NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1457429881|emb|SYQ19972|]
View 

RecF/RecN/SMC domain protein [Klebsiella pneumoniae]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG4637 COG4637
Predicted ATPase [General function prediction only];
1-360 2.97e-111

Predicted ATPase [General function prediction only];


:

Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 329.20  E-value: 2.97e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881   1 MIQYIRIQNFRSVKDIVLELGPLNIVFGPNGCGKSNIYNAIHLLTAAAEGRLSGFISEEGGLENMMWSGERSPldRHPRR 80
Cdd:COG4637     1 MITRIRIKNFKSLRDLELPLGPLTVLIGANGSGKSNLLDALRFLSDAARGGLQDALARRGGLEELLWRGPRTI--TEPIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881  81 LQIACRTD---SFDYELQIGFPEKlpyptqfMLDPIVKEENIWLAGYSRRPSSRVLQRKNQAaflvdVTGEKstftESIY 157
Cdd:COG4637    79 LELEFAEEderDLRYELELGLPEP-------GGRPEVKEERLWLKRGSGGRPFLDFRPKGRA-----VGGEP----ERLD 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 158 ENESVFGQLGEPHRFPEVSRVRETLRRWRFYHEfaigRHSPLRQPAVGYRSPVLDSDGQNLAAAFQTIVEI--GAEEILH 235
Cdd:COG4637   143 SPESLLSQLGDPERFPELRALREALRSWRFYDF----HPAPLRQPQPAGRTPVLAPDGSNLAAVLATLREThpERFERIL 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 236 EILADAFPGCQFYCENEHS--RFALKMRREGIRRPLLAAEMSDGTLRFLCLAVALLSPRPPAFLAINEPENSLHRDMLPA 313
Cdd:COG4637   219 EALRDAFPGFEDIEVEPDEdgRVLLEFREKGLDRPFPARELSDGTLRFLALLAALLSPRPPPLLCIEEPENGLHPDLLPA 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1457429881 314 LARLIIEASRYSQIWLTSHSAELAELIaagAPCQRYALE-NRGGETRI 360
Cdd:COG4637   299 LAELLREASERTQVIVTTHSPALLDAL---EPEEVLVLErEDDGETRI 343
 
Name Accession Description Interval E-value
COG4637 COG4637
Predicted ATPase [General function prediction only];
1-360 2.97e-111

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 329.20  E-value: 2.97e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881   1 MIQYIRIQNFRSVKDIVLELGPLNIVFGPNGCGKSNIYNAIHLLTAAAEGRLSGFISEEGGLENMMWSGERSPldRHPRR 80
Cdd:COG4637     1 MITRIRIKNFKSLRDLELPLGPLTVLIGANGSGKSNLLDALRFLSDAARGGLQDALARRGGLEELLWRGPRTI--TEPIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881  81 LQIACRTD---SFDYELQIGFPEKlpyptqfMLDPIVKEENIWLAGYSRRPSSRVLQRKNQAaflvdVTGEKstftESIY 157
Cdd:COG4637    79 LELEFAEEderDLRYELELGLPEP-------GGRPEVKEERLWLKRGSGGRPFLDFRPKGRA-----VGGEP----ERLD 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 158 ENESVFGQLGEPHRFPEVSRVRETLRRWRFYHEfaigRHSPLRQPAVGYRSPVLDSDGQNLAAAFQTIVEI--GAEEILH 235
Cdd:COG4637   143 SPESLLSQLGDPERFPELRALREALRSWRFYDF----HPAPLRQPQPAGRTPVLAPDGSNLAAVLATLREThpERFERIL 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 236 EILADAFPGCQFYCENEHS--RFALKMRREGIRRPLLAAEMSDGTLRFLCLAVALLSPRPPAFLAINEPENSLHRDMLPA 313
Cdd:COG4637   219 EALRDAFPGFEDIEVEPDEdgRVLLEFREKGLDRPFPARELSDGTLRFLALLAALLSPRPPPLLCIEEPENGLHPDLLPA 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1457429881 314 LARLIIEASRYSQIWLTSHSAELAELIaagAPCQRYALE-NRGGETRI 360
Cdd:COG4637   299 LAELLREASERTQVIVTTHSPALLDAL---EPEEVLVLErEDDGETRI 343
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 23-336 4.82e-26

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: 105.93  E-value: 4.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881  23 LNIVFGPNGCGKSNIYNAIHLLTAAAEGRLSGFISEEGGLENMMWSGERSPLD-RHPRRLQIAC---RTDSFDYELQIG- 97
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDpKEPIEFEISEfleDGVRYRYGLDLEr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881  98 --FPEKLPYPTQFMLDPIVKEENIWLAGYSRRPSSRVLQRKNQaaflVDVTGEKSTFTESIYENESVFGQLGEPHRFPEV 175
Cdd:pfam13304  81 edVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLD----VEERIELSLSELSDLISGLLLLSIISPLSFLLL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 176 SRVRETLRRWRFYHEFAIGRHSPLRQPAVGYRSPVLDSDGqnLAAAFQTIVEIGAEEILHEILADAFpgcqFYCENEHsr 255
Cdd:pfam13304 157 LDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLAD--LNLSDLGEGIEKSLLVDDRLRERGL----ILLENGG-- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 256 falkmrregiRRPLLAAEMSDGTLRFLCLAVALLSPRPP-AFLAINEPENSLHRDMLPALARLIIEASRY-SQIWLTSHS 333
Cdd:pfam13304 229 ----------GGELPAFELSDGTKRLLALLAALLSALPKgGLLLIDEPESGLHPKLLRRLLELLKELSRNgAQLILTTHS 298


                  ...
gi 1457429881 334 AEL 336
Cdd:pfam13304 299 PLL 301
recF PRK00064
recombination protein F; Reviewed
 2-44 5.17e-06

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 47.85  E-value: 5.17e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1457429881   2 IQYIRIQNFRSVKDIVLELGP-LNIVFGPNGCGKSNIYNAIHLL 44
Cdd:PRK00064    3 LTRLSLTDFRNYEELDLELSPgVNVLVGENGQGKTNLLEAIYLL 46
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
 2-61 7.32e-06

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: 45.76  E-value: 7.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1457429881   2 IQYIRIQNFRSVKDIVLELGP--LNIVFGPNGCGKSNIYNAIHLL---TAAAEGRLSGFISEEGG 61
Cdd:cd03239     1 IKQITLKNFKSYRDETVVGGSnsFNAIVGPNGSGKSNIVDAICFVlggKAAKLRRGSLLFLAGGG 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-41 2.61e-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: 40.04  E-value: 2.61e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1457429881    5 IRIQNFRSVKD---IVLELGPLNIVfGPNGCGKSNIYNAI 41
Cdd:TIGR02168    5 LELAGFKSFADpttINFDKGITGIV-GPNGCGKSNIVDAI 43
 
Name Accession Description Interval E-value
COG4637 COG4637
Predicted ATPase [General function prediction only];
1-360 2.97e-111

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 329.20  E-value: 2.97e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881   1 MIQYIRIQNFRSVKDIVLELGPLNIVFGPNGCGKSNIYNAIHLLTAAAEGRLSGFISEEGGLENMMWSGERSPldRHPRR 80
Cdd:COG4637     1 MITRIRIKNFKSLRDLELPLGPLTVLIGANGSGKSNLLDALRFLSDAARGGLQDALARRGGLEELLWRGPRTI--TEPIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881  81 LQIACRTD---SFDYELQIGFPEKlpyptqfMLDPIVKEENIWLAGYSRRPSSRVLQRKNQAaflvdVTGEKstftESIY 157
Cdd:COG4637    79 LELEFAEEderDLRYELELGLPEP-------GGRPEVKEERLWLKRGSGGRPFLDFRPKGRA-----VGGEP----ERLD 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 158 ENESVFGQLGEPHRFPEVSRVRETLRRWRFYHEfaigRHSPLRQPAVGYRSPVLDSDGQNLAAAFQTIVEI--GAEEILH 235
Cdd:COG4637   143 SPESLLSQLGDPERFPELRALREALRSWRFYDF----HPAPLRQPQPAGRTPVLAPDGSNLAAVLATLREThpERFERIL 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 236 EILADAFPGCQFYCENEHS--RFALKMRREGIRRPLLAAEMSDGTLRFLCLAVALLSPRPPAFLAINEPENSLHRDMLPA 313
Cdd:COG4637   219 EALRDAFPGFEDIEVEPDEdgRVLLEFREKGLDRPFPARELSDGTLRFLALLAALLSPRPPPLLCIEEPENGLHPDLLPA 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1457429881 314 LARLIIEASRYSQIWLTSHSAELAELIaagAPCQRYALE-NRGGETRI 360
Cdd:COG4637   299 LAELLREASERTQVIVTTHSPALLDAL---EPEEVLVLErEDDGETRI 343
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 23-336 4.82e-26

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: 105.93  E-value: 4.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881  23 LNIVFGPNGCGKSNIYNAIHLLTAAAEGRLSGFISEEGGLENMMWSGERSPLD-RHPRRLQIAC---RTDSFDYELQIG- 97
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDpKEPIEFEISEfleDGVRYRYGLDLEr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881  98 --FPEKLPYPTQFMLDPIVKEENIWLAGYSRRPSSRVLQRKNQaaflVDVTGEKSTFTESIYENESVFGQLGEPHRFPEV 175
Cdd:pfam13304  81 edVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLD----VEERIELSLSELSDLISGLLLLSIISPLSFLLL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 176 SRVRETLRRWRFYHEFAIGRHSPLRQPAVGYRSPVLDSDGqnLAAAFQTIVEIGAEEILHEILADAFpgcqFYCENEHsr 255
Cdd:pfam13304 157 LDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLAD--LNLSDLGEGIEKSLLVDDRLRERGL----ILLENGG-- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 256 falkmrregiRRPLLAAEMSDGTLRFLCLAVALLSPRPP-AFLAINEPENSLHRDMLPALARLIIEASRY-SQIWLTSHS 333
Cdd:pfam13304 229 ----------GGELPAFELSDGTKRLLALLAALLSALPKgGLLLIDEPESGLHPKLLRRLLELLKELSRNgAQLILTTHS 298


                  ...
gi 1457429881 334 AEL 336
Cdd:pfam13304 299 PLL 301
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
1-336 1.65e-18

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


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 85.10  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881   1 MIQYIRIQNFRSVKDIV--------LELGPLNIVFGPNGCGKSNIYNAIHLLTAAAegrLSGFISEEGGLENMMWSGERS 72
Cdd:COG1106     1 MLISFSIENFRSFKDELtlsmvasgLRLLRVNLIYGANASGKSNLLEALYFLRNLV---LNSSQPGDKLVEPFLLDSESK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881  73 PldrhprrlqiacRTDSFDYELqigFPEKLPYPTQFMLDP--IVKEeniWLAgysrrpssrvlqrknqaaFLvdvtgeks 150
Cdd:COG1106    78 N------------EPSEFEILF---LLDGVRYEYGFELDKerIISE---WLY------------------FL-------- 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 151 tftesiyeneSVFGQLGEPhrfpevsrVRETLRRWrFYHEFAIgrhsplrQPAVGYRSPVLDSDgqnlaaafqtivEIGA 230
Cdd:COG1106   114 ----------STAAQLNVP--------LLSPLYDW-FDNNISL-------DTSSDGLTLLLKED------------ESLK 155

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 231 EEILhEILADAFPGCQ-FYCENEHSRFALKMR----REGIRRPLLAAEMSDGTLRFLCLAVALLSP-RPPAFLAINEPEN 304
Cdd:COG1106   156 EELL-ELLKIADPGIEdIEVEEEEIEDLVERKlifkHKGGNVPLPLSEESDGTKRLLALAGALLDAlAKGGVLLIDEIEA 234

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1457429881 305 SLHRDMLPALARLIIEAS--RYSQIWLTSHSAEL 336
Cdd:COG1106   235 SLHPSLLRKLLKLFLDLAnkNNAQLIFTTHSTEL 268
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
 2-340 2.29e-10

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: 61.17  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881   2 IQYIRIQNFRSVKDIVLELGP-LNIVFGPNGCGKSNIYNAIHLLtaaaegrlsgfiseegglenmMWSGERSPLDRHprr 80
Cdd:COG3593     3 LEKIKIKNFRSIKDLSIELSDdLTVLVGENNSGKSSILEALRLL---------------------LGPSSSRKFDEE--- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881  81 lqiacrtdsfDYelqigfpeklPYPTQFMLDPIVKEenIWLAGYSRRPSSRVLQRKNQAAFLVDVTGEKSTFTESIYE-N 159
Cdd:COG3593    59 ----------DF----------YLGDDPDLPEIEIE--LTFGSLLSRLLRLLLKEEDKEELEEALEELNEELKEALKAlN 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 160 ESVFGQLGEPHRFPEVSRVRETLRRWRFYHEFAIgrhsplrqpavgyrspvldsdgqnlaaafqtiveigaeeilheila 239
Cdd:COG3593   117 ELLSEYLKELLDGLDLELELSLDELEDLLKSLSL---------------------------------------------- 150

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 240 dafpgcqfycenehsrfalkMRREGIRRPLlaAEMSDGTLRFLCLAVALL-----SPRPPAFLAINEPENSLHRDMLPAL 314
Cdd:COG3593   151 --------------------RIEDGKELPL--DRLGSGFQRLILLALLSAlaelkRAPANPILLIEEPEAHLHPQAQRRL 208

                         330       340
                  ....*....|....*....|....*..
gi 1457429881 315 ARLIIEASRYS-QIWLTSHSAELAELI 340
Cdd:COG3593   209 LKLLKELSEKPnQVIITTHSPHLLSEV 235
AAA_23 pfam13476
AAA domain;
5-43 5.42e-10

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 58.28  E-value: 5.42e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1457429881   5 IRIQNFRSVKDIVLELG-PLNIVFGPNGCGKSNIYNAIHL 43
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSkGLTLITGPNGSGKTTILDAIKL 40
COG4938 COG4938
Predicted ATPase [General function prediction only];
2-44 2.84e-09

Predicted ATPase [General function prediction only];


Pssm-ID: 443965 [Multi-domain]  Cd Length: 277  Bit Score: 57.29  E-value: 2.84e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1457429881   2 IQYIRIQNFRSVKDIVLELGPLNIVFGPNGCGKSNIYNAIHLL 44
Cdd:COG4938     1 IKSISIKNFGPFKEAELELKPLTLLIGPNGSGKSTLIQALLLL 43
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 2-337 2.35e-08

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: 55.30  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881   2 IQYIRIQNFRSVKDIVLELGP-LNIVFGPNGCGKSNIYNAI---------HLLTAAAEGRLSGFISEEGGLENMMWSGER 71
Cdd:pfam13175   3 IKSIIIKNFRCLKDTEIDLDEdLTVLIGKNNSGKSSILEALdiflnnkekFFEDDFLVLYLKDVIKIDKEDLNIFENISF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881  72 SpldrhpRRLQIAC--RTDSFDYELQI------GFPEKLPYPTQFMLDPIVKEENIWLAGYSRRPSSRVLQRKNQAAFLV 143
Cdd:pfam13175  83 S------IDIEIDVefLLILFGYLEIKkkylclASKGKAKEYEKTLHPKGANKADLLLELKISDLKKYLKQFKIYIYNNY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 144 DVTGEKSTFTESIYENESVFGQLGEPHRFPEVSRVRETLRR-WRFYHEFAIGRHSPLRQPAVGYR-------SPVLDSDG 215
Cdd:pfam13175 157 YLDEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKlINELEKSINYHENVLENLQIKKLlisadrnASDEDSEK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 216 QN--LAAAFQTIVE------IGAEEILHEILAD---------------------------AFPGCQFYCENEHSRFALKM 260
Cdd:pfam13175 237 INslLGALKQRIFEealqeeLELTEKLKETQNKlkeidktlaeelknilfkkidklkdfgYPPFLNPEIEIKKDDEDLPL 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457429881 261 RRE--GIRRPLLAAemsdgTLRFLCLAVALLSPRPPAFLAINEPENSLHRDMLPALARLIIEASR--YSQIWLTSHSAEL 336
Cdd:pfam13175 317 NKNgsGVQRLILLI-----FFIAEAERKEDEIEEKNVILAIEEPEAHLHPQAQRVLIKLLKELANdnKTQVIITTHSPHI 391


                  .
gi 1457429881 337 A 337
Cdd:pfam13175 392 I 392
RecF COG1195
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
2-44 6.53e-07

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


Pssm-ID: 440808 [Multi-domain]  Cd Length: 352  Bit Score: 50.54  E-value: 6.53e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1457429881   2 IQYIRIQNFRSVKDIVLELGP-LNIVFGPNGCGKSNIYNAIHLL 44
Cdd:COG1195     2 LKRLSLTNFRNYESLELEFSPgINVLVGPNGQGKTNLLEAIYLL 45
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
1-55 7.87e-07

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


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 50.00  E-value: 7.87e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1457429881   1 MIQYIRIQNFRSVKDIVLELGP---LNIVFGPNGCGKSNIYNAIHLLTAAAEGRLSGF 55
Cdd:COG3950     2 RIKSLTIENFRGFEDLEIDFDNpprLTVLVGENGSGKTTLLEAIALALSGLLSRLDDV 59
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1-41 2.07e-06

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: 49.58  E-value: 2.07e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1457429881    1 MIQYIRIQNFRSVKD-IVLELGP-LNIVFGPNGCGKSNIYNAI 41
Cdd:pfam02463    1 YLKRIEIEGFKSYAKtVILPFSPgFTAIVGPNGSGKSNILDAI 43
recF PRK00064
recombination protein F; Reviewed
 2-44 5.17e-06

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 47.85  E-value: 5.17e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1457429881   2 IQYIRIQNFRSVKDIVLELGP-LNIVFGPNGCGKSNIYNAIHLL 44
Cdd:PRK00064    3 LTRLSLTDFRNYEELDLELSPgVNVLVGENGQGKTNLLEAIYLL 46
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
 2-61 7.32e-06

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: 45.76  E-value: 7.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1457429881   2 IQYIRIQNFRSVKDIVLELGP--LNIVFGPNGCGKSNIYNAIHLL---TAAAEGRLSGFISEEGG 61
Cdd:cd03239     1 IKQITLKNFKSYRDETVVGGSnsFNAIVGPNGSGKSNIVDAICFVlggKAAKLRRGSLLFLAGGG 65
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 5-41 1.14e-05

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: 45.53  E-value: 1.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1457429881   5 IRIQNFRS-VKDIVLELGP-LNIVFGPNGCGKSNIYNAI 41
Cdd:cd03278     4 LELKGFKSfADKTTIPFPPgLTAIVGPNGSGKSNIIDAI 42
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1-44 1.25e-05

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 45.77  E-value: 1.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1457429881   1 MIQYIRIQNFRSVKD-IVLELG-PLNIVFGPNGCGKSNIYNAIHLL 44
Cdd:COG0419     1 KLLRLRLENFRSYRDtETIDFDdGLNLIVGPNGAGKSTILEAIRYA 46
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
 5-43 6.65e-05

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: 43.35  E-value: 6.65e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1457429881   5 IRIQNFRSVKDIVLELGP-LNIVFGPNGCGKSNIYNAIHL 43
Cdd:cd03277     6 IKLENFVTYDETEFRPGPsLNMIIGPNGSGKSSIVCAICL 45
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
 2-45 1.34e-04

ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including 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 with 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: 213209 [Multi-domain]  Cd Length: 270  Bit Score: 43.05  E-value: 1.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1457429881   2 IQYIRIQNFRSVKDIVLELGP-LNIVFGPNGCGKSNIYNAIHLLT 45
Cdd:cd03242     1 LKSLELRNFRNYAELELEFEPgVTVLVGENAQGKTNLLEAISLLA 45
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 2-41 1.66e-04

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: 42.63  E-value: 1.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1457429881   2 IQYIRIQNFRSVKD--IVLELGP-LNIVFGPNGCGKSNIYNAI 41
Cdd:cd03272     1 IKQVIIQGFKSYKDqtVIEPFSPkHNVVVGRNGSGKSNFFAAI 43
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-41 1.75e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1457429881   2 IQYIRIQNFRSVKDIVLELGP-LNIVFGPNGCGKSNIYNAI 41
Cdd:PRK03918    3 IEELKIKNFRSHKSSVVEFDDgINLIIGQNGSGKSSILEAI 43
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
 1-41 3.66e-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: 41.13  E-value: 3.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1457429881   1 MIQYIRIQNFRSVKDIVlELGPLNIVF----GPNGCGKSNIYNAI 41
Cdd:cd03274     2 IITKLVLENFKSYAGEQ-VIGPFHKSFsaivGPNGSGKSNVIDSM 45
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 2-41 1.31e-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: 39.86  E-value: 1.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1457429881   2 IQYIRIQNFRSVKDIVLeLGPL---NIVFGPNGCGKSNIYNAI 41
Cdd:cd03275     1 LKRLELENFKSYKGRHV-IGPFdrfTCIIGPNGSGKSNLMDAI 42
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-41 2.61e-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: 40.04  E-value: 2.61e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1457429881    5 IRIQNFRSVKD---IVLELGPLNIVfGPNGCGKSNIYNAI 41
Cdd:TIGR02168    5 LELAGFKSFADpttINFDKGITGIV-GPNGCGKSNIVDAI 43
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 5-48 3.06e-03

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 38.11  E-value: 3.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1457429881   5 IRIQNFRSVK---DIVLELGPLNIVFGPNGCGKSNIYNAIHLLTAAA 48
Cdd:cd03227     2 IVLGRFPSYFvpnDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGA 48
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 5-41 3.30e-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: 38.36  E-value: 3.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1457429881   5 IRIQNFRSVKD--IVLELGPLNIVFGPNGCGKSNIYNAI 41
Cdd:cd03240     4 LSIRNIRSFHErsEIEFFSPLTLIVGQNGAGKTTIIEAL 42
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
1-64 3.86e-03

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


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 39.33  E-value: 3.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1457429881   1 MIQYI-RIQNFRSVKD--IVLELGPLNIVFGPNGCGKSNIynaIHLLTAAAEGRLSGFISEEGGLEN 64
Cdd:COG4694     1 MITKIkKLKNVGAFKDfgWLAFFKKLNLIYGENGSGKSTL---SRILRSLELGDTSSEVIAEFEIEA 64
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 6-52 4.10e-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: 37.61  E-value: 4.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1457429881   6 RIQNFRSVKDIVLEL--GPLNIVFGPNGCGKSNIYNAIHLLTAAAEGRL 52
Cdd:cd00267     8 RYGGRTALDNVSLTLkaGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI 56
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
 2-58 4.15e-03

ATP-binding cassette domain of eukaryotic SM6 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: 213243 [Multi-domain]  Cd Length: 198  Bit Score: 37.96  E-value: 4.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1457429881   2 IQYIRIQNFRSVKDIVLELGP-LNIVFGPNGCGKSNIYNAIHL-LTAAAE-----GRLSGFISE 58
Cdd:cd03276     1 IESITLKNFMCHRHLQIEFGPrVNFIVGNNGSGKSAILTALTIgLGGKASdtnrgSSLKDLIKD 64
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-41 7.59e-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: 38.51  E-value: 7.59e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1457429881    2 IQYIRIQNFRSV-KDIVLELGP-LNIVFGPNGCGKSNIYNAI 41
Cdd:TIGR02169    2 IERIELENFKSFgKKKVIPFSKgFTVISGPNGSGKSNIGDAI 43
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-37 9.01e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 9.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1457429881   5 IRIQNFRS-VKDIVLELGP-LNIVFGPNGCGKSNI 37
Cdd:COG1196     6 LELAGFKSfADPTTIPFEPgITAIVGPNGSGKSNI 40
PRK01156 PRK01156
chromosome segregation protein; Provisional
 1-41 9.27e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 37.96  E-value: 9.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1457429881   1 MIQYIRIQNFRSVKDIVLELGP-LNIVFGPNGCGKSNIYNAI 41
Cdd:PRK01156    2 IIKRIRLKNFLSHDDSEIEFDTgINIITGKNGAGKSSIVDAI 43
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH