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Conserved domains on  [gi|52486747|ref|NP_001004107|]
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transforming acidic coiled-coil-containing protein 1 [Rattus norvegicus]

Protein Classification

transforming acidic coiled-coil-containing protein( domain architecture ID 12059788)

transforming acidic coiled-coil (TACC)-containing protein similar to human TACC1 that is involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 566-765 1.18e-101

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


:

Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 311.61  E-value: 1.18e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   566 SEADKTAVLTLIREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQRTNMSSQKSFQQLTMEKEQAL 645
Cdd:pfam05010   2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   646 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKAKAE 725
Cdd:pfam05010  82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 52486747   726 SAALHAGLRREQMKVESLERALQQKNQEIEELTKICDELI 765
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 566-765 1.18e-101

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 311.61  E-value: 1.18e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   566 SEADKTAVLTLIREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQRTNMSSQKSFQQLTMEKEQAL 645
Cdd:pfam05010   2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   646 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKAKAE 725
Cdd:pfam05010  82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 52486747   726 SAALHAGLRREQMKVESLERALQQKNQEIEELTKICDELI 765
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 568-771 6.17e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 6.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 568 ADKTAVLTLIREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQRTN---MSSQKSFQQLTMEKEQA 644
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrRELEERLEELEEELAEL 328

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 645 LADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKAKA 724
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 52486747 725 ESAALHAGLRREQMKVESLERALQQKNQEIEELTKICDELIAKLGKA 771
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 578-763 9.76e-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: 9.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    578 REEIITKEIEANEwkKKYEETREEVLEMRKIVAEYEKT---IAQMIEDEQRTNMSSQKSFQQLTMEKEQALADLNSVERS 654
Cdd:TIGR02168  254 ELEELTAELQELE--EKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    655 LSDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQE-EQRYQALkvhaEEKLDRANEEIAQVRSKAKAESAalhagl 733
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEA-ELEELEAELEElESRLEEL----EEQLETLRSKVAQLELQIASLNN------ 400

                          170       180       190
                   ....*....|....*....|....*....|..
gi 52486747    734 RREQMK--VESLERALQQKNQEIEELTKICDE 763
Cdd:TIGR02168  401 EIERLEarLERLEDRRERLQQEIEELLKKLEE 432
mukB PRK04863
chromosome partition protein MukB;
574-759 1.34e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 52.27  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   574 LTLIREEIITKEIEAnewkkkYEETREEVLEMRKIVAEYEKTIAQmIEDEQRTNMSSQKSFQQLTMEKEQALADLNSVE- 652
Cdd:PRK04863  884 LNLLADETLADRVEE------IREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKq 956

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   653 --RSLSDLFRR-----YENLKGVLEGFKKNEEALKKC---AQDYLARVKQE----EQRY-QALKVHA---------EEKL 708
Cdd:PRK04863  957 qaFALTEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRleqAEQERTRAREQlrqaQAQLaQYNQVLAslkssydakRQML 1036

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 52486747   709 DRANEEIAQ--VRSKAKAESAA------LHAGLRREQMKVESLERALQQKNQEIEELTK 759
Cdd:PRK04863 1037 QELKQELQDlgVPADSGAEERArarrdeLHARLSANRSRRNQLEKQLTFCEAEMDNLTK 1095
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 566-765 1.18e-101

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 311.61  E-value: 1.18e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   566 SEADKTAVLTLIREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQRTNMSSQKSFQQLTMEKEQAL 645
Cdd:pfam05010   2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   646 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKAKAE 725
Cdd:pfam05010  82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 52486747   726 SAALHAGLRREQMKVESLERALQQKNQEIEELTKICDELI 765
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 568-771 6.17e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 6.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 568 ADKTAVLTLIREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQRTN---MSSQKSFQQLTMEKEQA 644
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrRELEERLEELEEELAEL 328

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 645 LADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKAKA 724
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 52486747 725 ESAALHAGLRREQMKVESLERALQQKNQEIEELTKICDELIAKLGKA 771
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 569-766 8.90e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 8.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 569 DKTAVLTLIREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQRTNMSSQKSFQQLTMEKE---QAL 645
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrELE 315

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 646 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKK---CAQDYLARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKA 722
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEeleEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 52486747 723 KAESAALHAGLRREQMKVESLERALQQKNQEIEELTKICDELIA 766
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 578-763 9.76e-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: 9.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    578 REEIITKEIEANEwkKKYEETREEVLEMRKIVAEYEKT---IAQMIEDEQRTNMSSQKSFQQLTMEKEQALADLNSVERS 654
Cdd:TIGR02168  254 ELEELTAELQELE--EKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    655 LSDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQE-EQRYQALkvhaEEKLDRANEEIAQVRSKAKAESAalhagl 733
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEA-ELEELEAELEElESRLEEL----EEQLETLRSKVAQLELQIASLNN------ 400

                          170       180       190
                   ....*....|....*....|....*....|..
gi 52486747    734 RREQMK--VESLERALQQKNQEIEELTKICDE 763
Cdd:TIGR02168  401 EIERLEarLERLEDRRERLQQEIEELLKKLEE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 574-768 2.05e-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: 54.68  E-value: 2.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    574 LTLIREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQRtnmsSQKSFQQLTMEKEQALADLNSVER 653
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR----LEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    654 SLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALkvhaEEKLDRANEEIAQVRSKAKAESAALHAGL 733
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRIAATE 837

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 52486747    734 RREQMKVESLERA---LQQKNQEIEELTKICDELIAKL 768
Cdd:TIGR02168  838 RRLEDLEEQIEELsedIESLAAEIEELEELIEELESEL 875
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 578-757 3.00e-07

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 51.45  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   578 REEIITKEI-----EANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQRTNMSsQKSFQQLTMEKEQALADLNSVE 652
Cdd:pfam13851  41 KEERNEKLMseiqqENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVL-EKELKDLKWEHEVLEQRFEKVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   653 RSLSDLFRRYEnlkgvlegfkkneealkKCAQDYLARVKQE----EQRYQALkvhaEEKLDRANEEIAQVRSKAKAESAA 728
Cdd:pfam13851 120 RERDELYDKFE-----------------AAIQDVQQKTGLKnlllEKKLQAL----GETLEKKEAQLNEVLAAANLDPDA 178

                         170       180
                  ....*....|....*....|....*....
gi 52486747   729 LhaglrreQMKVESLERALQQKNQEIEEL 757
Cdd:pfam13851 179 L-------QAVTEKLEDVLESKNQLIKDL 200
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
567-768 3.54e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.62  E-value: 3.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 567 EADKTAVLTLIR---EEIITKEIEA---------NEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQRtnmssqksF 634
Cdd:COG4717  33 EAGKSTLLAFIRamlLERLEKEADElfkpqgrkpELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE--------L 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 635 QQLTMEKEQALADLNSVER--SLSDLFRRYENLKGVLEGFKKNEEALKKcaqdYLARVKQEEQRYQALKVHAEEKLDRAN 712
Cdd:COG4717 105 EELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELE 180

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 52486747 713 EEIAQVRSKAKAESAALHAGLRREQMKVESLERALQQKNQEIEELTKICDELIAKL 768
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 567-771 7.26e-07

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: 52.07  E-value: 7.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 567 EADKTAVLTLIREeiITKEIEANEwkKKYEETREEVLEMRKIVAEYEKTIAQMIE--DEQRTNMSSQKSFQQLTMEKEQA 644
Cdd:COG4942  47 KKEEKALLKQLAA--LERRIAALA--RRIRALEQELAALEAELAELEKEIAELRAelEAQKEELAELLRALYRLGRQPPL 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 645 LADLNSveRSLSDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQEEQRYQALKVHAEEKLDRANEEIAQvrskAKA 724
Cdd:COG4942 123 ALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEA----LKA 195

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 52486747 725 ESAALHAGLRREQmkvESLERALQQKNQEIEELTKICDELIAKLGKA 771
Cdd:COG4942 196 ERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAA 239
mukB PRK04863
chromosome partition protein MukB;
574-759 1.34e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 52.27  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   574 LTLIREEIITKEIEAnewkkkYEETREEVLEMRKIVAEYEKTIAQmIEDEQRTNMSSQKSFQQLTMEKEQALADLNSVE- 652
Cdd:PRK04863  884 LNLLADETLADRVEE------IREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKq 956

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   653 --RSLSDLFRR-----YENLKGVLEGFKKNEEALKKC---AQDYLARVKQE----EQRY-QALKVHA---------EEKL 708
Cdd:PRK04863  957 qaFALTEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRleqAEQERTRAREQlrqaQAQLaQYNQVLAslkssydakRQML 1036

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 52486747   709 DRANEEIAQ--VRSKAKAESAA------LHAGLRREQMKVESLERALQQKNQEIEELTK 759
Cdd:PRK04863 1037 QELKQELQDlgVPADSGAEERArarrdeLHARLSANRSRRNQLEKQLTFCEAEMDNLTK 1095
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 528-764 1.48e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 51.89  E-value: 1.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    528 QKMEEEELTVHGLLET-SSEKAPVSVACGGESPLDGICLSEADKTAVLTLIREEIITKEiEANEWKKKYEETREEVLEMR 606
Cdd:TIGR00618  639 QELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE-MLAQCQTLLRELETHIEEYD 717

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    607 KIVAEYEKTIAQMIEDEQRTNMSSQKSFQQLTME-----KEQALADLNSVERSLSDLFR--RYENLKGVLEGFKKNEEAL 679
Cdd:TIGR00618  718 REFNEIENASSSLGSDLAAREDALNQSLKELMHQartvlKARTEAHFNNNEEVTAALQTgaELSHLAAEIQFFNRLREED 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    680 KKCAQDYLARVKQEEQRYQALKVHAEEKLdraNEEIAQVRSKAKAESAALHAgLRREQMKVESLERALQQKNQEIEELTK 759
Cdd:TIGR00618  798 THLLKTLEAEIGQEIPSDEDILNLQCETL---VQEEEQFLSRLEEKSATLGE-ITHQLLKYEECSKQLAQLTQEQAKIIQ 873


                   ....*
gi 52486747    760 ICDEL 764
Cdd:TIGR00618  874 LSDKL 878
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 576-768 1.74e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 576 LIREEIITKEIEAN--------EWKKKYEE--TREEVLEMRKIVAEYEKTIAQMIEDEQRTnmssqksfQQLTMEKEQAL 645
Cdd:COG1196 188 LERLEDILGELERQleplerqaEKAERYRElkEELKELEAELLLLKLRELEAELEELEAEL--------EELEAELEELE 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 646 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCaqdyLARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSK---A 722
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELEEEleeL 335

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 52486747 723 KAESAALHAGLRREQMKVESLERALQQKNQEIEELTKICDELIAKL 768
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 577-725 1.34e-05

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: 47.23  E-value: 1.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 577 IREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQR-----TNMSSQKSFQQLTMEKEQALADLNSV 651
Cdd:COG1579  29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlGNVRNNKEYEALQKEIESLKRRISDL 108

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52486747 652 ERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKAKAE 725
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELE-------AELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 569-772 2.51e-05

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: 48.04  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    569 DKTAVLTLIREEIITKEIEANEWKKKYEE----TREEVLEMRKIVAEYEKTIAQMIEDEQRTNMSSQKSFQQL--TMEKE 642
Cdd:pfam02463  184 NLAELIIDLEELKLQELKLKEQAKKALEYyqlkEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSkqEIEKE 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    643 QALADLNSVERSLSdlfrryenlkgvlEGFKKNEEALKKCAQDYLARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKA 722
Cdd:pfam02463  264 EEKLAQVLKENKEE-------------EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 52486747    723 KAESaalHAGLRREQMKvESLERALQQKNQEIEELTKICDELIAKLGKAD 772
Cdd:pfam02463  331 KKEK---EEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
PTZ00121 PTZ00121
MAEBL; Provisional
 513-753 2.52e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   513 KSAGAEVKGVEKEAYQKMEEEELTVHGLLETSSEKAPVSVACGGESPLDGICLSEADKTAVLTLIREEIITKeieANEWK 592
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK---ADEAK 1397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   593 KKYEETREEVLEMRKIVAEYEKTiaqmieDEQRTNMSSQKSFQQLTMEKEQAladlnsveRSLSDLFRRYENLKGVLEGF 672
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKA------DEAKKKAEEKKKADEAKKKAEEA--------KKADEAKKKAEEAKKAEEAK 1463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   673 KKNEEALKKcaqDYLARVKQEEQRYQALKVHAEEKLDRANEeiaqVRSKAKAESAALHAGLRREQMKVESLERALQQKNQ 752
Cdd:PTZ00121 1464 KKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEAKKKADE----AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536


                  .
gi 52486747   753 E 753
Cdd:PTZ00121 1537 D 1537
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
599-764 3.33e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 3.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 599 REEVLEMRKIVAEYEKTIAQMIEDEQRTNMSSQKsfQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEA 678
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA--KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 679 LKKCA--QDYLARVKQEEQRYQALKVHAEEK---LDRANEEIAQVRSKAKAESAALHAGLRRE----QMKVESLERALQQ 749
Cdd:COG3206 259 LLQSPviQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAElealQAREASLQAQLAQ 338

                       170
                ....*....|....*
gi 52486747 750 KNQEIEELTKICDEL 764
Cdd:COG3206 339 LEARLAELPELEAEL 353
PTZ00121 PTZ00121
MAEBL; Provisional
 584-763 3.59e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   584 KEIEANEWKKKYEETREEvlEMRKIVAEYEKTIAQMIEdEQRTNMSSQKSFQQLTMEKEQALADlnSVERSLSDLFRRYE 663
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAE 1629

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   664 NLKGVLEGFKKNEEALKKCAQDY-------------LARvKQEEQRYQALKVHAEEKLDRANEEIAQVRSKAKAESAALH 730
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELkkaeeenkikaaeEAK-KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708

                         170       180       190
                  ....*....|....*....|....*....|...
gi 52486747   731 AGLRREQMKVESLERALQQKNQEIEELTKICDE 763
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 577-759 4.20e-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: 46.68  E-value: 4.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 577 IREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQmIEDEQRTnmsSQKSFQQLTMEKEQALADLNSVERSLS 656
Cdd:COG4942  32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-LEQELAA---LEAELAELEKEIAELRAELEAQKEELA 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 657 DLFR------RYENLKGVL--EGFKKNEEALKkcaqdYLARVkqeeqrYQALKVHAEEkLDRANEEIAQVRSKAKAESAA 728
Cdd:COG4942 108 ELLRalyrlgRQPPLALLLspEDFLDAVRRLQ-----YLKYL------APARREQAEE-LRADLAELAALRAELEAERAE 175

                       170       180       190
                ....*....|....*....|....*....|.
gi 52486747 729 LHAGLRREQMKVESLERALQQKNQEIEELTK 759
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEK 206
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
587-771 6.47e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 45.67  E-value: 6.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 587 EANEWKKKYEETREEVLEMRKIVAEY------EKTIAQMIEDEQRTNMSSQksfqqLTMEKEQALadlnsVERsLSDLFR 660
Cdd:COG1340  79 ERDELNEKLNELREELDELRKELAELnkaggsIDKLRKEIERLEWRQQTEV-----LSPEEEKEL-----VEK-IKELEK 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 661 RYENLKGVLEGFKKNEEALKKCAQdylARVKQEEQRyQALKVHAEEkLDRANEEIAQVRSKA---KAESAALHAGLRREQ 737
Cdd:COG1340 148 ELEKAKKALEKNEKLKELRAELKE---LRKEAEEIH-KKIKELAEE-AQELHEEMIELYKEAdelRKEADELHKEIVEAQ 222

                       170       180       190
                ....*....|....*....|....*....|....
gi 52486747 738 MKVESLERALQQKNQEIEELTKICDELIAKLGKA 771
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 572-759 6.49e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 6.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    572 AVLTLIREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQmiEDEQRTNMSSQKsfQQLTMEKEQALADLNSV 651
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS--LNNEIERLEARL--ERLEDRRERLQQEIEEL 426

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    652 ERSLSDLfrRYENLKGVLEGFKKNEEALKKCaqdyLARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKAKAesaalha 731
Cdd:TIGR02168  427 LKKLEEA--ELKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQARLDS------- 493

                          170       180
                   ....*....|....*....|....*...
gi 52486747    732 glrreqmkVESLERALQQKNQEIEELTK 759
Cdd:TIGR02168  494 --------LERLQENLEGFSEGVKALLK 513
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
592-759 7.71e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 7.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 592 KKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQRTNMSSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEG 671
Cdd:COG4372   5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 672 FKKNEEALKKCAQDYLARVKQEEQRYQALKVHAEEkLDRANEEIAQVRSKAKAESAALHAGLRREQMKVESLERALQQKN 751
Cdd:COG4372  85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163


                ....*...
gi 52486747 752 QEIEELTK 759
Cdd:COG4372 164 EELAALEQ 171
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
579-770 8.67e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 8.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  579 EEIITKEIEANewKKKYEETREEVLEMRKivaeyektiaqmiedEQRTNMSSQKSFQQLTMEKEQALADLNSVERSLSDL 658
Cdd:PRK03918 513 KKYNLEELEKK--AEEYEKLKEKLIKLKG---------------EIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  659 FRRYENLKgvLEGFKKNEEALKKCAQDY-----LARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKAKAESAAL---- 729
Cdd:PRK03918 576 LKELEELG--FESVEELEERLKELEPFYneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELeele 653

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 52486747  730 -------HAGLRREQMKvesLERALQQKNQEIEELTKICDELIAKLGK 770
Cdd:PRK03918 654 kkyseeeYEELREEYLE---LSRELAGLRAELEELEKRREEIKKTLEK 698
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 568-759 9.75e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 9.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    568 ADKTAVLTLIREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDeqrtnmssqksFQQLTMEKEQALAD 647
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-----------LEALLNERASLEEA 888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    648 LNSVERSLSDLFRRyenLKGVLEGFKKNEEALKKCAQdylaRVKQEEQRYQALKVHAEEKLDRANEE-------IAQVRS 720
Cdd:TIGR02168  889 LALLRSELEELSEE---LRELESKRSELRRELEELRE----KLAQLELRLEGLEVRIDNLQERLSEEysltleeAEALEN 961

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 52486747    721 KAKAESAALHAGLRREQMKVESL-------ERALQQKNQEIEELTK 759
Cdd:TIGR02168  962 KIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTA 1007
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 578-769 1.28e-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: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    578 REEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQM---IED-EQRTNMS----SQKSFQQLTMEKEQALADLN 649
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeeaLNDlEARLSHSripeIQAELSKLEEEVSRIEARLR 815

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    650 SVERSLSDLfrryENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKakaesaal 729
Cdd:TIGR02169  816 EIEQKLNRL----TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR-------- 883

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 52486747    730 HAGLRREQMKVES----LERALQQKNQEIEELTKICDELIAKLG 769
Cdd:TIGR02169  884 LGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLE 927
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 576-764 1.50e-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: 45.43  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    576 LIREEIITKEIEANewKKKYEETREEVLEMRKIVAEYEKTIAQMiedeqrtnmsSQKSFQQLTMEKEQALADLNSVERSL 655
Cdd:TIGR02168  188 LDRLEDILNELERQ--LKSLERQAEKAERYKELKAELRELELAL----------LVLRLEELREELEELQEELKEAEEEL 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    656 SDLFRRYENLKGVLEGFKKNEEALKKCAQDY----------LARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSK---A 722
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELqkelyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKldeL 335

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 52486747    723 KAESAALHAGLRREQMKVESLERALQQKNQEIEELTKICDEL 764
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 596-759 1.83e-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: 45.05  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    596 EETREEVLEMRKIVAEYEKTIAQMIEDEQRTNM---SSQKSFQQLTMEKEQALADLNSVERSLSDL---FRRYENLKGVL 669
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKalaELRKELEELEEELEQLRKELEELSRQISALrkdLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747    670 EGFKKNEEALKKCAQDYLARVKQEEQRYQALKVHAEEKLDRANEEIAQVR----------SKAKAESAALHAGLRREQMK 739
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkalrealDELRAELTLLNEEAANLRER 825

                          170       180
                   ....*....|....*....|
gi 52486747    740 VESLERALQQKNQEIEELTK 759
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEE 845
PRK12704 PRK12704
phosphodiesterase; Provisional
 591-729 4.01e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 4.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  591 WKKKYEETREEVlemRKIVAEYEKTiAQMIEDEQRTNmsSQKSFQQLTMEKEQALAD-LNSVERSLSDLFRRYENLKGVL 669
Cdd:PRK12704  29 AEAKIKEAEEEA---KRILEEAKKE-AEAIKKEALLE--AKEEIHKLRNEFEKELRErRNELQKLEKRLLQKEENLDRKL 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52486747  670 EGFKKNEEALKKCAQDYLAR---VKQEEQRYQALKVHAEEKLDRA----NEE-----IAQVRSKAKAESAAL 729
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKqqeLEKKEEELEELIEEQLQELERIsgltAEEakeilLEKVEEEARHEAAVL 174
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
578-770 6.43e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 6.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  578 REEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQM--IEDEQRTNMSSQKSFQQLTMEKEQALADLNSVERSL 655
Cdd:PRK03918 147 REKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTenIEELIKEKEKELEEVLREINEISSELPELREELEKL 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  656 SDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKVHAEEKLDRANE------------EIAQVRSKAK 723
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkelkekaeeyiKLSEFYEEYL 306

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 52486747  724 AESAALHAGLRREQMKVESLERALQQ---KNQEIEELTKICDELIAKLGK 770
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRLEE 356
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
579-772 6.71e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 6.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  579 EEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQRTNMSSQKSFQQLTMEKEQALADLNSVERSLSDL 658
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  659 FRRYENLKGVLEGFKKNEEALKKcaqdylARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKaKAESAALHAGLRREQM 738
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKK------AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKE-LKEIEEKERKLRKELR 483

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 52486747  739 KVESleraLQQKNQEIEELTKICDELIA---KLGKAD 772
Cdd:PRK03918 484 ELEK----VLKKESELIKLKELAEQLKEleeKLKKYN 516
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
570-737 1.24e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 570 KTAVLTLIREEIITKEI-EANEWKKKYEETREEVLEMRKIVAEYEKTIAQMieDEQRTNMSSQKSFQQLTMEKEQALADL 648
Cdd:COG4717  64 RKPELNLKELKELEEELkEAEEKEEEYAELQEELEELEEELEELEAELEEL--REELEKLEKLLQLLPLYQELEALEAEL 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 649 NSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQD-----------YLARVKQEEQRYQAL---KVHAEEKLDRANEE 714
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEEleelleqlslaTEEELQDLAEELEELqqrLAELEEELEEAQEE 221

                       170       180
                ....*....|....*....|...
gi 52486747 715 IAQVRSKAKAESAALHAGLRREQ 737
Cdd:COG4717 222 LEELEEELEQLENELEAAALEER 244
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 635-768 1.43e-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: 41.06  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 635 QQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQR---------YQAL----- 700
Cdd:COG1579  20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEALqkeie 99

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52486747 701 -----KVHAEEKLDRANEEIAQVRSKAKAESAALHAGLRREQMKVESLERALQQKNQEIEELTKICDELIAKL 768
Cdd:COG1579 100 slkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
PTZ00121 PTZ00121
MAEBL; Provisional
 566-759 1.83e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   566 SEADKTAVLtliREEIITKEIEanewKKKYEETREEVLEMRKIVAEYEKTiaqmiEDEQRTNMSSQKSFQQLTMEKEQAL 645
Cdd:PTZ00121 1572 AEEDKNMAL---RKAEEAKKAE----EARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEELKKAEEEKKKVEQLK 1639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   646 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKVHAEEKldRANEEIAQVRSKAKAE 725
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA--KKAEELKKKEAEEKKK 1717

                         170       180       190
                  ....*....|....*....|....*....|....
gi 52486747   726 SAALHAGLRREQMKVESLERALQQKNQEIEELTK 759
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
574-747 2.23e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  574 LTLIREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQmiedeqrtnmSSQKSFQQLTMEKEQALADLNSVER 653
Cdd:COG4913  290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG----------NGGDRLEQLEREIERLERELEERER 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  654 SLSDLFRRYENLK----GVLEGFKKNEEALKKCAQDYLARVKQ-EEQRYQALKVH--AEEKLDRANEEIAQVRSKAKAES 726
Cdd:COG4913  360 RRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEAlEEALAEAEAALrdLRRELRELEAEIASLERRKSNIP 439

                        170       180
                 ....*....|....*....|.
gi 52486747  727 AALHAgLRREqmkvesLERAL 747
Cdd:COG4913  440 ARLLA-LRDA------LAEAL 453
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 578-772 2.51e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.10  E-value: 2.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 578 REEIITKEIEANEWKKKYEETREEVlemrkivAEYEKTIaqMIEDEQrtnmsSQKSFQQLTMEKEQALADlnSVERSLSD 657
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKEKI-------AEYTKSI--DIKKAT-----ESLEEQLAAAEAEQELEE--SKRETETG 337

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 658 LFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQE--EQRYQALKVHAEEKLDRANEEIAQVRSKAKAESAALHAGLRR 735
Cdd:COG5185 338 IQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSksSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKA 417

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 52486747 736 EQMKVESLERALQQKNQEIEELTKICDELIAKLGKAD 772
Cdd:COG5185 418 ADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVM 454
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 568-756 3.87e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 3.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 568 ADKTAVLTLIREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIE--DEQRTNMSSQKSFQQLTMEKEQAL 645
Cdd:COG3883  26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeiEERREELGERARALYRSGGSVSYL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 646 ADLNSVErSLSDLFRRYENLKGVLEgfkKNEEALKKCAQDyLARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSKaKAE 725
Cdd:COG3883 106 DVLLGSE-SFSDFLDRLSALSKIAD---ADADLLEELKAD-KAELEAKKAELEAKLAELEALKAELEAAKAELEAQ-QAE 179

                       170       180       190
                ....*....|....*....|....*....|.
gi 52486747 726 SAALHAGLRREQMKVESLERALQQKNQEIEE 756
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
568-753 3.93e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  568 ADKTAVLTLIREEIITKEIEANEWKKKYEETREEVLEMRKI---------VAEYEKTIAQmIEDEQRTNMSSQKSFQQLT 638
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAE-LEAELERLDASSDDLAALE 691

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  639 MEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQEEQRYQALKVHAEEKLDRANEEIAQV 718
Cdd:COG4913  692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLARLELRALLEERFAAALGDAVERELREN 770

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 52486747  719 RSKAKAESAALHAGLRREqmkvesLERALQQKNQE 753
Cdd:COG4913  771 LEERIDALRARLNRAEEE------LERAMRAFNRE 799
PRK12704 PRK12704
phosphodiesterase; Provisional
 663-767 4.27e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 4.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  663 ENLKGVLEGFKKNEEALKKcaqDYLARVKQEEQRyqaLKVHAEEKLDRANEEIAQVRSKAKAESAAL---HAGLRREQMK 739
Cdd:PRK12704  38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEE 111

                         90       100
                 ....*....|....*....|....*...
gi 52486747  740 VESLERALQQKNQEIEELTKICDELIAK 767
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEE 139
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 638-771 5.33e-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: 39.14  E-value: 5.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 638 TMEKEQ-ALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKV---HAEEKLDRANE 713
Cdd:COG1579   1 AMPEDLrALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELeieEVEARIKKYEE 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52486747 714 EIAQVRSkAKAESAALH--AGLRREQ-----------MKVESLERALQQKNQEIEELTKICDELIAKLGKA 771
Cdd:COG1579  81 QLGNVRN-NKEYEALQKeiESLKRRIsdledeilelmERIEELEEELAELEAELAELEAELEEKKAELDEE 150
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 574-732 6.38e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 6.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 574 LTLIREEIITKEIEANEWKKKYEETREEVLEMRKIVAEYEKTIAQMIEDEQRTN-------MSSQKSF------------ 634
Cdd:COG4942  64 IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGrqpplalLLSPEDFldavrrlqylky 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 635 -----QQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKVHAEEKLD 709
Cdd:COG4942 144 laparREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223

                       170       180
                ....*....|....*....|...
gi 52486747 710 RANEEIAQVRSKAKAESAALHAG 732
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAA 246
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 573-658 7.68e-03

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 37.66  E-value: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747  573 VLTLI--REEIITKEI--------EANEWKKKYEEtreEVLEMRK----IVAEYEKTIAQMIEDEQRtnmSSQKSF---- 634
Cdd:CHL00118  47 LLKVLdeRKEYIRKNLtkaseilaKANELTKQYEQ---ELSKARKeaqlEITQSQKEAKEIVENELK---QAQKYIdsll 120

                         90       100
                 ....*....|....*....|....*...
gi 52486747  635 ----QQLTMEKEQALADLNSVERSLSDL 658
Cdd:CHL00118 121 neatKQLEAQKEKALKSLEEQVDTLSDQ 148
PTZ00121 PTZ00121
MAEBL; Provisional
 567-752 7.86e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 7.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   567 EADKTAVLTLIREEIITKEIEAnewkKKYEETREEVLEMRKivAEYEKtiaQMIEDEQRTNMSSQKSFQQLTMEKEQala 646
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKK--AEEEK---KKVEQLKKKEAEEKKKAEELKKAEEE--- 1658

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   647 dlNSVERSlsDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQEEQRYQALKVHAEEKLDRANE-EIAQVRSKAKAE 725
Cdd:PTZ00121 1659 --NKIKAA--EEAKKAEEDKKKAEEAKKAEEDEKK-AAEALKKEAEEAKKAEELKKKEAEEKKKAEElKKAEEENKIKAE 1733

                         170       180
                  ....*....|....*....|....*..
gi 52486747   726 SAALHAglRREQMKVESLERALQQKNQ 752
Cdd:PTZ00121 1734 EAKKEA--EEDKKKAEEAKKDEEEKKK 1758
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
578-767 8.60e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.12  E-value: 8.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 578 REEIITkeiEANEWKKK-------YEETREEVLEMRKIVAEYEKTIAQMIEDEQRTNMSSQKSFQQLTMEKEQaLADLNS 650
Cdd:COG1340  31 RDELNE---ELKELAEKrdelnaqVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKE-LAELNK 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747 651 VERSLSDLFRRYENLKGVLE--GFKKNEEalkkcaQDYLARVKQEEQRYQALK--VHAEEKLDRANEEIAQVRSKAKaes 726
Cdd:COG1340 107 AGGSIDKLRKEIERLEWRQQteVLSPEEE------KELVEKIKELEKELEKAKkaLEKNEKLKELRAELKELRKEAE--- 177

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 52486747 727 aALHAGLRREQMKVESLERALQQKNQEIEELTKICDELIAK 767
Cdd:COG1340 178 -EIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKE 217
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 587-757 9.69e-03

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


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.12  E-value: 9.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   587 EANEWKKKYEET----REEVLEMRKIVAEYEKTIAQMIEDEQRTNMSSQKSFQQLTMEKEQALADLNSVERSLSdlfrry 662
Cdd:pfam04012  12 NIHEGLDKAEDPekmlEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELA------ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52486747   663 enlkgvlegfkknEEAL--KKCAQDYLARVKQEEQRYQALKVHAEEKLDRANEEIAQVRSK-------AKAESAALHAGL 733
Cdd:pfam04012  86 -------------REALaeKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKknllkarLKAAKAQEAVQT 152

                         170       180
                  ....*....|....*....|....
gi 52486747   734 RREQMKVESLERALQQKNQEIEEL 757
Cdd:pfam04012 153 SLGSLSTSSATDSFERIEEKIEER 176
 
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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