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Conserved domains on  [gi|2449638158|ref|WP_274668908|]
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ATP-dependent endonuclease [Demequina sp. B12]

Protein Classification

ATP-dependent nuclease( domain architecture ID 11466458)

ATP-dependent nuclease is an OLD (overcoming lysogenization defect) family ATP-dependent nuclease which may have DNAse as well as RNAse activity; similar to Bacillus cereus endonuclease GajA and bacteriophage P2 OLD nuclease, which displays exonuclease activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
2-439 5.09e-38

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: 143.99  E-value: 5.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158   2 TIENFRGVKALDWTLpmDQRLVALIGPGDSGKSTILEAVHWLLGDRWSIPVSDTDFFGVDLSQTIRIQAVLVglpdalkr 81
Cdd:COG3593     7 KIKNFRSIKDLSIEL--SDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELT-------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158  82 dtaFGLWLSGVDSTGALHQDPDDTHTpaliAVLTIDDSLEPHwsvervdgqsqlltsaqrrhfstfkvddrtdaqlrwsr 161
Cdd:COG3593    77 ---FGSLLSRLLRLLLKEEDKEELEE----ALEELNEELKEA-------------------------------------- 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 162 asalgrmsqrdgadrdalaaasraaqqaivdhesspLSDLAEKVQKRANMIGGGRFSDIKPGLDTsRSSMGAGLALY--- 238
Cdd:COG3593   112 ------------------------------------LKALNELLSEYLKELLDGLDLELELSLDE-LEDLLKSLSLRied 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 239 EGAIPLASFGLGSRRLASLAV-QQLA----SGERSVAVIDELEEGLEPHRAVRLLQYLRDDDAYS-QVLVTTHSPVVVEQ 312
Cdd:COG3593   155 GKELPLDRLGSGFQRLILLALlSALAelkrAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPnQVIITTHSPHLLSE 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 313 AKTENLATVQSDSGVVTVTTLSGSTA-----VLQRLRRSRPSSLLARRVVVAEGKTEHGVLLACLDDWDEARSSvglsts 387
Cdd:COG3593   235 VPLENIRRLRRDSGGTTSTKLIDLDDedlrkLLRYLGVTRSELLFARKVILVEGDTEVILLPALARKLGKDLDE------ 308
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2449638158 388 agEGVAIQDAQGGSEVAPKASALHSLGYAVAGFMDADDPSVDVAVQEALDAG 439
Cdd:COG3593   309 --EGISIIPVGGKSNLKPLAKLLKALGIPVAVLTDGDEAGKAETIEKLKEKG 358
 
Name Accession Description Interval E-value
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
2-439 5.09e-38

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: 143.99  E-value: 5.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158   2 TIENFRGVKALDWTLpmDQRLVALIGPGDSGKSTILEAVHWLLGDRWSIPVSDTDFFGVDLSQTIRIQAVLVglpdalkr 81
Cdd:COG3593     7 KIKNFRSIKDLSIEL--SDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELT-------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158  82 dtaFGLWLSGVDSTGALHQDPDDTHTpaliAVLTIDDSLEPHwsvervdgqsqlltsaqrrhfstfkvddrtdaqlrwsr 161
Cdd:COG3593    77 ---FGSLLSRLLRLLLKEEDKEELEE----ALEELNEELKEA-------------------------------------- 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 162 asalgrmsqrdgadrdalaaasraaqqaivdhesspLSDLAEKVQKRANMIGGGRFSDIKPGLDTsRSSMGAGLALY--- 238
Cdd:COG3593   112 ------------------------------------LKALNELLSEYLKELLDGLDLELELSLDE-LEDLLKSLSLRied 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 239 EGAIPLASFGLGSRRLASLAV-QQLA----SGERSVAVIDELEEGLEPHRAVRLLQYLRDDDAYS-QVLVTTHSPVVVEQ 312
Cdd:COG3593   155 GKELPLDRLGSGFQRLILLALlSALAelkrAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPnQVIITTHSPHLLSE 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 313 AKTENLATVQSDSGVVTVTTLSGSTA-----VLQRLRRSRPSSLLARRVVVAEGKTEHGVLLACLDDWDEARSSvglsts 387
Cdd:COG3593   235 VPLENIRRLRRDSGGTTSTKLIDLDDedlrkLLRYLGVTRSELLFARKVILVEGDTEVILLPALARKLGKDLDE------ 308
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2449638158 388 agEGVAIQDAQGGSEVAPKASALHSLGYAVAGFMDADDPSVDVAVQEALDAG 439
Cdd:COG3593   309 --EGISIIPVGGKSNLKPLAKLLKALGIPVAVLTDGDEAGKAETIEKLKEKG 358
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
22-311 1.49e-16

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: 80.51  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158  22 LVALIGPGDSGKSTILEAVHWLLG-DRWSIPVSDTDFFGVDLSQTIRIQAVLVGLPDALKRDTAFGL----WLSGVDSTG 96
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADfDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEdgvrYRYGLDLER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158  97 ALHQDPDDTHTPALIAVLTIDDSLEPHW--SVERVDGQSQLLTSAQRRHFSTFKVDDRTDAQLRWSRASALGRMSQRDGA 174
Cdd:pfam13304  81 EDVEEKLSSKPTLLEKRLLLREDSEEREpkFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 175 DRDALAAASRAAQQAIVDHESSPLSDLAEKVQKRANMIGGGRFSDIKPGLDTSRSSMGAGLALYE----GAIPLASFGLG 250
Cdd:pfam13304 161 LLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLEngggGELPAFELSDG 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2449638158 251 SRRLASLAVQQL-ASGERSVAVIDELEEGLEPHRAVRLLQYLRDDDAY-SQVLVTTHSPVVVE 311
Cdd:pfam13304 241 TKRLLALLAALLsALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNgAQLILTTHSPLLLD 303
recF PRK00064
recombination protein F; Reviewed
2-43 2.33e-03

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 40.53  E-value: 2.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2449638158   2 TIENFRGVKALDWTLpmDQRLVALIGPGDSGKSTILEAVHWL 43
Cdd:PRK00064    7 SLTDFRNYEELDLEL--SPGVNVLVGENGQGKTNLLEAIYLL 46
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
15-47 2.90e-03

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. 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: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 39.37  E-value: 2.90e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2449638158  15 TLPMDQRLVALIGPGDSGKSTILEAVHWLLGDR 47
Cdd:cd03278    17 TIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQ 49
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
15-47 3.80e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 3.80e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2449638158   15 TLPMDQRLVALIGPGDSGKSTILEAVHWLLGDR 47
Cdd:TIGR02168   18 TINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQ 50
 
Name Accession Description Interval E-value
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
2-439 5.09e-38

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: 143.99  E-value: 5.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158   2 TIENFRGVKALDWTLpmDQRLVALIGPGDSGKSTILEAVHWLLGDRWSIPVSDTDFFGVDLSQTIRIQAVLVglpdalkr 81
Cdd:COG3593     7 KIKNFRSIKDLSIEL--SDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELT-------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158  82 dtaFGLWLSGVDSTGALHQDPDDTHTpaliAVLTIDDSLEPHwsvervdgqsqlltsaqrrhfstfkvddrtdaqlrwsr 161
Cdd:COG3593    77 ---FGSLLSRLLRLLLKEEDKEELEE----ALEELNEELKEA-------------------------------------- 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 162 asalgrmsqrdgadrdalaaasraaqqaivdhesspLSDLAEKVQKRANMIGGGRFSDIKPGLDTsRSSMGAGLALY--- 238
Cdd:COG3593   112 ------------------------------------LKALNELLSEYLKELLDGLDLELELSLDE-LEDLLKSLSLRied 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 239 EGAIPLASFGLGSRRLASLAV-QQLA----SGERSVAVIDELEEGLEPHRAVRLLQYLRDDDAYS-QVLVTTHSPVVVEQ 312
Cdd:COG3593   155 GKELPLDRLGSGFQRLILLALlSALAelkrAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPnQVIITTHSPHLLSE 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 313 AKTENLATVQSDSGVVTVTTLSGSTA-----VLQRLRRSRPSSLLARRVVVAEGKTEHGVLLACLDDWDEARSSvglsts 387
Cdd:COG3593   235 VPLENIRRLRRDSGGTTSTKLIDLDDedlrkLLRYLGVTRSELLFARKVILVEGDTEVILLPALARKLGKDLDE------ 308
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2449638158 388 agEGVAIQDAQGGSEVAPKASALHSLGYAVAGFMDADDPSVDVAVQEALDAG 439
Cdd:COG3593   309 --EGISIIPVGGKSNLKPLAKLLKALGIPVAVLTDGDEAGKAETIEKLKEKG 358
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
22-311 1.49e-16

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: 80.51  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158  22 LVALIGPGDSGKSTILEAVHWLLG-DRWSIPVSDTDFFGVDLSQTIRIQAVLVGLPDALKRDTAFGL----WLSGVDSTG 96
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADfDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEdgvrYRYGLDLER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158  97 ALHQDPDDTHTPALIAVLTIDDSLEPHW--SVERVDGQSQLLTSAQRRHFSTFKVDDRTDAQLRWSRASALGRMSQRDGA 174
Cdd:pfam13304  81 EDVEEKLSSKPTLLEKRLLLREDSEEREpkFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 175 DRDALAAASRAAQQAIVDHESSPLSDLAEKVQKRANMIGGGRFSDIKPGLDTSRSSMGAGLALYE----GAIPLASFGLG 250
Cdd:pfam13304 161 LLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLEngggGELPAFELSDG 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2449638158 251 SRRLASLAVQQL-ASGERSVAVIDELEEGLEPHRAVRLLQYLRDDDAY-SQVLVTTHSPVVVE 311
Cdd:pfam13304 241 TKRLLALLAALLsALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNgAQLILTTHSPLLLD 303
COG4637 COG4637
Predicted ATPase [General function prediction only];
2-334 1.25e-09

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 60.33  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158   2 TIENFRGVKALDWTLPmdqRLVALIGPGDSGKSTILEAVHWLlgdrwsipvsdTDFFGVDLSQTIR----IQAVLVGLPD 77
Cdd:COG4637     6 RIKNFKSLRDLELPLG---PLTVLIGANGSGKSNLLDALRFL-----------SDAARGGLQDALArrggLEELLWRGPR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158  78 ALKRDTAFGLWLSGVDSTG-----ALHQDPDDtHTPALIA-VLTIDDS------LEPHWSVERVDGQSQLLTSAQ----- 140
Cdd:COG4637    72 TITEPIRLELEFAEEDERDlryelELGLPEPG-GRPEVKEeRLWLKRGsggrpfLDFRPKGRAVGGEPERLDSPEsllsq 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 141 -------------RRHFSTFKVDDRTDAQLRwsRASALGRMSQ--RDGADrdalaaaSRAAQQAIVDHESSPLSDLAEKV 205
Cdd:COG4637   151 lgdperfpelralREALRSWRFYDFHPAPLR--QPQPAGRTPVlaPDGSN-------LAAVLATLRETHPERFERILEAL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 206 QKRAnmiggGRFSDIKPGLDTSRSSMgagLALYEGA----IPLASFGLGSRRLASLAVQQLASGERSVAVIDELEEGLEP 281
Cdd:COG4637   222 RDAF-----PGFEDIEVEPDEDGRVL---LEFREKGldrpFPARELSDGTLRFLALLAALLSPRPPPLLCIEEPENGLHP 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2449638158 282 HRAVRLLQYLRDDDAYSQVLVTTHSPVVVEQAKTENL-ATVQSDSGVVTVTTLS 334
Cdd:COG4637   294 DLLPALAELLREASERTQVIVTTHSPALLDALEPEEVlVLEREDDGETRIRRLS 347
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
2-318 2.65e-08

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


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 55.39  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158   2 TIENFRGVKALDWTLPMDQRLVALIGPGDSGKSTILEAVHWLLGDRWSiPVSDTDFFGVDLS--QTIRIQAVLVGLPdal 79
Cdd:COG3950     7 TIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLS-RLDDVKFRKLLIRngEFGDSAKLILYYG--- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158  80 krdtAFGLWLSGVDSTGALHQDPDDTHTPALiavltiDDSLEPHWSVERvdgqsqlLTSAQRRHFSTF--KVDDRTDAQL 157
Cdd:COG3950    83 ----TSRLLLDGPLKKLERLKEEYFSRLDGY------DSLLDEDSNLRE-------FLEWLREYLEDLenKLSDELDEKL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 158 RWSRaSALGRMsqRDGADRDALAAASRAAQQAIVDHESSPLSDLA--EKvqkraNMIgggrfsdikpgldtsrsSMGAGL 235
Cdd:COG3950   146 EAVR-EALNKL--LPDFKDIRIDRDPGRLVILDKNGEELPLNQLSdgER-----SLL-----------------ALVGDL 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 236 AlyegaiplasfglgsRRLASLAVQ-QLASGERSVAVIDELEEGLEPHRAVRLLQYLRDDDAYSQVLVTTHSPVVVEQAK 314
Cdd:COG3950   201 A---------------RRLAELNPAlENPLEGEGIVLIDEIDLHLHPKWQRRILPDLRKIFPNIQFIVTTHSPLILSSLE 265

                  ....
gi 2449638158 315 TENL 318
Cdd:COG3950   266 DEEV 269
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
2-307 1.59e-06

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


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 50.43  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158   2 TIENFRGVK---ALDWTLPMDQ--RLVALIGPGDSGKSTILEAVHWLLGdrwsiPVSDTDFFGVDLSQTIRIqavlvglp 76
Cdd:COG1106     6 SIENFRSFKdelTLSMVASGLRllRVNLIYGANASGKSNLLEALYFLRN-----LVLNSSQPGDKLVEPFLL-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158  77 dalkrdtafglwlsgvdstgalhqDPDDTHTPALIAVLTIDDSLEPHWSVERVDGQS-----QLLTSAqrrhfSTFKVDD 151
Cdd:COG1106    73 ------------------------DSESKNEPSEFEILFLLDGVRYEYGFELDKERIisewlYFLSTA-----AQLNVPL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 152 RTDAQLRWSRASALGRMSqrdgadrdalaaasraAQQAIVDHESSPLSDLAEKVQKRANM-IGGGRFSDIKPGLDTSRSS 230
Cdd:COG1106   124 LSPLYDWFDNNISLDTSS----------------DGLTLLLKEDESLKEELLELLKIADPgIEDIEVEEEEIEDLVERKL 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158 231 MgAGLALYEGAIPLASFGLGSRRLASLA---VQQLASGerSVAVIDELEEGLEPHRAVRLLQYLRDD--DAYSQVLVTTH 305
Cdd:COG1106   188 I-FKHKGGNVPLPLSEESDGTKRLLALAgalLDALAKG--GVLLIDEIEASLHPSLLRKLLKLFLDLanKNNAQLIFTTH 264

                  ..
gi 2449638158 306 SP 307
Cdd:COG1106   265 ST 266
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
1-46 9.89e-06

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: 47.98  E-value: 9.89e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2449638158   1 MTIENFRGVKalDWTLPMDQRLVALIGPGDSGKSTILEAVHWLLGD 46
Cdd:pfam13175   6 IIIKNFRCLK--DTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNN 49
AAA_23 pfam13476
AAA domain;
1-47 1.19e-05

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 46.34  E-value: 1.19e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2449638158   1 MTIENFRGVKalDWTLPMDQRLVALIGPGDSGKSTILEAVHWLLGDR 47
Cdd:pfam13476   1 LTIENFRSFR--DQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGK 45
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
2-47 2.84e-05

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 45.39  E-value: 2.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2449638158   2 TIENFRGVKALdWTLPMDQRLVALIGPGDSGKSTILEAVHWLLGDR 47
Cdd:COG0419     6 RLENFRSYRDT-ETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGK 50
COG3378 COG3378
DNA primase, phage- or plasmid-associated [Mobilome: prophages, transposons];
20-102 9.66e-04

DNA primase, phage- or plasmid-associated [Mobilome: prophages, transposons];


Pssm-ID: 442605 [Multi-domain]  Cd Length: 403  Bit Score: 41.85  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449638158  20 QRLVALIGPGDSGKSTILEAVHWLLGDRWSIPVSDTDFFGV--DLSQTIRIQAVLVG-LPDALKRDTAFGLWLSGVDSTG 96
Cdd:COG3378   143 QKFFFLYGPGGNGKSTFLNLLTALLGKDNASSASLETLTENrfDLARLKGKRLNIASeLEEGYRLDESLLKALTGGDPIT 222

                  ....*...
gi 2449638158  97 A--LHQDP 102
Cdd:COG3378   223 ArrKYKDP 230
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
3-47 1.74e-03

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: 41.50  E-value: 1.74e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2449638158    3 IENFR--GVKAldwTLPMDQRLVALIGPGDSGKSTILEAVHWLLGDR 47
Cdd:pfam02463    7 IEGFKsyAKTV---ILPFSPGFTAIVGPNGSGKSNILDAILFVLGER 50
recF PRK00064
recombination protein F; Reviewed
2-43 2.33e-03

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 40.53  E-value: 2.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2449638158   2 TIENFRGVKALDWTLpmDQRLVALIGPGDSGKSTILEAVHWL 43
Cdd:PRK00064    7 SLTDFRNYEELDLEL--SPGVNVLVGENGQGKTNLLEAIYLL 46
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
15-47 2.90e-03

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. 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: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 39.37  E-value: 2.90e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2449638158  15 TLPMDQRLVALIGPGDSGKSTILEAVHWLLGDR 47
Cdd:cd03278    17 TIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQ 49
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
15-47 3.80e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 3.80e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2449638158   15 TLPMDQRLVALIGPGDSGKSTILEAVHWLLGDR 47
Cdd:TIGR02168   18 TINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQ 50
 
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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