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Conserved domains on  [gi|2324452408|pdb|8E2L|A]
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Chain A, Twinkle mtDNA helicase

Protein Classification

bifunctional DNA primase/helicase( domain architecture ID 10099140)

bifunctional DNA primase/helicase similar to mitochondrial Twinkle protein, chloroplastic Twinkle homolog, and bacteriophage T7 gp4, which have both DNA primase and helicase activities

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Twinkle_C cd01122
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid ...
 246-509 4.50e-179

C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases.


:

Pssm-ID: 410867  Cd Length: 266  Bit Score: 504.46  E-value: 4.50e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      246 SIVSFKQLREDVYGELLNTEQVAGVKWTRFPELNRILKGHRKGELTVFTGPTGSGKTTFISEVALDLCIQGVNTLWGSFQ 325
Cdd:cd01122   1 SITTFDDLRELVYEELLNSEQVAGVQWKRFPSLNKLLKGHRRGELTIFTGPTGSGKTTFLSEYSLDLCMQGVNTLWGSFE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      326 INNVRLAKIMLTQFAMQRLEENLEQYDFWADKFEELPLYFMTFHGQQNIKTVLDTMQHAVYLYDINHVIIDNLQFMMGQE 405
Cdd:cd01122  81 IKNVRLAKTMLTQFAGKNLEDNLREFDEWADKFELLPMYFMKFHGSTDIDEVLDAMEHAVYVYDIQHIVIDNLQFMMGTQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      406 NLSIDKYAVQDHIIGAFRKFATNTSCHVTLIIHPRKEEDDRELQTASIFGSAKASQEADNVLILQEKKLVTCPGRRSLQV 485
Cdd:cd01122 161 ASGSDRFELQDLIIGKFRRFATNNNVHITLVIHPRKEDDDNELTTSSIFGSAKATQEADNVLILQDKRLISGEGKKFLQI 240

                       250       260
                ....*....|....*....|....
8E2L_A      486 TKNRFDGDVGIFPLDFIKSSLTFS 509
Cdd:cd01122 241 KKNRFDGDLGVIPLEFNKNSLTYS 264
TOPRIM_primases cd01029
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ...
 139-215 2.14e-03

TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in the active site regions of bacterial DnaG-type primases and their homologs. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. The prototypical bacterial primase. Escherichia coli DnaG is a single subunit enzyme.


:

Pssm-ID: 173779 [Multi-domain]  Cd Length: 79  Bit Score: 37.25  E-value: 2.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      139 EVVLTGHELDTLAVSQATGLPSVAlPRGVSCLPPmLLPYLEQF-KRVTLWLGHDIRSWEAS-KIFSRKLGL-RRCSLVRP 215
Cdd:cd01029   2 EVIIVEGYMDVLALHQAGIKNVVA-ALGTANTEE-QLRLLKRFaRTVILAFDNDEAGKKAAaRALELLLALgGRVRVPPL 79
 
Name Accession Description Interval E-value
Twinkle_C cd01122
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid ...
 246-509 4.50e-179

C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases.


Pssm-ID: 410867  Cd Length: 266  Bit Score: 504.46  E-value: 4.50e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      246 SIVSFKQLREDVYGELLNTEQVAGVKWTRFPELNRILKGHRKGELTVFTGPTGSGKTTFISEVALDLCIQGVNTLWGSFQ 325
Cdd:cd01122   1 SITTFDDLRELVYEELLNSEQVAGVQWKRFPSLNKLLKGHRRGELTIFTGPTGSGKTTFLSEYSLDLCMQGVNTLWGSFE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      326 INNVRLAKIMLTQFAMQRLEENLEQYDFWADKFEELPLYFMTFHGQQNIKTVLDTMQHAVYLYDINHVIIDNLQFMMGQE 405
Cdd:cd01122  81 IKNVRLAKTMLTQFAGKNLEDNLREFDEWADKFELLPMYFMKFHGSTDIDEVLDAMEHAVYVYDIQHIVIDNLQFMMGTQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      406 NLSIDKYAVQDHIIGAFRKFATNTSCHVTLIIHPRKEEDDRELQTASIFGSAKASQEADNVLILQEKKLVTCPGRRSLQV 485
Cdd:cd01122 161 ASGSDRFELQDLIIGKFRRFATNNNVHITLVIHPRKEDDDNELTTSSIFGSAKATQEADNVLILQDKRLISGEGKKFLQI 240

                       250       260
                ....*....|....*....|....
8E2L_A      486 TKNRFDGDVGIFPLDFIKSSLTFS 509
Cdd:cd01122 241 KKNRFDGDLGVIPLEFNKNSLTYS 264
AAA_25 pfam13481
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
 273-444 2.03e-23

AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.


Pssm-ID: 463892 [Multi-domain]  Cd Length: 193  Bit Score: 97.84  E-value: 2.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A        273 TRFPELNRILKGHR-KGELTVFTGPTGSGKTTFISEVALDLC-----------IQGVNTLWGSFQINNVRLAKIMLTQFA 340
Cdd:pfam13481  17 APPPPRRWLIKGLLpAGGLGLLAGAPGTGKTTLALDLAAAVAtgkpwlggprvPEQGKVLYVSAEGPADELRRRLRAAGA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A        341 MQRLEENLeqydFWADKFEELPLYFMTFHGQQNIKTVLDTMQHAVYLYDINHVIIDNLQFMM-GQENlsiDKYAVqDHII 419
Cdd:pfam13481  97 DLDLPARL----LFLSLVESLPLFFLDRGGPLLDADVDALEAALEEVEDPDLVVIDPLARALgGDEN---SNSDV-GRLV 168

                         170       180
                  ....*....|....*....|....*
8E2L_A        420 GAFRKFATNTSCHVTLIIHPRKEED 444
Cdd:pfam13481 169 KALDRLARRTGATVLLVHHVGKDGA 193
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
281-490 3.11e-11

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 64.54  E-value: 3.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      281 ILKGH-RKGELTVFTGPTGSGKTTFISEVALDL----------CIQGvNTLWGSFQINNVRLAKimltqfamqRLEENLE 349
Cdd:COG3598   5 LVPGLlPEGGVTLLAGPPGTGKSFLALQLAAAVaaggpwlgrrVPPG-KVLYLAAEDDRGELRR---------RLKALGA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      350 QYDFWADKFEElPLYFMTFHGQQNIKTVLDTMQHAVYLYDINHVIIDNLQ-FMMGQENlsidKYAVQDHIIGAFRKFATN 428
Cdd:COG3598  75 DLGLPFADLDG-RLRLLSLAGDLDDTDDLEALERAIEEEGPDLVVIDPLArVFGGDEN----DAEEMRAFLNPLDRLAER 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
8E2L_A      429 TSCHVTLIIHPRKEEDDrELQTASIFGSAKASQEADNVLILQEKKlvtCPGRRSLQVTKNRF 490
Cdd:COG3598 150 TGAAVLLVHHTGKGGAG-KDSGDRARGSSALRGAARSVLVLSREK---GEDLRVLTRAKSNY 207
PRK08506 PRK08506
replicative DNA helicase; Provisional
 231-406 2.49e-05

replicative DNA helicase; Provisional


Pssm-ID: 236278 [Multi-domain]  Cd Length: 472  Bit Score: 46.93  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A       231 NLSRIIKTSIPAAHKSIVSFKQLREdvygelLNTEQVAGVKwTRFPELNRILKGHRKGELTVFTGPTGSGKTTFISEVAL 310
Cdd:PRK08506 142 SNSEDFKDSKEVIESTMEHIKKQKR------LGNKDIIGLD-TGFVELNKMTKGFNKGDLIIIAARPSMGKTTLCLNMAL 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A       311 DLCIQGVNTLWGSFQINNVRLAKIML---TQFAMQRLEE-NL--EQYDFWADKFEEL---PLYFMTfHGQQNIKTVLDTM 381
Cdd:PRK08506 215 KALNQDKGVAFFSLEMPAEQLMLRMLsakTSIPLQNLRTgDLddDEWERLSDACDELskkKLFVYD-SGYVNIHQVRAQL 293

                        170       180       190
                 ....*....|....*....|....*....|
8E2L_A       382 -----QHAvylyDINHVIIDNLQFMMGQEN 406
Cdd:PRK08506 294 rklksQHP----EIGLAVIDYLQLMSGSGN 319
TOPRIM_primases cd01029
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ...
 139-215 2.14e-03

TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in the active site regions of bacterial DnaG-type primases and their homologs. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. The prototypical bacterial primase. Escherichia coli DnaG is a single subunit enzyme.


Pssm-ID: 173779 [Multi-domain]  Cd Length: 79  Bit Score: 37.25  E-value: 2.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      139 EVVLTGHELDTLAVSQATGLPSVAlPRGVSCLPPmLLPYLEQF-KRVTLWLGHDIRSWEAS-KIFSRKLGL-RRCSLVRP 215
Cdd:cd01029   2 EVIIVEGYMDVLALHQAGIKNVVA-ALGTANTEE-QLRLLKRFaRTVILAFDNDEAGKKAAaRALELLLALgGRVRVPPL 79
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
275-303 8.16e-03

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 38.20  E-value: 8.16e-03
                         10        20        30
                 ....*....|....*....|....*....|..
8E2L_A       275 FPELNRILKG---HRKGeLTVFTGPTGSGKTT 303
Cdd:NF041000 113 FPEQFQLLKQllqRRSG-LILFSGPTGSGKTT 143
 
Name Accession Description Interval E-value
Twinkle_C cd01122
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid ...
 246-509 4.50e-179

C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases.


Pssm-ID: 410867  Cd Length: 266  Bit Score: 504.46  E-value: 4.50e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      246 SIVSFKQLREDVYGELLNTEQVAGVKWTRFPELNRILKGHRKGELTVFTGPTGSGKTTFISEVALDLCIQGVNTLWGSFQ 325
Cdd:cd01122   1 SITTFDDLRELVYEELLNSEQVAGVQWKRFPSLNKLLKGHRRGELTIFTGPTGSGKTTFLSEYSLDLCMQGVNTLWGSFE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      326 INNVRLAKIMLTQFAMQRLEENLEQYDFWADKFEELPLYFMTFHGQQNIKTVLDTMQHAVYLYDINHVIIDNLQFMMGQE 405
Cdd:cd01122  81 IKNVRLAKTMLTQFAGKNLEDNLREFDEWADKFELLPMYFMKFHGSTDIDEVLDAMEHAVYVYDIQHIVIDNLQFMMGTQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      406 NLSIDKYAVQDHIIGAFRKFATNTSCHVTLIIHPRKEEDDRELQTASIFGSAKASQEADNVLILQEKKLVTCPGRRSLQV 485
Cdd:cd01122 161 ASGSDRFELQDLIIGKFRRFATNNNVHITLVIHPRKEDDDNELTTSSIFGSAKATQEADNVLILQDKRLISGEGKKFLQI 240

                       250       260
                ....*....|....*....|....
8E2L_A      486 TKNRFDGDVGIFPLDFIKSSLTFS 509
Cdd:cd01122 241 KKNRFDGDLGVIPLEFNKNSLTYS 264
AAA_25 pfam13481
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
 273-444 2.03e-23

AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.


Pssm-ID: 463892 [Multi-domain]  Cd Length: 193  Bit Score: 97.84  E-value: 2.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A        273 TRFPELNRILKGHR-KGELTVFTGPTGSGKTTFISEVALDLC-----------IQGVNTLWGSFQINNVRLAKIMLTQFA 340
Cdd:pfam13481  17 APPPPRRWLIKGLLpAGGLGLLAGAPGTGKTTLALDLAAAVAtgkpwlggprvPEQGKVLYVSAEGPADELRRRLRAAGA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A        341 MQRLEENLeqydFWADKFEELPLYFMTFHGQQNIKTVLDTMQHAVYLYDINHVIIDNLQFMM-GQENlsiDKYAVqDHII 419
Cdd:pfam13481  97 DLDLPARL----LFLSLVESLPLFFLDRGGPLLDADVDALEAALEEVEDPDLVVIDPLARALgGDEN---SNSDV-GRLV 168

                         170       180
                  ....*....|....*....|....*
8E2L_A        420 GAFRKFATNTSCHVTLIIHPRKEED 444
Cdd:pfam13481 169 KALDRLARRTGATVLLVHHVGKDGA 193
RecA-like_Gp4D_helicase cd19483
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ...
 291-499 4.73e-16

RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the RecA-like domain of the Gp4D fragment of the Gene4 helicase-primase (Gp4) from bacteriophage T7. Gp4D (residues 241-566) is the minimal fragment of the Gp4 that forms hexameric rings, it contains the helicase domain and the linker connecting the helicase and primase domains. Helicases are ring-shaped oligomeric enzymes that unwind DNA at the replication fork; they couple NTP hydrolysis to the unwinding of nucleic acid duplexes into their component strands. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410891 [Multi-domain]  Cd Length: 231  Bit Score: 77.61  E-value: 4.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      291 TVFTGPTGSGKTTFISEVALDLCI-QGVNTLWGSFQINNVRLAKIMLTQFAMQ-------RLEENLEQYDFWADKFEELP 362
Cdd:cd19483   1 VTIGAGSGIGKSTIVRELAYHLITeHGEKVGIISLEESVEETAKGLAGKHLGKpeplelpRDDITEEEEDDAFDNELGSG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      363 -LYFMTFHGQQNIKTVLDTMQHAVYLYDINHVIIDNLQ-FMMGQENLSIDKyaVQDHIIGAFRKFATNTSCHVTLIIHPR 440
Cdd:cd19483  81 rFFLYDHFGSLDWDNLKEKIRYMVKVLGCKVIVLDHLTiLVSGLDSSDERK--ELDEIMTELAALVKELGVTIILVSHLR 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
8E2L_A      441 K------EEDDRELQTASIFGSAKASQEADNVLILQEKKLVTCP---GRRSLQVTKNRFDGDVGIFPL 499
Cdd:cd19483 159 RpgggkgHEEGGEVSESDLRGSSAIAQLSDYVIGLERNKQADDPverNTTRVRVLKNRFTGETGIAGT 226
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
281-490 3.11e-11

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 64.54  E-value: 3.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      281 ILKGH-RKGELTVFTGPTGSGKTTFISEVALDL----------CIQGvNTLWGSFQINNVRLAKimltqfamqRLEENLE 349
Cdd:COG3598   5 LVPGLlPEGGVTLLAGPPGTGKSFLALQLAAAVaaggpwlgrrVPPG-KVLYLAAEDDRGELRR---------RLKALGA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      350 QYDFWADKFEElPLYFMTFHGQQNIKTVLDTMQHAVYLYDINHVIIDNLQ-FMMGQENlsidKYAVQDHIIGAFRKFATN 428
Cdd:COG3598  75 DLGLPFADLDG-RLRLLSLAGDLDDTDDLEALERAIEEEGPDLVVIDPLArVFGGDEN----DAEEMRAFLNPLDRLAER 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
8E2L_A      429 TSCHVTLIIHPRKEEDDrELQTASIFGSAKASQEADNVLILQEKKlvtCPGRRSLQVTKNRF 490
Cdd:COG3598 150 TGAAVLLVHHTGKGGAG-KDSGDRARGSSALRGAARSVLVLSREK---GEDLRVLTRAKSNY 207
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 291-456 8.34e-11

RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 59.44  E-value: 8.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      291 TVFTGPTGSGKTTFISEVALDLCIQGVNTLWGSFqinnvrlakimltqfamqrleenleqydfwadkfeelplyfmtfhg 370
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF---------------------------------------------- 34

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      371 qqniktvLDTMQHAVY----LYDINHVIIDNLQFMMGQENLSIDKYavQDHIIGAFRKFATNTSCHVTLIIHPRKEEDDR 446
Cdd:cd01120  35 -------LDTILEAIEdlieEKKLDIIIIDSLSSLARASQGDRSSE--LLEDLAKLLRAARNTGITVIATIHSDKFDIDR 105

                       170
                ....*....|
8E2L_A      447 ELQTASIFGS 456
Cdd:cd01120 106 GGSSNDERLL 115
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
273-489 2.06e-05

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 45.68  E-value: 2.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      273 TRFPELNRILK-GHRKGELTVFTGPTGSGKTTFISEVALDLCIQGVNTLWgsfqinnvrlakIMLTQFAmQRLEENLEQY 351
Cdd:COG0467   4 TGIPGLDELLGgGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLY------------VSFEESP-EQLLRRAESL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      352 DF-WADKFEELPLYFM---TFHGQQNIKTVLDTMQHAVYLYDINHVIIDNLqfmMGQENLSIDKYAVQDHIIgAFRKFAT 427
Cdd:COG0467  71 GLdLEEYIESGLLRIIdlsPEELGLDLEELLARLREAVEEFGAKRVVIDSL---SGLLLALPDPERLREFLH-RLLRYLK 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
8E2L_A      428 NTSChVTLIIhprkeeddreLQTASIFGSAKASQE---ADNVLILqekKLVTCPG--RRSLQVTKNR 489
Cdd:COG0467 147 KRGV-TTLLT----------SETGGLEDEATEGGLsylADGVILL---RYVELGGelRRALSVLKMR 199
PRK08506 PRK08506
replicative DNA helicase; Provisional
 231-406 2.49e-05

replicative DNA helicase; Provisional


Pssm-ID: 236278 [Multi-domain]  Cd Length: 472  Bit Score: 46.93  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A       231 NLSRIIKTSIPAAHKSIVSFKQLREdvygelLNTEQVAGVKwTRFPELNRILKGHRKGELTVFTGPTGSGKTTFISEVAL 310
Cdd:PRK08506 142 SNSEDFKDSKEVIESTMEHIKKQKR------LGNKDIIGLD-TGFVELNKMTKGFNKGDLIIIAARPSMGKTTLCLNMAL 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A       311 DLCIQGVNTLWGSFQINNVRLAKIML---TQFAMQRLEE-NL--EQYDFWADKFEEL---PLYFMTfHGQQNIKTVLDTM 381
Cdd:PRK08506 215 KALNQDKGVAFFSLEMPAEQLMLRMLsakTSIPLQNLRTgDLddDEWERLSDACDELskkKLFVYD-SGYVNIHQVRAQL 293

                        170       180       190
                 ....*....|....*....|....*....|
8E2L_A       382 -----QHAvylyDINHVIIDNLQFMMGQEN 406
Cdd:PRK08506 294 rklksQHP----EIGLAVIDYLQLMSGSGN 319
DnaB_C cd00984
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ...
 273-401 6.28e-05

C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase DnaB unwinds the DNA duplex at the chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.


Pssm-ID: 410864 [Multi-domain]  Cd Length: 256  Bit Score: 44.81  E-value: 6.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      273 TRFPELNRILKGHRKGELTVFTGPTGSGKTTFISEVALDLCI-QGVNTLWGSFQINNVRLAKIMLTQFA---MQRLEENL 348
Cdd:cd00984   4 TGFTDLDKLTGGLQPGDLIIIAARPSMGKTAFALNIAENIALdEGLPVLFFSLEMSAEQLAERLLSSESgvsLSKLRTGR 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
8E2L_A      349 EQYDFW------ADKFEELPLYfmtFHGQQNIkTVLD----TMQHAVYLYDINHVIIDNLQFM 401
Cdd:cd00984  84 LDDEDWerltaaMGELSELPLY---IDDTPGL-TVDEirakARRLKREHGGLGLIVIDYLQLI 142
TOPRIM_primases cd01029
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ...
 139-215 2.14e-03

TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in the active site regions of bacterial DnaG-type primases and their homologs. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. The prototypical bacterial primase. Escherichia coli DnaG is a single subunit enzyme.


Pssm-ID: 173779 [Multi-domain]  Cd Length: 79  Bit Score: 37.25  E-value: 2.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A      139 EVVLTGHELDTLAVSQATGLPSVAlPRGVSCLPPmLLPYLEQF-KRVTLWLGHDIRSWEAS-KIFSRKLGL-RRCSLVRP 215
Cdd:cd01029   2 EVIIVEGYMDVLALHQAGIKNVVA-ALGTANTEE-QLRLLKRFaRTVILAFDNDEAGKKAAaRALELLLALgGRVRVPPL 79
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 286-338 3.83e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 38.38  E-value: 3.83e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
8E2L_A      286 RKGELTVFTGPTGSGKTTFISevaldlCIQGVNTLW-GSFQINNVRLAKIMLTQ 338
Cdd:cd00267  23 KAGEIVALVGPNGSGKSTLLR------AIAGLLKPTsGEILIDGKDIAKLPLEE 70
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 277-399 3.83e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 38.25  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8E2L_A        277 ELNRILKGHRKG--ELTVFTGPTGSGKTTFISEVALDLCIQGVNTLWGSFQINNVRLA---KIMLTQFAMQRLEENLE-Q 350
Cdd:pfam13191  11 QLLDALDRVRSGrpPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPlleALTREGLLRQLLDELESsL 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
8E2L_A        351 YDFWADKFEELPLYFMTFHGQQnIKTVLDTMQHAVYLYDINH----VIIDNLQ 399
Cdd:pfam13191  91 LEAWRAALLEALAPVPELPGDL-AERLLDLLLRLLDLLARGErplvLVLDDLQ 142
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 286-333 6.26e-03

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 37.94  E-value: 6.26e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
8E2L_A      286 RKGELTVFTGPTGSGKTTFISevaldlCIQGVNTLW-GSFQINNVRLAK 333
Cdd:cd03229  24 EAGEIVALLGPSGSGKSTLLR------CIAGLEEPDsGSILIDGEDLTD 66
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 286-306 7.61e-03

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 37.83  E-value: 7.61e-03
                        10        20
                ....*....|....*....|.
8E2L_A      286 RKGELTVFTGPTGSGKTTFIS 306
Cdd:cd03250  29 PKGELVAIVGPVGSGKSSLLS 49
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
275-303 8.16e-03

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 38.20  E-value: 8.16e-03
                         10        20        30
                 ....*....|....*....|....*....|..
8E2L_A       275 FPELNRILKG---HRKGeLTVFTGPTGSGKTT 303
Cdd:NF041000 113 FPEQFQLLKQllqRRSG-LILFSGPTGSGKTT 143
DnaB COG0305
Replicative DNA helicase [Replication, recombination and repair];
245-313 8.20e-03

Replicative DNA helicase [Replication, recombination and repair];


Pssm-ID: 440074 [Multi-domain]  Cd Length: 429  Bit Score: 38.90  E-value: 8.20e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
8E2L_A      245 KSIVSFKQLREDVYGELL----NTEQVAGVKwTRFPELNRILKGHRKGELTVFTGPTGSGKTTFisevALDLC 313
Cdd:COG0305 145 KGFVSISDILKEALERIEelykNGGGITGVP-TGFTDLDKLTGGLQPGDLIILAARPSMGKTAF----ALNIA 212
 
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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