transcript cleavage factor [Escherichia coli O157:H7 str. Sakai]
transcription elongation factor GreA( domain architecture ID 11478349)
transcription elongation factor GreA induces cleavage of the nascent transcript to allow the resumption of elongation from the new 3' terminus; releases sequences of 2 to 3 nucleotides
List of domain hits
Name | Accession | Description | Interval | E-value | |||
greA | PRK00226 | transcription elongation factor GreA; Reviewed |
1-157 | 1.04e-92 | |||
transcription elongation factor GreA; Reviewed : Pssm-ID: 234693 [Multi-domain] Cd Length: 157 Bit Score: 265.43 E-value: 1.04e-92
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Name | Accession | Description | Interval | E-value | |||
greA | PRK00226 | transcription elongation factor GreA; Reviewed |
1-157 | 1.04e-92 | |||
transcription elongation factor GreA; Reviewed Pssm-ID: 234693 [Multi-domain] Cd Length: 157 Bit Score: 265.43 E-value: 1.04e-92
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GreA | COG0782 | Transcription elongation factor, GreA/GreB family [Transcription]; |
1-156 | 4.52e-81 | |||
Transcription elongation factor, GreA/GreB family [Transcription]; Pssm-ID: 440545 [Multi-domain] Cd Length: 156 Bit Score: 236.18 E-value: 4.52e-81
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greA | TIGR01462 | transcription elongation factor GreA; The GreA and GreB transcription elongation factors ... |
5-156 | 6.92e-76 | |||
transcription elongation factor GreA; The GreA and GreB transcription elongation factors enable to continuation of RNA transcription past template-encoded arresting sites. Among the Proteobacteria, distinct clades of GreA and GreB are found. GreA differs functionally in that it releases smaller oligonucleotides. Because members of the family outside the Proteobacteria resemble GreA more closely than GreB, the GreB clade (TIGR01461) forms a plausible outgroup and the remainder of the GreA/B family, included in this model, is designated GreA. In the Chlamydias and some spirochetes, the region described by this model is found as the C-terminal region of a much larger protein. [Transcription, Transcription factors] Pssm-ID: 273638 [Multi-domain] Cd Length: 151 Bit Score: 222.88 E-value: 6.92e-76
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GreA_GreB_N | pfam03449 | Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure. |
4-74 | 5.35e-35 | |||
Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure. Pssm-ID: 460920 [Multi-domain] Cd Length: 71 Bit Score: 116.71 E-value: 5.35e-35
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Name | Accession | Description | Interval | E-value | |||
greA | PRK00226 | transcription elongation factor GreA; Reviewed |
1-157 | 1.04e-92 | |||
transcription elongation factor GreA; Reviewed Pssm-ID: 234693 [Multi-domain] Cd Length: 157 Bit Score: 265.43 E-value: 1.04e-92
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GreA | COG0782 | Transcription elongation factor, GreA/GreB family [Transcription]; |
1-156 | 4.52e-81 | |||
Transcription elongation factor, GreA/GreB family [Transcription]; Pssm-ID: 440545 [Multi-domain] Cd Length: 156 Bit Score: 236.18 E-value: 4.52e-81
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greA | TIGR01462 | transcription elongation factor GreA; The GreA and GreB transcription elongation factors ... |
5-156 | 6.92e-76 | |||
transcription elongation factor GreA; The GreA and GreB transcription elongation factors enable to continuation of RNA transcription past template-encoded arresting sites. Among the Proteobacteria, distinct clades of GreA and GreB are found. GreA differs functionally in that it releases smaller oligonucleotides. Because members of the family outside the Proteobacteria resemble GreA more closely than GreB, the GreB clade (TIGR01461) forms a plausible outgroup and the remainder of the GreA/B family, included in this model, is designated GreA. In the Chlamydias and some spirochetes, the region described by this model is found as the C-terminal region of a much larger protein. [Transcription, Transcription factors] Pssm-ID: 273638 [Multi-domain] Cd Length: 151 Bit Score: 222.88 E-value: 6.92e-76
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greB | PRK01885 | transcription elongation factor GreB; Reviewed |
6-157 | 4.15e-45 | |||
transcription elongation factor GreB; Reviewed Pssm-ID: 179345 [Multi-domain] Cd Length: 157 Bit Score: 144.99 E-value: 4.15e-45
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GreA_GreB_N | pfam03449 | Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure. |
4-74 | 5.35e-35 | |||
Transcription elongation factor, N-terminal; This domain adopts a long alpha-hairpin structure. Pssm-ID: 460920 [Multi-domain] Cd Length: 71 Bit Score: 116.71 E-value: 5.35e-35
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GreA_GreB | pfam01272 | Transcription elongation factor, GreA/GreB, C-term; This domain has an FKBP-like fold. |
83-157 | 7.15e-34 | |||
Transcription elongation factor, GreA/GreB, C-term; This domain has an FKBP-like fold. Pssm-ID: 426171 [Multi-domain] Cd Length: 77 Bit Score: 113.77 E-value: 7.15e-34
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PRK14720 | PRK14720 | transcription elongation factor GreA; |
7-156 | 1.76e-31 | |||
transcription elongation factor GreA; Pssm-ID: 184804 [Multi-domain] Cd Length: 906 Bit Score: 118.33 E-value: 1.76e-31
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PRK06342 | PRK06342 | transcription elongation factor GreA; |
31-153 | 2.04e-16 | |||
transcription elongation factor GreA; Pssm-ID: 180535 [Multi-domain] Cd Length: 160 Bit Score: 71.67 E-value: 2.04e-16
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PRK06330 | PRK06330 | transcript cleavage factor/unknown domain fusion protein; Validated |
7-142 | 4.29e-10 | |||
transcript cleavage factor/unknown domain fusion protein; Validated Pssm-ID: 235780 [Multi-domain] Cd Length: 718 Bit Score: 57.07 E-value: 4.29e-10
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PRK05753 | PRK05753 | nucleoside diphosphate kinase regulator; Provisional |
66-157 | 4.27e-08 | |||
nucleoside diphosphate kinase regulator; Provisional Pssm-ID: 180236 [Multi-domain] Cd Length: 137 Bit Score: 49.18 E-value: 4.27e-08
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PRK05892 | PRK05892 | nucleoside diphosphate kinase regulator; Provisional |
14-155 | 8.11e-07 | |||
nucleoside diphosphate kinase regulator; Provisional Pssm-ID: 180307 [Multi-domain] Cd Length: 158 Bit Score: 45.92 E-value: 8.11e-07
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DDR_swiveling | pfam18427 | DD-reactivating factor swiveling domain; AdoCbl-dependent diol dehydratase (DD) (EC 4.2.1.28) ... |
93-148 | 9.76e-04 | |||
DD-reactivating factor swiveling domain; AdoCbl-dependent diol dehydratase (DD) (EC 4.2.1.28) is one of the enzymes that catalyzes the conversion of 1,2-propanediol, 1,2-ethanediol, and glycerol to the corresponding aldehydes. A DD-reactivating factor (DDR) is responsible for the rapid reactivation of the inactivated holoDD in the presence of AdoCbl, ATP, and Mg2+. DDR exists as a dimer of heterodimer (alpha-beta)2. The alpha subunit has four domains: ATPase domain, swiveling domain, linker domain, and insert domain. The beta subunit, composed of a single domain, has a similar fold to the beta subunit of diol dehydratase (DD). This entry describes the swiveling domain of DDR, which structurally connects the beta subunit and the ATPase domain of the other alpha subunit. Furthermore, the beta subunit moves with the swiveling domain while the linker domain acts as a flat spring or a hinge for the domain movement of the swiveling domain. Pssm-ID: 465763 Cd Length: 162 Bit Score: 37.49 E-value: 9.76e-04
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Blast search parameters | ||||
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