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Conserved domains on  [gi|1720430751|ref|XP_030100029|]
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ATP-dependent DNA helicase PIF1 isoform X1 [Mus musculus]

Protein Classification

DEAD/DEAH box helicase family protein( domain architecture ID 1000205)

DEAD/DEAH box helicase family protein such as a DEAD/DEAH box-containing ATP-dependent helicase, which catalyzes the unwinding of DNA or RNA

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 ...
216-513 1.80e-108

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 pfam05970:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 361  Bit Score: 332.42  E-value: 1.80e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 216 LSEEQAAVLRMVL------KGQSIFFTGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAACHI-GGTTLHAFAGIGSG 286
Cdd:pfam05970   1 LNDEQKKVFDAIIesvinnKGGVFFVYGYGGTGKTFLWKAIITSLRSEGkiVLAVASSGVAALLLpGGRTAHSRFGIPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 287 QAPLAQCmALANRPGVRQGWLNCQRLVIDEISMVEADFFDKLEAVARAVRQQK--KPFGGIQLIICGDFLQLPPVT-KGS 363
Cdd:pfam05970  81 IDELSTC-KIKRGSKLAELLEKTSLIVWDEAPMTHRHCFEALDRTLRDILSETddKPFGGKTVVLGGDFRQILPVIpKGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 364 QQPQFCF---QAKSWRRCVpvILELTEVWRQAD-----------QTFISLLQAVRLGRCSDEVTRQ-------------- 415
Cdd:pfam05970 160 RPEIVNAsitNSYLWKHVK--VLELTKNMRLLAdsldqteakelQDFSDWLLAIGDGKINDENEREqlidipidillntg 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 416 ---LRATAAHKVGRdgIVA-----------TRLCTHQDDVALTNEKWLKALPGDVHSFEAIDS--------------DPE 467
Cdd:pfam05970 238 gdpIEAIVSEVYPD--ILQnstdpnyleerAILCPTNEDVDEINNYRLSQLPGEEKEYLSSDSisksdndseidalyPTE 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1720430751 468 LSRTLDAQCPVSRVLQLKLGAQVMLVKNLAVSRGLVNGARGVVVGF 513
Cdd:pfam05970 316 FLNSLNANGLPNHVLKLKVGAPVMLLRNLDQSRGLCNGTRLIVTQL 361
 
Name Accession Description Interval E-value
PIF1 pfam05970
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits ...
216-513 1.80e-108

PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits telomerase activity and is cell cycle regulated. This family includes a large number of largely uncharacterized plant proteins. This family includes a P-loop motif that is involved in nucleotide binding.


Pssm-ID: 428699 [Multi-domain]  Cd Length: 361  Bit Score: 332.42  E-value: 1.80e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 216 LSEEQAAVLRMVL------KGQSIFFTGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAACHI-GGTTLHAFAGIGSG 286
Cdd:pfam05970   1 LNDEQKKVFDAIIesvinnKGGVFFVYGYGGTGKTFLWKAIITSLRSEGkiVLAVASSGVAALLLpGGRTAHSRFGIPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 287 QAPLAQCmALANRPGVRQGWLNCQRLVIDEISMVEADFFDKLEAVARAVRQQK--KPFGGIQLIICGDFLQLPPVT-KGS 363
Cdd:pfam05970  81 IDELSTC-KIKRGSKLAELLEKTSLIVWDEAPMTHRHCFEALDRTLRDILSETddKPFGGKTVVLGGDFRQILPVIpKGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 364 QQPQFCF---QAKSWRRCVpvILELTEVWRQAD-----------QTFISLLQAVRLGRCSDEVTRQ-------------- 415
Cdd:pfam05970 160 RPEIVNAsitNSYLWKHVK--VLELTKNMRLLAdsldqteakelQDFSDWLLAIGDGKINDENEREqlidipidillntg 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 416 ---LRATAAHKVGRdgIVA-----------TRLCTHQDDVALTNEKWLKALPGDVHSFEAIDS--------------DPE 467
Cdd:pfam05970 238 gdpIEAIVSEVYPD--ILQnstdpnyleerAILCPTNEDVDEINNYRLSQLPGEEKEYLSSDSisksdndseidalyPTE 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1720430751 468 LSRTLDAQCPVSRVLQLKLGAQVMLVKNLAVSRGLVNGARGVVVGF 513
Cdd:pfam05970 316 FLNSLNANGLPNHVLKLKVGAPVMLLRNLDQSRGLCNGTRLIVTQL 361
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
219-390 9.01e-88

DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350795 [Multi-domain]  Cd Length: 183  Bit Score: 272.20  E-value: 9.01e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 219 EQAAVLRMVLKGQSIFFTGSAGTGKSYLLKHILGSLP--PTGTVATASTGVAACHIGGTTLHAFAGIGSGQAPLAQC-MA 295
Cdd:cd18037     1 EQRRVLDLVLDGKNVFFTGSAGTGKSYLLRRIIRALPsrPKRVAVTASTGIAACNIGGTTLHSFAGIGLGSEPAEDLlER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 296 LANRPGVRQGWLNCQRLVIDEISMVEADFFDKLEAVARAVRQQKKPFGGIQLIICGDFLQLPPVTKGSQQP--------Q 367
Cdd:cd18037    81 VKRSPYLVQRWRKCDVLIIDEISMLDADLFDKLDRVAREVRGSDKPFGGIQLILCGDFLQLPPVTKNSERQafffrgdqQ 160
                         170       180
                  ....*....|....*....|...
gi 1720430751 368 FCFQAKSWRRCVPVILELTEVWR 390
Cdd:cd18037   161 FCFEAKSWERCIFLTVELTKVFR 183
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
210-567 5.27e-41

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 156.68  E-value: 5.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 210 PSTKPKLSEEQAAVLRMVLKGQSIFF-TGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAA------CHIGGTTLHAF 280
Cdd:COG0507   119 PRAGITLSDEQREAVALALTTRRVSVlTGGAGTGKTTTLRALLAALEALGlrVALAAPTGKAAkrlsesTGIEARTIHRL 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 281 AGIGSGQAPLaqcmalanRPGVRQGWLNCQRLVIDEISMVEADFFDKLeavARAVRQqkkpfGGIQLIICGDFLQLPPVT 360
Cdd:COG0507   199 LGLRPDSGRF--------RHNRDNPLTPADLLVVDEASMVDTRLMAAL---LEALPR-----AGARLILVGDPDQLPSVG 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 361 KGSqqpqfCFQAKSWRRCVPVIlELTEVWRQADQT-FISLLQAVRLGRCSDEVTRQLRA--------------------T 419
Cdd:COG0507   263 AGA-----VLRDLIESGTVPVV-ELTEVYRQADDSrIIELAHAIREGDAPEALNARYADvvfveaedaeeaaeaivelyA 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 420 AAHKVGRDGIVatrLCTHQDDVALTNEKWLKALPGdvhsfeaidsdpelSRTLDAQCPVSRVLQLKLGAQVMLVKNlAVS 499
Cdd:COG0507   337 DRPAGGEDIQV---LAPTNAGVDALNQAIREALNP--------------AGELERELAEDGELELYVGDRVMFTRN-DYD 398
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720430751 500 RGLVNGARGVVVGFESEGRGLpRVRFlcgitevirtDRW-TVQVTGGQYLSrqqlpLQLAWAISIHKSQ 567
Cdd:COG0507   399 LGVFNGDIGTVLSIDEDEGRL-TVRF----------DGReIVTYDPSELDQ-----LELAYAITVHKSQ 451
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
192-363 9.04e-11

exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273631 [Multi-domain]  Cd Length: 582  Bit Score: 64.78  E-value: 9.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 192 QTSTEAPRWPLPVKKLRMPSTKPKLSEEQAAVLRMVLKGQSIFFTGSAGTGKSYLLKHILGSL---------------PP 256
Cdd:TIGR01447 121 RTLLEARKRTAPSAILENLFPLLNEQNWRKTAVALALKSNFSLITGGPGTGKTTTVARLLLALvkqspkqgklrialaAP 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 257 TGTVAT---------------ASTGVAACHIGGTTLHAFAGIGSGQAPLAQCmalanrpgvRQGWLNCQRLVIDEISMVE 321
Cdd:TIGR01447 201 TGKAAArlaeslrkavknlaaAEALIAALPSEAVTIHRLLGIKPDTKRFRHH---------ERNPLPLDVLVVDEASMVD 271
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720430751 322 ADFFDKLeavARAVRqqkkpfGGIQLIICGDFLQLPPVTKGS 363
Cdd:TIGR01447 272 LPLMAKL---LKALP------PNTKLILLGDKNQLPSVEAGA 304
 
Name Accession Description Interval E-value
PIF1 pfam05970
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits ...
216-513 1.80e-108

PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits telomerase activity and is cell cycle regulated. This family includes a large number of largely uncharacterized plant proteins. This family includes a P-loop motif that is involved in nucleotide binding.


Pssm-ID: 428699 [Multi-domain]  Cd Length: 361  Bit Score: 332.42  E-value: 1.80e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 216 LSEEQAAVLRMVL------KGQSIFFTGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAACHI-GGTTLHAFAGIGSG 286
Cdd:pfam05970   1 LNDEQKKVFDAIIesvinnKGGVFFVYGYGGTGKTFLWKAIITSLRSEGkiVLAVASSGVAALLLpGGRTAHSRFGIPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 287 QAPLAQCmALANRPGVRQGWLNCQRLVIDEISMVEADFFDKLEAVARAVRQQK--KPFGGIQLIICGDFLQLPPVT-KGS 363
Cdd:pfam05970  81 IDELSTC-KIKRGSKLAELLEKTSLIVWDEAPMTHRHCFEALDRTLRDILSETddKPFGGKTVVLGGDFRQILPVIpKGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 364 QQPQFCF---QAKSWRRCVpvILELTEVWRQAD-----------QTFISLLQAVRLGRCSDEVTRQ-------------- 415
Cdd:pfam05970 160 RPEIVNAsitNSYLWKHVK--VLELTKNMRLLAdsldqteakelQDFSDWLLAIGDGKINDENEREqlidipidillntg 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 416 ---LRATAAHKVGRdgIVA-----------TRLCTHQDDVALTNEKWLKALPGDVHSFEAIDS--------------DPE 467
Cdd:pfam05970 238 gdpIEAIVSEVYPD--ILQnstdpnyleerAILCPTNEDVDEINNYRLSQLPGEEKEYLSSDSisksdndseidalyPTE 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1720430751 468 LSRTLDAQCPVSRVLQLKLGAQVMLVKNLAVSRGLVNGARGVVVGF 513
Cdd:pfam05970 316 FLNSLNANGLPNHVLKLKVGAPVMLLRNLDQSRGLCNGTRLIVTQL 361
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
219-390 9.01e-88

DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350795 [Multi-domain]  Cd Length: 183  Bit Score: 272.20  E-value: 9.01e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 219 EQAAVLRMVLKGQSIFFTGSAGTGKSYLLKHILGSLP--PTGTVATASTGVAACHIGGTTLHAFAGIGSGQAPLAQC-MA 295
Cdd:cd18037     1 EQRRVLDLVLDGKNVFFTGSAGTGKSYLLRRIIRALPsrPKRVAVTASTGIAACNIGGTTLHSFAGIGLGSEPAEDLlER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 296 LANRPGVRQGWLNCQRLVIDEISMVEADFFDKLEAVARAVRQQKKPFGGIQLIICGDFLQLPPVTKGSQQP--------Q 367
Cdd:cd18037    81 VKRSPYLVQRWRKCDVLIIDEISMLDADLFDKLDRVAREVRGSDKPFGGIQLILCGDFLQLPPVTKNSERQafffrgdqQ 160
                         170       180
                  ....*....|....*....|...
gi 1720430751 368 FCFQAKSWRRCVPVILELTEVWR 390
Cdd:cd18037   161 FCFEAKSWERCIFLTVELTKVFR 183
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
210-567 5.27e-41

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 156.68  E-value: 5.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 210 PSTKPKLSEEQAAVLRMVLKGQSIFF-TGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAA------CHIGGTTLHAF 280
Cdd:COG0507   119 PRAGITLSDEQREAVALALTTRRVSVlTGGAGTGKTTTLRALLAALEALGlrVALAAPTGKAAkrlsesTGIEARTIHRL 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 281 AGIGSGQAPLaqcmalanRPGVRQGWLNCQRLVIDEISMVEADFFDKLeavARAVRQqkkpfGGIQLIICGDFLQLPPVT 360
Cdd:COG0507   199 LGLRPDSGRF--------RHNRDNPLTPADLLVVDEASMVDTRLMAAL---LEALPR-----AGARLILVGDPDQLPSVG 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 361 KGSqqpqfCFQAKSWRRCVPVIlELTEVWRQADQT-FISLLQAVRLGRCSDEVTRQLRA--------------------T 419
Cdd:COG0507   263 AGA-----VLRDLIESGTVPVV-ELTEVYRQADDSrIIELAHAIREGDAPEALNARYADvvfveaedaeeaaeaivelyA 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 420 AAHKVGRDGIVatrLCTHQDDVALTNEKWLKALPGdvhsfeaidsdpelSRTLDAQCPVSRVLQLKLGAQVMLVKNlAVS 499
Cdd:COG0507   337 DRPAGGEDIQV---LAPTNAGVDALNQAIREALNP--------------AGELERELAEDGELELYVGDRVMFTRN-DYD 398
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720430751 500 RGLVNGARGVVVGFESEGRGLpRVRFlcgitevirtDRW-TVQVTGGQYLSrqqlpLQLAWAISIHKSQ 567
Cdd:COG0507   399 LGVFNGDIGTVLSIDEDEGRL-TVRF----------DGReIVTYDPSELDQ-----LELAYAITVHKSQ 451
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
219-389 2.78e-27

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member 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: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 108.03  E-value: 2.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 219 EQAAVLRMVLKGQSIFFTGSAGTGKSYLLKHILGSL--PPTGTVATASTGVAACHIG------GTTLHAFAGIGSGQAPL 290
Cdd:cd17933     1 EQKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAALeaEGKRVVLAAPTGKAAKRLSestgieASTIHRLLGINPGGGGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 291 AQCmalanrpgvRQGWLNCQRLVIDEISMVEADFFDKLEAVARAvrqqkkpfgGIQLIICGDFLQLPPVTKGSqQPQFCF 370
Cdd:cd17933    81 YYN---------EENPLDADLLIVDEASMVDTRLMAALLSAIPA---------GARLILVGDPDQLPSVGAGN-VLRDLI 141
                         170
                  ....*....|....*....
gi 1720430751 371 QAKSwrrcVPVIlELTEVW 389
Cdd:cd17933   142 ASKG----VPTV-ELTEVF 155
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
216-407 1.89e-12

AAA 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. There is a Walker A and Walker B.


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 66.43  E-value: 1.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 216 LSEEQAAVLRMVLKGQSIFF--TGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAA------CHIGGTTLHAFAGigs 285
Cdd:pfam13604   2 LNAEQAAAVRALLTSGDRVAvlVGPAGTGKTTALKALREAWEAAGyrVIGLAPTGRAAkvlgeeLGIPADTIAKLLH--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 286 gqaplaqcmalanRPGVRQGWLNCQRLVIDEISMVeaDFFDkLEAVARAVRQQkkpfgGIQLIICGDFLQLPPVTKGSQQ 365
Cdd:pfam13604  79 -------------RLGGRAGLDPGTLLIVDEAGMV--GTRQ-MARLLKLAEDA-----GARVILVGDPRQLPSVEAGGAF 137
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720430751 366 PQFCfqakswRRCVPVIlELTEVWRQADQTFISLLQAVRLGR 407
Cdd:pfam13604 138 RDLL------AAGIGTA-ELTEIVRQRDPWQRAASLALRDGD 172
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
192-363 9.04e-11

exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273631 [Multi-domain]  Cd Length: 582  Bit Score: 64.78  E-value: 9.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 192 QTSTEAPRWPLPVKKLRMPSTKPKLSEEQAAVLRMVLKGQSIFFTGSAGTGKSYLLKHILGSL---------------PP 256
Cdd:TIGR01447 121 RTLLEARKRTAPSAILENLFPLLNEQNWRKTAVALALKSNFSLITGGPGTGKTTTVARLLLALvkqspkqgklrialaAP 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 257 TGTVAT---------------ASTGVAACHIGGTTLHAFAGIGSGQAPLAQCmalanrpgvRQGWLNCQRLVIDEISMVE 321
Cdd:TIGR01447 201 TGKAAArlaeslrkavknlaaAEALIAALPSEAVTIHRLLGIKPDTKRFRHH---------ERNPLPLDVLVVDEASMVD 271
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720430751 322 ADFFDKLeavARAVRqqkkpfGGIQLIICGDFLQLPPVTKGS 363
Cdd:TIGR01447 272 LPLMAKL---LKALP------PNTKLILLGDKNQLPSVEAGA 304
AAA_19 pfam13245
AAA domain;
220-359 4.23e-08

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 52.61  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430751 220 QAAVLRMVLKGQSIFFTGSAGTGKSYLLKHILGSL-------------PPTGTVA---TASTGVAAchiggTTLHAFAGI 283
Cdd:pfam13245   1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLvalggvsfpillaAPTGRAAkrlSERTGLPA-----STIHRLLGF 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720430751 284 GsgqaPLAQCMALANRPGVRQGWLncqrLVIDEISMVEADFFDKL-EAVARavrqqkkpfgGIQLIICGDFLQLPPV 359
Cdd:pfam13245  76 D----DLEAGGFLRDEEEPLDGDL----LIVDEFSMVDLPLAYRLlKALPD----------GAQLLLVGDPDQLPSV 134
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
308-362 4.24e-03

DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to 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: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 37.60  E-value: 4.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720430751 308 NCQRLVIDEISMVEAdffdkLEAVARAVRQQKkpfggiqLIICGDFLQLPPVTKG 362
Cdd:cd17934    44 NVDVVIIDEASQITE-----PELLIALIRAKK-------VVLVGDPKQLPPVVQE 86
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
229-260 5.66e-03

ATP-binding cassette transport system involved in resistance to organic solvents; 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: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 39.02  E-value: 5.66e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720430751 229 KGQSIFFTGSAGTGKSYLLKHILGSLPPT-GTV 260
Cdd:cd03261    25 RGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEV 57
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
227-260 8.59e-03

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 38.42  E-value: 8.59e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720430751 227 VLKGQSIFFTGSAGTGKSYLLKHILGSLPPT-GTV 260
Cdd:COG1127    28 VPRGEILAIIGGSGSGKSVLLKLIIGLLRPDsGEI 62
 
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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