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Conserved domains on  [gi|755532279|ref|XP_011241326|]
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leucine-rich repeat flightless-interacting protein 2 isoform X32 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
47-405 3.56e-108

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


:

Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 323.19  E-value: 3.56e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   47 DIRMRELERQQREgvedtlslrslgshrLDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSL 117
Cdd:pfam09738  17 EIRMRELERQQKE---------------VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSIS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  118 IDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVL 197
Cdd:pfam09738  82 LEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  198 QHKMDELKEGLRQRDELIeenqrlqqkvdtmtkevfdlqetllwkdkalgalekqkehiaclrnerdvlreeladlrqtv 277
Cdd:pfam09738 162 QFQLAELKEQLKQRDELI-------------------------------------------------------------- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  278 ttaEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQ-K 356
Cdd:pfam09738 180 ---EKHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkR 256
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 755532279  357 CSRNDGMSGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDIAT 405
Cdd:pfam09738 257 NSTRSSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
230-480 3.86e-05

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 230 KEVFDLQETLLWKDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEkhglviipdstpngdvhhepvvgaitAV 309
Cdd:COG1196  222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------------------------LE 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 310 SQEAAQVLESAGEgpldvRLRKLAGEKDELLSQIRKLKLQLEEERQkcsRNDGMSGDLAGLQngsdlqfiEMQRDANRQI 389
Cdd:COG1196  276 LEELELELEEAQA-----EEYELLAELARLEQDIARLEERRRELEE---RLEELEEELAELE--------EELEELEEEL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 390 SEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKM 469
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
                        250
                 ....*....|.
gi 755532279 470 KANRTALLAQQ 480
Cdd:COG1196  420 EEELEELEEAL 430
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
47-405 3.56e-108

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 323.19  E-value: 3.56e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   47 DIRMRELERQQREgvedtlslrslgshrLDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSL 117
Cdd:pfam09738  17 EIRMRELERQQKE---------------VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSIS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  118 IDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVL 197
Cdd:pfam09738  82 LEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  198 QHKMDELKEGLRQRDELIeenqrlqqkvdtmtkevfdlqetllwkdkalgalekqkehiaclrnerdvlreeladlrqtv 277
Cdd:pfam09738 162 QFQLAELKEQLKQRDELI-------------------------------------------------------------- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  278 ttaEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQ-K 356
Cdd:pfam09738 180 ---EKHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkR 256
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 755532279  357 CSRNDGMSGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDIAT 405
Cdd:pfam09738 257 NSTRSSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
115-455 1.43e-08

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: 57.37  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   115 SSLIDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMC 194
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   195 SVLQHkmdELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkDKALGALEKQKEHIACLRNERDVLREELADLR 274
Cdd:TIGR02168  750 AQLSK---ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLR 823
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   275 QTVTTAEKhglviipdstpngdvHHEPVVGAITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQI-RKLKLQLEEE 353
Cdd:TIGR02168  824 ERLESLER---------------RIAATERRLEDLEEQIEELSEDIES--LAAEIEELEELIEELESELeALLNERASLE 886
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   354 RQKCSRNDGMSgDLAGLQNGSDLQFIEMQRD---ANRQISEYKFKLSKAEQDIATLEQSISRlegqvlRYKTAAENAEKI 430
Cdd:TIGR02168  887 EALALLRSELE-ELSEELRELESKRSELRREleeLREKLAQLELRLEGLEVRIDNLQERLSE------EYSLTLEEAEAL 959
                          330       340
                   ....*....|....*....|....*
gi 755532279   431 EDELKAERRKLQRELRTAQDKIEEM 455
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
230-480 3.86e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 230 KEVFDLQETLLWKDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEkhglviipdstpngdvhhepvvgaitAV 309
Cdd:COG1196  222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------------------------LE 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 310 SQEAAQVLESAGEgpldvRLRKLAGEKDELLSQIRKLKLQLEEERQkcsRNDGMSGDLAGLQngsdlqfiEMQRDANRQI 389
Cdd:COG1196  276 LEELELELEEAQA-----EEYELLAELARLEQDIARLEERRRELEE---RLEELEEELAELE--------EELEELEEEL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 390 SEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKM 469
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
                        250
                 ....*....|.
gi 755532279 470 KANRTALLAQQ 480
Cdd:COG1196  420 EEELEELEEAL 430
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
178-427 5.50e-05

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: 45.14  E-value: 5.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 178 RENEEKSKELERQkhmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQkehIA 257
Cdd:COG4942   23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 258 CLRNERDVLREELADLRQTVTTAEKHG--LVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEgpldvRLRKLAGE 335
Cdd:COG4942   94 ELRAELEAQKEELAELLRALYRLGRQPplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 336 KDELLSQIRKLKLQLEEERQKcsrndgmsgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEG 415
Cdd:COG4942  169 LEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
                        250
                 ....*....|..
gi 755532279 416 QVLRYKTAAENA 427
Cdd:COG4942  235 EAAAAAERTPAA 246
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
122-471 4.60e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 4.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 122 TSLSELRESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQ 198
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 199 HKMDELKEGLRQRDELIEenqRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQ----KEHIACLRNERDVLREELADLR 274
Cdd:PRK02224 293 EERDDLLAEAGLDDADAE---AVEARREELEDRDEELRDRLEECRVAAQAHNEEaeslREDADDLEERAEELREEAAELE 369
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 275 QTVTTAEkhglviipdstpngdVHHEPVVGAITAVSQEAAQVLESAGEGPLDV-----RLRKLAGEKDELLSQIRKLKLQ 349
Cdd:PRK02224 370 SELEEAR---------------EAVEDRREEIEELEEEIEELRERFGDAPVDLgnaedFLEELREERDELREREAELEAT 434
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 350 LEEERQKCSRNDGMsgdLAGLQNGSDLQFIEMQRDANRqISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEK 429
Cdd:PRK02224 435 LRTARERVEEAEAL---LEAGKCPECGQPVEGSPHVET-IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDR 510
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 755532279 430 IEDeLKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 471
Cdd:PRK02224 511 IER-LEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
47-405 3.56e-108

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 323.19  E-value: 3.56e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   47 DIRMRELERQQREgvedtlslrslgshrLDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSL 117
Cdd:pfam09738  17 EIRMRELERQQKE---------------VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSIS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  118 IDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVL 197
Cdd:pfam09738  82 LEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  198 QHKMDELKEGLRQRDELIeenqrlqqkvdtmtkevfdlqetllwkdkalgalekqkehiaclrnerdvlreeladlrqtv 277
Cdd:pfam09738 162 QFQLAELKEQLKQRDELI-------------------------------------------------------------- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  278 ttaEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQ-K 356
Cdd:pfam09738 180 ---EKHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkR 256
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 755532279  357 CSRNDGMSGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDIAT 405
Cdd:pfam09738 257 NSTRSSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
115-455 1.43e-08

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: 57.37  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   115 SSLIDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMC 194
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   195 SVLQHkmdELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkDKALGALEKQKEHIACLRNERDVLREELADLR 274
Cdd:TIGR02168  750 AQLSK---ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLR 823
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   275 QTVTTAEKhglviipdstpngdvHHEPVVGAITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQI-RKLKLQLEEE 353
Cdd:TIGR02168  824 ERLESLER---------------RIAATERRLEDLEEQIEELSEDIES--LAAEIEELEELIEELESELeALLNERASLE 886
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   354 RQKCSRNDGMSgDLAGLQNGSDLQFIEMQRD---ANRQISEYKFKLSKAEQDIATLEQSISRlegqvlRYKTAAENAEKI 430
Cdd:TIGR02168  887 EALALLRSELE-ELSEELRELESKRSELRREleeLREKLAQLELRLEGLEVRIDNLQERLSE------EYSLTLEEAEAL 959
                          330       340
                   ....*....|....*....|....*
gi 755532279   431 EDELKAERRKLQRELRTAQDKIEEM 455
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
148-456 2.61e-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: 50.07  E-value: 2.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   148 LDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDt 227
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE- 764
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   228 mtKEVFDLQETLLWKDKALGALEKQKEH--IACLRNERDVLREELADLRQTVTTAEK----------------HGLVIIP 289
Cdd:TIGR02169  765 --ARIEELEEDLHKLEEALNDLEARLSHsrIPEIQAELSKLEEEVSRIEARLREIEQklnrltlekeylekeiQELQEQR 842
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   290 DSTPNGDVHHEPVVGAITAVSQEAAQVLE--SAGEGPLDVRLRKLAGEKDELLSQIRKLKL---QLEEERQKcsRNDGMS 364
Cdd:TIGR02169  843 IDLKEQIKSIEKEIENLNGKKEELEEELEelEAALRDLESRLGDLKKERDELEAQLRELERkieELEAQIEK--KRKRLS 920
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   365 GDLAGLQNGSD-LQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQR 443
Cdd:TIGR02169  921 ELKAKLEALEEeLSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
                          330
                   ....*....|...
gi 755532279   444 ELRTAQDKIEEME 456
Cdd:TIGR02169 1001 ERKAILERIEEYE 1013
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
197-479 5.16e-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: 49.30  E-value: 5.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   197 LQHKMDELKeglRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGAL----EKQKEHIACLRNERDVLREELAD 272
Cdd:TIGR02169  679 LRERLEGLK---RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   273 LRQTVTTAEKhglviipdstpngdvhhepVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEE 352
Cdd:TIGR02169  756 VKSELKELEA-------------------RIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   353 ERQKCSRNDgmsgdlaglqngSDLQFIEMQR-DANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIE 431
Cdd:TIGR02169  817 IEQKLNRLT------------LEKEYLEKEIqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 755532279   432 DELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 479
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
181-456 2.86e-05

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: 46.97  E-value: 2.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   181 EEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDtmtKEVFDLQETLLWKDKALGALEKQKEHI---- 256
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQKQILrerl 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   257 ACLRNERDVLREELADLRQTVTTAEKhglvIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLES-AGEGPLDVRLRKLAGE 335
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAE----ELAELEEKLEELKEELESLEAELEELEAELEELeSRLEELEEQLETLRSK 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   336 KDELLSQIRKLKLQLEEERQKCSRndgmsgdlaglQNGSDLQFIEMQRDANRQISEYKFKLSKAEqdIATLEQSISRLEG 415
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLER-----------LEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQE 454
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 755532279   416 QVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEME 456
Cdd:TIGR02168  455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
230-480 3.86e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 230 KEVFDLQETLLWKDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEkhglviipdstpngdvhhepvvgaitAV 309
Cdd:COG1196  222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------------------------LE 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 310 SQEAAQVLESAGEgpldvRLRKLAGEKDELLSQIRKLKLQLEEERQkcsRNDGMSGDLAGLQngsdlqfiEMQRDANRQI 389
Cdd:COG1196  276 LEELELELEEAQA-----EEYELLAELARLEQDIARLEERRRELEE---RLEELEEELAELE--------EELEELEEEL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 390 SEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKM 469
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
                        250
                 ....*....|.
gi 755532279 470 KANRTALLAQQ 480
Cdd:COG1196  420 EEELEELEEAL 430
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
178-427 5.50e-05

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: 45.14  E-value: 5.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 178 RENEEKSKELERQkhmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQkehIA 257
Cdd:COG4942   23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 258 CLRNERDVLREELADLRQTVTTAEKHG--LVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEgpldvRLRKLAGE 335
Cdd:COG4942   94 ELRAELEAQKEELAELLRALYRLGRQPplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 336 KDELLSQIRKLKLQLEEERQKcsrndgmsgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEG 415
Cdd:COG4942  169 LEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
                        250
                 ....*....|..
gi 755532279 416 QVLRYKTAAENA 427
Cdd:COG4942  235 EAAAAAERTPAA 246
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
325-471 8.81e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 8.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  325 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCsrnDGMSGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 403
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532279  404 ATLEQSI-----------SRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 471
Cdd:COG4913   369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
121-282 1.01e-04

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: 45.06  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   121 DTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHK 200
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   201 MDELKeglRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTA 280
Cdd:TIGR02169  884 LGDLK---KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAEL 960

                   ..
gi 755532279   281 EK 282
Cdd:TIGR02169  961 QR 962
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
242-479 2.49e-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: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 242 KDKALGALEKQKEHIACLRNERDVLREELADLRQTVTTAEKhglviipdstpngdvhhepvvgAITAVSQEAAQvlesag 321
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR----------------------RIRALEQELAA------ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 322 egpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNdGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKfklskaEQ 401
Cdd:COG4942   81 ---LEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR------RE 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532279 402 DIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 479
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
122-471 4.60e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 4.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 122 TSLSELRESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQ 198
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 199 HKMDELKEGLRQRDELIEenqRLQQKVDTMTKEVFDLQETLLWKDKALGALEKQ----KEHIACLRNERDVLREELADLR 274
Cdd:PRK02224 293 EERDDLLAEAGLDDADAE---AVEARREELEDRDEELRDRLEECRVAAQAHNEEaeslREDADDLEERAEELREEAAELE 369
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 275 QTVTTAEkhglviipdstpngdVHHEPVVGAITAVSQEAAQVLESAGEGPLDV-----RLRKLAGEKDELLSQIRKLKLQ 349
Cdd:PRK02224 370 SELEEAR---------------EAVEDRREEIEELEEEIEELRERFGDAPVDLgnaedFLEELREERDELREREAELEAT 434
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 350 LEEERQKCSRNDGMsgdLAGLQNGSDLQFIEMQRDANRqISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEK 429
Cdd:PRK02224 435 LRTARERVEEAEAL---LEAGKCPECGQPVEGSPHVET-IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDR 510
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 755532279 430 IEDeLKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 471
Cdd:PRK02224 511 IER-LEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
mukB PRK04863
chromosome partition protein MukB;
124-453 7.20e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.25  E-value: 7.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  124 LSELRESLSEVEEKYKKA-----MVSNAQLDNEKNNLiYQVDTLKdvIEEQEEQMAEFYRENEEKSKELERQKhmcSVLQ 198
Cdd:PRK04863  316 LAELNEAESDLEQDYQAAsdhlnLVQTALRQQEKIER-YQADLEE--LEERLEEQNEVVEEADEQQEENEARA---EAAE 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  199 HKMDELKEGLRQRDELIEENQR----LQQKVDTmtkevfdLQETLLWKDKALGALEKQKEHIACLRNERDVLREELADLR 274
Cdd:PRK04863  390 EEVDELKSQLADYQQALDVQQTraiqYQQAVQA-------LERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLE 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  275 QTVTTAEkhglviipdstpngdvhhepvvgaitAVSQEAAQVLESagegpldvrLRKLAGEKD--ELLSQIRKLKLQLEE 352
Cdd:PRK04863  463 QKLSVAQ--------------------------AAHSQFEQAYQL---------VRKIAGEVSrsEAWDVARELLRRLRE 507
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  353 ERQKCSRNDGMSGDLAGLQngsdlQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENA----- 427
Cdd:PRK04863  508 QRHLAEQLQQLRMRLSELE-----QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEArerrm 582
                         330       340       350
                  ....*....|....*....|....*....|.
gi 755532279  428 --EKIEDELKAERRKLQR---ELRTAQDKIE 453
Cdd:PRK04863  583 alRQQLEQLQARIQRLAArapAWLAAQDALA 613
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
124-468 1.08e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 124 LSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIE--EQEEQMAEFYRENEEKSKELERqkhmcsvLQHKM 201
Cdd:COG4717   76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAE-------LPERL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 202 DELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDK-----ALGALEKQKEHIACLRNERDVLREELADLRQT 276
Cdd:COG4717  149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeelqdLAEELEELQQRLAELEEELEEAQEELEELEEE 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 277 VTTAEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGE---------GPLDVRLRKLAGEKDELLSQIRKLK 347
Cdd:COG4717  229 LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlGLLALLFLLLAREKASLGKEAEELQ 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 348 LQLEEERqkcSRNDGMSGDLAGLQNGSDLQfIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENA 427
Cdd:COG4717  309 ALPALEE---LEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 755532279 428 EKIED--ELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEK 468
Cdd:COG4717  385 EELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
174-471 1.10e-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: 41.59  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   174 AEFYRENEEKSKELERQKHMCSVLQHKMDELKEGL----RQRDELIEENQRLQQKVDTMTKE-VFDLQETLLWKDKALGA 248
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLerlrREREKAERYQALLKEKREYEGYElLKEKEALERQKEAIERQ 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   249 LEKQKEHIACLRNERDVLREELADLRQTVTTAEKHglviIPDSTPNGDVHHEPVVGAITA-VSQEAAQVLESAGE-GPLD 326
Cdd:TIGR02169  246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKK----IKDLGEEEQLRVKEKIGELEAeIASLERSIAEKERElEDAE 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   327 VRLRKLAGEKDELLSQIRKLKLQLEEERQkcsRNDGMSGDLAGLQNGSDLQFIEMQ------RDANRQISEYKFKLSKAE 400
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERK---RRDKLTEEYAELKEELEDLRAELEevdkefAETRDELKDYREKLEKLK 398
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755532279   401 QDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 471
Cdd:TIGR02169  399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
325-480 1.45e-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: 41.20  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   325 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRndgMSGDLAGLQnGSDLQFIEMQRDANRQISEYKFKLSKAEQDIA 404
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSE---LEEEIEELQ-KELYALANEISRLEQQKQILRERLANLERQLE 319
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755532279   405 TLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 480
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
383-471 2.03e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.61  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 383 RDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELkaerRKLQRELRTAQDKIEEMEMTNSHL 462
Cdd:COG2433  416 RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI----SRLDREIERLERELEEERERIEEL 491

                 ....*....
gi 755532279 463 AKRLEKMKA 471
Cdd:COG2433  492 KRKLERLKE 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
123-275 3.33e-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: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   123 SLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM-------AEFYRENEEKSKELERQKHMCS 195
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlrskvAQLELQIASLNNEIERLEARLE 410
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279   196 VLQHKMDELKEGLRQRDELIEENQR--LQQKVDTMTKEVFDLQETLlwkDKALGALEKQKEHIACLRNERDVLREELADL 273
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEEL---ERLEEALEELREELEEAEQALDAAERELAQL 487

                   ..
gi 755532279   274 RQ 275
Cdd:TIGR02168  488 QA 489
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
325-479 8.51e-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: 8.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 325 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 399
Cdd:COG1579   15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279 400 -----EQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEmtnSHLAKRLEKMKANRT 474
Cdd:COG1579   90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166

                 ....*
gi 755532279 475 ALLAQ 479
Cdd:COG1579  167 ELAAK 171
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
399-479 9.49e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 9.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532279  399 AEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQ-DKIEEMEMTNSHLAKRLEKMKANRTALL 477
Cdd:COG4913   286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLE 365

                  ..
gi 755532279  478 AQ 479
Cdd:COG4913   366 AL 367
 
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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