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Conserved domains on  [gi|2289947589|gb|UVM88886|]
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MAG: Utp25 [Bacteriophage sp.]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11437332)

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

CATH:  1.20.1320.20|3.40.50.300
EC:  3.6.4.-
Gene Ontology:  GO:0005524|GO:0004386|GO:0003676
PubMed:  20206133
SCOP:  3002019

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
101-452 2.30e-41

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


:

Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 155.95  E-value: 2.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 101 KYKLRPEQEKAVKAVINNKIGNTPFhiGVLDYTVNAGKTLIMSSLYLTYKKQLKTLLITNDSDWLNQAREEFKQYLPgeD 180
Cdd:COG1061    78 SFELRPYQQEALEALLAALERGGGR--GLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRRELLEQWAEELRRFLG--D 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 181 ITFVQGKVLNWSNFTIGMVQSISRNMRsYQKELSQIDMVLIDEADQGGSKQYQNVItRLFNTRIRIGLSGTIYMSklakD 260
Cdd:COG1061   154 PLAGGGKKDSDAPITVATYQSLARRAH-LDELGDRFGLVIIDEAHHAGAPSYRRIL-EAFPAAYRLGLTATPFRS----D 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 261 rvKNMNLECFFGKVIAEFKLKDSIKKGYSTKTVVKMVPGKpwYGNWESDCISYKEIYDDSITNCYTAWLMAYNRLLWNLN 340
Cdd:COG1061   228 --GREILLFLFDGIVYEYSLKEAIEDGYLAPPEYYGIRVD--LTDERAEYDALSERLREALAADAERKDKILRELLREHP 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 341 QGRyPALVVCKHIAHCENLYKFFKKKlgdAYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRYLLN 420
Cdd:COG1061   304 DDR-KTLVFCSSVDHAEALAELLNEA---GIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIL 379

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2289947589 421 AASMDSQEKSIQFLGRLVRTDKSKKKVYLDDL 452
Cdd:COG1061   380 LRPTGSPREFIQRLGRGLRPAPGKEDALVYDF 411
 
Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
101-452 2.30e-41

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 155.95  E-value: 2.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 101 KYKLRPEQEKAVKAVINNKIGNTPFhiGVLDYTVNAGKTLIMSSLYLTYKKQLKTLLITNDSDWLNQAREEFKQYLPgeD 180
Cdd:COG1061    78 SFELRPYQQEALEALLAALERGGGR--GLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRRELLEQWAEELRRFLG--D 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 181 ITFVQGKVLNWSNFTIGMVQSISRNMRsYQKELSQIDMVLIDEADQGGSKQYQNVItRLFNTRIRIGLSGTIYMSklakD 260
Cdd:COG1061   154 PLAGGGKKDSDAPITVATYQSLARRAH-LDELGDRFGLVIIDEAHHAGAPSYRRIL-EAFPAAYRLGLTATPFRS----D 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 261 rvKNMNLECFFGKVIAEFKLKDSIKKGYSTKTVVKMVPGKpwYGNWESDCISYKEIYDDSITNCYTAWLMAYNRLLWNLN 340
Cdd:COG1061   228 --GREILLFLFDGIVYEYSLKEAIEDGYLAPPEYYGIRVD--LTDERAEYDALSERLREALAADAERKDKILRELLREHP 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 341 QGRyPALVVCKHIAHCENLYKFFKKKlgdAYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRYLLN 420
Cdd:COG1061   304 DDR-KTLVFCSSVDHAEALAELLNEA---GIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIL 379

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2289947589 421 AASMDSQEKSIQFLGRLVRTDKSKKKVYLDDL 452
Cdd:COG1061   380 LRPTGSPREFIQRLGRGLRPAPGKEDALVYDF 411
uvsW PHA02558
UvsW helicase; Provisional
 24-470 6.01e-23

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 101.62  E-value: 6.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589  24 LYNEFAIRHPNAFYLRTRQRGmqNWDGKIHYITKTGQFKIGLLPKVYDMCIEMGIKPKV---VDMRQPLPK------VSK 94
Cdd:PHA02558   26 LRDYFSFEVPGYKFNPKFKYG--GWDGKIRLLDYNGLLPYGLVGQLKKFAKNRGYSIWVdprIEENEDISRedfdewVSS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589  95 VVTNIGKYKLRPE--QEKAVKAVINN--KIGNTPfhigvldytVNAGKTLIMSSL--YLTYKKQLKTLLITNDSDWLNQA 168
Cdd:PHA02558  104 LEIYSGNKKIEPHwyQYDAVYEGLKNnrRLLNLP---------TSAGKSLIQYLLsrYYLENYEGKVLIIVPTTSLVTQM 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 169 REEFKQY--LPGEDITFVQGKVLNWSN--FTIGMVQSISRNMRSYqkeLSQIDMVLIDEADQGGSKQYQNVITRLFNTRI 244
Cdd:PHA02558  175 IDDFVDYrlFPREAMHKIYSGTAKDTDapIVVSTWQSAVKQPKEW---FDQFGMVIVDECHLFTGKSLTSIITKLDNCKF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 245 RIGLSGTiymskLAKDRVKNMNLECFFGKVIAEFKLKDSIKKGYSTKTVVKMVpgkpWYGNWESDCISYK-EIYDDSITn 323
Cdd:PHA02558  252 KFGLTGS-----LRDGKANILQYVGLFGDIFKPVTTSQLMEEGQVTDLKINSI----FLRYPDEDRVKLKgEDYQEEIK- 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 324 cYTAWLMAYNRLLWN----LNQGRYPALVVCKHIAHCENLYKFFkKKLGDayNIAYVHVNTKSKLRQQIMKDFRDGK-ID 398
Cdd:PHA02558  322 -YITSHTKRNKWIANlalkLAKKGENTFVMFKYVEHGKPLYEML-KKVYD--KVYYVSGEVDTEDRNEMKKIAEGGKgII 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2289947589 399 ILVSTTIIARGKNFPKLRYLLNAASMDSQEKSIQFLGRLVRTDKSKKKVYL----DDLHYPGPYLDRHGKHRKQYY 470
Cdd:PHA02558  398 IVASYGVFSTGISIKNLHHVIFAHPSKSKIIVLQSIGRVLRKHGSKSIATVwdiiDDLSVKPKSANAKKKYVHLNY 473
ResIII pfam04851
Type III restriction enzyme, res subunit;
101-251 3.35e-18

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 81.56  E-value: 3.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 101 KYKLRPEQEKAVKAVINnKIGNTPFHiGVLDYTVNAGKTLIMSSLYLTYKKQL---KTLLITNDSDWLNQAREEFKQYLP 177
Cdd:pfam04851   1 KLELRPYQIEAIENLLE-SIKNGQKR-GLIVMATGSGKTLTAAKLIARLFKKGpikKVLFLVPRKDLLEQALEEFKKFLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 178 GED--ITFVQGK----VLNWSNFTIGMVQSISRNMRSYQKELS--QIDMVLIDEADQGGSKQYQNVItRLFNTRIRIGLS 249
Cdd:pfam04851  79 NYVeiGEIISGDkkdeSVDDNKIVVTTIQSLYKALELASLELLpdFFDVIIIDEAHRSGASSYRNIL-EYFKPAFLLGLT 157


                  ..
gi 2289947589 250 GT 251
Cdd:pfam04851 158 AT 159
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 104-251 2.50e-15

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 73.11  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 104 LRPEQEKAVKAVINNKIGNTpfhiGVLDYTVNAGKTLIMSSLYLtYKKQLKTLLITNDSDWLNQAREEFKQYLPGEDITF 183
Cdd:cd17926     1 LRPYQEEALEAWLAHKNNRR----GILVLPTGSGKTLTALALIA-YLKELRTLIVVPTDALLDQWKERFEDFLGDSSIGL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2289947589 184 VQG---KVLNWSNFTIGMVQSISRNMRSYQKELSQIDMVLIDEADQGGSKQYQNVITRlFNTRIRIGLSGT 251
Cdd:cd17926    76 IGGgkkKDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSEILKE-LNAKYRLGLTAT 145
HELICc smart00490
helicase superfamily c-terminal domain;
357-439 1.85e-12

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 62.61  E-value: 1.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589  357 ENLYKFFKKKlgdAYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRYLLNAASMDSQEKSIQFLGR 436
Cdd:smart00490   1 EELAELLKEL---GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77


                   ...
gi 2289947589  437 LVR 439
Cdd:smart00490  78 AGR 80
 
Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
101-452 2.30e-41

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 155.95  E-value: 2.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 101 KYKLRPEQEKAVKAVINNKIGNTPFhiGVLDYTVNAGKTLIMSSLYLTYKKQLKTLLITNDSDWLNQAREEFKQYLPgeD 180
Cdd:COG1061    78 SFELRPYQQEALEALLAALERGGGR--GLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRRELLEQWAEELRRFLG--D 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 181 ITFVQGKVLNWSNFTIGMVQSISRNMRsYQKELSQIDMVLIDEADQGGSKQYQNVItRLFNTRIRIGLSGTIYMSklakD 260
Cdd:COG1061   154 PLAGGGKKDSDAPITVATYQSLARRAH-LDELGDRFGLVIIDEAHHAGAPSYRRIL-EAFPAAYRLGLTATPFRS----D 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 261 rvKNMNLECFFGKVIAEFKLKDSIKKGYSTKTVVKMVPGKpwYGNWESDCISYKEIYDDSITNCYTAWLMAYNRLLWNLN 340
Cdd:COG1061   228 --GREILLFLFDGIVYEYSLKEAIEDGYLAPPEYYGIRVD--LTDERAEYDALSERLREALAADAERKDKILRELLREHP 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 341 QGRyPALVVCKHIAHCENLYKFFKKKlgdAYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRYLLN 420
Cdd:COG1061   304 DDR-KTLVFCSSVDHAEALAELLNEA---GIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIL 379

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2289947589 421 AASMDSQEKSIQFLGRLVRTDKSKKKVYLDDL 452
Cdd:COG1061   380 LRPTGSPREFIQRLGRGLRPAPGKEDALVYDF 411
uvsW PHA02558
UvsW helicase; Provisional
 24-470 6.01e-23

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 101.62  E-value: 6.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589  24 LYNEFAIRHPNAFYLRTRQRGmqNWDGKIHYITKTGQFKIGLLPKVYDMCIEMGIKPKV---VDMRQPLPK------VSK 94
Cdd:PHA02558   26 LRDYFSFEVPGYKFNPKFKYG--GWDGKIRLLDYNGLLPYGLVGQLKKFAKNRGYSIWVdprIEENEDISRedfdewVSS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589  95 VVTNIGKYKLRPE--QEKAVKAVINN--KIGNTPfhigvldytVNAGKTLIMSSL--YLTYKKQLKTLLITNDSDWLNQA 168
Cdd:PHA02558  104 LEIYSGNKKIEPHwyQYDAVYEGLKNnrRLLNLP---------TSAGKSLIQYLLsrYYLENYEGKVLIIVPTTSLVTQM 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 169 REEFKQY--LPGEDITFVQGKVLNWSN--FTIGMVQSISRNMRSYqkeLSQIDMVLIDEADQGGSKQYQNVITRLFNTRI 244
Cdd:PHA02558  175 IDDFVDYrlFPREAMHKIYSGTAKDTDapIVVSTWQSAVKQPKEW---FDQFGMVIVDECHLFTGKSLTSIITKLDNCKF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 245 RIGLSGTiymskLAKDRVKNMNLECFFGKVIAEFKLKDSIKKGYSTKTVVKMVpgkpWYGNWESDCISYK-EIYDDSITn 323
Cdd:PHA02558  252 KFGLTGS-----LRDGKANILQYVGLFGDIFKPVTTSQLMEEGQVTDLKINSI----FLRYPDEDRVKLKgEDYQEEIK- 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 324 cYTAWLMAYNRLLWN----LNQGRYPALVVCKHIAHCENLYKFFkKKLGDayNIAYVHVNTKSKLRQQIMKDFRDGK-ID 398
Cdd:PHA02558  322 -YITSHTKRNKWIANlalkLAKKGENTFVMFKYVEHGKPLYEML-KKVYD--KVYYVSGEVDTEDRNEMKKIAEGGKgII 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2289947589 399 ILVSTTIIARGKNFPKLRYLLNAASMDSQEKSIQFLGRLVRTDKSKKKVYL----DDLHYPGPYLDRHGKHRKQYY 470
Cdd:PHA02558  398 IVASYGVFSTGISIKNLHHVIFAHPSKSKIIVLQSIGRVLRKHGSKSIATVwdiiDDLSVKPKSANAKKKYVHLNY 473
ResIII pfam04851
Type III restriction enzyme, res subunit;
101-251 3.35e-18

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 81.56  E-value: 3.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 101 KYKLRPEQEKAVKAVINnKIGNTPFHiGVLDYTVNAGKTLIMSSLYLTYKKQL---KTLLITNDSDWLNQAREEFKQYLP 177
Cdd:pfam04851   1 KLELRPYQIEAIENLLE-SIKNGQKR-GLIVMATGSGKTLTAAKLIARLFKKGpikKVLFLVPRKDLLEQALEEFKKFLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 178 GED--ITFVQGK----VLNWSNFTIGMVQSISRNMRSYQKELS--QIDMVLIDEADQGGSKQYQNVItRLFNTRIRIGLS 249
Cdd:pfam04851  79 NYVeiGEIISGDkkdeSVDDNKIVVTTIQSLYKALELASLELLpdFFDVIIIDEAHRSGASSYRNIL-EYFKPAFLLGLT 157


                  ..
gi 2289947589 250 GT 251
Cdd:pfam04851 158 AT 159
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 104-251 2.50e-15

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 73.11  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 104 LRPEQEKAVKAVINNKIGNTpfhiGVLDYTVNAGKTLIMSSLYLtYKKQLKTLLITNDSDWLNQAREEFKQYLPGEDITF 183
Cdd:cd17926     1 LRPYQEEALEAWLAHKNNRR----GILVLPTGSGKTLTALALIA-YLKELRTLIVVPTDALLDQWKERFEDFLGDSSIGL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2289947589 184 VQG---KVLNWSNFTIGMVQSISRNMRSYQKELSQIDMVLIDEADQGGSKQYQNVITRlFNTRIRIGLSGT 251
Cdd:cd17926    76 IGGgkkKDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSEILKE-LNAKYRLGLTAT 145
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 346-439 6.50e-14

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 67.62  E-value: 6.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 346 ALVVCKHIAHCEnlYKFFKKKLGdaYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRYLLNAASMD 425
Cdd:pfam00271  18 VLIFSQTKKTLE--AELLLEKEG--IKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPW 93

                          90
                  ....*....|....
gi 2289947589 426 SQEKSIQFLGRLVR 439
Cdd:pfam00271  94 NPASYIQRIGRAGR 107
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
 73-415 7.31e-14

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 73.37  E-value: 7.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589  73 CIEMG-IKP--KVVDMRQPLPKVSKVVTNIGKYKLRPEQEKAVKAVINNKIGNTPFhigvLDYTV-NAGKTLIM-SSLYL 147
Cdd:COG4098    77 CIQMGrVSSctPLYYWPGPNKKEPKSNPLTWEGTLTPAQQKASDELLEAIKKKEEH----LVWAVcGAGKTEMLfPAIAE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 148 TYKKQLKTLLITNDSDWLNQAREEFKQYLPGEDITFVQGKVLN---WSNFTIGMVQSIsrnMRSYQKelsqIDMVLIDEA 224
Cdd:COG4098   153 ALKQGGRVCIATPRVDVVLELAPRLQQAFPGVDIAALYGGSEEkyrYAQLVIATTHQL---LRFYQA----FDLLIIDEV 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 225 DQ---GGSKQYQNVITRLFNTRiriglSGTIYMSklAKDRVKnmnlecffgkviaefkLKDSIKKGystKTVVKMVP--- 298
Cdd:COG4098   226 DAfpySGDPMLQYAVKRARKPD-----GKLIYLT--ATPSKA----------------LQRQVKRG---KLKVVKLPary 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 299 -GKP-------WYGNWEsdcisyKEIYDDSITNCYTAWLMAYnrllwnLNQGRyPALVVCKHIAHCENLYKFFKKKLGDa 370
Cdd:COG4098   280 hGHPlpvpkfkWLGNWK------KRLRRGKLPRKLLKWLKKR------LKEGR-QLLIFVPTIELLEQLVALLQKLFPE- 345

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2289947589 371 YNIAYVHvnTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPKL 415
Cdd:COG4098   346 ERIAGVH--AEDPERKEKVQAFRDGEIPILVTTTILERGVTFPNV 388
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
 104-251 1.41e-12

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 65.66  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 104 LRPEQEKAVKAVIN------NKIGntpfhigvldyTVNA---GKTLIMSSLYLTYKKQL---KTLLITNDSDWLNQAREE 171
Cdd:cd18032     1 PRYYQQEAIEALEEarekgqRRAL-----------LVMAtgtGKTYTAAFLIKRLLEANrkkRILFLAHREELLEQAERS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 172 FKQYLPGEDITFVQG--KVLNWSNFTIGMVQSISRNMRSYQKELSQIDMVLIDEADQGGSKQYQNVITRlFNTRIRIGLS 249
Cdd:cd18032    70 FKEVLPDGSFGNLKGgkKKPDDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHHAIASSYRKILEY-FEPAFLLGLT 148


                  ..
gi 2289947589 250 GT 251
Cdd:cd18032   149 AT 150
HELICc smart00490
helicase superfamily c-terminal domain;
357-439 1.85e-12

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 62.61  E-value: 1.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589  357 ENLYKFFKKKlgdAYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRYLLNAASMDSQEKSIQFLGR 436
Cdd:smart00490   1 EELAELLKEL---GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77


                   ...
gi 2289947589  437 LVR 439
Cdd:smart00490  78 AGR 80
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 331-424 1.15e-10

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 60.05  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 331 AYNRLLWNLNQGRyPALVVCKHIAHCE--------NLYKFFKKKLGDAYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVS 402
Cdd:cd18811    15 VYEFVREEIAKGR-QAYVIYPLIEESEkldlkaavAMYEYLKERFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVS 93

                          90       100
                  ....*....|....*....|..
gi 2289947589 403 TTIIARGKNFPklryllNAASM 424
Cdd:cd18811    94 TTVIEVGVDVP------NATVM 109
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 344-420 3.05e-10

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 57.90  E-value: 3.05e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2289947589 344 YPALVVCKHIAHCENLYKFFKKKlgdAYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRYLLN 420
Cdd:cd18787    28 GKAIIFVNTKKRVDRLAELLEEL---GIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVDHVIN 101
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 357-424 2.28e-08

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 53.42  E-value: 2.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2289947589 357 ENLYKFFKKKLGDaYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPklryllNAASM 424
Cdd:cd18792    48 EALAEELKELVPE-ARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVP------NANTM 108
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
357-406 4.07e-08

RecG-like helicase [Replication, recombination and repair];


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 55.83  E-value: 4.07e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2289947589 357 ENLYKFFKKKLGDaYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTII 406
Cdd:COG1200   491 EETYEELREAFPG-LRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVI 539
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
 357-406 1.63e-07

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 54.00  E-value: 1.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2289947589 357 ENLYKFFKKKLGDaYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTII 406
Cdd:PRK10917  493 EETYEELQEAFPE-LRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVI 541
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
 379-449 3.99e-07

C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350191 [Multi-domain]  Cd Length: 238  Bit Score: 51.09  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 379 NTKSK-LRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRY--------LLNAASMDSQEKSIQFL----GRLVRTDKsKK 445
Cdd:cd18804   126 TTRKKgALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLvgilnadsGLNSPDFRASERAFQLLtqvsGRAGRGDK-PG 204


                  ....
gi 2289947589 446 KVYL 449
Cdd:cd18804   205 KVII 208
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
334-409 1.39e-06

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 50.53  E-value: 1.39e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2289947589 334 RLLWNL--NQGRYPALVVCKHIAHCENLYKFFKKKLgdaYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARG 409
Cdd:COG0513   230 ELLRRLlrDEDPERAIVFCNTKRGADRLAEKLQKRG---ISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARG 304
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 346-452 2.98e-06

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 46.01  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 346 ALVVCKHIAHCENLYKFFKKKLGDAYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRYLLNAASMD 425
Cdd:cd18799     9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEALILLFFGELKPPILVTVDLLTTGVDIPEVDNVVFLRPTE 88

                          90       100
                  ....*....|....*....|....*..
gi 2289947589 426 SQEKSIQFLGRLVRTDKSKKKVYLDDL 452
Cdd:cd18799    89 SRTLFLQMLGRGLRLHEGKDFFTILDF 115
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
 103-251 5.50e-05

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 43.83  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 103 KLRPEQEKAVKAVINNKIGNTpfhiGVLDYTVNAGKTLIMSSLYLTYKKQlkTLLITNDSDWLNQAREEFKQY--LPGED 180
Cdd:cd18029     8 QLRPYQEKALSKMFGNGRARS----GVIVLPCGAGKTLVGITAACTIKKS--TLVLCTSAVSVEQWRRQFLDWttIDDEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 181 IT-FVQGKvlnWSNF--------TIGMVQSISRNMRSYQKELSQID-----MVLIDEADQGGSKQYQNVITrLFNTRIRI 246
Cdd:cd18029    82 IGrFTSDK---KEIFpeagvtvsTYSMLANTRKRSPESEKFMEFITerewgLIILDEVHVVPAPMFRRVLT-LQKAHCKL 157


                  ....*
gi 2289947589 247 GLSGT 251
Cdd:cd18029   158 GLTAT 162
PRK05580 PRK05580
primosome assembly protein PriA; Validated
 377-415 1.83e-04

primosome assembly protein PriA; Validated


Pssm-ID: 235514 [Multi-domain]  Cd Length: 679  Bit Score: 43.99  E-value: 1.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2289947589 377 HVNTKSKLRQQImKDFRDGKIDILVSTTIIARGKNFPKL 415
Cdd:PRK05580  462 TTRRKGALEQLL-AQFARGEADILIGTQMLAKGHDFPNV 499
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 383-443 3.81e-04

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 42.65  E-value: 3.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2289947589 383 KLRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRYLLNAASMDSQEKSIQFLGRLVRTDKS 443
Cdd:PRK04837  292 KKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGAS 352
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 369-441 6.21e-04

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 42.10  E-value: 6.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2289947589 369 DAYNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRYLLNAASMDSQEKSIQFLGRLVRTD 441
Cdd:PRK10590  268 DGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAA 340
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 371-439 1.28e-03

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 41.37  E-value: 1.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 371 YNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRYLLN-AASMDSqEKSIQFLGRLVR 439
Cdd:PRK11634  270 YNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNyDIPMDS-ESYVHRIGRTGR 338
PriA COG1198
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ...
 386-415 1.35e-03

Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440811 [Multi-domain]  Cd Length: 728  Bit Score: 41.26  E-value: 1.35e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2289947589 386 QQIMKDFRDGKIDILVSTTIIARGKNFPKL 415
Cdd:COG1198   521 EKLLEAFARGEADILVGTQMLAKGHDFPNV 550
PTZ00424 PTZ00424
helicase 45; Provisional
 344-436 1.87e-03

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 40.58  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289947589 344 YPALVVCKHIAHCENLYK--FFKKKLGDA-YNIAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFPKLRYLLN 420
Cdd:PTZ00424  262 YETLTITQAIIYCNTRRKvdYLTKKMHERdFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVIN 341

                          90
                  ....*....|....*.
gi 2289947589 421 AASMDSQEKSIQFLGR 436
Cdd:PTZ00424  342 YDLPASPENYIHRIGR 357
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
 373-413 7.14e-03

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 37.32  E-value: 7.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2289947589 373 IAYVHVNTKSKLRQQIMKDFRDGKIDILVSTTIIARGKNFP 413
Cdd:cd18810    54 IAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIP 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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