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Pr110 [Mouse mammary tumor virus]
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
Gag_p24 | pfam00607 | gag protein p24 N-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA ... |
284-409 | 3.96e-45 | |||
gag protein p24 N-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro. : Pssm-ID: 459864 Cd Length: 128 Bit Score: 158.21 E-value: 3.96e-45
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RVP | pfam00077 | Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ... |
751-849 | 2.08e-39 | |||
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026). : Pssm-ID: 425454 Cd Length: 101 Bit Score: 140.97 E-value: 2.08e-39
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Gag_p10 | pfam02337 | Retroviral GAG p10 protein; This family consists of various retroviral GAG (core) polyproteins ... |
8-92 | 1.19e-38 | |||
Retroviral GAG p10 protein; This family consists of various retroviral GAG (core) polyproteins and encompasses the p10 region producing the p10 protein upon proteolytic cleavage of GAG by retroviral protease. The p10 or matrix protein (MA) is associated with the virus envelope glycoproteins in most mammalian retroviruses and may be involved in virus particle assembly, transport and budding. Some of the GAG polyproteins have alternate cleavage sites leading to the production of alternative and longer cleavage products (e.g. p19) the alignment of this family only covers the approximately N-terminal (GAG) 100 amino acid region of homology to p10. : Pssm-ID: 426727 Cd Length: 85 Bit Score: 138.25 E-value: 1.19e-38
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dUTPase | pfam00692 | dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate. |
619-741 | 1.00e-35 | |||
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate. : Pssm-ID: 395562 [Multi-domain] Cd Length: 129 Bit Score: 131.64 E-value: 1.00e-35
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Gag_p24_C | pfam19317 | Gag protein p24 C-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA ... |
409-482 | 1.19e-34 | |||
Gag protein p24 C-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro. : Pssm-ID: 466038 Cd Length: 74 Bit Score: 126.44 E-value: 1.19e-34
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zf-CCHC_5 | pfam14787 | GAG-polyprotein viral zinc-finger; |
550-584 | 2.04e-16 | |||
GAG-polyprotein viral zinc-finger; : Pssm-ID: 373297 Cd Length: 36 Bit Score: 73.36 E-value: 2.04e-16
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AIR1 super family | cl34894 | Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ... |
525-567 | 1.89e-05 | |||
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion]; The actual alignment was detected with superfamily member COG5082: Pssm-ID: 227414 [Multi-domain] Cd Length: 190 Bit Score: 46.38 E-value: 1.89e-05
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Name | Accession | Description | Interval | E-value | |||
Gag_p24 | pfam00607 | gag protein p24 N-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA ... |
284-409 | 3.96e-45 | |||
gag protein p24 N-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro. Pssm-ID: 459864 Cd Length: 128 Bit Score: 158.21 E-value: 3.96e-45
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RVP | pfam00077 | Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ... |
751-849 | 2.08e-39 | |||
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026). Pssm-ID: 425454 Cd Length: 101 Bit Score: 140.97 E-value: 2.08e-39
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Gag_p10 | pfam02337 | Retroviral GAG p10 protein; This family consists of various retroviral GAG (core) polyproteins ... |
8-92 | 1.19e-38 | |||
Retroviral GAG p10 protein; This family consists of various retroviral GAG (core) polyproteins and encompasses the p10 region producing the p10 protein upon proteolytic cleavage of GAG by retroviral protease. The p10 or matrix protein (MA) is associated with the virus envelope glycoproteins in most mammalian retroviruses and may be involved in virus particle assembly, transport and budding. Some of the GAG polyproteins have alternate cleavage sites leading to the production of alternative and longer cleavage products (e.g. p19) the alignment of this family only covers the approximately N-terminal (GAG) 100 amino acid region of homology to p10. Pssm-ID: 426727 Cd Length: 85 Bit Score: 138.25 E-value: 1.19e-38
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dUTPase | pfam00692 | dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate. |
619-741 | 1.00e-35 | |||
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate. Pssm-ID: 395562 [Multi-domain] Cd Length: 129 Bit Score: 131.64 E-value: 1.00e-35
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Gag_p24_C | pfam19317 | Gag protein p24 C-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA ... |
409-482 | 1.19e-34 | |||
Gag protein p24 C-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro. Pssm-ID: 466038 Cd Length: 74 Bit Score: 126.44 E-value: 1.19e-34
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HIV_retropepsin_like | cd05482 | Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family ... |
757-842 | 2.71e-31 | |||
Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A. Pssm-ID: 133149 Cd Length: 87 Bit Score: 117.37 E-value: 2.71e-31
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dut | TIGR00576 | deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ... |
611-741 | 7.07e-23 | |||
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is in maintaining the levels of dUTP in the cell to prevent dUTP incorporation into DNA during DNA replication. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism] Pssm-ID: 273149 [Multi-domain] Cd Length: 142 Bit Score: 95.38 E-value: 7.07e-23
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Dut | COG0756 | dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ... |
611-741 | 1.05e-22 | |||
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis Pssm-ID: 440519 [Multi-domain] Cd Length: 143 Bit Score: 94.70 E-value: 1.05e-22
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dut | PRK00601 | dUTP diphosphatase; |
621-741 | 3.19e-20 | |||
dUTP diphosphatase; Pssm-ID: 234802 [Multi-domain] Cd Length: 150 Bit Score: 87.91 E-value: 3.19e-20
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trimeric_dUTPase | cd07557 | Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ... |
631-715 | 9.90e-19 | |||
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface. Pssm-ID: 143638 [Multi-domain] Cd Length: 92 Bit Score: 81.77 E-value: 9.90e-19
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zf-CCHC_5 | pfam14787 | GAG-polyprotein viral zinc-finger; |
550-584 | 2.04e-16 | |||
GAG-polyprotein viral zinc-finger; Pssm-ID: 373297 Cd Length: 36 Bit Score: 73.36 E-value: 2.04e-16
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AIR1 | COG5082 | Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ... |
525-567 | 1.89e-05 | |||
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion]; Pssm-ID: 227414 [Multi-domain] Cd Length: 190 Bit Score: 46.38 E-value: 1.89e-05
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IgV_L_lambda | cd04984 | Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ... |
733-765 | 4.41e-04 | |||
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409373 Cd Length: 105 Bit Score: 40.52 E-value: 4.41e-04
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ZnF_C2HC | smart00343 | zinc finger; |
526-541 | 5.71e-04 | |||
zinc finger; Pssm-ID: 197667 [Multi-domain] Cd Length: 17 Bit Score: 37.81 E-value: 5.71e-04
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PTZ00368 | PTZ00368 | universal minicircle sequence binding protein (UMSBP); Provisional |
527-570 | 6.88e-04 | |||
universal minicircle sequence binding protein (UMSBP); Provisional Pssm-ID: 173561 [Multi-domain] Cd Length: 148 Bit Score: 40.95 E-value: 6.88e-04
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zf-CCHC | pfam00098 | Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ... |
525-541 | 1.50e-03 | |||
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger. Pssm-ID: 395050 [Multi-domain] Cd Length: 18 Bit Score: 36.74 E-value: 1.50e-03
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Name | Accession | Description | Interval | E-value | |||
Gag_p24 | pfam00607 | gag protein p24 N-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA ... |
284-409 | 3.96e-45 | |||
gag protein p24 N-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro. Pssm-ID: 459864 Cd Length: 128 Bit Score: 158.21 E-value: 3.96e-45
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RVP | pfam00077 | Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ... |
751-849 | 2.08e-39 | |||
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026). Pssm-ID: 425454 Cd Length: 101 Bit Score: 140.97 E-value: 2.08e-39
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Gag_p10 | pfam02337 | Retroviral GAG p10 protein; This family consists of various retroviral GAG (core) polyproteins ... |
8-92 | 1.19e-38 | |||
Retroviral GAG p10 protein; This family consists of various retroviral GAG (core) polyproteins and encompasses the p10 region producing the p10 protein upon proteolytic cleavage of GAG by retroviral protease. The p10 or matrix protein (MA) is associated with the virus envelope glycoproteins in most mammalian retroviruses and may be involved in virus particle assembly, transport and budding. Some of the GAG polyproteins have alternate cleavage sites leading to the production of alternative and longer cleavage products (e.g. p19) the alignment of this family only covers the approximately N-terminal (GAG) 100 amino acid region of homology to p10. Pssm-ID: 426727 Cd Length: 85 Bit Score: 138.25 E-value: 1.19e-38
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dUTPase | pfam00692 | dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate. |
619-741 | 1.00e-35 | |||
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate. Pssm-ID: 395562 [Multi-domain] Cd Length: 129 Bit Score: 131.64 E-value: 1.00e-35
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Gag_p24_C | pfam19317 | Gag protein p24 C-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA ... |
409-482 | 1.19e-34 | |||
Gag protein p24 C-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro. Pssm-ID: 466038 Cd Length: 74 Bit Score: 126.44 E-value: 1.19e-34
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HIV_retropepsin_like | cd05482 | Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family ... |
757-842 | 2.71e-31 | |||
Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A. Pssm-ID: 133149 Cd Length: 87 Bit Score: 117.37 E-value: 2.71e-31
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dut | TIGR00576 | deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ... |
611-741 | 7.07e-23 | |||
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is in maintaining the levels of dUTP in the cell to prevent dUTP incorporation into DNA during DNA replication. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism] Pssm-ID: 273149 [Multi-domain] Cd Length: 142 Bit Score: 95.38 E-value: 7.07e-23
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Dut | COG0756 | dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ... |
611-741 | 1.05e-22 | |||
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis Pssm-ID: 440519 [Multi-domain] Cd Length: 143 Bit Score: 94.70 E-value: 1.05e-22
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dut | PRK00601 | dUTP diphosphatase; |
621-741 | 3.19e-20 | |||
dUTP diphosphatase; Pssm-ID: 234802 [Multi-domain] Cd Length: 150 Bit Score: 87.91 E-value: 3.19e-20
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trimeric_dUTPase | cd07557 | Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ... |
631-715 | 9.90e-19 | |||
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface. Pssm-ID: 143638 [Multi-domain] Cd Length: 92 Bit Score: 81.77 E-value: 9.90e-19
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zf-CCHC_5 | pfam14787 | GAG-polyprotein viral zinc-finger; |
550-584 | 2.04e-16 | |||
GAG-polyprotein viral zinc-finger; Pssm-ID: 373297 Cd Length: 36 Bit Score: 73.36 E-value: 2.04e-16
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PLN02547 | PLN02547 | dUTP pyrophosphatase |
623-741 | 1.17e-13 | |||
dUTP pyrophosphatase Pssm-ID: 215302 Cd Length: 157 Bit Score: 69.44 E-value: 1.17e-13
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PHA03094 | PHA03094 | dUTPase; Provisional |
625-741 | 7.01e-11 | |||
dUTPase; Provisional Pssm-ID: 165376 [Multi-domain] Cd Length: 144 Bit Score: 60.93 E-value: 7.01e-11
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PHA02703 | PHA02703 | ORF007 dUTPase; Provisional |
625-741 | 3.56e-10 | |||
ORF007 dUTPase; Provisional Pssm-ID: 165079 Cd Length: 165 Bit Score: 59.61 E-value: 3.56e-10
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dut | PRK13956 | dUTP diphosphatase; |
623-743 | 2.51e-07 | |||
dUTP diphosphatase; Pssm-ID: 184417 [Multi-domain] Cd Length: 147 Bit Score: 50.95 E-value: 2.51e-07
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PTZ00143 | PTZ00143 | deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional |
628-742 | 1.52e-05 | |||
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional Pssm-ID: 240288 [Multi-domain] Cd Length: 155 Bit Score: 45.88 E-value: 1.52e-05
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AIR1 | COG5082 | Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ... |
525-567 | 1.89e-05 | |||
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion]; Pssm-ID: 227414 [Multi-domain] Cd Length: 190 Bit Score: 46.38 E-value: 1.89e-05
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IgV_L_lambda | cd04984 | Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ... |
733-765 | 4.41e-04 | |||
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology. Pssm-ID: 409373 Cd Length: 105 Bit Score: 40.52 E-value: 4.41e-04
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ZnF_C2HC | smart00343 | zinc finger; |
526-541 | 5.71e-04 | |||
zinc finger; Pssm-ID: 197667 [Multi-domain] Cd Length: 17 Bit Score: 37.81 E-value: 5.71e-04
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AIR1 | COG5082 | Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ... |
526-569 | 6.33e-04 | |||
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion]; Pssm-ID: 227414 [Multi-domain] Cd Length: 190 Bit Score: 41.76 E-value: 6.33e-04
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PTZ00368 | PTZ00368 | universal minicircle sequence binding protein (UMSBP); Provisional |
527-570 | 6.88e-04 | |||
universal minicircle sequence binding protein (UMSBP); Provisional Pssm-ID: 173561 [Multi-domain] Cd Length: 148 Bit Score: 40.95 E-value: 6.88e-04
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zf-CCHC | pfam00098 | Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ... |
525-541 | 1.50e-03 | |||
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger. Pssm-ID: 395050 [Multi-domain] Cd Length: 18 Bit Score: 36.74 E-value: 1.50e-03
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dCTP_deam | TIGR02274 | deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ... |
651-715 | 1.64e-03 | |||
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli monofunctional deoxycytidine triphosphate deaminase (dCTP deaminase) and a Methanocaldococcus jannaschii bifunctional dCTP deaminase (3.5.4.13)/dUTP diphosphatase (EC 3.6.1.23), which has the EC number 3.5.4.30 for the overall operation. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism] Pssm-ID: 274062 Cd Length: 179 Bit Score: 40.38 E-value: 1.64e-03
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CE4_SpCDA1 | cd10980 | Putative catalytic domain of Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), and ... |
248-355 | 7.78e-03 | |||
Putative catalytic domain of Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), and similar proteins; This family is represented by Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), encoded by the cda1 gene. The general function of chitin deacetylase (CDA) is the synthesis of chitosan from chitin, a polymer of N-acetyl glucosamine, to build up the proper ascospore wall. The actual function of SpCDA1 might be involved in allantoin hydrolysis. It is likely an ortholog to bacterial PuuE allantoinase, whereas it is more distantly related to the CDAs found in other fungi, such as Saccharomyces cerevisiae and Mucor rouxii. Those CDAs are similar with rizobial NodB protein and are not included in this family. Pssm-ID: 200602 [Multi-domain] Cd Length: 297 Bit Score: 39.45 E-value: 7.78e-03
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Blast search parameters | ||||
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