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Conserved domains on  [gi|1034636413|ref|XP_016862965|]
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leucine-rich repeat flightless-interacting protein 2 isoform X22 [Homo sapiens]

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 ...
47-414 1.53e-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: 324.34  E-value: 1.53e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  47 DIRMRELERQQKELDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiyd 117
Cdd:pfam09738  17 EIRMRELERQQKEVEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH--- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 118 lkdqiqdvegrymqglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELE 197
Cdd:pfam09738  94 ---------------------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 198 RQKHMCSVLQHKMEELKEGLRQRDELIeekqrmqqkidtmtkevfdlqetllwkdkkigalekqkeyiaclrnerdmlre 277
Cdd:pfam09738 153 RLKRNLRRLQFQLAELKEQLKQRDELI----------------------------------------------------- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 278 eladlqetvktgEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKL 357
Cdd:pfam09738 180 ------------EKHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKL 247
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034636413 358 QLEEERQ-KCSRNDGTVGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDITT 414
Cdd:pfam09738 248 QLEEEKSkRNSTRSSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
389-480 3.48e-03

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


The actual alignment was detected with superfamily member COG2433:

Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 389 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKtaAENA-------------EKVEDELKAEKRKLQRELR 455
Cdd:COG2433   385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--AEVEeleaeleekderiERLERELSEARSEERREIR 462
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034636413 456 -----TALD--------KIEEMEMTNSHLAKRLEKMKA 480
Cdd:COG2433   463 kdreiSRLDreierlerELEEERERIEELKRKLERLKE 500
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
47-414 1.53e-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: 324.34  E-value: 1.53e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  47 DIRMRELERQQKELDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiyd 117
Cdd:pfam09738  17 EIRMRELERQQKEVEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH--- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 118 lkdqiqdvegrymqglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELE 197
Cdd:pfam09738  94 ---------------------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 198 RQKHMCSVLQHKMEELKEGLRQRDELIeekqrmqqkidtmtkevfdlqetllwkdkkigalekqkeyiaclrnerdmlre 277
Cdd:pfam09738 153 RLKRNLRRLQFQLAELKEQLKQRDELI----------------------------------------------------- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 278 eladlqetvktgEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKL 357
Cdd:pfam09738 180 ------------EKHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKL 247
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034636413 358 QLEEERQ-KCSRNDGTVGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDITT 414
Cdd:pfam09738 248 QLEEEKSkRNSTRSSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
87-465 1.49e-08

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: 57.39  E-value: 1.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413   87 LSGNSSRRGSGDTSSLIDPDTSLSELRDIYDLKDQ---IQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNN 163
Cdd:TIGR02169  655 MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRElssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  164 LIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQrdELIEEKQRMQQKIDtmtKEVFD 243
Cdd:TIGR02169  735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLE---EEVSR 809
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  244 LQETLLWKDKKIGALEKQKEYiacLRNERDMLREELADLQETVKTGEKhglviipdgtpNGDVSHEPVAGAITVVSQEAA 323
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIKSIEK-----------EIENLNGKKEELEEELEELEA 875
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  324 QVLEsagegpLDVRLRKLAGEKEELLSQIRKLKL---QLEEERQKCSRNDGTVGDLAGLQNGsDLQFIEMQRDANRQISE 400
Cdd:TIGR02169  876 ALRD------LESRLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEE-ELSEIEDPKGEDEEIPE 948
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034636413  401 YKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 465
Cdd:TIGR02169  949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
187-436 1.31e-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: 43.98  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 187 RENEEKSKELERQkhmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQkeyIA 266
Cdd:COG4942    23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 267 CLRNERDMLREELAD-LQETVKTGEKHGL-VIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpldvRLRKLAGE 344
Cdd:COG4942    94 ELRAELEAQKEELAElLRALYRLGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 345 KEELLSQIRKLKLQLEEERQKcsrndgtvgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEG 424
Cdd:COG4942   169 LEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
                         250
                  ....*....|..
gi 1034636413 425 QVLRYKTAAENA 436
Cdd:COG4942   235 EAAAAAERTPAA 246
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
389-480 3.48e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 389 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKtaAENA-------------EKVEDELKAEKRKLQRELR 455
Cdd:COG2433   385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--AEVEeleaeleekderiERLERELSEARSEERREIR 462
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034636413 456 -----TALD--------KIEEMEMTNSHLAKRLEKMKA 480
Cdd:COG2433   463 kdreiSRLDreierlerELEEERERIEELKRKLERLKE 500
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
165-265 5.94e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.42  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 165 IYQVDTLK--DVI---EEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEglrQRDELIEE-KQRMQQKIDTMT 238
Cdd:PRK00409  510 LIGEDKEKlnELIaslEELERELEQKAEEAEALLKEAEKLK---EELEEKKEKLQE---EEDKLLEEaEKEAQQAIKEAK 583
                          90       100
                  ....*....|....*....|....*..
gi 1034636413 239 KEVFDLQETLLWKDKKIGALEKQKEYI 265
Cdd:PRK00409  584 KEADEIIKELRQLQKGGYASVKAHELI 610
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
47-414 1.53e-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: 324.34  E-value: 1.53e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  47 DIRMRELERQQKELDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiyd 117
Cdd:pfam09738  17 EIRMRELERQQKEVEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH--- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 118 lkdqiqdvegrymqglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELE 197
Cdd:pfam09738  94 ---------------------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 198 RQKHMCSVLQHKMEELKEGLRQRDELIeekqrmqqkidtmtkevfdlqetllwkdkkigalekqkeyiaclrnerdmlre 277
Cdd:pfam09738 153 RLKRNLRRLQFQLAELKEQLKQRDELI----------------------------------------------------- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 278 eladlqetvktgEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKL 357
Cdd:pfam09738 180 ------------EKHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKL 247
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034636413 358 QLEEERQ-KCSRNDGTVGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDITT 414
Cdd:pfam09738 248 QLEEEKSkRNSTRSSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
87-465 1.49e-08

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: 57.39  E-value: 1.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413   87 LSGNSSRRGSGDTSSLIDPDTSLSELRDIYDLKDQ---IQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNN 163
Cdd:TIGR02169  655 MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRElssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  164 LIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQrdELIEEKQRMQQKIDtmtKEVFD 243
Cdd:TIGR02169  735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLE---EEVSR 809
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  244 LQETLLWKDKKIGALEKQKEYiacLRNERDMLREELADLQETVKTGEKhglviipdgtpNGDVSHEPVAGAITVVSQEAA 323
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIKSIEK-----------EIENLNGKKEELEEELEELEA 875
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  324 QVLEsagegpLDVRLRKLAGEKEELLSQIRKLKL---QLEEERQKCSRNDGTVGDLAGLQNGsDLQFIEMQRDANRQISE 400
Cdd:TIGR02169  876 ALRD------LESRLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEE-ELSEIEDPKGEDEEIPE 948
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034636413  401 YKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 465
Cdd:TIGR02169  949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
133-464 4.59e-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: 52.75  E-value: 4.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  133 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 212
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  213 LKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQETLlwkDKKIGALEKQKEYIACLRNERDMLREELADLQETVKTGEKh 292
Cdd:TIGR02168  759 LEA---EIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLER- 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  293 glviipdgtpngdvSHEPVAGAITVVSQEAAQVLEsagegpldvRLRKLAGEKEELLSQIRKLKLQLE---EERQKCSRN 369
Cdd:TIGR02168  832 --------------RIAATERRLEDLEEQIEELSE---------DIESLAAEIEELEELIEELESELEallNERASLEEA 888
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  370 DGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVL-RYKTAAENAEKVEDELKAEKR 448
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEE 968
                          330
                   ....*....|....*.
gi 1034636413  449 KLQRELRTALDKIEEM 464
Cdd:TIGR02168  969 EARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
133-464 4.26e-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: 49.67  E-value: 4.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  133 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 212
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  213 LKEGLRQ----RDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALE----KQKEYIACLRNERDMLREELADLQE 284
Cdd:TIGR02168  766 LEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaaNLRERLESLERRIAATERRLEDLEE 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  285 TVKTGEKHGLVI---IPDGTPNGDVSHEPVAGAITVV-SQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLE 360
Cdd:TIGR02168  846 QIEELSEDIESLaaeIEELEELIEELESELEALLNERaSLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  361 EERQKCSrndGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVE 440
Cdd:TIGR02168  926 QLELRLE---GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERY 1002
                          330       340
                   ....*....|....*....|....
gi 1034636413  441 DELKAEKRKLQRELRTALDKIEEM 464
Cdd:TIGR02168 1003 DFLTAQKEDLTEAKETLEEAIEEI 1026
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
134-486 6.65e-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: 48.91  E-value: 6.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  134 KELKESLSEVEEKYKKamvsnaqLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEEL 213
Cdd:TIGR02169  670 RSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  214 KEGLRQRDELIEEKQRMQQKIDtmtKEVFDLQETLLWKDKKIGALEKQ--KEYIACLRNERDMLREELADLQETVKTGEK 291
Cdd:TIGR02169  743 EEDLSSLEQEIENVKSELKELE---ARIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  292 hglvIIPDGTPNGDVSHEPVAGAItvvsqeaAQVLEsagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDG 371
Cdd:TIGR02169  820 ----KLNRLTLEKEYLEKEIQELQ-------EQRID------LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  372 TVGDLAGLQNGSDLQFIEMQR---DANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENaEKVEDELKAEKR 448
Cdd:TIGR02169  883 RLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQ 961
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1034636413  449 KLQRELRT-------ALDKIEEMEMTNSHLAKRLEKMKANRTALL 486
Cdd:TIGR02169  962 RVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
133-455 8.70e-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: 45.43  E-value: 8.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  133 LKELKESLSEVEEKYKKAmVSNAQLDNEKNNLiyQVDTLKDVIEEQEEQMAEF---YRENEEKSKELERQKHMcsvLQHK 209
Cdd:TIGR02168  195 LNELERQLKSLERQAEKA-ERYKELKAELREL--ELALLVLRLEELREELEELqeeLKEAEEELEELTAELQE---LEEK 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  210 MEELKEGLRQRDELIEEKQR----MQQKIDTMTKEVFDLQETLLWKDKKIGALEkqkEYIACLRNERDMLREELADLQET 285
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANLERQLEELE---AQLEELESKLDELAEELAELEEK 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  286 VKTGEKhglviipdgtpngdvSHEPVAGAITvVSQEAAQVLESAGEGpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQK 365
Cdd:TIGR02168  346 LEELKE---------------ELESLEAELE-ELEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  366 CSRNDGTVGDLAGLQNGSDLQFIEMQRDA-NRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELK 444
Cdd:TIGR02168  409 LERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
                          330
                   ....*....|.
gi 1034636413  445 AEKRKLQRELR 455
Cdd:TIGR02168  489 ARLDSLERLQE 499
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
187-436 1.31e-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: 43.98  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 187 RENEEKSKELERQkhmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQkeyIA 266
Cdd:COG4942    23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 267 CLRNERDMLREELAD-LQETVKTGEKHGL-VIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpldvRLRKLAGE 344
Cdd:COG4942    94 ELRAELEAQKEELAElLRALYRLGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 345 KEELLSQIRKLKLQLEEERQKcsrndgtvgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEG 424
Cdd:COG4942   169 LEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
                         250
                  ....*....|..
gi 1034636413 425 QVLRYKTAAENA 436
Cdd:COG4942   235 EAAAAAERTPAA 246
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
334-480 3.65e-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: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  334 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCsrnDGTVGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 412
Cdd:COG4913    293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034636413  413 TTLEQSI-----------SRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 480
Cdd:COG4913    369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
116-291 5.19e-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: 42.74  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  116 YDLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKE 195
Cdd:TIGR02168  291 YALANEISRLEQQ----KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  196 LErqkhmcsVLQHKMEELKEGL-RQRDELIEEKQRMQQ---KIDTMTKEVFDLQETL---------LWKDKKIGALEKQK 262
Cdd:TIGR02168  367 LE-------ELESRLEELEEQLeTLRSKVAQLELQIASlnnEIERLEARLERLEDRRerlqqeieeLLKKLEEAELKELQ 439
                          170       180
                   ....*....|....*....|....*....
gi 1034636413  263 EYIACLRNERDMLREELADLQETVKTGEK 291
Cdd:TIGR02168  440 AELEELEEELEELQEELERLEEALEELRE 468
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
114-333 5.24e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 114 DIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEFYRENE 190
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEalqAEIDKLQAEIAEAEAEIEERREELGERARALY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 191 EKSKE----------------LERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllwKDKK 254
Cdd:COG3883    97 RSGGSvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---KAEL 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034636413 255 IGALEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGP 333
Cdd:COG3883   174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
337-489 6.27e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 337 RLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAglqngsdlqfiEMQRDANRQISEYKFKLSKAEQDITTLE 416
Cdd:COG1196   289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-----------EELEELEEELEELEEELEEAEEELEEAE 357
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034636413 417 QSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 489
Cdd:COG1196   358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
167-480 1.53e-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: 41.21  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  167 QVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVlqhkmeELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQE 246
Cdd:TIGR02169  185 NIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY------EGYELLKEKEALERQKEAIERQLASLEEELEKLTE 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  247 TLLWKDKKIGALEKQKEYIAclRNERDMLREELADLQETVKTGEkhglviipdgtpngdVSHEPVAGAITVVSQEAAQvl 326
Cdd:TIGR02169  259 EISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELE---------------AEIASLERSIAEKERELED-- 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  327 esagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNG--SDLQFIEMQRDANRQ-ISEYKF 403
Cdd:TIGR02169  320 -------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlrAELEEVDKEFAETRDeLKDYRE 392
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034636413  404 KLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 480
Cdd:TIGR02169  393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
334-489 1.83e-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: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  334 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlQFIEMQRDANRQISEYKFKLSKAEQDIT 413
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISRLEQQKQILRERLANLERQLE 319
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034636413  414 TLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 489
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
267-489 2.49e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  267 CLRNERDMLREELADLQETVKTGEKhglviipdgtpngdvshepvagAITVVSQEAAQVLEsagegpldvRLRKLAGEKE 346
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEK----------------------ALAELRKELEELEE---------ELEQLRKELE 722
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  347 ELLSQIRKLKLQLEEERQKCSRndgtVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQV 426
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034636413  427 LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 489
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
389-480 3.48e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 389 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKtaAENA-------------EKVEDELKAEKRKLQRELR 455
Cdd:COG2433   385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--AEVEeleaeleekderiERLERELSEARSEERREIR 462
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034636413 456 -----TALD--------KIEEMEMTNSHLAKRLEKMKA 480
Cdd:COG2433   463 kdreiSRLDreierlerELEEERERIEELKRKLERLKE 500
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
334-488 3.93e-03

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: 39.36  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 334 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNdGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKfklskaEQDIT 413
Cdd:COG4942    81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR------REQAE 153
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034636413 414 TLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 488
Cdd:COG4942   154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
117-291 4.07e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.49  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 117 DLKDQIQDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 196
Cdd:pfam07888  77 ELESRVAELK----EELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 197 ERQKhmcsvlqhkmEELKEGLRQRDELIEEKQRMQQKIDTMTKEV----FDLQETLLWKDKKIGALEKQKEYIACLRN-- 270
Cdd:pfam07888 153 ERMK----------ERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslsKEFQELRNSLAQRDTQVLQLQDTITTLTQkl 222
                         170       180
                  ....*....|....*....|....*....
gi 1034636413 271 --------ERDMLREELADLQETVKTGEK 291
Cdd:pfam07888 223 ttahrkeaENEALLEELRSLQERLNASER 251
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
165-265 5.94e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.42  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413 165 IYQVDTLK--DVI---EEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEglrQRDELIEE-KQRMQQKIDTMT 238
Cdd:PRK00409  510 LIGEDKEKlnELIaslEELERELEQKAEEAEALLKEAEKLK---EELEEKKEKLQE---EEDKLLEEaEKEAQQAIKEAK 583
                          90       100
                  ....*....|....*....|....*..
gi 1034636413 239 KEVFDLQETLLWKDKKIGALEKQKEYI 265
Cdd:PRK00409  584 KEADEIIKELRQLQKGGYASVKAHELI 610
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
183-466 9.00e-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: 38.90  E-value: 9.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  183 AEFYRENEEKSKELERQKHMCSVLQHKMEELKEglrQRDELIEEKQRmQQKIDTMTKEVFDLQETLLWKDKKigALEKQK 262
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREK-AERYQALLKEKREYEGYELLKEKE--ALERQK 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  263 EYIaclRNERDMLREELADLQETVKTGEKHglviipdgtpngdvshepVAGAITVVSQEAAQVLESAGEGPLDVR--LRK 340
Cdd:TIGR02169  240 EAI---ERQLASLEEELEKLTEEISELEKR------------------LEEIEQLLEELNKKIKDLGEEEQLRVKekIGE 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  341 LAGEKEELLSQIRKLKLQLE----EERQKCSRNDGTVGDLAGLQngSDLQFIEMQRDA-NRQISEYKFKLSKAEQDITTL 415
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEdaeeRLAKLEAEIDKLLAEIEELE--REIEEERKRRDKlTEEYAELKEELEDLRAELEEV 376
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034636413  416 EQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEM 466
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
258-485 9.33e-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: 38.88  E-value: 9.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  258 LEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLviipdgtpngDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVR 337
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELE----------ELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  338 LRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQ----------ISEYKFKLSK 407
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlrerLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636413  408 AEQDITTLEQSISRLEGQVLR-------YKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 480
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESlaaeieeLEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915

                   ....*
gi 1034636413  481 NRTAL 485
Cdd:TIGR02168  916 ELEEL 920
 
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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