NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119392094|ref|NP_002171|]
View 

DNA-binding protein SMUBP-2 [Homo sapiens]

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
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
19-641 0e+00

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: 898.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094   19 LERDAEVEERRSWQENISLKELQSRGVCLLKLQVSsQRTGLYGRLLVTFEpRRYGSAAALPSnsftsGDIVGLYDAaNEG 98
Cdd:TIGR00376   1 LERDAEISAMMNEIRRLSLKQRERRGRAILNLQGK-IRGGLLGFLLVRFG-RRKAIATEISV-----GDIVLVSRG-NPL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094   99 SQLATGILTRVTQKSVTVAFDEShDFQLSLDRensYRLLKLANDVTYRRLKKALIALKKYHSgpasSLIEVLFGRSAPSP 178
Cdd:TIGR00376  73 QSDLTGVVTRVGKRFITVALEES-VPQWSLKR---VRIDLYANDVTFKRMKEALRALTENHS----RLLEFLLGREAPSK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  179 ASEIHPLTFFNTCLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALC 258
Cdd:TIGR00376 145 ASEIHDFQFFDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALC 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  259 KQRILRLGHPARLLESIQQHSLDAVLARSDSAQIVADIRKDIDQVFVK-NKKTQDKREKSNFRNEIKLLRKELKEReEAA 337
Cdd:TIGR00376 225 DQKIVRLGHPARLLKSNKQHSLDYLIENHPKYQIVADIREKIDELIEErNKKTKPSPQKRRGLSDIKILRKALKKR-EAR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  338 MLESLTSANVVLATNTGASADGPLKLLPES---------------------------YFDVVVIDECAQALEASCWIPLL 390
Cdd:TIGR00376 304 GIESLKIASMAEWIETNKSIDRLLKLLPESeerimneilaesdatnsmagseilngqYFDVAVIDEASQAMEPSCLIPLL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  391 KARKCILAGDHKQLPPTTVSHKAalAGLSLSLMERLAEEYGARvVRTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARH 470
Cdd:TIGR00376 384 KARKLILAGDHKQLPPTILSHDA--EELSLTLFERLIKEYPER-SRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANI 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  471 LLRDLPGVAATEE-----TGVPLLLVDTAGCGLFELEEEDEQSKGNPGEVRLVSLHIQALVDAGVPARDIAVVSPYNLQV 545
Cdd:TIGR00376 461 LLRDLPKVEATESeddleTGIPLLFIDTSGCELFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQV 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  546 DLLRQSLVHRHPELEIKSVDGFQGREKEAVILSFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSRTVNNHAFLKT 625
Cdd:TIGR00376 541 DLLRQLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKR 620
                         650
                  ....*....|....*.
gi 119392094  626 LVEYFTQHGEVRTAFE 641
Cdd:TIGR00376 621 LIEWCKQHGEVREAFK 636
R3H_Smubp-2_like cd02641
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and ...
726-784 1.38e-27

R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and an AN1-like Zinc finger domain and have been shown to bind single-stranded DNA. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.


:

Pssm-ID: 100070  Cd Length: 60  Bit Score: 105.90  E-value: 1.38e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 726 VDHFRAMIVEFMAS-KKMQLEFPPSLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd02641    1 VKHLKAMVKAFMKDpKATELEFPPTLSSHDRLLVHELAEELGLRHESTGEGSDRVITVSK 60
ZnF_AN1 smart00154
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ...
902-937 1.18e-08

AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis.


:

Pssm-ID: 197545  Cd Length: 39  Bit Score: 51.62  E-value: 1.18e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 119392094   902 CTAGVTTLGQFCQLCSRRYCLSHHLPEIHGCGERAR 937
Cdd:smart00154   4 CRKKVGLTGFKCRHCGNLFCGEHRLPEDHDCPGDYK 39
PRK12438 super family cl46960
hypothetical protein; Provisional
786-845 1.05e-04

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PRK12438:

Pssm-ID: 171499 [Multi-domain]  Cd Length: 991  Bit Score: 46.39  E-value: 1.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 786 APRPRAALGPPAGTGGPAPLQPVPPtPAQTEQPPREQRGPDQPDLRTLHLER-LQRVRSAQ 845
Cdd:PRK12438 905 APGGDAASAPPPGAGPPAPPQAVPP-PRTTQPPAAPPRGPDVPPAAVAELREtLADLRSAQ 964
 
Name Accession Description Interval E-value
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
19-641 0e+00

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: 898.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094   19 LERDAEVEERRSWQENISLKELQSRGVCLLKLQVSsQRTGLYGRLLVTFEpRRYGSAAALPSnsftsGDIVGLYDAaNEG 98
Cdd:TIGR00376   1 LERDAEISAMMNEIRRLSLKQRERRGRAILNLQGK-IRGGLLGFLLVRFG-RRKAIATEISV-----GDIVLVSRG-NPL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094   99 SQLATGILTRVTQKSVTVAFDEShDFQLSLDRensYRLLKLANDVTYRRLKKALIALKKYHSgpasSLIEVLFGRSAPSP 178
Cdd:TIGR00376  73 QSDLTGVVTRVGKRFITVALEES-VPQWSLKR---VRIDLYANDVTFKRMKEALRALTENHS----RLLEFLLGREAPSK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  179 ASEIHPLTFFNTCLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALC 258
Cdd:TIGR00376 145 ASEIHDFQFFDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALC 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  259 KQRILRLGHPARLLESIQQHSLDAVLARSDSAQIVADIRKDIDQVFVK-NKKTQDKREKSNFRNEIKLLRKELKEReEAA 337
Cdd:TIGR00376 225 DQKIVRLGHPARLLKSNKQHSLDYLIENHPKYQIVADIREKIDELIEErNKKTKPSPQKRRGLSDIKILRKALKKR-EAR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  338 MLESLTSANVVLATNTGASADGPLKLLPES---------------------------YFDVVVIDECAQALEASCWIPLL 390
Cdd:TIGR00376 304 GIESLKIASMAEWIETNKSIDRLLKLLPESeerimneilaesdatnsmagseilngqYFDVAVIDEASQAMEPSCLIPLL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  391 KARKCILAGDHKQLPPTTVSHKAalAGLSLSLMERLAEEYGARvVRTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARH 470
Cdd:TIGR00376 384 KARKLILAGDHKQLPPTILSHDA--EELSLTLFERLIKEYPER-SRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANI 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  471 LLRDLPGVAATEE-----TGVPLLLVDTAGCGLFELEEEDEQSKGNPGEVRLVSLHIQALVDAGVPARDIAVVSPYNLQV 545
Cdd:TIGR00376 461 LLRDLPKVEATESeddleTGIPLLFIDTSGCELFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQV 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  546 DLLRQSLVHRHPELEIKSVDGFQGREKEAVILSFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSRTVNNHAFLKT 625
Cdd:TIGR00376 541 DLLRQLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKR 620
                         650
                  ....*....|....*.
gi 119392094  626 LVEYFTQHGEVRTAFE 641
Cdd:TIGR00376 621 LIEWCKQHGEVREAFK 636
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
191-443 5.81e-111

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: 340.74  E-value: 5.81e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 191 CLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALCKQRILRLGHPAR 270
Cdd:cd18044    1 NLNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 271 LLESIQQHSLDAVLArsdsaqivadirkdidqvfvknkktqdkreksnfrneikllrkelkereeaamlesltsANVVLA 350
Cdd:cd18044   81 LLESVLDHSLDALVA-----------------------------------------------------------AQVVLA 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 351 TNTGASADGplkLLPESYFDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVSHKAALAGLSLSLMERLAEEY 430
Cdd:cd18044  102 TNTGAGSRQ---LLPNELFDVVVIDEAAQALEASCWIPLLKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLY 178
                        250
                 ....*....|...
gi 119392094 431 GARVVRTLTVQYR 443
Cdd:cd18044  179 GESVVRMLTVQYR 191
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
418-615 6.38e-73

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: 238.99  E-value: 6.38e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  418 LSLSLMERLAEEYGARVVrTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARHLLRDLPgvaATEETGVPLLLVDTAGCg 497
Cdd:pfam13087   1 LDRSLFERLQELGPSAVV-MLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDF---HLPDPLGPLVFIDVDGS- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  498 lFELEEEDEQSKGNPGEVRLVSLHIQALVDAGVPA-RDIAVVSPYNLQVDLLRQSLVHRH---PELEIKSVDGFQGREKE 573
Cdd:pfam13087  76 -EEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRKLggkLEIEVNTVDGFQGREKD 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 119392094  574 AVILSFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSR 615
Cdd:pfam13087 155 VIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
14-630 2.16e-69

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 248.12  E-value: 2.16e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  14 LDLLELERDAEVEERRSWQENISLKELQSRGVCLLKLQVSSQRTGLYGRLLVTFEPRRYGSAAALPSNSFTSGDIVGLYD 93
Cdd:COG1112  206 LLLLLLLLALLLLLALLLLLDALLLLLAALALLALALLLALLLLLLALLLLAALALLRAALRLDLLAALELLAALSLALL 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  94 AANEGSQLATGILTRVTQKSVTVAFDESHDFQLSLDRENSYRLLKLANDVTYRRLKKALIALKKYHSGPASSLIEVLFGR 173
Cdd:COG1112  286 ALLAALALALLLLAALALLLALALAALLALLALLALLAARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLL 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 174 SAPSPASEIHPLTFFNTCLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVE 253
Cdd:COG1112  366 ALALLLLLALEELLLLALLRLLAEGLALLLLLLLAALLRLARALLLLALLLAAAAAALAALLLLALALLAALLALLLLLA 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 254 RLALCKQRILRLGHPARLLESIQQHSLDAVLARSDSAQIVADIRKDIDQVFvkNKKTQDKREKSNFRNEIKLLRKELKER 333
Cdd:COG1112  446 AALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEEL--EKLIAELREAARLRRALRRELKKRREL 523
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 334 EEAAMLESLTSANVVLATNTGASADGPLKllpESYFDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVS--- 410
Cdd:COG1112  524 RKLLWDALLELAPVVGMTPASVARLLPLG---EGSFDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPPVVFGeea 600
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 411 HKAALAGLSLSLMERLAEEYGARVVrTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARHLLRDLPGvaateetgvPLLL 490
Cdd:COG1112  601 EEVAEEGLDESLLDRLLARLPERGV-MLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDS---------PLVF 670
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 491 VDTAGCGlfeleEEDEQSKGNPGEVRLVSLHIQALVDAGVPARDIAVVSPYNLQVDLLRQSL----VHRHPELEIKSVDG 566
Cdd:COG1112  671 IDVDGVY-----ERRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLrealGDGLEPVFVGTVDR 745
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 567 FQGREKEAVILSFVRSNRK---GEVGFLAED-RRINVAVTRARRHVAVICDSRTV---NNHAFLKTLVEYF 630
Cdd:COG1112  746 FQGDERDVIIFSLVYSNDEdvpRNFGFLNGGpRRLNVAVSRARRKLIVVGSRELLdsdPSTPALKRLLEYL 816
R3H_Smubp-2_like cd02641
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and ...
726-784 1.38e-27

R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and an AN1-like Zinc finger domain and have been shown to bind single-stranded DNA. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.


Pssm-ID: 100070  Cd Length: 60  Bit Score: 105.90  E-value: 1.38e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 726 VDHFRAMIVEFMAS-KKMQLEFPPSLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd02641    1 VKHLKAMVKAFMKDpKATELEFPPTLSSHDRLLVHELAEELGLRHESTGEGSDRVITVSK 60
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
706-785 1.19e-18

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 81.19  E-value: 1.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094   706 APSQPSLNGGSPEGVESQDGVDHFRAMIVEFMASKKMQLEFPPsLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSKR 785
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVKSTKESVELPP-MNSYERKIVHELAEKYGLESESFGEGPKRRVVISKK 79
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
733-784 1.17e-11

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 60.58  E-value: 1.17e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119392094  733 IVEFMASKKMQLEFPPsLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:pfam01424  10 LAEFVKDTGKSLELPP-MSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
ZnF_AN1 smart00154
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ...
902-937 1.18e-08

AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis.


Pssm-ID: 197545  Cd Length: 39  Bit Score: 51.62  E-value: 1.18e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 119392094   902 CTAGVTTLGQFCQLCSRRYCLSHHLPEIHGCGERAR 937
Cdd:smart00154   4 CRKKVGLTGFKCRHCGNLFCGEHRLPEDHDCPGDYK 39
zf-AN1 pfam01428
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ...
897-934 2.02e-08

AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis. The following pattern describes the zinc finger. C-X2-C-X(9-12)-C-X(1-2)-C-X4-C-X2-H-X5-H-X-C Where X can be any amino acid, and numbers in brackets indicate the number of residues.


Pssm-ID: 460208  Cd Length: 37  Bit Score: 50.77  E-value: 2.02e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 119392094  897 CGFAKCTAGVTTLGQfCQLCSRRYCLSHHLPEIHGCGE 934
Cdd:pfam01428   1 CSFKGCKKKDFLPFK-CRFCGKNFCLKHRLPEDHDCSG 37
DEXDc smart00487
DEAD-like helicases superfamily;
196-256 1.93e-07

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 52.49  E-value: 1.93e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119392094   196 QKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGL--KVLCCAPSNIAVDNLVERLA 256
Cdd:smart00487  13 QKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELK 75
PRK12438 PRK12438
hypothetical protein; Provisional
786-845 1.05e-04

hypothetical protein; Provisional


Pssm-ID: 171499 [Multi-domain]  Cd Length: 991  Bit Score: 46.39  E-value: 1.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 786 APRPRAALGPPAGTGGPAPLQPVPPtPAQTEQPPREQRGPDQPDLRTLHLER-LQRVRSAQ 845
Cdd:PRK12438 905 APGGDAASAPPPGAGPPAPPQAVPP-PRTTQPPAAPPRGPDVPPAAVAELREtLADLRSAQ 964
PHA03247 PHA03247
large tegument protein UL36; Provisional
662-878 2.29e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  662 AATKPQGPATSTRTGSQRQEGGQEAAAPARQgrkKPAGKSLASEAPSQPSLNGGSPEGVESQDGVDHFRAMIVEFMASKK 741
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAA---PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP 2820
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  742 MQLEFPPSLNSHDRLRVH-QIAEEHGLRHDSSGEGKRRFITVSKRAPRPRAALGPPAGTGGPAPLQPVPPTPAQTE---Q 817
Cdd:PHA03247 2821 AASPAGPLPPPTSAQPTApPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsfaL 2900
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094  818 PPREQRGPDQPDLRTLHLERLQRVRSAQGQPAsKEQQASGQQKLPEKKKKKAKGHPATDLP 878
Cdd:PHA03247 2901 PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP-PPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
204-275 3.26e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 3.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119392094 204 LSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCcapsnIAVDNLVERLALCKQRilrlGHPARLLESI 275
Cdd:NF038214  87 IERAENVLLLGPPGTGKTHLAIALGYAACRQGYRVRF-----TTAADLVEQLAQARAD----GRLGRLLRRL 149
 
Name Accession Description Interval E-value
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
19-641 0e+00

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: 898.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094   19 LERDAEVEERRSWQENISLKELQSRGVCLLKLQVSsQRTGLYGRLLVTFEpRRYGSAAALPSnsftsGDIVGLYDAaNEG 98
Cdd:TIGR00376   1 LERDAEISAMMNEIRRLSLKQRERRGRAILNLQGK-IRGGLLGFLLVRFG-RRKAIATEISV-----GDIVLVSRG-NPL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094   99 SQLATGILTRVTQKSVTVAFDEShDFQLSLDRensYRLLKLANDVTYRRLKKALIALKKYHSgpasSLIEVLFGRSAPSP 178
Cdd:TIGR00376  73 QSDLTGVVTRVGKRFITVALEES-VPQWSLKR---VRIDLYANDVTFKRMKEALRALTENHS----RLLEFLLGREAPSK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  179 ASEIHPLTFFNTCLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALC 258
Cdd:TIGR00376 145 ASEIHDFQFFDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALC 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  259 KQRILRLGHPARLLESIQQHSLDAVLARSDSAQIVADIRKDIDQVFVK-NKKTQDKREKSNFRNEIKLLRKELKEReEAA 337
Cdd:TIGR00376 225 DQKIVRLGHPARLLKSNKQHSLDYLIENHPKYQIVADIREKIDELIEErNKKTKPSPQKRRGLSDIKILRKALKKR-EAR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  338 MLESLTSANVVLATNTGASADGPLKLLPES---------------------------YFDVVVIDECAQALEASCWIPLL 390
Cdd:TIGR00376 304 GIESLKIASMAEWIETNKSIDRLLKLLPESeerimneilaesdatnsmagseilngqYFDVAVIDEASQAMEPSCLIPLL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  391 KARKCILAGDHKQLPPTTVSHKAalAGLSLSLMERLAEEYGARvVRTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARH 470
Cdd:TIGR00376 384 KARKLILAGDHKQLPPTILSHDA--EELSLTLFERLIKEYPER-SRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANI 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  471 LLRDLPGVAATEE-----TGVPLLLVDTAGCGLFELEEEDEQSKGNPGEVRLVSLHIQALVDAGVPARDIAVVSPYNLQV 545
Cdd:TIGR00376 461 LLRDLPKVEATESeddleTGIPLLFIDTSGCELFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQV 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  546 DLLRQSLVHRHPELEIKSVDGFQGREKEAVILSFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSRTVNNHAFLKT 625
Cdd:TIGR00376 541 DLLRQLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKR 620
                         650
                  ....*....|....*.
gi 119392094  626 LVEYFTQHGEVRTAFE 641
Cdd:TIGR00376 621 LIEWCKQHGEVREAFK 636
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
191-443 5.81e-111

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: 340.74  E-value: 5.81e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 191 CLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALCKQRILRLGHPAR 270
Cdd:cd18044    1 NLNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 271 LLESIQQHSLDAVLArsdsaqivadirkdidqvfvknkktqdkreksnfrneikllrkelkereeaamlesltsANVVLA 350
Cdd:cd18044   81 LLESVLDHSLDALVA-----------------------------------------------------------AQVVLA 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 351 TNTGASADGplkLLPESYFDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVSHKAALAGLSLSLMERLAEEY 430
Cdd:cd18044  102 TNTGAGSRQ---LLPNELFDVVVIDEAAQALEASCWIPLLKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLY 178
                        250
                 ....*....|...
gi 119392094 431 GARVVRTLTVQYR 443
Cdd:cd18044  179 GESVVRMLTVQYR 191
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
418-615 6.38e-73

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: 238.99  E-value: 6.38e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  418 LSLSLMERLAEEYGARVVrTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARHLLRDLPgvaATEETGVPLLLVDTAGCg 497
Cdd:pfam13087   1 LDRSLFERLQELGPSAVV-MLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDF---HLPDPLGPLVFIDVDGS- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  498 lFELEEEDEQSKGNPGEVRLVSLHIQALVDAGVPA-RDIAVVSPYNLQVDLLRQSLVHRH---PELEIKSVDGFQGREKE 573
Cdd:pfam13087  76 -EEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRKLggkLEIEVNTVDGFQGREKD 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 119392094  574 AVILSFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSR 615
Cdd:pfam13087 155 VIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
14-630 2.16e-69

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 248.12  E-value: 2.16e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  14 LDLLELERDAEVEERRSWQENISLKELQSRGVCLLKLQVSSQRTGLYGRLLVTFEPRRYGSAAALPSNSFTSGDIVGLYD 93
Cdd:COG1112  206 LLLLLLLLALLLLLALLLLLDALLLLLAALALLALALLLALLLLLLALLLLAALALLRAALRLDLLAALELLAALSLALL 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  94 AANEGSQLATGILTRVTQKSVTVAFDESHDFQLSLDRENSYRLLKLANDVTYRRLKKALIALKKYHSGPASSLIEVLFGR 173
Cdd:COG1112  286 ALLAALALALLLLAALALLLALALAALLALLALLALLAARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLL 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 174 SAPSPASEIHPLTFFNTCLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVE 253
Cdd:COG1112  366 ALALLLLLALEELLLLALLRLLAEGLALLLLLLLAALLRLARALLLLALLLAAAAAALAALLLLALALLAALLALLLLLA 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 254 RLALCKQRILRLGHPARLLESIQQHSLDAVLARSDSAQIVADIRKDIDQVFvkNKKTQDKREKSNFRNEIKLLRKELKER 333
Cdd:COG1112  446 AALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEEL--EKLIAELREAARLRRALRRELKKRREL 523
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 334 EEAAMLESLTSANVVLATNTGASADGPLKllpESYFDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVS--- 410
Cdd:COG1112  524 RKLLWDALLELAPVVGMTPASVARLLPLG---EGSFDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPPVVFGeea 600
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 411 HKAALAGLSLSLMERLAEEYGARVVrTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARHLLRDLPGvaateetgvPLLL 490
Cdd:COG1112  601 EEVAEEGLDESLLDRLLARLPERGV-MLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDS---------PLVF 670
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 491 VDTAGCGlfeleEEDEQSKGNPGEVRLVSLHIQALVDAGVPARDIAVVSPYNLQVDLLRQSL----VHRHPELEIKSVDG 566
Cdd:COG1112  671 IDVDGVY-----ERRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLrealGDGLEPVFVGTVDR 745
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 567 FQGREKEAVILSFVRSNRK---GEVGFLAED-RRINVAVTRARRHVAVICDSRTV---NNHAFLKTLVEYF 630
Cdd:COG1112  746 FQGDERDVIIFSLVYSNDEdvpRNFGFLNGGpRRLNVAVSRARRKLIVVGSRELLdsdPSTPALKRLLEYL 816
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
195-410 2.24e-68

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: 228.77  E-value: 2.24e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  195 SQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGL-------KVLCCAPSNIAVDNLVERLALCKQ----RIL 263
Cdd:pfam13086   1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPAtsaaagpRILVCAPSNAAVDNILERLLRKGQkygpKIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  264 RLGHPARLLESIQQHSLDAVLAR----SDSAQIVADIRK------------------DIDQVFVKNKKTQDKREKSNFRN 321
Cdd:pfam13086  81 RIGHPAAISEAVLPVSLDYLVESklnnEEDAQIVKDISKeleklakalrafekeiivEKLLKSRNKDKSKLEQERRKLRS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  322 EIKLLRKELKEREEAAMLESLTSANVVLATNTGASADgplKLLPESYFDVVVIDECAQALEASCWIPLLKA-RKCILAGD 400
Cdd:pfam13086 161 ERKELRKELRRREQSLEREILDEAQIVCSTLSGAGSR---LLSSLANFDVVIIDEAAQALEPSTLIPLLRGpKKVVLVGD 237
                         250
                  ....*....|
gi 119392094  401 HKQLPPTTVS 410
Cdd:pfam13086 238 PKQLPPTVIS 247
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
444-630 3.24e-59

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: 200.54  E-value: 3.24e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 444 MHQAIMRWASDTMYLGQLTAHSSVARHLLRDlpgvaATEETGVPLLLVDTAGCglfELEEEDEQSKGNPGEVRLVSLHIQ 523
Cdd:cd18808    1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPP-----PLPGPSKPLVFVDVSGG---EEREESGTSKSNEAEAELVVELVK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 524 ALVDAGVPARDIAVVSPYNLQVDLLRQSLVHRH---PELEIKSVDGFQGREKEAVILSFVRSNRKGE-VGFLAEDRRINV 599
Cdd:cd18808   73 YLLKSGVKPSSIGVITPYRAQVALIRELLRKRGgllEDVEVGTVDNFQGREKDVIILSLVRSNESGGsIGFLSDPRRLNV 152
                        170       180       190
                 ....*....|....*....|....*....|.
gi 119392094 600 AVTRARRHVAVICDSRTVNNHAFLKTLVEYF 630
Cdd:cd18808  153 ALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
191-443 6.27e-45

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: 160.86  E-value: 6.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 191 CLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALCKQRILRLGHPAR 270
Cdd:cd18041    1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 271 LLESIQQHSLDAVLARSDSAQivadirkdidqvfvknkktqdkreksnfrneikllrkELKereeaamlESLTSANVVLA 350
Cdd:cd18041   81 IHPDVQEFTLEAILKSCKSVE-------------------------------------ELE--------SKYESVSVVAT 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 351 TNTGASADgplkLLPESYFDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVSHKAALAGLSLSLMERLAEEY 430
Cdd:cd18041  116 TCLGINHP----IFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAH 191
                        250
                 ....*....|...
gi 119392094 431 GARVVrTLTVQYR 443
Cdd:cd18041  192 PDAVV-QLTIQYR 203
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
192-443 6.96e-45

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: 162.03  E-value: 6.96e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALsQKELAIIHGPPGTGKTTTVVEIILQAVKQGL-KVLCCAPSNIAVDNLVERLALCKQRILRLghPAR 270
Cdd:cd18039    2 LNHSQVDAVKTAL-QRPLSLIQGPPGTGKTVTSATIVYHLVKQGNgPVLVCAPSNVAVDQLTEKIHQTGLKVVRL--CAK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 271 LLESIQQHSLDAVLARsdsaqivaDIRK-DIDQVFVKNKKTQDKREKSNFRNEIKLlrKELKEREEAAMLESltsANVVL 349
Cdd:cd18039   79 SREAVESPVSFLALHN--------QVRNlDSAEKLELLKLLKLETGELSSADEKRY--RKLKRKAERELLRN---ADVIC 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 350 ATNTGAsADgplKLLPESYFDVVVIDECAQALEASCWIPLLK-ARKCILAGDHKQLPPTTVSHKAALAGLSLSLMERLAe 428
Cdd:cd18039  146 CTCVGA-GD---PRLSKMKFRTVLIDEATQATEPECLIPLVHgAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLV- 220
                        250
                 ....*....|....*
gi 119392094 429 EYGARVVRtLTVQYR 443
Cdd:cd18039  221 QLGIRPIR-LQVQYR 234
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
192-443 1.29e-37

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: 140.43  E-value: 1.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALS-QKELAIIHGPPGTGKTTTVVEII-------------------------LQAVKQGLKVLCCAPSN 245
Cdd:cd18042    1 LNESQLEAIASALQnSPGITLIQGPPGTGKTKTIVGILsvllagkyrkyyekvkkklrklqrnLNNKKKKNRILVCAPSN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 246 IAVDNLVERLalckqrilrlghparllesiqqhsldavlarsdsaqivadirkdidqvfvKNKKTQDKREKSNFRNEIKL 325
Cdd:cd18042   81 AAVDEIVLRL--------------------------------------------------LSEGFLDGDGRSYKPNVVRV 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 326 LRKELKEreeaamlESLTSANVVLATNTGASADgPLKLLPESyFDVVVIDECAQALEASCWIPL-LKARKCILAGDHKQL 404
Cdd:cd18042  111 GRQELRA-------SILNEADIVCTTLSSSGSD-LLESLPRG-FDTVIIDEAAQAVELSTLIPLrLGCKRLILVGDPKQL 181
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 119392094 405 PPTTVSHKAALAGLSLSLMERLaEEYGARVVrTLTVQYR 443
Cdd:cd18042  182 PATVFSKVAQKLGYDRSLFERL-QLAGYPVL-MLTTQYR 218
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
196-443 1.89e-37

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: 140.45  E-value: 1.89e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 196 QKEAVLFALSQKELA---IIHGPPGTGKTTTVVEIILQAVKQ--GLKVLCCAPSNIAVDNLVERLA---LCKQRILRLGH 267
Cdd:cd18038    6 QKLAVRNIVTGTSRPppyIIFGPPGTGKTVTLVEAILQVLRQppEARILVCAPSNSAADLLAERLLnalVTKREILRLNA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 268 PARllesiqqhsldavlarsdsaqivadIRKDIDQVFVKnkktqdkreksnFRNEIKLLRKELKEREEaamlesLTSANV 347
Cdd:cd18038   86 PSR-------------------------DRASVPPELLP------------YCNSKAEGTFRLPSLEE------LKKYRI 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 348 VLATNTGASadgplKL----LPESYFDVVVIDECAQALEASCWIPL----LKARKCILAGDHKQLPPTTVSHKAALAGLS 419
Cdd:cd18038  123 VVCTLMTAG-----RLvqagVPNGHFTHIFIDEAGQATEPEALIPLselaSKNTQIVLAGDPKQLGPVVRSPLARKYGLG 197
                        250       260       270
                 ....*....|....*....|....*....|..
gi 119392094 420 LSLMERLAE--------EYGARVVRTLTVQYR 443
Cdd:cd18038  198 KSLLERLMErplyykdgEYNPSYITKLLKNYR 229
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
209-443 3.56e-30

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: 115.41  E-value: 3.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 209 LAIIHGPPGTGKTTTVVEIILQAVKQ--GLKVLCCAPSNIAVDNLverlalckqrilrlghparllesiqqhsldavlar 286
Cdd:cd17934    1 ISLIQGPPGTGKTTTIAAIVLQLLKGlrGKRVLVTAQSNVAVDNV----------------------------------- 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 287 sdsaqivadirkdidqvfvknkktqdkreksnfrneikllrkelkereeaamlesltsanvvlatntgasadgplkllpe 366
Cdd:cd17934      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119392094 367 syfDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVSHKAALAGLS--LSLMERLAEEYGARVVRTLTVQYR 443
Cdd:cd17934   46 ---DVVIIDEASQITEPELLIALIRAKKVVLVGDPKQLPPVVQEDHAALLGLSfiLSLLLLFRLLLPGSPKVMLDTQYR 121
R3H_Smubp-2_like cd02641
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and ...
726-784 1.38e-27

R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and an AN1-like Zinc finger domain and have been shown to bind single-stranded DNA. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.


Pssm-ID: 100070  Cd Length: 60  Bit Score: 105.90  E-value: 1.38e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 726 VDHFRAMIVEFMAS-KKMQLEFPPSLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd02641    1 VKHLKAMVKAFMKDpKATELEFPPTLSSHDRLLVHELAEELGLRHESTGEGSDRVITVSK 60
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
191-443 1.40e-25

DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain]  Cd Length: 230  Bit Score: 106.30  E-value: 1.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 191 CLDTSQKEAV---LFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQ--GLKVLCCAPSNIAVDNLVERLALCKqrILRL 265
Cdd:cd18078    1 DLNELQKEAVkriLGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNlpRSRILVCAPSNSAADLVTSRLHESK--VLKP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 266 GHPARllesiqqhsLDAVLARSDsaqIVADIRKDIDqvfvknKKTQDKREKSNFRneikllrkelkereeaamlesltsa 345
Cdd:cd18078   79 GDMVR---------LNAVNRFES---TVIDARKLYC------RLGEDLSKASRHR------------------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 346 nVVLATNTGASADGPLKlLPESYFDVVVIDECAQALEASCWIPL----LKARKCILAGDHKQLPPTTVSHKAALAGLSLS 421
Cdd:cd18078  116 -IVISTCSTAGLLYQMG-LPVGHFTHVFVDEAGQATEPESLIPLglisSRDGQIILAGDPMQLGPVIKSRLASAYGLGVS 193
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 119392094 422 LMERLAEE---------------YGARVVRTLTVQYR 443
Cdd:cd18078  194 FLERLMNRplylrdpnrfgesggYNPLLVTKLVDNYR 230
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
192-443 6.16e-20

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: 91.05  E-value: 6.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALSqKELAIIHGPPGTGKTTTVVEIILQAVKQ-------------GLKVLCCAPSNIAVDNLVERL-AL 257
Cdd:cd18040    2 LNPSQNHAVRTALT-KPFTLIQGPPGTGKTVTGVHIAYWFAKQnreiqsvsgegdgGPCVLYCGPSNKSVDVVAELLlKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 258 CKQRILRL-GHPARLLE----SIQQHSLDAVLARSDSAQIVADI--RKDIDQVfvKNKKTQDKREksnFRNEIKLLRKEL 330
Cdd:cd18040   81 PGLKILRVySEQIETTEypipNEPRHPNKKSERESKPNSELSSItlHHRIRQP--SNPHSQQIKA---FEARFERTQEKI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 331 KEREE--------AAMLESLTSANVVLATNTGASADgplKLLPESYFDVVVIDECAQALEASCWIPLLKARKC---ILAG 399
Cdd:cd18040  156 TEEDIktykiliwEARFEELETVDVILCTCSEAASQ---KMRTHANVKQCIVDECGMCTEPESLIPIVSAPRAeqvVLIG 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 119392094 400 DHKQLPPTTVSHKAALAGLSLSLMERLAEEygarvVRTLTVQYR 443
Cdd:cd18040  233 DHKQLRPVVQNKEAQKLGLGRSLFERYAEK-----ACMLDTQYR 271
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
192-442 9.07e-20

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: 87.60  E-value: 9.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALSQkELAIIHGPPGTGKTTT---VVEIILQAVKQGLK--VLCCAPSNIAVDNLVER-LALCKQRILRL 265
Cdd:cd17936    2 LDPSQLEALKHALTS-ELALIQGPPGTGKTFLgvkLVRALLQNQDLSITgpILVVCYTNHALDQFLEGlLDFGPTKIVRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 266 GhparllesiqqhsldavlarsdsaqivadirkdidqvfvknkktqdkreksnfrneikllrkelkereeaamlesltsA 345
Cdd:cd17936   81 G------------------------------------------------------------------------------A 82
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 346 NVVLATNTGASADgpLKLLPESYFDVVVIDECAQALEA---SCWIPllKARKCILAGDHKQLPPTTVSHKAALAG--LSL 420
Cdd:cd17936   83 RVIGMTTTGAAKY--RELLQALGPKVVIVEEAAEVLEAhilAALTP--STEHLILIGDHKQLRPKVNVYELTAKKynLDV 158
                        250       260
                 ....*....|....*....|..
gi 119392094 421 SLMERLAEEyGARVVrTLTVQY 442
Cdd:cd17936  159 SLFERLVKN-GLPFV-TLNVQR 178
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
706-785 1.19e-18

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 81.19  E-value: 1.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094   706 APSQPSLNGGSPEGVESQDGVDHFRAMIVEFMASKKMQLEFPPsLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSKR 785
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVKSTKESVELPP-MNSYERKIVHELAEKYGLESESFGEGPKRRVVISKK 79
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
192-430 4.17e-13

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: 69.82  E-value: 4.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALSQKELAI----IHGPPGTGKTTTVVEIILQAVKQ-GLKVLCCAPSNIAVDNLVERLAlckqrilrlg 266
Cdd:cd18077    2 LNAKQKEAVLAITTPLSIQLppvlLIGPFGTGKTFTLAQAVKHILQQpETRILICTHSNSAADLYIKEYL---------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 267 HPARLLESIQQHSLdAVLARSDSaqiVADIRKDIDQVFVKNkktqdkrEKSNFRNEIKllrkelkereeaamlESLTSAN 346
Cdd:cd18077   72 HPYVETGNPRARPL-RVYYRNRW---VKTVHPVVQKYCLID-------EHGTFRMPTR---------------EDVMRHR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 347 VVLATNTGASADGPLKLLPeSYFDVVVIDECAQALEASCWIPLLKARK---CILAGDHKQLPPTTVSHKAALAGLSLSLM 423
Cdd:cd18077  126 VVVVTLSTSQYLCQLDLEP-GFFTHILLDEAAQAMECEAIMPLALATKstrIVLAGDHMQLSPEVYSEFARERNLHISLL 204

                 ....*..
gi 119392094 424 ERLAEEY 430
Cdd:cd18077  205 ERLYEHY 211
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
192-253 6.24e-12

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: 69.24  E-value: 6.24e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119392094 192 LDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVE 253
Cdd:COG0507  125 LSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRLSE 186
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
726-784 8.81e-12

R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100064  Cd Length: 59  Bit Score: 61.09  E-value: 8.81e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 726 VDHFRAMIVEFMASK-KMQLEFPPsLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd02325    1 REEREEELEAFAKDAaGKSLELPP-MNSYERKLIHDLAEYYGLKSESEGEGPNRRVVITK 59
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
733-784 1.17e-11

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 60.58  E-value: 1.17e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119392094  733 IVEFMASKKMQLEFPPsLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:pfam01424  10 LAEFVKDTGKSLELPP-MSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
195-450 1.38e-11

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: 64.76  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 195 SQKEAVLFAlSQKELAIIHGPPGTGKTTTVVEII--LQAVKQGLKVLCCAPSNIAVDNLVERL--ALCKQR-ILRLGHPA 269
Cdd:cd17935    9 TQIEAIRSG-MQPGLTMVVGPPGTGKTDVAVQIIsnLYHNFPNQRTLIVTHSNQALNQLFEKImaLDIDERhLLRLGHGA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 270 RLLESIQQHsldAVLARSDsaqivadirkdidqvFVknkktqdkreKSNFRneikllrkelkereeaamlesltsanvvl 349
Cdd:cd17935   88 KIIAMTCTH---AALKRGE---------------LV----------ELGFK----------------------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 350 atntgasadgplkllpesyFDVVVIDECAQALEASCWIPLL---------KARKCILAGDHKQLPPttVSHKAALAGLS- 419
Cdd:cd17935  111 -------------------YDNILMEEAAQILEIETFIPLLlqnpedgpnRLKRLIMIGDHHQLPP--VIKNMAFQKYSn 169
                        250       260       270
                 ....*....|....*....|....*....|...
gi 119392094 420 --LSLMERLAeEYGARVVRtLTVQYRMHQAIMR 450
Cdd:cd17935  170 meQSLFTRLV-RLGVPTVD-LDAQGRARASISS 200
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
193-406 2.76e-11

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: 61.83  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 193 DTSQKEAVLFALSQKeLAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDnlverlalckqrilrlghparll 272
Cdd:cd18043    1 DSSQEAAIISARNGK-NVVIQGPPGTGKSQTIANIIANALARGKRVLFVSEKKAALD----------------------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 273 esiqqhsldaVLARSdsaqivadirkdidqvfvknkktqdkreksnfrneikllrkelkereeaAMLESLTSANVVLATN 352
Cdd:cd18043   57 ----------VVRFP-------------------------------------------------CWIMSPLSVSQYLPLN 77
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119392094 353 TGasadgplkllpesYFDVVVIDECAQALEASCwIPLL-KARKCILAGDHKQLPP 406
Cdd:cd18043   78 RN-------------LFDLVIFDEASQIPIEEA-LPALfRGKQVVVVGDDKQLPP 118
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
196-253 3.50e-10

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: 59.49  E-value: 3.50e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119392094 196 QKEAVLFALSQKeLAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVE 253
Cdd:cd17933    2 QKAAVRLVLRNR-VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAPTGKAAKRLSE 58
R3H_G-patch cd02646
R3H domain of a group of fungal and plant proteins with unknown function, who also contain a ...
726-784 4.81e-09

R3H domain of a group of fungal and plant proteins with unknown function, who also contain a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the R3H domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100075  Cd Length: 58  Bit Score: 53.34  E-value: 4.81e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119392094 726 VDHFRAMIVEFMASKKMQLEFPPsLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd02646    1 IEDIKDEIEAFLLDSRDSLSFPP-MDKHGRKTIHKLANCYNLKSKSRGKGKKRFVTVTK 58
ZnF_AN1 smart00154
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ...
902-937 1.18e-08

AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis.


Pssm-ID: 197545  Cd Length: 39  Bit Score: 51.62  E-value: 1.18e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 119392094   902 CTAGVTTLGQFCQLCSRRYCLSHHLPEIHGCGERAR 937
Cdd:smart00154   4 CRKKVGLTGFKCRHCGNLFCGEHRLPEDHDCPGDYK 39
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
533-608 1.45e-08

C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. 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. The 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: 350173 [Multi-domain]  Cd Length: 89  Bit Score: 52.82  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 533 RDIAVVSPYNLQVDLLRQSLVHRH------PELEIKSVDGFQGREKEAVILSFVRSNrkgevgfLAEDRRINVAVTRARR 606
Cdd:cd18786   11 YKGVVLTPYHRDRAYLNQYLQGLSldefdlQLVGAITIDSSQGLTFDVVTLYLPTAN-------SLTPRRLYVALTRARK 83

                 ..
gi 119392094 607 HV 608
Cdd:cd18786   84 RL 85
AAA_19 pfam13245
AAA domain;
196-265 1.55e-08

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 54.15  E-value: 1.55e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119392094  196 QKEAVLFALSQKeLAIIHGPPGTGKTTTVVEIILQAVKQG---LKVLCCAPSNIAVDNLVERLALCKQRILRL 265
Cdd:pfam13245   1 QREAVRTALPSK-VVLLTGGPGTGKTTTIRHIVALLVALGgvsFPILLAAPTGRAAKRLSERTGLPASTIHRL 72
zf-AN1 pfam01428
AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in ...
897-934 2.02e-08

AN1-like Zinc finger; Zinc finger at the C-terminus of An1, a ubiquitin-like protein in Xenopus laevis. The following pattern describes the zinc finger. C-X2-C-X(9-12)-C-X(1-2)-C-X4-C-X2-H-X5-H-X-C Where X can be any amino acid, and numbers in brackets indicate the number of residues.


Pssm-ID: 460208  Cd Length: 37  Bit Score: 50.77  E-value: 2.02e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 119392094  897 CGFAKCTAGVTTLGQfCQLCSRRYCLSHHLPEIHGCGE 934
Cdd:pfam01428   1 CSFKGCKKKDFLPFK-CRFCGKNFCLKHRLPEDHDCSG 37
R3H_DEXH_helicase cd06007
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may ...
732-784 2.61e-08

R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may function as ATP-dependent DNA or RNA helicases. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100077  Cd Length: 59  Bit Score: 51.16  E-value: 2.61e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119392094 732 MIVEFMASKKMQLEFPPSLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd06007    7 ALEDFRASDNEEYEFPSSLTNHERAVIHRLCRKLGLKSKSKGKGSNRRLSVYK 59
DEXDc smart00487
DEAD-like helicases superfamily;
196-256 1.93e-07

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 52.49  E-value: 1.93e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119392094   196 QKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGL--KVLCCAPSNIAVDNLVERLA 256
Cdd:smart00487  13 QKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELK 75
R3H_NRF cd02640
R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB ...
730-784 2.05e-07

R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB proteins that can silence the IFNbeta promoter via binding to a negative regulatory element (NRE). Beside R3H NRF also contains a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100069  Cd Length: 60  Bit Score: 48.55  E-value: 2.05e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119392094 730 RAMIVEFMASKKMQ-LEFPPSLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSK 784
Cdd:cd02640    5 RQIIQNYAHSDDIRdMVFSPEFSKEERALIHQIAQKYGLKSRSYGSGNDRYLVISK 60
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
192-280 3.33e-07

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: 51.80  E-value: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  192 LDTSQKEAV-LFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALCKQRILRLGHPAR 270
Cdd:pfam13604   2 LNAEQAAAVrALLTSGDRVAVLVGPAGTGKTTALKALREAWEAAGYRVIGLAPTGRAAKVLGEELGIPADTIAKLLHRLG 81
                          90
                  ....*....|
gi 119392094  271 LLESIQQHSL 280
Cdd:pfam13604  82 GRAGLDPGTL 91
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
346-442 7.82e-07

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: 49.02  E-value: 7.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 346 NVVLATNTGASADgplkllpesYFDVVVIDECAQALEASCWIP---LLKARKCILAGDHKQLPPTTVSHKAALAGLSLSL 422
Cdd:cd17914   33 RILLVTPTNKAAA---------QLDNILVDEAAQILEPETSRLidlALDQGRVILVGDHDQLGPVWRGAVLAKICNEQSL 103
                         90       100
                 ....*....|....*....|
gi 119392094 423 MERLAeEYGARVVRtLTVQY 442
Cdd:cd17914  104 FTRLV-RLGVSLIR-LQVQY 121
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
192-406 8.12e-07

N-terminal DEXXQ-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: 350834 [Multi-domain]  Cd Length: 230  Bit Score: 51.04  E-value: 8.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALSQKELA------IIHGPPGTGKTTTVVEIILQAVKQ-GLKVLCCAPSNIAVDNLVERLAlckQRILR 264
Cdd:cd18076    2 GNNKQQLAFNFIAGKPSEArfvpplLIYGPFGTGKTFTLAMAALEVIREpGTKVLICTHTNSAADIYIREYF---HPYVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 265 LGHPArlLESIQQHSLDAVLARSDSAQIVADIRKDIDQVFvknkktqdkreksnfrneikllrkELKEREEaamlesLTS 344
Cdd:cd18076   79 KGHPE--ARPLRIKATDRPNAITDPDTITYCCLTKDRQCF------------------------RLPTRDE------LDF 126
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119392094 345 ANVVLATNTGASAdgpLKLLPeSYFDVVVIDECAQALEASCWIPLLKA---RKCILAGDHKQLPP 406
Cdd:cd18076  127 HNIVITTTAMAFN---LHVLS-GFFTHIFIDEAAQMLECEALIPLSYAgpkTRVVLAGDHMQMTP 187
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
192-555 5.06e-06

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


Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 50.32  E-value: 5.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 192 LDTSQKEAVLFALSQkeLAIIHGPpGTGKTTTVVEIILQAVKQGL----KVLCCAPSNIAVDNLVERL------------ 255
Cdd:COG0210    7 LNPEQRAAVEHPEGP--LLVLAGA-GSGKTRVLTHRIAYLIAEGGvdpeQILAVTFTNKAAREMRERIeallgrlarglw 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 256 -----ALCkQRILRLgHPARL-LESIQQhsldaVLARSDSAQIVADIRKDIDQvfvknkkTQDKREKSNFRNEIKLLRKE 329
Cdd:COG0210   84 vgtfhSLA-LRILRR-HAELLgLPPNFT-----ILDGDDQLRLIKELLKELGL-------DEKRFPPRELLSLISRAKNE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 330 LKEREEAAMLESLTSANVVLAT----------NTGAsAD------GPLKLL---PE------SYFDVVVIDEC-----AQ 379
Cdd:COG0210  150 GLTPEELAELLAADPEWRAAAElyeayqerlrANNA-LDfddlllLAVRLLeenPEvlekyqNRFRYILVDEYqdtnpAQ 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 380 ALeascwipLLKArkciLAGDHKQLpptTV---------SHKAAlaglSLSLMERLAEEYGARVVRTLTVQYRMHQAImr 450
Cdd:COG0210  229 YE-------LLRL----LAGDGRNL---CVvgdddqsiyGFRGA----DPENILRFEKDFPDAKVIKLEQNYRSTQNI-- 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 451 wasdtmylgqLTAHSSVARHLLRDLPGVAATE-ETGVPLLLVdtagcglfELEEEDEqskgnpgEVRLVSLHIQALVDAG 529
Cdd:COG0210  289 ----------LDAANAVIANNPGRLGKNLWTDnGEGEKVRLY--------VAPDEEE-------EARFVADEIRELHEEG 343
                        410       420
                 ....*....|....*....|....*.
gi 119392094 530 VPARDIAVVSPYNLQVDLLRQSLVHR 555
Cdd:COG0210  344 VPLSDIAVLYRTNAQSRALEEALRRA 369
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
209-251 6.20e-06

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: 46.33  E-value: 6.20e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 119392094 209 LAIIHGPPGTGKTTTVVEIIL----QAVKQGLKVLCCAPSNIAVDNL 251
Cdd:cd17914    1 LSLIQGPPGTGKTRVLVKIVAalmqNKNGEPGRILLVTPTNKAAAQL 47
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
733-785 5.49e-05

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 41.82  E-value: 5.49e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119392094 733 IVEFMASKK-MQLEFPPSlNSHDRLRVHQIAEEHGLRHDSSGEGKRRfITVSKR 785
Cdd:cd02642   12 LLAFIKDSTrQSLELPPM-NSYYRLLAHRVAQYYGLDHNVDNSGGKC-VIVNKT 63
PRK12438 PRK12438
hypothetical protein; Provisional
786-845 1.05e-04

hypothetical protein; Provisional


Pssm-ID: 171499 [Multi-domain]  Cd Length: 991  Bit Score: 46.39  E-value: 1.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 786 APRPRAALGPPAGTGGPAPLQPVPPtPAQTEQPPREQRGPDQPDLRTLHLER-LQRVRSAQ 845
Cdd:PRK12438 905 APGGDAASAPPPGAGPPAPPQAVPP-PRTTQPPAAPPRGPDVPPAAVAELREtLADLRSAQ 964
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
173-275 1.19e-04

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: 45.91  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  173 RSAPSPASE-IHPLTFFNTcldtSQKEAVLFALSQKeLAIIHGPPGTGKTTTVVEIIL----QAVKQG-LKVLCCAPSNI 246
Cdd:TIGR01447 129 RTAPSAILEnLFPLLNEQN----WRKTAVALALKSN-FSLITGGPGTGKTTTVARLLLalvkQSPKQGkLRIALAAPTGK 203
                          90       100
                  ....*....|....*....|....*....
gi 119392094  247 AVDNLVERLalcKQRILRLGHPARLLESI 275
Cdd:TIGR01447 204 AAARLAESL---RKAVKNLAAAEALIAAL 229
SF1_C_UvrD cd18807
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ...
501-612 1.52e-04

C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD family helicases 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: 350194 [Multi-domain]  Cd Length: 150  Bit Score: 42.99  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 501 LEEEDEQSkgnpgEVRLVSLHIQALVDAG-VPARDIAVVSPYNLQVDLLRQSLvhrhpELEIKSVDGFQGREKEAVILSF 579
Cdd:cd18807   37 LLAKDEAD-----EAKAIADEIKRLIESGpVQYSDIAILVRTNRQARVIEEAL-----RVTLMTIHASKGLEFPVVFIVG 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119392094 580 VRSNRKGEVGF----------LAEDRRI-NVAVTRARRHVAVIC 612
Cdd:cd18807  107 LGEGFIPSDASyhaakedeerLEEERRLlYVALTRAKKELYLVG 150
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
207-255 2.31e-04

DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 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: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 42.54  E-value: 2.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 119392094 207 KELAIIHGPPGTGKTTTVV-EIILQAVKQGLKVLCCAPSNIAVDNLVERL 255
Cdd:cd17931    1 GQLTVLDLHPGAGKTTRVLpQIIREAIKKRLRTLVLAPTRVVAAEMYEAL 50
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
211-359 2.31e-04

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 43.75  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 211 IIHGPPGTGKTTTVVEIILQAVKQGLKVLCcapsnIAVDNLVERLalcKQRILRLGHP-ARLLES--IQQHSLDAVLARS 287
Cdd:COG0467   24 LLSGPPGTGKTTLALQFLAEGLRRGEKGLY-----VSFEESPEQL---LRRAESLGLDlEEYIESglLRIIDLSPEELGL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 288 DSAQIVADIRKDIDqvfvknkKTQDKR--------------EKSNFRNEIKLLRKELKEREEAAMLESLTSANVVLATNT 353
Cdd:COG0467   96 DLEELLARLREAVE-------EFGAKRvvidslsglllalpDPERLREFLHRLLRYLKKRGVTTLLTSETGGLEDEATEG 168

                 ....*...
gi 119392094 354 GAS--ADG 359
Cdd:COG0467  169 GLSylADG 176
PHA03247 PHA03247
large tegument protein UL36; Provisional
662-878 2.29e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  662 AATKPQGPATSTRTGSQRQEGGQEAAAPARQgrkKPAGKSLASEAPSQPSLNGGSPEGVESQDGVDHFRAMIVEFMASKK 741
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAA---PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP 2820
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  742 MQLEFPPSLNSHDRLRVH-QIAEEHGLRHDSSGEGKRRFITVSKRAPRPRAALGPPAGTGGPAPLQPVPPTPAQTE---Q 817
Cdd:PHA03247 2821 AASPAGPLPPPTSAQPTApPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsfaL 2900
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094  818 PPREQRGPDQPDLRTLHLERLQRVRSAQGQPAsKEQQASGQQKLPEKKKKKAKGHPATDLP 878
Cdd:PHA03247 2901 PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP-PPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
211-268 2.30e-03

DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family 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: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 39.75  E-value: 2.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119392094 211 IIHGPPGTGKTTTVVEIILQA---VKQGLKVLCCAPSNIAVDNLVERLAlcKQRILRLGHP 268
Cdd:cd17917    5 VIVGETGSGKTTQVPQFLLEDglaKGGKGRIVCTQPRRIAAISVAERVA--EERGEKLGEE 63
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
211-293 2.36e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.66  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094   211 IIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALCKQRILRLGHPARLLESIQQhsldavLARSDSA 290
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA------LARKLKP 79

                   ...
gi 119392094   291 QIV 293
Cdd:smart00382  80 DVL 82
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
194-266 3.08e-03

DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 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: 350746 [Multi-domain]  Cd Length: 180  Bit Score: 39.79  E-value: 3.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119392094 194 TSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIIL-QAVKQGL--KVLCCAPSNIAVDNLVERlaLCKQRILRLG 266
Cdd:cd17988    4 YAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILdHYYKRGKycNIVVTQPRRIAAISIARR--VSQEREWTLG 77
PHA03247 PHA03247
large tegument protein UL36; Provisional
657-863 3.20e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  657 QGSSHAATKPQGPATSTRTGSQRQEGGQEAAAPARQGRKKP-------AGKSLASEAP--SQPSLNGGSPEGVESQDG-- 725
Cdd:PHA03247  255 PAPPPVVGEGADRAPETARGATGPPPPPEAAAPNGAAAPPDgvwgaalAGAPLALPAPpdPPPPAPAGDAEEEDDEDGam 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094  726 -----VDHFRAMIVEFMASKKMQLEFPPS----LNS---HDRLRVHQIAEEHGLRHDSS--GEGKRRFITVSKRAPRPrA 791
Cdd:PHA03247  335 evvspLPRPRQHYPLGFPKRRRPTWTPPSsledLSAgrhHPKRASLPTRKRRSARHAATpfARGPGGDDQTRPAAPVP-A 413
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119392094  792 ALGPPAGTGGPAPLQPVPPTPAQTEQPPrEQRGPDQPDLRTLHLERLQRVRSAQGQPASKEQQASGQQKLPE 863
Cdd:PHA03247  414 SVPTPAPTPVPASAPPPPATPLPSAEPG-SDDGPAPPPERQPPAPATEPAPDDPDDATRKALDALRERRPPE 484
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
204-275 3.26e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 3.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119392094 204 LSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCcapsnIAVDNLVERLALCKQRilrlGHPARLLESI 275
Cdd:NF038214  87 IERAENVLLLGPPGTGKTHLAIALGYAACRQGYRVRF-----TTAADLVEQLAQARAD----GRLGRLLRRL 149
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
195-256 4.12e-03

DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD 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: 350690 [Multi-domain]  Cd Length: 189  Bit Score: 39.42  E-value: 4.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119392094 195 SQKEAVLfaLSQKELAIIHGPpGTGKTTTVVEIILQAVKQGlkvlCCAPSNI--------AVDNLVERLA 256
Cdd:cd17932    3 EQREAVT--HPDGPLLVLAGA-GSGKTRVLTHRIAYLILEG----GVPPERIlavtftnkAAKEMRERLR 65
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
196-239 7.79e-03

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 37.90  E-value: 7.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 119392094 196 QKEAVLFALSQKELA--IIHGPPGTGKTTTVVEIILQAVKQGLKVL 239
Cdd:cd00009    6 AIEALREALELPPPKnlLLYGPPGTGKTTLARAIANELFRPGAPFL 51
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
197-267 8.61e-03

DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 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: 350732 [Multi-domain]  Cd Length: 174  Bit Score: 38.25  E-value: 8.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119392094 197 KEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQA--VKQGLKVLCCAPSNIAVDNLVERLAlcKQRILRLGH 267
Cdd:cd17974    7 RDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAgyTKGGGKIGCTQPRRVAAMSVAARVA--EEMGVKLGN 77
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
204-260 9.33e-03

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.99  E-value: 9.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119392094 204 LSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCcapsnIAVDNLVERLALCKQ 260
Cdd:COG1484   96 IERGENLILLGPPGTGKTHLAIALGHEACRAGYRVRF-----TTAPDLVNELKEARA 147
 
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