mitochondrial topoisomerase I [Danio rerio]
Protein Classification
Topoisomer_IB_N_htopoI_like and Topo_IB_C domain-containing protein( domain architecture ID 11556523)
Topoisomer_IB_N_htopoI_like and Topo_IB_C domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| TOPEUc | smart00435 | DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
196-571 | 0e+00 | ||||||
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras : Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 581.62 E-value: 0e+00
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| Topoisomer_IB_N_htopoI_like | cd03488 | Topoisomer_IB_N_htopoI_like : N-terminal DNA binding fragment found in eukaryotic DNA ... |
52-266 | 5.25e-143 | ||||||
Topoisomer_IB_N_htopoI_like : N-terminal DNA binding fragment found in eukaryotic DNA topoisomerase (topo) IB proteins similar to the monomeric yeast and human topo I. Topo I enzymes are divided into: topo type IA (bacterial) and type IB (eukaryotic). Topo I relaxes superhelical tension in duplex DNA by creating a single-strand nick, the broken strand can then rotate around the unbroken strand to remove DNA supercoils and, the nick is religated, liberating topo I. These enzymes regulate the topological changes that accompany DNA replication, transcription and other nuclear processes. Human topo I is the target of a diverse set of anticancer drugs including camptothecins (CPTs). CPTs bind to the topo I-DNA complex and inhibit religation of the single-strand nick, resulting in the accumulation of topo I-DNA adducts. This family may represent more than one structural domain. : Pssm-ID: 239570 Cd Length: 215 Bit Score: 412.89 E-value: 5.25e-143
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| Name | Accession | Description | Interval | E-value | ||||||
| TOPEUc | smart00435 | DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
196-571 | 0e+00 | ||||||
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 581.62 E-value: 0e+00
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| Topoisomer_IB_N_htopoI_like | cd03488 | Topoisomer_IB_N_htopoI_like : N-terminal DNA binding fragment found in eukaryotic DNA ... |
52-266 | 5.25e-143 | ||||||
Topoisomer_IB_N_htopoI_like : N-terminal DNA binding fragment found in eukaryotic DNA topoisomerase (topo) IB proteins similar to the monomeric yeast and human topo I. Topo I enzymes are divided into: topo type IA (bacterial) and type IB (eukaryotic). Topo I relaxes superhelical tension in duplex DNA by creating a single-strand nick, the broken strand can then rotate around the unbroken strand to remove DNA supercoils and, the nick is religated, liberating topo I. These enzymes regulate the topological changes that accompany DNA replication, transcription and other nuclear processes. Human topo I is the target of a diverse set of anticancer drugs including camptothecins (CPTs). CPTs bind to the topo I-DNA complex and inhibit religation of the single-strand nick, resulting in the accumulation of topo I-DNA adducts. This family may represent more than one structural domain. Pssm-ID: 239570 Cd Length: 215 Bit Score: 412.89 E-value: 5.25e-143
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| Topoisom_I_N | pfam02919 | Eukaryotic DNA topoisomerase I, DNA binding fragment; Topoisomerase I promotes the relaxation ... |
51-265 | 3.84e-139 | ||||||
Eukaryotic DNA topoisomerase I, DNA binding fragment; Topoisomerase I promotes the relaxation of DNA superhelical tension by introducing a transient single-stranded break in duplex DNA and are vital for the processes of replication, transcription, and recombination. This family may be more than one structural domain. Pssm-ID: 460746 Cd Length: 213 Bit Score: 403.01 E-value: 3.84e-139
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| Topoisom_I | pfam01028 | Eukaryotic DNA topoisomerase I, catalytic core; Topoisomerase I promotes the relaxation of DNA ... |
268-470 | 7.38e-123 | ||||||
Eukaryotic DNA topoisomerase I, catalytic core; Topoisomerase I promotes the relaxation of DNA superhelical tension by introducing a transient single-stranded break in duplex DNA and are vital for the processes of replication, transcription, and recombination. Pssm-ID: 460030 [Multi-domain] Cd Length: 198 Bit Score: 360.68 E-value: 7.38e-123
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| Topo_IB_C | cd00659 | DNA topoisomerase IB, C-terminal catalytic domain; Topoisomerase I promotes the relaxation of ... |
274-473 | 4.61e-78 | ||||||
DNA topoisomerase IB, C-terminal catalytic domain; Topoisomerase I promotes the relaxation of both positive and negative DNA superhelical tension by introducing a transient single-stranded break in duplex DNA. This function is vital for the processes of replication, transcription, and recombination. Unlike Topo IA enzymes, Topo IB enzymes do not require a single-stranded region of DNA or metal ions for their function. The type IB family of DNA topoisomerases includes eukaryotic nuclear topoisomerase I, topoisomerases of poxviruses, and bacterial versions of Topo IB. They belong to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their C-terminal catalytic domain and the overall reaction mechanism with tyrosine recombinases. The C-terminal catalytic domain in topoisomerases is linked to a divergent N-terminal domain that shows no sequence or structure similarity to the N-terminal domains of tyrosine recombinases. Pssm-ID: 271176 [Multi-domain] Cd Length: 210 Bit Score: 246.03 E-value: 4.61e-78
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| gimC_beta | TIGR02338 | prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular ... |
477-548 | 9.90e-03 | ||||||
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related. Pssm-ID: 131391 [Multi-domain] Cd Length: 110 Bit Score: 36.17 E-value: 9.90e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| TOPEUc | smart00435 | DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
196-571 | 0e+00 | ||||||
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 581.62 E-value: 0e+00
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| Topoisomer_IB_N_htopoI_like | cd03488 | Topoisomer_IB_N_htopoI_like : N-terminal DNA binding fragment found in eukaryotic DNA ... |
52-266 | 5.25e-143 | ||||||
Topoisomer_IB_N_htopoI_like : N-terminal DNA binding fragment found in eukaryotic DNA topoisomerase (topo) IB proteins similar to the monomeric yeast and human topo I. Topo I enzymes are divided into: topo type IA (bacterial) and type IB (eukaryotic). Topo I relaxes superhelical tension in duplex DNA by creating a single-strand nick, the broken strand can then rotate around the unbroken strand to remove DNA supercoils and, the nick is religated, liberating topo I. These enzymes regulate the topological changes that accompany DNA replication, transcription and other nuclear processes. Human topo I is the target of a diverse set of anticancer drugs including camptothecins (CPTs). CPTs bind to the topo I-DNA complex and inhibit religation of the single-strand nick, resulting in the accumulation of topo I-DNA adducts. This family may represent more than one structural domain. Pssm-ID: 239570 Cd Length: 215 Bit Score: 412.89 E-value: 5.25e-143
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| Topoisom_I_N | pfam02919 | Eukaryotic DNA topoisomerase I, DNA binding fragment; Topoisomerase I promotes the relaxation ... |
51-265 | 3.84e-139 | ||||||
Eukaryotic DNA topoisomerase I, DNA binding fragment; Topoisomerase I promotes the relaxation of DNA superhelical tension by introducing a transient single-stranded break in duplex DNA and are vital for the processes of replication, transcription, and recombination. This family may be more than one structural domain. Pssm-ID: 460746 Cd Length: 213 Bit Score: 403.01 E-value: 3.84e-139
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| Topoisomer_IB_N | cd00660 | Topoisomer_IB_N: N-terminal DNA binding fragment found in eukaryotic DNA topoisomerase (topo) ... |
52-266 | 9.85e-138 | ||||||
Topoisomer_IB_N: N-terminal DNA binding fragment found in eukaryotic DNA topoisomerase (topo) IB proteins similar to the monomeric yeast and human topo I and heterodimeric topo I from Leishmania donvanni. Topo I enzymes are divided into: topo type IA (bacterial) and type IB (eukaryotic). Topo I relaxes superhelical tension in duplex DNA by creating a single-strand nick, the broken strand can then rotate around the unbroken strand to remove DNA supercoils and, the nick is religated, liberating topo I. These enzymes regulate the topological changes that accompany DNA replication, transcription and other nuclear processes. Human topo I is the target of a diverse set of anticancer drugs including camptothecins (CPTs). CPTs bind to the topo I-DNA complex and inhibit re-ligation of the single-strand nick, resulting in the accumulation of topo I-DNA adducts. In addition to differences in structure and some biochemical properties, Trypanosomatid parasite topo I differ from human topo I in their sensitivity to CPTs and other classical topo I inhibitors. Trypanosomatid topos I play putative roles in organizing the kinetoplast DNA network unique to these parasites. This family may represent more than one structural domain. Pssm-ID: 238356 Cd Length: 215 Bit Score: 399.33 E-value: 9.85e-138
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| Topoisom_I | pfam01028 | Eukaryotic DNA topoisomerase I, catalytic core; Topoisomerase I promotes the relaxation of DNA ... |
268-470 | 7.38e-123 | ||||||
Eukaryotic DNA topoisomerase I, catalytic core; Topoisomerase I promotes the relaxation of DNA superhelical tension by introducing a transient single-stranded break in duplex DNA and are vital for the processes of replication, transcription, and recombination. Pssm-ID: 460030 [Multi-domain] Cd Length: 198 Bit Score: 360.68 E-value: 7.38e-123
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| Topoisomer_IB_N_LdtopoI_like | cd03489 | Topoisomer_IB_N_LdtopoI_like: N-terminal DNA binding fragment found in eukaryotic DNA ... |
52-265 | 4.27e-79 | ||||||
Topoisomer_IB_N_LdtopoI_like: N-terminal DNA binding fragment found in eukaryotic DNA topoisomerase (topo) IB proteins similar to the heterodimeric topo I from Leishmania donvanni. Topo I enzymes are divided into: topo type IA (bacterial) and type IB (eukaryotic). Topo I relaxes superhelical tension in duplex DNA by creating a single-strand nick, the broken strand can then rotate around the unbroken strand to remove DNA supercoils and, the nick is religated, liberating topo I. These enzymes regulate the topological changes that accompany DNA replication, transcription and other nuclear processes. Human topo I is the target of a diverse set of anticancer drugs including camptothecins (CPTs). CPTs bind to the topo I-DNA complex and inhibit re-ligation of the single-strand nick, resulting in the accumulation of topo I-DNA adducts. In addition to differences in structure and some biochemical properties, Trypanosomatid parasite topo I differ from human topo I in their sensitivity to CPTs and other classical topo I inhibitors. Trypanosomatid topo I play putative roles in organizing the kinetoplast DNA network unique to these parasites. This family may represent more than one structural domain. Pssm-ID: 239571 Cd Length: 212 Bit Score: 248.64 E-value: 4.27e-79
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| Topo_IB_C | cd00659 | DNA topoisomerase IB, C-terminal catalytic domain; Topoisomerase I promotes the relaxation of ... |
274-473 | 4.61e-78 | ||||||
DNA topoisomerase IB, C-terminal catalytic domain; Topoisomerase I promotes the relaxation of both positive and negative DNA superhelical tension by introducing a transient single-stranded break in duplex DNA. This function is vital for the processes of replication, transcription, and recombination. Unlike Topo IA enzymes, Topo IB enzymes do not require a single-stranded region of DNA or metal ions for their function. The type IB family of DNA topoisomerases includes eukaryotic nuclear topoisomerase I, topoisomerases of poxviruses, and bacterial versions of Topo IB. They belong to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their C-terminal catalytic domain and the overall reaction mechanism with tyrosine recombinases. The C-terminal catalytic domain in topoisomerases is linked to a divergent N-terminal domain that shows no sequence or structure similarity to the N-terminal domains of tyrosine recombinases. Pssm-ID: 271176 [Multi-domain] Cd Length: 210 Bit Score: 246.03 E-value: 4.61e-78
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| Topoisomer_IB_N_1 | cd03490 | Topoisomer_IB_N_1: A subgroup of the N-terminal DNA binding fragment found in eukaryotic DNA ... |
52-266 | 1.57e-62 | ||||||
Topoisomer_IB_N_1: A subgroup of the N-terminal DNA binding fragment found in eukaryotic DNA topoisomerase (topo) IB. Topo IB proteins include the monomeric yeast and human topo I and heterodimeric topo I from Leishmania donvanni. Topo I enzymes are divided into: topo type IA (bacterial) and type IB (eukaryotic). Topo I relaxes superhelical tension in duplex DNA by creating a single-strand nick, the broken strand can then rotate around the unbroken strand to remove DNA supercoils and, the nick is religated, liberating topo I. These enzymes regulate the topological changes that accompany DNA replication, transcription and other nuclear processes. Human topo I is the target of a diverse set of anticancer drugs including camptothecins (CPTs). CPTs bind to the topo I-DNA complex and inhibit religation of the single-strand nick, resulting in the accumulation of topo I-DNA adducts. In addition to differences in structure and some biochemical properties, Trypanosomatid parasite topos I differ from human topo I in their sensitivity to CPTs and other classical topo I inhibitors. Trypanosomatid topos I have putative roles in organizing the kinetoplast DNA network unique to these parasites. This family may represent more than one structural domain. Pssm-ID: 239572 Cd Length: 217 Bit Score: 205.52 E-value: 1.57e-62
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| Topo_C_assoc | pfam14370 | C-terminal topoisomerase domain; This domain is found at the C-terminal of topoisomerase and ... |
531-598 | 3.41e-34 | ||||||
C-terminal topoisomerase domain; This domain is found at the C-terminal of topoisomerase and other similar enzymes. Pssm-ID: 464154 [Multi-domain] Cd Length: 68 Bit Score: 123.83 E-value: 3.41e-34
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| MAT1 | pfam06391 | CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
448-543 | 4.04e-03 | ||||||
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger. Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 38.76 E-value: 4.04e-03
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| gimC_beta | TIGR02338 | prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular ... |
477-548 | 9.90e-03 | ||||||
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related. Pssm-ID: 131391 [Multi-domain] Cd Length: 110 Bit Score: 36.17 E-value: 9.90e-03
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