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Conserved domains on  [gi|512057744|gb|EPD57231|]
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hypothetical protein HMPREF1211_06961 [Streptomyces sp. HGB0020]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
 446-495 9.60e-08

N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.


The actual alignment was detected with superfamily member pfam12696:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 125  Bit Score: 50.73  E-value: 9.60e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 512057744  446 PLTLVLDDVAAVAPLPQLPELLATGAERGLPTLALLRSREQGRSRWPHDE 495
Cdd:pfam12696   1 PVLFVLDEFANLGKIPDLEKLISTGRSRGISLMLILQSIAQLEELYGKDG 50
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
 398-491 1.33e-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: 50.68  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057744 398 GTLYVVGESIEDPRTnpgamPLLTALVASVVERGRHMAeRSSSGRLDPPLTLVLDDVAAVAPLPQLPELLATGAERGLPT 477
Cdd:cd01127   37 GELFLVIPDRDDSFA-----ALRALFFNQLFRALTELA-SLSPGRLPRRVWFILDEFANLGRIPNLPNLLATGRKRGISV 110

                         90
                 ....*....|....
gi 512057744 478 LALLRSREQGRSRW 491
Cdd:cd01127  111 VLILQSLAQLEAVY 124
PHA03269 super family cl29788
envelope glycoprotein C; Provisional
 127-177 1.16e-03

envelope glycoprotein C; Provisional


The actual alignment was detected with superfamily member PHA03269:

Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 41.64  E-value: 1.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 512057744 127 APTP--FEKPAPSPLPSLTQEPQPAPEPLATQHEVPTPRtaPPEPPTTVPDRE 177
Cdd:PHA03269  73 APTPaaSEKFDPAPAPHQAASRAPDPAVAPQLAAAPKPD--AAEAFTSAAQAH 123
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
125-233 2.15e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14950:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 585  Bit Score: 40.56  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057744 125 RTAPTPFEKPAPSPLPSLtqePQPAPEPLATQHEVPTPRTAPPEP----PTTVPDREATAPLF----SSEPLAGGQEKIV 196
Cdd:PRK14950 363 VPAPQPAKPTAAAPSPVR---PTPAPSTRPKAAAAANIPPKEPVRetatPPPVPPRPVAPPVPhtpeSAPKLTRAAIPVD 439

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 512057744 197 VGPRDSRQATATQAVRDAEGPALVITSNPAVWSDTKD 233
Cdd:PRK14950 440 EKPKYTPPAPPKEEEKALIADGDVLEQLEAIWKQILR 476
 
Name Accession Description Interval E-value
TraG-D_C pfam12696
TraM recognition site of TraD and TraG; This family includes both TraG and TraD as well as ...
 446-495 9.60e-08

TraM recognition site of TraD and TraG; This family includes both TraG and TraD as well as VirD4 proteins. TraG is essential for DNA transfer in bacterial conjugation. These proteins are thought to mediate interactions between the DNA-processing (Dtr) and the mating pair formation (Mpf) systems. This domain interacts with the relaxosome component TraM via the latter's tetramerization domain. TraD is a hexameric ring ATPase that forms the cytoplasmic face of the conjugative pore.


Pssm-ID: 432726 [Multi-domain]  Cd Length: 125  Bit Score: 50.73  E-value: 9.60e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 512057744  446 PLTLVLDDVAAVAPLPQLPELLATGAERGLPTLALLRSREQGRSRWPHDE 495
Cdd:pfam12696   1 PVLFVLDEFANLGKIPDLEKLISTGRSRGISLMLILQSIAQLEELYGKDG 50
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
 398-491 1.33e-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: 50.68  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057744 398 GTLYVVGESIEDPRTnpgamPLLTALVASVVERGRHMAeRSSSGRLDPPLTLVLDDVAAVAPLPQLPELLATGAERGLPT 477
Cdd:cd01127   37 GELFLVIPDRDDSFA-----ALRALFFNQLFRALTELA-SLSPGRLPRRVWFILDEFANLGRIPNLPNLLATGRKRGISV 110

                         90
                 ....*....|....
gi 512057744 478 LALLRSREQGRSRW 491
Cdd:cd01127  111 VLILQSLAQLEAVY 124
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 127-177 1.16e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 41.64  E-value: 1.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 512057744 127 APTP--FEKPAPSPLPSLTQEPQPAPEPLATQHEVPTPRtaPPEPPTTVPDRE 177
Cdd:PHA03269  73 APTPaaSEKFDPAPAPHQAASRAPDPAVAPQLAAAPKPD--AAEAFTSAAQAH 123
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 125-233 2.15e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.56  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057744 125 RTAPTPFEKPAPSPLPSLtqePQPAPEPLATQHEVPTPRTAPPEP----PTTVPDREATAPLF----SSEPLAGGQEKIV 196
Cdd:PRK14950 363 VPAPQPAKPTAAAPSPVR---PTPAPSTRPKAAAAANIPPKEPVRetatPPPVPPRPVAPPVPhtpeSAPKLTRAAIPVD 439

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 512057744 197 VGPRDSRQATATQAVRDAEGPALVITSNPAVWSDTKD 233
Cdd:PRK14950 440 EKPKYTPPAPPKEEEKALIADGDVLEQLEAIWKQILR 476
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 126-174 4.53e-03

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 39.47  E-value: 4.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 512057744  126 TAPTPFEKPAPSPLPSLTQEPQPAPePLATQHEVPTPRTAPPEPPTTVP 174
Cdd:TIGR01348 198 TAPAPASAQPAAQSPAATQPEPAAA-PAAAKAQAPAPQQAGTQNPAKVD 245
 
Name Accession Description Interval E-value
TraG-D_C pfam12696
TraM recognition site of TraD and TraG; This family includes both TraG and TraD as well as ...
 446-495 9.60e-08

TraM recognition site of TraD and TraG; This family includes both TraG and TraD as well as VirD4 proteins. TraG is essential for DNA transfer in bacterial conjugation. These proteins are thought to mediate interactions between the DNA-processing (Dtr) and the mating pair formation (Mpf) systems. This domain interacts with the relaxosome component TraM via the latter's tetramerization domain. TraD is a hexameric ring ATPase that forms the cytoplasmic face of the conjugative pore.


Pssm-ID: 432726 [Multi-domain]  Cd Length: 125  Bit Score: 50.73  E-value: 9.60e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 512057744  446 PLTLVLDDVAAVAPLPQLPELLATGAERGLPTLALLRSREQGRSRWPHDE 495
Cdd:pfam12696   1 PVLFVLDEFANLGKIPDLEKLISTGRSRGISLMLILQSIAQLEELYGKDG 50
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
 398-491 1.33e-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: 50.68  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057744 398 GTLYVVGESIEDPRTnpgamPLLTALVASVVERGRHMAeRSSSGRLDPPLTLVLDDVAAVAPLPQLPELLATGAERGLPT 477
Cdd:cd01127   37 GELFLVIPDRDDSFA-----ALRALFFNQLFRALTELA-SLSPGRLPRRVWFILDEFANLGRIPNLPNLLATGRKRGISV 110

                         90
                 ....*....|....
gi 512057744 478 LALLRSREQGRSRW 491
Cdd:cd01127  111 VLILQSLAQLEAVY 124
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 127-177 1.16e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 41.64  E-value: 1.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 512057744 127 APTP--FEKPAPSPLPSLTQEPQPAPEPLATQHEVPTPRtaPPEPPTTVPDRE 177
Cdd:PHA03269  73 APTPaaSEKFDPAPAPHQAASRAPDPAVAPQLAAAPKPD--AAEAFTSAAQAH 123
PRK11633 PRK11633
cell division protein DedD; Provisional
 127-178 1.89e-03

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 39.99  E-value: 1.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 512057744 127 APTPFEKPAPSPLPSLTqePQPAPEPLATQHEVPTPRTAPPEPPTTVPDREA 178
Cdd:PRK11633 100 EPAPVEPPKPKPVEKPK--PKPKPQQKVEAPPAPKPEPKPVVEEKAAPTGKA 149
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 125-233 2.15e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.56  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057744 125 RTAPTPFEKPAPSPLPSLtqePQPAPEPLATQHEVPTPRTAPPEP----PTTVPDREATAPLF----SSEPLAGGQEKIV 196
Cdd:PRK14950 363 VPAPQPAKPTAAAPSPVR---PTPAPSTRPKAAAAANIPPKEPVRetatPPPVPPRPVAPPVPhtpeSAPKLTRAAIPVD 439

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 512057744 197 VGPRDSRQATATQAVRDAEGPALVITSNPAVWSDTKD 233
Cdd:PRK14950 440 EKPKYTPPAPPKEEEKALIADGDVLEQLEAIWKQILR 476
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 126-174 4.53e-03

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 39.47  E-value: 4.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 512057744  126 TAPTPFEKPAPSPLPSLTQEPQPAPePLATQHEVPTPRTAPPEPPTTVP 174
Cdd:TIGR01348 198 TAPAPASAQPAAQSPAATQPEPAAA-PAAAKAQAPAPQQAGTQNPAKVD 245
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
127-221 4.70e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 39.37  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057744 127 APTPFEKPAPSPLPSL--TQEPQPAPEPLATQHEVPTPRTAPPEPPTTVPDrEATAPLFSSEPLAGGQEKIVVGPRDSRQ 204
Cdd:PRK14971 389 APQPSAAAAASPSPSQssAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNP-PSTAPQAVRPAQFKEEKKIPVSKVSSLG 467

                         90
                 ....*....|....*...
gi 512057744 205 ATATQAVRD-AEGPALVI 221
Cdd:PRK14971 468 PSTLRPIQEkAEQATGNI 485
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 126-213 4.99e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 39.49  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057744  126 TAPTPFEKPAPSPLPSLTQEPQPAPEPLATQHEVPTPRTAPPEPPTTVPDREATAPLFSSEPLAGGQEKIVVGPRDSRQA 205
Cdd:PRK12270   58 PAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEV 137


                  ....*....
gi 512057744  206 -TATqAVRD 213
Cdd:PRK12270  138 pTAT-SVRA 145
ENaC TIGR00859
sodium channel transporter; The Epithelial Na+ Channel (ENaC) Family (TC 1.A.06)The ENaC ...
 86-173 5.07e-03

sodium channel transporter; The Epithelial Na+ Channel (ENaC) Family (TC 1.A.06)The ENaC family consists of sodium channels from animals and has no recognizable homologues in other eukaryotes or bacteria. The vertebrate ENaC proteins from epithelial cells cluster tightly together on the phylogenetic tree: voltage-insensitive ENaC homologues are also found in the brain. Eleven sequenced C. elegans proteins, including the degenerins, are distantly related to the vertebrate proteins as well as to each other. At least some ofthese proteins form part of a mechano-transducing complex for touch sensitivity. Other members of the ENaC family, the acid-sensing ion channels, ASIC1-3,are homo- or hetero-oligomeric neuronal H+-gated channels that mediate pain sensation in response to tissue acidosis. The homologous Helix aspersa(FMRF-amide)-activated Na+ channel is the first peptide neurotransmitter-gated ionotropic receptor to be sequenced.Mammalian ENaC is important for the maintenance of Na+ balance and the regulation of blood pressure. Three homologous ENaC subunits, a, b and g, havebeen shown to assemble to form the highly Na+-selective channel.This model is designed from the vertebrate members of the ENaC family. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273304 [Multi-domain]  Cd Length: 595  Bit Score: 39.33  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057744   86 LSGYGLFWGLFIGQ--LMVLVVLTVF-------VMGTLARWRAVRLKRRTAP---TPFEKPAPSPLPslTQEPQPAPEPL 153
Cdd:TIGR00859 495 LSNLGGQMGLWMGAsvLCVLELLELIidlifitLLRLLWRFRKWWQRRRGPPyaePPEPVSADTPPS--LQLDDPPTFPS 572

                          90       100
                  ....*....|....*....|
gi 512057744  154 ATQHEVPTPRTAPPEPPTTV 173
Cdd:TIGR00859 573 ALPLPHASGLSLPGTPPPNY 592
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 137-182 9.56e-03

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 36.76  E-value: 9.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 512057744 137 SPLPSLTQEPQPAPEPLATQHEVPTPRTAPPEPPTTVPDREATAPL 182
Cdd:PRK05641  46 SAVQEQVPTPAPAPAPAVPSAPTPVAPAAPAPAPASAGENVVTAPM 91
 
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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