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Conserved domains on  [gi|1209185300|ref|NP_001339715|]
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transforming acidic coiled-coil-containing protein 1 isoform 13 [Homo sapiens]

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 ...
 525-724 1.77e-98

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: 301.98  E-value: 1.77e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 525 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQAL 604
Cdd:pfam05010   2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 605 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 684
Cdd:pfam05010  82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1209185300 685 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 724
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 ...
 525-724 1.77e-98

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: 301.98  E-value: 1.77e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 525 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQAL 604
Cdd:pfam05010   2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 605 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 684
Cdd:pfam05010  82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1209185300 685 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 724
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 528-727 8.82e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 8.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 528 DKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQ---KSFQQLTMEKEQAL 604
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 605 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 684
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1209185300 685 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 727
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 536-716 2.27e-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: 2.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  536 IREEIitKEIEANEWKKKYEETRQEVLEMRKIVAEYEktiaQMIEDEQRTSMTSQKSFQQLTMEKeqaladlNSVERSLS 615
Cdd:TIGR02168  218 LKAEL--RELELALLVLRLEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLEV-------SELEEEIE 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  616 DLFRRYENLKGVLEGFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---AKAESAALHAGL 692
Cdd:TIGR02168  285 ELQKELYALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKleeLKEELESLEAEL 360

                          170       180
                   ....*....|....*....|....
gi 1209185300  693 RKEQMKVESLERALQQKNQEIEEL 716
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLETL 384
mukB PRK04863
chromosome partition protein MukB;
533-718 1.66e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.41  E-value: 1.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  533 LTLIREEIITKEIEAnewkkkYEETRQEVLEMRKIVAEYEKTIAQmIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVE- 611
Cdd:PRK04863   884 LNLLADETLADRVEE------IREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKq 956

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  612 --RSLSDLFRR-----YENLKGVLEGFKKNEEALKKC---AQDYLARVKQE-----------EQRYQALK--IHA-EEKL 667
Cdd:PRK04863   957 qaFALTEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRleqAEQERTRAREQlrqaqaqlaqyNQVLASLKssYDAkRQML 1036

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1209185300  668 DKANEEIAQ--VRTKAKAESAA------LHAGLRKEQMKVESLERALQQKNQEIEELTK 718
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 ...
 525-724 1.77e-98

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: 301.98  E-value: 1.77e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 525 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQAL 604
Cdd:pfam05010   2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 605 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 684
Cdd:pfam05010  82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1209185300 685 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 724
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 528-727 8.82e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 8.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 528 DKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQ---KSFQQLTMEKEQAL 604
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 605 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 684
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1209185300 685 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 727
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 536-716 2.27e-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: 2.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  536 IREEIitKEIEANEWKKKYEETRQEVLEMRKIVAEYEktiaQMIEDEQRTSMTSQKSFQQLTMEKeqaladlNSVERSLS 615
Cdd:TIGR02168  218 LKAEL--RELELALLVLRLEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLEV-------SELEEEIE 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  616 DLFRRYENLKGVLEGFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---AKAESAALHAGL 692
Cdd:TIGR02168  285 ELQKELYALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKleeLKEELESLEAEL 360

                          170       180
                   ....*....|....*....|....
gi 1209185300  693 RKEQMKVESLERALQQKNQEIEEL 716
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLETL 384
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 526-727 1.46e-06

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: 50.92  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 526 ESDKTAVLTLIREeiITKEIEANEwkKKYEETRQEVLEMRKIVAEYEKTIAQMIE--DEQRTSMTSQKSFQQLTMEKEQA 603
Cdd:COG4942    47 KKEEKALLKQLAA--LERRIAALA--RRIRALEQELAALEAELAELEKEIAELRAelEAQKEELAELLRALYRLGRQPPL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 604 LADLNSveRSLSDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQvrtkAKA 683
Cdd:COG4942   123 ALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEA----LKA 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1209185300 684 ESAALHAGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 727
Cdd:COG4942   196 ERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEA 236
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
552-727 1.68e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 552 KKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRtsmtsqksFQQLTMEKEQALADLNSVER--SLSDLFRRYENLKGVLE 629
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEE--------LEELEAELEELREELEKLEKllQLLPLYQELEALEAELA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 630 GFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQK 709
Cdd:COG4717   143 ELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218

                         170
                  ....*....|....*...
gi 1209185300 710 NQEIEELTKICDELIAKL 727
Cdd:COG4717   219 QEELEELEEELEQLENEL 236
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 537-716 1.97e-06

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: 49.13  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 537 REEIITKEI-----EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTsQKSFQQLTMEKEQALADLNSVE 611
Cdd:pfam13851  41 KEERNEKLMseiqqENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVL-EKELKDLKWEHEVLEQRFEKVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 612 RSLSDLFRRYEnlkgvlegfkkneealkKCAQDYLARVKQE----EQRYQALkihaEEKLDKANEEIAQVRTKAKAESAA 687
Cdd:pfam13851 120 RERDELYDKFE-----------------AAIQDVQQKTGLKnlllEKKLQAL----GETLEKKEAQLNEVLAAANLDPDA 178

                         170       180
                  ....*....|....*....|....*....
gi 1209185300 688 LhaglrkeQMKVESLERALQQKNQEIEEL 716
Cdd:pfam13851 179 L-------QAVTEKLEDVLESKNQLIKDL 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 531-725 2.61e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 531 AVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRK----IVAEYEKTIAQMIEDEQRTSMTSQKSfQQLTMEKEQALAD 606
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEELELeleeAQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEE 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 607 LNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKcaqdylARVKQEEQRYQALK--IHAEEKLDKANEEIAQVRTKAKAE 684
Cdd:COG1196   325 LAELEEELEELEEELEELEEELEEAEEELEEAEA------ELAEAEEALLEAEAelAEAEEELEELAEELLEALRAAAEL 398

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1209185300 685 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIA 725
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 535-727 3.20e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 535 LIREEIITKEIEAN---------------EWKKKYEETRQE--VLEMRKIVAEYEKTIAQMiedeqrtsmtsqksfQQLT 597
Cdd:COG1196   188 LERLEDILGELERQleplerqaekaeryrELKEELKELEAEllLLKLRELEAELEELEAEL---------------EELE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 598 MEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCaqdyLARVKQEEQRYQALKIHAEEKLDKANEEIAQV 677
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAEL 328

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1209185300 678 RTK---AKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 727
Cdd:COG1196   329 EEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 537-722 4.13e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 4.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  537 REEIITKEIEANEwkKKYEETRQEVLEMRKIVAEYEKT---IAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERS 613
Cdd:TIGR02168  254 ELEELTAELQELE--EKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  614 LSDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQE-EQRYQALkihaEEKLDKANEEIAQVRTKAKAESAALHAgL 692
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEA-ELEELEAELEElESRLEEL----EEQLETLRSKVAQLELQIASLNNEIER-L 405

                          170       180       190
                   ....*....|....*....|....*....|
gi 1209185300  693 RKEqmkVESLERALQQKNQEIEELTKICDE 722
Cdd:TIGR02168  406 EAR---LERLEDRRERLQQEIEELLKKLEE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 533-727 7.38e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 7.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  533 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRtsmtSQKSFQQLTMEKEQALADLNSVER 612
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR----LEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  613 SLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALkihaEEKLDKANEEIAQVRTKAKAESAALHAGL 692
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRIAATE 837

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1209185300  693 RKEQMKVESLERA---LQQKNQEIEELTKICDELIAKL 727
Cdd:TIGR02168  838 RRLEDLEEQIEELsedIESLAAEIEELEELIEELESEL 875
mukB PRK04863
chromosome partition protein MukB;
533-718 1.66e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.41  E-value: 1.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  533 LTLIREEIITKEIEAnewkkkYEETRQEVLEMRKIVAEYEKTIAQmIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVE- 611
Cdd:PRK04863   884 LNLLADETLADRVEE------IREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKq 956

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  612 --RSLSDLFRR-----YENLKGVLEGFKKNEEALKKC---AQDYLARVKQE-----------EQRYQALK--IHA-EEKL 667
Cdd:PRK04863   957 qaFALTEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRleqAEQERTRAREQlrqaqaqlaqyNQVLASLKssYDAkRQML 1036

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1209185300  668 DKANEEIAQ--VRTKAKAESAA------LHAGLRKEQMKVESLERALQQKNQEIEELTK 718
Cdd:PRK04863  1037 QELKQELQDlgVPADSGAEERArarrdeLHARLSANRSRRNQLEKQLTFCEAEMDNLTK 1095
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 533-723 4.44e-05

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: 46.89  E-value: 4.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  533 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQmiedEQRTSMTSQKSFQQL--TMEKEQALADLNSV 610
Cdd:TIGR00618  692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA----REDALNQSLKELMHQarTVLKARTEAHFNNN 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  611 ERSLSDLFR--RYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKaneEIAQVRTKAKAESAAL 688
Cdd:TIGR00618  768 EEVTAALQTgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ---EEEQFLSRLEEKSATL 844

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1209185300  689 HAgLRKEQMKVESLERALQQKNQEIEELTKICDEL 723
Cdd:TIGR00618  845 GE-ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
PTZ00121 PTZ00121
MAEBL; Provisional
 543-722 4.77e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 4.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  543 KEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMIEdEQRTSMTSQKSFQQLTMEKEQALADlnSVERSLSDLFRRYE 622
Cdd:PTZ00121  1555 EELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAE 1629

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  623 NLKGVLEGFKKNE-------EALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEE--IAQVRTKAKAESAALHAGLR 693
Cdd:PTZ00121  1630 EEKKKVEQLKKKEaeekkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKKAEEDekKAAEALKKEAEEAKKAEELK 1708

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1209185300  694 K----EQMKVESLERALQQKNQEIEELTKICDE 722
Cdd:PTZ00121  1709 KkeaeEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 555-718 4.80e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 4.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  555 EETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSM---TSQKSFQQLTMEKEQALADLNSVERSLSDL---FRRYENLKGVL 628
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKalaELRKELEELEEELEQLRKELEELSRQISALrkdLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  629 EGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVR----------TKAKAESAALHAGLRKEQMK 698
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkalrealDELRAELTLLNEEAANLRER 825

                          170       180
                   ....*....|....*....|
gi 1209185300  699 VESLERALQQKNQEIEELTK 718
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEE 845
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 536-694 5.94e-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: 45.30  E-value: 5.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 536 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQR-----TSMTSQKSFQQLTMEKEQALADLNSV 610
Cdd:COG1579    29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlGNVRNNKEYEALQKEIESLKRRISDL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 611 ERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHA 690
Cdd:COG1579   109 EDEILELMERIEELEEELAELEAELAELE-------AELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYE 181


                  ....
gi 1209185300 691 GLRK 694
Cdd:COG1579   182 RIRK 185
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 546-703 8.04e-05

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: 44.67  E-value: 8.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 546 EANEWKKKYEET----RQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLS-DLFRR 620
Cdd:pfam04012  12 NIHEGLDKAEDPekmlEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELArEALAE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 621 YENLKGVLEGFKKN-------EEALKKCAQDYLARVKQEEQRYQALKihAEEKLDKANEEIAQVRTKAKAESAAlhAGLR 693
Cdd:pfam04012  92 KKSLEKQAEALETQlaqqrsaVEQLRKQLAALETKIQQLKAKKNLLK--ARLKAAKAQEAVQTSLGSLSTSSAT--DSFE 167

                         170
                  ....*....|
gi 1209185300 694 KEQMKVESLE 703
Cdd:pfam04012 168 RIEEKIEERE 177
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
546-730 9.59e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.90  E-value: 9.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 546 EANEWKKKYEETRQEVLEMRKIVAEY------EKTIAQMIEDEQRTSMTSQksfqqLTMEKEQALadlnsVERsLSDLFR 619
Cdd:COG1340    79 ERDELNEKLNELREELDELRKELAELnkaggsIDKLRKEIERLEWRQQTEV-----LSPEEEKEL-----VEK-IKELEK 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 620 RYENLKGVLEGFKKNEEALKKCAQdylARVKQEEQRyQALKIHAEEkLDKANEEIAQVRTKA---KAESAALHAGLRKEQ 696
Cdd:COG1340   148 ELEKAKKALEKNEKLKELRAELKE---LRKEAEEIH-KKIKELAEE-AQELHEEMIELYKEAdelRKEADELHKEIVEAQ 222

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1209185300 697 MKVESLERALQQKNQEIEELTKICDELIAKLGKT 730
Cdd:COG1340   223 EKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
546-723 1.10e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 546 EANEW-KKKYEETRQEVLEMRKIVAEYeKTIAQMIEDEQRTSMTSQKSfQQLTMEKEQALADLNSVERSLSDLFRRYENL 624
Cdd:COG3206   175 KALEFlEEQLPELRKELEEAEAALEEF-RQKNGLVDLSEEAKLLLQQL-SELESQLAEARAELAEAEARLAALRAQLGSG 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 625 KGVLEGFKKNEEAlkkcaQDYLARVKQEEQRYQALKIHAEEK---LDKANEEIAQVRTKAKAESAALHAGLRKE----QM 697
Cdd:COG3206   253 PDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAElealQA 327

                         170       180
                  ....*....|....*....|....*.
gi 1209185300 698 KVESLERALQQKNQEIEELTKICDEL 723
Cdd:COG3206   328 REASLQAQLAQLEARLAELPELEAEL 353
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
551-718 1.93e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 551 KKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEG 630
Cdd:COG4372     5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 631 FKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKN 710
Cdd:COG4372    85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163


                  ....*...
gi 1209185300 711 QEIEELTK 718
Cdd:COG4372   164 EELAALEQ 171
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 537-728 3.79e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 3.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  537 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQM---IED-EQRTSM----TSQKSFQQLTMEKEQALADLN 608
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeeaLNDlEARLSHsripEIQAELSKLEEEVSRIEARLR 815

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  609 SVERSLSDLfrryENLKGVLEGFKKNEEALKKCAQDylaRVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAesaal 688
Cdd:TIGR02169  816 EIEQKLNRL----TLEKEYLEKEIQELQEQRIDLKE---QIKSIEKEIENLNGKKEELEEELEELEAALRDLESR----- 883

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1209185300  689 HAGLRKEQMKVES----LERALQQKNQEIEELTKICDELIAKLG 728
Cdd:TIGR02169  884 LGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLE 927
PTZ00121 PTZ00121
MAEBL; Provisional
 552-722 4.44e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 4.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  552 KKYEETRQEVLEMRKivAEYEKTIAQMIE-DEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEG 630
Cdd:PTZ00121  1230 KKAEEAKKDAEEAKK--AEEERNNEEIRKfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  631 FKKNEEALKkcAQDYLARVKQEEQRYQALKIHAEEKldKANEEIAQVRTKAKAESAalhaglRKEQMKVESLERALQQKN 710
Cdd:PTZ00121  1308 KKKAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEA--KKAAEAAKAEAEAAADEA------EAAEEKAEAAEKKKEEAK 1377

                          170
                   ....*....|..
gi 1209185300  711 QEIEELTKICDE 722
Cdd:PTZ00121  1378 KKADAAKKKAEE 1389
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
534-729 6.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 534 TLIREEIITKEIEanEWKKKYEETRQEVLEMRKivAEYEKTIAQMI--EDEQRTSMTSQKSFQQLTMEKEQALADLNSVE 611
Cdd:PRK03918  494 ELIKLKELAEQLK--ELEEKLKKYNLEELEKKA--EEYEKLKEKLIklKGEIKSLKKELEKLEELKKKLAELEKKLDELE 569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 612 RSLSDLFRRYENLKgvLEGFKKNEEALKKCAQDY-----LARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESA 686
Cdd:PRK03918  570 EELAELLKELEELG--FESVEELEERLKELEPFYneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1209185300 687 AL-----------HAGLRKEQMKvesLERALQQKNQEIEELTKICDELIAKLGK 729
Cdd:PRK03918  648 ELeelekkyseeeYEELREEYLE---LSRELAGLRAELEELEKRREEIKKTLEK 698
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
538-729 6.87e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 6.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 538 EEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDL 617
Cdd:PRK03918  331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 618 FRRYENLKGVLEGFKKNEEALKK-------CAQ--------DYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAK 682
Cdd:PRK03918  411 TARIGELKKEIKELKKAIEELKKakgkcpvCGRelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1209185300 683 AESAALHagLRKEQMKVESLERALQQKN-QEIEELTKICDELIAKLGK 729
Cdd:PRK03918  491 KESELIK--LKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
PTZ00121 PTZ00121
MAEBL; Provisional
 526-715 9.13e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 9.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  526 ESDKTAVLTLIREEIITKEIEAnewkKKYEETRQEVLEMRKivaeyEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALA 605
Cdd:PTZ00121  1591 EARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKK-----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  606 DLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLA----RVKQEEQRYQALKIHAEEKLDKANEEIAQVRT-- 679
Cdd:PTZ00121  1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAee 1741

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1209185300  680 -KAKAESAALHAGlrkEQMKVESLERALQQKNQEIEE 715
Cdd:PTZ00121  1742 dKKKAEEAKKDEE---EKKKIAHLKKEEEKKAEEIRK 1775
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
536-643 1.20e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 536 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLS 615
Cdd:COG4717   137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216

                          90       100
                  ....*....|....*....|....*...
gi 1209185300 616 DLFRRYENLKGVLEGFKKNEEALKKCAQ 643
Cdd:COG4717   217 EAQEELEELEEELEQLENELEAAALEER 244
PRK12704 PRK12704
phosphodiesterase; Provisional
 622-726 1.59e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 622 ENLKGVLEGFKKNEEALKKcaqDYLARVKQEEQRyqaLKIHAEEKLDKANEEIAQVRTKAKAESAAL---HAGLRKEQMK 698
Cdd:PRK12704   38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEE 111

                          90       100
                  ....*....|....*....|....*...
gi 1209185300 699 VESLERALQQKNQEIEELTKICDELIAK 726
Cdd:PRK12704  112 LEKKEKELEQKQQELEKKEEELEELIEE 139
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 594-727 2.43e-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: 40.29  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 594 QQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQR---------YQAL----- 659
Cdd:COG1579    20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEALqkeie 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1209185300 660 -----KIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 727
Cdd:COG1579   100 slkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
527-696 3.07e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 527 SDKTAVLTLIREEIITKEI-EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMieDEQRTSMTSQKSFQQLTMEKEQALA 605
Cdd:COG4717    62 QGRKPELNLKELKELEEELkEAEEKEEEYAELQEELEELEEELEELEAELEEL--REELEKLEKLLQLLPLYQELEALEA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 606 DLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQD-----------YLARVKQEEQRYQAL---KIHAEEKLDKAN 671
Cdd:COG4717   140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEEleelleqlslaTEEELQDLAEELEELqqrLAELEEELEEAQ 219

                         170       180
                  ....*....|....*....|....*
gi 1209185300 672 EEIAQVRTKAKAESAALHAGLRKEQ 696
Cdd:COG4717   220 EELEELEEELEQLENELEAAALEER 244
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 526-727 4.55e-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: 40.34  E-value: 4.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  526 ESDKTAVLTLIREEIITKEIEANEWKKKYEETRQ----EVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQL--TME 599
Cdd:pfam02463  182 TENLAELIIDLEELKLQELKLKEQAKKALEYYQLkeklELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSkqEIE 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  600 KEQALADLNSVERSLSdlfrryenlkgvlEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQvrt 679
Cdd:pfam02463  262 KEEEKLAQVLKENKEE-------------EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK--- 325

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1209185300  680 KAKAESAALHAGLRKEQMKvESLERALQQKNQEIEELTKICDELIAKL 727
Cdd:pfam02463  326 AEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLE 372
PTZ00121 PTZ00121
MAEBL; Provisional
 538-718 4.89e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  538 EEIITKEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMI--EDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLS 615
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIE--EVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  616 DLFRRYENLKGVLEGFKKNEEALKKCAQDylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKE 695
Cdd:PTZ00121  1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEE--AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728

                          170       180
                   ....*....|....*....|...
gi 1209185300  696 QMKVESLERALQQKNQEIEELTK 718
Cdd:PTZ00121  1729 KIKAEEAKKEAEEDKKKAEEAKK 1751
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
537-730 5.01e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 537 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSmTSQKSFQqltmEKEQALADLNSVERSLSD 616
Cdd:PRK03918  147 REKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK-EKEKELE----EVLREINEISSELPELRE 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 617 -------LFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEEIAQVRTKAKA--ESAA 687
Cdd:PRK03918  222 eleklekEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEyiKLSE 300

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1209185300 688 LHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKT 730
Cdd:PRK03918  301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 599-731 5.80e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  599 EKEQALA-DLNSVERSLSDLFRRYENLKGVL-EGFKKNEEALKKC--AQDYLARVKQEEQRYQALKIHAEEKLDKANEEI 674
Cdd:TIGR02169  674 AELQRLReRLEGLKRELSSLQSELRRIENRLdELSQELSDASRKIgeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1209185300  675 AQVRTKAK---AESAALHAGLRKEQMKVESLERAL-----QQKNQEIEELTKICDELIAKLGKTD 731
Cdd:TIGR02169  754 ENVKSELKeleARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIE 818
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 597-727 6.26e-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: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 597 TMEKEQ-ALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKI---HAEEKLDKANE 672
Cdd:COG1579     1 AMPEDLrALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELeieEVEARIKKYEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1209185300 673 EIAQVRTkAKAESAALH--AGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 727
Cdd:COG1579    81 QLGNVRN-NKEYEALQKeiESLKRRI---SDLEDEILELMERIEELEEELAELEAEL 133
PRK12704 PRK12704
phosphodiesterase; Provisional
 543-688 6.51e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 6.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 543 KEIEAN-EWKKKYEETRQEVLEMRKIVAEYEKTIAQmiedeqrtsmtsqksfqqltmeKEQALadlnsvERSLSDLFRRY 621
Cdd:PRK12704   58 ALLEAKeEIHKLRNEFEKELRERRNELQKLEKRLLQ----------------------KEENL------DRKLELLEKRE 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209185300 622 ENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQAL-KIHAEEkldkANEEI-AQVRTKAKAESAAL 688
Cdd:PRK12704  110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAEE----AKEILlEKVEEEARHEAAVL 174
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 527-715 6.70e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 527 SDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIE--DEQRTSMTSQKSFQQLTMEKEQAL 604
Cdd:COG3883    26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeiEERREELGERARALYRSGGSVSYL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 605 ADLNSVErSLSDLFRRYENLKGVLEGfkkneealkkcAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---- 680
Cdd:COG3883   106 DVLLGSE-SFSDFLDRLSALSKIADA-----------DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkael 173

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1209185300 681 --AKAESAALHAGLRKEQMKVESLERALQQKNQEIEE 715
Cdd:COG3883   174 eaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 533-691 8.09e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 8.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 533 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTS-------MTSQKSF------------ 593
Cdd:COG4942    64 IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGrqpplalLLSPEDFldavrrlqylky 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 594 -----QQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLD 668
Cdd:COG4942   144 laparREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223

                         170       180
                  ....*....|....*....|...
gi 1209185300 669 KANEEIAQVRTKAKAESAALHAG 691
Cdd:COG4942   224 ELEALIARLEAEAAAAAERTPAA 246
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 516-729 8.44e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 8.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  516 ESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAqmiedeqrtsmtsqksfqq 595
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE------------------- 871

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300  596 ltmEKEQALADLnsvERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKihaeEKLDKANEEIA 675
Cdd:TIGR02169  872 ---ELEAALRDL---ESRLGDLKKERDELEAQLRELERKIEELE-------AQIEKKRKRLSELK----AKLEALEEELS 934

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1209185300  676 QVRTKAKA--ESAALHAGLRKEQMKVESLERALQQKN-------QEIEELTKICDELIAKLGK 729
Cdd:TIGR02169  935 EIEDPKGEdeEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAK 997
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
537-705 8.94e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 537 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQ--KSFQQLTMEKEQALADLNSVERSL 614
Cdd:PRK03918  268 IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEeiNGIEERIKELEEKEERLEELKKKL 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185300 615 SDLFRRYENLKGVLEGFkknEEALKKCAQdyLARVKQEEQRYQALKIHAE-EKLDKANEEIAQVRTKAKAESAALHaGLR 693
Cdd:PRK03918  348 KELEKRLEELEERHELY---EEAKAKKEE--LERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELK-KEI 421

                         170
                  ....*....|...
gi 1209185300 694 KEQMK-VESLERA 705
Cdd:PRK03918  422 KELKKaIEELKKA 434
 
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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