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Conserved domains on  [gi|585334195|ref|WP_024215845|]
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helicase HerA-like C-terminal domain-containing protein [Escherichia coli]

Protein Classification

helicase HerA-like C-terminal domain-containing protein( domain architecture ID 12067122)

helicase HerA-like C-terminal domain-containing protein, also known as DUF853 domain-containing protein, may be an ATP-binding protein; similar to Escherichia coli uncharacterized protein YjgR

Gene Ontology:  GO:0005524

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HerA_C pfam05872
Helicase HerA-like C-terminal; HerA is a DNA helicase able to utilize either 3' or 5' ...
 3-498 0e+00

Helicase HerA-like C-terminal; HerA is a DNA helicase 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 entry represents the C-terminal domain of HerA which seems to be involved in the conversion of ATP hydrolysis into DNA translocation.


:

Pssm-ID: 428657 [Multi-domain]  Cd Length: 503  Bit Score: 899.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195    3 EPLLIARTPDTELFLLPGMANRHGLITGATGTGKTVTLQKLAESLSEIGVPVFMADVKGDLTGIAQAGTASEKLLTRLKN 82
Cdd:pfam05872   1 EPLLGAGTPGQPLGLALKLANRHGLIAGATGTGKTVTLQTLAESFSDAGVPVFMADVKGDLSGIAAPGEPQDKLAARAAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195   83 IGVNDWQPHANPVVVWDIFGEKGHSVRATVSDLGPLLLARQLNLNDVQSGVLNIIFRIADDQGLLLLDFKDLRAITQYIG 162
Cdd:pfam05872  81 MGLDDYQPAAFPVIFWDLFGEKGHPVRATISEMGPLLLARLLNLNDTQEGVLNIAFRVADDEGLLLLDLKDLRALLTYVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  163 DNAKSFQNQYGNISSASVGAIQRGLLSLEQQGAAHFFGEPMLDIKDWMRTDTNGKGVINILSAEKLYQMPKLYAASLLWM 242
Cdd:pfam05872 161 DNAKELGNQYGNVSPASVGAIQRALLTLEQQGAEHFFGEPALDIEDLMRTDADGRGVISLLAADKLINAPKLYSTFLLWL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  243 LSELYEQLPEAGDLEKPKLVFFFDEAHLLFNDAPQVLLDKIEQVIRLIRSKGVGVWFVSQNPSDIPDNVLGQLGNRVQHA 322
Cdd:pfam05872 241 LSELFEQLPEVGDPDKPKLVFFFDEAHLLFNDAPKALLDKVEQVVRLIRSKGVGVYFVTQNPLDLPDTVLGQLGNRVQHA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  323 LRAFTPKDQKAVKAAAQTMRANPAFDTEKAIQELGTGEALISFLDAKGSPSVVERAMVIAPCSRMGPVTEDERNGLINHS 402
Cdd:pfam05872 321 LRAFTPRDQKAVKAAADTFRPNPAFDTEEAITSLGTGEALVSTLDEKGAPSIVQRTLVRPPASRIGPLTDEERAALVAAS 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  403 PVYGKYEDDVDRESAYEMLQKGVQASTEQQKNPPTKGkEVAVDDGILGGLKDILFGT----TGPRGGKKDGVVQTMAKSA 478
Cdd:pfam05872 401 PVAGVYDQPIDRESAYEMLAGKAAAAAEAQAQAPAEQ-EKGGRSGLLGGLDDTALGPmpakVGPRGGKRETVVEALAKSA 479

                         490       500
                  ....*....|....*....|....
gi 585334195  479 AR----QVTNQIVRGMLGSLLGGR 498
Cdd:pfam05872 480 VRsvasQVGREIVRGILGSLLRKR 503
 
Name Accession Description Interval E-value
HerA_C pfam05872
Helicase HerA-like C-terminal; HerA is a DNA helicase able to utilize either 3' or 5' ...
 3-498 0e+00

Helicase HerA-like C-terminal; HerA is a DNA helicase 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 entry represents the C-terminal domain of HerA which seems to be involved in the conversion of ATP hydrolysis into DNA translocation.


Pssm-ID: 428657 [Multi-domain]  Cd Length: 503  Bit Score: 899.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195    3 EPLLIARTPDTELFLLPGMANRHGLITGATGTGKTVTLQKLAESLSEIGVPVFMADVKGDLTGIAQAGTASEKLLTRLKN 82
Cdd:pfam05872   1 EPLLGAGTPGQPLGLALKLANRHGLIAGATGTGKTVTLQTLAESFSDAGVPVFMADVKGDLSGIAAPGEPQDKLAARAAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195   83 IGVNDWQPHANPVVVWDIFGEKGHSVRATVSDLGPLLLARQLNLNDVQSGVLNIIFRIADDQGLLLLDFKDLRAITQYIG 162
Cdd:pfam05872  81 MGLDDYQPAAFPVIFWDLFGEKGHPVRATISEMGPLLLARLLNLNDTQEGVLNIAFRVADDEGLLLLDLKDLRALLTYVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  163 DNAKSFQNQYGNISSASVGAIQRGLLSLEQQGAAHFFGEPMLDIKDWMRTDTNGKGVINILSAEKLYQMPKLYAASLLWM 242
Cdd:pfam05872 161 DNAKELGNQYGNVSPASVGAIQRALLTLEQQGAEHFFGEPALDIEDLMRTDADGRGVISLLAADKLINAPKLYSTFLLWL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  243 LSELYEQLPEAGDLEKPKLVFFFDEAHLLFNDAPQVLLDKIEQVIRLIRSKGVGVWFVSQNPSDIPDNVLGQLGNRVQHA 322
Cdd:pfam05872 241 LSELFEQLPEVGDPDKPKLVFFFDEAHLLFNDAPKALLDKVEQVVRLIRSKGVGVYFVTQNPLDLPDTVLGQLGNRVQHA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  323 LRAFTPKDQKAVKAAAQTMRANPAFDTEKAIQELGTGEALISFLDAKGSPSVVERAMVIAPCSRMGPVTEDERNGLINHS 402
Cdd:pfam05872 321 LRAFTPRDQKAVKAAADTFRPNPAFDTEEAITSLGTGEALVSTLDEKGAPSIVQRTLVRPPASRIGPLTDEERAALVAAS 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  403 PVYGKYEDDVDRESAYEMLQKGVQASTEQQKNPPTKGkEVAVDDGILGGLKDILFGT----TGPRGGKKDGVVQTMAKSA 478
Cdd:pfam05872 401 PVAGVYDQPIDRESAYEMLAGKAAAAAEAQAQAPAEQ-EKGGRSGLLGGLDDTALGPmpakVGPRGGKRETVVEALAKSA 479

                         490       500
                  ....*....|....*....|....
gi 585334195  479 AR----QVTNQIVRGMLGSLLGGR 498
Cdd:pfam05872 480 VRsvasQVGREIVRGILGSLLRKR 503
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
 2-388 6.46e-119

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: 354.30  E-value: 6.46e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195   2 SEPLLIAR--TPDTELFL-LPGMANRHGLITGATGTGKTVTLQKLAESLSEIGVPVFMADVKGDLTGIAQAGTASEKllt 78
Cdd:COG0433   23 GGGILIGKllSPGVPVYLdLDKLLNRHILILGATGSGKSNTLQVLLEELSRAGVPVLVFDPHGEYSGLAEPGAERAD--- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  79 rlknigVNDWQPHAN---PVVVWDIFgekghsvrATVSDLGPLLLARqLNLNDVQSGVLNIIFRIADDQGLLLLDFKDLR 155
Cdd:COG0433  100 ------VGVFDPGAGrplPINPWDLF--------ATASELGPLLLSR-LDLNDTQRGVLREALRLADDKGLLLLDLKDLI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195 156 AitqYIGDNAKsFQNQYGNISSASVGAIQRGLLSLEQqgAAHFFGEPMLDIKDWMRTDTNgkgvINILSAEKLyqMPKLY 235
Cdd:COG0433  165 A---LLEEGEE-LGEEYGNVSAASAGALLRRLESLES--ADGLFGEPGLDLEDLLRTDGR----VTVIDLSGL--PEELQ 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195 236 AASLLWMLSELYEQLPEAGDLE--KPKLVFFFDEAHLLFNDAPQVLLDKIEQVIRLIRSKGVGVWFVSQNPSDIPDNVLG 313
Cdd:COG0433  233 STFVLWLLRELFEARPEVGDADdrKLPLVLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPSDIDEDVLS 312

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585334195 314 QLGNrvQHALRAFTPKDQKAVKAAAQTMranpAFDTEKAIQELGTGEALISfLDAKGSPSVVERAMviaPCSRMG 388
Cdd:COG0433  313 QLGT--QIILRLFNPRDQKAVKAAAETL----SEDLLERLPSLGTGEALVL-GEGIPLPVLVKIRL---PESRPG 377
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
 198-307 2.41e-07

TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also 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.


Pssm-ID: 410871 [Multi-domain]  Cd Length: 144  Bit Score: 49.91  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195 198 FFGEPMLDIkdWMR------TDTNGKGVINILSAEKlyQMPKLYAASLLWMLSELYEQLPEAGDLEKPKLVFFFDEAHLL 271
Cdd:cd01127   15 SIVIPLLDQ--AARggsviiTDPKGELFLVIPDRDD--SFAALRALFFNQLFRALTELASLSPGRLPRRVWFILDEFANL 90

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 585334195 272 fndapqVLLDKIEQVIRLIRSKGVGVWFVSQNPSDI 307
Cdd:cd01127   91 ------GRIPNLPNLLATGRKRGISVVLILQSLAQL 120
cdc6 PRK00411
ORC1-type DNA replication protein;
27-54 4.82e-03

ORC1-type DNA replication protein;


Pssm-ID: 234751 [Multi-domain]  Cd Length: 394  Bit Score: 39.45  E-value: 4.82e-03
                         10        20
                 ....*....|....*....|....*...
gi 585334195  27 LITGATGTGKTVTLQKLAESLSEIGVPV 54
Cdd:PRK00411  59 LIYGPPGTGKTTTVKKVFEELEEIAVKV 86
 
Name Accession Description Interval E-value
HerA_C pfam05872
Helicase HerA-like C-terminal; HerA is a DNA helicase able to utilize either 3' or 5' ...
 3-498 0e+00

Helicase HerA-like C-terminal; HerA is a DNA helicase 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 entry represents the C-terminal domain of HerA which seems to be involved in the conversion of ATP hydrolysis into DNA translocation.


Pssm-ID: 428657 [Multi-domain]  Cd Length: 503  Bit Score: 899.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195    3 EPLLIARTPDTELFLLPGMANRHGLITGATGTGKTVTLQKLAESLSEIGVPVFMADVKGDLTGIAQAGTASEKLLTRLKN 82
Cdd:pfam05872   1 EPLLGAGTPGQPLGLALKLANRHGLIAGATGTGKTVTLQTLAESFSDAGVPVFMADVKGDLSGIAAPGEPQDKLAARAAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195   83 IGVNDWQPHANPVVVWDIFGEKGHSVRATVSDLGPLLLARQLNLNDVQSGVLNIIFRIADDQGLLLLDFKDLRAITQYIG 162
Cdd:pfam05872  81 MGLDDYQPAAFPVIFWDLFGEKGHPVRATISEMGPLLLARLLNLNDTQEGVLNIAFRVADDEGLLLLDLKDLRALLTYVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  163 DNAKSFQNQYGNISSASVGAIQRGLLSLEQQGAAHFFGEPMLDIKDWMRTDTNGKGVINILSAEKLYQMPKLYAASLLWM 242
Cdd:pfam05872 161 DNAKELGNQYGNVSPASVGAIQRALLTLEQQGAEHFFGEPALDIEDLMRTDADGRGVISLLAADKLINAPKLYSTFLLWL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  243 LSELYEQLPEAGDLEKPKLVFFFDEAHLLFNDAPQVLLDKIEQVIRLIRSKGVGVWFVSQNPSDIPDNVLGQLGNRVQHA 322
Cdd:pfam05872 241 LSELFEQLPEVGDPDKPKLVFFFDEAHLLFNDAPKALLDKVEQVVRLIRSKGVGVYFVTQNPLDLPDTVLGQLGNRVQHA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  323 LRAFTPKDQKAVKAAAQTMRANPAFDTEKAIQELGTGEALISFLDAKGSPSVVERAMVIAPCSRMGPVTEDERNGLINHS 402
Cdd:pfam05872 321 LRAFTPRDQKAVKAAADTFRPNPAFDTEEAITSLGTGEALVSTLDEKGAPSIVQRTLVRPPASRIGPLTDEERAALVAAS 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  403 PVYGKYEDDVDRESAYEMLQKGVQASTEQQKNPPTKGkEVAVDDGILGGLKDILFGT----TGPRGGKKDGVVQTMAKSA 478
Cdd:pfam05872 401 PVAGVYDQPIDRESAYEMLAGKAAAAAEAQAQAPAEQ-EKGGRSGLLGGLDDTALGPmpakVGPRGGKRETVVEALAKSA 479

                         490       500
                  ....*....|....*....|....
gi 585334195  479 AR----QVTNQIVRGMLGSLLGGR 498
Cdd:pfam05872 480 VRsvasQVGREIVRGILGSLLRKR 503
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
 2-388 6.46e-119

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: 354.30  E-value: 6.46e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195   2 SEPLLIAR--TPDTELFL-LPGMANRHGLITGATGTGKTVTLQKLAESLSEIGVPVFMADVKGDLTGIAQAGTASEKllt 78
Cdd:COG0433   23 GGGILIGKllSPGVPVYLdLDKLLNRHILILGATGSGKSNTLQVLLEELSRAGVPVLVFDPHGEYSGLAEPGAERAD--- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  79 rlknigVNDWQPHAN---PVVVWDIFgekghsvrATVSDLGPLLLARqLNLNDVQSGVLNIIFRIADDQGLLLLDFKDLR 155
Cdd:COG0433  100 ------VGVFDPGAGrplPINPWDLF--------ATASELGPLLLSR-LDLNDTQRGVLREALRLADDKGLLLLDLKDLI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195 156 AitqYIGDNAKsFQNQYGNISSASVGAIQRGLLSLEQqgAAHFFGEPMLDIKDWMRTDTNgkgvINILSAEKLyqMPKLY 235
Cdd:COG0433  165 A---LLEEGEE-LGEEYGNVSAASAGALLRRLESLES--ADGLFGEPGLDLEDLLRTDGR----VTVIDLSGL--PEELQ 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195 236 AASLLWMLSELYEQLPEAGDLE--KPKLVFFFDEAHLLFNDAPQVLLDKIEQVIRLIRSKGVGVWFVSQNPSDIPDNVLG 313
Cdd:COG0433  233 STFVLWLLRELFEARPEVGDADdrKLPLVLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPSDIDEDVLS 312

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585334195 314 QLGNrvQHALRAFTPKDQKAVKAAAQTMranpAFDTEKAIQELGTGEALISfLDAKGSPSVVERAMviaPCSRMG 388
Cdd:COG0433  313 QLGT--QIILRLFNPRDQKAVKAAAETL----SEDLLERLPSLGTGEALVL-GEGIPLPVLVKIRL---PESRPG 377
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
 23-314 4.11e-15

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


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 77.68  E-value: 4.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  23 NRHGLITGATGTGKTVTLQKLAESLSEIGVPVFMADVKGDLTGIAQA--GTASEklLTRLKNIGVNdwqphanPVVVWDI 100
Cdd:COG3451  204 NGNTLILGPSGSGKSFLLKLLLLQLLRYGARIVIFDPGGSYEILVRAlgGTYID--LSPGSPTGLN-------PFDLEDT 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195 101 FGEkghsvRATVSDLGPLLLARQ-LNLNDVQSGVL----NIIFRIADDQgllllDFKDLRAITQYIGDNAKSfqnqygni 175
Cdd:COG3451  275 EEK-----RDFLLELLELLLGREgEPLTPEERAAIdravRALYRRADPE-----ERTTLSDLYELLKEQPEA-------- 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195 176 ssasvGAIQRGLLSLEQQGA-AHFF-GEPMLDIKDwmrtdtngkGVINILSAEKLYQMPKLYAASLLWMLSELYEQLPEA 253
Cdd:COG3451  337 -----KDLAARLEPYTKGGSyGWLFdGPTNLDLSD---------ARFVVFDLTELLDNPELRPPVLLYLLHRIWNRLRKN 402

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 585334195 254 GDlEKPKLVFFfDEAHLLFNDapQVLLDKIEQVIRLIRSKGVGVWFVSQNPSDIPDNVLGQ 314
Cdd:COG3451  403 ND-GRPTLIVI-DEAWLLLDN--PAFAEFLEEWLKTLRKYNGAVIFATQSVEDFLSSPIAE 459
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
 25-332 4.17e-13

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: 70.78  E-value: 4.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195  25 HGLITGATGTGKTVTLQKLAesLSEI--GVPVFMADVKGDLTgiaqagtasEKLLTRLKNIGvndwqphaNPVVVWDiFG 102
Cdd:COG3505    1 HVLVIGPTGSGKTVGLVIPN--LTQLarGESVVVTDPKGDLA---------ELTAGFRRRAG--------YDVYVFD-PF 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195 103 EKGHSVR----ATVSDLG-PLLLARQLNLNDVQSGVLNIIFRIADDQ---GLLLL----DFKDLRAITQYIGDNAKSFQN 170
Cdd:COG3505   61 DPERSHRwnplDEIRDPAdAQELAEALIPALGGGGGGDPFWREAARAllaALILAlaeeGRRTLADVYRLLSEPEEELRE 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195 171 QYGNISSASVGAIQRGLLSLEQ-------------QGAAHFFGEPML---------DIKDWMRtdtnGKGVINILSAEKL 228
Cdd:COG3505  141 LLEALPESPHPPVADTLAAFLNaaektrssvlstlASALELLSDPEVaaltsgsdfDLRDLIR----EKGTLYLVLPPDD 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195 229 YQMPKLYAASLLWML-SELYEQLPEAGDLeKPKLVFFFDEAHLLfndapqVLLDKIEQVIRLIRSKGVGVWFVSQNPSDI 307
Cdd:COG3505  217 LSTLAPLLRLLLSQLiRALLRRAERSGRL-PRPVLLLLDEFANL------GRLPSLETLLATGRGYGIRLVLILQSLAQL 289

                        330       340       350
                 ....*....|....*....|....*....|...
gi 585334195 308 PD--------NVLGQLGNRVqhalrAFTPKDQK 332
Cdd:COG3505  290 EAiygeegaeTILGNCGTKI-----FLGVNDPE 317
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
 198-307 2.41e-07

TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also 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.


Pssm-ID: 410871 [Multi-domain]  Cd Length: 144  Bit Score: 49.91  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195 198 FFGEPMLDIkdWMR------TDTNGKGVINILSAEKlyQMPKLYAASLLWMLSELYEQLPEAGDLEKPKLVFFFDEAHLL 271
Cdd:cd01127   15 SIVIPLLDQ--AARggsviiTDPKGELFLVIPDRDD--SFAALRALFFNQLFRALTELASLSPGRLPRRVWFILDEFANL 90

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 585334195 272 fndapqVLLDKIEQVIRLIRSKGVGVWFVSQNPSDI 307
Cdd:cd01127   91 ------GRIPNLPNLLATGRKRGISVVLILQSLAQL 120
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 8-69 1.37e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 40.54  E-value: 1.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585334195   8 ARTPDTELF------------LLPGMANRHG--LITGATGTGKTVTLQKLAESLSEIGVPVFMADVKGDLTGIAQA 69
Cdd:COG3267   14 SLTPDPRFLflspshrealarLEYALAQGGGfvVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNPQLSPAELLRA 89
DUF87 pfam01935
Helicase HerA, central domain; This entry represents the central domain found in archaeal ...
 18-154 2.11e-03

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: 39.66  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585334195   18 LPGMANRHGLITGATGTGKTVTLQKLAESLSE-IGVPVFMADVKGDLTGIAQAGTASE-KLLTRLKNIGVNdwqphanpv 95
Cdd:pfam01935  18 VNKLVSRHFAILGSTGSGKSNTVAVLLEELLEkKGATVLIFDPHGEYGTLFRDLGAENvNVITPDPELKIN--------- 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 585334195   96 vVWDIfgekghsvraTVSDLGPLLLARQLNLNDVQSGVLNIIFRIADDQGLLLLDFKDL 154
Cdd:pfam01935  89 -PWLL----------SPEDLADLLEELNLPNAEVQRSILEEALDQLKSEELGKLSIDEL 136
AAA_22 pfam13401
AAA domain;
24-62 2.52e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 2.52e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 585334195   24 RHGLITGATGTGKTVTLQKLAESLSEIGVPVFMADVKGD 62
Cdd:pfam13401   6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSG 44
cdc6 PRK00411
ORC1-type DNA replication protein;
27-54 4.82e-03

ORC1-type DNA replication protein;


Pssm-ID: 234751 [Multi-domain]  Cd Length: 394  Bit Score: 39.45  E-value: 4.82e-03
                         10        20
                 ....*....|....*....|....*...
gi 585334195  27 LITGATGTGKTVTLQKLAESLSEIGVPV 54
Cdd:PRK00411  59 LIYGPPGTGKTTTVKKVFEELEEIAVKV 86
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 27-82 5.05e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 37.51  E-value: 5.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 585334195  27 LITGATGTGKTVTLQKLAESLSEIGVPVF---MADVKGDLTGIAQAGTASEKLLTRLKN 82
Cdd:cd00009   23 LLYGPPGTGKTTLARAIANELFRPGAPFLylnASDLLEGLVVAELFGHFLVRLLFELAE 81
TrwB_AAD_bind pfam10412
Type IV secretion-system coupling protein DNA-binding domain; The plasmid conjugative coupling ...
 4-65 5.97e-03

Type IV secretion-system coupling protein DNA-binding domain; The plasmid conjugative coupling protein TrwB forms hexamers from six structurally very similar protomers. This hexamer contains a central channel running from the cytosolic pole (made up by the AADs) to the membrane pole ending at the transmembrane pore shaped by 12 transmembrane helices, rendering an overall mushroom-like structure. The TrwB_AAD (all-alpha domain) domain appears to be the DNA-binding domain of the structure. TrwB, a basic integral inner-membrane nucleoside-triphosphate-binding protein, is the structural prototype for the type IV secretion system coupling proteins, a family of proteins essential for macromolecular transport between cells and export.


Pssm-ID: 431268 [Multi-domain]  Cd Length: 386  Bit Score: 38.82  E-value: 5.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585334195    4 PLLIARTPdtelfLLPGMANRHGLITGATGTGKTVTLQKLAESLSEIGVPVFMADVKGDLTG 65
Cdd:pfam10412   1 RYTIAGVP-----LPKRSETRHTLIIGTTGSGKTQALRGLLDQARARGDRAIIFDLTGAFTE 57
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
 25-63 8.09e-03

TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also 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.


Pssm-ID: 410871 [Multi-domain]  Cd Length: 144  Bit Score: 36.81  E-value: 8.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 585334195  25 HGLITGATGTGKTVTLQKLAESLSEIGVPVFMADVKGDL 63
Cdd:cd01127    1 NTLVLGTTGSGKTTSIVIPLLDQAARGGSVIITDPKGEL 39
 
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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