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Conserved domains on  [gi|1959262027|ref|WP_201733441|]
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helicase HerA domain-containing protein [Acidithrix sp. C25]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
VirB4 super family cl43870
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
43-425 1.99e-22

Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];


The actual alignment was detected with superfamily member COG3451:

Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 99.64  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027  43 FGFNPFELYRdgvisNPNAFVFGQVGKGKSALLKSYLARMFLLGYPSVVFDPKGEYGALARFFGFDPIDY-LASKRGVNP 121
Cdd:COG3451   194 VFFDFHDGLD-----NGNTLILGPSGSGKSFLLKLLLLQLLRYGARIVIFDPGGSYEILVRALGGTYIDLsPGSPTGLNP 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 122 FvevegapnGLLARELNSEMATYVISVALGR---RPTEIEHLAISEALNEISRGVD------FFKLRSCLEKIDRSGgpt 192
Cdd:COG3451   269 F--------DLEDTEEKRDFLLELLELLLGRegePLTPEERAAIDRAVRALYRRADpeerttLSDLYELLKEQPEAK--- 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 193 twrgsysigslaSLLAVLDSLIESGLVAQ---SESSFDLGKvlgKSILVFDLSGLFGSGRyplvvalllgaLRA------ 263
Cdd:COG3451   338 ------------DLAARLEPYTKGGSYGWlfdGPTNLDLSD---ARFVVFDLTELLDNPE-----------LRPpvllyl 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 264 -----HKMTRDLP--PLIIAIDEIWALMSDSNIASWLGSYWKLSRGIGIANIGVSHRLSDFSGgddvgahlksqslnsst 336
Cdd:COG3451   392 lhriwNRLRKNNDgrPTLIVIDEAWLLLDNPAFAEFLEEWLKTLRKYNGAVIFATQSVEDFLS----------------- 454
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 337 nysngpnrtviSEINRglGMINDTETIVSFALEVDEAHHLCSAFGFSLEVAPLLRQLRKGS--ALWKIGERNLLVDHYLT 414
Cdd:COG3451   455 -----------SPIAE--AIIENSATKILLPQPKADIEDYAELLGLSERELELIRSAGRGKrdFLIKQGNGSVVFRLDLS 521
                         410
                  ....*....|.
gi 1959262027 415 SIETALFNTDA 425
Cdd:COG3451   522 PEELALLSTKP 532
 
Name Accession Description Interval E-value
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
43-425 1.99e-22

Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 99.64  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027  43 FGFNPFELYRdgvisNPNAFVFGQVGKGKSALLKSYLARMFLLGYPSVVFDPKGEYGALARFFGFDPIDY-LASKRGVNP 121
Cdd:COG3451   194 VFFDFHDGLD-----NGNTLILGPSGSGKSFLLKLLLLQLLRYGARIVIFDPGGSYEILVRALGGTYIDLsPGSPTGLNP 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 122 FvevegapnGLLARELNSEMATYVISVALGR---RPTEIEHLAISEALNEISRGVD------FFKLRSCLEKIDRSGgpt 192
Cdd:COG3451   269 F--------DLEDTEEKRDFLLELLELLLGRegePLTPEERAAIDRAVRALYRRADpeerttLSDLYELLKEQPEAK--- 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 193 twrgsysigslaSLLAVLDSLIESGLVAQ---SESSFDLGKvlgKSILVFDLSGLFGSGRyplvvalllgaLRA------ 263
Cdd:COG3451   338 ------------DLAARLEPYTKGGSYGWlfdGPTNLDLSD---ARFVVFDLTELLDNPE-----------LRPpvllyl 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 264 -----HKMTRDLP--PLIIAIDEIWALMSDSNIASWLGSYWKLSRGIGIANIGVSHRLSDFSGgddvgahlksqslnsst 336
Cdd:COG3451   392 lhriwNRLRKNNDgrPTLIVIDEAWLLLDNPAFAEFLEEWLKTLRKYNGAVIFATQSVEDFLS----------------- 454
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 337 nysngpnrtviSEINRglGMINDTETIVSFALEVDEAHHLCSAFGFSLEVAPLLRQLRKGS--ALWKIGERNLLVDHYLT 414
Cdd:COG3451   455 -----------SPIAE--AIIENSATKILLPQPKADIEDYAELLGLSERELELIRSAGRGKrdFLIKQGNGSVVFRLDLS 521
                         410
                  ....*....|.
gi 1959262027 415 SIETALFNTDA 425
Cdd:COG3451   522 PEELALLSTKP 532
DUF87 pfam01935
Helicase HerA, central domain; This entry represents the central domain found in archaeal ...
63-244 2.07e-04

Helicase HerA, central domain; This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.


Pssm-ID: 376671 [Multi-domain]  Cd Length: 220  Bit Score: 42.35  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027  63 VFGQVGKGKSALLKSYLARMFL-LGYPSVVFDPKGEYGALARFFGFDPIDYL-ASKRGVNPFVEVEGAPNGLLARELNSE 140
Cdd:pfam01935  28 ILGSTGSGKSNTVAVLLEELLEkKGATVLIFDPHGEYGTLFRDLGAENVNVItPDPELKINPWLLSPEDLADLLEELNLP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 141 MAT---YVISVALGR-RPTEIEHLAISEALNEISRgvdffKLRSCLEKIDRSggpttwrgsySIGSLASLLAVLDSLIES 216
Cdd:pfam01935 108 NAEvqrSILEEALDQlKSEELGKLSIDELIEKILE-----ELLTEAAELNKL----------SNDAIRRVLDKLERLLRS 172
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1959262027 217 GLVAQSESSF--DLGKVL--GKSILVFDLSGL 244
Cdd:pfam01935 173 GGLILTSTDIikLILDILskGGKVNIIDLSGV 204
 
Name Accession Description Interval E-value
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
43-425 1.99e-22

Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 99.64  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027  43 FGFNPFELYRdgvisNPNAFVFGQVGKGKSALLKSYLARMFLLGYPSVVFDPKGEYGALARFFGFDPIDY-LASKRGVNP 121
Cdd:COG3451   194 VFFDFHDGLD-----NGNTLILGPSGSGKSFLLKLLLLQLLRYGARIVIFDPGGSYEILVRALGGTYIDLsPGSPTGLNP 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 122 FvevegapnGLLARELNSEMATYVISVALGR---RPTEIEHLAISEALNEISRGVD------FFKLRSCLEKIDRSGgpt 192
Cdd:COG3451   269 F--------DLEDTEEKRDFLLELLELLLGRegePLTPEERAAIDRAVRALYRRADpeerttLSDLYELLKEQPEAK--- 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 193 twrgsysigslaSLLAVLDSLIESGLVAQ---SESSFDLGKvlgKSILVFDLSGLFGSGRyplvvalllgaLRA------ 263
Cdd:COG3451   338 ------------DLAARLEPYTKGGSYGWlfdGPTNLDLSD---ARFVVFDLTELLDNPE-----------LRPpvllyl 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 264 -----HKMTRDLP--PLIIAIDEIWALMSDSNIASWLGSYWKLSRGIGIANIGVSHRLSDFSGgddvgahlksqslnsst 336
Cdd:COG3451   392 lhriwNRLRKNNDgrPTLIVIDEAWLLLDNPAFAEFLEEWLKTLRKYNGAVIFATQSVEDFLS----------------- 454
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 337 nysngpnrtviSEINRglGMINDTETIVSFALEVDEAHHLCSAFGFSLEVAPLLRQLRKGS--ALWKIGERNLLVDHYLT 414
Cdd:COG3451   455 -----------SPIAE--AIIENSATKILLPQPKADIEDYAELLGLSERELELIRSAGRGKrdFLIKQGNGSVVFRLDLS 521
                         410
                  ....*....|.
gi 1959262027 415 SIETALFNTDA 425
Cdd:COG3451   522 PEELALLSTKP 532
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
58-244 8.94e-09

Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];


Pssm-ID: 440202 [Multi-domain]  Cd Length: 388  Bit Score: 56.92  E-value: 8.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027  58 NPNAFVFGQVGKGKSALLKSYLARMFLLGYPSVVFDPKGEYGALAR-FFGFDPIDYLASKRGVNPFVEvegaPNGLLARE 136
Cdd:COG0433    47 NRHILILGATGSGKSNTLQVLLEELSRAGVPVLVFDPHGEYSGLAEpGAERADVGVFDPGAGRPLPIN----PWDLFATA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 137 lnSEMATYVISV-ALGRRPTEIEHLAISEALNEISRGVDFFKLRSCLEKIDRSGgptTWRGSYSIGSLASLLAVLDSLIE 215
Cdd:COG0433   123 --SELGPLLLSRlDLNDTQRGVLREALRLADDKGLLLLDLKDLIALLEEGEELG---EEYGNVSAASAGALLRRLESLES 197
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1959262027 216 SGLVAqSESSFDLGKVLGKS--ILVFDLSGL 244
Cdd:COG0433   198 ADGLF-GEPGLDLEDLLRTDgrVTVIDLSGL 227
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
60-242 2.89e-05

Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442728 [Multi-domain]  Cd Length: 402  Bit Score: 46.13  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027  60 NAFVFGQVGKGKSALLKSYLARMFLLGYPSVVFDPKGEY----GALARFFG-----FDPIDYLASKRgVNPFVEVEGAPN 130
Cdd:COG3505     1 HVLVIGPTGSGKTVGLVIPNLTQLARGESVVVTDPKGDLaeltAGFRRRAGydvyvFDPFDPERSHR-WNPLDEIRDPAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 131 gllARELnsemATYVISVALGRRPTE--------------IEHLAISEA--LNEISRGV--DFFKLRSCLEKIDRSGGPT 192
Cdd:COG3505    80 ---AQEL----AEALIPALGGGGGGDpfwreaarallaalILALAEEGRrtLADVYRLLsePEEELRELLEALPESPHPP 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1959262027 193 ---TWRGSYS---------IGSLASLLAVLDslieSGLVAQ--SESSFDLGKVL-GKSILVFDLS 242
Cdd:COG3505   153 vadTLAAFLNaaektrssvLSTLASALELLS----DPEVAAltSGSDFDLRDLIrEKGTLYLVLP 213
DUF87 pfam01935
Helicase HerA, central domain; This entry represents the central domain found in archaeal ...
63-244 2.07e-04

Helicase HerA, central domain; This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.


Pssm-ID: 376671 [Multi-domain]  Cd Length: 220  Bit Score: 42.35  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027  63 VFGQVGKGKSALLKSYLARMFL-LGYPSVVFDPKGEYGALARFFGFDPIDYL-ASKRGVNPFVEVEGAPNGLLARELNSE 140
Cdd:pfam01935  28 ILGSTGSGKSNTVAVLLEELLEkKGATVLIFDPHGEYGTLFRDLGAENVNVItPDPELKINPWLLSPEDLADLLEELNLP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027 141 MAT---YVISVALGR-RPTEIEHLAISEALNEISRgvdffKLRSCLEKIDRSggpttwrgsySIGSLASLLAVLDSLIES 216
Cdd:pfam01935 108 NAEvqrSILEEALDQlKSEELGKLSIDELIEKILE-----ELLTEAAELNKL----------SNDAIRRVLDKLERLLRS 172
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1959262027 217 GLVAQSESSF--DLGKVL--GKSILVFDLSGL 244
Cdd:pfam01935 173 GGLILTSTDIikLILDILskGGKVNIIDLSGV 204
AAA_10 pfam12846
AAA-like domain; This family of domains contain a P-loop motif that is characteriztic of the ...
58-172 4.56e-04

AAA-like domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins, including VirB4 components of the Type IV secretory pathway and conjugal transfer protein TrbE. This entry includes the arcaheal Vir4/HerA homolog CedB, a membrane-bound protein that is highly induced upon UV treatment and essential for DNA transfer between Sulfolobus cells.


Pssm-ID: 315512 [Multi-domain]  Cd Length: 362  Bit Score: 42.00  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262027  58 NPNAFVFGQVGKGKSALLKSYLARMFLLGYPSVVFDPKGEYG-------ALARFFGFDPIDYLASKRGV-NPFVevegap 129
Cdd:pfam12846  21 APHSAIIGDLGGGKSVLNKTLFYYIVLLGGKALYIDPKKERGqwketlpEIAHEINFVTLDSETENHGLlDPIV------ 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1959262027 130 ngLLARELNSE-MATYVISVALGRRPTEIEHL-AISEALNEISRG 172
Cdd:pfam12846  95 --LLPREKEAEsTAIDILTNLTGDSSRDDEKFpALRKAVEAVTEG 137
 
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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