NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|894216300|ref|NP_001297661|]
View 

leucine-rich repeat flightless-interacting protein 1 isoform 4 [Mus musculus]

Protein Classification

leucine-rich repeat flightless-interacting protein( domain architecture ID 12101455)

leucine-rich repeat flightless-interacting protein (LRRFIP) similar to human LRRFIP2 that may function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
 235-588 3.23e-89

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: 280.04  E-value: 3.23e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  235 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKelnelkdqiqdvegkym 305
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  306 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQF 385
Cdd:pfam09738  93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  386 AEVKEALRQREEMLEeirqlqqkqagfireisdlqetiewkdkkigalerqkeffdsirserddlreetvklkeelkKHG 465
Cdd:pfam09738 166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  466 IILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--KNNKL 543
Cdd:pfam09738 184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTR 260

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 894216300  544 DLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 588
Cdd:pfam09738 261 SSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
365-472 5.93e-04

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: 42.92  E-value: 5.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 365 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRqlqqkqagfiREISDLQETIEWKDKKIGALERQKEFFDSIR 444
Cdd:COG2433  388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457

                         90       100
                 ....*....|....*....|....*...
gi 894216300 445 SERDDLREETVKLKEELKKhgiiLNSEI 472
Cdd:COG2433  458 RREIRKDREISRLDREIER----LEREL 481
DUF3450 super family cl26418
Protein of unknown function (DUF3450); This family of proteins are functionally ...
 604-663 9.16e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


The actual alignment was detected with superfamily member pfam11932:

Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 38.37  E-value: 9.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  604 RSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 663
Cdd:pfam11932  27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
 235-588 3.23e-89

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: 280.04  E-value: 3.23e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  235 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKelnelkdqiqdvegkym 305
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  306 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQF 385
Cdd:pfam09738  93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  386 AEVKEALRQREEMLEeirqlqqkqagfireisdlqetiewkdkkigalerqkeffdsirserddlreetvklkeelkKHG 465
Cdd:pfam09738 166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  466 IILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--KNNKL 543
Cdd:pfam09738 184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTR 260

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 894216300  544 DLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 588
Cdd:pfam09738 261 SSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 257-638 1.52e-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: 58.14  E-value: 1.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   257 ATLASLGGTSSRRGSGDTSISMDTEASI----REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQL 332
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSIlerrREIEELEEK--------------IEELEEKIAELEKALAELRKELEEL 710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   333 DNEktnfmyqVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAgf 412
Cdd:TIGR02168  711 EEE-------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-- 781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   413 iREISDLQETIewkdkkigalERQKEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQAptK 492
Cdd:TIGR02168  782 -AEIEELEAQI----------EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--E 848

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   493 ITKEELNALKSAGEgTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNnkLDLLRAEdgilENGTDAHVMDLQRDANRqi 572
Cdd:TIGR02168  849 ELSEDIESLAAEIE-ELEELIEELESELEALLNERASLEEALALLRSE--LEELSEE----LRELESKRSELRRELEE-- 919

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 894216300   573 sdLKFKLAKSEQEITALEQNVIRLESQVT-RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 638
Cdd:TIGR02168  920 --LREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 362-663 4.54e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 4.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 362 RQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAgfiREISDLQETIEWKDKKIGALERQKEffd 441
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIA--- 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 442 SIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETsdtvndvgyqaptkitKEELNALKSAGEGTLDVRLKKLIDERE 521
Cdd:COG1196  306 RLEERRRELEERLEELEEELAE----LEEELEELEEE----------------LEELEEELEEAEEELEEAEAELAEAEE 365

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 522 cLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILEngtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVT 601
Cdd:COG1196  366 -ALLEAEAELAEAEEELEELAEELLEALRAAAE-------------LAAQLEELEEAEEALLERLERLEEELEELEEALA 431

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 894216300 602 RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 663
Cdd:COG1196  432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
274-659 2.39e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 274 TSISMDTEASIREIKELNELKDQIQDVE---GKYMQGLKEMKDSLAEVEEKYKKAmvsnAQLDNEKTNFMYQVDTLKDML 350
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEkrlSRLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEERH 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 351 LE--LEEQLAESQRQYEEKNKEFEREKHAhsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEW--- 425
Cdd:PRK03918 362 ELyeEAKAKKEELERLKKRLTGLTPEKLE--------KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkk 433

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 426 -------------KDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKHGIILN--SEIATNGETSDTVNDVgYQAP 490
Cdd:PRK03918 434 akgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKEL-EEKL 512

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 491 TKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGqLEGRQK--NNKLDLLRAE----DGILENGTDAHVMDL 564
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKE-KLIKLKGEIKSLKKELEKLEE-LKKKLAelEKKLDELEEElaelLKELEELGFESVEEL 590

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 565 Q----------------RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDE-----LKAEKRK 623
Cdd:PRK03918 591 EerlkelepfyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLE 670

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 894216300 624 LQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 659
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
365-472 5.93e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 5.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 365 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRqlqqkqagfiREISDLQETIEWKDKKIGALERQKEFFDSIR 444
Cdd:COG2433  388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457

                         90       100
                 ....*....|....*....|....*...
gi 894216300 445 SERDDLREETVKLKEELKKhgiiLNSEI 472
Cdd:COG2433  458 RREIRKDREISRLDREIER----LEREL 481
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
 604-663 9.16e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 38.37  E-value: 9.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  604 RSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 663
Cdd:pfam11932  27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
 235-588 3.23e-89

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: 280.04  E-value: 3.23e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  235 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKelnelkdqiqdvegkym 305
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  306 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQF 385
Cdd:pfam09738  93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  386 AEVKEALRQREEMLEeirqlqqkqagfireisdlqetiewkdkkigalerqkeffdsirserddlreetvklkeelkKHG 465
Cdd:pfam09738 166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  466 IILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--KNNKL 543
Cdd:pfam09738 184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTR 260

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 894216300  544 DLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 588
Cdd:pfam09738 261 SSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 257-638 1.52e-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: 58.14  E-value: 1.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   257 ATLASLGGTSSRRGSGDTSISMDTEASI----REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQL 332
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSIlerrREIEELEEK--------------IEELEEKIAELEKALAELRKELEEL 710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   333 DNEktnfmyqVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAgf 412
Cdd:TIGR02168  711 EEE-------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-- 781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   413 iREISDLQETIewkdkkigalERQKEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQAptK 492
Cdd:TIGR02168  782 -AEIEELEAQI----------EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--E 848

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   493 ITKEELNALKSAGEgTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNnkLDLLRAEdgilENGTDAHVMDLQRDANRqi 572
Cdd:TIGR02168  849 ELSEDIESLAAEIE-ELEELIEELESELEALLNERASLEEALALLRSE--LEELSEE----LRELESKRSELRRELEE-- 919

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 894216300   573 sdLKFKLAKSEQEITALEQNVIRLESQVT-RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 638
Cdd:TIGR02168  920 --LREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 332-639 1.87e-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: 57.77  E-value: 1.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   332 LDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAG 411
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   412 firEISDLQETIEWKDKKIGALERQ--KEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVND-VGYQ 488
Cdd:TIGR02169  766 ---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElQEQR 842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   489 APTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTDAHvmdlqrDA 568
Cdd:TIGR02169  843 IDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE------KK 915

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   569 NRQISDLKFKLAKSEQEITALEQNVIRLES---QVTRYRSAAENAEKIE------------------------DELKAEK 621
Cdd:TIGR02169  916 RKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEeeiralepvnmlaiqeyeevlkrlDELKEKR 995

                          330
                   ....*....|....*...
gi 894216300   622 RKLQRELRSALDKTEELE 639
Cdd:TIGR02169  996 AKLEEERKAILERIEEYE 1013
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 386-662 7.43e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 7.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   386 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQkefFDSIRSERDDLREETVKLKEELKKhg 465
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---IAQLSKELTELEAEIEELEERLEE-- 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   466 iiLNSEIATNGETSDTVNDV--GYQAPTKITKEELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKl 543
Cdd:TIGR02168  773 --AEEELAEAEAEIEELEAQieQLKEELKALREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE- 848

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   544 dllRAEDGILEngtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRK 623
Cdd:TIGR02168  849 ---ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 894216300   624 LQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 662
Cdd:TIGR02168  913 LRREL-------EELREKLAQLELRLEGLEVRIDNLQER 944
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 366-662 3.22e-07

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: 53.92  E-value: 3.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   366 EKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKeffDSIRS 445
Cdd:TIGR02169  689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL---KELEA 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   446 ERDDLREETVKLKEELkkhgiilnseiatngetsdtvndvgyqaptkitkEELNALKSagegtlDVRLKKLIDERECLLE 525
Cdd:TIGR02169  766 RIEELEEDLHKLEEAL----------------------------------NDLEARLS------HSRIPEIQAELSKLEE 805

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   526 QIKKLKGQL-EGRQKNNKLDLLRAedgILEngtdahvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYR 604
Cdd:TIGR02169  806 EVSRIEARLrEIEQKLNRLTLEKE---YLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 894216300   605 SAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 662
Cdd:TIGR02169  875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 361-639 9.95e-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: 52.37  E-value: 9.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   361 QRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----RQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQ 436
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   437 KEFFDSIR----SERDDLREETVKLKEELkkhgiilnseiatngeTSDTVNDVGYQAPTKITKEELNALKSAgEGTLDVR 512
Cdd:TIGR02168  318 LEELEAQLeeleSKLDELAEELAELEEKL----------------EELKEELESLEAELEELEAELEELESR-LEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   513 LKKLIDERECLLEQIKKLKGQLEgRQKNNKLDLLRAEDGILENGTDAhvmdLQRDANRQISDLKFKLAKSEQEITALEQN 592
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQEIEEL----LKKLEEAELKELQAELEELEEELEELQEE 455

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 894216300   593 VIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELE 639
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 390-643 1.17e-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: 51.99  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   390 EALRQREEMLE---EIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFD----SIRSERDDLREETVKLKEELK 462
Cdd:TIGR02169  288 EQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreieEERKRRDKLTEEYAELKEELE 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   463 KhgiiLNSEIATNGETSDTvndvgyqaptkiTKEELNALKsagegtldVRLKKLIDERECLLEQIKKL---KGQLEGRQK 539
Cdd:TIGR02169  368 D----LRAELEEVDKEFAE------------TRDELKDYR--------EKLEKLKREINELKRELDRLqeeLQRLSEELA 423

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   540 NNKLDLLRAEDGILENGTDAHVMDLQ-RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRyrsaaenAEKIEDELK 618
Cdd:TIGR02169  424 DLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-------LQRELAEAE 496

                          250       260
                   ....*....|....*....|....*
gi 894216300   619 AEKRKLQRELRSALDKTEELEVSNG 643
Cdd:TIGR02169  497 AQARASEERVRGGRAVEEVLKASIQ 521
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 362-663 4.54e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 4.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 362 RQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAgfiREISDLQETIEWKDKKIGALERQKEffd 441
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIA--- 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 442 SIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETsdtvndvgyqaptkitKEELNALKSAGEGTLDVRLKKLIDERE 521
Cdd:COG1196  306 RLEERRRELEERLEELEEELAE----LEEELEELEEE----------------LEELEEELEEAEEELEEAEAELAEAEE 365

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 522 cLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILEngtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVT 601
Cdd:COG1196  366 -ALLEAEAELAEAEEELEELAEELLEALRAAAE-------------LAAQLEELEEAEEALLERLERLEEELEELEEALA 431

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 894216300 602 RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 663
Cdd:COG1196  432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
386-639 1.52e-05

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 47.21  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 386 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETiewKDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKHG 465
Cdd:COG1340    8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 466 IILNS---EIATNGETSDTVNDVGYqaPTKITKEELNALksagEGTLDVRLKKLIDEREcLLEQIKKLKGQLEGRQK--- 539
Cdd:COG1340   85 EKLNElreELDELRKELAELNKAGG--SIDKLRKEIERL----EWRQQTEVLSPEEEKE-LVEKIKELEKELEKAKKale 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 540 -NNKLDLLRAE-DGILENGTDAHvMDLQRDANrQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDEL 617
Cdd:COG1340  158 kNEKLKELRAElKELRKEAEEIH-KKIKELAE-EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235

                        250       260
                 ....*....|....*....|..
gi 894216300 618 KAEKRKLQRELRSALDKTEELE 639
Cdd:COG1340  236 QKELRELRKELKKLRKKQRALK 257
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
274-659 2.39e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 274 TSISMDTEASIREIKELNELKDQIQDVE---GKYMQGLKEMKDSLAEVEEKYKKAmvsnAQLDNEKTNFMYQVDTLKDML 350
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEkrlSRLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEERH 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 351 LE--LEEQLAESQRQYEEKNKEFEREKHAhsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEW--- 425
Cdd:PRK03918 362 ELyeEAKAKKEELERLKKRLTGLTPEKLE--------KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkk 433

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 426 -------------KDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKHGIILN--SEIATNGETSDTVNDVgYQAP 490
Cdd:PRK03918 434 akgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKEL-EEKL 512

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 491 TKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGqLEGRQK--NNKLDLLRAE----DGILENGTDAHVMDL 564
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKE-KLIKLKGEIKSLKKELEKLEE-LKKKLAelEKKLDELEEElaelLKELEELGFESVEEL 590

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 565 Q----------------RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDE-----LKAEKRK 623
Cdd:PRK03918 591 EerlkelepfyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLE 670

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 894216300 624 LQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 659
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 288-639 2.91e-05

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: 47.32  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  288 KELNELKDQIQDVEGKYMQGL-KEMKDSLAEVEEKYKkamvsnaQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEE 366
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  367 KNKEFErEKHAhsilqfqfaEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdSIRSE 446
Cdd:TIGR04523 361 KQRELE-EKQN---------EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---LLEKE 427

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  447 RDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVGYQAPTKI--TKEELNALKSAGEGT---------------- 508
Cdd:TIGR04523 428 IERLKETIIKNNSEIKD----LTNQDSVKELIIKNLDNTRESLETQLkvLSRSINKIKQNLEQKqkelkskekelkklne 503

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  509 ----LDVRLKKLIDERECLLEQIKKLKgqLEGRQKNNKLDLLRAEDGILENGTDAHVMDLQRDANRQ--------ISDLK 576
Cdd:TIGR04523 504 ekkeLEEKVKDLTKKISSLKEKIEKLE--SEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKeieelkqtQKSLK 581

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 894216300  577 FKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELE 639
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
284-654 6.40e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 6.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 284 IREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaeSQRQ 363
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKE 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 364 YEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWK---DKKIGALERQKEFF 440
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELreiEKRLSRLEEEINGI 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 441 DSIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKSAGEGTLDVRLKKLIDE- 519
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEA------KAKKEELERLKKRLTGLTPEKLEKELEEl 396

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 520 ---RECLLEQIKKL---KGQLEGRQKNNKLDL--LRAEDGIL----ENGTDAHVMDLQRDANRQISDLKFKLAKSEQEIT 587
Cdd:PRK03918 397 ekaKEEIEEEISKItarIGELKKEIKELKKAIeeLKKAKGKCpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKER 476

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 894216300 588 ALEQNVIRLE------SQVTRYRSAAENAEKIEDELKA----EKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 654
Cdd:PRK03918 477 KLRKELRELEkvlkkeSELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 279-619 1.06e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   279 DTEASIREI--------KELNELKDQIQDVEgkymQGLKEMKDSLAEVEEKYKKaMVSNAQLdnektnfmyqvdTLKDML 350
Cdd:TIGR02169  234 ALERQKEAIerqlasleEELEKLTEEISELE----KRLEEIEQLLEELNKKIKD-LGEEEQL------------RVKEKI 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   351 LELEEQLAESQRQYEEKNKEFERekhAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKI 430
Cdd:TIGR02169  297 GELEAEIASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   431 GALERQkefFDSIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETSdtvndvgyqaptKITKEELNALKSAGEGTLD 510
Cdd:TIGR02169  374 EEVDKE---FAETRDELKDYREKLEKLKREINE----LKRELDRLQEEL------------QRLSEELADLNAAIAGIEA 434

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   511 vRLKKLIDERECLLEQIKKLKGQLEGRQKNNKldllraedgilengtdahvmdlqrDANRQISDLKFKLAKSEQEITALE 590
Cdd:TIGR02169  435 -KINELEEEKEDKALEIKKQEWKLEQLAADLS------------------------KYEQELYDLKEEYDRVEKELSKLQ 489

                          330       340
                   ....*....|....*....|....*....
gi 894216300   591 QNVIRLESQVTRYRSAAENAEKIEDELKA 619
Cdd:TIGR02169  490 RELAEAEAQARASEERVRGGRAVEEVLKA 518
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
387-618 1.57e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  387 EVKEALRQREeMLEEIRQLQQKQAGFIREISDLQETIEWkdkkiGALERQKEFFDSIRSERDDLREETVKLKEELKKHgi 466
Cdd:COG4913   243 ALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  467 ilnseiatngetsdtvndvgyQAPTKITKEELNALK----SAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEGRQKNNK 542
Cdd:COG4913   315 ---------------------EARLDALREELDELEaqirGNGGDRLE-QLEREIERLERELEERERRRARLEALLAALG 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  543 LDLLRAEDGILENGTDAH------------VMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSA-AEN 609
Cdd:COG4913   373 LPLPASAEEFAALRAEAAallealeeeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlAEA 452


                  ....*....
gi 894216300  610 AEKIEDELK 618
Cdd:COG4913   453 LGLDEAELP 461
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 286-633 2.81e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 286 EIKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAMVSNAQLDNEktnfmyqVDTLKDMLLELEEQLAESQRQYE 365
Cdd:COG1196  223 KELEAELLLLKLRELEAE----LEELEAELEELEAELEELEAELAELEAE-------LEELRLELEELELELEEAQAEEY 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 366 EKNKEFEREKHAHSILQfqfAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRS 445
Cdd:COG1196  292 ELLAELARLEQDIARLE---ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 446 ERDDLREETVKLKEELKKHgiilnseiatngetsdtvndvgYQAPTKITKEELNALKSAGEgtldvRLKKLIDERECLLE 525
Cdd:COG1196  369 EAEAELAEAEEELEELAEE----------------------LLEALRAAAELAAQLEELEE-----AEEALLERLERLEE 421

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 526 QIKKLKGQLEgRQKNNKLDLLRAEDGILEngTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRS 605
Cdd:COG1196  422 ELEELEEALA-ELEEEEEEEEEALEEAAE--EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498

                        330       340
                 ....*....|....*....|....*....
gi 894216300 606 AAENAE-KIEDELKAEKRKLQRELRSALD 633
Cdd:COG1196  499 AEADYEgFLEGVKAALLLAGLRGLAGAVA 527
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 281-555 3.06e-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: 3.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   281 EASIREIKELNELKDQIQdvegkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 360
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   361 QRQYEEKNKEFEREKhahsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEff 440
Cdd:TIGR02168  343 EEKLEELKEELESLE----------AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-- 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   441 dSIRSERDDLREETVKLKEELKKHGIilnSEIATNGETsdtvndvgyqaptkiTKEELNALKSAGEgTLDVRLKKLIDER 520
Cdd:TIGR02168  411 -RLEDRRERLQQEIEELLKKLEEAEL---KELQAELEE---------------LEEELEELQEELE-RLEEALEELREEL 470

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 894216300   521 ECLLEQIKKLKGQLEgrQKNNKLDLLRAEDGILEN 555
Cdd:TIGR02168  471 EEAEQALDAAERELA--QLQARLDSLERLQENLEG 503
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
284-638 5.22e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 5.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 284 IREIKELNELKDQIQDVEGKYmqglKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES--Q 361
Cdd:COG4717   70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAelP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 362 RQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQ-AGFIREISDLQETIEWKDKKIGALERQKEff 440
Cdd:COG4717  146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE-- 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 441 dSIRSERDDLREETV--KLKEELKKHGIILNSEIAtngetsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLID 518
Cdd:COG4717  224 -ELEEELEQLENELEaaALEERLKEARLLLLIAAA-------LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAR 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 519 ERECLLEQIKKLKGQLEGRQ-KNNKLDLLRAEDGILENGTDAHVMDLQrdanRQISDLKFKLAKSEQEITALEQNVIRLE 597
Cdd:COG4717  296 EKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELL----DRIEELQELLREAEELEEELQLEELEQE 371

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 894216300 598 SQ----------VTRYRSAAENAEKIEdELKAEKRKLQRELRSALDKTEEL 638
Cdd:COG4717  372 IAallaeagvedEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEEL 421
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 414-659 5.84e-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: 42.83  E-value: 5.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 414 REISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEELKKhgiilnseiatngetsdtvndvgyqaptki 493
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA------------------------------ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 494 TKEELNALKSagegtldvRLKKLIDERECLLEQIKKLKGQLEGR----QKNNKLDLLRaedgILENGTDAhvmdlqRDAN 569
Cdd:COG4942   74 LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPLA----LLLSPEDF------LDAV 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 570 RQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRL 649
Cdd:COG4942  136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215

                        250
                 ....*....|
gi 894216300 650 EKMKANRSAL 659
Cdd:COG4942  216 AELQQEAEEL 225
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
365-472 5.93e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 5.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 365 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRqlqqkqagfiREISDLQETIEWKDKKIGALERQKEFFDSIR 444
Cdd:COG2433  388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457

                         90       100
                 ....*....|....*....|....*...
gi 894216300 445 SERDDLREETVKLKEELKKhgiiLNSEI 472
Cdd:COG2433  458 RREIRKDREISRLDREIER----LEREL 481
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 508-637 7.63e-04

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: 41.45  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 508 TLDVRLKKLIDERECLLEQIKKLKGQLEGRQK-----NNKLDLLRAEDGILENGTDAHVMDLQRD--------ANRQISD 574
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 894216300 575 LKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 637
Cdd:COG1579   94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
288-656 7.95e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 7.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 288 KELNELKDQIQDVE-GKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLE--------LEEQLA 358
Cdd:PRK03918 372 EELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRK 451

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 359 ESQRQYEEKNKEFEREKhahsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGFI--REISDLQETIEWKDKKIGA--LE 434
Cdd:PRK03918 452 ELLEEYTAELKRIEKEL----------KEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLeeLE 521

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 435 RQKEFFDSIRSERDDLREETVKLKEELKKhGIILNSEIATNGETSDTVndvgyQAPTKITKEELNALKSAGEGTLDVRLK 514
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAELEKKLDEL-----EEELAELLKELEELGFESVEELEERLK 595

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 515 KL--IDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTDAhvmdlqRDANRQISDLKFKLakSEQEITALEQN 592
Cdd:PRK03918 596 ELepFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL------EELRKELEELEKKY--SEEEYEELREE 667

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 894216300 593 VIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 656
Cdd:PRK03918 668 YLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 384-663 8.59e-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: 8.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 384 QFAEVKEALRQRE--EMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEEL 461
Cdd:COG1196  214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEE 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 462 kkhgiilnseiatngetsdtvndvgyqaptkitkEELNALKSAGEGTLDVRLKKLIDEREcLLEQIKKLKGQLEGRQKNN 541
Cdd:COG1196  291 ----------------------------------YELLAELARLEQDIARLEERRRELEE-RLEELEEELAELEEELEEL 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 542 KLDLLRAEDgilengtdahvmdlqrdanrqisdlkfKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEK 621
Cdd:COG1196  336 EEELEELEE---------------------------ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 894216300 622 RKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 663
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 361-657 1.16e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.27  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   361 QRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQagfirEISDLQETIEWKDKKIGALERQKEFF 440
Cdd:pfam02463  210 LEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ-----EIEKEEEKLAQVLKENKEEEKEKKLQ 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   441 DSIRSERDDLREEtVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLdvRLKKLIDER 520
Cdd:pfam02463  285 EEELKLLAKEEEE-LKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE--AEEEEEEEL 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   521 ECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQV 600
Cdd:pfam02463  362 EKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 894216300   601 TRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 657
Cdd:pfam02463  442 KQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 379-555 1.29e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.84  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 379 SILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQ--ETIEWKDKKIGALERQKEFFDSIRSErddlreetvk 456
Cdd:PRK05771  86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVGTVPED---------- 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 457 LKEELKKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELN-----ALKSAGEGTLDVRLKKLIDERECLLEQIKKLK 531
Cdd:PRK05771 156 KLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKklgfeRLELEEEGTPSELIREIKEELEEIEKERESLL 235

                        170       180
                 ....*....|....*....|....*
gi 894216300 532 GQLEgrQKNNKL-DLLRAEDGILEN 555
Cdd:PRK05771 236 EELK--ELAKKYlEELLALYEYLEI 258
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
365-555 1.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 365 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIR 444
Cdd:COG4717   53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 445 sERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEGTLDVRLKKLIDERECLL 524
Cdd:COG4717  133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205

                        170       180       190
                 ....*....|....*....|....*....|.
gi 894216300 525 EQIKKLKGQLEgrQKNNKLDLLRAEDGILEN 555
Cdd:COG4717  206 QRLAELEEELE--EAQEELEELEEELEQLEN 234
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 389-663 1.60e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.96  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  389 KEALRQREEMLEEIRQLQQKQAgfireISDLQETIEWKDKKIGALERQKEFFDSIrserDDLREETVKLKEELKKHgiil 468
Cdd:PRK10929   25 EKQITQELEQAKAAKTPAQAEI-----VEALQSALNWLEERKGSLERAKQYQQVI----DNFPKLSAELRQQLNNE---- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  469 nseiatngetSDTVNDVgyqaPTKITKEELNalksagEGTLDVRLKKLIDERECLLEQ-----IKKLKGQLEGRQKNNKL 543
Cdd:PRK10929   92 ----------RDEPRSV----PPNMSTDALE------QEILQVSSQLLEKSRQAQQEQdrareISDSLSQLPQQQTEARR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  544 DLLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITAL----EQNVIRLESQVTRYRSaaenaEKIEDELKA 619
Cdd:PRK10929  152 QLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLsannRQELARLRSELAKKRS-----QQLDAYLQA 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 894216300  620 EKRKL----QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 663
Cdd:PRK10929  227 LRNQLnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 287-663 2.09e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.58  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   287 IKELNELKDQIQDVE---GKYMQGLKEMkDSLAEVEEKYKKAMVSNAQLDNEKTNF----------MYQVDTLKDMLLEL 353
Cdd:TIGR01612 1249 IEDLDEIKEKSPEIEnemGIEMDIKAEM-ETFNISHDDDKDHHIISKKHDENISDIrekslkiiedFSEESDINDIKKEL 1327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   354 EEQLAESQRQYEEKNKEFEREKHAHSILQFQ-----FAEVKEALRQREEMLEEIRQLQQKQAGFIREISD---------- 418
Cdd:TIGR01612 1328 QKNLLDAQKHNSDINLYLNEIANIYNILKLNkikkiIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDdinleecksk 1407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   419 LQETIEWKDKKiGALERQKEFFDSIRSERDDLREETVKLKEELKKHGIILNS-EIATNG-------ETSDTVNDVGYQap 490
Cdd:TIGR01612 1408 IESTLDDKDID-ECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNiEMADNKsqhilkiKKDNATNDHDFN-- 1484

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   491 tkITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEgrqknNKLDLLRAEDGILENGTDAH-VMDLQRDAN 569
Cdd:TIGR01612 1485 --INELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELL-----NKYSALAIKNKFAKTKKDSEiIIKEIKDAH 1557

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   570 RQISdlkFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKL------QRELRSALDKTEELE--VS 641
Cdd:TIGR01612 1558 KKFI---LEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFlkisdiKKKINDCLKETESIEkkIS 1634

                          410       420
                   ....*....|....*....|..
gi 894216300   642 NGHLVKRLEKMKANRSALLSQQ 663
Cdd:TIGR01612 1635 SFSIDSQDTELKENGDNLNSLQ 1656
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 359-612 2.75e-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: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 359 ESQRQYEEKNKEFEREKhahsilqfqfaevkealRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKE 438
Cdd:COG4942   31 QLQQEIAELEKELAALK-----------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 439 ffdSIRSERDDLREETVKLKEELKKHGIILNSEIATNGET-SDTVNDVGY-QAPTKITKEELNALKSAGEgtldvRLKKL 516
Cdd:COG4942   94 ---ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYlKYLAPARREQAEELRADLA-----ELAAL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 517 IDERECLLEQIKKLKGQLEGRQKnnKLDLLRAEdgilengtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRL 596
Cdd:COG4942  166 RAELEAERAELEALLAELEEERA--ALEALKAE------------------RQKLLARLEKELAELAAELAELQQEAEEL 225

                        250
                 ....*....|....*.
gi 894216300 597 ESQVTRYRSAAENAEK 612
Cdd:COG4942  226 EALIARLEAEAAAAAE 241
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 381-662 2.84e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.87  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   381 LQFQFAE---VKEALRQR-EEMLEEIRQ-------LQQKQAGFIREISD----LQETIEWKDKKIGALERqkeffdsIRS 445
Cdd:pfam15921  553 LKLQMAEkdkVIEILRQQiENMTQLVGQhgrtagaMQVEKAQLEKEINDrrleLQEFKILKDKKDAKIRE-------LEA 625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   446 ERDDLREETVKLKEELKKHgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKSAGEgtldVRLKKLIDERECLLE 525
Cdd:pfam15921  626 RVSDLELEKVKLVNAGSER---LRAVKDIKQERDQLLNEV------KTSRNELNSLSEDYE----VLKRNFRNKSEEMET 692

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   526 QIKKLKGQLEGRQknNKLDLLRAEDGILEnGTDAHVMDLQRDANRQISdlkfklAKSEQeITALEQNVIRLESQVTryrs 605
Cdd:pfam15921  693 TTNKLKMQLKSAQ--SELEQTRNTLKSME-GSDGHAMKVAMGMQKQIT------AKRGQ-IDALQSKIQFLEEAMT---- 758

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 894216300   606 aaeNAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 662
Cdd:pfam15921  759 ---NANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
427-641 3.99e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 427 DKKIGALERQKEFFDS-IRSERDDLREETVKLKEELKKHGII-LNSEIATNGETSDTVND--VGYQAPTKITKEELNALK 502
Cdd:COG3206  167 ELRREEARKALEFLEEqLPELRKELEEAEAALEEFRQKNGLVdLSEEAKLLLQQLSELESqlAEARAELAEAEARLAALR 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 503 SAGEGTLDVRLKKLIDEreclleQIKKLKGQLegrqknnkLDLLRAEDGILENGTDAH--VMDLQR---DANRQISD-LK 576
Cdd:COG3206  247 AQLGSGPDALPELLQSP------VIQQLRAQL--------AELEAELAELSARYTPNHpdVIALRAqiaALRAQLQQeAQ 312

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 894216300 577 FKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELkaekRKLQRELRSA-------LDKTEELEVS 641
Cdd:COG3206  313 RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL----RRLEREVEVArelyeslLQRLEEARLA 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 363-654 4.36e-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: 4.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   363 QYEEKNKEFEREKHAHSILQFQFAEvkealRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdS 442
Cdd:TIGR02168  214 RYKELKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE---E 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   443 IRSERDDLREETVKLKEELKkhgiilnseiatngetsdtvndvgyqaptkITKEELNALKSAGEgTLDVRLKKLIDEREC 522
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQ------------------------------ILRERLANLERQLE-ELEAQLEELESKLDE 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   523 LLEQIKKLKGQLEGRQKN-----NKLDLLRAEDGILENGtdahvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLE 597
Cdd:TIGR02168  335 LAEELAELEEKLEELKEElesleAELEELEAELEELESR--------LEELEEQLETLRSKVAQLELQIASLNNEIERLE 406

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 894216300   598 SQVT-----RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 654
Cdd:TIGR02168  407 ARLErledrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 259-452 5.09e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 5.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   259 LASLGGTSSRRGSGDTSISMDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTN 338
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   339 FMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEM-LEEIRQLQQKQAGFIREIS 417
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEAR 971

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 894216300   418 DLQETIEWKDKKIGA--------LERQKEFFDSIRSERDDLRE 452
Cdd:TIGR02168  972 RRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 286-663 5.17e-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: 40.00  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  286 EIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYE 365
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  366 EKNKEFEREKHahsilqfqfAEVKEALRQREemlEEIRQLQQKQAGFIREISDLQETIEwkdkkigalerqkeffdSIRS 445
Cdd:TIGR04523 299 DLNNQKEQDWN---------KELKSELKNQE---KKLEEIQNQISQNNKIISQLNEQIS-----------------QLKK 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  446 ERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQA---PTKITK-EELNALKsagegtlDVRLKKLIDERE 521
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIndlESKIQNqEKLNQQK-------DEQIKKLQQEKE 422

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  522 CLLEQIKKLKGQLEgrQKNNKLDLLRAEDGILENGTDAH----------VMDLQRDANRQISDLKFK---LAKSEQEITA 588
Cdd:TIGR04523 423 LLEKEIERLKETII--KNNSEIKDLTNQDSVKELIIKNLdntresletqLKVLSRSINKIKQNLEQKqkeLKSKEKELKK 500

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  589 LEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALD---------KTEELEVSNGHLVKRLEKMKANRSAL 659
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQKSL 580


                  ....
gi 894216300  660 LSQQ 663
Cdd:TIGR04523 581 KKKQ 584
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
391-589 5.31e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  391 ALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFF------DSIRSERDDLREETVKLKEElkkh 464
Cdd:COG4913   608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDAS---- 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  465 giilNSEIATNGETSDTVndvgyqaptkitKEELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLD 544
Cdd:COG4913   684 ----SDDLAALEEQLEEL------------EAELEELEEE-LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 894216300  545 L-LRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITAL 589
Cdd:COG4913   747 LrALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
290-637 8.10e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 8.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 290 LNELKDQIQDVEGK--------YMQGLKEMKDSLAEVEEKYKKAMVSNAQLD---NEKTNFMYQVDTLKDMLLELEEQLA 358
Cdd:PRK02224 189 LDQLKAQIEEKEEKdlherlngLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIA 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 359 esqrqyeeknkEFEREKHAHSilqfqfAEVKEALRQREEMLEEIRQ--------------LQQKQAGFIREISDLQETIE 424
Cdd:PRK02224 269 -----------ETEREREELA------EEVRDLRERLEELEEERDDllaeaglddadaeaVEARREELEDRDEELRDRLE 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 425 WKDKKIGALERQKEffdSIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTvndvgYQAPTKITKEELNALKSA 504
Cdd:PRK02224 332 ECRVAAQAHNEEAE---SLREDADDLEERAEELREEAAE----LESELEEAREAVED-----RREEIEELEEEIEELRER 399

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 505 GEGTlDVRLKKLIDERECLLEQikklKGQLEGRQKNNKLDLLRAEDGILENGT---------------DAHVMDLQRDAN 569
Cdd:PRK02224 400 FGDA-PVDLGNAEDFLEELREE----RDELREREAELEATLRTARERVEEAEAlleagkcpecgqpveGSPHVETIEEDR 474

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300 570 RQISDLKFKLAKSEQEITALEQNVIRL------ESQVTRYRSAAENAEKI---------EDELKAE-KRKLQRELRSALD 633
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELiaerretieEKRERAEeLRERAAELEAEAE 554


                 ....
gi 894216300 634 KTEE 637
Cdd:PRK02224 555 EKRE 558
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 499-663 8.62e-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: 39.27  E-value: 8.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   499 NALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEG--RQKNN---KLDLLRAEDGILENGTDAHVMDL------QRD 567
Cdd:TIGR02168  220 AELRELELALLVLRLEELREELEELQEELKEAEEELEEltAELQEleeKLEELRLEVSELEEEIEELQKELyalaneISR 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300   568 ANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVK 647
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379

                          170
                   ....*....|....*.
gi 894216300   648 RLEKMKANRSALLSQQ 663
Cdd:TIGR02168  380 QLETLRSKVAQLELQI 395
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
 604-663 9.16e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 38.37  E-value: 9.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216300  604 RSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 663
Cdd:pfam11932  27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH