| IED ID | IndEnz0002001324 |
| Enzyme Type ID | protease001324 |
| Protein Name |
Replicase polyprotein 1ab ORF1ab polyprotein Cleaved into: Nsp1 EC 3.4.22.- ; Nsp1-alpha papain-like cysteine proteinase EC 3.4.22.- PCP1-alpha ; Nsp1-beta papain-like cysteine proteinase EC 3.4.22.- PCP1-beta ; Nsp2 cysteine proteinase EC 3.4.19.12 EC 3.4.22.- CP2 CP ; Non-structural protein 3 Nsp3 ; Serine protease nsp4 3CLSP EC 3.4.21.- 3C-like serine proteinase Nsp4 ; Non-structural protein 5-6-7 Nsp5-6-7 ; Non-structural protein 5 Nsp5 ; Non-structural protein 6 Nsp6 ; Non-structural protein 7-alpha Nsp7-alpha ; Non-structural protein 7-beta Nsp7-beta ; Non-structural protein 8 Nsp8 ; RNA-directed RNA polymerase Pol RdRp EC 2.7.7.48 Nsp9 ; Helicase nsp10 Hel EC 3.6.4.12 EC 3.6.4.13 Nsp10 ; Uridylate-specific endoribonuclease nsp11 EC 4.6.1.- Non-structural protein 11 Nsp11 ; Non-structural protein 12 Nsp12 |
| Gene Name | rep 1a-1b |
| Organism | Porcine reproductive and respiratory syndrome virus (strain Lelystad) (PRRSV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Arnidovirineae Arteriviridae Variarterivirinae Betaarterivirus Eurpobartevirus Betaarterivirus suid 1 Porcine reproductive and respiratory syndrome virus 1 Porcine reproductive and respiratory syndrome virus (strain Lelystad) (PRRSV) |
| Enzyme Sequence | MSGTFSRCMCTPAARVFWNAGQVFCTRCLSARSLLSPELQDTDLGAVGLFYKPRDKLHWKVPIGIPQVECTPSGCCWLSAVFPLARMTSGNHNFLQRLVKVADVLYRDGCLAPRHLRELQVYERGCNWYPITGPVPGMGLFANSMHVSDQPFPGATHVLTNSPLPQQACRQPFCPFEEAHSSVYRWKKFVVFTDSSLNGRSRMMWTPESDDSAALEVLPPELERQVEILIRSFPAHHPVDLADWELTESPENGFSFNTSHSCGHLVQNPDVFDGKCWLSCFLGQSVEVRCHEEHLADAFGYQTKWGVHGKYLQRRLQVRGIRAVVDPDGPIHVEALSCPQSWIRHLTLDDDVTPGFVRLTSLRIVPNTEPTTSRIFRFGAHKWYGAAGKRARAKRAAKSEKDSAPTPKVALPVPTCGITTYSPPTDGSCGWHVLAAIMNRMINGDFTSPLTQYNRPEDDWASDYDLVQAIQCLRLPATVVRNRACPNAKYLIKLNGVHWEVEVRSGMAPRSLSRECVVGVCSEGCVAPPYPADGLPKRALEALASAYRLPSDCVSSGIADFLANPPPQEFWTLDKMLTSPSPERSGFSSLYKLLLEVVPQKCGATEGAFIYAVERMLKDCPSSKQAMALLAKIKVPSSKAPSVSLDECFPTDVLADFEPASQERPQSSGAAVVLCSPDAKEFEEAAPEEVQESGHKAVHSALLAEGPNNEQVQVVAGEQLKLGGCGLAVGNAHEGALVSAGLINLVGGNLSPSDPMKENMLNSREDEPLDLSQPAPASTTTLVREQTPDNPGSDAGALPVTVREFVPTGPILCHVEHCGTESGDSSSPLDLSDAQTLDQPLNLSLAAWPVRATASDPGWVHGRREPVFVKPRNAFSDGDSALQFGELSESSSVIEFDRTKDAPVVDAPVDLTTSNEALSVVDPFEFAELKRPRFSAQALIDRGGPLADVHAKIKNRVYEQCLQACEPGSRATPATREWLDKMWDRVDMKTWRCTSQFQAGRILASLKFLPDMIQDTPPPVPRKNRASDNAGLKQLVAQWDRKLSVTPPPKPVGPVLDQIVPPPTDIQQEDVTPSDGPPHAPDFPSRVSTGGSWKGLMLSGTRLAGSISQRLMTWVFEVFSHLPAFMLTLFSPRGSMAPGDWLFAGVVLLALLLCRSYPILGCLPLLGVFSGSLRRVRLGVFGSWMAFAVFLFSTPSNPVGSSCDHDSPECHAELLALEQRQLWEPVRGLVVGPSGLLCVILGKLLGGSRYLWHVLLRLCMLADLALSLVYVVSQGRCHKCWGKCIRTAPAEVALNVFPFSRATRVSLVSLCDRFQTPKGVDPVHLATGWRGCWRGESPIHQPHQKPIAYANLDEKKMSAQTVVAVPYDPSQAIKCLKVLQAGGAIVDQPTPEVVRVSEIPFSAPFFPKVPVNPDCRVVVDSDTFVAAVRCGYSTAQLVLGRGNFAKLNQTPPRNSISTKTTGGASYTLAVAQVSAWTLVHFILGLWFTSPQVCGRGTADPWCSNPFSYPTYGPGVVCSSRLCVSADGVTLPLFSAVAQLSGREVGIFILVLVSLTALAHRMALKADMLVVFSAFCAYAWPMSSWLICFFPILLKWVTLHPLTMLWVHSFLVFCLPAAGILSLGITGLLWAIGRFTQVAGIITPYDIHQYTSGPRGAAAVATAPEGTYMAAVRRAALTGRTLIFTPSAVGSLLEGAFRTHKPCLNTVNVVGSSLGSGGVFTIDGRRTVVTAAHVLNGDTARVTGDSYNRMHTFKTNGDYAWSHADDWQGVAPVVKVAKGYRGRAYWQTSTGVEPGIIGEGFAFCFTNCGDSGSPVISESGDLIGIHTGSNKLGSGLVTTPEGETCTIKETKLSDLSRHFAGPSVPLGDIKLSPAIIPDVTSIPSDLASLLASVPVVEGGLSTVQLLCVFFLLWRMMGHAWTPIVAVGFFLLNEILPAVLVRAVFSFALFVLAWATPWSAQVLMIRLLTASLNRNKLSLAFYALGGVVGLAAEIGTFAGRLSELSQALSTYCFLPRVLAMTSCVPTIIIGGLHTLGVILWLFKYRCLHNMLVGDGSFSSAFFLRYFAEGNLRKGVSQSCGMNNESLTAALACKLSQADLDFLSSLTNFKCFVSASNMKNAAGQYIEAAYAKALRQELASLVQIDKMKGVLSKLEAFAETATPSLDIGDVIVLLGQHPHGSILDINVGTERKTVSVQETRSLGGSKFSVCTVVSNTPVDALTGIPLQTPTPLFENGPRHRSEEDDLKVERMKKHCVSLGFHNINGKVYCKIWDKSTGDTFYTDDSRYTQDHAFQDRSADYRDRDYEGVQTTPQQGFDPKSETPVGTVVIGGITYNRYLIKGKEVLVPKPDNCLEAAKLSLEQALAGMGQTCDLTAAEVEKLKRIISQLQGLTTEQALNCLLAASGLTRCGRGGLVVTETAVKIIKYHSRTFTLGPLDLKVTSEVEVKKSTEQGHAVVANLCSGVILMRPHPPSLVDVLLKPGLDTIPGIQPGHGAGNMGVDGSIWDFETAPTKAELELSKQIIQACEVRRGDAPNLQLPYKLYPVRGDPERHKGRLINTRFGDLPYKTPQDTKSAIHAACCLHPNGAPVSDGKSTLGTTLQHGFELYVPTVPYSVMEYLDSRPDTPFMCTKHGTSKAAAEDLQKYDLSTQGFVLPGVLRLVRRFIFGHIGKAPPLFLPSTYPAKNSMAGINGQRFPTKDVQSIPEIDEMCARAVKENWQTVTPCTLKKQYCSKPKTRTILGTNNFIALAHRSALSGVTQAFMKKAWKSPIALGKNKFKELHCTVAGRCLEADLASCDRSTPAIVRWFVANLLYELAGCEEYLPSYVLNCCHDLVATQDGAFTKRGGLSSGDPVTSVSNTVYSLVIYAQHMVLSALKMGHEIGLKFLEEQLKFEDLLEIQPMLVYSDDLVLYAERPTFPNYHWWVEHLDLMLGFRTDPKKTVITDKPSFLGCRIEAGRQLVPNRDRILAALAYHMKAQNASEYYASAAAILMDSCACIDHDPEWYEDLICGIARCARQDGYSFPGPAFFMSMWEKLRSHNEGKKFRHCGICDAKADYASACGLDLCLFHSHFHQHCPVTLSCGHHAGSKECSQCQSPVGAGRSPLDAVLKQIPYKPPRTVIMKVGNKTTALDPGRYQSRRGLVAVKRGIAGNEVDLSDGDYQVVPLLPTCKDINMVKVACNVLLSKFIVGPPGSGKTTWLLSQVQDDDVIYTPTHQTMFDIVSALKVCRYSIPGASGLPFPPPARSGPWVRLIASGHVPGRVSYLDEAGYCNHLDILRLLSKTPLVCLGDLQQLHPVGFDSYCYVFDQMPQKQLTTIYRFGPNICAAIQPCYREKLESKARNTRVVFTTRPVAFGQVLTPYHKDRIGSAITIDSSQGATFDIVTLHLPSPKSLNKSRALVAITRARHGLFIYDPHNQLQEFFNLTPERTDCNLVFSRGDELVVLNADNAVTTVAKALETGPSRFRVSDPRCKSLLAACSASLEGSCMPLPQVAHNLGFYFSPDSPTFAPLPKELAPHWPVVTHQNNRAWPDRLVASMRPIDARYSKPMVGAGYVVGPSTFLGTPGVVSYYLTLYIRGEPQALPETLVSTGRIATDCREYLDAAEEEAAKELPHAFIGDVKGTTVGGCHHITSKYLPRSLPKDSVAVVGVSSPGRAAKAVCTLTDVYLPELRPYLQPETASKCWKLKLDFRDVRLMVWKGATAYFQLEGLTWSALPDYARFIQLPKDAVVYIDPCIGPATANRKVVRTTDWRADLAVTPYDYGAQNILTTAWFEDLGPQWKILGLQPFRRAFGFENTEDWAILARRMNDGKDYTDYNWNCVRERPHAIYGRARDHTYHFAPGTELQVELGKPRLPPGQVP |
| Enzyme Length | 3855 |
| Uniprot Accession Number | Q04561 |
| Absorption | |
| Active Site | ACT_SITE 76; /note="For nsp1-alpha papain-like cysteine proteinase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00872, ECO:0000269|PubMed:7769711"; ACT_SITE 146; /note="For nsp1-alpha papain-like cysteine proteinase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00872, ECO:0000269|PubMed:7769711"; ACT_SITE 276; /note="For nsp1-beta papain-like cysteine proteinase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00873, ECO:0000269|PubMed:7769711"; ACT_SITE 345; /note="For nsp1-beta papain-like cysteine proteinase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00873, ECO:0000269|PubMed:7769711"; ACT_SITE 429; /note="For nsp2 cysteine proteinase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"; ACT_SITE 498; /note="For nsp2 cysteine proteinase activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"; ACT_SITE 1732; /note="Charge relay system; for serine protease nsp4 activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00826, ECO:0000269|PubMed:19646449, ECO:0000269|PubMed:25008936"; ACT_SITE 1757; /note="Charge relay system; for serine protease nsp4 activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00826, ECO:0000269|PubMed:19646449, ECO:0000269|PubMed:25008936"; ACT_SITE 1810; /note="Charge relay system; for serine protease nsp4 activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00826, ECO:0000269|PubMed:19646449, ECO:0000269|PubMed:25008936"; ACT_SITE 3609; /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"; ACT_SITE 3624; /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"; ACT_SITE 3653; /evidence="ECO:0000255|PROSITE-ProRule:PRU01303" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; 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; 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=3.6.4.13; CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease nsp11]: Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284, ChEBI:CHEBI:173079, ChEBI:CHEBI:173080; Evidence={ECO:0000250|UniProtKB:P19811}; |
| DNA Binding | |
| EC Number | 3.4.22.-; 3.4.22.-; 3.4.22.-; 3.4.19.12; 3.4.22.-; 3.4.21.-; 2.7.7.48; 3.6.4.12; 3.6.4.13; 4.6.1.- |
| Enzyme Function | FUNCTION: [Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.; FUNCTION: [Nsp1-alpha papain-like cysteine proteinase]: Inhibits host IFN-beta production. Plays a role in the degradation of the host transcriptional activator CREBBP protein. The degradation of host CREBBP which is a key component of the IFN enhanceosome is likely responsible for the inhibition of interferon mediated by Nsp1-alpha. Participates also in the inhibition of host NF-kappa-B activation by counteracting LUBAC-dependent induction of NF-kappa-B. Reduces host NEMO ubiquitination by blocking the interaction between the two LUBAC complex components RNF31 and SHARPIN. {ECO:0000250|UniProtKB:Q9WJB2, ECO:0000269|PubMed:23287061, ECO:0000269|PubMed:27881655}.; FUNCTION: [Nsp1-beta papain-like cysteine proteinase]: Plays a role in blocking host mRNA nuclear export to the cytoplasm and subversion of host protein synthesis (PubMed:28235682). Additionally, inhibits the interferon-activated JAK/STAT signal transduction by mediating the ubiquitination and subsequent proteasomal degradation of host KPNA1. {ECO:0000250|UniProtKB:Q9WJB2, ECO:0000269|PubMed:28235682}.; FUNCTION: [Nsp2 cysteine proteinase]: Multifunctional protein that acts as a viral protease and as a viral antagonist of host immune response. Cleaves the nsp2/nsp3 site in the viral polyprotein. Displays deubiquitinating activity that cleaves both ubiquitinated and ISGylated products and therefore inhibits ubiquitin and ISG15-dependent host innate immunity. Deubiquitinates also host NFKBIA, thereby interfering with NFKBIA degradation and impairing subsequent NF-kappa-B activation. {ECO:0000250|UniProtKB:A0MD28}.; FUNCTION: [Non-structural protein 3]: Plays a role in the inhibition of the immune response by interacting with host IFITM1. This interaction leads to the proteasomal degradation of the IFN-induced antiviral protein IFITM1. {ECO:0000269|PubMed:25102331}.; FUNCTION: [Serine protease nsp4]: Cleaves the majority of cleavage sites present in the C-terminus of the polyprotein. Triggers host apoptosis through caspase-3, -8, and -9 activations. Subverts host innate immune responses through its protease activity. Targets the NF-kappa-B essential modulator NEMO and mediates its cleavage (PubMed:25008936). Blocks host interferon beta induction and downstream signaling by cleaving mitochondrial MAVS, dislodging it from the mitochondria (PubMed:27329948). Impairs host defense by cleaving host mRNA-decapping enzyme DCP1A to attenuate its antiviral activity (PubMed:30158128). {ECO:0000269|PubMed:19646449, ECO:0000269|PubMed:23936003, ECO:0000269|PubMed:25008936, ECO:0000269|PubMed:27329948, ECO:0000269|PubMed:30158128}.; FUNCTION: [Non-structural protein 5-6-7]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. {ECO:0000269|PubMed:21799305}.; FUNCTION: [Non-structural protein 5]: Plays a role in the inhibition of host STAT3 signaling pathway by inducing the degradation of STAT3. {ECO:0000269|PubMed:27881658}.; FUNCTION: [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000269|PubMed:25449571}.; FUNCTION: [Helicase nsp10]: Displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000269|PubMed:12127789}.; FUNCTION: [Uridylate-specific endoribonuclease nsp11]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, PKR (By similarity) and NLRP3 inflammasome (PubMed:26398903). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). Plays also a role in the inhibition of host type I interferon production by recruiting host OTULIN to promote removal of linear ubiquitination targeting host NEMO (PubMed:29444948). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P19811, ECO:0000269|PubMed:26398903, ECO:0000269|PubMed:29444948}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 3186..3193; /note=ATP; /evidence=ECO:0000250 |
| Features | Active site (12); Alternative sequence (1); Chain (17); Compositional bias (1); Domain (11); Erroneous initiation (2); Metal binding (12); Mutagenesis (17); Nucleotide binding (1); Region (9); Sequence conflict (2); Site (13); Transmembrane (12); Zinc finger (1) |
| Keywords | ATP-binding;Activation of host autophagy by virus;Endonuclease;Helicase;Host cytoplasm;Host endoplasmic reticulum;Host membrane;Host nucleus;Host-virus interaction;Hydrolase;Inhibition of host ISG15 by virus;Inhibition of host NF-kappa-B by virus;Inhibition of host STAT1 by virus;Inhibition of host innate immune response by virus;Inhibition of host interferon signaling pathway by virus;Lyase;Membrane;Metal-binding;Modulation of host ubiquitin pathway by viral deubiquitinase;Modulation of host ubiquitin pathway by virus;Multifunctional enzyme;Nuclease;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-directed RNA polymerase;Reference proteome;Ribosomal frameshifting;Serine protease;Thiol protease;Transferase;Transmembrane;Transmembrane helix;Viral RNA replication;Viral immunoevasion;Zinc;Zinc-finger |
| Interact With | A0A068CA64; A5D9M6 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Nsp1]: Host nucleus {ECO:0000269|PubMed:23287061}. Host cytoplasm {ECO:0000269|PubMed:23287061}.; SUBCELLULAR LOCATION: [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000269|PubMed:23287061, ECO:0000269|PubMed:28235682}. Host cytoplasm {ECO:0000269|PubMed:23287061, ECO:0000269|PubMed:28235682}.; SUBCELLULAR LOCATION: [Nsp1-beta papain-like cysteine proteinase]: Host nucleus {ECO:0000269|PubMed:23287061, ECO:0000269|PubMed:28235682}.; SUBCELLULAR LOCATION: [Nsp2 cysteine proteinase]: Host cytoplasm {ECO:0000269|PubMed:28648849}. Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 5-6-7]: Host endoplasmic reticulum {ECO:0000269|PubMed:21799305}. Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Serine protease nsp4]: Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000269|PubMed:25449571}. Host cytoplasm, host perinuclear region {ECO:0000305}.; SUBCELLULAR LOCATION: [Helicase nsp10]: Host cytoplasm {ECO:0000269|PubMed:28648849}. Host cytoplasm, host perinuclear region {ECO:0000305}.; SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease nsp11]: Host cytoplasm {ECO:0000269|PubMed:29444948}. Host nucleus {ECO:0000269|PubMed:29444948}.; SUBCELLULAR LOCATION: [Non-structural protein 12]: Host cytoplasm {ECO:0000269|PubMed:29920289}. |
| Modified Residue | |
| Post Translational Modification | PTM: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. Nsp1 is autocleaved into two subunits, Nsp1-alpha and Nsp1-beta. There are two alternative pathways for processing. Either nsp4-5 is cleaved, which represents the major pathway or the nsp5-6 and nsp6-7 are processed, which represents the minor pathway. The major pathway occurs when nsp2 acts as cofactor for nsp4 (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 421,332 |
| Kinetics | |
| Metal Binding | METAL 3044; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00985; METAL 3047; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00985; METAL 3057; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00985; METAL 3062; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00985; METAL 3065; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00985; METAL 3067; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00985; METAL 3069; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00985; METAL 3071; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00985; METAL 3078; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00985; METAL 3080; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00985; METAL 3087; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00985; METAL 3090; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00985 |
| Rhea ID | RHEA:21248; RHEA:13065; RHEA:67732 |
| Cross Reference Brenda |