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Conserved domains on  [gi|2468166099|ref|WP_276618956|]
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MULTISPECIES: AAA family ATPase [Alistipes]

Protein Classification

AAA family ATPase( domain architecture ID 11468604)

AAA family ATPase containing an AAA (ATPases Associated with various cellular Activities) domain, may function as an ATP-dependent endonuclease or the ATPase component of an ABC-type transporter

CATH:  3.40.50.300
Gene Ontology:  GO:0016887|GO:0005524
PubMed:  15037233|18208389|16828312|18466635|16072036|11916378|15037234|17897320
SCOP:  2000039

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4637 COG4637
Predicted ATPase [General function prediction only];
2-394 6.80e-122

Predicted ATPase [General function prediction only];


:

Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 357.70  E-value: 6.80e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   2 KIEKIKIENYKVYRNTEIRnLSNFSVFLGANGAGKSTLFDVFGFLSDALKANVKTALNKRGGYREVYSRDGE---GPILF 78
Cdd:COG4637     1 MITRIRIKNFKSLRDLELP-LGPLTVLIGANGSGKSNLLDALRFLSDAARGGLQDALARRGGLEELLWRGPRtitEPIRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  79 EIKFRNdkiegETQPLITYRLEIGFE--NGLPIITTEILSYRRGGYGRPyrFLDFhRGEGTAIINEDeysssssstfqdr 156
Cdd:COG4637    80 ELEFAE-----EDERDLRYELELGLPepGGRPEVKEERLWLKRGSGGRP--FLDF-RPKGRAVGGEP------------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 157 reqQTLDSPDILaIKGLGQFQKFKAISSFRRLLDDWYVSNFQIQEARNVEDVGFSEHLSTSGNNLAQVTRYIWENHRNVF 236
Cdd:COG4637   139 ---ERLDSPESL-LSQLGDPERFPELRALREALRSWRFYDFHPAPLRQPQPAGRTPVLAPDGSNLAAVLATLRETHPERF 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 237 NTILEKFRKRVPGVENVIAEETQDGRIVLKFKDNSFQDPFVARFVSDGTIKMFAYLVLLNDPVKHPLLCVEEPENYLHPE 316
Cdd:COG4637   215 ERILEALRDAFPGFEDIEVEPDEDGRVLLEFREKGLDRPFPARELSDGTLRFLALLAALLSPRPPPLLCIEEPENGLHPD 294

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468166099 317 LLPELAEEFREYADKgGQVFISTHSPDFVNALQPDELFWLQK-SNGATTIRKASEDATIKALyaNGDKLGWLWREGYLK 394
Cdd:COG4637   295 LLPALAELLREASER-TQVIVTTHSPALLDALEPEEVLVLEReDDGETRIRRLSDLELPEWL--EGYSLGELWARGLLG 370
 
Name Accession Description Interval E-value
COG4637 COG4637
Predicted ATPase [General function prediction only];
2-394 6.80e-122

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 357.70  E-value: 6.80e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   2 KIEKIKIENYKVYRNTEIRnLSNFSVFLGANGAGKSTLFDVFGFLSDALKANVKTALNKRGGYREVYSRDGE---GPILF 78
Cdd:COG4637     1 MITRIRIKNFKSLRDLELP-LGPLTVLIGANGSGKSNLLDALRFLSDAARGGLQDALARRGGLEELLWRGPRtitEPIRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  79 EIKFRNdkiegETQPLITYRLEIGFE--NGLPIITTEILSYRRGGYGRPyrFLDFhRGEGTAIINEDeysssssstfqdr 156
Cdd:COG4637    80 ELEFAE-----EDERDLRYELELGLPepGGRPEVKEERLWLKRGSGGRP--FLDF-RPKGRAVGGEP------------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 157 reqQTLDSPDILaIKGLGQFQKFKAISSFRRLLDDWYVSNFQIQEARNVEDVGFSEHLSTSGNNLAQVTRYIWENHRNVF 236
Cdd:COG4637   139 ---ERLDSPESL-LSQLGDPERFPELRALREALRSWRFYDFHPAPLRQPQPAGRTPVLAPDGSNLAAVLATLRETHPERF 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 237 NTILEKFRKRVPGVENVIAEETQDGRIVLKFKDNSFQDPFVARFVSDGTIKMFAYLVLLNDPVKHPLLCVEEPENYLHPE 316
Cdd:COG4637   215 ERILEALRDAFPGFEDIEVEPDEDGRVLLEFREKGLDRPFPARELSDGTLRFLALLAALLSPRPPPLLCIEEPENGLHPD 294

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468166099 317 LLPELAEEFREYADKgGQVFISTHSPDFVNALQPDELFWLQK-SNGATTIRKASEDATIKALyaNGDKLGWLWREGYLK 394
Cdd:COG4637   295 LLPALAELLREASER-TQVIVTTHSPALLDALEPEEVLVLEReDDGETRIRRLSDLELPEWL--EGYSLGELWARGLLG 370
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 25-346 1.92e-29

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 115.95  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  25 FSVFLGANGAGKSTLFDVFGFLSDALKANVKTALNKRGGY------REVYSRDGEGPILFEI-KFRNDKIegetqplity 97
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGgiggipSLLNGIDPKEPIEFEIsEFLEDGV---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  98 RLEIGFENGLPIITTEILSYRRGGYGRPYRFLDFHRGEGTAIINEDEysssSSSTFQDRREQQTLDSPDILAIKGLGQFQ 177
Cdd:pfam13304  71 RYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEE----LRLGLDVEERIELSLSELSDLISGLLLLS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 178 KFKAISSFRRLLDDWYVSNFQIQEARNvedvgfseHLSTSGNNLAQVTRYIWENHRNVFNTILEKFRKRVPGVENViaee 257
Cdd:pfam13304 147 IISPLSFLLLLDEGLLLEDWAVLDLAA--------DLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDD---- 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 258 tQDGRIVLKFKDNSFQDPFVARFVSDGTIKMFAYLV-LLNDPVKHPLLCVEEPENYLHPELLPELAEEFREYADKGGQVF 336
Cdd:pfam13304 215 -RLRERGLILLENGGGGELPAFELSDGTKRLLALLAaLLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLI 293

                         330
                  ....*....|
gi 2468166099 337 ISTHSPDFVN 346
Cdd:pfam13304 294 LTTHSPLLLD 303
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 3-84 5.76e-05

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 44.17  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   3 IEKIKIENYKVYRN-TEIRNLSN-FSVFLGANGAGKSTLFDVFGF-LSDALKanvktalNKRGGYREVYSRDGEGP---- 75
Cdd:cd03272     1 IKQVIIQGFKSYKDqTVIEPFSPkHNVVVGRNGSGKSNFFAAIRFvLSDEYT-------HLREEQRQALLHEGSGPsvms 73


                  ....*....
gi 2468166099  76 ILFEIKFRN 84
Cdd:cd03272    74 AYVEIIFDN 82
retron_eff_Eco8 NF038234
retron Eco8 family effector endonuclease; This ATPase, found as the effector protein partner ...
 1-345 8.28e-05

retron Eco8 family effector endonuclease; This ATPase, found as the effector protein partner next to a reverse transcriptase in Eco8 type retron systems, is a predicted OLD family endonuclease.


Pssm-ID: 468422 [Multi-domain]  Cd Length: 679  Bit Score: 44.63  E-value: 8.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   1 MKIEKIKIENYKVYRNTEIRNLSNFSVFLGANGAGKSTLFDVFGFLSDAL--KANVKTALNKRggyrevYSRDGEgpilf 78
Cdd:NF038234    1 MPIKSIKIKNLLSFDDLEIDDLKDINCIIGKNNVGKSNLLKALKFFYKNLtgEKVIPPILDSN------YSSKGE----- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  79 eIKFRNDkiegetqplityrleigfenglpiiTTEILSYRRGGYGR----PYRFLDFHRGEGTAIINEDEYSSSSSST-F 153
Cdd:NF038234   70 -ISITYD-------------------------TSRLKRIARSNTNKneyfKHIYNPFFKKIIFSFKKYLDKNTLFTLTlK 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 154 QDRREQQTLDSPDILAIKGLGQFQKFKAISSFRRLLDDW-----YVSNFQIQEARNVEDVGFSEHLSTSGNNlaqvtryi 228
Cdd:NF038234  124 IYKNGSISWSIKDYETRKLLSYLFPFFFIESRHINLYDWdelwdLIGRLKKFNLSGLSNEEIIDFFDEKISS-------- 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 229 weNHRNVFNTILEKFRKRVPgVENVIAEETQDGRIVLKFKDNSFQ-DPFVARFVSDGT-----IKMFAYLVLL--NDPVK 300
Cdd:NF038234  196 --NYSNSYKDIIEEIKKSIE-TKPYSYKEKILSYIKLGLGGYKFNiDGEELKTQSDGTnsfnfIKLFLNLLITlsRREYI 272

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2468166099 301 HPLLCVEEPENYLHPELLPELAEE-FREYADKGG-------QVFISTHSPDFV 345
Cdd:NF038234  273 TPFIFIDEPELGLHPKLNEQLINEiYESYSFKKKdnktpypKIILATHSPRII 325
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1-41 3.58e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 3.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2468166099   1 MKIEKIKIENYKVYRNTEIRNLSNFSVFLGANGAGKSTLFD 41
Cdd:PRK03918    1 MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILE 41
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-101 1.54e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099    3 IEKIKIENYKVYR-NTEIRNLSNFSVFLGANGAGKSTLFDVFGFL-----SDALKANVKTALnkrggyreVYSRDGEGPI 76
Cdd:TIGR02169    2 IERIELENFKSFGkKKVIPFSKGFTVISGPNGSGKSNIGDAILFAlglssSKAMRAERLSDL--------ISNGKNGQSG 73

                           90       100
                   ....*....|....*....|....*...
gi 2468166099   77 LF---EIKFRNDKIEGETQPLITYRLEI 101
Cdd:TIGR02169   74 NEayvTVTFKNDDGKFPDELEVVRRLKV 101
 
Name Accession Description Interval E-value
COG4637 COG4637
Predicted ATPase [General function prediction only];
2-394 6.80e-122

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 357.70  E-value: 6.80e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   2 KIEKIKIENYKVYRNTEIRnLSNFSVFLGANGAGKSTLFDVFGFLSDALKANVKTALNKRGGYREVYSRDGE---GPILF 78
Cdd:COG4637     1 MITRIRIKNFKSLRDLELP-LGPLTVLIGANGSGKSNLLDALRFLSDAARGGLQDALARRGGLEELLWRGPRtitEPIRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  79 EIKFRNdkiegETQPLITYRLEIGFE--NGLPIITTEILSYRRGGYGRPyrFLDFhRGEGTAIINEDeysssssstfqdr 156
Cdd:COG4637    80 ELEFAE-----EDERDLRYELELGLPepGGRPEVKEERLWLKRGSGGRP--FLDF-RPKGRAVGGEP------------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 157 reqQTLDSPDILaIKGLGQFQKFKAISSFRRLLDDWYVSNFQIQEARNVEDVGFSEHLSTSGNNLAQVTRYIWENHRNVF 236
Cdd:COG4637   139 ---ERLDSPESL-LSQLGDPERFPELRALREALRSWRFYDFHPAPLRQPQPAGRTPVLAPDGSNLAAVLATLRETHPERF 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 237 NTILEKFRKRVPGVENVIAEETQDGRIVLKFKDNSFQDPFVARFVSDGTIKMFAYLVLLNDPVKHPLLCVEEPENYLHPE 316
Cdd:COG4637   215 ERILEALRDAFPGFEDIEVEPDEDGRVLLEFREKGLDRPFPARELSDGTLRFLALLAALLSPRPPPLLCIEEPENGLHPD 294

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468166099 317 LLPELAEEFREYADKgGQVFISTHSPDFVNALQPDELFWLQK-SNGATTIRKASEDATIKALyaNGDKLGWLWREGYLK 394
Cdd:COG4637   295 LLPALAELLREASER-TQVIVTTHSPALLDALEPEEVLVLEReDDGETRIRRLSDLELPEWL--EGYSLGELWARGLLG 370
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 25-346 1.92e-29

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 115.95  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  25 FSVFLGANGAGKSTLFDVFGFLSDALKANVKTALNKRGGY------REVYSRDGEGPILFEI-KFRNDKIegetqplity 97
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGgiggipSLLNGIDPKEPIEFEIsEFLEDGV---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  98 RLEIGFENGLPIITTEILSYRRGGYGRPYRFLDFHRGEGTAIINEDEysssSSSTFQDRREQQTLDSPDILAIKGLGQFQ 177
Cdd:pfam13304  71 RYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEE----LRLGLDVEERIELSLSELSDLISGLLLLS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 178 KFKAISSFRRLLDDWYVSNFQIQEARNvedvgfseHLSTSGNNLAQVTRYIWENHRNVFNTILEKFRKRVPGVENViaee 257
Cdd:pfam13304 147 IISPLSFLLLLDEGLLLEDWAVLDLAA--------DLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDD---- 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 258 tQDGRIVLKFKDNSFQDPFVARFVSDGTIKMFAYLV-LLNDPVKHPLLCVEEPENYLHPELLPELAEEFREYADKGGQVF 336
Cdd:pfam13304 215 -RLRERGLILLENGGGGELPAFELSDGTKRLLALLAaLLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLI 293

                         330
                  ....*....|
gi 2468166099 337 ISTHSPDFVN 346
Cdd:pfam13304 294 LTTHSPLLLD 303
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
3-381 4.53e-23

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 98.58  E-value: 4.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   3 IEKIKIENYKVYRN-------TEIRNLSNFSVFLGANGAGKSTLFDVFGFLSDAlkanVKTALNKRGGYREVYSRDGEG- 74
Cdd:COG1106     2 LISFSIENFRSFKDeltlsmvASGLRLLRVNLIYGANASGKSNLLEALYFLRNL----VLNSSQPGDKLVEPFLLDSESk 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  75 --PILFEIKFRNDKIegetqpLITYRLEIGFENglpiITTEILSyrrggygrpyrFLDFHRGEGTAIINEDEysssssst 152
Cdd:COG1106    78 nePSEFEILFLLDGV------RYEYGFELDKER----IISEWLY-----------FLSTAAQLNVPLLSPLY-------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 153 fqdrreqqtldspdilaikglgqfqkfkaissfrrlldDWYVSNFQIqearNVEDVGFSEHLSTSgnnlaqvtryiwENH 232
Cdd:COG1106   129 --------------------------------------DWFDNNISL----DTSSDGLTLLLKED------------ESL 154

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 233 RNVFNTILEKFrkrVPGVENVIAEETQDGRIV---LKFKDNSFQDPFVARFVSDGTIKMFAYLVLLNDPVKHP-LLCVEE 308
Cdd:COG1106   155 KEELLELLKIA---DPGIEDIEVEEEEIEDLVerkLIFKHKGGNVPLPLSEESDGTKRLLALAGALLDALAKGgVLLIDE 231

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 309 PENYLHPELLPELAEEF-REYADKGGQVFISTHSPD----FVNALQPDELFWLQKS-NGATTIR-----KASEDATIKAL 377
Cdd:COG1106   232 IEASLHPSLLRKLLKLFlDLANKNNAQLIFTTHSTElldaFLELLRRDQIWFVEKDkDGASELYsledfKVRKDENLEKG 311


                  ....
gi 2468166099 378 YANG 381
Cdd:COG1106   312 YLQG 315
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
 1-367 1.89e-20

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 91.60  E-value: 1.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   1 MKIEKIKIENYKVYRNTEIRNLSNFSVFLGANGAGKSTLFDvfgflsdalkanvktALNkrggyrevysrdgegpILFEi 80
Cdd:COG3593     1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILE---------------ALR----------------LLLG- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  81 kfrndkiegetqplityrleigfenglpiitteilsyrrGGYGRPYRFLDFHRGEGTAIInedeysssssstfqdrreqq 160
Cdd:COG3593    49 ---------------------------------------PSSSRKFDEEDFYLGDDPDLP-------------------- 69

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 161 tldspdILAIKGlgqfqKFKAIssFRRLLDDWYVSNFQIQEARNVEDvgFSEHLSTSGNNLAQVTRYIWENHRNVFNTIL 240
Cdd:COG3593    70 ------EIEIEL-----TFGSL--LSRLLRLLLKEEDKEELEEALEE--LNEELKEALKALNELLSEYLKELLDGLDLEL 134

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 241 EKfrkrvpgveNVIAEETQDGRIVLKFKDNsfqDPFVARFVSDGT-----IKMFAYLVLLNDPVKHPLLCVEEPENYLHP 315
Cdd:COG3593   135 EL---------SLDELEDLLKSLSLRIEDG---KELPLDRLGSGFqrlilLALLSALAELKRAPANPILLIEEPEAHLHP 202

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2468166099 316 ELLPELAEEFREYADKGGQVFISTHSPDFVNALQPDELFWLQKSNGATTIRK 367
Cdd:COG3593   203 QAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPLENIRRLRRDSGGTTSTK 254
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 1-345 1.24e-18

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


Pssm-ID: 433011 [Multi-domain]  Cd Length: 392  Bit Score: 86.88  E-value: 1.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   1 MKIEKIKIENYKVYRNTEIRNLSNFSVFLGANGAGKSTLFDVFG-FLSDALKANVKTALN---------KRGGYREVYSR 70
Cdd:pfam13175   1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDiFLNNKEKFFEDDFLVlylkdvikiDKEDLNIFENI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  71 DGEGPILFEIKFRNDKIE-----------GETQPLITYRLEIGFENGLPIITTEILSYRRGGYGRPYRFLDFHRGEGTAI 139
Cdd:pfam13175  81 SFSIDIEIDVEFLLILFGyleikkkylclASKGKAKEYEKTLHPKGANKADLLLELKISDLKKYLKQFKIYIYNNYYLDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 140 INEDEYSSSSSSTFQDRREQQTLDSPDILA----IKGLGQFQKFKAISSFRRLLDDWYVSNFqIQEARNVEDvGFSEHls 215
Cdd:pfam13175 161 KKNVFDKKSKYELPSLKEEFLNSEKEEIKVdkedLKKLINELEKSINYHENVLENLQIKKLL-ISADRNASD-EDSEK-- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 216 tSGNNLAQVTRYIWENHRNVFNTILEK---FRKRVPGVENVIAEETQD-----GRIVLKFKDNSFQDPFVARFVSDGTI- 286
Cdd:pfam13175 237 -INSLLGALKQRIFEEALQEELELTEKlkeTQNKLKEIDKTLAEELKNilfkkIDKLKDFGYPPFLNPEIEIKKDDEDLp 315

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468166099 287 --------KMFAYLVLL---------NDPVKHPLLCVEEPENYLHPELLPELAEEFREYA-DKGGQVFISTHSPDFV 345
Cdd:pfam13175 316 lnkngsgvQRLILLIFFiaeaerkedEIEEKNVILAIEEPEAHLHPQAQRVLIKLLKELAnDNKTQVIITTHSPHII 392
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
1-360 5.09e-13

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 68.87  E-value: 5.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   1 MKIEKIKIENYKVYRNTEI--RNLSNFSVFLGANGAGKSTLfdvfgflsdaLKAnVKTALNkrggyrevysrdGEGPILF 78
Cdd:COG3950     1 MRIKSLTIENFRGFEDLEIdfDNPPRLTVLVGENGSGKTTL----------LEA-IALALS------------GLLSRLD 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  79 EIKFRNDKIEGETqplityrleigFENGLPIITteilsyrrgGYGrPYRFLdfhrgegtaiiNEDEYSSSSSSTFQDRRE 158
Cdd:COG3950    58 DVKFRKLLIRNGE-----------FGDSAKLIL---------YYG-TSRLL-----------LDGPLKKLERLKEEYFSR 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 159 QQTLDSpdilaikglgqfqKFKAISSFRRLLdDWYVSNFQIQEARNVEDvgfsehlstsgnnlaqvtryiWENHRNVFNT 238
Cdd:COG3950   106 LDGYDS-------------LLDEDSNLREFL-EWLREYLEDLENKLSDE---------------------LDEKLEAVRE 150

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 239 ILEKFrkrVPGVENVIAEETQDGRIVLKFKDNSFqdPFVArfVSDG---TIKMFAYLVL--------LNDPVKHP-LLCV 306
Cdd:COG3950   151 ALNKL---LPDFKDIRIDRDPGRLVILDKNGEEL--PLNQ--LSDGersLLALVGDLARrlaelnpaLENPLEGEgIVLI 223

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2468166099 307 EEPENYLHP----ELLPELAEEFreyadKGGQVFISTHSPDFVNALQPDELFWLQKSN 360
Cdd:COG3950   224 DEIDLHLHPkwqrRILPDLRKIF-----PNIQFIVTTHSPLILSSLEDEEVIVLERDE 276
COG4938 COG4938
Predicted ATPase [General function prediction only];
234-373 3.51e-10

Predicted ATPase [General function prediction only];


Pssm-ID: 443965 [Multi-domain]  Cd Length: 277  Bit Score: 60.37  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 234 NVFNTILEKFRKRVPGVENVIAEeTQDGRIVLKFKDNSFQDPFVarFVSDGtIKMFAYLV--LLNDPVKHPLLCVEEPEN 311
Cdd:COG4938    98 ELLEQVEEWLEKIFPGKVEVDAS-SDLVRLVFRPSGNGKRIPLS--NVGSG-VSELLPILlaLLSAAKPGSLLIIEEPEA 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468166099 312 YLHPELLPELAEEFREYADKGGQVFISTHSPDFVNALQ----------PDE--LFWLQKSNGATTIRKASEDAT 373
Cdd:COG4938   174 HLHPKAQSALAELLAELANSGVQVIIETHSDYILNGLRnlikegklldPDDvaVYFFERDGGGSELRRIEIDEN 247
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-62 5.04e-08

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.77  E-value: 5.04e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468166099   1 MKIEKIKIENYKVYRNTEIRNLSNFSVFLGANGAGKSTLFD-VFGFLSDALKANVKTALNKRG 62
Cdd:COG4717     1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAfIRAMLLERLEKEADELFKPQG 63
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
2-95 3.43e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 47.31  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   2 KIEKIKIENYKVYRNTEIRNLS-NFSVFLGANGAGKSTLFDVFGFlsdALKANVKTALNKRGGYREVYSRDGEGPILFEI 80
Cdd:COG0419     1 KLLRLRLENFRSYRDTETIDFDdGLNLIVGPNGAGKSTILEAIRY---ALYGKARSRSKLRSDLINVGSEEASVELEFEH 77

                          90
                  ....*....|....*...
gi 2468166099  81 KFRNDKIE---GETQPLI 95
Cdd:COG0419    78 GGKRYRIErrqGEFAEFL 95
AAA_23 pfam13476
AAA domain;
6-91 3.68e-05

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 44.02  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   6 IKIENYKVYRNTEIRNLSNFSVFLGANGAGKSTLFD-----VFGFLSDALKANVKTAL---------NKRGGYREVYSRD 71
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDaiklaLYGKTSRLKRKSGGGFVkgdirigleGKGKAYVEITFEN 80

                          90       100
                  ....*....|....*....|
gi 2468166099  72 GEGPILFEIKFRNDKIEGET 91
Cdd:pfam13476  81 NDGRYTYAIERSRELSKKKG 100
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 2-47 3.95e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.12  E-value: 3.95e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2468166099    2 KIEKIKIENYKVYRNTEIRNLS-NFSVFLGANGAGKSTLFD----VFGFLS 47
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILPFSpGFTAIVGPNGSGKSNILDailfVLGERS 51
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 3-84 5.76e-05

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 44.17  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   3 IEKIKIENYKVYRN-TEIRNLSN-FSVFLGANGAGKSTLFDVFGF-LSDALKanvktalNKRGGYREVYSRDGEGP---- 75
Cdd:cd03272     1 IKQVIIQGFKSYKDqTVIEPFSPkHNVVVGRNGSGKSNFFAAIRFvLSDEYT-------HLREEQRQALLHEGSGPsvms 73


                  ....*....
gi 2468166099  76 ILFEIKFRN 84
Cdd:cd03272    74 AYVEIIFDN 82
retron_eff_Eco8 NF038234
retron Eco8 family effector endonuclease; This ATPase, found as the effector protein partner ...
 1-345 8.28e-05

retron Eco8 family effector endonuclease; This ATPase, found as the effector protein partner next to a reverse transcriptase in Eco8 type retron systems, is a predicted OLD family endonuclease.


Pssm-ID: 468422 [Multi-domain]  Cd Length: 679  Bit Score: 44.63  E-value: 8.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   1 MKIEKIKIENYKVYRNTEIRNLSNFSVFLGANGAGKSTLFDVFGFLSDAL--KANVKTALNKRggyrevYSRDGEgpilf 78
Cdd:NF038234    1 MPIKSIKIKNLLSFDDLEIDDLKDINCIIGKNNVGKSNLLKALKFFYKNLtgEKVIPPILDSN------YSSKGE----- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099  79 eIKFRNDkiegetqplityrleigfenglpiiTTEILSYRRGGYGR----PYRFLDFHRGEGTAIINEDEYSSSSSST-F 153
Cdd:NF038234   70 -ISITYD-------------------------TSRLKRIARSNTNKneyfKHIYNPFFKKIIFSFKKYLDKNTLFTLTlK 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 154 QDRREQQTLDSPDILAIKGLGQFQKFKAISSFRRLLDDW-----YVSNFQIQEARNVEDVGFSEHLSTSGNNlaqvtryi 228
Cdd:NF038234  124 IYKNGSISWSIKDYETRKLLSYLFPFFFIESRHINLYDWdelwdLIGRLKKFNLSGLSNEEIIDFFDEKISS-------- 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099 229 weNHRNVFNTILEKFRKRVPgVENVIAEETQDGRIVLKFKDNSFQ-DPFVARFVSDGT-----IKMFAYLVLL--NDPVK 300
Cdd:NF038234  196 --NYSNSYKDIIEEIKKSIE-TKPYSYKEKILSYIKLGLGGYKFNiDGEELKTQSDGTnsfnfIKLFLNLLITlsRREYI 272

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2468166099 301 HPLLCVEEPENYLHPELLPELAEE-FREYADKGG-------QVFISTHSPDFV 345
Cdd:NF038234  273 TPFIFIDEPELGLHPKLNEQLINEiYESYSFKKKdnktpypKIILATHSPRII 325
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
 3-84 8.55e-05

The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.


Pssm-ID: 213206 [Multi-domain]  Cd Length: 178  Bit Score: 43.07  E-value: 8.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   3 IEKIKIENYKVYRNTEIRNLSN-FSVFLGANGAGKSTLFD----VFGFLSDALKANVKTALNKRGGYREVYSRDgegpil 77
Cdd:cd03239     1 IKQITLKNFKSYRDETVVGGSNsFNAIVGPNGSGKSNIVDaicfVLGGKAAKLRRGSLLFLAGGGVKAGINSAS------ 74


                  ....*..
gi 2468166099  78 FEIKFRN 84
Cdd:cd03239    75 VEITFDK 81
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1-41 3.58e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 3.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2468166099   1 MKIEKIKIENYKVYRNTEIRNLSNFSVFLGANGAGKSTLFD 41
Cdd:PRK03918    1 MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILE 41
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 1-98 3.69e-04

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 41.49  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099   1 MKIEKIKIENYKVYRNTEI---RNLSNFSVFL--GANGAGKSTLFDVFGFlsdALKANVKTALNKRGGYREVYSRDGEGP 75
Cdd:cd03279     1 MKPLKLELKNFGPFREEQVidfTGLDNNGLFLicGPTGAGKSTILDAITY---ALYGKTPRYGRQENLRSVFAPGEDTAE 77

                          90       100
                  ....*....|....*....|...
gi 2468166099  76 ILFEIKFRNDKIEGETQPLITYR 98
Cdd:cd03279    78 VSFTFQLGGKKYRVERSRGLDYD 100
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1-41 3.97e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 3.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2468166099   1 MKIEKIKIENYKVYRNTEIRNLSNFSVFLGANGAGKSTLFD 41
Cdd:PRK02224    1 MRFDRVRLENFKCYADADLRLEDGVTVIHGVNGSGKSSLLE 41
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 6-40 4.83e-04

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 40.46  E-value: 4.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2468166099   6 IKIEN-YKVYRNTE-IRNLSnFSV-------FLGANGAGKSTLF 40
Cdd:cd03230     1 IEVRNlSKRYGKKTaLDDIS-LTVekgeiygLLGPNGAGKTTLI 43
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
2-49 9.63e-04

Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 41.26  E-value: 9.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2468166099   2 KIEKI-KIENYKVYRN-TEIRNLSNFSVFLGANGAGKSTLFDVFGFLSDA 49
Cdd:COG4694     1 MITKIkKLKNVGAFKDfGWLAFFKKLNLIYGENGSGKSTLSRILRSLELG 50
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
 3-45 9.78e-04

ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213241 [Multi-domain]  Cd Length: 212  Bit Score: 40.36  E-value: 9.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2468166099   3 IEKIKIENYKVYRNT-EIRNL-SNFSVFLGANGAGKSTLFD----VFGF 45
Cdd:cd03274     3 ITKLVLENFKSYAGEqVIGPFhKSFSAIVGPNGSGKSNVIDsmlfVFGF 51
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-101 1.54e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468166099    3 IEKIKIENYKVYR-NTEIRNLSNFSVFLGANGAGKSTLFDVFGFL-----SDALKANVKTALnkrggyreVYSRDGEGPI 76
Cdd:TIGR02169    2 IERIELENFKSFGkKKVIPFSKGFTVISGPNGSGKSNIGDAILFAlglssSKAMRAERLSDL--------ISNGKNGQSG 73

                           90       100
                   ....*....|....*....|....*...
gi 2468166099   77 LF---EIKFRNDKIEGETQPLITYRLEI 101
Cdd:TIGR02169   74 NEayvTVTFKNDDGKFPDELEVVRRLKV 101
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 292-358 1.54e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 38.77  E-value: 1.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468166099 292 LVLLNDPvkhPLLCVEEPENYLHPELLPELAEEFREYADKGGQVFISTHSPDFVNALqPDELFWLQK 358
Cdd:cd00267    93 RALLLNP---DLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELA-ADRVIVLKD 155
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 3-45 2.36e-03

ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213242 [Multi-domain]  Cd Length: 247  Bit Score: 39.48  E-value: 2.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2468166099   3 IEKIKIENYKVYRNTE-IRNLSNFSVFLGANGAGKSTLFDVFGF 45
Cdd:cd03275     1 LKRLELENFKSYKGRHvIGPFDRFTCIIGPNGSGKSNLMDAISF 44
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
6-40 3.42e-03

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 38.89  E-value: 3.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2468166099   6 IKIEN-YKVYRNTE-IRNLSnFSV-------FLGANGAGKSTLF 40
Cdd:COG1131     1 IEVRGlTKRYGDKTaLDGVS-LTVepgeifgLLGPNGAGKTTTI 43
RecF COG1195
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
2-39 3.66e-03

Recombinational DNA repair ATPase RecF [Replication, recombination and repair];


Pssm-ID: 440808 [Multi-domain]  Cd Length: 352  Bit Score: 38.98  E-value: 3.66e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2468166099   2 KIEKIKIENYKVYRNTEIRNLSNFSVFLGANGAGKSTL 39
Cdd:COG1195     1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNL 38
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
 1-46 4.07e-03

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213240 [Multi-domain]  Cd Length: 251  Bit Score: 38.43  E-value: 4.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2468166099   1 MKIEKIKIENYKVY-RNTEIRNLS-NFSVFLGANGAGKSTLFDVFGFL 46
Cdd:cd03273     1 MHIKEIILDGFKSYaTRTVISGFDpQFNAITGLNGSGKSNILDAICFV 48
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 3-41 4.66e-03

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 37.97  E-value: 4.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2468166099   3 IEKIKIENYK-VYRNTEIRNLSNFSVFLGANGAGKSTLFD 41
Cdd:cd03240     1 IDKLSIRNIRsFHERSEIEFFSPLTLIVGQNGAGKTTIIE 40
recF PRK00064
recombination protein F; Reviewed
 1-39 5.23e-03

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 38.60  E-value: 5.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2468166099   1 MKIEKIKIENYKVYRNTEIRNLSNFSVFLGANGAGKSTL 39
Cdd:PRK00064    1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNL 39
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
 3-39 6.83e-03

ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213244 [Multi-domain]  Cd Length: 213  Bit Score: 37.58  E-value: 6.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2468166099   3 IEKIKIENYKVYRNTEIRNLSNFSVFLGANGAGKSTL 39
Cdd:cd03277     3 IVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSI 39
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 6-40 7.57e-03

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 37.76  E-value: 7.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2468166099   6 IKIEN-YKVYRNTEIrnLSNFSV---------FLGANGAGKSTLF 40
Cdd:COG4604     2 IEIKNvSKRYGGKVV--LDDVSLtipkggitaLIGPNGAGKSTLL 44
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 6-40 9.12e-03

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 37.48  E-value: 9.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2468166099   6 IKIEN-YKVYRNTE---IRNLSnFSV-------FLGANGAGKSTLF 40
Cdd:cd03263     1 LQIRNlTKTYKKGTkpaVDDLS-LNVykgeifgLLGHNGAGKTTTL 45
 
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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