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Conserved domains on  [gi|1584727233|gb|QBH90594|]
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D1133L [African swine fever virus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13211647)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

CATH:  3.40.50.300
EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0004386|GO:0005524
PubMed:  20206133|20225155

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HELICc smart00490
helicase superfamily c-terminal domain;
596-672 9.36e-11

helicase superfamily c-terminal domain;


:

Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 58.76  E-value: 9.36e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1584727233   596 VRFTILHSEIEPAVRERSLALFNASSNleghqlRILIGSKVIVEGLNFQAVRYEMIMSLPLDIPRLIQVFGRVVRKN 672
Cdd:smart00490   12 IKVARLHGGLSQEEREEILDKFNNGKI------KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
 276-340 3.14e-04

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 cd18011:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 207  Bit Score: 43.05  E-value: 3.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584727233  276 GLLIADEIHNV---YNIQERNNYGIALQYVldafppHQAPRAVFMSATPVTGSVMEYVDLLNLLVPRH 340
Cdd:cd18011    122 DLVVVDEAHKLrnsGGGKETKRYKLGRLLA------KRARHVLLLTATPHNGKEEDFRALLSLLDPGR 183
 
Name Accession Description Interval E-value
HELICc smart00490
helicase superfamily c-terminal domain;
596-672 9.36e-11

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 58.76  E-value: 9.36e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1584727233   596 VRFTILHSEIEPAVRERSLALFNASSNleghqlRILIGSKVIVEGLNFQAVRYEMIMSLPLDIPRLIQVFGRVVRKN 672
Cdd:smart00490   12 IKVARLHGGLSQEEREEILDKFNNGKI------KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 525-672 7.81e-10

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 57.22  E-value: 7.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584727233  525 MKDILSIIRQGRG-KILIYHNRVRMsgvLILQEILQSNGIlnevsspvgttrcsicaairdehthsdhqfipvRFTILHS 603
Cdd:pfam00271    3 LEALLELLKKERGgKVLIFSQTKKT---LEAELLLEKEGI---------------------------------KVARLHG 46

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1584727233  604 EIEPAVRERSLALFNASSnleghqLRILIGSKVIVEGLNFQAVRYEMIMSLPLDIPRLIQVFGRVVRKN 672
Cdd:pfam00271   47 DLSQEEREEILEDFRKGK------IDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 276-340 3.14e-04

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 43.05  E-value: 3.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584727233  276 GLLIADEIHNV---YNIQERNNYGIALQYVldafppHQAPRAVFMSATPVTGSVMEYVDLLNLLVPRH 340
Cdd:cd18011    122 DLVVVDEAHKLrnsGGGKETKRYKLGRLLA------KRARHVLLLTATPHNGKEEDFRALLSLLDPGR 183
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
599-710 3.42e-04

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 44.63  E-value: 3.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584727233  599 TILHSEIEPAVRERSLALFNASsnleghQLRILIGSKVIVEGLNFQAVRYEMIMSlPLDIPRL-IQVFGRVVRKnshmel 677
Cdd:COG1061    333 AVVTGDTPKKEREEILEAFRDG------ELRILVTVDVLNEGVDVPRLDVAILLR-PTGSPREfIQRLGRGLRP------ 399

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1584727233  678 PPSERNVTIYLYVSTTPDGGPELAKYAQKLKEY 710
Cdd:COG1061    400 APGKEDALVYDFVGNDVPVLEELAKDLRDLAGY 432
 
Name Accession Description Interval E-value
HELICc smart00490
helicase superfamily c-terminal domain;
596-672 9.36e-11

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 58.76  E-value: 9.36e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1584727233   596 VRFTILHSEIEPAVRERSLALFNASSNleghqlRILIGSKVIVEGLNFQAVRYEMIMSLPLDIPRLIQVFGRVVRKN 672
Cdd:smart00490   12 IKVARLHGGLSQEEREEILDKFNNGKI------KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 525-672 7.81e-10

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 57.22  E-value: 7.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584727233  525 MKDILSIIRQGRG-KILIYHNRVRMsgvLILQEILQSNGIlnevsspvgttrcsicaairdehthsdhqfipvRFTILHS 603
Cdd:pfam00271    3 LEALLELLKKERGgKVLIFSQTKKT---LEAELLLEKEGI---------------------------------KVARLHG 46

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1584727233  604 EIEPAVRERSLALFNASSnleghqLRILIGSKVIVEGLNFQAVRYEMIMSLPLDIPRLIQVFGRVVRKN 672
Cdd:pfam00271   47 DLSQEEREEILEDFRKGK------IDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 276-340 3.14e-04

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 43.05  E-value: 3.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584727233  276 GLLIADEIHNV---YNIQERNNYGIALQYVldafppHQAPRAVFMSATPVTGSVMEYVDLLNLLVPRH 340
Cdd:cd18011    122 DLVVVDEAHKLrnsGGGKETKRYKLGRLLA------KRARHVLLLTATPHNGKEEDFRALLSLLDPGR 183
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
599-710 3.42e-04

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 44.63  E-value: 3.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584727233  599 TILHSEIEPAVRERSLALFNASsnleghQLRILIGSKVIVEGLNFQAVRYEMIMSlPLDIPRL-IQVFGRVVRKnshmel 677
Cdd:COG1061    333 AVVTGDTPKKEREEILEAFRDG------ELRILVTVDVLNEGVDVPRLDVAILLR-PTGSPREfIQRLGRGLRP------ 399

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1584727233  678 PPSERNVTIYLYVSTTPDGGPELAKYAQKLKEY 710
Cdd:COG1061    400 APGKEDALVYDFVGNDVPVLEELAKDLRDLAGY 432
 
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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