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Conserved domains on  [gi|1209185315|ref|NP_001339728|]
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transforming acidic coiled-coil-containing protein 1 isoform 18 [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 ...
 375-573 3.61e-96

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: 291.96  E-value: 3.61e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 375 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIDE-QRTSMTSQKSFQQLTMEKEQAL 453
Cdd:pfam05010   2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEkQKQKELEHAEIQKVLEEKDQAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 454 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 533
Cdd:pfam05010  82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1209185315 534 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 573
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 ...
 375-573 3.61e-96

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: 291.96  E-value: 3.61e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 375 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIDE-QRTSMTSQKSFQQLTMEKEQAL 453
Cdd:pfam05010   2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEkQKQKELEHAEIQKVLEEKDQAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 454 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 533
Cdd:pfam05010  82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1209185315 534 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 573
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 378-576 5.16e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 5.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 378 DKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRK----IVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKEQAL 453
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyeLLAELARLEQDIARLEERRRELEERLEELEEELAELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 454 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 533
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1209185315 534 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 576
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 386-565 2.20e-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: 50.83  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  386 IREEIitKEIEANEWKKKYEETRQEVLEMRKIVAEYEKtiaQMIDEQRTSMTSQKSFQQLTMEKeqaladlNSVERSLSD 465
Cdd:TIGR02168  218 LKAEL--RELELALLVLRLEELREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLEV-------SELEEEIEE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  466 LFRRYENLKGVLEGFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---AKAESAALHAGLR 542
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKleeLKEELESLEAELE 361

                          170       180
                   ....*....|....*....|...
gi 1209185315  543 KEQMKVESLERALQQKNQEIEEL 565
Cdd:TIGR02168  362 ELEAELEELESRLEELEEQLETL 384
PTZ00121 PTZ00121
MAEBL; Provisional
 393-571 5.21e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 5.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  393 KEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKEQALADlnSVERSLSDLFRRYEN 472
Cdd:PTZ00121  1555 EELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAEE 1630

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  473 LKGVLEGFKKNE-------EALKKCAQDYLARVKQEEQRYQALKIHAEE-KLDKANEEIAQVRTKAKAESAALHAGLRK- 543
Cdd:PTZ00121  1631 EKKKVEQLKKKEaeekkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKk 1710

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1209185315  544 ---EQMKVESLERALQQKNQEIEELTKICDE 571
Cdd:PTZ00121  1711 eaeEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 375-573 3.61e-96

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: 291.96  E-value: 3.61e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 375 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIDE-QRTSMTSQKSFQQLTMEKEQAL 453
Cdd:pfam05010   2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEkQKQKELEHAEIQKVLEEKDQAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 454 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 533
Cdd:pfam05010  82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1209185315 534 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 573
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 378-576 5.16e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 5.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 378 DKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRK----IVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKEQAL 453
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyeLLAELARLEQDIARLEERRRELEERLEELEEELAELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 454 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 533
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1209185315 534 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 576
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 376-576 1.14e-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: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 376 ESDKTAVLTLIREeiITKEIEANEwkKKYEETRQEVLEMRKIVAEYEKTIAQM---IDEQRTSMTSQKSFQQLTMEKEQA 452
Cdd:COG4942    47 KKEEKALLKQLAA--LERRIAALA--RRIRALEQELAALEAELAELEKEIAELraeLEAQKEELAELLRALYRLGRQPPL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 453 LADLNSveRSLSDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQvrtkAKA 532
Cdd:COG4942   123 ALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEA----LKA 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1209185315 533 ESAALHAGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 576
Cdd:COG4942   196 ERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEA 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 386-565 2.20e-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: 50.83  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  386 IREEIitKEIEANEWKKKYEETRQEVLEMRKIVAEYEKtiaQMIDEQRTSMTSQKSFQQLTMEKeqaladlNSVERSLSD 465
Cdd:TIGR02168  218 LKAEL--RELELALLVLRLEELREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLEV-------SELEEEIEE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  466 LFRRYENLKGVLEGFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---AKAESAALHAGLR 542
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKleeLKEELESLEAELE 361

                          170       180
                   ....*....|....*....|...
gi 1209185315  543 KEQMKVESLERALQQKNQEIEEL 565
Cdd:TIGR02168  362 ELEAELEELESRLEELEEQLETL 384
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 385-576 3.43e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 385 LIREEIITKEIEAN---------------EWKKKYEETRQE--VLEMRKIVAEYEKTIAQMideqrtsmtsqksfQQLTM 447
Cdd:COG1196   188 LERLEDILGELERQleplerqaekaeryrELKEELKELEAEllLLKLRELEAELEELEAEL--------------EELEA 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 448 EKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCaqdyLARVKQEEQRYQALKIHAEEKLDKANEEIAQVR 527
Cdd:COG1196   254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELE 329

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1209185315 528 TK---AKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 576
Cdd:COG1196   330 EEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
PTZ00121 PTZ00121
MAEBL; Provisional
 393-571 5.21e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 5.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  393 KEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKEQALADlnSVERSLSDLFRRYEN 472
Cdd:PTZ00121  1555 EELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAEE 1630

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  473 LKGVLEGFKKNE-------EALKKCAQDYLARVKQEEQRYQALKIHAEE-KLDKANEEIAQVRTKAKAESAALHAGLRK- 543
Cdd:PTZ00121  1631 EKKKVEQLKKKEaeekkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKk 1710

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1209185315  544 ---EQMKVESLERALQQKNQEIEELTKICDE 571
Cdd:PTZ00121  1711 eaeEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 387-571 5.97e-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: 49.28  E-value: 5.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  387 REEIITKEIEANEwkKKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTsMTSQKSFQQltMEKEQALADLNSVERSLSDL 466
Cdd:TIGR02168  254 ELEELTAELQELE--EKLEELRLEVSELEEEIEELQKELYALANEISR-LEQQKQILR--ERLANLERQLEELEAQLEEL 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  467 FRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIH---AEEKLDKANEEIAQVRTKAKAESAALHAgLRK 543
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELQIASLNNEIER-LEA 407

                          170       180
                   ....*....|....*....|....*...
gi 1209185315  544 EqmkVESLERALQQKNQEIEELTKICDE 571
Cdd:TIGR02168  408 R---LERLEDRRERLQQEIEELLKKLEE 432
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
376-576 7.69e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 7.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 376 ESDKTAVLTLIR---EEIITKEIEA--NEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKE 450
Cdd:COG4717    33 EAGKSTLLAFIRamlLERLEKEADElfKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 451 QALADLNSVER--SLSDLFRRYENLKGVLEGFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRT 528
Cdd:COG4717   113 ELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSL 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1209185315 529 KAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 576
Cdd:COG4717   189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 387-565 1.58e-05

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: 46.05  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 387 REEIITKEI-----EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQM--IDEQRTSMtsQKSFQQLTMEKEQALADLNSV 459
Cdd:pfam13851  41 KEERNEKLMseiqqENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLknLKARLKVL--EKELKDLKWEHEVLEQRFEKV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 460 ERSLSDLFRRYEnlkgvlegfkkneealkKCAQDYLARVKQE----EQRYQALkihaEEKLDKANEEIAQVRTKAKAESA 535
Cdd:pfam13851 119 ERERDELYDKFE-----------------AAIQDVQQKTGLKnlllEKKLQAL----GETLEKKEAQLNEVLAAANLDPD 177

                         170       180       190
                  ....*....|....*....|....*....|
gi 1209185315 536 ALhaglrkeQMKVESLERALQQKNQEIEEL 565
Cdd:pfam13851 178 AL-------QAVTEKLEDVLESKNQLIKDL 200
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 383-572 4.62e-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: 46.50  E-value: 4.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  383 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSMTSQKSfQQLTMEKEQALADLNSVERS 462
Cdd:TIGR00618  692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH-QARTVLKARTEAHFNNNEEV 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  463 LSDLFR--RYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKaneEIAQVRTKAKAESAALHAg 540
Cdd:TIGR00618  771 TAALQTgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ---EEEQFLSRLEEKSATLGE- 846

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1209185315  541 LRKEQMKVESLERALQQKNQEIEELTKICDEL 572
Cdd:TIGR00618  847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
mukB PRK04863
chromosome partition protein MukB;
383-567 4.70e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.49  E-value: 4.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  383 LTLIREEIITKEIEAnewkkkYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKEQALADLNSVE-- 460
Cdd:PRK04863   884 LNLLADETLADRVEE------IREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqq 957

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  461 -RSLSDLFRR-----YENLKGVLEGFKKNEEALKKC---AQDYLARVKQE-----------EQRYQALK--IHA-EEKLD 517
Cdd:PRK04863   958 aFALTEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRleqAEQERTRAREQlrqaqaqlaqyNQVLASLKssYDAkRQMLQ 1037

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1209185315  518 KANEEIAQ--VRTKAKAESAA------LHAGLRKEQMKVESLERALQQKNQEIEELTK 567
Cdd:PRK04863  1038 ELKQELQDlgVPADSGAEERArarrdeLHARLSANRSRRNQLEKQLTFCEAEMDNLTK 1095
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
396-572 6.49e-05

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: 6.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 396 EANEW-KKKYEETRQEVLEMRKIVAEY-EKTIAQMIDEQRTSMTSQKSfqQLTMEKEQALADLNSVERSLSDLFRRYENL 473
Cdd:COG3206   175 KALEFlEEQLPELRKELEEAEAALEEFrQKNGLVDLSEEAKLLLQQLS--ELESQLAEARAELAEAEARLAALRAQLGSG 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 474 KGVLEGFKKNEEAlkkcaQDYLARVKQEEQRYQALKIHAEEK---LDKANEEIAQVRTKAKAESAALHAGLRKE----QM 546
Cdd:COG3206   253 PDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAElealQA 327

                         170       180
                  ....*....|....*....|....*.
gi 1209185315 547 KVESLERALQQKNQEIEELTKICDEL 572
Cdd:COG3206   328 REASLQAQLAQLEARLAELPELEAEL 353
PTZ00121 PTZ00121
MAEBL; Provisional
 402-571 6.90e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 6.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  402 KKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFK 481
Cdd:PTZ00121  1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  482 KNEEALKkcAQDYLARVKQEEQRYQALKIHAEEKldKANEEIAQVRTKAKAESAalhaglRKEQMKVESLERALQQKNQE 561
Cdd:PTZ00121  1310 KAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEA--KKAAEAAKAEAEAAADEA------EAAEEKAEAAEKKKEEAKKK 1379

                          170
                   ....*....|
gi 1209185315  562 IEELTKICDE 571
Cdd:PTZ00121  1380 ADAAKKKAEE 1389
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 386-567 8.01e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 8.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 386 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSmtsQKSFQQLTMEKEQALADLNSVERSLSD 465
Cdd:COG4942    32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAELRAELEAQKEELAE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 466 LFR------RYENLKGVL--EGFKKNEEALKkcaqdYLARVKQEEQRyqalkihAEEKLDKANEEIAQVRTKAKAESAAL 537
Cdd:COG4942   109 LLRalyrlgRQPPLALLLspEDFLDAVRRLQ-----YLKYLAPARRE-------QAEELRADLAELAALRAELEAERAEL 176

                         170       180       190
                  ....*....|....*....|....*....|
gi 1209185315 538 HAGLRKEQMKVESLERALQQKNQEIEELTK 567
Cdd:COG4942   177 EALLAELEEERAALEALKAERQKLLARLEK 206
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 383-576 8.04e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 8.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  383 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEyektIAQMIDEQRTSM-TSQKSFQQLTMEKEQALADLNSVER 461
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDLaRLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  462 SLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALkihaEEKLDKANEEIAQVRTKAKAESAALHAGL 541
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRIAATE 837

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1209185315  542 RKEQMKVESLERA---LQQKNQEIEELTKICDELIAKL 576
Cdd:TIGR02168  838 RRLEDLEEQIEELsedIESLAAEIEELEELIEELESEL 875
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 386-543 9.58e-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: 44.15  E-value: 9.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 386 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQM---IDEQRTSM---TSQKSFQQLTMEKEQALADLNSV 459
Cdd:COG1579    29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearIKKYEEQLgnvRNNKEYEALQKEIESLKRRISDL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 460 ERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHA 539
Cdd:COG1579   109 EDEILELMERIEELEEELAELEAELAELE-------AELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYE 181


                  ....
gi 1209185315 540 GLRK 543
Cdd:COG1579   182 RIRK 185
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 406-567 4.11e-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: 43.51  E-value: 4.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  406 ETRQEVLEMRKIVAEYEKTIAQmIDEQRTsmTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEgfkkNEE 485
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAE-LEKALA--ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLE 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  486 ALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVR---TKAKAESAALHAGLRKEQMKVESLERALQQKNQEI 562
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqiEQLKEELKALREALDELRAELTLLNEEAANLRERL 826


                   ....*
gi 1209185315  563 EELTK 567
Cdd:TIGR02168  827 ESLER 831
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
396-579 1.14e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 396 EANEWKKKYEETRQEVLEMRKIVAEY----------EKTIAQMIDEQRTSmtsqksfqQLTMEKEQALadlnsVERsLSD 465
Cdd:COG1340    79 ERDELNEKLNELREELDELRKELAELnkaggsidklRKEIERLEWRQQTE--------VLSPEEEKEL-----VEK-IKE 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 466 LFRRYENLKGVLEGFKKNEEALKKCAQdylARVKQEEQRyQALKIHAEEkLDKANEEIAQVRTKA---KAESAALHAGLR 542
Cdd:COG1340   145 LEKELEKAKKALEKNEKLKELRAELKE---LRKEAEEIH-KKIKELAEE-AQELHEEMIELYKEAdelRKEADELHKEIV 219

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1209185315 543 KEQMKVESLERALQQKNQEIEELTKICDELIAKLGKT 579
Cdd:COG1340   220 EAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 377-564 1.16e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 377 SDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQM---IDEQRTSMTSQKSFQQLTMEKEQAL 453
Cdd:COG3883    26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeaeIEERREELGERARALYRSGGSVSYL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 454 ADLNSVErSLSDLFRRYENLKGVLEGfkkneealkkcAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---- 529
Cdd:COG3883   106 DVLLGSE-SFSDFLDRLSALSKIADA-----------DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkael 173

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1209185315 530 --AKAESAALHAGLRKEQMKVESLERALQQKNQEIEE 564
Cdd:COG3883   174 eaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
401-567 1.17e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 401 KKKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSMTS-QKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEG 479
Cdd:COG4372     5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKlQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 480 FKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKN 559
Cdd:COG4372    85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163


                  ....*...
gi 1209185315 560 QEIEELTK 567
Cdd:COG4372   164 EELAALEQ 171
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 396-552 1.24e-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: 40.43  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 396 EANEWKKKYEET----RQEVLEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTME-KEQALADLNSVERSLS-DLFRR 469
Cdd:pfam04012  12 NIHEGLDKAEDPekmlEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKlEEKAQAALTKGNEELArEALAE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 470 YENLKGVLEGFKKN-------EEALKKCAQDYLARVKQEEQRYQALKihAEEKLDKANEEIAQVRTKAKAESAAlhAGLR 542
Cdd:pfam04012  92 KKSLEKQAEALETQlaqqrsaVEQLRKQLAALETKIQQLKAKKNLLK--ARLKAAKAQEAVQTSLGSLSTSSAT--DSFE 167

                         170
                  ....*....|
gi 1209185315 543 KEQMKVESLE 552
Cdd:pfam04012 168 RIEEKIEERE 177
PRK12704 PRK12704
phosphodiesterase; Provisional
 471-575 1.46e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 471 ENLKGVLEGFKKNEEALKKcaqDYLARVKQEEQRyqaLKIHAEEKLDKANEEIAQVRTKAKAESAAL---HAGLRKEQMK 547
Cdd:PRK12704   38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEE 111

                          90       100
                  ....*....|....*....|....*...
gi 1209185315 548 VESLERALQQKNQEIEELTKICDELIAK 575
Cdd:PRK12704  112 LEKKEKELEQKQQELEKKEEELEELIEE 139
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
377-545 2.35e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 377 SDKTAVLTLIREEIITKEI-EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQmIDEQRTSMTSQKSFQQLTMEKEQALAD 455
Cdd:COG4717    62 QGRKPELNLKELKELEEELkEAEEKEEEYAELQEELEELEEELEELEAELEE-LREELEKLEKLLQLLPLYQELEALEAE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 456 LNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQD-----------YLARVKQEEQRYQAL---KIHAEEKLDKANE 521
Cdd:COG4717   141 LAELPERLEELEERLEELRELEEELEELEAELAELQEEleelleqlslaTEEELQDLAEELEELqqrLAELEEELEEAQE 220

                         170       180
                  ....*....|....*....|....
gi 1209185315 522 EIAQVRTKAKAESAALHAGLRKEQ 545
Cdd:COG4717   221 ELEELEEELEQLENELEAAALEER 244
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
388-578 2.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 388 EEIITKEIEANewKKKYEETRQEVLEMRKivaeyektiaqmidEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLF 467
Cdd:PRK03918  513 KKYNLEELEKK--AEEYEKLKEKLIKLKG--------------EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 468 RRYENLKgvLEGFKKNEEALKKCAQDY-----LARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAAL----- 537
Cdd:PRK03918  577 KELEELG--FESVEELEERLKELEPFYneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELeelek 654

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1209185315 538 ------HAGLRKEQMKvesLERALQQKNQEIEELTKICDELIAKLGK 578
Cdd:PRK03918  655 kyseeeYEELREEYLE---LSRELAGLRAELEELEKRREEIKKTLEK 698
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 443-576 3.38e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 443 QQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQR---------YQAL----- 508
Cdd:COG1579    20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEALqkeie 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1209185315 509 -----KIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 576
Cdd:COG1579   100 slkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
387-579 4.59e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 387 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQqltmEKEQALADLNSVERSLSD- 465
Cdd:PRK03918  147 REKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELE----EVLREINEISSELPELREe 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 466 ------LFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEEIAQVRTKAKAESA--AL 537
Cdd:PRK03918  223 leklekEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEYIKlsEF 301

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1209185315 538 HAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKT 579
Cdd:PRK03918  302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
PRK12704 PRK12704
phosphodiesterase; Provisional
 393-537 4.64e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 393 KEIEAN-EWKKKYEETRQEVLEMRKIVAEYEKTIAQmideqrtsmtsqksfqqltmeKEQALadlnsvERSLSDLFRRYE 471
Cdd:PRK12704   58 ALLEAKeEIHKLRNEFEKELRERRNELQKLEKRLLQ---------------------KEENL------DRKLELLEKREE 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209185315 472 NLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQAL-KIHAEEkldkANEEI-AQVRTKAKAESAAL 537
Cdd:PRK12704  111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAEE----AKEILlEKVEEEARHEAAVL 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 385-572 5.70e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 5.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  385 LIREEIITKEIEANewKKKYEETRQEVLEMRKIVAEYEKTiaqmideQRTSMTsqKSFQQLTMEKEQALADLNSVERSLS 464
Cdd:TIGR02168  188 LDRLEDILNELERQ--LKSLERQAEKAERYKELKAELREL-------ELALLV--LRLEELREELEELQEELKEAEEELE 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  465 DLFRRYENLKGVLEGFKKNEEALKKCAQDY----------LARVKQEEQRYQALKIHAEEKLDKANEEIAQV---RTKAK 531
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEELqkelyalaneISRLEQQKQILRERLANLERQLEELEAQLEELeskLDELA 336

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1209185315  532 AESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDEL 572
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 394-578 8.60e-03

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 38.10  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 394 EIEANEWKKKYEETRQEVL-EMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFR---- 468
Cdd:pfam15665  13 EAEIQALKEAHEEEIQQILaETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEERELkaea 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 469 ----RYENL-KGVLEGFKKNEEALKKCAQdylARVKQEEQRYQALkihaEEKLDKANEEIAQVRTKAKaesaALHAGLRK 543
Cdd:pfam15665  93 ehrqRVVELsREVEEAKRAFEEKLESFEQ---LQAQFEQEKRKAL----EELRAKHRQEIQELLTTQR----AQSASSLA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1209185315 544 EQMKVESLERA-LQQKNQEIEELT----KICDELIAKLGK 578
Cdd:pfam15665 162 EQEKLEELHKAeLESLRKEVEDLRkekkKLAEEYEQKLSK 201
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 366-578 9.42e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 9.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  366 ESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAqmideqrtsmtsqksfqql 445
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE------------------- 871

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315  446 tmEKEQALADLnsvERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKihaeEKLDKANEEIAQ 525
Cdd:TIGR02169  872 --ELEAALRDL---ESRLGDLKKERDELEAQLRELERKIEELE-------AQIEKKRKRLSELK----AKLEALEEELSE 935

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209185315  526 VRTKAKA--ESAALHAGLRKEQMKVESLERALQQKN-------QEIEELTKICDELIAKLGK 578
Cdd:TIGR02169  936 IEDPKGEdeEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAK 997
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 446-576 9.80e-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: 37.98  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 446 TMEKEQ-ALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKI---HAEEKLDKANE 521
Cdd:COG1579     1 AMPEDLrALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELeieEVEARIKKYEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1209185315 522 EIAQVRTkAKAESAALH--AGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 576
Cdd:COG1579    81 QLGNVRN-NKEYEALQKeiESLKRRI---SDLEDEILELMERIEELEEELAELEAEL 133
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 374-578 9.99e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 38.76  E-value: 9.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 374 LSESDKTAVLTLIREEIIT--------KEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQmIDEQRTSMTSQKSfqQL 445
Cdd:PRK05771   36 LKEELSNERLRKLRSLLTKlsealdklRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEK-IEKEIKELEEEIS--EL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185315 446 TMEKEQALADLNSVE--RSLS---DLFRRYENLKGVLEGFKKNEEALKKCA--QDYLARVKQEEQRYQALKIHAEEKLDK 518
Cdd:PRK05771  113 ENEIKELEQEIERLEpwGNFDldlSLLLGFKYVSVFVGTVPEDKLEELKLEsdVENVEYISTDKGYVYVVVVVLKELSDE 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1209185315 519 ANEEIAQvrtkakaesaalhAGLRKEQMKVE-SLERALQQKNQEIEELTKICDELIAKLGK 578
Cdd:PRK05771  193 VEEELKK-------------LGFERLELEEEgTPSELIREIKEELEEIEKERESLLEELKE 240
 
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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