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Conserved domains on  [gi|1622936123|ref|XP_001090684|]
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ATPase WRNIP1 [Macaca mulatta]

Protein Classification

replication-associated recombination protein A( domain architecture ID 12219000)

replication-associated recombination protein A is a DNA-dependent ATPase that plays important roles in cellular responses to stalled DNA replication processes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
225-661 0e+00

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


:

Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 612.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 225 KPLADTMRPDTLQDYFGQSRAVGQDTLLRSLLETNEIPSLILWGPPGCGKTTLAHIIANNSKKHsirFVTLSATNAKTND 304
Cdd:COG2256    13 APLAERMRPRTLDEVVGQEHLLGPGKPLRRAIEAGRLSSMILWGPPGTGKTTLARLIANATDAE---FVALSAVTSGVKD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 305 VRDVIKQAQNEKSFfKRKTVLFIDEIHRFNKSQQDTFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEKLPVEA 384
Cdd:COG2256    90 IREVIEEARERRAY-GRRTILFVDEIHRFNKAQQDALLPHVEDGTITLIGATTENPSFEVNSALLSRCRVFVLKPLSEED 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 385 MVTILMRAINSLGIHVLDSSRPtdplshssnsssepamfIEDKAVDTLAYLSDGDARAGLNGLQLAVLARLSSrkmfckk 464
Cdd:COG2256   169 LEQLLERALADDERGLGGYKLE-----------------LDDEALEALARLADGDARRALNALELAVLSAPPD------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 465 sgqsyspSRVLITENDVKEGLQRSHILYDRAGEEHYNCISALHKSMRGSDQNASLYWLARMLEGGEDPLYVARRLVRFAS 544
Cdd:COG2256   225 -------GVIEITLELVEEALQRRALRYDKDGDEHYDLISAFIKSIRGSDPDAALYWLARMLEAGEDPRFIARRLVIMAS 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 545 EDIGLADPSALTQAVAAYQGCHFIGMPECEVLLAQCVVYFARAPKSIEVYSAYNNVKACLRnhQGPLPPVPLHLRNAPTR 624
Cdd:COG2256   298 EDIGLADPQALQIAVAAAQAVERLGMPEGRIALAQAVIYLATAPKSNAAYLAINAALADVR--EGGSLPVPLHLRNAPTK 375
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1622936123 625 LMKDLGYGKGYKYnpMYSEP---VDQEYLPEELRGVDFFK 661
Cdd:COG2256   376 LMKELGYGKGYKY--PHDYPggyVGQQYLPDELKGRRYYE 413
ZnF_Rad18 smart00734
Rad18-like CCHC zinc finger; Yeast Rad18p functions with Rad5p in error-free post-replicative ...
17-40 3.77e-09

Rad18-like CCHC zinc finger; Yeast Rad18p functions with Rad5p in error-free post-replicative DNA repair. This zinc finger is likely to bind nucleic-acids.


:

Pssm-ID: 128973 [Multi-domain]  Cd Length: 24  Bit Score: 52.22  E-value: 3.77e-09
                           10        20
                   ....*....|....*....|....
gi 1622936123   17 QVQCPVCQQMMPAAHINSHLDRCL 40
Cdd:smart00734   1 LVQCPVCFREVPENLINSHLDSCL 24
RAD18 super family cl35000
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
18-83 7.48e-04

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5432:

Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 42.38  E-value: 7.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936123  18 VQCPVCQQMMPAAHINSHLDRCLLLH--PAGHAEP---AAGSH-RAGERAKGPSPPGAKRRRLSESSALKQP 83
Cdd:COG5432   161 VHCPACSNLVPHNQINQHLDSCLNSPssPSSSSSPyknKDNSKsNSLLSFKTDDDSITKRRLRSFNSADELP 232
 
Name Accession Description Interval E-value
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
225-661 0e+00

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 612.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 225 KPLADTMRPDTLQDYFGQSRAVGQDTLLRSLLETNEIPSLILWGPPGCGKTTLAHIIANNSKKHsirFVTLSATNAKTND 304
Cdd:COG2256    13 APLAERMRPRTLDEVVGQEHLLGPGKPLRRAIEAGRLSSMILWGPPGTGKTTLARLIANATDAE---FVALSAVTSGVKD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 305 VRDVIKQAQNEKSFfKRKTVLFIDEIHRFNKSQQDTFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEKLPVEA 384
Cdd:COG2256    90 IREVIEEARERRAY-GRRTILFVDEIHRFNKAQQDALLPHVEDGTITLIGATTENPSFEVNSALLSRCRVFVLKPLSEED 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 385 MVTILMRAINSLGIHVLDSSRPtdplshssnsssepamfIEDKAVDTLAYLSDGDARAGLNGLQLAVLARLSSrkmfckk 464
Cdd:COG2256   169 LEQLLERALADDERGLGGYKLE-----------------LDDEALEALARLADGDARRALNALELAVLSAPPD------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 465 sgqsyspSRVLITENDVKEGLQRSHILYDRAGEEHYNCISALHKSMRGSDQNASLYWLARMLEGGEDPLYVARRLVRFAS 544
Cdd:COG2256   225 -------GVIEITLELVEEALQRRALRYDKDGDEHYDLISAFIKSIRGSDPDAALYWLARMLEAGEDPRFIARRLVIMAS 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 545 EDIGLADPSALTQAVAAYQGCHFIGMPECEVLLAQCVVYFARAPKSIEVYSAYNNVKACLRnhQGPLPPVPLHLRNAPTR 624
Cdd:COG2256   298 EDIGLADPQALQIAVAAAQAVERLGMPEGRIALAQAVIYLATAPKSNAAYLAINAALADVR--EGGSLPVPLHLRNAPTK 375
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1622936123 625 LMKDLGYGKGYKYnpMYSEP---VDQEYLPEELRGVDFFK 661
Cdd:COG2256   376 LMKELGYGKGYKY--PHDYPggyVGQQYLPDELKGRRYYE 413
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
226-661 0e+00

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 604.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 226 PLADTMRPDTLQDYFGQSRAVGQDTLLRSLLETNEIPSLILWGPPGCGKTTLAHIIANNSKKHsirFVTLSATNAKTNDV 305
Cdd:PRK13342    1 PLAERMRPKTLDEVVGQEHLLGPGKPLRRMIEAGRLSSMILWGPPGTGKTTLARIIAGATDAP---FEALSAVTSGVKDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 306 RDVIKQAQNEKSFfKRKTVLFIDEIHRFNKSQQDTFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEKLPVEAM 385
Cdd:PRK13342   78 REVIEEARQRRSA-GRRTILFIDEIHRFNKAQQDALLPHVEDGTITLIGATTENPSFEVNPALLSRAQVFELKPLSEEDI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 386 VTILMRAINslgihvlDSSRPTDPlshssnsssepamfIEDKAVDTLAYLSDGDARAGLNGLQLAVLarlssrkmfckks 465
Cdd:PRK13342  157 EQLLKRALE-------DKERGLVE--------------LDDEALDALARLANGDARRALNLLELAAL------------- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 466 gqsyspSRVLITENDVKEGLQRSHILYDRAGEEHYNCISALHKSMRGSDQNASLYWLARMLEGGEDPLYVARRLVRFASE 545
Cdd:PRK13342  203 ------GVDSITLELLEEALQKRAARYDKDGDEHYDLISALHKSIRGSDPDAALYYLARMLEAGEDPLFIARRLVIIASE 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 546 DIGLADPSALTQAVAAYQGCHFIGMPECEVLLAQCVVYFARAPKSIEVYSAYNNVKACLRNhqGPLPPVPLHLRNAPTRL 625
Cdd:PRK13342  277 DIGLADPNALQVAVAAADAVERIGMPEGRIALAQAVIYLALAPKSNAAYTAINAALADVRE--GGSLPVPLHLRNAPTKL 354
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1622936123 626 MKDLGYGKGYKYnpMYSEP---VDQEYLPEELRGVDFFK 661
Cdd:PRK13342  355 MKELGYGKGYKY--PHDYPngyVGQQYLPDELKGKRYYE 391
MgsA_C pfam12002
MgsA AAA+ ATPase C terminal; The MgsA protein possesses DNA-dependent ATPase and ssDNA ...
512-661 3.13e-81

MgsA AAA+ ATPase C terminal; The MgsA protein possesses DNA-dependent ATPase and ssDNA annealing activities. MgsA contributes to the recovery of stalled replication forks and therefore prevents genomic instability caused by aberrant DNA replication. Additionally, MgsA may play a role in chromosomal segregation. This is consistent with a report that MgsA co-localizes with the replisome and affects chromosome segregation. This domain represents the C terminal region of MgsA.


Pssm-ID: 463426 [Multi-domain]  Cd Length: 158  Bit Score: 253.81  E-value: 3.13e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 512 GSDQNASLYWLARMLEGGEDPLYVARRLVRFASEDIGLADPSALTQAVAAYQGCHFIGMPECEVLLAQCVVYFARAPKSI 591
Cdd:pfam12002   1 GSDPDAALYWLARMLEAGEDPLFIARRLVIIASEDIGLADPQALVVAVAAAQAVERIGMPEARIPLAQAVIYLALAPKSN 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622936123 592 EVYSAYNNVKACLRNhqGPLPPVPLHLRNAPTRLMKDLGYGKGYKYNPMYSE-PVDQEYLPEELRGVDFFK 661
Cdd:pfam12002  81 SAYLAIDAALADVRE--GGSLPVPLHLRNAPTKLMKKLGYGKGYKYPHDYPNgYVKQQYLPDELKGRRYYE 149
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
240-376 2.52e-21

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: 90.67  E-value: 2.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 240 FGQSRAVGQdtlLRSLLETNEIPSLILWGPPGCGKTTLAHIIANNSKKHSIRFVTLSATNAKTNDVRDVIKQAQNEKSFF 319
Cdd:cd00009     1 VGQEEAIEA---LREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 320 KRK-----TVLFIDEIHRFNKSQQDTFLP--------HVECGTITLIGATTENPSFQVNAALLSRCRVIV 376
Cdd:cd00009    78 ELAekakpGVLFIDEIDSLSRGAQNALLRvletlndlRIDRENVRVIGATNRPLLGDLDRALYDRLDIRI 147
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
263-380 1.14e-12

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: 65.86  E-value: 1.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123  263 SLILWGPPGCGKTTLAHIIANNSKKHSIRFVTLSATNAKTNDVRDVIKQAQNEKSFF----------------KRKTVLF 326
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASgsgelrlrlalalarkLKPDVLI 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622936123  327 IDEIHRFNKSQQD----------TFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEKL 380
Cdd:smart00382  84 LDEITSLLDAEQEallllleelrLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLI 147
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
235-398 1.30e-12

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: 68.87  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 235 TLQDYFGQSRAVGQ-DTLLRSLLETNEIPS-LILWGPPGCGKTTLAHIIANNSKKhSIRfVTLSATNAKTNDVRDVIkqa 312
Cdd:TIGR00635   2 LLAEFIGQEKVKEQlQLFIEAAKMRQEALDhLLLYGPPGLGKTTLAHIIANEMGV-NLK-ITSGPALEKPGDLAAIL--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 313 qnekSFFKRKTVLFIDEIHRFNKSQQDTFLPHVE-------------CGTI-------TLIGATTEnpSFQVNAALLSRC 372
Cdd:TIGR00635  77 ----TNLEEGDVLFIDEIHRLSPAVEELLYPAMEdfrldivigkgpsARSVrldlppfTLVGATTR--AGMLTSPLRDRF 150
                         170       180
                  ....*....|....*....|....*..
gi 1622936123 373 RVIV-LEKLPVEAMVTILMRAINSLGI 398
Cdd:TIGR00635 151 GIILrLEFYTVEELAEIVSRSAGLLNV 177
ZnF_Rad18 smart00734
Rad18-like CCHC zinc finger; Yeast Rad18p functions with Rad5p in error-free post-replicative ...
17-40 3.77e-09

Rad18-like CCHC zinc finger; Yeast Rad18p functions with Rad5p in error-free post-replicative DNA repair. This zinc finger is likely to bind nucleic-acids.


Pssm-ID: 128973 [Multi-domain]  Cd Length: 24  Bit Score: 52.22  E-value: 3.77e-09
                           10        20
                   ....*....|....*....|....
gi 1622936123   17 QVQCPVCQQMMPAAHINSHLDRCL 40
Cdd:smart00734   1 LVQCPVCFREVPENLINSHLDSCL 24
zf-WRNIP1_ubi pfam18279
Werner helicase-interacting protein 1 ubiquitin-binding domain; This domain is found in the ...
16-36 5.48e-09

Werner helicase-interacting protein 1 ubiquitin-binding domain; This domain is found in the Werner helicase-interacting protein 1 present in Homo sapiens. The domain is a zinc finger responsible and has a zinc-coordinating B-B-A fold. WRNIP1 UBZ binds ubiquitin in a similar manner to Rad18 UBZ.


Pssm-ID: 375706  Cd Length: 21  Bit Score: 51.75  E-value: 5.48e-09
                          10        20
                  ....*....|....*....|.
gi 1622936123  16 HQVQCPVCQQMMPAAHINSHL 36
Cdd:pfam18279   1 HQVQCPVCQQMMPAAHINSHL 21
cell_div_CdvC NF041006
cell division protein CdvC;
264-330 1.31e-04

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 44.73  E-value: 1.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622936123 264 LILWGPPGCGKTTLAHIIANNSKKHsirFVTLSATN--------AKTNdVRDVIKQAQNEKSFFKRKTVLFIDEI 330
Cdd:NF041006  137 ILLYGPPGCGKTMLAAAVANEIDSE---FIHVDAASimskwlgeAEKN-VAKIFKKAREKSKEEGKPAIIFIDEI 207
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
18-83 7.48e-04

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 42.38  E-value: 7.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936123  18 VQCPVCQQMMPAAHINSHLDRCLLLH--PAGHAEP---AAGSH-RAGERAKGPSPPGAKRRRLSESSALKQP 83
Cdd:COG5432   161 VHCPACSNLVPHNQINQHLDSCLNSPssPSSSSSPyknKDNSKsNSLLSFKTDDDSITKRRLRSFNSADELP 232
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
235-330 2.98e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 39.76  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 235 TLQDY-FGQSRAVGQDTL--LRSL--LETNEipSLILWGPPGCGKTTLAHIIANNS--KKHSIRFVTlsatnakTNDVRD 307
Cdd:NF038214   61 TLEDFdFTAAPGLDKAQIreLATLdfIERAE--NVLLLGPPGTGKTHLAIALGYAAcrQGYRVRFTT-------AADLVE 131
                          90       100
                  ....*....|....*....|....*....
gi 1622936123 308 VIKQAQNEKSFFKRKT------VLFIDEI 330
Cdd:NF038214  132 QLAQARADGRLGRLLRrlarydLLIIDEL 160
 
Name Accession Description Interval E-value
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
225-661 0e+00

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 612.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 225 KPLADTMRPDTLQDYFGQSRAVGQDTLLRSLLETNEIPSLILWGPPGCGKTTLAHIIANNSKKHsirFVTLSATNAKTND 304
Cdd:COG2256    13 APLAERMRPRTLDEVVGQEHLLGPGKPLRRAIEAGRLSSMILWGPPGTGKTTLARLIANATDAE---FVALSAVTSGVKD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 305 VRDVIKQAQNEKSFfKRKTVLFIDEIHRFNKSQQDTFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEKLPVEA 384
Cdd:COG2256    90 IREVIEEARERRAY-GRRTILFVDEIHRFNKAQQDALLPHVEDGTITLIGATTENPSFEVNSALLSRCRVFVLKPLSEED 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 385 MVTILMRAINSLGIHVLDSSRPtdplshssnsssepamfIEDKAVDTLAYLSDGDARAGLNGLQLAVLARLSSrkmfckk 464
Cdd:COG2256   169 LEQLLERALADDERGLGGYKLE-----------------LDDEALEALARLADGDARRALNALELAVLSAPPD------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 465 sgqsyspSRVLITENDVKEGLQRSHILYDRAGEEHYNCISALHKSMRGSDQNASLYWLARMLEGGEDPLYVARRLVRFAS 544
Cdd:COG2256   225 -------GVIEITLELVEEALQRRALRYDKDGDEHYDLISAFIKSIRGSDPDAALYWLARMLEAGEDPRFIARRLVIMAS 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 545 EDIGLADPSALTQAVAAYQGCHFIGMPECEVLLAQCVVYFARAPKSIEVYSAYNNVKACLRnhQGPLPPVPLHLRNAPTR 624
Cdd:COG2256   298 EDIGLADPQALQIAVAAAQAVERLGMPEGRIALAQAVIYLATAPKSNAAYLAINAALADVR--EGGSLPVPLHLRNAPTK 375
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1622936123 625 LMKDLGYGKGYKYnpMYSEP---VDQEYLPEELRGVDFFK 661
Cdd:COG2256   376 LMKELGYGKGYKY--PHDYPggyVGQQYLPDELKGRRYYE 413
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
226-661 0e+00

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 604.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 226 PLADTMRPDTLQDYFGQSRAVGQDTLLRSLLETNEIPSLILWGPPGCGKTTLAHIIANNSKKHsirFVTLSATNAKTNDV 305
Cdd:PRK13342    1 PLAERMRPKTLDEVVGQEHLLGPGKPLRRMIEAGRLSSMILWGPPGTGKTTLARIIAGATDAP---FEALSAVTSGVKDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 306 RDVIKQAQNEKSFfKRKTVLFIDEIHRFNKSQQDTFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEKLPVEAM 385
Cdd:PRK13342   78 REVIEEARQRRSA-GRRTILFIDEIHRFNKAQQDALLPHVEDGTITLIGATTENPSFEVNPALLSRAQVFELKPLSEEDI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 386 VTILMRAINslgihvlDSSRPTDPlshssnsssepamfIEDKAVDTLAYLSDGDARAGLNGLQLAVLarlssrkmfckks 465
Cdd:PRK13342  157 EQLLKRALE-------DKERGLVE--------------LDDEALDALARLANGDARRALNLLELAAL------------- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 466 gqsyspSRVLITENDVKEGLQRSHILYDRAGEEHYNCISALHKSMRGSDQNASLYWLARMLEGGEDPLYVARRLVRFASE 545
Cdd:PRK13342  203 ------GVDSITLELLEEALQKRAARYDKDGDEHYDLISALHKSIRGSDPDAALYYLARMLEAGEDPLFIARRLVIIASE 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 546 DIGLADPSALTQAVAAYQGCHFIGMPECEVLLAQCVVYFARAPKSIEVYSAYNNVKACLRNhqGPLPPVPLHLRNAPTRL 625
Cdd:PRK13342  277 DIGLADPNALQVAVAAADAVERIGMPEGRIALAQAVIYLALAPKSNAAYTAINAALADVRE--GGSLPVPLHLRNAPTKL 354
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1622936123 626 MKDLGYGKGYKYnpMYSEP---VDQEYLPEELRGVDFFK 661
Cdd:PRK13342  355 MKELGYGKGYKY--PHDYPngyVGQQYLPDELKGKRYYE 391
PRK13341 PRK13341
AAA family ATPase;
220-660 3.17e-134

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 410.99  E-value: 3.17e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 220 QMLQG-KPLADTMRPDTLQDYFGQSRAVGQDTLLRSLLETNEIPSLILWGPPGCGKTTLAHIIANNSKKHsirFVTLSAT 298
Cdd:PRK13341   10 QMSQSeAPLADRLRPRTLEEFVGQDHILGEGRLLRRAIKADRVGSLILYGPPGVGKTTLARIIANHTRAH---FSSLNAV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 299 NAKTNDVRDVIKQAQNEKSFFKRKTVLFIDEIHRFNKSQQDTFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLE 378
Cdd:PRK13341   87 LAGVKDLRAEVDRAKERLERHGKRTILFIDEVHRFNKAQQDALLPWVENGTITLIGATTENPYFEVNKALVSRSRLFRLK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 379 KLPVEAMVTILMRAINslgihvlDSSRPTDPLshssnsssepAMFIEDKAVDTLAYLSDGDARAGLNGLQLAVlarlssr 458
Cdd:PRK13341  167 SLSDEDLHQLLKRALQ-------DKERGYGDR----------KVDLEPEAEKHLVDVANGDARSLLNALELAV------- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 459 kmfckksgQSYSP---SRVLITENDVKEGLQRSHILYDRAGEEHYNCISALHKSMRGSDQNASLYWLARMLEGGEDPLYV 535
Cdd:PRK13341  223 --------ESTPPdedGLIDITLAIAEESIQQRAVLYDKEGDAHFDTISAFIKSLRGSDPDAALYWLARMVEAGEDPRFI 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 536 ARRLVRFASEDIGLADPSALTQAVAAYQGCHFIGMPECEVLLAQCVVYFARAPKSIEVYSAYNNVKAClrnHQGPLPPVP 615
Cdd:PRK13341  295 FRRMLIAASEDVGLADPQALVVVEACAAAFERVGLPEGLYPLAQAALYLATAPKSNSVLGFFDALKKV---REEQVQDVP 371
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1622936123 616 LHLRNaPTRLMKDLGYGKGYKYNPMYSEP-VDQEYLPEELRGVDFF 660
Cdd:PRK13341  372 NHLRD-ANRDGKAFGDGVGYRYPHAFRDHwVAQQYLPEALQGEVFW 416
MgsA_C pfam12002
MgsA AAA+ ATPase C terminal; The MgsA protein possesses DNA-dependent ATPase and ssDNA ...
512-661 3.13e-81

MgsA AAA+ ATPase C terminal; The MgsA protein possesses DNA-dependent ATPase and ssDNA annealing activities. MgsA contributes to the recovery of stalled replication forks and therefore prevents genomic instability caused by aberrant DNA replication. Additionally, MgsA may play a role in chromosomal segregation. This is consistent with a report that MgsA co-localizes with the replisome and affects chromosome segregation. This domain represents the C terminal region of MgsA.


Pssm-ID: 463426 [Multi-domain]  Cd Length: 158  Bit Score: 253.81  E-value: 3.13e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 512 GSDQNASLYWLARMLEGGEDPLYVARRLVRFASEDIGLADPSALTQAVAAYQGCHFIGMPECEVLLAQCVVYFARAPKSI 591
Cdd:pfam12002   1 GSDPDAALYWLARMLEAGEDPLFIARRLVIIASEDIGLADPQALVVAVAAAQAVERIGMPEARIPLAQAVIYLALAPKSN 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622936123 592 EVYSAYNNVKACLRNhqGPLPPVPLHLRNAPTRLMKDLGYGKGYKYNPMYSE-PVDQEYLPEELRGVDFFK 661
Cdd:pfam12002  81 SAYLAIDAALADVRE--GGSLPVPLHLRNAPTKLMKKLGYGKGYKYPHDYPNgYVKQQYLPDELKGRRYYE 149
PRK14700 PRK14700
recombination factor protein RarA; Provisional
342-655 1.96e-45

recombination factor protein RarA; Provisional


Pssm-ID: 173163 [Multi-domain]  Cd Length: 300  Bit Score: 163.65  E-value: 1.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 342 LPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEKLPVEAMVTILMRAINS---LGIHVLDssrptdplshssnsss 418
Cdd:PRK14700    1 MPYVESGKIILIGATTENPTYYLNDALVSRLFILRLKRLSLVATQKLIEKALSQdevLAKHKFK---------------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 419 epamfIEDKAVDTLAYLSDGDARAGLNGLQLAVLARLSSRKMFCKKSgqsyspsrvlITENDVKEGLQRSHilydRAGEE 498
Cdd:PRK14700   65 -----IDDGLYNAMHNYNEGDCRKILNLLERMFLISTRGDEIYLNKE----------LFDQAVGETSRDFH----REGKE 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 499 HYNCISALHKSMRGSDQNASLYWLARMLEGGEDPLYVARRLVRFASEDIGLADPSALTQAVAAYQGCHFIGMPECEVLLA 578
Cdd:PRK14700  126 FYEQLSAFHKSVRGTDPDAAIFWLSVMLDNGVDPLVIARRMLCIASEDIGNADPQALRVAMDAWNAYEKLGMPEGRLVLA 205
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936123 579 QCVVYFARAPKSIEVYSAYNNVKACLRNhQGPLpPVPLHLRNaptrlMKDLGYGKGYKYNPMYsepVDQEYLPEELR 655
Cdd:PRK14700  206 QAAIYLAVAPKSNACYKALAQAQQLVKS-LGNI-DVPQHLKN-----YKDSNYLYPHNYPNSY---VIQQYLPDNII 272
AAA_assoc_2 pfam16193
AAA C-terminal domain; AAA_assoc_2 is found at the C-terminus of a relatively small set of AAA ...
424-511 1.70e-29

AAA C-terminal domain; AAA_assoc_2 is found at the C-terminus of a relatively small set of AAA domains in proteins ranging from archaeal to fungi, plants and mammals.


Pssm-ID: 465057  Cd Length: 81  Bit Score: 111.41  E-value: 1.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 424 IEDKAVDTLAYLSDGDARAGLNGLQLAVLARLSSRKmfckksgqsyspsRVLITENDVKEGLQRSHILYDRAGEEHYNCI 503
Cdd:pfam16193   7 LDDEALEALAELADGDARRALNALELAVLSTPPDDG-------------GIHITLEILEEALQRKALRYDKDGDEHYDLI 73

                  ....*...
gi 1622936123 504 SALHKSMR 511
Cdd:pfam16193  74 SAFHKSIR 81
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
240-376 2.52e-21

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: 90.67  E-value: 2.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 240 FGQSRAVGQdtlLRSLLETNEIPSLILWGPPGCGKTTLAHIIANNSKKHSIRFVTLSATNAKTNDVRDVIKQAQNEKSFF 319
Cdd:cd00009     1 VGQEEAIEA---LREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 320 KRK-----TVLFIDEIHRFNKSQQDTFLP--------HVECGTITLIGATTENPSFQVNAALLSRCRVIV 376
Cdd:cd00009    78 ELAekakpGVLFIDEIDSLSRGAQNALLRvletlndlRIDRENVRVIGATNRPLLGDLDRALYDRLDIRI 147
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
264-377 1.60e-19

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: 84.95  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 264 LILWGPPGCGKTTLAHIIANNSKkhsIRFVTLSATN-------AKTNDVRDVIKQAQNeksffKRKTVLFIDEIHRFNKS 336
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELG---APFIEISGSElvskyvgESEKRLRELFEAAKK-----LAPCVIFIDEIDALAGS 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936123 337 Q-----------QDTFLPHVE-----CGTITLIGATTEnpSFQVNAALLSRCRVIVL 377
Cdd:pfam00004  73 RgsggdsesrrvVNQLLTELDgftssNSKVIVIAATNR--PDKLDPALLGRFDRIIE 127
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
230-398 8.74e-16

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 79.02  E-value: 8.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 230 TMRPDTLQDYFGQSRAVGQ-DTLLRSLLETNEIPS-LILWGPPGCGKTTLAHIIAN--NSKkhsirFVTLSA-------- 297
Cdd:PRK00080   18 SLRPKSLDEFIGQEKVKENlKIFIEAAKKRGEALDhVLLYGPPGLGKTTLANIIANemGVN-----IRITSGpalekpgd 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 298 -----TNAKTNDvrdvikqaqneksffkrktVLFIDEIHRFNKSQQDTFLPHVECGTI--------------------TL 352
Cdd:PRK00080   93 laailTNLEEGD-------------------VLFIDEIHRLSPVVEEILYPAMEDFRLdimigkgpaarsirldlppfTL 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622936123 353 IGATTEnpsfqvnAALLS---RCR---VIVLEKLPVEAMVTILMRAINSLGI 398
Cdd:PRK00080  154 IGATTR-------AGLLTsplRDRfgiVQRLEFYTVEELEKIVKRSARILGV 198
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
230-398 1.20e-15

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 78.58  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 230 TMRPDTLQDYFGQSRAVGQ-DTLLRSLLETNE-IPSLILWGPPGCGKTTLAHIIANNSKKhSIRfVT----------LSA 297
Cdd:COG2255    21 SLRPKRLDEYIGQEKVKENlKIFIEAAKKRGEaLDHVLLYGPPGLGKTTLAHIIANEMGV-NIR-ITsgpaiekpgdLAA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 298 --TNAKTNDvrdvikqaqneksffkrktVLFIDEIHRFNKSQQDTFLPHVECGTI--------------------TLIGA 355
Cdd:COG2255    99 ilTNLEEGD-------------------VLFIDEIHRLSRVVEEILYPAMEDFRLdivigkgpaarsirldlppfTLVGA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622936123 356 TTenpsfqvNAALLS---RCRVIVLEKL---PVEAMVTILMRAINSLGI 398
Cdd:COG2255   160 TT-------RAGLLTsplRDRFGIVLRLefyTVEELAEIVKRSARILGV 201
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
231-357 5.07e-14

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 70.22  E-value: 5.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 231 MRPDTLQDYFGQSRAVGQ-DTLLRSLLETNEIPS-LILWGPPGCGKTTLAHIIANNSKKhSIRfVT----------LSA- 297
Cdd:pfam05496   1 LRPRTLDEYIGQEKVKENlKIFIEAAKQRGEALDhVLLYGPPGLGKTTLANIIANEMGV-NIR-ITsgpaierpgdLAAi 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 298 -TNAKTNDvrdvikqaqneksffkrktVLFIDEIHRFNKSQQDTFLPHVECGTI--------------------TLIGAT 356
Cdd:pfam05496  79 lTNLEPGD-------------------VLFIDEIHRLNRAVEEILYPAMEDFRLdivigkgpsarsirldlppfTLVGAT 139

                  .
gi 1622936123 357 T 357
Cdd:pfam05496 140 T 140
PRK04195 PRK04195
replication factor C large subunit; Provisional
226-487 1.94e-13

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 73.03  E-value: 1.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 226 PLADTMRPDTLQDYFGQSRAVGQdtlLRSLLET--NEIPS--LILWGPPGCGKTTLAHIIANnskkhSIRF--VTLSATN 299
Cdd:PRK04195    3 PWVEKYRPKTLSDVVGNEKAKEQ---LREWIESwlKGKPKkaLLLYGPPGVGKTSLAHALAN-----DYGWevIELNASD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 300 AKTNDV-RDVIKQAQNEKSFF-KRKTVLFIDE---IHrfnkSQQDTflphvecG---TITLIGATTENPSfqVNAA---- 367
Cdd:PRK04195   75 QRTADViERVAGEAATSGSLFgARRKLILLDEvdgIH----GNEDR-------GgarAILELIKKAKQPI--ILTAndpy 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 368 ------LLSRCRVIVLEKLPVEAMVTILMRAINSLGIhvldssrptdplshssnsssepamFIEDKAVDTLAYLSDGDAR 441
Cdd:PRK04195  142 dpslreLRNACLMIEFKRLSTRSIVPVLKRICRKEGI------------------------ECDDEALKEIAERSGGDLR 197
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1622936123 442 AGLNGLQLAVLARLSsrkmfckksgqsyspsrvlITENDVKEGLQR 487
Cdd:PRK04195  198 SAINDLQAIAEGYGK-------------------LTLEDVKTLGRR 224
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
233-444 2.46e-13

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 71.76  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 233 PDTLQDYFGQSRAVgqdTLLRSLLETNEIP-SLILWGPPGCGKTTLAHIIA---N-------------------NSKKHS 289
Cdd:COG2812     6 PQTFDDVVGQEHVV---RTLKNALASGRLAhAYLFTGPRGVGKTTLARILAkalNcengptgepcgecescraiAAGSHP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 290 -IRFVTLSATNAKTNDVRDVIKQAQNeKSFFKRKTVLFIDEIHRFNKSQQDTFL-------PHVecgtiTLIGATTEnPS 361
Cdd:COG2812    83 dVIEIDAEASNIGVDDIRELIEKVSY-APVEGRYKVYIIDEAHMLTTEAFNALLktleeppPHV-----VFILATTE-PQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 362 fQVNAALLSRCRVIVLEKLPVEAMVTILMRAINSLGIHvldssrptdplshssnsssepamfIEDKAVDTLAYLSDGDAR 441
Cdd:COG2812   156 -KLLPTILSRCQRFDFRRLPPEEIAEHLAKIAEREGIE------------------------IEPEALALIARAADGSMR 210

                  ...
gi 1622936123 442 AGL 444
Cdd:COG2812   211 DAL 213
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
263-380 1.14e-12

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: 65.86  E-value: 1.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123  263 SLILWGPPGCGKTTLAHIIANNSKKHSIRFVTLSATNAKTNDVRDVIKQAQNEKSFF----------------KRKTVLF 326
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASgsgelrlrlalalarkLKPDVLI 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622936123  327 IDEIHRFNKSQQD----------TFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEKL 380
Cdd:smart00382  84 LDEITSLLDAEQEallllleelrLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLI 147
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
235-398 1.30e-12

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: 68.87  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 235 TLQDYFGQSRAVGQ-DTLLRSLLETNEIPS-LILWGPPGCGKTTLAHIIANNSKKhSIRfVTLSATNAKTNDVRDVIkqa 312
Cdd:TIGR00635   2 LLAEFIGQEKVKEQlQLFIEAAKMRQEALDhLLLYGPPGLGKTTLAHIIANEMGV-NLK-ITSGPALEKPGDLAAIL--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 313 qnekSFFKRKTVLFIDEIHRFNKSQQDTFLPHVE-------------CGTI-------TLIGATTEnpSFQVNAALLSRC 372
Cdd:TIGR00635  77 ----TNLEEGDVLFIDEIHRLSPAVEELLYPAMEdfrldivigkgpsARSVrldlppfTLVGATTR--AGMLTSPLRDRF 150
                         170       180
                  ....*....|....*....|....*..
gi 1622936123 373 RVIV-LEKLPVEAMVTILMRAINSLGI 398
Cdd:TIGR00635 151 GIILrLEFYTVEELAEIVSRSAGLLNV 177
44 PHA02544
clamp loader, small subunit; Provisional
250-375 2.06e-11

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 65.40  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 250 TLLRSLLETNEIPSLILWGP-PGCGKTTLAHIIANNSkkhSIRFVTLSATNAKTNDVRDVIKQAQNEKSFFKRKTVLFID 328
Cdd:PHA02544   31 ETFKSIVKKGRIPNMLLHSPsPGTGKTTVAKALCNEV---GAEVLFVNGSDCRIDFVRNRLTRFASTVSLTGGGKVIIID 107
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622936123 329 EIHRfnksqqdTFLPHVECGTITLIGATTENPSF--------QVNAALLSRCRVI 375
Cdd:PHA02544  108 EFDR-------LGLADAQRHLRSFMEAYSKNCSFiitannknGIIEPLRSRCRVI 155
PRK05896 PRK05896
DNA polymerase III subunits gamma and tau; Validated
232-448 6.83e-11

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235638 [Multi-domain]  Cd Length: 605  Bit Score: 65.25  E-value: 6.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 232 RPDTLQDYFGQSRAvgQDTLLRSLLETNEIPSLILWGPPGCGKTTLAHIIA--------------NN-------SKKHSI 290
Cdd:PRK05896   11 RPHNFKQIIGQELI--KKILVNAILNNKLTHAYIFSGPRGIGKTSIAKIFAkainclnpkdgdccNScsvcesiNTNQSV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 291 RFVTL-SATNAKTNDVRDVIKQAQNEKSFFKRKtVLFIDEIHRFNKSQQDTFLPHVE--CGTITLIGATTEnpSFQVNAA 367
Cdd:PRK05896   89 DIVELdAASNNGVDEIRNIIDNINYLPTTFKYK-VYIIDEAHMLSTSAWNALLKTLEepPKHVVFIFATTE--FQKIPLT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 368 LLSRCRVIVLEKLPveamvtilmraiNSLGIHVLDSSRPTDPLShssnsssepamfIEDKAVDTLAYLSDGDARAGLNGL 447
Cdd:PRK05896  166 IISRCQRYNFKKLN------------NSELQELLKSIAKKEKIK------------IEDNAIDKIADLADGSLRDGLSIL 221

                  .
gi 1622936123 448 Q 448
Cdd:PRK05896  222 D 222
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
227-399 9.74e-11

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 65.11  E-value: 9.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 227 LADTMRPDTLQDYFGQSRAVgqDTLLRSLLETNEIPSLILWGPPGCGKTTLAHIIANN------------------SKKH 288
Cdd:PRK08691    6 LARKWRPKTFADLVGQEHVV--KALQNALDEGRLHHAYLLTGTRGVGKTTIARILAKSlncenaqhgepcgvcqscTQID 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 289 SIRFVTL----SATNAKTNDVRDVIKQAQNEKSFFKRKtVLFIDEIHRFNKSQQDTFLPHVE--CGTITLIGATTEnPSf 362
Cdd:PRK08691   84 AGRYVDLleidAASNTGIDNIREVLENAQYAPTAGKYK-VYIIDEVHMLSKSAFNAMLKTLEepPEHVKFILATTD-PH- 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622936123 363 QVNAALLSRCRVIVLEKLPVEAMVTILMRAINSLGIH 399
Cdd:PRK08691  161 KVPVTVLSRCLQFVLRNMTAQQVADHLAHVLDSEKIA 197
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
264-389 1.68e-10

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: 63.39  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 264 LILWGPPGCGKTTLAHIIANNSKKHSIRfVTLSA--------TNAKtndVRDVIKQAQNEKsffkrKTVLFIDEI----- 330
Cdd:COG0464   194 LLLYGPPGTGKTLLARALAGELGLPLIE-VDLSDlvskyvgeTEKN---LREVFDKARGLA-----PCVLFIDEAdalag 264
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936123 331 ------HRFNKSQQDTFLPHVECGT--ITLIGATteNPSFQVNAALLSRCRVIVLEKLP-VEAMVTIL 389
Cdd:COG0464   265 krgevgDGVGRRVVNTLLTEMEELRsdVVVIAAT--NRPDLLDPALLRRFDEIIFFPLPdAEERLEIF 330
PLN03025 PLN03025
replication factor C subunit; Provisional
226-448 4.19e-10

replication factor C subunit; Provisional


Pssm-ID: 178596 [Multi-domain]  Cd Length: 319  Bit Score: 61.67  E-value: 4.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 226 PLADTMRPDTLQDYFGQSRAVGQdtlLRSLLETNEIPSLILWGPPGCGKTT----LAHIIANNSKKHSIrfVTLSATNAK 301
Cdd:PLN03025    2 PWVEKYRPTKLDDIVGNEDAVSR---LQVIARDGNMPNLILSGPPGTGKTTsilaLAHELLGPNYKEAV--LELNASDDR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 302 TND-VRDVIKQ-AQNEKSFFK-RKTVLFIDEIHRFNKSQQDTFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLE 378
Cdd:PLN03025   77 GIDvVRNKIKMfAQKKVTLPPgRHKIVILDEADSMTSGAQQALRRTMEIYSNTTRFALACNTSSKIIEPIQSRCAIVRFS 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 379 KLPVEAMVTILMRAINSLGIhvldssrPTDPlshssnsssepamfiedKAVDTLAYLSDGDARAGLNGLQ 448
Cdd:PLN03025  157 RLSDQEILGRLMKVVEAEKV-------PYVP-----------------EGLEAIIFTADGDMRQALNNLQ 202
PRK14970 PRK14970
DNA polymerase III subunits gamma and tau; Provisional
228-383 8.97e-10

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184934 [Multi-domain]  Cd Length: 367  Bit Score: 61.04  E-value: 8.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 228 ADTMRPDTLQDYFGQSRAVgqDTLLRSLlETNEIPSLILW-GPPGCGKTTLAHIIA-----------NNSKKHSIrFVTL 295
Cdd:PRK14970    8 ARKYRPQTFDDVVGQSHIT--NTLLNAI-ENNHLAQALLFcGPRGVGKTTCARILArkinqpgyddpNEDFSFNI-FELD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 296 SATNAKTNDVRDVIKQAQNEKSFFKRKtVLFIDEIHRFNKSQQDTFLPHVE--CGTITLIGATTENpsFQVNAALLSRCR 373
Cdd:PRK14970   84 AASNNSVDDIRNLIDQVRIPPQTGKYK-IYIIDEVHMLSSAAFNAFLKTLEepPAHAIFILATTEK--HKIIPTILSRCQ 160
                         170
                  ....*....|
gi 1622936123 374 VIVLEKLPVE 383
Cdd:PRK14970  161 IFDFKRITIK 170
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
252-454 1.31e-09

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 59.60  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 252 LRSLLETNEIP-SLILWGPPGCGKTTLAHIIAN------------NSKKHSIR--------FVTLSATNAKT----NDVR 306
Cdd:COG0470     8 LLAAAESGRLPhALLLHGPPGIGKTTLALALARdllcenpeggkaCGQCHSRLmaagnhpdLLELNPEEKSDqigiDQIR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 307 DVIKQAQNeKSFFKRKTVLFIDEIHRFNKSQQDTFL-----PHVECgTITLIgatTENPSfQVNAALLSRCRVIVLEKLP 381
Cdd:COG0470    88 ELGEFLSL-TPLEGGRKVVIIDEADAMNEAAANALLktleePPKNT-PFILI---ANDPS-RLLPTIRSRCQVIRFRPPS 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936123 382 VEAMVTILMRAinslgihvldssrptdplshssnsssepamFIEDKAVDTLAYLSDGDARAGLNGLQLAVLAR 454
Cdd:COG0470   162 EEEALAWLREE------------------------------GVDEDALEAILRLAGGDPRAAINLLQALAGRK 204
rfc PRK00440
replication factor C small subunit; Reviewed
232-450 2.04e-09

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 59.50  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 232 RPDTLQDYFGQSRAVGQdtlLRSLLETNEIPSLILWGPPGCGKTTLAHIIA-----NNSKKHsirFVTLSATNAKTNDV- 305
Cdd:PRK00440   12 RPRTLDEIVGQEEIVER---LKSYVKEKNMPHLLFAGPPGTGKTTAALALArelygEDWREN---FLELNASDERGIDVi 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 306 RDVIKQAQNEKSF----FKrktVLFIDEIHRFNKSQQdtflpHVECGTITLIGATTE-----NPSFQVNAALLSRCRVIV 376
Cdd:PRK00440   86 RNKIKEFARTAPVggapFK---IIFLDEADNLTSDAQ-----QALRRTMEMYSQNTRfilscNYSSKIIDPIQSRCAVFR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622936123 377 LEKLPVEAMVTILMRAINSLGIHvldssrptdplshssnsssepamfIEDKAVDTLAYLSDGDARAGLNGLQLA 450
Cdd:PRK00440  158 FSPLKKEAVAERLRYIAENEGIE------------------------ITDDALEAIYYVSEGDMRKAINALQAA 207
HLD_clamp_RarA cd18139
helical lid domain of recombination factor protein RarA; Recombination factor RarA ...
380-486 2.58e-09

helical lid domain of recombination factor protein RarA; Recombination factor RarA (Replication associated recombination gene/protein A, also known as MgsA (Maintenance of genome stability A) or Mgs1 in yeast and WRNIP1 in mammals) is a member of the clamp-loader clade of the AAA+ superfamily. It functions as a tetramer. RarA co-localize with the replication fork throughout the cell cycle and may play a role in the rescue of stalled replication forks.


Pssm-ID: 350841 [Multi-domain]  Cd Length: 75  Bit Score: 54.17  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 380 LPVEAMVTILMRAINSLGIHvldssrptdplshssnssSEPAMFIEDKAVDTLAYLSDGDARAGLNGLQLAVLArlssrk 459
Cdd:cd18139     1 LSEEDLEKLLKRALEDKERG------------------GDRKVTIDDEALELLAEAADGDARSALNLLELAVLS------ 56
                          90       100
                  ....*....|....*....|....*..
gi 1622936123 460 mfCKKSGqsyspsRVLITENDVKEGLQ 486
Cdd:cd18139    57 --AEEDG------GIVITLEDLEEVLQ 75
ZnF_Rad18 smart00734
Rad18-like CCHC zinc finger; Yeast Rad18p functions with Rad5p in error-free post-replicative ...
17-40 3.77e-09

Rad18-like CCHC zinc finger; Yeast Rad18p functions with Rad5p in error-free post-replicative DNA repair. This zinc finger is likely to bind nucleic-acids.


Pssm-ID: 128973 [Multi-domain]  Cd Length: 24  Bit Score: 52.22  E-value: 3.77e-09
                           10        20
                   ....*....|....*....|....
gi 1622936123   17 QVQCPVCQQMMPAAHINSHLDRCL 40
Cdd:smart00734   1 LVQCPVCFREVPENLINSHLDSCL 24
zf-WRNIP1_ubi pfam18279
Werner helicase-interacting protein 1 ubiquitin-binding domain; This domain is found in the ...
16-36 5.48e-09

Werner helicase-interacting protein 1 ubiquitin-binding domain; This domain is found in the Werner helicase-interacting protein 1 present in Homo sapiens. The domain is a zinc finger responsible and has a zinc-coordinating B-B-A fold. WRNIP1 UBZ binds ubiquitin in a similar manner to Rad18 UBZ.


Pssm-ID: 375706  Cd Length: 21  Bit Score: 51.75  E-value: 5.48e-09
                          10        20
                  ....*....|....*....|.
gi 1622936123  16 HQVQCPVCQQMMPAAHINSHL 36
Cdd:pfam18279   1 HQVQCPVCQQMMPAAHINSHL 21
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
229-453 9.08e-09

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 57.69  E-value: 9.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 229 DTMRPDTLQDYFGQSRAVGQdtlLRSLLETNEIPSLILWGPPGCGKTT----LAHIIANNSKKHSI-------------- 290
Cdd:PRK12402    7 EKYRPALLEDILGQDEVVER---LSRAVDSPNLPHLLVQGPPGSGKTAavraLARELYGDPWENNFtefnvadffdqgkk 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 291 ------RFVTLSATNAKTN-DVRDVIKQAQNEKSFFKR-----KTVLFiDEIHRFNKSQQDTFLPHVE--CGTITLIGAT 356
Cdd:PRK12402   84 ylvedpRFAHFLGTDKRIRsSKIDNFKHVLKEYASYRPlsadyKTILL-DNAEALREDAQQALRRIMEqySRTCRFIIAT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 357 TeNPSfQVNAALLSRCRVIVLEKLPVEAMVTILmrainslgIHVLDSSRPTdplshssnsssepamfIEDKAVDTLAYLS 436
Cdd:PRK12402  163 R-QPS-KLIPPIRSRCLPLFFRAPTDDELVDVL--------ESIAEAEGVD----------------YDDDGLELIAYYA 216
                         250
                  ....*....|....*..
gi 1622936123 437 DGDARAGLNGLQLAVLA 453
Cdd:PRK12402  217 GGDLRKAILTLQTAALA 233
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
232-330 1.87e-08

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 56.55  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 232 RPDTLQDYFGqsravGQDTLLRSLLETNEIP----------------SLILWGPPGCGKTTLAHIIANNSKKHSIR---- 291
Cdd:COG1222    72 SPDVTFDDIG-----GLDEQIEEIREAVELPlknpelfrkygieppkGVLLYGPPGTGKTLLAKAVAGELGAPFIRvrgs 146
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622936123 292 -----FVTLSATNaktndVRDVIKQAQNeksffKRKTVLFIDEI 330
Cdd:COG1222   147 elvskYIGEGARN-----VREVFELARE-----KAPSIIFIDEI 180
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
262-374 1.45e-07

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: 51.51  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 262 PSLILWGPPGCGKTTLAHIIANNSKKHSIRfVTLSATNAKTND-----VRDVIKQAQNeksffKRKTVLFIDEIH----- 331
Cdd:cd19481    27 KGILLYGPPGTGKTLLAKALAGELGLPLIV-VKLSSLLSKYVGeseknLRKIFERARR-----LAPCILFIDEIDaigrk 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622936123 332 RFNKSQQDTFLPHV-----------ECGTITLIGATteNPSFQVNAALLSRCRV 374
Cdd:cd19481   101 RDSSGESGELRRVLnqllteldgvnSRSKVLVIAAT--NRPDLLDPALLRPGRF 152
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
249-335 2.29e-07

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 53.41  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 249 DTLLRSLLETNEIpsLILWGPPGCGKTTLA-HIIANNSKKHSIRFVTLSATNAKTNDVRDVIKQAqneKSFFKRKTVLFI 327
Cdd:COG1373    10 LDKLLKLLDNRKA--VVITGPRQVGKTTLLkQLAKELENILYINLDDPRLRALAEEDPDDLLEAL---KELYPGKTYLFL 84

                  ....*...
gi 1622936123 328 DEIHRFNK 335
Cdd:COG1373    85 DEIQRVPE 92
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
232-448 4.99e-07

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 52.89  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 232 RPDTLQDYFGQSRAVgqDTLlRSLLETNEIPSLILW-GPPGCGKTTLAHIIA------NNSKK----------------H 288
Cdd:PRK14950   11 RSQTFAELVGQEHVV--QTL-RNAIAEGRVAHAYLFtGPRGVGKTSTARILAkavnctTNDPKgrpcgtcemcraiaegS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 289 SIRFVTL-SATNAKTNDVRDVIKQAQNEKSFFkRKTVLFIDEIHRFNKSQQDTFL-------PHVecgtiTLIGATTEnp 360
Cdd:PRK14950   88 AVDVIEMdAASHTSVDDAREIIERVQFRPALA-RYKVYIIDEVHMLSTAAFNALLktleeppPHA-----IFILATTE-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 361 SFQVNAALLSRCRVIVLEKLPVEAMVTILMRAINSLGIhvldssrptdplshssnsssepamFIEDKAVDTLAYLSDGDA 440
Cdd:PRK14950  160 VHKVPATILSRCQRFDFHRHSVADMAAHLRKIAAAEGI------------------------NLEPGALEAIARAATGSM 215

                  ....*...
gi 1622936123 441 RAGLNGLQ 448
Cdd:PRK14950  216 RDAENLLQ 223
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
264-341 1.18e-06

Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 50.96  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 264 LILWGPPGCGKTTLAHIIANNSKKH--SIRFVTLSATNAkTNDVRDVIKQAQNEKsfFKRK----TVLFIDEIHRF--NK 335
Cdd:COG0593    37 LFLYGGVGLGKTHLLHAIGNEALENnpGARVVYLTAEEF-TNDFINAIRNNTIEE--FKEKyrsvDVLLIDDIQFLagKE 113

                  ....*.
gi 1622936123 336 SQQDTF 341
Cdd:COG0593   114 ATQEEF 119
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
264-400 1.27e-06

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 50.27  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 264 LILWGPPGCGKTTLAHIIANNSKKHSI---------RFVTLSATNaktndVRDVIKQAQNeksffkRKTVLFIDEIH--- 331
Cdd:COG1223    38 ILFYGPPGTGKTMLAEALAGELKLPLLtvrldsligSYLGETARN-----LRKLFDFARR------APCVIFFDEFDaia 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 332 --RFNKS-------------QQDTFLPhvecGTITLIGATteNPSFQVNAALLSRCRVIVLEKLP-VEAMVTILMRAINS 395
Cdd:COG1223   107 kdRGDQNdvgevkrvvnallQELDGLP----SGSVVIAAT--NHPELLDSALWRRFDEVIEFPLPdKEERKEILELNLKK 180

                  ....*
gi 1622936123 396 LGIHV 400
Cdd:COG1223   181 FPLPF 185
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
232-386 1.84e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 50.93  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 232 RPDTLQDYFGQSRAVgqdTLLRSLLETNEIPSLILW-GPPGCGKTTLAHIIANN----------------------SKKH 288
Cdd:PRK14971   12 RPSTFESVVGQEALT---TTLKNAIATNKLAHAYLFcGPRGVGKTTCARIFAKTincqnltadgeacnecescvafNEQR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 289 SIRFVTL-SATNAKTNDVRDVIKQAQNEKSFFKRKtVLFIDEIHRFNKSQQDTFL------PHvecgTITLIGATTENps 361
Cdd:PRK14971   89 SYNIHELdAASNNSVDDIRNLIEQVRIPPQIGKYK-IYIIDEVHMLSQAAFNAFLktleepPS----YAIFILATTEK-- 161
                         170       180
                  ....*....|....*....|....*
gi 1622936123 362 FQVNAALLSRCRVIVLEKLPVEAMV 386
Cdd:PRK14971  162 HKILPTILSRCQIFDFNRIQVADIV 186
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
264-330 6.99e-06

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like 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: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 46.63  E-value: 6.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622936123 264 LILWGPPGCGKTTLAHIIANNSKkhsIRFVTLSATN-------AKTNDVRDVIKQAQNEKSffkrkTVLFIDEI 330
Cdd:cd19518    37 VLLHGPPGCGKTMLANAIAGELK---VPFLKISATEivsgvsgESEEKIRELFDQAISNAP-----CIVFIDEI 102
DNA_pol3_delta2 pfam13177
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ...
241-381 1.59e-05

DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalyzed reaction. The delta subunit is also known as HolA.


Pssm-ID: 433013 [Multi-domain]  Cd Length: 161  Bit Score: 45.66  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 241 GQSRAVgqdTLLRSLLETNEIPSLILW-GPPGCGKTTLAHIIA-----------------NNSKK-----HS-IRFVTLS 296
Cdd:pfam13177   1 GQPEAI---QLLQNSLENGRLSHAYLFsGPEGVGKLELALAFAkalfceepgddlpcgqcRSCRRiesgnHPdLVIIEPE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 297 ATNAKTNDVRDVIKQAQnEKSFFKRKTVLFIDEIHRFNKSQQDTFL-----PHVEcgtiTLIGATTENPSfQVNAALLSR 371
Cdd:pfam13177  78 GQSIKIDQIRELQKEFS-KSPYEGKKKVYIIEDAEKMTASAANSLLkfleePPGN----TVIILLTENPS-RLLPTIRSR 151
                         170
                  ....*....|
gi 1622936123 372 CRVIVLEKLP 381
Cdd:pfam13177 152 CQIIRFKPLS 161
rad24 TIGR00602
checkpoint protein rad24; All proteins in this family for which functions are known are ...
224-469 2.21e-05

checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129690 [Multi-domain]  Cd Length: 637  Bit Score: 47.64  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 224 GKPLADTMRPDTLQDYFGQSRAVG--QDTLLRSLLETNEIPSLILWGPPGCGKTTLAHIIA--------NNSKKHSIRF- 292
Cdd:TIGR00602  71 NEPWVEKYKPETQHELAVHKKKIEevETWLKAQVLENAPKRILLITGPSGCGKSTTIKILSkelgiqvqEWSNPTLPDFq 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 293 -----VTLSATNAKTNDV------RDVIKQAQNE-----KSFFKRKTVLFIDEI----HRFNKSQQDTF-LPHVECGTIT 351
Cdd:TIGR00602 151 kndhkVTLSLESCFSNFQsqievfSEFLLRATNKlqmlgDDLMTDKKIILVEDLpnqfYRDTRALHEILrWKYVSIGRCP 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 352 LIGATTEN------------PSFQV-NAALLSRCRVIVLEKLPVEAmvTILMRAINSLgihvldssrptdpLSHSSNSSS 418
Cdd:TIGR00602 231 LVFIITESlegdnnqrrllfPAETImNKEILEEPRVSNISFNPIAP--TIMKKFLNRI-------------VTIEAKKNG 295
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622936123 419 EPAMFIEDKAVDTLAYLSDGDARAGLNGLQLAVlARLSSRKMFCKKSGQSY 469
Cdd:TIGR00602 296 EKIKVPKKTSVELLCQGCSGDIRSAINSLQFSS-SKSGSLPIKKRMSTKSD 345
AAA_14 pfam13173
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
264-332 2.68e-05

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


Pssm-ID: 463799 [Multi-domain]  Cd Length: 128  Bit Score: 44.12  E-value: 2.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936123 264 LILWGPPGCGKTTLA-HIIANNSKKHSIRFVTL---SATNAKTNDVRDVIkqaqnEKSFFKRKTVLFIDEIHR 332
Cdd:pfam13173   5 LVITGPRQVGKTTLLlQLIKELLPPENILYINLddpRLLKLADFELLELF-----LELLYPGKTYLFLDEIQR 72
PRK12422 PRK12422
chromosomal replication initiator protein DnaA;
266-493 3.58e-05

chromosomal replication initiator protein DnaA;


Pssm-ID: 183521 [Multi-domain]  Cd Length: 445  Bit Score: 46.75  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 266 LWGPPGCGKTTL----AHIIANNSKKhsIRFVtlsATNAKTNDVRDVIK--QAQNEKSFFKRKTVLFIDEIHRFNK---S 336
Cdd:PRK12422  146 LFGPEGSGKTHLmqaaVHALRESGGK--ILYV---RSELFTEHLVSAIRsgEMQRFRQFYRNVDALFIEDIEVFSGkgaT 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 337 QQDTFLP----HVECGTITLIGATTENPSFQVNAALLSRCR---VIVLEKLPVEAMVTILMRAINSLGIHvldssrptdp 409
Cdd:PRK12422  221 QEEFFHTfnslHTEGKLIVISSTCAPQDLKAMEERLISRFEwgiAIPLHPLTKEGLRSFLERKAEALSIR---------- 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 410 lshssnsssepamfIEDKAVDTLAYLSDGDARAGLNGLQLavlarLSSRKMFCKKSGQsyspsrvLITENDVKeglqrsH 489
Cdd:PRK12422  291 --------------IEETALDFLIEALSSNVKSLLHALTL-----LAKRVAYKKLSHQ-------LLYVDDIK------A 338

                  ....
gi 1622936123 490 ILYD 493
Cdd:PRK12422  339 LLHD 342
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
265-330 5.38e-05

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: 43.81  E-value: 5.38e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936123 265 ILWGPPGCGKTTLAHIIANNSKkhsIRFVTLSATNAKT-------NDVRDVIKQAQNEKSffkrkTVLFIDEI 330
Cdd:cd19511    31 LLYGPPGCGKTLLAKALASEAG---LNFISVKGPELFSkyvgeseRAVREIFQKARQAAP-----CIIFFDEI 95
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
263-372 5.64e-05

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 43.44  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 263 SLILWGPPGCGKTTLAHIIANNSKKHSIRFVTLSAtNAKTNDVRDVIKQAQNEKSF--------FKRKTVLFIDEIHRFN 334
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTR-DTTEEDLFGRRNIDPGGASWvdgplvraAREGEIAVLDEINRAN 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936123 335 KSQQDTFLP-------HVECGT---------ITLIgATTENPSFQVN---AALLSRC 372
Cdd:pfam07728  80 PDVLNSLLSllderrlLLPDGGelvkaapdgFRLI-ATMNPLDRGLNelsPALRSRF 135
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
264-337 7.27e-05

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in 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 second 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_r2-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: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 43.65  E-value: 7.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936123 264 LILWGPPGCGKTTLAHIIANNSKKHSI-----RFVTLSATNAKTNdVRDVIKQAQNEKSffkrkTVLFIDEIHRFNKSQ 337
Cdd:cd19528    30 VLFYGPPGCGKTLLAKAIANECQANFIsvkgpELLTMWFGESEAN-VRDIFDKARAAAP-----CVLFFDELDSIAKAR 102
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
266-330 1.02e-04

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 45.21  E-value: 1.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622936123 266 LWGPPGCGKTTLAHIIANNSKKHSIRFVTLSATN------AKTndVRDVIKQAQnEKSffkrKTVLFIDEI 330
Cdd:PRK03992  170 LYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQkfigegARL--VRELFELAR-EKA----PSIIFIDEI 233
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
264-330 1.23e-04

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: 43.05  E-value: 1.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936123 264 LILWGPPGCGKTTLAHIIANNSKkhsIRFVTLSA----------TNAKtndVRDVIKQAQNEKsffkrKTVLFIDEI 330
Cdd:cd19503    37 VLLHGPPGTGKTLLARAVANEAG---ANFLSISGpsivskylgeSEKN---LREIFEEARSHA-----PSIIFIDEI 102
cell_div_CdvC NF041006
cell division protein CdvC;
264-330 1.31e-04

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 44.73  E-value: 1.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622936123 264 LILWGPPGCGKTTLAHIIANNSKKHsirFVTLSATN--------AKTNdVRDVIKQAQNEKSFFKRKTVLFIDEI 330
Cdd:NF041006  137 ILLYGPPGCGKTMLAAAVANEIDSE---FIHVDAASimskwlgeAEKN-VAKIFKKAREKSKEEGKPAIIFIDEI 207
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
264-340 1.51e-04

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. 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: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 42.80  E-value: 1.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936123 264 LILWGPPGCGKTTLAHIIAnnsKKHSIRFVTLSATNAKTNDVRDVIKQAQNEKSFFKR--KTVLFIDEIHRFNKSQQDT 340
Cdd:cd19520    38 VLLYGPPGCGKTMLAKATA---KEAGARFINLQVSSLTDKWYGESQKLVAAVFSLASKlqPSIIFIDEIDSFLRQRSST 113
ftsH CHL00176
cell division protein; Validated
253-330 1.52e-04

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 45.04  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 253 RSLLETNEIPS-LILWGPPGCGKTTLAHIIANNSKK--HSI-------RFVTLSATNaktndVRDVIKQAQNeksffKRK 322
Cdd:CHL00176  207 RFTAVGAKIPKgVLLVGPPGTGKTLLAKAIAGEAEVpfFSIsgsefveMFVGVGAAR-----VRDLFKKAKE-----NSP 276

                  ....*...
gi 1622936123 323 TVLFIDEI 330
Cdd:CHL00176  277 CIVFIDEI 284
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
216-330 1.60e-04

second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like 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: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 42.48  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 216 EEIRQMLQGKPLADTMRPDtlqdyfgQSRAVGQDTllrslletneiPS-LILWGPPGCGKTTLAHIIANNSKKHSIRFVT 294
Cdd:cd19530     2 DHVREELTMSILRPIKRPD-------IYKALGIDL-----------PTgVLLYGPPGCGKTLLAKAVANESGANFISVKG 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622936123 295 LSATNAKTND----VRDVIKQAQNEKSffkrkTVLFIDEI 330
Cdd:cd19530    64 PELLNKYVGEseraVRQVFQRARASAP-----CVIFFDEV 98
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
264-329 1.72e-04

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. 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: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 42.42  E-value: 1.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622936123 264 LILWGPPGCGKTTLAHIIANNSkkhSIRFVTLSA-------TNAKTNDVRDVIKQAQNEKSffkrkTVLFIDE 329
Cdd:cd19526    30 ILLYGPPGCGKTLLASAIASEC---GLNFISVKGpellnkyIGASEQNVRDLFSRAQSAKP-----CILFFDE 94
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
265-330 2.83e-04

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN 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: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 41.94  E-value: 2.83e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 265 ILWGPPGCGKTTLAHIIANNSKKHSIRFVTLSATNAKTND----VRDVIKQAQNeksffKRKTVLFIDEI 330
Cdd:cd19502    41 LLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEgarlVRELFEMARE-----KAPSIIFIDEI 105
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
235-330 3.07e-04

IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.


Pssm-ID: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 42.82  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 235 TLQDY-FGQSRAVGQDTL--LRSLLETNEIPSLILWGPPGCGKTTLAHIIANNSKKH--SIRFVTlsatnakTNDVRDVI 309
Cdd:pfam01695  63 TLEDFdFTFAPGLDQRIVaeLASLSFIDRAQNVVLLGPPGVGKTHLAIALGVEACRAgySVRFTS-------AADLVNQL 135
                          90       100
                  ....*....|....*....|....*..
gi 1622936123 310 KQAQNEKSF------FKRKTVLFIDEI 330
Cdd:pfam01695 136 KRAHGDGKLtrklqqLLKPDVLILDEW 162
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
263-371 4.25e-04

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). 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: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 41.57  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 263 SLILWGPPGCGKTTLAHIIANNSkkhSIRFVTLSATN-------AKTNDVRDVIKQAQneksfFKRKTVLFIDEIHRFNK 335
Cdd:cd19509    34 GILLYGPPGTGKTLLARAVASES---GSTFFSISASSlvskwvgESEKIVRALFALAR-----ELQPSIIFIDEIDSLLS 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622936123 336 SQQDT-----------FL------PHVECGTITLIGATteNPSFQVNAALLSR 371
Cdd:cd19509   106 ERGSGeheasrrvkteFLvqmdgvLNKPEDRVLVLGAT--NRPWELDEAFLRR 156
PRK04132 PRK04132
replication factor C small subunit; Provisional
225-283 4.50e-04

replication factor C small subunit; Provisional


Pssm-ID: 235223 [Multi-domain]  Cd Length: 846  Bit Score: 43.67  E-value: 4.50e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622936123 225 KPLADTMRPDTLQDYFGQSRAVGQdtlLRSLLETNEIPSLILWGPPGCGK--TTLAHIIAN 283
Cdd:PRK04132    7 KPWVEKYRPQRLDDIVGQEHIVKR---LKHYVKTGSMPHLLFAGPPGVGKclTGDTKVIAN 64
Bac_DnaA pfam00308
Bacterial dnaA protein;
264-338 5.46e-04

Bacterial dnaA protein;


Pssm-ID: 278724 [Multi-domain]  Cd Length: 219  Bit Score: 41.93  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 264 LILWGPPGCGKTTLAHIIANN--SKKHSIRFVTLSATNAkTNDVRDVIKqaQNEKSFFKRK----TVLFIDEIHRFNKSQ 337
Cdd:pfam00308  37 LFIYGGVGLGKTHLLHAIGNYalQNAPNLRVVYLTAEEF-LNDFVDAIR--DNKTNQFKEKyrnvDVLLIDDIQFLAGKE 113

                  .
gi 1622936123 338 Q 338
Cdd:pfam00308 114 G 114
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
205-401 5.72e-04

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 43.04  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 205 GGRPHPRALAAEE-----IRQmLQGKPLADTMRPDTLQDYFGQSRAV---GQDTLLRSLLETNEIpsLILWGPPGCGKTT 276
Cdd:COG0507    79 GRRYLTRLLEAEQrlarrLRR-LARPALDEADVEAALAALEPRAGITlsdEQREAVALALTTRRV--SVLTGGAGTGKTT 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 277 LAHIIANNSKKHSIRFVTLSATNaktndvrdviKQAQN--EKSFFKRKTvlfideIHRfnksqqdtflphvecgtitLIG 354
Cdd:COG0507   156 TLRALLAALEALGLRVALAAPTG----------KAAKRlsESTGIEART------IHR-------------------LLG 200
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622936123 355 ATTENPSFQVNA-ALLSRCRVIVLEklpvEA-MVTI-----LMRAINSLGIHVL 401
Cdd:COG0507   201 LRPDSGRFRHNRdNPLTPADLLVVD----EAsMVDTrlmaaLLEALPRAGARLI 250
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
260-330 6.88e-04

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: 41.06  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 260 EIP-SLILWGPPGCGKTTLAHIIANNSKkhsIRFVTLSATN---------AKTndVRDVIKQAqneksffKRKT--VLFI 327
Cdd:cd19501    35 KIPkGVLLVGPPGTGKTLLAKAVAGEAG---VPFFSISGSDfvemfvgvgASR--VRDLFEQA-------KKNApcIVFI 102

                  ...
gi 1622936123 328 DEI 330
Cdd:cd19501   103 DEI 105
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
18-83 7.48e-04

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 42.38  E-value: 7.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936123  18 VQCPVCQQMMPAAHINSHLDRCLLLH--PAGHAEP---AAGSH-RAGERAKGPSPPGAKRRRLSESSALKQP 83
Cdd:COG5432   161 VHCPACSNLVPHNQINQHLDSCLNSPssPSSSSSPyknKDNSKsNSLLSFKTDDDSITKRRLRSFNSADELP 232
AAA_22 pfam13401
AAA domain;
263-333 7.54e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 40.02  E-value: 7.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 263 SLILWGPPGCGKTTLAHIIANNSKKHSIRFVTLSATNAKT-NDVRDVIKQA--------QNEKSFF----------KRKT 323
Cdd:pfam13401   7 ILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSpKDLLRALLRAlglplsgrLSKEELLaalqqlllalAVAV 86
                          90
                  ....*....|
gi 1622936123 324 VLFIDEIHRF 333
Cdd:pfam13401  87 VLIIDEAQHL 96
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
260-330 1.16e-03

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 41.94  E-value: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936123 260 EIPSLILW-GPPGCGKTTLAHIIANNSKkhsIRFVTLSATN-------AKTNDVRDVIKQAQNEKSffkrkTVLFIDEI 330
Cdd:PRK10733  183 KIPKGVLMvGPPGTGKTLLAKAIAGEAK---VPFFTISGSDfvemfvgVGASRVRDMFEQAKKAAP-----CIIFIDEI 253
clpC CHL00095
Clp protease ATP binding subunit
265-389 1.26e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 41.97  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 265 ILWGPPGCGKTT----LAHIIANNSKK---HSIRFVTLSATN--AKTND-------VRDVIKQAQNEKsffkrKTVLFID 328
Cdd:CHL00095  204 ILIGEPGVGKTAiaegLAQRIVNRDVPdilEDKLVITLDIGLllAGTKYrgefeerLKRIFDEIQENN-----NIILVID 278
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936123 329 EIHR-FNKSQQDT-------FLPHVECGTITLIGATTEN---PSFQVNAALLSRCRVIVLEKLPVEAMVTIL 389
Cdd:CHL00095  279 EVHTlIGAGAAEGaidaaniLKPALARGELQCIGATTLDeyrKHIEKDPALERRFQPVYVGEPSVEETIEIL 350
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
264-330 1.30e-03

26S protease regulatory subunit 6B-like protein; Provisional


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 41.67  E-value: 1.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622936123 264 LILWGPPGCGKTTLAHIIANNSKKHSIRFVTLSATNAKTND----VRDVIKQAQnEKSffkrKTVLFIDEI 330
Cdd:PTZ00454  182 VLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEgprmVRDVFRLAR-ENA----PSIIFIDEV 247
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
268-327 1.89e-03

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 40.03  E-value: 1.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 268 GPPGCGKTTLAHIIANNSKKHSIRFVtlsATNAKTNDVRDVIKQAQNEKSFfkRKTVLFI 327
Cdd:pfam00006  21 GGSGVGKTVLAGMIARQASADVVVYA---LIGERGREVREFIEELLGSGAL--KRTVVVV 75
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
251-331 2.28e-03

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 39.30  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 251 LLRSLLeTNEIPSLiLWGPPGCGKTTlahIIAN-----NSKKHSIRFVTLSA-TNAktNDVRDVIkqaqnEKSFFKR--- 321
Cdd:pfam12775  23 LLDLLL-KNGKPVL-LVGPTGTGKTV---IIQNllrklDKEKYLPLFINFSAqTTS--NQTQDII-----ESKLEKRrkg 90
                          90
                  ....*....|....*...
gi 1622936123 322 --------KTVLFIDEIH 331
Cdd:pfam12775  91 vygppggkKLVVFIDDLN 108
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
248-284 2.78e-03

DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350801 [Multi-domain]  Cd Length: 127  Bit Score: 38.33  E-value: 2.78e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622936123 248 QDTLLRSLLETneiPSLILWGPPGCGKT-TLAHIIANN 284
Cdd:cd18043     4 QEAAIISARNG---KNVVIQGPPGTGKSqTIANIIANA 38
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
235-330 2.98e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 39.76  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 235 TLQDY-FGQSRAVGQDTL--LRSL--LETNEipSLILWGPPGCGKTTLAHIIANNS--KKHSIRFVTlsatnakTNDVRD 307
Cdd:NF038214   61 TLEDFdFTAAPGLDKAQIreLATLdfIERAE--NVLLLGPPGTGKTHLAIALGYAAcrQGYRVRFTT-------AADLVE 131
                          90       100
                  ....*....|....*....|....*....
gi 1622936123 308 VIKQAQNEKSFFKRKT------VLFIDEI 330
Cdd:NF038214  132 QLAQARADGRLGRLLRrlarydLLIIDEL 160
Rad17 pfam03215
Rad17 P-loop domain;
223-381 3.02e-03

Rad17 P-loop domain;


Pssm-ID: 367398 [Multi-domain]  Cd Length: 186  Bit Score: 39.17  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 223 QGKPLADTMRPDTLQDYFGQSRAVG--QDTLLRSLLETNEIPSLILWGPPGCGKTTLAHIIannSKKHSIRFVT-LSATN 299
Cdd:pfam03215   5 GGEQWYEKYKPNCLEQLAVHKRKIKdvQEWLDAMFLENAKHRILLISGPSGCGKSTVIKEL---SKELGPKYREwSNPTS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 300 AKTNDvrdvikqaqNEKSFFKRKTVLFideihrfnksqqDTFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEK 379
Cdd:pfam03215  82 FRSPP---------NQVTDFRGDCIVN------------SRFLSQMESFSEFELKGARYLVMQKRGKNAQGNKKLILIED 140

                  ..
gi 1622936123 380 LP 381
Cdd:pfam03215 141 LP 142
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
248-348 3.35e-03

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: 38.44  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 248 QDTLLRSLLETNEIPSLILWGPPGCGKT-TLAHIIANNSKKHSI--------------RFVT---------LSATNAKTN 303
Cdd:cd17926     5 QEEALEAWLAHKNNRRGILVLPTGSGKTlTALALIAYLKELRTLivvptdalldqwkeRFEDflgdssiglIGGGKKKDF 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622936123 304 DVRDVI--------KQAQNEKSFFKRKTVLFIDEIHRFNKSQQDTFLPHVECG 348
Cdd:cd17926    85 DDANVVvatyqslsNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSEILKELNAK 137
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
264-283 3.41e-03

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: 37.58  E-value: 3.41e-03
                          10        20
                  ....*....|....*....|
gi 1622936123 264 LILWGPPGCGKTTLAHIIAN 283
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLAR 20
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
264-354 3.43e-03

DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 37.98  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 264 LILWGPPGCGKT-TLAHIIANNSKKHSIRFVTLSATnakTNDVRDVIkqaqneksffkrkTVLFIDEIhrfnkSQQ---D 339
Cdd:cd17934     2 SLIQGPPGTGKTtTIAAIVLQLLKGLRGKRVLVTAQ---SNVAVDNV-------------DVVIIDEA-----SQItepE 60
                          90
                  ....*....|....*
gi 1622936123 340 TFLPHVECGTITLIG 354
Cdd:cd17934    61 LLIALIRAKKVVLVG 75
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
235-346 4.34e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.38  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 235 TLQDY-FGQSRAVGQDTL--LRSL--LETNEipSLILWGPPGCGKTTLAHIIANN--SKKHSIRFVTlsatnakTNDVRD 307
Cdd:COG1484    70 TLEDFdFDAQPGLDRRQIleLATLdfIERGE--NLILLGPPGTGKTHLAIALGHEacRAGYRVRFTT-------APDLVN 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622936123 308 VIKQAQNEKSF------FKRKTVLFIDEI--HRFNKSQQDTFLPHVE 346
Cdd:COG1484   141 ELKEARADGRLerllkrLAKVDLLILDELgyLPLDAEGAELLFELIS 187
dnaA PRK00149
chromosomal replication initiator protein DnaA;
264-341 7.91e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 234667 [Multi-domain]  Cd Length: 401  Bit Score: 38.96  E-value: 7.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 264 LILWGPPGCGKTTLAHIIANNSKKHS----IRFVTlsaTNAKTNDVRDVIKQAQNEKsfFKRKT----VLFIDEIHRF-N 334
Cdd:PRK00149  102 LFIYGGVGLGKTHLLHAIGNYILEKNpnakVVYVT---SEKFTNDFVNALRNNTMEE--FKEKYrsvdVLLIDDIQFLaG 176

                  ....*...
gi 1622936123 335 KSQ-QDTF 341
Cdd:PRK00149  177 KERtQEEF 184
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
246-330 8.56e-03

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. 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: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 37.52  E-value: 8.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936123 246 VGQDTLLRSLLETNEIPS---------------LILWGPPGCGKTTLAHIIANNSKkhsIRFVTLSATNAKTNDVRDVIK 310
Cdd:cd19524     3 AGQDLAKQALQEMVILPSlrpelftglrapargLLLFGPPGNGKTMLAKAVAAESN---ATFFNISAASLTSKYVGEGEK 79
                          90       100
                  ....*....|....*....|....*
gi 1622936123 311 QAqneKSFFK-----RKTVLFIDEI 330
Cdd:cd19524    80 LV---RALFAvarelQPSIIFIDEV 101
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
246-294 9.55e-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: 37.48  E-value: 9.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622936123 246 VGQDTLLRSLLE------TNEIPSLILWGPPGCGKTTLAHIIANNSKKHSIRFVT 294
Cdd:pfam13191   3 VGREEELEQLLDaldrvrSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLR 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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