nuclear prelamin A recognition factor isoform a [Homo sapiens]
nuclear prelamin A recognition factor family protein( domain architecture ID 10502698)
nuclear prelamin A recognition factor (NARF) family protein similar to NARF that evolved from an ancestral Fe-hydrogenase but does not produce hydrogen
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
Fe_hyd_lg_C | pfam02906 | Iron only hydrogenase large subunit, C-terminal domain; |
92-381 | 1.55e-80 | |||||
Iron only hydrogenase large subunit, C-terminal domain; : Pssm-ID: 397172 Cd Length: 277 Bit Score: 250.61 E-value: 1.55e-80
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Fe_hyd_SSU | smart00902 | Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, ... |
398-446 | 1.93e-15 | |||||
Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, nitrogen-fixing, photosynthetic, or sulphate-reducing bacteria, metabolise hydrogen. Hydrogen activation is mediated by a family of enzymes, termed hydrogenases, which either provide these organisms with reducing power from hydrogen oxidation, or act as electron sinks. There are two hydrogenases families that differ functionally from each other: NiFe hydrogenases tend to be more involved in hydrogen oxidation, while Iron-only FeFe (Fe only) hydrogenases in hydrogen production. Fe only hydrogenases show a common core structure, which contains a moiety, deeply buried inside the protein, with an Fe-Fe dinuclear centre, nonproteic bridging, terminal CO and CN- ligands attached to each of the iron atoms, and a dithio moiety, which also bridges the two iron atoms and has been tentatively assigned as a di(thiomethyl)amine. This common core also harbours three [4Fe-4S] iron-sulphur clusters. In FeFe hydrogenases, as in NiFe hydrogenases, the set of iron-sulphur clusters is dispersed regularly between the dinuclear Fe-Fe centre and the molecular surface. These clusters are distant by about 1.2 nm from each other but the [4Fe-4S] cluster closest to the dinuclear centre is covalently bound to one of the iron atoms though a thiolate bridging ligand. The moiety including the dinuclear centre, the thiolate bridging ligand, and the proximal [4Fe-4S] cluster is known as the H-cluster. A channel, lined with hydrophobic amino acid side chains, nearly connects the dinuclear centre and the molecular surface. Furthermore hydrogen-bonded water molecule sites have been identified at the interior and at the surface of the protein. The small subunit is comprised of alternating random coil and alpha helical structures that encompass the large subunit in a novel protein fold. : Pssm-ID: 214899 [Multi-domain] Cd Length: 52 Bit Score: 70.36 E-value: 1.93e-15
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Name | Accession | Description | Interval | E-value | |||||||
Fe_hyd_lg_C | pfam02906 | Iron only hydrogenase large subunit, C-terminal domain; |
92-381 | 1.55e-80 | |||||||
Iron only hydrogenase large subunit, C-terminal domain; Pssm-ID: 397172 Cd Length: 277 Bit Score: 250.61 E-value: 1.55e-80
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Nar1 | COG4624 | Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
46-443 | 1.52e-59 | |||||||
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 201.41 E-value: 1.52e-59
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Fe_hyd_SSU | smart00902 | Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, ... |
398-446 | 1.93e-15 | |||||||
Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, nitrogen-fixing, photosynthetic, or sulphate-reducing bacteria, metabolise hydrogen. Hydrogen activation is mediated by a family of enzymes, termed hydrogenases, which either provide these organisms with reducing power from hydrogen oxidation, or act as electron sinks. There are two hydrogenases families that differ functionally from each other: NiFe hydrogenases tend to be more involved in hydrogen oxidation, while Iron-only FeFe (Fe only) hydrogenases in hydrogen production. Fe only hydrogenases show a common core structure, which contains a moiety, deeply buried inside the protein, with an Fe-Fe dinuclear centre, nonproteic bridging, terminal CO and CN- ligands attached to each of the iron atoms, and a dithio moiety, which also bridges the two iron atoms and has been tentatively assigned as a di(thiomethyl)amine. This common core also harbours three [4Fe-4S] iron-sulphur clusters. In FeFe hydrogenases, as in NiFe hydrogenases, the set of iron-sulphur clusters is dispersed regularly between the dinuclear Fe-Fe centre and the molecular surface. These clusters are distant by about 1.2 nm from each other but the [4Fe-4S] cluster closest to the dinuclear centre is covalently bound to one of the iron atoms though a thiolate bridging ligand. The moiety including the dinuclear centre, the thiolate bridging ligand, and the proximal [4Fe-4S] cluster is known as the H-cluster. A channel, lined with hydrophobic amino acid side chains, nearly connects the dinuclear centre and the molecular surface. Furthermore hydrogen-bonded water molecule sites have been identified at the interior and at the surface of the protein. The small subunit is comprised of alternating random coil and alpha helical structures that encompass the large subunit in a novel protein fold. Pssm-ID: 214899 [Multi-domain] Cd Length: 52 Bit Score: 70.36 E-value: 1.93e-15
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Fe_hyd_SSU | pfam02256 | Iron hydrogenase small subunit; This family represents the small subunit of the Fe-only ... |
393-444 | 1.31e-11 | |||||||
Iron hydrogenase small subunit; This family represents the small subunit of the Fe-only hydrogenases EC:1.18.99.1. The subunit is comprised of alternating random coil and alpha helical structures that encompasses the large subunit in a novel protein fold. Pssm-ID: 460511 [Multi-domain] Cd Length: 56 Bit Score: 59.44 E-value: 1.31e-11
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Name | Accession | Description | Interval | E-value | |||||||
Fe_hyd_lg_C | pfam02906 | Iron only hydrogenase large subunit, C-terminal domain; |
92-381 | 1.55e-80 | |||||||
Iron only hydrogenase large subunit, C-terminal domain; Pssm-ID: 397172 Cd Length: 277 Bit Score: 250.61 E-value: 1.55e-80
|
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Nar1 | COG4624 | Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
46-443 | 1.52e-59 | |||||||
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 201.41 E-value: 1.52e-59
|
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Fe_hyd_SSU | smart00902 | Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, ... |
398-446 | 1.93e-15 | |||||||
Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, nitrogen-fixing, photosynthetic, or sulphate-reducing bacteria, metabolise hydrogen. Hydrogen activation is mediated by a family of enzymes, termed hydrogenases, which either provide these organisms with reducing power from hydrogen oxidation, or act as electron sinks. There are two hydrogenases families that differ functionally from each other: NiFe hydrogenases tend to be more involved in hydrogen oxidation, while Iron-only FeFe (Fe only) hydrogenases in hydrogen production. Fe only hydrogenases show a common core structure, which contains a moiety, deeply buried inside the protein, with an Fe-Fe dinuclear centre, nonproteic bridging, terminal CO and CN- ligands attached to each of the iron atoms, and a dithio moiety, which also bridges the two iron atoms and has been tentatively assigned as a di(thiomethyl)amine. This common core also harbours three [4Fe-4S] iron-sulphur clusters. In FeFe hydrogenases, as in NiFe hydrogenases, the set of iron-sulphur clusters is dispersed regularly between the dinuclear Fe-Fe centre and the molecular surface. These clusters are distant by about 1.2 nm from each other but the [4Fe-4S] cluster closest to the dinuclear centre is covalently bound to one of the iron atoms though a thiolate bridging ligand. The moiety including the dinuclear centre, the thiolate bridging ligand, and the proximal [4Fe-4S] cluster is known as the H-cluster. A channel, lined with hydrophobic amino acid side chains, nearly connects the dinuclear centre and the molecular surface. Furthermore hydrogen-bonded water molecule sites have been identified at the interior and at the surface of the protein. The small subunit is comprised of alternating random coil and alpha helical structures that encompass the large subunit in a novel protein fold. Pssm-ID: 214899 [Multi-domain] Cd Length: 52 Bit Score: 70.36 E-value: 1.93e-15
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Fe_hyd_SSU | pfam02256 | Iron hydrogenase small subunit; This family represents the small subunit of the Fe-only ... |
393-444 | 1.31e-11 | |||||||
Iron hydrogenase small subunit; This family represents the small subunit of the Fe-only hydrogenases EC:1.18.99.1. The subunit is comprised of alternating random coil and alpha helical structures that encompasses the large subunit in a novel protein fold. Pssm-ID: 460511 [Multi-domain] Cd Length: 56 Bit Score: 59.44 E-value: 1.31e-11
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Blast search parameters | ||||
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