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Conserved domains on  [gi|530413462|ref|XP_005256397|]
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nuclear prelamin A recognition factor isoform X2 [Homo sapiens]

Protein Classification

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Fe_hyd_lg_C pfam02906
Iron only hydrogenase large subunit, C-terminal domain;
33-322 2.62e-81

Iron only hydrogenase large subunit, C-terminal domain;


:

Pssm-ID: 397172  Cd Length: 277  Bit Score: 250.61  E-value: 2.62e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462   33 KVLVVSVCPQSLPYFAAKFNLSVTDASRRLCGFLKSLGVHYVFDTTIAADFSILESQKEFVRRYrqhsEEERTLPMLTSA 112
Cdd:pfam02906   1 KKVVAQIAPAVRGAFGEEFGLPPTVTTGKLVAALRKLGFDYVFDTAFGADLTIMEEATEFLERL----EKGKKLPMFTSC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462  113 CPGWVRYAERVLGRpITAHLCTAKSPQQVMGSLVKDYFARQqnlspEKIFHVIVAPCYDKKLEALQESLppalHGSRGAD 192
Cdd:pfam02906  77 CPGWVKYVEKYYPE-LLPNLSTCKSPMQMFGALIKTYYAED-----LKIYVVSIMPCTAKKFEAARPEM----KGDRDVD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462  193 CVLTSGEIAQIMEQGDL---SVRDAAVDTLFGDlkedkvTRHDG---ASSDGHLAHIFRHAAKELFNEDVEEVTYRALRN 266
Cdd:pfam02906 147 AVLTTRELAAMIKEAGIdfaKLEDEEFDNPLGE------SSGAGrifGVTGGVMEAALRTAYELLTGKELPAIEFKEVRG 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530413462  267 -KDFQEVTLEKNGeVVLRFAAAYGFRNIQNMILKLKKGKFPFHFVEVLACAGGCLNG 322
Cdd:pfam02906 221 lEGIKEATVEIGG-TTVKVAVVSGLKNARKLLEKIKAGELKYHFIEVMACPGGCIGG 276
Fe_hyd_SSU smart00902
Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, ...
339-387 1.78e-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: 69.97  E-value: 1.78e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530413462   339 RQMEGIYADI---PVRRPESSAHVQELYQEWLEGINSPKAREVLHTTYQSQE 387
Cdd:smart00902   1 QRAEALYNIDkslPLRKSHENPAVKKLYEEFLGGPLSHKAHELLHTHYHDRE 52
 
Name Accession Description Interval E-value
Fe_hyd_lg_C pfam02906
Iron only hydrogenase large subunit, C-terminal domain;
33-322 2.62e-81

Iron only hydrogenase large subunit, C-terminal domain;


Pssm-ID: 397172  Cd Length: 277  Bit Score: 250.61  E-value: 2.62e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462   33 KVLVVSVCPQSLPYFAAKFNLSVTDASRRLCGFLKSLGVHYVFDTTIAADFSILESQKEFVRRYrqhsEEERTLPMLTSA 112
Cdd:pfam02906   1 KKVVAQIAPAVRGAFGEEFGLPPTVTTGKLVAALRKLGFDYVFDTAFGADLTIMEEATEFLERL----EKGKKLPMFTSC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462  113 CPGWVRYAERVLGRpITAHLCTAKSPQQVMGSLVKDYFARQqnlspEKIFHVIVAPCYDKKLEALQESLppalHGSRGAD 192
Cdd:pfam02906  77 CPGWVKYVEKYYPE-LLPNLSTCKSPMQMFGALIKTYYAED-----LKIYVVSIMPCTAKKFEAARPEM----KGDRDVD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462  193 CVLTSGEIAQIMEQGDL---SVRDAAVDTLFGDlkedkvTRHDG---ASSDGHLAHIFRHAAKELFNEDVEEVTYRALRN 266
Cdd:pfam02906 147 AVLTTRELAAMIKEAGIdfaKLEDEEFDNPLGE------SSGAGrifGVTGGVMEAALRTAYELLTGKELPAIEFKEVRG 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530413462  267 -KDFQEVTLEKNGeVVLRFAAAYGFRNIQNMILKLKKGKFPFHFVEVLACAGGCLNG 322
Cdd:pfam02906 221 lEGIKEATVEIGG-TTVKVAVVSGLKNARKLLEKIKAGELKYHFIEVMACPGGCIGG 276
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
12-384 1.67e-60

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 202.18  E-value: 1.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462  12 QNAK----DFFRVLNLNKkcdtSKHKVlVVSVCPqSlpyFAAKFNLSVTdaSRRLCGFLKSLGVHYVFDTTIAADFSILE 87
Cdd:COG4624  134 FGAIteksDIEKVKKALK----DPEKV-VAQVAP-A---VRGQFGGTVT--PGKLVAALKKLGFDDVFETAFGADLTIME 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462  88 SQKEFVRRYrqhseEERTLPMLTSACPGWVRYAERVlgRP-ITAHLCTAKSPQQVMGSLVKDYFArqqnlspEKIFHVIV 166
Cdd:COG4624  203 EAKELLERL-----KKGKLPMITSCCPAWVKLIEKY--YPeLLPNLSPCKSPMQAFGALIKTYYA-------PDIKVVFI 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462 167 APCYDKKLEALQESLPPALhgsrgaDCVLTSGEIAQIMEQGDLSvrdaavdtlFGDLKEDKVtrhDGASSdgHLAHIF-- 244
Cdd:COG4624  269 GPCIAKKFEAKRPEMKGDV------DYVLTFRELARMIKEAGID---------LANLEEEEF---DNESS--GAGRIFgv 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462 245 --------RHAAKELFNEDVEevtyralrnkdfqevtlekngevvLRFAAAYGFRNIQNMILKLKKGKFPFHFVEVLACA 316
Cdd:COG4624  329 tggvmeaaLRTAYELLPDGLE------------------------LKVAVVSGLKNCRKLLEEIKAGKIDYHFIEVMACP 384
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530413462 317 GGCLNGRGQaqtPDGHADKALLRQMEGIYADI-PVRRPESSAHVQELYQEWLEGINSPKAREVLHTTYQ 384
Cdd:COG4624  385 GGCIGGPGQ---PIPPGSLEKRRKRVALYAKEaPIRKSHENPEILDLYREFLGKPLSEKAHELLHTHYR 450
Fe_hyd_SSU smart00902
Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, ...
339-387 1.78e-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: 69.97  E-value: 1.78e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530413462   339 RQMEGIYADI---PVRRPESSAHVQELYQEWLEGINSPKAREVLHTTYQSQE 387
Cdd:smart00902   1 QRAEALYNIDkslPLRKSHENPAVKKLYEEFLGGPLSHKAHELLHTHYHDRE 52
Fe_hyd_SSU pfam02256
Iron hydrogenase small subunit; This family represents the small subunit of the Fe-only ...
334-385 1.28e-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: 1.28e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530413462  334 DKALLRQMEGIYAD---IPVRRPESSAHVQELYQEWLEGINSPKAREVLHTTYQS 385
Cdd:pfam02256   1 DDIRKKRAEALYKIdknKPLRKSHENPAVKKLYEEFLGEPLSHKAHELLHTHYTP 55
 
Name Accession Description Interval E-value
Fe_hyd_lg_C pfam02906
Iron only hydrogenase large subunit, C-terminal domain;
33-322 2.62e-81

Iron only hydrogenase large subunit, C-terminal domain;


Pssm-ID: 397172  Cd Length: 277  Bit Score: 250.61  E-value: 2.62e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462   33 KVLVVSVCPQSLPYFAAKFNLSVTDASRRLCGFLKSLGVHYVFDTTIAADFSILESQKEFVRRYrqhsEEERTLPMLTSA 112
Cdd:pfam02906   1 KKVVAQIAPAVRGAFGEEFGLPPTVTTGKLVAALRKLGFDYVFDTAFGADLTIMEEATEFLERL----EKGKKLPMFTSC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462  113 CPGWVRYAERVLGRpITAHLCTAKSPQQVMGSLVKDYFARQqnlspEKIFHVIVAPCYDKKLEALQESLppalHGSRGAD 192
Cdd:pfam02906  77 CPGWVKYVEKYYPE-LLPNLSTCKSPMQMFGALIKTYYAED-----LKIYVVSIMPCTAKKFEAARPEM----KGDRDVD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462  193 CVLTSGEIAQIMEQGDL---SVRDAAVDTLFGDlkedkvTRHDG---ASSDGHLAHIFRHAAKELFNEDVEEVTYRALRN 266
Cdd:pfam02906 147 AVLTTRELAAMIKEAGIdfaKLEDEEFDNPLGE------SSGAGrifGVTGGVMEAALRTAYELLTGKELPAIEFKEVRG 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530413462  267 -KDFQEVTLEKNGeVVLRFAAAYGFRNIQNMILKLKKGKFPFHFVEVLACAGGCLNG 322
Cdd:pfam02906 221 lEGIKEATVEIGG-TTVKVAVVSGLKNARKLLEKIKAGELKYHFIEVMACPGGCIGG 276
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
12-384 1.67e-60

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 202.18  E-value: 1.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462  12 QNAK----DFFRVLNLNKkcdtSKHKVlVVSVCPqSlpyFAAKFNLSVTdaSRRLCGFLKSLGVHYVFDTTIAADFSILE 87
Cdd:COG4624  134 FGAIteksDIEKVKKALK----DPEKV-VAQVAP-A---VRGQFGGTVT--PGKLVAALKKLGFDDVFETAFGADLTIME 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462  88 SQKEFVRRYrqhseEERTLPMLTSACPGWVRYAERVlgRP-ITAHLCTAKSPQQVMGSLVKDYFArqqnlspEKIFHVIV 166
Cdd:COG4624  203 EAKELLERL-----KKGKLPMITSCCPAWVKLIEKY--YPeLLPNLSPCKSPMQAFGALIKTYYA-------PDIKVVFI 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462 167 APCYDKKLEALQESLPPALhgsrgaDCVLTSGEIAQIMEQGDLSvrdaavdtlFGDLKEDKVtrhDGASSdgHLAHIF-- 244
Cdd:COG4624  269 GPCIAKKFEAKRPEMKGDV------DYVLTFRELARMIKEAGID---------LANLEEEEF---DNESS--GAGRIFgv 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413462 245 --------RHAAKELFNEDVEevtyralrnkdfqevtlekngevvLRFAAAYGFRNIQNMILKLKKGKFPFHFVEVLACA 316
Cdd:COG4624  329 tggvmeaaLRTAYELLPDGLE------------------------LKVAVVSGLKNCRKLLEEIKAGKIDYHFIEVMACP 384
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530413462 317 GGCLNGRGQaqtPDGHADKALLRQMEGIYADI-PVRRPESSAHVQELYQEWLEGINSPKAREVLHTTYQ 384
Cdd:COG4624  385 GGCIGGPGQ---PIPPGSLEKRRKRVALYAKEaPIRKSHENPEILDLYREFLGKPLSEKAHELLHTHYR 450
Fe_hyd_SSU smart00902
Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, ...
339-387 1.78e-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: 69.97  E-value: 1.78e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530413462   339 RQMEGIYADI---PVRRPESSAHVQELYQEWLEGINSPKAREVLHTTYQSQE 387
Cdd:smart00902   1 QRAEALYNIDkslPLRKSHENPAVKKLYEEFLGGPLSHKAHELLHTHYHDRE 52
Fe_hyd_SSU pfam02256
Iron hydrogenase small subunit; This family represents the small subunit of the Fe-only ...
334-385 1.28e-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: 1.28e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530413462  334 DKALLRQMEGIYAD---IPVRRPESSAHVQELYQEWLEGINSPKAREVLHTTYQS 385
Cdd:pfam02256   1 DDIRKKRAEALYKIdknKPLRKSHENPAVKKLYEEFLGEPLSHKAHELLHTHYTP 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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