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Conserved domains on  [gi|34925080|sp|P83571|]
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RecName: Full=RuvB-like 2; AltName: Full=Reptin; AltName: Full=zReptin

Protein Classification

RuvB-like helicase( domain architecture ID 15918217)

RuvB-like helicase is a DNA helicase that plays an essential role in various complexes involved in fundamental processes such as transcription regulation, DNA damage response and apoptosis (via the chromatin remodelling complexes SWR1, INO80 and TIP60), maturation of small nuclear ribonucleoproteins, cellular development, cancer metastasis, and regulation of mitosis

EC:  3.6.4.12
Gene Ontology:  GO:0005524|GO:0003678|GO:0006259
PubMed:  10787406

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 21-365 0e+00

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


:

Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 613.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080    21 RIGAHSHIRGLGLDDALEPRQVSQGMVGQLASRRAAGLILEMIKDGQIAGRAVLIAGQPGTGKTAIAMGIAQSLGPDTPF 100
Cdd:pfam06068   1 RISAHSHIRGLGLDEDGEARYVSGGLVGQEKAREAAGVIVEMIKEGKIAGRAVLIAGPPGTGKTALAIAISKELGEDTPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080   101 TALAGSEIFSLEMSKTEALSQAFRKAIGVRIKEETEIIEGEVVEIQI---DRPATG-TGAKVGKLTLKTTEMETIYDLGT 176
Cdd:pfam06068  81 TSISGSEVYSLEMKKTEALTQAFRKAIGVRIKEEKEVYEGEVVELEIeeaENPLSGgKTIKGGKITLKTTKMEKTLKLGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080   177 KMIESLSKERVQAGDVITIDKATGKISKLGRSFTRARDYDAmgAQTQFVQCPEGELQKRKEVVHTVSLHEIDVINSRTQG 256
Cdd:pfam06068 161 KIYEQLQKEKVSAGDVIYIDKNTGRVKKLGRSFARATDFDL--EATEFVPCPKGEVHKRKEVVQTVTLHDIDVANARPQG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080   257 FLALFSGDTGEIKSEVREQINAKVSEWREEGKAEIIPGVLFIDEVHMLDIECFSFLNRALESDLSPVLIMATNRGITRIR 336
Cdd:pfam06068 239 ILSLFSPKKGEITSELREEINKKVNKWIEEGKAEIVPGVLFIDEVHMLDIECFSFLNRALESDLAPIVILATNRGICTIR 318

                         330       340
                  ....*....|....*....|....*....
gi 34925080   337 GTNYQSPHGIPIDMLDRLLIIATTPYTEK 365
Cdd:pfam06068 319 GTDIISPHGIPLDLLDRLLIITTEPYTRE 347
TIP49_C pfam17856
TIP49 AAA-lid domain; This family consists of the C-terminal region of several eukaryotic and ...
 370-435 5.79e-18

TIP49 AAA-lid domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


:

Pssm-ID: 436097 [Multi-domain]  Cd Length: 66  Bit Score: 77.69  E-value: 5.79e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34925080   370 ILKIRCEEEDVELSEEAHTVLTRIGQETSLRYAIQLISTAGLVCRKRRGTEVQVEDIKRVYSLFLD 435
Cdd:pfam17856   1 ILKIRAQEEGVKIDEEALDLLAKIGTETSLRYAIQLLTPASILAKKRGGKEVEVQDVEEAYELFLD 66
 
Name Accession Description Interval E-value
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 21-365 0e+00

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 613.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080    21 RIGAHSHIRGLGLDDALEPRQVSQGMVGQLASRRAAGLILEMIKDGQIAGRAVLIAGQPGTGKTAIAMGIAQSLGPDTPF 100
Cdd:pfam06068   1 RISAHSHIRGLGLDEDGEARYVSGGLVGQEKAREAAGVIVEMIKEGKIAGRAVLIAGPPGTGKTALAIAISKELGEDTPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080   101 TALAGSEIFSLEMSKTEALSQAFRKAIGVRIKEETEIIEGEVVEIQI---DRPATG-TGAKVGKLTLKTTEMETIYDLGT 176
Cdd:pfam06068  81 TSISGSEVYSLEMKKTEALTQAFRKAIGVRIKEEKEVYEGEVVELEIeeaENPLSGgKTIKGGKITLKTTKMEKTLKLGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080   177 KMIESLSKERVQAGDVITIDKATGKISKLGRSFTRARDYDAmgAQTQFVQCPEGELQKRKEVVHTVSLHEIDVINSRTQG 256
Cdd:pfam06068 161 KIYEQLQKEKVSAGDVIYIDKNTGRVKKLGRSFARATDFDL--EATEFVPCPKGEVHKRKEVVQTVTLHDIDVANARPQG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080   257 FLALFSGDTGEIKSEVREQINAKVSEWREEGKAEIIPGVLFIDEVHMLDIECFSFLNRALESDLSPVLIMATNRGITRIR 336
Cdd:pfam06068 239 ILSLFSPKKGEITSELREEINKKVNKWIEEGKAEIVPGVLFIDEVHMLDIECFSFLNRALESDLAPIVILATNRGICTIR 318

                         330       340
                  ....*....|....*....|....*....
gi 34925080   337 GTNYQSPHGIPIDMLDRLLIIATTPYTEK 365
Cdd:pfam06068 319 GTDIISPHGIPLDLLDRLLIITTEPYTRE 347
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
12-451 2.86e-178

DNA helicase TIP49, TBP-interacting protein [Transcription];


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 506.43  E-value: 2.86e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080  12 EVRDITRIERIGAHSHIRGLGLDDALEPRQVSQGMVGQLASRRAAGLILEMIKDGQIAGRAVLIAGQPGTGKTAIAMGIA 91
Cdd:COG1224   6 EIEKVKEFERISAHSHIRGLGLDENGKAKFVADGLVGQVEAREAAGIVVKMIKEGKMAGKGILIVGPPGTGKTALAVAIA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080  92 QSLGPDTPFTALAGSEIFSLEMSKTEALSQAFRKAIGVRIKEETEIIEGEVVEIQIDR---PATGTgAKV---GKLTLKT 165
Cdd:COG1224  86 RELGEDTPFVAISGSEIYSAELKKTEFLMQALRKAIGVRVREKRKVYEGVVKEIKIRYarhPYNPY-VKVpreATITLAT 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080 166 TEMETIYDLGTKMIESLSKERVQAGDVITIDKATGKISKLGRS-FTRARDYDAmgAQTQFVQCPEGELQKRKEVVHTVSL 244
Cdd:COG1224 165 KDEEKTLTVGEEIAQQLVELGIRKGDVIWIDAETGRVSKLGRAkGEGAKTYDI--ETKRIVEVPSGPVKKEKEIVRTLTL 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080 245 HEIDVINSRTQG-FLALFS-GDTGEIKSEVREQINAKVSEWREEGKAEIIPGVLFIDEVHMLDIECFSFLNRALESDLSP 322
Cdd:COG1224 243 HDLDLYLAAQRAaFSALFGfFEEREIPSEVRKQVDELVKKWIEEGKAELVPGVLFIDDAHMLDIEAFSFLTRAMESELAP 322

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080 323 VLIMATNRGITRIRGTNYQSPHGIPIDMLDRLLIIATTPYTEKETRQILKIRCEEEDVELSEEAHTVLTRIGQETSLRYA 402
Cdd:COG1224 323 IIILATNRGITKIRGTDIESPHGIPLDLLDRLLIIPTRPYTEDEIREIIKIRAEEEDIELSDDALEELTKIGVERSLRYA 402

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 34925080 403 IQLISTAGLVCRKRRGTEVQVEDIKRVYSLFLDEARSSQYMKEYQDSFL 451
Cdd:COG1224 403 VQLLEPAYIIAKRRGRSKVTVEDVEEASKLFADVKESVEYVKEYEELFL 451
TIP49_C pfam17856
TIP49 AAA-lid domain; This family consists of the C-terminal region of several eukaryotic and ...
 370-435 5.79e-18

TIP49 AAA-lid domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 436097 [Multi-domain]  Cd Length: 66  Bit Score: 77.69  E-value: 5.79e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34925080   370 ILKIRCEEEDVELSEEAHTVLTRIGQETSLRYAIQLISTAGLVCRKRRGTEVQVEDIKRVYSLFLD 435
Cdd:pfam17856   1 ILKIRAQEEGVKIDEEALDLLAKIGTETSLRYAIQLLTPASILAKKRGGKEVEVQDVEEAYELFLD 66
DnaB_C cd00984
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ...
 73-117 1.17e-05

C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase DnaB unwinds the DNA duplex at the chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.


Pssm-ID: 410864 [Multi-domain]  Cd Length: 256  Bit Score: 46.74  E-value: 1.17e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 34925080  73 VLIAGQPGTGKTAIAMGIAQSLGPDTPFTALagseIFSLEMSKTE 117
Cdd:cd00984  22 IIIAARPSMGKTAFALNIAENIALDEGLPVL----FFSLEMSAEQ 62
PRK07773 PRK07773
replicative DNA helicase; Validated
 70-117 8.42e-05

replicative DNA helicase; Validated


Pssm-ID: 236093 [Multi-domain]  Cd Length: 886  Bit Score: 45.13  E-value: 8.42e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 34925080   70 GRAVLIAGQPGTGKTAIAMGIAQSLGpdtpFTALAGSEIFSLEMSKTE 117
Cdd:PRK07773 217 GQLIIVAARPSMGKTTFGLDFARNCA----IRHRLAVAIFSLEMSKEQ 260
DnaB TIGR00665
replicative DNA helicase; This model describes the helicase DnaB, a homohexameric protein ...
 73-117 6.97e-04

replicative DNA helicase; This model describes the helicase DnaB, a homohexameric protein required for DNA replication. The homohexamer can form a ring around a single strand of DNA near a replication fork. An intein of > 400 residues is found at a conserved location in DnaB of Synechocystis PCC6803, Rhodothermus marinus (both experimentally confirmed), and Mycobacterium tuberculosis. The intein removes itself by a self-splicing reaction. The seed alignment contains inteins so that the model built from the seed alignment will model a low cost at common intein insertion sites. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273206 [Multi-domain]  Cd Length: 432  Bit Score: 42.03  E-value: 6.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 34925080    73 VLIAGQPGTGKTAIAMGIAQSLGPDTPFTALagseIFSLEMSKTE 117
Cdd:TIGR00665 197 IILAARPSMGKTAFALNIAENAAIKEGKPVA----FFSLEMSAEQ 237
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 70-139 1.86e-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: 38.89  E-value: 1.86e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34925080     70 GRAVLIAGQPGTGKTAIAMGIAQSLGPDT-PFTALAGSEIFSLEMSKTEALSQAFRKAIGVRIKEETEIIE 139
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA 72
 
Name Accession Description Interval E-value
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 21-365 0e+00

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 613.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080    21 RIGAHSHIRGLGLDDALEPRQVSQGMVGQLASRRAAGLILEMIKDGQIAGRAVLIAGQPGTGKTAIAMGIAQSLGPDTPF 100
Cdd:pfam06068   1 RISAHSHIRGLGLDEDGEARYVSGGLVGQEKAREAAGVIVEMIKEGKIAGRAVLIAGPPGTGKTALAIAISKELGEDTPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080   101 TALAGSEIFSLEMSKTEALSQAFRKAIGVRIKEETEIIEGEVVEIQI---DRPATG-TGAKVGKLTLKTTEMETIYDLGT 176
Cdd:pfam06068  81 TSISGSEVYSLEMKKTEALTQAFRKAIGVRIKEEKEVYEGEVVELEIeeaENPLSGgKTIKGGKITLKTTKMEKTLKLGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080   177 KMIESLSKERVQAGDVITIDKATGKISKLGRSFTRARDYDAmgAQTQFVQCPEGELQKRKEVVHTVSLHEIDVINSRTQG 256
Cdd:pfam06068 161 KIYEQLQKEKVSAGDVIYIDKNTGRVKKLGRSFARATDFDL--EATEFVPCPKGEVHKRKEVVQTVTLHDIDVANARPQG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080   257 FLALFSGDTGEIKSEVREQINAKVSEWREEGKAEIIPGVLFIDEVHMLDIECFSFLNRALESDLSPVLIMATNRGITRIR 336
Cdd:pfam06068 239 ILSLFSPKKGEITSELREEINKKVNKWIEEGKAEIVPGVLFIDEVHMLDIECFSFLNRALESDLAPIVILATNRGICTIR 318

                         330       340
                  ....*....|....*....|....*....
gi 34925080   337 GTNYQSPHGIPIDMLDRLLIIATTPYTEK 365
Cdd:pfam06068 319 GTDIISPHGIPLDLLDRLLIITTEPYTRE 347
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
12-451 2.86e-178

DNA helicase TIP49, TBP-interacting protein [Transcription];


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 506.43  E-value: 2.86e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080  12 EVRDITRIERIGAHSHIRGLGLDDALEPRQVSQGMVGQLASRRAAGLILEMIKDGQIAGRAVLIAGQPGTGKTAIAMGIA 91
Cdd:COG1224   6 EIEKVKEFERISAHSHIRGLGLDENGKAKFVADGLVGQVEAREAAGIVVKMIKEGKMAGKGILIVGPPGTGKTALAVAIA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080  92 QSLGPDTPFTALAGSEIFSLEMSKTEALSQAFRKAIGVRIKEETEIIEGEVVEIQIDR---PATGTgAKV---GKLTLKT 165
Cdd:COG1224  86 RELGEDTPFVAISGSEIYSAELKKTEFLMQALRKAIGVRVREKRKVYEGVVKEIKIRYarhPYNPY-VKVpreATITLAT 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080 166 TEMETIYDLGTKMIESLSKERVQAGDVITIDKATGKISKLGRS-FTRARDYDAmgAQTQFVQCPEGELQKRKEVVHTVSL 244
Cdd:COG1224 165 KDEEKTLTVGEEIAQQLVELGIRKGDVIWIDAETGRVSKLGRAkGEGAKTYDI--ETKRIVEVPSGPVKKEKEIVRTLTL 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080 245 HEIDVINSRTQG-FLALFS-GDTGEIKSEVREQINAKVSEWREEGKAEIIPGVLFIDEVHMLDIECFSFLNRALESDLSP 322
Cdd:COG1224 243 HDLDLYLAAQRAaFSALFGfFEEREIPSEVRKQVDELVKKWIEEGKAELVPGVLFIDDAHMLDIEAFSFLTRAMESELAP 322

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080 323 VLIMATNRGITRIRGTNYQSPHGIPIDMLDRLLIIATTPYTEKETRQILKIRCEEEDVELSEEAHTVLTRIGQETSLRYA 402
Cdd:COG1224 323 IIILATNRGITKIRGTDIESPHGIPLDLLDRLLIIPTRPYTEDEIREIIKIRAEEEDIELSDDALEELTKIGVERSLRYA 402

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 34925080 403 IQLISTAGLVCRKRRGTEVQVEDIKRVYSLFLDEARSSQYMKEYQDSFL 451
Cdd:COG1224 403 VQLLEPAYIIAKRRGRSKVTVEDVEEASKLFADVKESVEYVKEYEELFL 451
TIP49_C pfam17856
TIP49 AAA-lid domain; This family consists of the C-terminal region of several eukaryotic and ...
 370-435 5.79e-18

TIP49 AAA-lid domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 436097 [Multi-domain]  Cd Length: 66  Bit Score: 77.69  E-value: 5.79e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34925080   370 ILKIRCEEEDVELSEEAHTVLTRIGQETSLRYAIQLISTAGLVCRKRRGTEVQVEDIKRVYSLFLD 435
Cdd:pfam17856   1 ILKIRAQEEGVKIDEEALDLLAKIGTETSLRYAIQLLTPASILAKKRGGKEVEVQDVEEAYELFLD 66
DnaB_C pfam03796
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ...
 73-117 4.23e-06

DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.


Pssm-ID: 427509 [Multi-domain]  Cd Length: 254  Bit Score: 48.18  E-value: 4.23e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 34925080    73 VLIAGQPGTGKTAIAMGIAQSLGPDTPFTALagseIFSLEMSKTE 117
Cdd:pfam03796  22 IIIAARPSMGKTAFALNIARNAAVKHKKPVA----IFSLEMSAEQ 62
DnaB_C cd00984
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ...
 73-117 1.17e-05

C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase DnaB unwinds the DNA duplex at the chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.


Pssm-ID: 410864 [Multi-domain]  Cd Length: 256  Bit Score: 46.74  E-value: 1.17e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 34925080  73 VLIAGQPGTGKTAIAMGIAQSLGPDTPFTALagseIFSLEMSKTE 117
Cdd:cd00984  22 IIIAARPSMGKTAFALNIAENIALDEGLPVL----FFSLEMSAEQ 62
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 64-126 4.29e-05

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: 43.81  E-value: 4.29e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34925080  64 KDGQIAGRAVLIAGQPGTGKTAIAMGIAQSLGPdtPFTALAGSEIFSLEMSKTEA-LSQAFRKA 126
Cdd:cd19481  20 RYGLGLPKGILLYGPPGTGKTLLAKALAGELGL--PLIVVKLSSLLSKYVGESEKnLRKIFERA 81
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 71-126 5.05e-05

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: 43.43  E-value: 5.05e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 34925080  71 RAVLIAGQPGTGKTAIAMGIAQSLGpdTPFTALAGSEIFSLEMSKTE-ALSQAFRKA 126
Cdd:cd19503  35 RGVLLHGPPGTGKTLLARAVANEAG--ANFLSISGPSIVSKYLGESEkNLREIFEEA 89
PRK07773 PRK07773
replicative DNA helicase; Validated
 70-117 8.42e-05

replicative DNA helicase; Validated


Pssm-ID: 236093 [Multi-domain]  Cd Length: 886  Bit Score: 45.13  E-value: 8.42e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 34925080   70 GRAVLIAGQPGTGKTAIAMGIAQSLGpdtpFTALAGSEIFSLEMSKTE 117
Cdd:PRK07773 217 GQLIIVAARPSMGKTTFGLDFARNCA----IRHRLAVAIFSLEMSKEQ 260
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 73-126 1.09e-04

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 41.81  E-value: 1.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 34925080    73 VLIAGQPGTGKTAIAMGIAQSLGpdTPFTALAGSEIFSLEMSKTEA-LSQAFRKA 126
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELG--APFIEISGSELVSKYVGESEKrLRELFEAA 53
DnaB COG0305
Replicative DNA helicase [Replication, recombination and repair];
73-117 1.48e-04

Replicative DNA helicase [Replication, recombination and repair];


Pssm-ID: 440074 [Multi-domain]  Cd Length: 429  Bit Score: 43.91  E-value: 1.48e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 34925080  73 VLIAGQPGTGKTAIAMGIAQSLGPDTPFTALagseIFSLEMSKTE 117
Cdd:COG0305 194 IILAARPSMGKTAFALNIARNAAIKEGKPVA----IFSLEMSAEQ 234
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 70-126 1.81e-04

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 43.75  E-value: 1.81e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34925080  70 GRAVLIAGQPGTGKTAIAMGIAQSLGPdtPFTALAGSEIFSLEMSKTE-ALSQAFRKA 126
Cdd:COG0464 191 PRGLLLYGPPGTGKTLLARALAGELGL--PLIEVDLSDLVSKYVGETEkNLREVFDKA 246
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 71-126 2.16e-04

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). 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: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 41.50  E-value: 2.16e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 34925080  71 RAVLIAGQPGTGKTAIAMGIAQSLGPDtpFTALAGSEIFSLEMSKTE-ALSQAFRKA 126
Cdd:cd19511  28 KGVLLYGPPGCGKTLLAKALASEAGLN--FISVKGPELFSKYVGESErAVREIFQKA 82
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 71-126 2.88e-04

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. 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: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 41.33  E-value: 2.88e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 34925080  71 RAVLIAGQPGTGKTAIAMGIAQSLGPDtpFTALAGSEIFSLEMSKTE-ALSQAFRKA 126
Cdd:cd19529  28 KGILLYGPPGTGKTLLAKAVATESNAN--FISVKGPELLSKWVGESEkAIREIFRKA 82
DnaB TIGR00665
replicative DNA helicase; This model describes the helicase DnaB, a homohexameric protein ...
 73-117 6.97e-04

replicative DNA helicase; This model describes the helicase DnaB, a homohexameric protein required for DNA replication. The homohexamer can form a ring around a single strand of DNA near a replication fork. An intein of > 400 residues is found at a conserved location in DnaB of Synechocystis PCC6803, Rhodothermus marinus (both experimentally confirmed), and Mycobacterium tuberculosis. The intein removes itself by a self-splicing reaction. The seed alignment contains inteins so that the model built from the seed alignment will model a low cost at common intein insertion sites. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273206 [Multi-domain]  Cd Length: 432  Bit Score: 42.03  E-value: 6.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 34925080    73 VLIAGQPGTGKTAIAMGIAQSLGPDTPFTALagseIFSLEMSKTE 117
Cdd:TIGR00665 197 IILAARPSMGKTAFALNIAENAAIKEGKPVA----FFSLEMSAEQ 237
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 71-126 1.23e-03

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 41.43  E-value: 1.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 34925080    71 RAVLIAGQPGTGKTAIAMGIAQSLGPDtpFTALAGSEIFSLEMSKTE-ALSQAFRKA 126
Cdd:TIGR01243 488 KGVLLFGPPGTGKTLLAKAVATESGAN--FIAVRGPEILSKWVGESEkAIREIFRKA 542
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 70-110 1.28e-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: 39.44  E-value: 1.28e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 34925080  70 GRAVLIAGQPGTGKTAIAMGIAQSLG-PDTPFTALAGSEIFS 110
Cdd:cd00009  19 PKNLLLYGPPGTGKTTLARAIANELFrPGAPFLYLNASDLLE 60
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 70-139 1.86e-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: 38.89  E-value: 1.86e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34925080     70 GRAVLIAGQPGTGKTAIAMGIAQSLGPDT-PFTALAGSEIFSLEMSKTEALSQAFRKAIGVRIKEETEIIE 139
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA 72
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 71-113 4.00e-03

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and 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: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 37.98  E-value: 4.00e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 34925080  71 RAVLIAGQPGTGKTAIAMGIAQSLGpdTPFTALAGSEIfsLEM 113
Cdd:cd19501  38 KGVLLVGPPGTGKTLLAKAVAGEAG--VPFFSISGSDF--VEM 76
PRK05636 PRK05636
replicative DNA helicase; Provisional
 48-131 4.00e-03

replicative DNA helicase; Provisional


Pssm-ID: 180177 [Multi-domain]  Cd Length: 505  Bit Score: 39.44  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080   48 GQLASRRAAGLI-LEMIKDGQIAGRAVLIAGQPGTGKTAIAMGIAQSLGPDTPFTALagseIFSLEMSKTEALSQAFRKA 126
Cdd:PRK05636 242 GGIATGIPTGFKdLDDLTNGLRGGQMIIVAARPGVGKSTLALDFMRSASIKHNKASV----IFSLEMSKSEIVMRLLSAE 317


                 ....*
gi 34925080  127 IGVRI 131
Cdd:PRK05636 318 AEVRL 322
PRK05748 PRK05748
replicative DNA helicase; Provisional
 73-114 4.03e-03

replicative DNA helicase; Provisional


Pssm-ID: 180232 [Multi-domain]  Cd Length: 448  Bit Score: 39.55  E-value: 4.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 34925080   73 VLIAGQPGTGKTAIAMGIAQSLGPDTPFTALagseIFSLEMS 114
Cdd:PRK05748 206 IIVAARPSVGKTAFALNIAQNVATKTDKNVA----IFSLEMG 243
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
46-126 4.51e-03

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 38.71  E-value: 4.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080  46 MVGQLASRRAAGLILE-------MIKDGQIAGRAVLIAGQPGTGKTAIAMGIAQSLGpdTPFTALAGSEIFSLEMSKTEA 118
Cdd:COG1223   4 VVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELK--LPLLTVRLDSLIGSYLGETAR 81


                ....*....
gi 34925080 119 -LSQAFRKA 126
Cdd:COG1223  82 nLRKLFDFA 90
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 71-126 4.91e-03

first of two ATPase domains of CDC48 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. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like 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: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 37.80  E-value: 4.91e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 34925080  71 RAVLIAGQPGTGKTAIAMGIAQSLGPDtpFTALAGSEIFSLEMSKTEA-LSQAFRKA 126
Cdd:cd19519  35 RGILLYGPPGTGKTLIARAVANETGAF--FFLINGPEIMSKLAGESESnLRKAFEEA 89
ftsH CHL00176
cell division protein; Validated
 73-107 7.44e-03

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 38.88  E-value: 7.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 34925080   73 VLIAGQPGTGKTAIAMGIAQSLGpdTPFTALAGSE 107
Cdd:CHL00176 219 VLLVGPPGTGKTLLAKAIAGEAE--VPFFSISGSE 251
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 66-119 7.80e-03

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 38.45  E-value: 7.80e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 34925080  66 GQIAGRAVLIAGQPGTGKTAIAMGIAQSLGpdTPFTALAGSEIFSLEMSKTEAL 119
Cdd:COG1222 108 GIEPPKGVLLYGPPGTGKTLLAKAVAGELG--APFIRVRGSELVSKYIGEGARN 159
PRK14964 PRK14964
DNA polymerase III subunits gamma and tau; Provisional
 295-358 8.60e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237870 [Multi-domain]  Cd Length: 491  Bit Score: 38.61  E-value: 8.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34925080  295 VLFIDEVHMLDIECFSFLNRALESDLSPV-LIMATNR----GITRIRGTNYQSPHGIPIDML-DRLLIIA 358
Cdd:PRK14964 119 VYIIDEVHMLSNSAFNALLKTLEEPAPHVkFILATTEvkkiPVTIISRCQRFDLQKIPTDKLvEHLVDIA 188
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
 295-328 8.96e-03

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 37.27  E-value: 8.96e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 34925080 295 VLFIDEVHMLDIECFSFLNRALESDL----SPVLIM-AT 328
Cdd:cd17930 133 VVVLDEVQAYDPEYMALLLKALLELLgelgGPVVLMtAT 171
 
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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