQGVIQSESGP... | 2.2.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P07342}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P07342}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250|UniProtKB:P07342}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250... | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | acetolactate synthase complex [GO:0005948]; mitochondrion [GO:0005739] | acetolactate synthase activity [GO:0003984]; flavin adenine dinucleotide binding [GO:0050660]; magnesium ion binding [GO:0000287]; pyruvate decarboxylase activity [GO:0004737]; thiamine pyrophosphate binding [GO:0030976] | PF02775;PF00205;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2; Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6; Evidence={ECO:0000250|UniProtKB:P07342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25250; Evidence={ECO:0000250|UniProtKB:P... | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4. {ECO:0000250|UniProtKB:P07342}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4. {ECO:0000250|UniProtKB:P07342}. | null | null | FUNCTION: Acetolactate synthase catalytic subunit, mitochondrial; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity (PubMed:36704842). Is not direcly involved in chlorflavonin biosynthesis but acts as a self-resistant protein that... | Aspergillus candidus |
A0A2I2F2N6 | CFOA_ASPCN | MSRPELIPDILIRHAGESCEKVAFAGPGWTITYGDLEKRTRRLAAHLVHAGIGRGDFVAIVLGRCLQTVESVLAITRAGAVGVPLDSRSPSSELAKVLEHSGARVIITDGRYLTTVRTAAAEGSLIILSTEEIPKMDAIEGKHQIARYQDWIEDAEYSTLDIQIDNLREDEQAFLHYTSGTTSLPKGVLSNQRSWLLNVNSLVSAFELTPEDRFFWPLPLFHCIGHLLCIMGTVVVGASAYLPDADQTLFDSLRDTNAQETTLIVGAPTTFHDLMDAAKRSDPTSPLFLPRLRACMYAGSSASGSLGAQIKEYLGVPLLN... | 2.3.1.-; 6.3.2.- | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|PROSITE-ProRule:PRU00258}; | fatty acid biosynthetic process [GO:0006633]; flavonoid biosynthetic process [GO:0009813]; heterocycle biosynthetic process [GO:0018130]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF13193;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765;PF00975; | 3.30.300.30;3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.40.366.10;3.40.50.12780;3.40.50.720;3.10.129.110; | NRP synthetase family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis. {ECO:0000269|PubMed:36704842}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity (PubMed:36704842). Within the pathway, the PKS-NRPS cfoA, is responsible for the generation of the key precursor chalcone (PubMed:36704842). T... | Aspergillus candidus |
A0A2I4E5L6 | VCL6_JUGRE | MAFKPKIPIALLLLTSLLAICAGLALAMQDPELKQCKHQCRHQRQFDEQEKEHCQRSCDEYHIEKKARERAERRRSEEGSSREEGYEEEELGGEREEENPYVFEDEDFETRVRTDEGRIQVLEKFTKRSKLLRGIENFRVAILEANPQTFISPAHFDAELVVFVAKGRATITTVREEKRENFNVEQGDIMRIPAGTPVYLINRDENEKLYIVKILRPVSVPGHFEAFHGSGGEDPESFYRAFSWEVLEAALKTRRDQLEKLFGKQTQGVIIKASKEQIRSMSKHEETTPRIWPFGGDSTHPFNLFHKRPSQSNQFGRLFE... | null | null | protein homotrimerization [GO:0070207]; seed maturation [GO:0010431] | extraorganismal space [GO:0043245] | nutrient reservoir activity [GO:0045735] | PF00190; | 2.60.120.10; | 7S seed storage protein family | PTM: N-glycosylated; paucimannose-type structures containing xylose. {ECO:0000269|PubMed:30054513}. | null | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Denaturation starts at 45 degrees Celsius. At temperatures above 75 degrees Celsius, begins to precipitate, and eventually becomes irreversibly denatured. Cannot be resolubilized in aqueous solution after being heated up to 95 degrees Celsius and then cooled down ... | FUNCTION: Seed storage protein. {ECO:0000305|PubMed:30054513}. | Juglans regia (English walnut) |
A0A2I6PJ05 | GGS1_HYPPI | MVPNANSNTVSLQSPNAIPPRTSSTGYITPFPPAKSVLRPVPESDWLGQNNTRNRSSSTTAIPLTGMHATGPQDPARYETEDLNYTSRKTWSEQKEKVLVGPFEYLFAHPGKDFRTLMVNSFNAWLEVPQESLDVITKVVGMLHTASLLVDDVEDNSLLRRGLPVAHSIFGTAQTINSANYVYFCALQELQKLKNPEAINVYTEELLNLHRGQGMDLFWRDTLTCPTEEEYLEMVGNKTGGLFRLAIKLMQAESGTPIDCVPLVNILGIIFQIQDDYRNLSSPEYGQNKGLCEDLTEGKFSFLIIHSIRSNPSNLQLLNI... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:29283570}. | null | null | FUNCTION: Catalyzes the trans-addition of the 3 molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranylgeranyl pyrophosphate (GGPP). GGPP is a precursor for the biosynthesis of many secondary metabolites, including the indole diterpenes nodulisporic acids (NA). {ECO:0000305|Pub... | Hypoxylon pulicicidum |
A0A2I7G3B0 | ALDH1_TANCI | MSSGANGNSKSLAYDIKFTKLFINGEFVDSISGSTFETIDPATEEVLATVAEGREEDVDLAVKAAREAFDNGPWPRLSGEARRKILLKFADLIEENADEIATLEVIDTGKPFQIARYVENSWTSETFRYFAGAADKIRGATLKMSSDFQAYTLREPIGVVGHIIPWNAPAYLFAMKVAPALAAGCTVVIKPAENTPLVGLFMAYLSKLAGVPDGVINVVNGFGSTAGAAVSSHMDIDAVTFTGSTKVGRTIMQAAAASNLKPVSLELGGKSPFIVFDDADIEKAAEIAVLGVLSNKGELCVAGSRVFVHEGIYDAFVKKL... | 1.2.1.-; 1.2.1.5 | null | isoprenoid biosynthetic process [GO:0008299] | null | aldehyde dehydrogenase (NAD+) activity [GO:0004029]; aldehyde dehydrogenase (NADP+) activity [GO:0033721] | PF00171; | null | Aldehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.5; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.6 uM for trans-chrysanthemal (in the presence of NAD(+)) {ECO:0000269|PubMed:29122986}; KM=4.4 uM for trans-chrysanthemal (in the presence of NADP(+)) {ECO:0000269|PubMed:29122986}; KM=20.4 uM for NAD(+) {ECO:0000269|PubMed:29122986}; KM=68.6 uM for NADP(+) {ECO:... | PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:29122986}. | null | null | FUNCTION: Component of the monoterpenoid pyrethrins biosynthesis; pyrethrins are widely used plant-derived pesticide (PubMed:30468448). Mediates the conversion of trans-chrysanthemal into trans-chrysanthemic acid (PubMed:29122986). Can also use octanal, hept-2-enal, dodecanal, citral, farnesal, citronellal and perillyl... | Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum cinerariifolium) |
A0A2I7G3B3 | ADH2_TANCI | MSLNTPDVIICKAAVVRELGRSVMVEEIKVDPPKATEVRIKMLFASICHTDMLCFDGFPTPLFPRIPGHEGVGMVESVGEDIKTKLKPGDIVMPLFMGECGQCLNCKSKRTNLCHAYPLTLSGLLLDGTSRMSIAKTEETIYHHLSCSTWSEYMVIDINYVLKIDPKMHLPYASFLSCGFTTGFGAPWKETQITKGSIVAVFGLGAVGLGAIKGAQMQGASIIIGVDINENKAAKGKAFGMTHFINPKDHPNQLVSDMVRDITDGLGVDYCFECTGIASLLKEIIEASKIGFGTTILIGAAPDNVPISSLSLINGRTLKG... | 1.1.1.-; 1.1.1.144; 1.1.1.347 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P40394}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P40394}; | formaldehyde catabolic process [GO:0046294]; isoprenoid biosynthetic process [GO:0008299] | cytosol [GO:0005829] | alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; perillyl-alcohol dehydrogenase activity [GO:0018457]; S-(hydroxymethyl)glutathione dehydrogenase activity [GO:0051903]; zinc ion binding [GO:0008270] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family, Class-IV subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(R,R)-chrysanthemol + NAD(+) = (1R,3R)-chrysanthemal + H(+) + NADH; Xref=Rhea:RHEA:60668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:143898, ChEBI:CHEBI:143899; Evidence={ECO:0000269|PubMed:29122986}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60669; Evid... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=236 uM for trans-chrysanthemol {ECO:0000269|PubMed:29122986}; KM=193 uM for NAD(+) {ECO:0000269|PubMed:29122986}; Note=kcat is 0.75 sec(-1) with trans-chrysanthemol as substrate (in the presence of NAD(+)) (PubMed:29122986). kcat is 0.64 sec(-1) with NAD(+) as subs... | PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:29122986}. | null | null | FUNCTION: Component of the monoterpenoid pyrethrins biosynthesis; pyrethrins are widely used plant-derived pesticide (PubMed:30468448). Mediates the conversion of trans-chrysanthemol into trans-chrysanthemal (PubMed:29122986). {ECO:0000269|PubMed:29122986, ECO:0000303|PubMed:30468448}. | Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum cinerariifolium) |
A0A2J6L8Y7 | IF4E1_LACSA | MVEEIMKSEEQKLIDVNKHRGVRSDGEEDEQLEEGEIVGGDADTLSSSSSSRPGTAIAQHPLEHSWTFWFDTPSAKSKQVAWGSSMRPIYTFSSVEEFWSLYNNIHRPSKLAQGADFYCFKNKIEPKWEDPVCANGGKWTMTFTKAKSDTCWLYTLLAMIGEQFDHGDDICGAVVNVRARQEKIALWTKNAANESAQLSIGKQWKEFIDYNDTIGFIFHEDAKTLDRSAKNKYTV | null | null | defense response to virus [GO:0051607]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634] | RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-133-Cys-171 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}. | null | null | null | null | null | FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiatio... | Lactuca sativa (Garden lettuce) |
A0A2J8C362 | CUTI1_VERDA | MQTSALLLAAQALVASAGLIERQSCPSIHVFGARETTVGPGYGSAGTVVNLILNAYPGSTAEAIVYPACGGQSSCGGISYGNSAMQGTNAVASAVNSFNQRCPNTQIVLVGYSQGGQIMDNALCGGGDPGSGITNTAVPLTASAVTAVKAAILMGSPRYRAGFPYNVGTCTAQGFAARPAGFVCPSGSKIQNYCDSPDPYCCTGNNQAVHQGYGGVYGQAALTFVRSKLNSGGSPPTTPPTTPPTTPPTTPPTTPPPSGSCAALYGQCGGQGWNGATCCSQGTCRASNQWYSQCL | 3.1.1.74 | null | carbohydrate metabolic process [GO:0005975]; symbiont entry into host [GO:0044409] | extracellular region [GO:0005576] | carboxylic ester hydrolase activity [GO:0052689]; cellulose binding [GO:0030248] | PF00734;PF01083; | 3.40.50.1820; | Cutinase family | PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. {ECO:0000250|UniProtKB:P11373}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29068240}. | CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000305|PubMed:29068240}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:29068240). May degrade cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:29068240). May also degrade suberin, a specialized macromolecule found in the cell wall of various plant tissue... | Verticillium dahliae (Verticillium wilt) |
A0A2K1ZPK4 | NRP32_POPTR | MPVEENYQPLLQEEEERAYDSDEKVLIIGVDSDTESGGSTVLPPFSWKKLWLFTGPGFLMSIAFLDPGNLEGDLQAGAIAGYSLLWLLLWATAMGLLVQLLSARLGVATGRHLAELCREEYPTWASMVLWIMAELALIGADIQEVIGSAIAIKILSNGFVPLWAGVTITACDCFIFLFLENYGVRKLEAVFAVLIGIMAVTFGWMFADAKPSASELFLGILIPKLSSRTIQQAVGVVGCIIMPHNVFLHSALVQSREIDHNKKDRVQEALRYYSIESTTALVISFVINLFVTTVFAKGFYGTELANSIGLVNAGQYLQDK... | null | null | defense response to bacterium [GO:0042742]; intracellular iron ion homeostasis [GO:0006879]; iron ion transmembrane transport [GO:0034755]; iron ion transport [GO:0006826]; manganese ion transmembrane transport [GO:0071421]; manganese ion transport [GO:0006828]; positive regulation of reactive oxygen species metabolic ... | plant-type vacuole membrane [GO:0009705]; vacuolar membrane [GO:0005774] | cadmium ion transmembrane transporter activity [GO:0015086]; manganese ion transmembrane transporter activity [GO:0005384]; metal ion transmembrane transporter activity [GO:0046873] | PF01566; | null | NRAMP (TC 2.A.55) family | null | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:35700212}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Mn(2+)(in) = Mn(2+)(out); Xref=Rhea:RHEA:28699, ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:35700212}; CATALYTIC ACTIVITY: Reaction=Fe(2+)(in) = Fe(2+)(out); Xref=Rhea:RHEA:28486, ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:35700212}; | null | null | null | null | FUNCTION: Divalent metal transporter (PubMed:35700212). Can transport manganese (Mn) and iron (Fe) (PubMed:35700212). Involved in the release of metals stored in the vacuole (PubMed:35700212). {ECO:0000269|PubMed:35700212}. | Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) |
A0A2K3D5Z7 | CMD1_CHLRE | MSVALASEYQLVQNAQLPQRWSQSARKSLAILEATARKEATAQMEAAGGSFCGQFPVDPAFKVLSLEYSAPNPDIARAIRRVDSVPNPPLPSHVVAIQSTAVDADLSLAMGVSLTPGRHTSYLVDARALQQSNSAAVAARKADGDKWGPACDEMFRGCRCVTGQEVVFYTAVKEPAGEVEGGEGSLFKPSFDGPAFRPSWGELSGKATGVVACVLQVPIGKETDIICAEYDNLVSKGQFATVDRFGGDHTVNMTGNALIQNDGKAISKGYAVAHRARVTSNVYGKANDVSLQRLAETVWSVVEKRLSFMPAYRDLVITEQ... | 1.14.99.- | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:31043749, ECO:0000269|PubMed:33531488}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:33531488}; | 5-methylcytosine catabolic process [GO:0006211]; regulation of photosynthesis [GO:0010109] | nucleus [GO:0005634] | dioxygenase activity [GO:0051213]; iron ion binding [GO:0005506]; methylcytosine to 5-glyceryl-methylcytosine dioxygenase activity [GO:0120204] | null | null | TET family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 5-methyl-2'-deoxycytidine in DNA + L-ascorbate + O2 = a (8S,9S)-5-glyceryl-2'-deoxycytidine in DNA + CO2 + glyoxylate; Xref=Rhea:RHEA:60132, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:15515, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:36655, ChEBI:CHEBI:38290, ChEBI:CHEBI:85454, ChEBI:CHE... | null | null | null | null | FUNCTION: Dioxygenase that catalyzes DNA modification by mediating the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-glyceryl-methylcytosine (5gmC) (PubMed:31043749, PubMed:33531488). Catalyzes the conjugation of a glyceryl moiety from L-ascorbate (vitamin C) to the methyl group of 5mC through a... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A0A2K3DU55 | PGPP1_CHLRE | MRSVPGPSPPCTRSLAHSCRAAARGPCGSARPRARSVSARAHSSEASDMARVQQNFNSAGVGLFFSLFGGNQSLALPHLAAPDIRHVDWRALKAAGFKGLVFDKDNTLSLPFALEVEPRLQPALAGCLEAFGGRAVLYSNSAGLQQYDPEGKEAAALEAALGIPVLRHADKKPGGGCAELEAHFGCPAPQLIMVGDRYLTDIAFGNRHGMLTVHVQPLTTSGEPFGVVMARRIEEFWVARWTSFGVHPPAHSLAPHDTLAAYVKDQPIA | 3.1.3.27 | null | cardiolipin biosynthetic process [GO:0032049]; chloroplast organization [GO:0009658]; glycerolipid metabolic process [GO:0046486]; phospholipid dephosphorylation [GO:0046839]; photosynthesis [GO:0015979]; thylakoid membrane organization [GO:0010027] | chloroplast [GO:0009507]; mitochondrion [GO:0005739] | phosphatase activity [GO:0016791]; phosphatidylglycerophosphatase activity [GO:0008962] | PF09419; | 3.40.50.1000; | HAD-like hydrolase superfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate; Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27; Evidence={ECO:0000269|PubMed:25910650}; Physiolog... | null | PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2. {ECO:0000269|PubMed:25910650}. | null | null | FUNCTION: Phosphatidylglycerophosphate phosphatase involved in the biosynthesis of phosphatidylglycerol (PG), a phosphoglycerolipid predominantly present in chloroplastic thylakoid membranes and which has important photosynthetic function (PubMed:25910650). Required for thylakoid membranes development and chloroplast f... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A0A2K3DZC4 | BSD2_CHLRE | MNSAALNARTASVAPQPQACHACKCRQLLSRRVPPAQRQVECSAIAPETLQDIIVGGAVVGAVSVALYAGLKKDPVPCSLCQGTGGIRCFACGGDGRNATVSRDDLYDSKALGGGVAPPKRDPLGRTINPRDCKVCRGAGLVLCSQCKGTGFQSAF | null | null | chaperone-mediated protein folding [GO:0061077]; ribulose bisphosphate carboxylase complex assembly [GO:0110102] | chloroplast stroma [GO:0009570]; protein folding chaperone complex [GO:0101031] | metal ion binding [GO:0046872]; protein folding chaperone [GO:0044183] | null | null | BSD2 chaperone family | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:25124725}. Note=Associates with chloroplastic polysomes. {ECO:0000269|PubMed:25124725}. | null | null | null | null | null | FUNCTION: Chloroplast chaperone required for RuBisCo biogenesis and translational regulation of the RuBisCo large subunit (RbcL) (PubMed:25124725). Stabilizes an end-state assembly intermediate of eight RbcL subunits until the small subunits (RBCSs) become available to produce a complete stable RuBisCo complex containi... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A0A2K5QCI5 | APOA1_CEBIM | MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDSVKDSGRDYVSQFESSALGKQLNLKLLDNWDSLTSTVNKLREDLGPVTQEFWDNLEKETGWLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEVKLYSQKLEPLRTEFQEGALQKLQDLQEKLSPLAEQVRDRARAHVDTLRTQLAPYSDELRQRLATRLEVLKESGGASLAEYHAKASEHLSALGEKAKPALEDLRQGLLPVLESFKVSFLSALEEYAKKLSSQ | null | null | adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor sig... | endocytic vesicle [GO:0030139]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:000... | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02647}. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. {ECO:0000250|UniProtKB:P02647}... | Cebus imitator (Panamanian white-faced capuchin) (Cebus capucinus imitator) |
A0A2K5TU92 | SIR6_MACFA | MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVWQSSHVVFHTGAGISTASGIPDFRGPHGVWTMEERGLAPKFDTTFESARPTQTHMALVQLERVGLLRFLVSQNVDGLHVRSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKATGRLCTVAKARGLRACRGELRDTILDWEDSLPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGRLVIVNLQPTKHDRHADLRIHGYVDEVMTRLMKHLGLEIPAWDGPHVLERALPPLPRPPTPKLEPKEESPTRINGSIPAGSCLEPC... | 2.3.1.-; 2.3.1.286; 2.4.2.- | null | cardiac muscle cell differentiation [GO:0055007]; circadian regulation of gene expression [GO:0032922]; double-strand break repair [GO:0006302]; ketone biosynthetic process [GO:0042181]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of glycolytic process [GO:0045820]; negative regulation of p... | chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; damaged DNA binding [GO:0003684]; DNA damage sensor activity [GO:0140612]; metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD+-protein-arginine ADP-ribosyltransferase activity [GO:0106274]; NAD-dependent histone H3K18 deacetylase activity [GO:0097372]; NAD-dependent histo... | PF02146; | 2.20.28.200;3.40.50.1220; | Sirtuin family, Class IV subfamily | PTM: Acetylated at Lys-33. Deacetylation at Lys-33 by SIRT1 promotes homomultimerization and binding to double-strand breaks (DSBs) sites. {ECO:0000250|UniProtKB:Q8N6T7}.; PTM: Phosphorylation at Ser-10 by MAPK8/JNK1 in response to oxidative stress stimulates the mono-ADP-ribosyltransferase activity on PARP1, leading t... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P59941}. Chromosome {ECO:0000250|UniProtKB:Q8N6T7}. Chromosome, telomere {ECO:0000250|UniProtKB:Q8N6T7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P59941}. Note=Predominantly nuclear. Associated with pericentric heterochromatin and telomeric heterochromatin region... | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=... | null | null | null | null | FUNCTION: NAD-dependent protein deacetylase, deacylase and mono-ADP-ribosyltransferase that plays an essential role in DNA damage repair, telomere maintenance, metabolic homeostasis, inflammation, tumorigenesis and aging (PubMed:30135584). Displays protein-lysine deacetylase or defatty-acylase (demyristoylase and depal... | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
A0A2K8FQU5 | TAT_CATRO | MASKMVEIVSKMFIKPSSPTPQSLRRYNLSSIDQTIDSEVTSLAFFYTYNPSHESSKIGDLLKNSLSKTLVSYYQFAGRLIENDYIDCNDEGVEFVEVRIHGRMNDILKRGKSFATDLVLPTRIIALHEDSLLIVQLSHFDCGGIAIGFGASHKVSDGVSNVMFMKDWASSTSLSTFHKPTPLLTADSIFPPEDNKLLSNKSIVSFQQCLGKRFVFSTEAIEKLKSKAIEYGIQKPSRVEVVTAFLCQCAANCDLPRKKPYAIISAVNLRPYLALPQNSIGNIFSFYFCINDEGMDNQFSALISKLRNGKQKLLENIISK... | 2.3.1.- | null | indole alkaloid biosynthetic process [GO:0035835]; response to jasmonic acid [GO:0009753] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | acetyltransferase activity [GO:0016407] | PF02458; | 3.30.559.10; | Plant acyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29438577}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:29438577}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + horhammericine = 19-O-acetylhorhammericine + CoA; Xref=Rhea:RHEA:61068, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:144375, ChEBI:CHEBI:144376; Evidence={ECO:0000269|PubMed:29438577, ECO:0000269|PubMed:31009114}; CATALYTIC ACTIVITY: Reaction=(-)-(R)-19-hydroxytabersonine ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for acetyl-CoA (at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577}; KM=9 uM for (-)-minovincinine (at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:29438577}; KM=58 uM for horhammericine (at pH 7.6 and 30 degrees Celsius) {ECO:0000269|PubMed:... | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:31009114}. | null | null | FUNCTION: Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway; MIAs are used in cancer treatment and other medical applications (PubMed:31009114). Acyltransferase catalyzing the conversion of horhammericine t... | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
A0A2K9RFZ2 | TPS2_VITAC | MSLRFNLIVTPFSNHRIRNRRETFPAQEFPVATSKSAVKVKCNLITSTDLVGKVREKINGKVDNSLEVPAIHPVDIPSNLCMIDTLERLGVDRYFQSEIDGVLEETYRLWQQKEKDIFADVTCRAMAFRLLRVKGYEVSSDELAPYADQAHVNLQISDVTAVIELYRASQERIYEEESTLEKLHAWTSTYLKQQLVSGTISDKKLHKQVEYYLKNYHGILDLVGIRRSLDLYDIDHYQILKAADRFRTICKDLLAFSRQDFNNCQAQYQRELQLLQRWYEDCRLDKLNYGRDVLRISYFVSSAIIGDPELSDARLAFAKY... | 4.2.3.-; 4.2.3.189 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q40577}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577}; | gibberellin biosynthetic process [GO:0009686] | chloroplast [GO:0009507] | (13S)-vitexifolin A synthase activity [GO:0062204]; 9,13-epoxylabda-14-ene synthase activity [GO:0106239]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]; Viteagnusin D synthase activity [GO:0062203] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=9alpha-copalyl diphosphate + H2O = (13S)-vitexifolin A + diphosphate; Xref=Rhea:RHEA:40027, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58622, ChEBI:CHEBI:76954; Evidence={ECO:0000269|PubMed:29315936}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40028; Evidence={ECO:0000269|P... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:29315936, ECO:0000305|PubMed:30468448}. | null | null | FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including cleroda-dienols, and peregrinol lactones and furan derivatives, dopaminergic diterpenoids that can bind to dopamine receptors in the human pituitary gland, have probably ability to lower prolactin levels, and are used to treat menstrual cycle ... | Vitex agnus-castus (Chaste tree) |
A0A2L0ART2 | TXF1A_SCOMU | MEKKIIFLVFLVALLALPGFISTEVIKKDTPYKKRKFPYKSECLKACATSFTGGDESRIQEGKPGFFKCTCYFTTG | null | null | envenomation resulting in positive regulation of blood pressure in another organism [GO:0044499]; negative regulation of voltage-gated potassium channel activity [GO:1903817]; positive regulation of vasoconstriction [GO:0045907] | extracellular region [GO:0005576] | potassium channel regulator activity [GO:0015459]; toxin activity [GO:0090729] | null | null | Scoloptoxin-15 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29358396}. | null | null | null | null | null | FUNCTION: Blocks voltage-gated potassium channels Kv7.4/KCNQ4 (IC(50)=2.5 uM), Kv7.1/KCNQ1 (IC(50)=2.8 uM), Kv7.2/KCNQ2 (IC(50)=2.7 uM) and Kv7.5/KCNQ5 (IC(50)=2.7 uM). Targets the pore domain, in particular negatively charged residues 'Asp-266' and 'Asp-288', of KCNQ4 and probably other KCNQ channel family members whe... | Scolopendra mutilans (Chinese red-headed centipede) (Scolopendra subspinipes mutilans) |
A0A2L0VXR5 | PLE4_CLIPA | MRIPNVFLSYLRQVAVDGTLSSCSGVKSRKPVIAYGFDDSQDSLVDENDEKILEPFGYYRHLLKGKSARTVLMHCFNAFLGLPEDWVIGVTKAIEDLHNASLLIDDIEDESALRRGSPAAHMKYGIALTMNAGNLVYFTVLQDVYDLGMKTGGTQVANAMARIYTEEMIELHRGQGIEIWWRDQRSPPSVDQYIHMLEQKTGGLLRLGVRLLQCHPGVNNRADLSDIALRIGVYYQLRDDYINLMSTSYHDERGFAEDMTEGKYTFPMLHSLKRSPDSGLREILDLKPADIALKKKAIAIMQDTGSLVATRNLLGAVKND... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | antibiotic biosynthetic process [GO:0017000]; plastoquinone biosynthetic process [GO:0010236]; terpenoid biosynthetic process [GO:0016114]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:27143514, ECO:0000269|PubMed:29388775}. | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of pleuromutilin, a tricyclic diterpene showing antibacterial properties (PubMed:27143514, PubMed:29388775). The geranylgeranyl diphosphate (GGPP) synthase catalyzes the first step in pleuromutilin biosynthesis (Pub... | Clitopilus passeckerianus (Pleurotus passeckerianus) |
A0A2L2DDD0 | FIG02_BOARA | MAFLKKSLFLVLFLGIVSLSVCEEEKREGEEKEEKREEEEGKEENEDGNEEHKEKRFLGAILKIGHALAKTVLPMVTNAFKPKQ | null | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; defense response to protozoan [GO:0042832]; defense response to virus [GO:0051607]; hemolysis in another organism [GO:0044179]; innate immune response [GO:0045087]; regulation of defense response to virus... | extracellular region [GO:0005576] | null | PF03032; | null | Frog skin active peptide (FSAP) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32443921}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide that displays antibacterial, antiprotozoal, and antiviral activity (PubMed:32443921). Exhibits antibacterial activity against the Gram-positive bacteria S.epidermidis ATCC 12228 (MIC=4 uM), E.casseliflavus ATCC 700327 (MIC=4 uM), S.aureus ATCC 25923 (MIC=8 uM) and E.faecalis ATCC 29212 (... | Boana raniceps (Chaco tree frog) (Hyla roeschmanni) |
A0A2L2DDE6 | FIG01_BOARA | MAFLKKSLFLVLFLGLVSLSIGEEEKREEEEKNEEGANQEENAENKEKRFIGTLIPLALGALTKLFKG | null | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; defense response to protozoan [GO:0042832]; hemolysis in another organism [GO:0044179]; innate immune response [GO:0045087] | extracellular region [GO:0005576] | null | PF03032; | null | Frog skin active peptide (FSAP) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32967114}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide that displays antibacterial and antiprotozoal activity (PubMed:32967114). Exhibits antibacterial activity against the Gram-positive bacteria S.epidermidis ATCC 12228 (MIC=2 uM), E.casseliflavus ATCC 700327 (MIC=16 uM), S.aureus ATCC 25923 (MIC=4 uM) and E.faecalis ATCC 29212 (MIC=8 uM), ... | Boana raniceps (Chaco tree frog) (Hyla roeschmanni) |
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