NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1418894889|ref|XP_025408046|]
View 

NFX1-type zinc finger-containing protein 1-like isoform X3 [Sipha flava]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
368-572 2.46e-87

EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 271.34  E-value: 2.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 368 GLDSAQSMAFKAALTKEFTIIQGPPGTGKTYIGLQIVKSIIENMYKtnILKNPIIVVCYTNHALDQFLEGL--INITKCV 445
Cdd:cd17936     1 TLDPSQLEALKHALTSELALIQGPPGTGKTFLGVKLVRALLQNQDL--SITGPILVVCYTNHALDQFLEGLldFGPTKIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 446 tRIGrgcksdivkshvlrntntflAQkrlknsyVVGFTTTGASMKRSLLLKLKPPIVIVEEAAEVLESHVVASLTKFCQH 525
Cdd:cd17936    79 -RLG--------------------AR-------VIGMTTTGAAKYRELLQALGPKVVIVEEAAEVLEAHILAALTPSTEH 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1418894889 526 VILIGDHKQLRPRTASFRLS-KLFNLDVSLFERMVKNGFPCYTLDTQH 572
Cdd:cd17936   131 LILIGDHKQLRPKVNVYELTaKKYNLDVSLFERLVKNGLPFVTLNVQR 178
DNA2 super family cl34114
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
460-687 1.15e-19

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG1112:

Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 94.04  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 460 HVLRNTNTFLAQKRLKNSYVVGftTTGASMKRSLLLKLKP-PIVIVEEAAEVLESHVVASLTKfCQHVILIGDHKQLRPR 538
Cdd:COG1112   518 KKRRELRKLLWDALLELAPVVG--MTPASVARLLPLGEGSfDLVIIDEASQATLAEALGALAR-AKRVVLVGDPKQLPPV 594
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 539 TASFRLSKL--FNLDVSLFERMVKN-GFPCYTLDTQHRMRPEISALIKPIY--PFLRDHEIVKDRSdIRGVTKNIYFIHH 613
Cdd:COG1112   595 VFGEEAEEVaeEGLDESLLDRLLARlPERGVMLREHYRMHPEIIAFSNRLFydGKLVPLPSPKARR-LADPDSPLVFIDV 673
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418894889 614 NIHEEKviGSNSYKNSHEVNFFMKFARYLFSQGYHQHQITLLVTYRE--ELLElQKIRE-SSSVLEDFRIECVDGFQ 687
Cdd:COG1112   674 DGVYER--RGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAqvALIR-ELLREaLGDGLEPVFVGTVDRFQ 747
 
Name Accession Description Interval E-value
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
368-572 2.46e-87

EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 271.34  E-value: 2.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 368 GLDSAQSMAFKAALTKEFTIIQGPPGTGKTYIGLQIVKSIIENMYKtnILKNPIIVVCYTNHALDQFLEGL--INITKCV 445
Cdd:cd17936     1 TLDPSQLEALKHALTSELALIQGPPGTGKTFLGVKLVRALLQNQDL--SITGPILVVCYTNHALDQFLEGLldFGPTKIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 446 tRIGrgcksdivkshvlrntntflAQkrlknsyVVGFTTTGASMKRSLLLKLKPPIVIVEEAAEVLESHVVASLTKFCQH 525
Cdd:cd17936    79 -RLG--------------------AR-------VIGMTTTGAAKYRELLQALGPKVVIVEEAAEVLEAHILAALTPSTEH 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1418894889 526 VILIGDHKQLRPRTASFRLS-KLFNLDVSLFERMVKNGFPCYTLDTQH 572
Cdd:cd17936   131 LILIGDHKQLRPKVNVYELTaKKYNLDVSLFERLVKNGLPFVTLNVQR 178
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
460-687 1.15e-19

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 94.04  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 460 HVLRNTNTFLAQKRLKNSYVVGftTTGASMKRSLLLKLKP-PIVIVEEAAEVLESHVVASLTKfCQHVILIGDHKQLRPR 538
Cdd:COG1112   518 KKRRELRKLLWDALLELAPVVG--MTPASVARLLPLGEGSfDLVIIDEASQATLAEALGALAR-AKRVVLVGDPKQLPPV 594
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 539 TASFRLSKL--FNLDVSLFERMVKN-GFPCYTLDTQHRMRPEISALIKPIY--PFLRDHEIVKDRSdIRGVTKNIYFIHH 613
Cdd:COG1112   595 VFGEEAEEVaeEGLDESLLDRLLARlPERGVMLREHYRMHPEIIAFSNRLFydGKLVPLPSPKARR-LADPDSPLVFIDV 673
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418894889 614 NIHEEKviGSNSYKNSHEVNFFMKFARYLFSQGYHQHQITLLVTYRE--ELLElQKIRE-SSSVLEDFRIECVDGFQ 687
Cdd:COG1112   674 DGVYER--RGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAqvALIR-ELLREaLGDGLEPVFVGTVDRFQ 747
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
574-687 7.78e-16

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 76.12  E-value: 7.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 574 MRPEISALIKPIYP--FLRDHEIVKDRS---DIRGVTKNIYFIHHNIHEEKVIGSNSYKNSHEVNFFMKFARYLFSQGYH 648
Cdd:cd18808     1 MHPEISEFPSKLFYegKLKAGVSVAARLnppPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSGVK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1418894889 649 QHQITLLVTYREELLEL-QKIRESSSVLEDFRIECVDGFQ 687
Cdd:cd18808    81 PSSIGVITPYRAQVALIrELLRKRGGLLEDVEVGTVDNFQ 120
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
550-687 1.17e-15

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.


Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 76.05  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 550 LDVSLFERMVKNGF-PCYTLDTQHRMRPEISALikPIYPF----LRDHEIVKDRS--DIRGVT---KNIYFIH-HNIHEE 618
Cdd:pfam13087   1 LDRSLFERLQELGPsAVVMLDTQYRMHPEIMEF--PSKLFyggkLKDGPSVAERPlpDDFHLPdplGPLVFIDvDGSEEE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1418894889 619 KVIGSNSYKNSHEVNFFMKFARYLFSQGYHQH-QITLLVTYREELLELQK-IRESSSVLEDFRIECVDGFQ 687
Cdd:pfam13087  79 ESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPsDIGVITPYRAQVRLIRKlLKRKLGGKLEIEVNTVDGFQ 149
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
369-687 1.39e-15

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 80.63  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 369 LDSAQSMAFKAAL-TKEFTIIQGPPGTGKTYIGLQIVKSIienmyktnILKNPIIVVCY-TNHALDQFLEGLINITKCVT 446
Cdd:TIGR00376 158 LNESQKEAVLFALsSKDLFLIHGPPGTGKTRTVVELIRQL--------VKRGLRVLVTApSNIAVDNLLERLALCDQKIV 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 447 RIGRGCK-SDIVKSHVL------------------------RNTNTFLAQKR--------------------------LK 475
Cdd:TIGR00376 230 RLGHPARlLKSNKQHSLdylienhpkyqivadirekideliEERNKKTKPSPqkrrglsdikilrkalkkreargiesLK 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 476 NSYVVGFTTTGASMKR--SLLLKLKPPI---------------------------VIVEEAAEVLESHVVASLTKfCQHV 526
Cdd:TIGR00376 310 IASMAEWIETNKSIDRllKLLPESEERImneilaesdatnsmagseilngqyfdvAVIDEASQAMEPSCLIPLLK-ARKL 388
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 527 ILIGDHKQLRPRTASFRLSklfNLDVSLFERMVKNgFPCY--TLDTQHRMRPEISALikPIYPF----LRDHEIVKDRS- 599
Cdd:TIGR00376 389 ILAGDHKQLPPTILSHDAE---ELSLTLFERLIKE-YPERsrTLNVQYRMNQKIMEF--PSREFyngkLTAHESVANILl 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 600 -DIRGV--TKNIYFIHHNI------------HEEKVIGSNSYKNSHEVNFFMKFARYLFSQGYHQHQITLLVTYREELLE 664
Cdd:TIGR00376 463 rDLPKVeaTESEDDLETGIpllfidtsgcelFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDL 542
                         410       420
                  ....*....|....*....|...
gi 1418894889 665 LQKIRESSSVleDFRIECVDGFQ 687
Cdd:TIGR00376 543 LRQLLEHRHI--DIEVSSVDGFQ 563
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
376-537 1.97e-13

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.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 70.45  E-value: 1.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 376 AFKAALTK-EFTIIQGPPGTGKTYIGLQIVKSIIENMYKTNILKNPIIVVCYTNHALDQFLEGLINITKC----VTRIGR 450
Cdd:pfam13086   5 AIRSALSSsHFTLIQGPPGTGKTTTIVELIRQLLSYPATSAAAGPRILVCAPSNAAVDNILERLLRKGQKygpkIVRIGH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 451 G---------------------------------------------CKSDIVKSHVLRNTNTFLAQKR------------ 473
Cdd:pfam13086  85 PaaiseavlpvsldylvesklnneedaqivkdiskeleklakalraFEKEIIVEKLLKSRNKDKSKLEqerrklrserke 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 474 ----------------LKNSYVVGFTTTGASmkRSLLLKLKPP-IVIVEEAAEVLESHVVASLTKFCQHVILIGDHKQLR 536
Cdd:pfam13086 165 lrkelrrreqslereiLDEAQIVCSTLSGAG--SRLLSSLANFdVVIIDEAAQALEPSTLIPLLRGPKKVVLVGDPKQLP 242

                  .
gi 1418894889 537 P 537
Cdd:pfam13086 243 P 243
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
345-410 1.53e-04

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 44.76  E-value: 1.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418894889 345 IYTINGLQFDILNNNLWPDNKFLGLDSAQSMAFKAAL-TKEFTIIQGPPGTGKTYIGLQIVKSIIEN 410
Cdd:COG1401   182 SAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALkTKKNVILAGPPGTGKTYLARRLAEALGGE 248
 
Name Accession Description Interval E-value
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
368-572 2.46e-87

EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 271.34  E-value: 2.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 368 GLDSAQSMAFKAALTKEFTIIQGPPGTGKTYIGLQIVKSIIENMYKtnILKNPIIVVCYTNHALDQFLEGL--INITKCV 445
Cdd:cd17936     1 TLDPSQLEALKHALTSELALIQGPPGTGKTFLGVKLVRALLQNQDL--SITGPILVVCYTNHALDQFLEGLldFGPTKIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 446 tRIGrgcksdivkshvlrntntflAQkrlknsyVVGFTTTGASMKRSLLLKLKPPIVIVEEAAEVLESHVVASLTKFCQH 525
Cdd:cd17936    79 -RLG--------------------AR-------VIGMTTTGAAKYRELLQALGPKVVIVEEAAEVLEAHILAALTPSTEH 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1418894889 526 VILIGDHKQLRPRTASFRLS-KLFNLDVSLFERMVKNGFPCYTLDTQH 572
Cdd:cd17936   131 LILIGDHKQLRPKVNVYELTaKKYNLDVSLFERLVKNGLPFVTLNVQR 178
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
372-587 4.12e-30

EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It 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: 350693 [Multi-domain]  Cd Length: 207  Bit Score: 117.91  E-value: 4.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 372 AQSMAFKAALTKEFTIIQGPPGTGKTYIGLQIvksiIENMYKtNILKNPIIVVCYTNHALDQFLEGLInitkcvtrigrg 451
Cdd:cd17935     9 TQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQI----ISNLYH-NFPNQRTLIVTHSNQALNQLFEKIM------------ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 452 cKSDIVKSHVLRntntfLAQkrlkNSYVVGFTTTGASMKRSLLLKL--KPPIVIVEEAAEVLESHVVASL---TKFCQH- 525
Cdd:cd17935    72 -ALDIDERHLLR-----LGH----GAKIIAMTCTHAALKRGELVELgfKYDNILMEEAAQILEIETFIPLllqNPEDGPn 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418894889 526 ----VILIGDHKQLRPRTASFRLSKLFNLDVSLFERMVKNGFPCYTLDTQHRMRPEISALIKPIYP 587
Cdd:cd17935   142 rlkrLIMIGDHHQLPPVIKNMAFQKYSNMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYNWRYK 207
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
369-573 2.76e-27

DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX 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: 438712 [Multi-domain]  Cd Length: 218  Bit Score: 110.00  E-value: 2.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 369 LDSAQSMAFKAALTKE--FTIIQGPPGTGKTYIGLQIVKSIIENMYKTNI------------------LKNPIIVVCYTN 428
Cdd:cd18042     1 LNESQLEAIASALQNSpgITLIQGPPGTGKTKTIVGILSVLLAGKYRKYYekvkkklrklqrnlnnkkKKNRILVCAPSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 429 HALDQFLEGLINiTKCVTRIGRGCKSDIVKshVLRNTntflAQKR-LKNSYVVgFTTTGASmKRSLLLKLKPPI--VIVE 505
Cdd:cd18042    81 AAVDEIVLRLLS-EGFLDGDGRSYKPNVVR--VGRQE----LRASiLNEADIV-CTTLSSS-GSDLLESLPRGFdtVIID 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418894889 506 EAAEVLESHVVASLTKFCQHVILIGDHKQLrPRTASFRLSKLFNLDVSLFERMVKNGFPCYTLDTQHR 573
Cdd:cd18042   152 EAAQAVELSTLIPLRLGCKRLILVGDPKQL-PATVFSKVAQKLGYDRSLFERLQLAGYPVLMLTTQYR 218
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
369-573 5.80e-24

DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain]  Cd Length: 191  Bit Score: 99.61  E-value: 5.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 369 LDSAQSMAFKAAL-TKEFTIIQGPPGTGKTyiglqivKSIIENMYKTNILKNPIIVVCYTNHALDQFLEGLINITKCVTR 447
Cdd:cd18044     2 LNDSQKEAVKFALsQKDVALIHGPPGTGKT-------TTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 448 IG---RGCKSdiVKSHVLrntntflaqKRLKNSYVVGFTTTGASmKRSLLLKLKPPIVIVEEAAEVLESHVVASLTKFcQ 524
Cdd:cd18044    75 IGhpaRLLES--VLDHSL---------DALVAAQVVLATNTGAG-SRQLLPNELFDVVVIDEAAQALEASCWIPLLKA-R 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1418894889 525 HVILIGDHKQLRPRTASfRLSKLFNLDVSLFERMVKNGFP-CYT-LDTQHR 573
Cdd:cd18044   142 RCILAGDHKQLPPTILS-DKAARGGLGVTLFERLVNLYGEsVVRmLTVQYR 191
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
369-573 1.76e-22

DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 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: 350797 [Multi-domain]  Cd Length: 234  Bit Score: 96.93  E-value: 1.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 369 LDSAQSMAFKAALTKEFTIIQGPPGTGKTYIGLQIVKSIIENMyktnilKNPIIVVCYTNHALDQFLEGLINITKCVTRI 448
Cdd:cd18039     2 LNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQG------NGPVLVCAPSNVAVDQLTEKIHQTGLKVVRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 449 ----------------------GRGCKSDIVKSHVLRNTNTFLAQ------KRLKNSY---------VVGFTTTGASMKR 491
Cdd:cd18039    76 caksreavespvsflalhnqvrNLDSAEKLELLKLLKLETGELSSadekryRKLKRKAerellrnadVICCTCVGAGDPR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 492 slLLKLKPPIVIVEEAAEVLESHVVASLTKFCQHVILIGDHKQLRPRTASFRLSKLfNLDVSLFERMVKNGFPCYTLDTQ 571
Cdd:cd18039   156 --LSKMKFRTVLIDEATQATEPECLIPLVHGAKQVILVGDHCQLGPVVMCKKAAKA-GLSQSLFERLVQLGIRPIRLQVQ 232

                  ..
gi 1418894889 572 HR 573
Cdd:cd18039   233 YR 234
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
368-573 8.38e-21

C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It belongs 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: 350798 [Multi-domain]  Cd Length: 271  Bit Score: 92.97  E-value: 8.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 368 GLDSAQSMAFKAALTKEFTIIQGPPGTGKTYIGLQIV----KSIIENMYKTNI-LKNPIIVVCY-TNHALDQFLEGLINI 441
Cdd:cd18040     1 KLNPSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIAywfaKQNREIQSVSGEgDGGPCVLYCGpSNKSVDVVAELLLKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 442 ---------------------------TKCVTRIGRGCK--SDIVKSHVLR----------------------------- 463
Cdd:cd18040    81 pglkilrvyseqietteypipneprhpNKKSERESKPNSelSSITLHHRIRqpsnphsqqikafearfertqekiteedi 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 464 --NTNTFLAQK--RLKNSYVVGFTTTGASMKRsllLKLKPPI--VIVEEAAEVLESHVVASLTKF--CQHVILIGDHKQL 535
Cdd:cd18040   161 ktYKILIWEARfeELETVDVILCTCSEAASQK---MRTHANVkqCIVDECGMCTEPESLIPIVSAprAEQVVLIGDHKQL 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1418894889 536 RPRTASFRLSKLfNLDVSLFERMVKNgfpCYTLDTQHR 573
Cdd:cd18040   238 RPVVQNKEAQKL-GLGRSLFERYAEK---ACMLDTQYR 271
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
368-573 2.55e-20

DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 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: 350799 [Multi-domain]  Cd Length: 203  Bit Score: 89.60  E-value: 2.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 368 GLDSAQSMAFKAALT-KEFTIIQGPPGTGKTYIGLQIVKSIIEnmyktniLKNPIIVVCYTNHALDQFLEGLINITKCVT 446
Cdd:cd18041     1 GLNKDQRQAIKKVLNaKDYALILGMPGTGKTTTIAALVRILVA-------LGKSVLLTSYTHSAVDNILLKLKKFGVNFL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 447 RIGRGCK-SDIVKSHVLRNTNTFLA-----QKRLKNSYVVGFTTTGASMkrSLLLKLKPPIVIVEEAAEVLESHVVASLT 520
Cdd:cd18041    74 RLGRLKKiHPDVQEFTLEAILKSCKsveelESKYESVSVVATTCLGINH--PIFRRRTFDYCIVDEASQITLPICLGPLR 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1418894889 521 kFCQHVILIGDHKQLRPRTASfRLSKLFNLDVSLFERM-VKNGFPCYTLDTQHR 573
Cdd:cd18041   152 -LAKKFVLVGDHYQLPPLVKS-REARELGMDESLFKRLsEAHPDAVVQLTIQYR 203
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
460-687 1.15e-19

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 94.04  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 460 HVLRNTNTFLAQKRLKNSYVVGftTTGASMKRSLLLKLKP-PIVIVEEAAEVLESHVVASLTKfCQHVILIGDHKQLRPR 538
Cdd:COG1112   518 KKRRELRKLLWDALLELAPVVG--MTPASVARLLPLGEGSfDLVIIDEASQATLAEALGALAR-AKRVVLVGDPKQLPPV 594
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 539 TASFRLSKL--FNLDVSLFERMVKN-GFPCYTLDTQHRMRPEISALIKPIY--PFLRDHEIVKDRSdIRGVTKNIYFIHH 613
Cdd:COG1112   595 VFGEEAEEVaeEGLDESLLDRLLARlPERGVMLREHYRMHPEIIAFSNRLFydGKLVPLPSPKARR-LADPDSPLVFIDV 673
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418894889 614 NIHEEKviGSNSYKNSHEVNFFMKFARYLFSQGYHQHQITLLVTYRE--ELLElQKIRE-SSSVLEDFRIECVDGFQ 687
Cdd:COG1112   674 DGVYER--RGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAqvALIR-ELLREaLGDGLEPVFVGTVDRFQ 747
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
386-572 9.19e-18

DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 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: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 79.84  E-value: 9.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 386 TIIQGPPGTGKTYIGLQIVKSIIENmykTNILKNPIIVVCYTNHALDQFleglinitkcvtrigrgcksdivkshvlrnt 465
Cdd:cd17914     2 SLIQGPPGTGKTRVLVKIVAALMQN---KNGEPGRILLVTPTNKAAAQL------------------------------- 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 466 ntflaqkrlknsyvvgftttgasmkrslllklkpPIVIVEEAAEVLESH--VVASLTKFCQHVILIGDHKQLRPRTASFR 543
Cdd:cd17914    48 ----------------------------------DNILVDEAAQILEPEtsRLIDLALDQGRVILVGDHDQLGPVWRGAV 93
                         170       180
                  ....*....|....*....|....*....
gi 1418894889 544 LSKLFNlDVSLFERMVKNGFPCYTLDTQH 572
Cdd:cd17914    94 LAKICN-EQSLFTRLVRLGVSLIRLQVQY 121
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
574-687 7.78e-16

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 76.12  E-value: 7.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 574 MRPEISALIKPIYP--FLRDHEIVKDRS---DIRGVTKNIYFIHHNIHEEKVIGSNSYKNSHEVNFFMKFARYLFSQGYH 648
Cdd:cd18808     1 MHPEISEFPSKLFYegKLKAGVSVAARLnppPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSGVK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1418894889 649 QHQITLLVTYREELLEL-QKIRESSSVLEDFRIECVDGFQ 687
Cdd:cd18808    81 PSSIGVITPYRAQVALIrELLRKRGGLLEDVEVGTVDNFQ 120
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
550-687 1.17e-15

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.


Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 76.05  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 550 LDVSLFERMVKNGF-PCYTLDTQHRMRPEISALikPIYPF----LRDHEIVKDRS--DIRGVT---KNIYFIH-HNIHEE 618
Cdd:pfam13087   1 LDRSLFERLQELGPsAVVMLDTQYRMHPEIMEF--PSKLFyggkLKDGPSVAERPlpDDFHLPdplGPLVFIDvDGSEEE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1418894889 619 KVIGSNSYKNSHEVNFFMKFARYLFSQGYHQH-QITLLVTYREELLELQK-IRESSSVLEDFRIECVDGFQ 687
Cdd:pfam13087  79 ESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPsDIGVITPYRAQVRLIRKlLKRKLGGKLEIEVNTVDGFQ 149
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
387-575 1.25e-15

DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members 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: 350796 [Multi-domain]  Cd Length: 229  Bit Score: 76.50  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 387 IIQGPPGTGKTYIGLQIVKSIIENMYKTNILknpiiVVCYTNHALDQFLEGLINITKC---------VTRIGRGCKSDIV 457
Cdd:cd18038    24 IIFGPPGTGKTVTLVEAILQVLRQPPEARIL-----VCAPSNSAADLLAERLLNALVTkreilrlnaPSRDRASVPPELL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 458 -KSHVLRNTNTFLAQ-KRLKNSYVVGFTTTGASMKRSllLKLKPPI---VIVEEAAEVLESHVVASLTKFCQ---HVILI 529
Cdd:cd18038    99 pYCNSKAEGTFRLPSlEELKKYRIVVCTLMTAGRLVQ--AGVPNGHfthIFIDEAGQATEPEALIPLSELASkntQIVLA 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1418894889 530 GDHKQLRPRTASfRLSKLFNLDVSLFERMVKngFPCYTLDTQHRMR 575
Cdd:cd18038   177 GDPKQLGPVVRS-PLARKYGLGKSLLERLME--RPLYYKDGEYNPS 219
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
369-687 1.39e-15

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 80.63  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 369 LDSAQSMAFKAAL-TKEFTIIQGPPGTGKTYIGLQIVKSIienmyktnILKNPIIVVCY-TNHALDQFLEGLINITKCVT 446
Cdd:TIGR00376 158 LNESQKEAVLFALsSKDLFLIHGPPGTGKTRTVVELIRQL--------VKRGLRVLVTApSNIAVDNLLERLALCDQKIV 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 447 RIGRGCK-SDIVKSHVL------------------------RNTNTFLAQKR--------------------------LK 475
Cdd:TIGR00376 230 RLGHPARlLKSNKQHSLdylienhpkyqivadirekideliEERNKKTKPSPqkrrglsdikilrkalkkreargiesLK 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 476 NSYVVGFTTTGASMKR--SLLLKLKPPI---------------------------VIVEEAAEVLESHVVASLTKfCQHV 526
Cdd:TIGR00376 310 IASMAEWIETNKSIDRllKLLPESEERImneilaesdatnsmagseilngqyfdvAVIDEASQAMEPSCLIPLLK-ARKL 388
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 527 ILIGDHKQLRPRTASFRLSklfNLDVSLFERMVKNgFPCY--TLDTQHRMRPEISALikPIYPF----LRDHEIVKDRS- 599
Cdd:TIGR00376 389 ILAGDHKQLPPTILSHDAE---ELSLTLFERLIKE-YPERsrTLNVQYRMNQKIMEF--PSREFyngkLTAHESVANILl 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 600 -DIRGV--TKNIYFIHHNI------------HEEKVIGSNSYKNSHEVNFFMKFARYLFSQGYHQHQITLLVTYREELLE 664
Cdd:TIGR00376 463 rDLPKVeaTESEDDLETGIpllfidtsgcelFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDL 542
                         410       420
                  ....*....|....*....|...
gi 1418894889 665 LQKIRESSSVleDFRIECVDGFQ 687
Cdd:TIGR00376 543 LRQLLEHRHI--DIEVSSVDGFQ 563
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
385-573 6.06e-15

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: 71.50  E-value: 6.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 385 FTIIQGPPGTGKTYIGLQIVKSIIENMYKTNILknpiiVVCYTNHALDqflegliNITkcvtrigrgcksdivkshvlrn 464
Cdd:cd17934     1 ISLIQGPPGTGKTTTIAAIVLQLLKGLRGKRVL-----VTAQSNVAVD-------NVD---------------------- 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 465 tntflaqkrlknsyvvgftttgasmkrslllklkppIVIVEEAAEVLESHVVASLTKfCQHVILIGDHKQLRPRTASFRL 544
Cdd:cd17934    47 ------------------------------------VVIIDEASQITEPELLIALIR-AKKVVLVGDPKQLPPVVQEDHA 89
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1418894889 545 SKL---FNLDVSLFERMVKNGFPCYTLDTQHR 573
Cdd:cd17934    90 ALLglsFILSLLLLFRLLLPGSPKVMLDTQYR 121
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
376-537 1.97e-13

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.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 70.45  E-value: 1.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 376 AFKAALTK-EFTIIQGPPGTGKTYIGLQIVKSIIENMYKTNILKNPIIVVCYTNHALDQFLEGLINITKC----VTRIGR 450
Cdd:pfam13086   5 AIRSALSSsHFTLIQGPPGTGKTTTIVELIRQLLSYPATSAAAGPRILVCAPSNAAVDNILERLLRKGQKygpkIVRIGH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 451 G---------------------------------------------CKSDIVKSHVLRNTNTFLAQKR------------ 473
Cdd:pfam13086  85 PaaiseavlpvsldylvesklnneedaqivkdiskeleklakalraFEKEIIVEKLLKSRNKDKSKLEqerrklrserke 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 474 ----------------LKNSYVVGFTTTGASmkRSLLLKLKPP-IVIVEEAAEVLESHVVASLTKFCQHVILIGDHKQLR 536
Cdd:pfam13086 165 lrkelrrreqslereiLDEAQIVCSTLSGAG--SRLLSSLANFdVVIIDEAAQALEPSTLIPLLRGPKKVVLVGDPKQLP 242

                  .
gi 1418894889 537 P 537
Cdd:pfam13086 243 P 243
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
387-568 1.79e-06

DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases 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: 350835 [Multi-domain]  Cd Length: 226  Bit Score: 49.41  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 387 IIQGPPGTGKTYIGLQIVKSIIENMyktnilKNPIIVVCYTNHALDQFLEGLI-------NITKCVTRI---GRGCKS-- 454
Cdd:cd18077    25 LLIGPFGTGKTFTLAQAVKHILQQP------ETRILICTHSNSAADLYIKEYLhpyvetgNPRARPLRVyyrNRWVKTvh 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 455 DIVKSHVLRNTN-TFL---AQKRLKNSYVVGFTTTGASMKRSLLLKLKPPIVIVEEAAEVLESHVVASLTKFCQ--HVIL 528
Cdd:cd18077    99 PVVQKYCLIDEHgTFRmptREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAMECEAIMPLALATKstRIVL 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1418894889 529 IGDHKQLRPRTASfRLSKLFNLDVSLFERMVKN---GFPCYTL 568
Cdd:cd18077   179 AGDHMQLSPEVYS-EFARERNLHISLLERLYEHypsEHPCRIL 220
AAA_19 pfam13245
AAA domain;
373-535 8.22e-06

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 46.06  E-value: 8.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 373 QSMAFKAALTKEFTIIQGPPGTGKTYiglqIVKSIIENMYKTNILKNPIIVVCYTNHALDQFLEglinitkcvtRIGRgc 452
Cdd:pfam13245   1 QREAVRTALPSKVVLLTGGPGTGKTT----TIRHIVALLVALGGVSFPILLAAPTGRAAKRLSE----------RTGL-- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 453 ksDIVKSHVLrntntflaqkrlknsyvVGFTTTGA-SMKRSLLLKLKPPIVIVEEAAEV---LESHVVASLTKFCqHVIL 528
Cdd:pfam13245  65 --PASTIHRL-----------------LGFDDLEAgGFLRDEEEPLDGDLLIVDEFSMVdlpLAYRLLKALPDGA-QLLL 124

                  ....*..
gi 1418894889 529 IGDHKQL 535
Cdd:pfam13245 125 VGDPDQL 131
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
370-539 1.33e-05

DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases are members 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: 350801 [Multi-domain]  Cd Length: 127  Bit Score: 44.88  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 370 DSAQSMAFKAALTKEFTIIQGPPGTGKTyiglQIVKSIIENMYKTNilKNpIIVVCYTNHALDqfleglinitkcvtrig 449
Cdd:cd18043     1 DSSQEAAIISARNGKNVVIQGPPGTGKS----QTIANIIANALARG--KR-VLFVSEKKAALD----------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 450 rgcksdivkshVLrntntflaqkrlknsYVVGFTTTGASMKRSLLLKLKP-PIVIVEEAAEVLESHVVASLTKfCQHVIL 528
Cdd:cd18043    57 -----------VV---------------RFPCWIMSPLSVSQYLPLNRNLfDLVIFDEASQIPIEEALPALFR-GKQVVV 109
                         170
                  ....*....|.
gi 1418894889 529 IGDHKQLRPRT 539
Cdd:cd18043   110 VGDDKQLPPSI 120
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
345-410 1.53e-04

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 44.76  E-value: 1.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418894889 345 IYTINGLQFDILNNNLWPDNKFLGLDSAQSMAFKAAL-TKEFTIIQGPPGTGKTYIGLQIVKSIIEN 410
Cdd:COG1401   182 SAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALkTKKNVILAGPPGTGKTYLARRLAEALGGE 248
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
376-537 3.06e-04

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: 41.77  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 376 AFKAALTKEFTIIQGPPGTGKTYIGLQIVKSIIENMYKtnilknpiIVVCytnhALdqflegliniTkcvtriGRgcksd 455
Cdd:cd17933     5 AVRLVLRNRVSVLTGGAGTGKTTTLKALLAALEAEGKR--------VVLA----AP----------T------GK----- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 456 ivkshvlrntntflAQKRLKNSYVVGFTT----TGASMKRSLLLKLKPP-----IVIVEEAAEV---LESHVVASLTKFC 523
Cdd:cd17933    52 --------------AAKRLSESTGIEASTihrlLGINPGGGGFYYNEENpldadLLIVDEASMVdtrLMAALLSAIPAGA 117
                         170
                  ....*....|....
gi 1418894889 524 QhVILIGDHKQLRP 537
Cdd:cd17933   118 R-LILVGDPDQLPS 130
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
376-450 7.96e-04

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 42.70  E-value: 7.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418894889 376 AFKAALTKEFT--IIQGPPGTGKTYIGLQIVKSIIEnmyktnilKNPIIVVCYTNHALDQFLEGLINITKCVTRIGR 450
Cdd:COG1061    91 ALLAALERGGGrgLVVAPTGTGKTVLALALAAELLR--------GKRVLVLVPRRELLEQWAEELRRFLGDPLAGGG 159
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
368-575 1.01e-03

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: 40.63  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 368 GLDSAQSMAFKAALTKE--FTIIQGPPGTGKTYIgLQIVKSIIENmyktniLKNPIIVVCYTNHALDQFLEGLinitkcv 445
Cdd:pfam13604   1 TLNAEQAAAVRALLTSGdrVAVLVGPAGTGKTTA-LKALREAWEA------AGYRVIGLAPTGRAAKVLGEEL------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418894889 446 trigrGCKSDIVKSHVLRNtntflaqkrlknsyvvgftttgasmkRSLLLKLKPPIVIVEEAAeVLESHVVASLTKFCQH 525
Cdd:pfam13604  67 -----GIPADTIAKLLHRL--------------------------GGRAGLDPGTLLIVDEAG-MVGTRQMARLLKLAED 114
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1418894889 526 ----VILIGDHKQLRPRTASfrlsklfnldvSLFERMVKNGFPCYTLDTQHRMR 575
Cdd:pfam13604 115 agarVILVGDPRQLPSVEAG-----------GAFRDLLAAGIGTAELTEIVRQR 157
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
369-409 2.51e-03

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: 41.12  E-value: 2.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1418894889 369 LDSAQSMAFKAALTKE-FTIIQGPPGTGKTYiglqIVKSIIE 409
Cdd:COG0507   125 LSDEQREAVALALTTRrVSVLTGGAGTGKTT----TLRALLA 162
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH