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Conserved domains on  [gi|1816481790|ref|WP_163486940|]
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PspA/IM30 family protein [Halogeometricum borinquense]

Protein Classification

PspA/IM30 family protein( domain architecture ID 11448776)

PspA/IM30 family protein similar to Bacillus subtilis phage shock protein A homolog and Arabidopsis thaliana membrane-associated protein VIPP1, which is required for plastid vesicle formation and thylakoid membrane biogenesis

PubMed:  12079332|10629175

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
2-230 1.10e-53

Phage shock protein A [Transcription, Signal transduction mechanisms];


:

Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 173.47  E-value: 1.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   2 GILSRASYVVRSKINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVRQ 81
Cdd:COG1842     1 GIFKRLSDIIRANINALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  82 DRDDLAKRALEKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAVSGVGD 161
Cdd:COG1842    81 GREDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816481790 162 EmgDVSRALERAEDQTDEMEARSAAMDELvdtgafdemmSDKDAIDRELETGRANSEVDTELETLKTEM 230
Cdd:COG1842   161 D--DATSALERMEEKIEEMEARAEAAAEL----------AAGDSLDDELAELEADSEVEDELAALKAKM 217
 
Name Accession Description Interval E-value
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
2-230 1.10e-53

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 173.47  E-value: 1.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   2 GILSRASYVVRSKINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVRQ 81
Cdd:COG1842     1 GIFKRLSDIIRANINALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  82 DRDDLAKRALEKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAVSGVGD 161
Cdd:COG1842    81 GREDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816481790 162 EmgDVSRALERAEDQTDEMEARSAAMDELvdtgafdemmSDKDAIDRELETGRANSEVDTELETLKTEM 230
Cdd:COG1842   161 D--DATSALERMEEKIEEMEARAEAAAEL----------AAGDSLDDELAELEADSEVEDELAALKAKM 217
phageshock_pspA TIGR02977
phage shock protein A; Members of this family are the phage shock protein PspA, from the phage ...
 1-232 7.04e-23

phage shock protein A; Members of this family are the phage shock protein PspA, from the phage shock operon. This is a narrower family than the set of PspA and its homologs, sometimes several in a genome, as described by pfam04012. PspA appears to maintain the protonmotive force under stress conditions that include overexpression of certain phage secretins, heat shock, ethanol, and protein export defects. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 274372 [Multi-domain]  Cd Length: 219  Bit Score: 93.50  E-value: 7.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   1 MGILSRASYVVRSKINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVR 80
Cdd:TIGR02977   1 MGIFSRFADIVNSNLNALLDKAEDPEKMIRLIIQEMEDTLVEVRTASARTIADKKELERRVSRLEAQVADWQDKAELALS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  81 QDRDDLAKRALEKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAVSgvG 160
Cdd:TIGR02977  81 KGREDLARAALIEKQKAQELAEALERELAAVEETLAKLQEDIAKLQAKLAEARARQKALAIRHQAASSRLDVRRQLD--S 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816481790 161 DEMGDVSRALERAEDQTDEMEARSAAMDelvdtgafdemMSDKDAIDRELETGRANSEVDTELETLKTEMGK 232
Cdd:TIGR02977 159 GRSDEAMARFEQYERRVDELEAQAESYD-----------LGRKPSLEDEFAELEADDEIERELAALKAKMKK 219
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 3-198 7.07e-21

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 88.20  E-value: 7.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   3 ILSRASYVVRSKINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVRQD 82
Cdd:pfam04012   1 IFKRLGRLVRANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  83 RDDLAKRALEKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAVSGVGDE 162
Cdd:pfam04012  81 NEELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSLGSLSTS 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1816481790 163 mgDVSRALERAEDQTDEMEARSAAMDELVDTGAFDE 198
Cdd:pfam04012 161 --SATDSFERIEEKIEEREARADAAAELASAVDLDA 194
PRK10698 PRK10698
phage shock protein PspA; Provisional
 1-234 1.52e-15

phage shock protein PspA; Provisional


Pssm-ID: 182657 [Multi-domain]  Cd Length: 222  Bit Score: 73.65  E-value: 1.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   1 MGILSRASYVVRSKINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVR 80
Cdd:PRK10698    1 MGIFSRFADIVNANINALLEKAEDPQKLVRLMIQEMEDTLVEVRSTSARALAEKKQLTRRIEQAEAQQVEWQEKAELALR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  81 QDRDDLAKRALEKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAV-SGV 159
Cdd:PRK10698   81 KEKEDLARAALIEKQKLTDLIATLEHEVTLVDETLARMKKEIGELENKLSETRARQQALMLRHQAASSSRDVRRQLdSGK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816481790 160 GDEmgdVSRALERAEDQTDEMEARSAAMDelvdtgafdemMSDKDAIDRELETGRANSEVDTELETLKTEMGKST 234
Cdd:PRK10698  161 LDE---AMARFESFERRIDQMEAEAESHG-----------FGKQKSLDQQFAELKADDEISEQLAALKAKMKQDN 221
 
Name Accession Description Interval E-value
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
2-230 1.10e-53

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 173.47  E-value: 1.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   2 GILSRASYVVRSKINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVRQ 81
Cdd:COG1842     1 GIFKRLSDIIRANINALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  82 DRDDLAKRALEKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAVSGVGD 161
Cdd:COG1842    81 GREDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816481790 162 EmgDVSRALERAEDQTDEMEARSAAMDELvdtgafdemmSDKDAIDRELETGRANSEVDTELETLKTEM 230
Cdd:COG1842   161 D--DATSALERMEEKIEEMEARAEAAAEL----------AAGDSLDDELAELEADSEVEDELAALKAKM 217
phageshock_pspA TIGR02977
phage shock protein A; Members of this family are the phage shock protein PspA, from the phage ...
 1-232 7.04e-23

phage shock protein A; Members of this family are the phage shock protein PspA, from the phage shock operon. This is a narrower family than the set of PspA and its homologs, sometimes several in a genome, as described by pfam04012. PspA appears to maintain the protonmotive force under stress conditions that include overexpression of certain phage secretins, heat shock, ethanol, and protein export defects. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 274372 [Multi-domain]  Cd Length: 219  Bit Score: 93.50  E-value: 7.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   1 MGILSRASYVVRSKINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVR 80
Cdd:TIGR02977   1 MGIFSRFADIVNSNLNALLDKAEDPEKMIRLIIQEMEDTLVEVRTASARTIADKKELERRVSRLEAQVADWQDKAELALS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  81 QDRDDLAKRALEKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAVSgvG 160
Cdd:TIGR02977  81 KGREDLARAALIEKQKAQELAEALERELAAVEETLAKLQEDIAKLQAKLAEARARQKALAIRHQAASSRLDVRRQLD--S 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816481790 161 DEMGDVSRALERAEDQTDEMEARSAAMDelvdtgafdemMSDKDAIDRELETGRANSEVDTELETLKTEMGK 232
Cdd:TIGR02977 159 GRSDEAMARFEQYERRVDELEAQAESYD-----------LGRKPSLEDEFAELEADDEIERELAALKAKMKK 219
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 3-198 7.07e-21

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 88.20  E-value: 7.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   3 ILSRASYVVRSKINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVRQD 82
Cdd:pfam04012   1 IFKRLGRLVRANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  83 RDDLAKRALEKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAVSGVGDE 162
Cdd:pfam04012  81 NEELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSLGSLSTS 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1816481790 163 mgDVSRALERAEDQTDEMEARSAAMDELVDTGAFDE 198
Cdd:pfam04012 161 --SATDSFERIEEKIEEREARADAAAELASAVDLDA 194
PRK10698 PRK10698
phage shock protein PspA; Provisional
 1-234 1.52e-15

phage shock protein PspA; Provisional


Pssm-ID: 182657 [Multi-domain]  Cd Length: 222  Bit Score: 73.65  E-value: 1.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   1 MGILSRASYVVRSKINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVR 80
Cdd:PRK10698    1 MGIFSRFADIVNANINALLEKAEDPQKLVRLMIQEMEDTLVEVRSTSARALAEKKQLTRRIEQAEAQQVEWQEKAELALR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  81 QDRDDLAKRALEKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAV-SGV 159
Cdd:PRK10698   81 KEKEDLARAALIEKQKLTDLIATLEHEVTLVDETLARMKKEIGELENKLSETRARQQALMLRHQAASSSRDVRRQLdSGK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816481790 160 GDEmgdVSRALERAEDQTDEMEARSAAMDelvdtgafdemMSDKDAIDRELETGRANSEVDTELETLKTEMGKST 234
Cdd:PRK10698  161 LDE---AMARFESFERRIDQMEAEAESHG-----------FGKQKSLDQQFAELKADDEISEQLAALKAKMKQDN 221
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-260 3.49e-07

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: 51.21  E-value: 3.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   31 YSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNeqARQAVRQDRDDLAKRALekkQAKMNQIEDLESQIAN 110
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEIEELQKEL---YALANEISRLEQQKQI 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  111 LQETQDNLVDKKNELQNRIEEFRTKKEtmkaryEAAEASSRVSEAVSGVGDEMGDVSRALERAEDQTDEMEARSAAMDEL 190
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLD------ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816481790  191 VDT--GAFDEMMSDKDAIDRELEtgransEVDTELETLKTEMGKSTAEPEAESENGGETSSADLDEELDQVD 260
Cdd:TIGR02168  381 LETlrSKVAQLELQIASLNNEIE------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 31-258 2.17e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  31 YSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEkhneQARQAVRQDRDDLaKRALEKKQAKMNQIEDLESQIAN 110
Cdd:COG1196   232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELEL-EEAQAEEYELLAELARLEQDIAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790 111 LQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAvsgvgdEMGDVSRALERAEDQTDEMEARSAAMDEL 190
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE------ELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816481790 191 VDTGAFDEMMSDKDAID---RELETGRANSEVDTELETLKTEMGKSTAEPEAESENGGETSSADLDEELDQ 258
Cdd:COG1196   381 LEELAEELLEALRAAAElaaQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 16-236 2.84e-06

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: 48.51  E-value: 2.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   16 NSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVRQdrddlAKRALEKKQ 95
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ-----LEELEAQLE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   96 AKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAE-----ASSRVSEAVSGVGDEMGDVSRA- 169
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqletLRSKVAQLELQIASLNNEIERLe 406

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  170 --LERAEDQTDEMEARSAAMDELVDTGAFDEMMSDKDAIDRELETGRA-NSEVDTELETLKTEMGKSTAE 236
Cdd:TIGR02168  407 arLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEeLERLEEALEELREELEEAEQA 476
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 34-259 2.91e-06

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: 48.53  E-value: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   34 EKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNE-QARQAVRQDRDdlAKRALEKKQAKMNQIEDLESQIANLQ 112
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  113 ETQDNLVDKKNELQNRIEEFRTKKETMKARYEA--AEASSRVSEAVSGVGDEMGDVSRALERAEDQTDEMEARSAAMDEL 190
Cdd:TIGR02169  251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816481790  191 VdtgafDEMMSDKDAIDRELETGRANSE-VDTELETLKTEMGKSTAEPEAESENGGET--SSADLDEELDQV 259
Cdd:TIGR02169  331 I-----DKLLAEIEELEREIEEERKRRDkLTEEYAELKEELEDLRAELEEVDKEFAETrdELKDYREKLEKL 397
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
53-236 4.40e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 4.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   53 QKKRLEIQKRRLEENVEKHNEQARQAvrqdrdDLAKRALEKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQnRIEEF 132
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEAL------EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELE-RLDAS 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  133 RTKKETMKARYEAAEAS-SRVSEAVSGVGDEMGDVSRALERAEDQTDEMEARSAAMDELVDTGAFDEMMSDKDAIDRELE 211
Cdd:COG4913    684 SDDLAALEEQLEELEAElEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763

                          170       180
                   ....*....|....*....|....*
gi 1816481790  212 TGRANSEVDTELETLKTEMGKSTAE 236
Cdd:COG4913    764 ERELRENLEERIDALRARLNRAEEE 788
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 12-199 1.08e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  12 RSKINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVRQDR-------- 83
Cdd:COG4942    50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllspe 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  84 --DDLAKRAL---EKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETM-KARYEAAEASSRVSEAVS 157
Cdd:COG4942   130 dfLDAVRRLQylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALeALKAERQKLLARLEKELA 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1816481790 158 GVGDEMGDVSRALERAEDQTDEMEARSAAMDELVDTGAFDEM 199
Cdd:COG4942   210 ELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
39-187 1.22e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   39 ELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVRQdrddlakraleKKQAKMNQIEDLESQIANLQETQDNL 118
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ-----------IRGNGGDRLEQLEREIERLERELEER 357

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816481790  119 VDKKNELQNRIEEFR-----TKKETMKARYEAAEASSRVSEAVSGVGDEMGDVSRALERAEDQTDEMEARSAAM 187
Cdd:COG4913    358 ERRRARLEALLAALGlplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
21-242 1.98e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  21 RAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQ---AVRQDRDDLAKR-----ALE 92
Cdd:PRK02224  311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAElesELEEAREAVEDRreeieELE 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  93 KK-QAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEA---------------SSRVSEAV 156
Cdd:PRK02224  391 EEiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpveGSPHVETI 470

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790 157 SGVGDEMGDVSRALERAEDQTDEMEARSAAMDELVDTGA-FDEMMSDKDAIDRELETGRANSEVDTE-LETLKTEMGKST 234
Cdd:PRK02224  471 EEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDrIERLEERREDLEELIAERRETIEEKRErAEELRERAAELE 550


                  ....*...
gi 1816481790 235 AEPEAESE 242
Cdd:PRK02224  551 AEAEEKRE 558
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 37-257 2.99e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  37 RDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQAR--QAVRQDRDDLAKRALEKKQAKMNQIEDLESQIANLQET 114
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeaEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790 115 QDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAvsgvgdEMGDVSRALERAEDQTDEMEARSAAMDELVDTG 194
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE------EEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816481790 195 AFDEMMSDKDAIDRELETGRANSEVDTELETLKTEMGKSTAEPEAESENGGETSSADLDEELD 257
Cdd:COG1196   469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 34-229 4.36e-04

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: 41.58  E-value: 4.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   34 EKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNE--QARQAVRQDRDDLAKRALEKKQAKMN----QIEDLESQ 107
Cdd:TIGR02168  182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAElrELELALLVLRLEELREELEELQEELKeaeeELEELTAE 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  108 IANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRV-SEAVSGVGDEMGDVSRALERAEDQTDEMEARSAA 186
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIlRERLANLERQLEELEAQLEELESKLDELAEELAE 341

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1816481790  187 MDE-----LVDTGAFDEMMSDKDAIDRELEtgRANSEVDTELETLKTE 229
Cdd:TIGR02168  342 LEEkleelKEELESLEAELEELEAELEELE--SRLEELEEQLETLRSK 387
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 34-211 5.16e-04

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: 41.58  E-value: 5.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   34 EKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHnEQARQAVRQDRDDLAKRALEKKQakmnQIEDLESQIANLQE 113
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARL-EAEVEQLEERIAQLSKELTELEA----EIEELEERLEEAEE 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  114 TQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEA--------SSRVSEAVSGVGDEMGDVSRALERAEDQTDEMEARSA 185
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltllneeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855

                          170       180
                   ....*....|....*....|....*.
gi 1816481790  186 AMdelvdTGAFDEMMSDKDAIDRELE 211
Cdd:TIGR02168  856 SL-----AAEIEELEELIEELESELE 876
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
48-257 6.64e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 6.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  48 ADLTTQKKRLEIQKRRLEENVEKHNEQARQAVRqdRDDLAKRALEKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQN 127
Cdd:PRK02224  202 KDLHERLNGLESELAELDEEIERYEEQREQARE--TRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790 128 RIEEFRTKKETMkaryeaaeaSSRVSEAVSGVGDEMGDVSRALERAED-QTDEMEARSAAMDELVDTGAFDEmmsdkdAI 206
Cdd:PRK02224  280 EVRDLRERLEEL---------EEERDDLLAEAGLDDADAEAVEARREElEDRDEELRDRLEECRVAAQAHNE------EA 344

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1816481790 207 DRELETGRANSEVDTELETLKTEMGKSTAEPEAESENgGETSSADLDEELD 257
Cdd:PRK02224  345 ESLREDADDLEERAEELREEAAELESELEEAREAVED-RREEIEELEEEIE 394
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
105-261 1.14e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  105 ESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAVsgvgDEMGDVSRALERAEDQTDEMEARS 184
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE----IDVASAEREIAELEAELERLDASS 684

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816481790  185 AAMDELVDtgAFDEMMSDKDAIDREL-ETGRANSEVDTELETLKTEMGKSTAEPEAESENGGETSSADLDEELDQVDV 261
Cdd:COG4913    685 DDLAALEE--QLEELEAELEELEEELdELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
34-152 2.70e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   34 EKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQ--------ARQAVRQDRDDLAKRALEKKQAKMnQIEDLE 105
Cdd:COG4913    620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvasaerEIAELEAELERLDASSDDLAALEE-QLEELE 698

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1816481790  106 SQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRV 152
Cdd:COG4913    699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 42-192 3.10e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 38.78  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  42 QVKQGIADLTTQKKRLEIQKRRLEenvekhneqARQAvRQDRDDLAKRALEKKQA---KMNQIEDLESQIANLQETQDNL 118
Cdd:PRK05035  433 QAKAEIRAIEQEKKKAEEAKARFE---------ARQA-RLEREKAAREARHKKAAearAAKDKDAVAAALARVKAKKAAA 502

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816481790 119 VDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEAVSGVGDEMGDVSRALERAEDQTDEMEARSAAMDELVD 192
Cdd:PRK05035  503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVD 576
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 13-152 3.16e-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: 38.88  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   13 SKINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKhneqARQAVRQDRDDLAKRALE 92
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAELK 436

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   93 KKQAkmnQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTkkETMKARYEAAEASSRV 152
Cdd:TIGR02168  437 ELQA---ELEELEEELEELQEELERLEEALEELREELEEAEQ--ALDAAERELAQLQARL 491
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
34-190 3.54e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  34 EKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVRQDRDDLAKRALEKKQAKMNQIEDLESQIANLQE 113
Cdd:COG4717    84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE 163

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816481790 114 TQDNLVDKKNELQNRIEEFRTKKETMKARY--EAAEASSRVSEAVSGVGDEMGDVSRALERAEDQTDEMEARSAAMDEL 190
Cdd:COG4717   164 ELEELEAELAELQEELEELLEQLSLATEEElqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 14-155 3.75e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.98  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  14 KINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHneQARQAVRQDRDDLAK----- 88
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV--EARIKKYEEQLGNVRnnkey 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816481790  89 RALEKKQAKMN-QIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEA 155
Cdd:COG1579    92 EALQKEIESLKrRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 33-238 4.01e-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: 4.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   33 YEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVRQDRDDLAKR-ALEKKQAKMNQ-IEDLESQIAN 110
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIeQLEQEEEKLKErLEELEEDLSS 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  111 LQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEaVSGVGDEMGDVSRALERAEDQTDEMEARSAamDEL 190
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR-IPEIQAELSKLEEEVSRIEARLREIEQKLN--RLT 825

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1816481790  191 VDTGAFDEMMSDKDAIDRELETGRAnsEVDTELETLKTEMGKSTAEPE 238
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKEQIK--SIEKEIENLNGKKEELEEELE 871
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
64-183 4.24e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  64 LEENVEKHNEQARQAVR--QDRDDLAKRALEKKQAKMNQIEdLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKA 141
Cdd:COG3206   162 LEQNLELRREEARKALEflEEQLPELRKELEEAEAALEEFR-QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1816481790 142 RYEAAE---ASSRVSEAVSGVGDEMGDVSRALERAEDQTDEMEAR 183
Cdd:COG3206   241 RLAALRaqlGSGPDALPELLQSPVIQQLRAQLAELEAELAELSAR 285
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
34-148 4.46e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 4.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   34 EKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVE--------------KHNEQARQAVRQDRDDLAKRALEKKQAKMN 99
Cdd:COG4913    298 EELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleqlereiERLERELEERERRRARLEALLAALGLPLPA 377

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1816481790  100 QIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEA 148
Cdd:COG4913    378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 14-152 5.88e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 37.88  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  14 KINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKhneQARQAVRQdrddlAKRALEK 93
Cdd:PRK00409  517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK---EAQQAIKE-----AKKEADE 588

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1816481790  94 KQAKMNQIEDLESQIANLQETQdnlvDKKNELQNRIEEFRTKKETMKARYEAAEASSRV 152
Cdd:PRK00409  589 IIKELRQLQKGGYASVKAHELI----EARKRLNKANEKKEKKKKKQKEKQEELKVGDEV 643
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-193 7.37e-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: 37.74  E-value: 7.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790    3 ILSRASYVVRSKINSLLNRAEDPTETLdysyEKMRDELQQVKQGIADLTTQKKRLEIQKrrLEENVEKHNEQARQAVR-- 80
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEARLSHSRIPEIQAELSK--LEEEVSRIEARLREIEQkl 821

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   81 QDRDDLAKRALEKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKKETMKARYEAAEAS-SRVSEAVSGV 159
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKErDELEAQLREL 901

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1816481790  160 GDEMGDVSRALERAEDQTDEMEARSAAMDELVDT 193
Cdd:TIGR02169  902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 12-136 7.91e-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: 37.73  E-value: 7.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790   12 RSKINSLLNRAEDPTETLDYSYEKMRDELQQVKQGIADLTTQKKRLEIQKRRLEENVEKHNEQARQAVRQDRDDLAKRAL 91
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE 443

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1816481790   92 EKKQAKMNQIEDLESQIANLQETQDNLVDKKNELQNRIEEFRTKK 136
Cdd:TIGR02168  444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
39-155 8.51e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.44  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816481790  39 ELQQVKQGIADLTTQKKRLEIQKRRLEEnVEKHNEQARQAVRQDRDDLAKRALEKKQAKMNQIEDLESQIANLQETQDNL 118
Cdd:COG4717   133 ELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1816481790 119 VDKKNELQNRIEEFRTKKETMKARYEAAEASSRVSEA 155
Cdd:COG4717   212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
 
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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