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Conserved domains on  [gi|1391839237|gb|AWM96670|]
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polyprotein, partial [Goose calicivirus]

Protein Classification

RNA helicase domain-containing protein( domain architecture ID 10468696)

RNA helicase domain-containing protein may be involved in duplex unwinding during viral RNA replication

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 397-492 6.92e-28

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


:

Pssm-ID: 459992  Cd Length: 102  Bit Score: 108.08  E-value: 6.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237 397 WIFaGPPGIGKTHLVHLIAKSLSK----NNPSVFT--CQVDHHDGYTGEQVCIWDEFDTDPKAEFVEKTIQMVNNTPMLL 470
Cdd:pfam00910   2 WLY-GPPGCGKSTLAKYLARALLKklglPKDSVYSrnPDDDFWDGYTGQPVVIIDDFGQNPDGPDEAELIRLVSSTPYPP 80

                          90       100
                  ....*....|....*....|..
gi 1391839237 471 NCDLAENKGKMFTSSVILATTN 492
Cdd:pfam00910  81 PMAALEEKGTPFTSKFVIVTSN 102
COG3899 super family cl28481
Predicted ATPase [General function prediction only];
178-431 1.28e-03

Predicted ATPase [General function prediction only];


The actual alignment was detected with superfamily member COG3899:

Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 42.54  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237  178 PAALVAILSTYSGTQASFLAVLVAVLQLYDMFDPELVSSIVTHLGDTLWTLVQKGFAFLTGNPLGPILQAPGDHISLLAA 257
Cdd:COG3899     90 RLALLLALALALLAALLLLLALALLLLALLALALLALLLALLLAAGVLGLLLGGLLLAALAALLALAALAAAAAAAAAAA 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237  258 LAAGTIIYLFGNLPAPLSKNVRNLLTGATTVMGILKA-FQLIYRLLTDWWTRKCVVSLLEQATAVTTSLINPAVFSQASQ 336
Cdd:COG3899    170 AARAARLRRARAARLAALALRALLLLVLLLLLLLLLLgLLLAAAAALAAAAAAAAAAAPAAPVVLVAALLLALAALLALL 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237  337 LRKLKVHVDKLHEQVLTKLADPQFSSHATSLRALQTS---------LQTLEQRISVLLAGShertpPQMWIFAGPPGIGK 407
Cdd:COG3899    250 LLAARLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPqplvgreaeLAALLAALERARAGR-----GELVLVSGEAGIGK 324

                          250       260
                   ....*....|....*....|....
gi 1391839237  408 THLVHLIAKSLSKNNPSVFTCQVD 431
Cdd:COG3899    325 SRLVRELARRARARGGRVLRGKCD 348
 
Name Accession Description Interval E-value
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 397-492 6.92e-28

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 108.08  E-value: 6.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237 397 WIFaGPPGIGKTHLVHLIAKSLSK----NNPSVFT--CQVDHHDGYTGEQVCIWDEFDTDPKAEFVEKTIQMVNNTPMLL 470
Cdd:pfam00910   2 WLY-GPPGCGKSTLAKYLARALLKklglPKDSVYSrnPDDDFWDGYTGQPVVIIDDFGQNPDGPDEAELIRLVSSTPYPP 80

                          90       100
                  ....*....|....*....|..
gi 1391839237 471 NCDLAENKGKMFTSSVILATTN 492
Cdd:pfam00910  81 PMAALEEKGTPFTSKFVIVTSN 102
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 398-513 1.97e-07

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: 51.38  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237 398 IFAGPPGIGKTHLVHLIAKSLSKNNPSVFTcqVDHHDGYTGEQVCIWDEFDtdpkaEFVEKTIQMVNNTPMLLNCD---- 473
Cdd:cd00009    23 LLYGPPGTGKTTLARAIANELFRPGAPFLY--LNASDLLEGLVVAELFGHF-----LVRLLFELAEKAKPGVLFIDeids 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1391839237 474 --------------LAENKGKMFTSSVILATTNQDTPVLPNYPRAHAFYRRVNI 513
Cdd:cd00009    96 lsrgaqnallrvleTLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVI 149
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 393-513 5.77e-06

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: 46.98  E-value: 5.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237  393 PPQMWIFAGPPGIGKTHLVHLIAKSLSKNNPSVFTCQVDHHDGYTGEQ---VCIWDEFDTDPKAEFVEKTIQMVNNT-PM 468
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLALALARKLkPD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391839237  469 LLNCD--------------------LAENKGKMFTSSVILATTNQDTPVLPNYPRaHAFYRRVNI 513
Cdd:smart00382  81 VLILDeitslldaeqeallllleelRLLLLLKSEKNLTVILTTNDEKDLGPALLR-RRFDRRIVL 144
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 391-440 3.26e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 44.38  E-value: 3.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1391839237 391 RTPPQMwIFAGPPGIGKTHLVHLIAKSLSKNNPS-VFTCQVdhHDGYTGEQ 440
Cdd:COG1401   219 KTKKNV-ILAGPPGTGKTYLARRLAEALGGEDNGrIEFVQF--HPSWSYED 266
COG3899 COG3899
Predicted ATPase [General function prediction only];
178-431 1.28e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 42.54  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237  178 PAALVAILSTYSGTQASFLAVLVAVLQLYDMFDPELVSSIVTHLGDTLWTLVQKGFAFLTGNPLGPILQAPGDHISLLAA 257
Cdd:COG3899     90 RLALLLALALALLAALLLLLALALLLLALLALALLALLLALLLAAGVLGLLLGGLLLAALAALLALAALAAAAAAAAAAA 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237  258 LAAGTIIYLFGNLPAPLSKNVRNLLTGATTVMGILKA-FQLIYRLLTDWWTRKCVVSLLEQATAVTTSLINPAVFSQASQ 336
Cdd:COG3899    170 AARAARLRRARAARLAALALRALLLLVLLLLLLLLLLgLLLAAAAALAAAAAAAAAAAPAAPVVLVAALLLALAALLALL 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237  337 LRKLKVHVDKLHEQVLTKLADPQFSSHATSLRALQTS---------LQTLEQRISVLLAGShertpPQMWIFAGPPGIGK 407
Cdd:COG3899    250 LLAARLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPqplvgreaeLAALLAALERARAGR-----GELVLVSGEAGIGK 324

                          250       260
                   ....*....|....*....|....
gi 1391839237  408 THLVHLIAKSLSKNNPSVFTCQVD 431
Cdd:COG3899    325 SRLVRELARRARARGGRVLRGKCD 348
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 375-421 7.81e-03

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 39.21  E-value: 7.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1391839237 375 QTLEQRISVLLAGSHER-TPPQMWIFAGPPGIGKTHLVHLIAKSLSKN 421
Cdd:TIGR00635  10 EKVKEQLQLFIEAAKMRqEALDHLLLYGPPGLGKTTLAHIIANEMGVN 57
 
Name Accession Description Interval E-value
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 397-492 6.92e-28

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 108.08  E-value: 6.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237 397 WIFaGPPGIGKTHLVHLIAKSLSK----NNPSVFT--CQVDHHDGYTGEQVCIWDEFDTDPKAEFVEKTIQMVNNTPMLL 470
Cdd:pfam00910   2 WLY-GPPGCGKSTLAKYLARALLKklglPKDSVYSrnPDDDFWDGYTGQPVVIIDDFGQNPDGPDEAELIRLVSSTPYPP 80

                          90       100
                  ....*....|....*....|..
gi 1391839237 471 NCDLAENKGKMFTSSVILATTN 492
Cdd:pfam00910  81 PMAALEEKGTPFTSKFVIVTSN 102
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 398-513 1.97e-07

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: 51.38  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237 398 IFAGPPGIGKTHLVHLIAKSLSKNNPSVFTcqVDHHDGYTGEQVCIWDEFDtdpkaEFVEKTIQMVNNTPMLLNCD---- 473
Cdd:cd00009    23 LLYGPPGTGKTTLARAIANELFRPGAPFLY--LNASDLLEGLVVAELFGHF-----LVRLLFELAEKAKPGVLFIDeids 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1391839237 474 --------------LAENKGKMFTSSVILATTNQDTPVLPNYPRAHAFYRRVNI 513
Cdd:cd00009    96 lsrgaqnallrvleTLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVI 149
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 393-513 5.77e-06

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: 46.98  E-value: 5.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237  393 PPQMWIFAGPPGIGKTHLVHLIAKSLSKNNPSVFTCQVDHHDGYTGEQ---VCIWDEFDTDPKAEFVEKTIQMVNNT-PM 468
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLALALARKLkPD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391839237  469 LLNCD--------------------LAENKGKMFTSSVILATTNQDTPVLPNYPRaHAFYRRVNI 513
Cdd:smart00382  81 VLILDeitslldaeqeallllleelRLLLLLKSEKNLTVILTTNDEKDLGPALLR-RRFDRRIVL 144
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 377-513 2.18e-04

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 42.66  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237 377 LEQRISVLLAGS----HERTPPQMWIFAGPPGIGKTHLVHLIAKSLSK-----NNPSVFTcqvdHHDGYTGEQV------ 441
Cdd:cd19481     5 LREAVEAPRRGSrlrrYGLGLPKGILLYGPPGTGKTLLAKALAGELGLplivvKLSSLLS----KYVGESEKNLrkifer 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237 442 ------CI--WDEFDT-----DPKAEfVEKTIQMVNNtpMLLNCDLAENKGKmftsSVILATTNQDTPVLPNYPRAHAFY 508
Cdd:cd19481    81 arrlapCIlfIDEIDAigrkrDSSGE-SGELRRVLNQ--LLTELDGVNSRSK----VLVIAATNRPDLLDPALLRPGRFD 153


                  ....*
gi 1391839237 509 RRVNI 513
Cdd:cd19481   154 EVIEF 158
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 391-440 3.26e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 44.38  E-value: 3.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1391839237 391 RTPPQMwIFAGPPGIGKTHLVHLIAKSLSKNNPS-VFTCQVdhHDGYTGEQ 440
Cdd:COG1401   219 KTKKNV-ILAGPPGTGKTYLARRLAEALGGEDNGrIEFVQF--HPSWSYED 266
COG3899 COG3899
Predicted ATPase [General function prediction only];
178-431 1.28e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 42.54  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237  178 PAALVAILSTYSGTQASFLAVLVAVLQLYDMFDPELVSSIVTHLGDTLWTLVQKGFAFLTGNPLGPILQAPGDHISLLAA 257
Cdd:COG3899     90 RLALLLALALALLAALLLLLALALLLLALLALALLALLLALLLAAGVLGLLLGGLLLAALAALLALAALAAAAAAAAAAA 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237  258 LAAGTIIYLFGNLPAPLSKNVRNLLTGATTVMGILKA-FQLIYRLLTDWWTRKCVVSLLEQATAVTTSLINPAVFSQASQ 336
Cdd:COG3899    170 AARAARLRRARAARLAALALRALLLLVLLLLLLLLLLgLLLAAAAALAAAAAAAAAAAPAAPVVLVAALLLALAALLALL 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237  337 LRKLKVHVDKLHEQVLTKLADPQFSSHATSLRALQTS---------LQTLEQRISVLLAGShertpPQMWIFAGPPGIGK 407
Cdd:COG3899    250 LLAARLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPqplvgreaeLAALLAALERARAGR-----GELVLVSGEAGIGK 324

                          250       260
                   ....*....|....*....|....
gi 1391839237  408 THLVHLIAKSLSKNNPSVFTCQVD 431
Cdd:COG3899    325 SRLVRELARRARARGGRVLRGKCD 348
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 392-513 2.76e-03

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 39.58  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237 392 TPPQMWIFAGPPGIGKTHLVHLIAKS-----LSKNNPSVftcqvdhHDGYTGE---------------QVCI--WDEFDT 449
Cdd:cd19503    32 KPPRGVLLHGPPGTGKTLLARAVANEaganfLSISGPSI-------VSKYLGEseknlreifeearshAPSIifIDEIDA 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391839237 450 -----DPKAEFVEKTIqmvnnTPMLLNC-DLAENKGKMftssVILATTNQDTPVLPNYPRAHAFYRRVNI 513
Cdd:cd19503   105 lapkrEEDQREVERRV-----VAQLLTLmDGMSSRGKV----VVIAATNRPDAIDPALRRPGRFDREVEI 165
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 379-436 3.81e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 39.02  E-value: 3.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1391839237 379 QRISVLLAGSHERTPPQMWIfAGPPGIGKTHLVHLIAKSLSKNNPSVFTCQVDHHDGY 436
Cdd:pfam13191  10 EQLLDALDRVRSGRPPSVLL-TGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPY 66
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
397-418 7.25e-03

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 39.57  E-value: 7.25e-03
                          10        20
                  ....*....|....*....|..
gi 1391839237 397 WIFAGPPGIGKTHLVHLIAKSL 418
Cdd:COG0470    21 LLLHGPPGIGKTTLALALARDL 42
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 375-421 7.81e-03

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 39.21  E-value: 7.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1391839237 375 QTLEQRISVLLAGSHER-TPPQMWIFAGPPGIGKTHLVHLIAKSLSKN 421
Cdd:TIGR00635  10 EKVKEQLQLFIEAAKMRqEALDHLLLYGPPGLGKTTLAHIIANEMGVN 57
 
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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