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Conserved domains on  [gi|530373325|ref|XP_005265608|]
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leucine-rich repeat flightless-interacting protein 2 isoform X18 [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 ...
47-465 6.74e-101

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: 306.62  E-value: 6.74e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   47 DIRMRELERQQKEyslhsfdrkwgqiqkwledseraryshrsshhrpylgvedalsirsvgshrLDEKSDKQYAENYT-- 124
Cdd:pfam09738  17 EIRMRELERQQKE---------------------------------------------------VEENADRVFDMSSSsg 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  125 -------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqiqdvegrymqglkelkeSLSEVEEK 197
Cdd:pfam09738  46 adtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH------------------------ELKEVEEK 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  198 YKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIee 277
Cdd:pfam09738 102 YRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELI-- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  278 kqrmqqkidtmtkevfdlqetllwkdkkigalekqkeyiaclrnerdmlreeladlqetvktgEKHGLVIIPDGTPNGDV 357
Cdd:pfam09738 180 ---------------------------------------------------------------EKHGLVIVPDENTNGEE 196
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  358 SHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ-KCSRNDGTVGDLAGLQNGSDL 436
Cdd:pfam09738 197 ENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTRSSQSPDGFGLENGSHV 276
                         410       420
                  ....*....|....*....|....*....
gi 530373325  437 qfIEMQRDANRQISEYKFKLSKAEQDITT 465
Cdd:pfam09738 277 --IEVQREANKQISDYKFKLQKAEQEITT 303
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
440-531 2.90e-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: 40.23  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 440 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKtaAENA-------------EKVEDELKAEKRKLQRELR 506
Cdd:COG2433  385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--AEVEeleaeleekderiERLERELSEARSEERREIR 462
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 530373325 507 -----TALD--------KIEEMEMTNSHLAKRLEKMKA 531
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 ...
47-465 6.74e-101

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: 306.62  E-value: 6.74e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   47 DIRMRELERQQKEyslhsfdrkwgqiqkwledseraryshrsshhrpylgvedalsirsvgshrLDEKSDKQYAENYT-- 124
Cdd:pfam09738  17 EIRMRELERQQKE---------------------------------------------------VEENADRVFDMSSSsg 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  125 -------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqiqdvegrymqglkelkeSLSEVEEK 197
Cdd:pfam09738  46 adtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH------------------------ELKEVEEK 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  198 YKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIee 277
Cdd:pfam09738 102 YRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELI-- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  278 kqrmqqkidtmtkevfdlqetllwkdkkigalekqkeyiaclrnerdmlreeladlqetvktgEKHGLVIIPDGTPNGDV 357
Cdd:pfam09738 180 ---------------------------------------------------------------EKHGLVIVPDENTNGEE 196
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  358 SHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ-KCSRNDGTVGDLAGLQNGSDL 436
Cdd:pfam09738 197 ENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTRSSQSPDGFGLENGSHV 276
                         410       420
                  ....*....|....*....|....*....
gi 530373325  437 qfIEMQRDANRQISEYKFKLSKAEQDITT 465
Cdd:pfam09738 277 --IEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
138-516 2.50e-09

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: 60.08  E-value: 2.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   138 LSGNSSRRGSGDTSSLIDPDTSLSELRDIYDLKDQ---IQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNN 214
Cdd:TIGR02169  655 MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRElssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   215 LIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQrdELIEEKQRMQQKIDtmtKEVFD 294
Cdd:TIGR02169  735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLE---EEVSR 809
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   295 LQETLLWKDKKIGALEKQKEYiacLRNERDMLREELADLQETVKTGEKhglviipdgtpNGDVSHEPVAGAITVVSQEAA 374
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIKSIEK-----------EIENLNGKKEELEEELEELEA 875
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   375 QVLEsagegpLDVRLRKLAGEKEELLSQIRKLKL---QLEEERQKCSRNDGTVGDLAGLQNGsDLQFIEMQRDANRQISE 451
Cdd:TIGR02169  876 ALRD------LESRLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEE-ELSEIEDPKGEDEEIPE 948
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530373325   452 YKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 516
Cdd:TIGR02169  949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
238-487 3.89e-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: 45.91  E-value: 3.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 238 RENEEKSKELERQkhmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQkeyIA 317
Cdd:COG4942   23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 318 CLRNERDMLREELAD-LQETVKTGEKHGL-VIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpldvRLRKLAGE 395
Cdd:COG4942   94 ELRAELEAQKEELAElLRALYRLGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 396 KEELLSQIRKLKLQLEEERQKcsrndgtvgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEG 475
Cdd:COG4942  169 LEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
                        250
                 ....*....|..
gi 530373325 476 QVLRYKTAAENA 487
Cdd:COG4942  235 EAAAAAERTPAA 246
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
168-531 5.80e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 168 DLKDQIQDVE--------GRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEF 236
Cdd:PRK02224 191 QLKAQIEEKEekdlherlNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAET 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 237 YRENEEKSKELERQKHMCSVLqhkmEELKEGLRQRDELIE-EKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEy 315
Cdd:PRK02224 271 EREREELAEEVRDLRERLEEL----EEERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE- 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 316 iaCLRNERDMLREELADLQETVKTGEKhglviipdGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPldVRLRKLAGE 395
Cdd:PRK02224 346 --SLREDADDLEERAEELREEAAELES--------ELEEAREAVEDRREEIEELEEEIEELRERFGDAP--VDLGNAEDF 413
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 396 KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDL----QFIEMQRDANRqISEYKFKLSKAEQDITTLEQSIS 471
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgQPVEGSPHVET-IEEDRERVEELEAELEDLEEEVE 492
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530373325 472 RLEGQVLRYKTAAENAEKVEDelKAEKRKLQRELR-TALDKIEEMEMTNSHLAKRLEKMKA 531
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIER--LEERREDLEELIaERRETIEEKRERAEELRERAAELEA 551
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
440-531 2.90e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 440 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKtaAENA-------------EKVEDELKAEKRKLQRELR 506
Cdd:COG2433  385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--AEVEeleaeleekderiERLERELSEARSEERREIR 462
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 530373325 507 -----TALD--------KIEEMEMTNSHLAKRLEKMKA 531
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 ...
47-465 6.74e-101

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: 306.62  E-value: 6.74e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   47 DIRMRELERQQKEyslhsfdrkwgqiqkwledseraryshrsshhrpylgvedalsirsvgshrLDEKSDKQYAENYT-- 124
Cdd:pfam09738  17 EIRMRELERQQKE---------------------------------------------------VEENADRVFDMSSSsg 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  125 -------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqiqdvegrymqglkelkeSLSEVEEK 197
Cdd:pfam09738  46 adtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH------------------------ELKEVEEK 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  198 YKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIee 277
Cdd:pfam09738 102 YRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELI-- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  278 kqrmqqkidtmtkevfdlqetllwkdkkigalekqkeyiaclrnerdmlreeladlqetvktgEKHGLVIIPDGTPNGDV 357
Cdd:pfam09738 180 ---------------------------------------------------------------EKHGLVIVPDENTNGEE 196
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  358 SHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ-KCSRNDGTVGDLAGLQNGSDL 436
Cdd:pfam09738 197 ENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTRSSQSPDGFGLENGSHV 276
                         410       420
                  ....*....|....*....|....*....
gi 530373325  437 qfIEMQRDANRQISEYKFKLSKAEQDITT 465
Cdd:pfam09738 277 --IEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
138-516 2.50e-09

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: 60.08  E-value: 2.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   138 LSGNSSRRGSGDTSSLIDPDTSLSELRDIYDLKDQ---IQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNN 214
Cdd:TIGR02169  655 MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRElssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   215 LIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQrdELIEEKQRMQQKIDtmtKEVFD 294
Cdd:TIGR02169  735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLE---EEVSR 809
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   295 LQETLLWKDKKIGALEKQKEYiacLRNERDMLREELADLQETVKTGEKhglviipdgtpNGDVSHEPVAGAITVVSQEAA 374
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIKSIEK-----------EIENLNGKKEELEEELEELEA 875
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   375 QVLEsagegpLDVRLRKLAGEKEELLSQIRKLKL---QLEEERQKCSRNDGTVGDLAGLQNGsDLQFIEMQRDANRQISE 451
Cdd:TIGR02169  876 ALRD------LESRLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEE-ELSEIEDPKGEDEEIPE 948
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530373325   452 YKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 516
Cdd:TIGR02169  949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
184-515 9.34e-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: 55.06  E-value: 9.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   184 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 263
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   264 LKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQETLlwkDKKIGALEKQKEYIACLRNERDMLREELADLQETVKTGEKh 343
Cdd:TIGR02168  759 LEA---EIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLER- 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   344 glviipdgtpngdvSHEPVAGAITVVSQEAAQVLESAGEgpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGT 423
Cdd:TIGR02168  832 --------------RIAATERRLEDLEEQIEELSEDIES--LAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   424 VGDLAGLQNGSDLQFIEMQRD---ANRQISEYKFKLSKAEQDITTLEQSISRlegqvlRYKTAAENAEKVEDELKAEKRK 500
Cdd:TIGR02168  896 LEELSEELRELESKRSELRREleeLREKLAQLELRLEGLEVRIDNLQERLSE------EYSLTLEEAEALENKIEDDEEE 969
                          330
                   ....*....|....*
gi 530373325   501 LQRELRTALDKIEEM 515
Cdd:TIGR02168  970 ARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
164-515 1.04e-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: 51.60  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   164 RDIYDLKDQIQDVEGRYMQGLKELKESLSEVEEkYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEK 243
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEE-LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   244 SKELERQKhmcSVLQHKMEELKEGLrqrDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALE----KQKEYIACL 319
Cdd:TIGR02168  756 LTELEAEI---EELEERLEEAEEEL---AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaaNLRERLESL 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   320 RNERDMLREELADLQETVKTGEKHGLVI---IPDGTPNGDVSHEPVAGAITVV-SQEAAQVLESAGEGPLDVRLRKLAGE 395
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERaSLEEALALLRSELEELSEELRELESK 909
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   396 KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLagLQNGSDLQFIEMQrDANRQISEYKFKLSKAEQDITTLEQSISRLEG 475
Cdd:TIGR02168  910 RSELRRELEELREKLAQLELRLEGLEVRIDNL--QERLSEEYSLTLE-EAEALENKIEDDEEEARRRLKRLENKIKELGP 986
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 530373325   476 QVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEM 515
Cdd:TIGR02168  987 VNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
184-516 1.20e-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: 48.13  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   184 LKELKESL------SEVEEKYKkamvsnaQLDNEKNNLiyQVDTLKDVIEEQEEQMAEF---YRENEEKSKELERQKHMc 254
Cdd:TIGR02168  195 LNELERQLkslerqAEKAERYK-------ELKAELREL--ELALLVLRLEELREELEELqeeLKEAEEELEELTAELQE- 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   255 svLQHKMEELKEGLRQRDELIEEKQR----MQQKIDTMTKEVFDLQETLLWKDKKIGALEkqkEYIACLRNERDMLREEL 330
Cdd:TIGR02168  265 --LEEKLEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANLERQLEELE---AQLEELESKLDELAEEL 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   331 ADLQETVKTGEKhglviipdgtpngdvSHEPVAGAITvVSQEAAQVLESAGEGpLDVRLRKLAGEKEELLSQIRKLKLQL 410
Cdd:TIGR02168  340 AELEEKLEELKE---------------ELESLEAELE-ELEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEI 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   411 EEERQKCSRNDGTVGdlaglqngsdlQFIEMQRDANRQISEYKFKLSKAEqdITTLEQSISRLEGQVLRYKTAAENAEKV 490
Cdd:TIGR02168  403 ERLEARLERLEDRRE-----------RLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREE 469
                          330       340
                   ....*....|....*....|....*.
gi 530373325   491 EDELKAEKRKLQRELRTALDKIEEME 516
Cdd:TIGR02168  470 LEEAEQALDAAERELAQLQARLDSLE 495
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
238-487 3.89e-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: 45.91  E-value: 3.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 238 RENEEKSKELERQkhmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQkeyIA 317
Cdd:COG4942   23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 318 CLRNERDMLREELAD-LQETVKTGEKHGL-VIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpldvRLRKLAGE 395
Cdd:COG4942   94 ELRAELEAQKEELAElLRALYRLGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 396 KEELLSQIRKLKLQLEEERQKcsrndgtvgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEG 475
Cdd:COG4942  169 LEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
                        250
                 ....*....|..
gi 530373325 476 QVLRYKTAAENA 487
Cdd:COG4942  235 EAAAAAERTPAA 246
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
165-384 1.32e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 165 DIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEFYRENE 241
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEalqAEIDKLQAEIAEAEAEIEERREELGERARALY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 242 EKSKE----------------LERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllwKDKK 305
Cdd:COG3883   97 RSGGSvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---KAEL 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373325 306 IGALEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGP 384
Cdd:COG3883  174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
167-342 1.54e-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: 44.66  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   167 YDLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKE 246
Cdd:TIGR02168  291 YALANEISRLEQQ----KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   247 LErqkhmcsVLQHKMEELKEGL-RQRDELIEEKQRMQQ---KIDTMTKEVFDLQETL---------LWKDKKIGALEKQK 313
Cdd:TIGR02168  367 LE-------ELESRLEELEEQLeTLRSKVAQLELQIASlnnEIERLEARLERLEDRRerlqqeieeLLKKLEEAELKELQ 439
                          170       180
                   ....*....|....*....|....*....
gi 530373325   314 EYIACLRNERDMLREELADLQETVKTGEK 342
Cdd:TIGR02168  440 AELEELEEELEELQEELERLEEALEELRE 468
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
170-433 1.99e-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: 44.28  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   170 KDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKN-------NLIYQVDTLKDVIEEQEEQMAEFYRENEE 242
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEE 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   243 KSKELERQKhmcSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ----KEYIAC 318
Cdd:TIGR02168  321 LEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlELQIAS 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   319 LRNERDMLREELADLQETVktgEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpLDVRLRKLAGEKEE 398
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER--LEEALEELREELEE 472
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 530373325   399 LLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNG 433
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
371-540 2.95e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 2.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 371 QEAAQVLESAGEgpldvRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAglqngsdlqfiEMQRDANRQIS 450
Cdd:COG1196  277 EELELELEEAQA-----EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-----------EELEELEEELE 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 451 EYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMK 530
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
                        170
                 ....*....|
gi 530373325 531 ANRTALLAQQ 540
Cdd:COG1196  421 EELEELEEAL 430
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
385-531 3.18e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  385 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCsrnDGTVGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 463
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373325  464 TTLEQSI-----------SRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 531
Cdd:COG4913   369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
218-531 3.87e-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: 43.52  E-value: 3.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   218 QVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVlqhkmeELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQE 297
Cdd:TIGR02169  185 NIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY------EGYELLKEKEALERQKEAIERQLASLEEELEKLTE 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   298 TLLWKDKKIGALEKQKEYIAclRNERDMLREELADLQETVktGEKHGLViipdgtpngdvshEPVAGAITVVSQEAAQvl 377
Cdd:TIGR02169  259 EISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKI--GELEAEI-------------ASLERSIAEKERELED-- 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   378 esagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNG--SDLQFIEMQRDANRQ-ISEYKF 454
Cdd:TIGR02169  320 -------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlrAELEEVDKEFAETRDeLKDYRE 392
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530373325   455 KLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 531
Cdd:TIGR02169  393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
168-531 5.80e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 168 DLKDQIQDVE--------GRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEF 236
Cdd:PRK02224 191 QLKAQIEEKEekdlherlNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAET 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 237 YRENEEKSKELERQKHMCSVLqhkmEELKEGLRQRDELIE-EKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEy 315
Cdd:PRK02224 271 EREREELAEEVRDLRERLEEL----EEERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE- 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 316 iaCLRNERDMLREELADLQETVKTGEKhglviipdGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPldVRLRKLAGE 395
Cdd:PRK02224 346 --SLREDADDLEERAEELREEAAELES--------ELEEAREAVEDRREEIEELEEEIEELRERFGDAP--VDLGNAEDF 413
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 396 KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDL----QFIEMQRDANRqISEYKFKLSKAEQDITTLEQSIS 471
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgQPVEGSPHVET-IEEDRERVEELEAELEDLEEEVE 492
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530373325 472 RLEGQVLRYKTAAENAEKVEDelKAEKRKLQRELR-TALDKIEEMEMTNSHLAKRLEKMKA 531
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIER--LEERREDLEELIaERRETIEEKRERAEELRERAAELEA 551
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
318-540 8.44e-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: 42.35  E-value: 8.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   318 CLRNERDMLREELADLQETVKTGEKhglviipdgtpngdvshepvagAITVVSQEAAQVLEsagegpldvRLRKLAGEKE 397
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEK----------------------ALAELRKELEELEE---------ELEQLRKELE 722
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   398 ELLSQIRKLKLQLEEERQKCSRndgtVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQV 477
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373325   478 LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 540
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
388-540 8.74e-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: 42.35  E-value: 8.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   388 RLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlqfiemqrDANRQISEYKFKLSKAEQDITTLE 467
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-----------RLEQQKQILRERLANLERQLEELE 322
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373325   468 QSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 540
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
168-342 1.51e-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: 41.03  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  168 DLKDQIQDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 247
Cdd:pfam07888  77 ELESRVAELK----EELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  248 ERQKhmcsvlqhkmEELKEGLRQRDELIEEKQRMQQKIDTMTKEV----FDLQETLLWKDKKIGALEKQKEYIACLRN-- 321
Cdd:pfam07888 153 ERMK----------ERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslsKEFQELRNSLAQRDTQVLQLQDTITTLTQkl 222
                         170       180
                  ....*....|....*....|....*....
gi 530373325  322 --------ERDMLREELADLQETVKTGEK 342
Cdd:pfam07888 223 ttahrkeaENEALLEELRSLQERLNASER 251
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
234-517 1.95e-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: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   234 AEFYRENEEKSKELERQKHMCSVLQHKMEELKEglrQRDELIEEKQRmQQKIDTMTKEVFDLQETLLWKDKKigALEKQK 313
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREK-AERYQALLKEKREYEGYELLKEKE--ALERQK 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   314 EYIaclRNERDMLREELADLQETVKTGEKHglviipdgtpngdvshepVAGAITVVSQEAAQVLESAGEGPLDVR--LRK 391
Cdd:TIGR02169  240 EAI---ERQLASLEEELEKLTEEISELEKR------------------LEEIEQLLEELNKKIKDLGEEEQLRVKekIGE 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   392 LAGEKEELLSQIRKLKLQLE----EERQKCSRNDGTVGDLAGLQngSDLQFIEMQRDA-NRQISEYKFKLSKAEQDITTL 466
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEdaeeRLAKLEAEIDKLLAEIEELE--REIEEERKRRDKlTEEYAELKEELEDLRAELEEV 376
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 530373325   467 EQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEM 517
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
385-539 2.09e-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: 40.52  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 385 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNdGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKfklskaEQDIT 464
Cdd:COG4942   81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR------REQAE 153
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530373325 465 TLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 539
Cdd:COG4942  154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
168-531 2.37e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 168 DLKDQIQDVEGRYMQGLKELKESLSEVE---------EKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYR 238
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPelreeleklEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 239 ENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQEtllwkdkKIGALEKQKEYIAC 318
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEE 342
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 319 LRNERDMLREELADLQETVKTGEKhglviipdgtpngdvshepvAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEE 398
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEE--------------------AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 399 LLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQI-SEYKFKLSKAEQDITTLEQSISRL---- 473
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLrkel 482
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530373325 474 ---------EGQVLRYKTAAENAEKVEDELKA----EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 531
Cdd:PRK03918 483 relekvlkkESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
385-539 2.44e-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: 39.52  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 385 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 459
Cdd:COG1579   15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 460 -----EQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEmtnSHLAKRLEKMKANRT 534
Cdd:COG1579   90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166

                 ....*
gi 530373325 535 ALLAQ 539
Cdd:COG1579  167 ELAAK 171
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
440-531 2.90e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 440 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKtaAENA-------------EKVEDELKAEKRKLQRELR 506
Cdd:COG2433  385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--AEVEeleaeleekderiERLERELSEARSEERREIR 462
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 530373325 507 -----TALD--------KIEEMEMTNSHLAKRLEKMKA 531
Cdd:COG2433  463 kdreiSRLDreierlerELEEERERIEELKRKLERLKE 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
309-536 3.23e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   309 LEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLviipdgtpngDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVR 388
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELE----------ELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   389 LRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQ----------ISEYKFKLSK 458
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlrerLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   459 AEQDITTLEQSISRLEGQVLR-------YKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 531
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESlaaeieeLEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915

                   ....*
gi 530373325   532 NRTAL 536
Cdd:TIGR02168  916 ELEEL 920
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
216-316 3.90e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 216 IYQVDTLK--DVI---EEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEglrQRDELIEE-KQRMQQKIDTMT 289
Cdd:PRK00409 510 LIGEDKEKlnELIaslEELERELEQKAEEAEALLKEAEKLK---EELEEKKEKLQE---EEDKLLEEaEKEAQQAIKEAK 583
                         90       100
                 ....*....|....*....|....*..
gi 530373325 290 KEVFDLQETLLWKDKKIGALEKQKEYI 316
Cdd:PRK00409 584 KEADEIIKELRQLQKGGYASVKAHELI 610
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
226-536 5.44e-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: 39.67  E-value: 5.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   226 IEEQEEQMAEFYRENEEKSKELER------QKHMCSVLQHKMEELK--EGLRQRDELIEEKQRMQQKIDTMTKEVFDLQE 297
Cdd:TIGR02169  179 LEEVEENIERLDLIIDEKRQQLERlrrereKAERYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTE 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   298 TLLWKDKKIGALEKQKEYIAclRNERDMLREELADLQETVK--TGEKHGLV-IIPDGTPNGDVSHEPVAGAITVVSQEAA 374
Cdd:TIGR02169  259 EISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGelEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLA 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   375 QVLESAGE-GPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKcsrNDGTVGDLAGLQNGSDlQFIEMQRDANRQISEYK 453
Cdd:TIGR02169  337 EIEELEREiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE---FAETRDELKDYREKLE-KLKREINELKRELDRLQ 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   454 FKLSKAEQDITTLEQSISRLEGQVLRYKTAAENA----EKVEDELK---AEKRKLQRELRTALDKIEEMEMTNSHLAKRL 526
Cdd:TIGR02169  413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleiKKQEWKLEqlaADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
                          330
                   ....*....|
gi 530373325   527 EKMKANRTAL 536
Cdd:TIGR02169  493 AEAEAQARAS 502
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
157-416 7.45e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.14  E-value: 7.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 157 DTSLSELRD-----IYDLKDQIQDVEGR----YMQGLKELKESLSEVEEKYKKAmvsnaqldnEKNNLIYQVDTLKDVIE 227
Cdd:PRK05771  19 DEVLEALHElgvvhIEDLKEELSNERLRklrsLLTKLSEALDKLRSYLPKLNPL---------REEKKKVSVKSLEELIK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 228 EQEEQMAEFYRENEEKSKELErqkhmcsvlqhkmeelkeglrqrdELIEEKQRMQQKIDTMTK-EVFDLQETLLWKDKKI 306
Cdd:PRK05771  90 DVEEELEKIEKEIKELEEEIS------------------------ELENEIKELEQEIERLEPwGNFDLDLSLLLGFKYV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 307 ----GALEKQKEyiaclrnERDMLREELADLQETVKTGEKHGLVIIPDgtpngdvshepvAGAITVVSQEAAQV----LE 378
Cdd:PRK05771 146 svfvGTVPEDKL-------EELKLESDVENVEYISTDKGYVYVVVVVL------------KELSDEVEEELKKLgferLE 206
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 530373325 379 SAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQK 416
Cdd:PRK05771 207 LEEEGTPSELIREIKEELEEIEKERESLLEELKELAKK 244
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
164-342 8.20e-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: 39.28  E-value: 8.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   164 RDIYDLKDQIQDVEGRYMQGLKELKESLSEVEE---KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 240
Cdd:TIGR02169  308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325   241 EEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEkqrMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIAclr 320
Cdd:TIGR02169  388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA--- 461
                          170       180
                   ....*....|....*....|..
gi 530373325   321 NERDMLREELADLQETVKTGEK 342
Cdd:TIGR02169  462 ADLSKYEQELYDLKEEYDRVEK 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
184-510 8.68e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 8.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 184 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM----AEFYRENEEKSKELERQKHMCSVLQH 259
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRRELEERLEE 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 260 KMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLlwKDKKIGALEKQKEYIACLRNERDMLREELADLQEtvkt 339
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL--AEAEEALLEAEAELAEAEEELEELAEELLEALRA---- 394
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 340 gekhglviipdgtpngdvshepvagaitvVSQEAAQVLEsagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSR 419
Cdd:COG1196  395 -----------------------------AAELAAQLEE------LEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325 420 NDGTVGDLAGLQNGSDLQfiemQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAE-KVEDELKAEK 498
Cdd:COG1196  440 EEEALEEAAEEEAELEEE----EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALL 515
                        330
                 ....*....|..
gi 530373325 499 RKLQRELRTALD 510
Cdd:COG1196  516 LAGLRGLAGAVA 527
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
168-330 9.45e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 9.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  168 DLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 247
Cdd:TIGR04523 311 ELKSELKNQEKK----LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373325  248 ERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDtmtKEVFDLQETLLWKDKKIGALEKQKEYIACLRNERDMLR 327
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE---KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463

                  ...
gi 530373325  328 EEL 330
Cdd:TIGR04523 464 ESL 466
 
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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