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Conserved domains on  [gi|1209185276|ref|NP_001339730|]
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transforming acidic coiled-coil-containing protein 1 isoform 20 [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 ...
172-371 9.55e-89

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: 266.16  E-value: 9.55e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 172 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQAL 251
Cdd:pfam05010   2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 252 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 331
Cdd:pfam05010  82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1209185276 332 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 371
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 ...
172-371 9.55e-89

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: 266.16  E-value: 9.55e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 172 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQAL 251
Cdd:pfam05010   2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 252 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 331
Cdd:pfam05010  82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1209185276 332 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 371
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-376 1.31e-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: 1.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276    2 AFSPWQILSPVQWAKWTWSAVRGGAAGEDEAGGPEGDPEEEDSQAETKSLSFRTTEQVKFLCFLLSGCKVKKHETQSLAL 81
Cdd:TIGR02168  558 AKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALEL 637
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276   82 DACSRDEGAVISQISDISNRDGHATDEEKLASTSCGQKSagAEVKGIEKEtCQKMEED---GSTVLGLLESSAEKApvsv 158
Cdd:TIGR02168  638 AKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERR--REIEELEEK-IEELEEKiaeLEKALAELRKELEEL---- 710
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  159 scggESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQK 238
Cdd:TIGR02168  711 ----EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  239 ---SFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKiHAEEKLD 315
Cdd:TIGR02168  787 leaQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-AEIEELE 865
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1209185276  316 KANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGK 376
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
175-374 1.83e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 175 DKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQ---KSFQQLTMEKEQAL 251
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELE 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 252 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 331
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1209185276 332 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 374
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
PTZ00121 PTZ00121
MAEBL; Provisional
190-369 2.89e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  190 KEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMIEdEQRTSMTSQKSFQQLTMEKEQALADlnSVERSLSDLFRRYE 269
Cdd:PTZ00121  1555 EELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAE 1629
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  270 NLKGVLEGFKKNE-------EALKKCAQDYLARVKQEEQRYQALKIHAEE-KLDKANEEIAQVRTKAKAESAALHAGLRK 341
Cdd:PTZ00121  1630 EEKKKVEQLKKKEaeekkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1209185276  342 ----EQMKVESLERALQQKNQEIEELTKICDE 369
Cdd:PTZ00121  1710 keaeEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
172-371 9.55e-89

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: 266.16  E-value: 9.55e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 172 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQAL 251
Cdd:pfam05010   2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 252 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 331
Cdd:pfam05010  82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1209185276 332 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 371
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-376 1.31e-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: 1.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276    2 AFSPWQILSPVQWAKWTWSAVRGGAAGEDEAGGPEGDPEEEDSQAETKSLSFRTTEQVKFLCFLLSGCKVKKHETQSLAL 81
Cdd:TIGR02168  558 AKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALEL 637
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276   82 DACSRDEGAVISQISDISNRDGHATDEEKLASTSCGQKSagAEVKGIEKEtCQKMEED---GSTVLGLLESSAEKApvsv 158
Cdd:TIGR02168  638 AKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERR--REIEELEEK-IEELEEKiaeLEKALAELRKELEEL---- 710
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  159 scggESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQK 238
Cdd:TIGR02168  711 ----EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  239 ---SFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKiHAEEKLD 315
Cdd:TIGR02168  787 leaQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-AEIEELE 865
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1209185276  316 KANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGK 376
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
175-374 1.83e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 175 DKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQ---KSFQQLTMEKEQAL 251
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELE 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 252 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 331
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1209185276 332 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 374
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
183-363 1.54e-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: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  183 IREEIitKEIEANEWKKKYEETRQEVLEMRKIVAEYEktiaQMIEDEQRTSMTSQKSFQQLTMEKeqaladlNSVERSLS 262
Cdd:TIGR02168  218 LKAEL--RELELALLVLRLEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLEV-------SELEEEIE 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  263 DLFRRYENLKGVLEGFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---AKAESAALHAGL 339
Cdd:TIGR02168  285 ELQKELYALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKleeLKEELESLEAEL 360
                          170       180
                   ....*....|....*....|....
gi 1209185276  340 RKEQMKVESLERALQQKNQEIEEL 363
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLETL 384
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
175-372 8.32e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 8.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 175 DKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKE---QAL 251
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrELE 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 252 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQ-EEQRYQALK--IHAEEKLDKANEEIAQVRTKA 328
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaEEALLEAEAelAEAEEELEELAEELLEALRAA 395
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1209185276 329 KAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIA 372
Cdd:COG1196   396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
180-374 1.39e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 180 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQmIEDEQRTSMTSQKSFQQLTMEKEQALADLNSV-- 257
Cdd:COG4942    36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEAQKEELAELLRAly 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 258 -------------ERSLSDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQv 324
Cdd:COG4942   115 rlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEA- 192
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1209185276 325 rtkAKAESAALHAGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 374
Cdd:COG4942   193 ---LKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEA 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
184-369 2.02e-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: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  184 REEIITKEIEANEwkKKYEETRQEVLEMRKIVAEYEKT---IAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERS 260
Cdd:TIGR02168  254 ELEELTAELQELE--EKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  261 LSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALkihaEEKLDKANEEIAQVRTKAKAESAALHAgLR 340
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL----EEQLETLRSKVAQLELQIASLNNEIER-LE 406
                          170       180
                   ....*....|....*....|....*....
gi 1209185276  341 KEqmkVESLERALQQKNQEIEELTKICDE 369
Cdd:TIGR02168  407 AR---LERLEDRRERLQQEIEELLKKLEE 432
PTZ00121 PTZ00121
MAEBL; Provisional
190-369 2.89e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  190 KEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMIEdEQRTSMTSQKSFQQLTMEKEQALADlnSVERSLSDLFRRYE 269
Cdd:PTZ00121  1555 EELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAE 1629
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  270 NLKGVLEGFKKNE-------EALKKCAQDYLARVKQEEQRYQALKIHAEE-KLDKANEEIAQVRTKAKAESAALHAGLRK 341
Cdd:PTZ00121  1630 EEKKKVEQLKKKEaeekkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1209185276  342 ----EQMKVESLERALQQKNQEIEELTKICDE 369
Cdd:PTZ00121  1710 keaeEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
182-374 3.77e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 182 LIREEIITKEIEAN--------EWKKKYEETRQE--VLEMRKIVAEYEKTIAQMIEDEQRTsmtsqksfQQLTMEKEQAL 251
Cdd:COG1196   188 LERLEDILGELERQleplerqaEKAERYRELKEElkELEAELLLLKLRELEAELEELEAEL--------EELEAELEELE 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 252 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCaqdyLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---A 328
Cdd:COG1196   260 AELAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELEEEleeL 335
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1209185276 329 KAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 374
Cdd:COG1196   336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
199-374 5.51e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 199 KKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRtsmtsqksFQQLTMEKEQALADLNSVER--SLSDLFRRYENLKGVLE 276
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEE--------LEELEAELEELREELEKLEKllQLLPLYQELEALEAELA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 277 GFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQK 356
Cdd:COG4717   143 ELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
                         170
                  ....*....|....*...
gi 1209185276 357 NQEIEELTKICDELIAKL 374
Cdd:COG4717   219 QEELEELEEELEQLENEL 236
mukB PRK04863
chromosome partition protein MukB;
180-365 5.93e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.25  E-value: 5.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  180 LTLIREEIITKEIEAnewkkkYEETRQEVLEMRKIVAEYEKTIAQmIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVE- 258
Cdd:PRK04863   884 LNLLADETLADRVEE------IREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKq 956
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  259 --RSLSDLFRR-----YENLKGVLEGFKKNEEALKKC---AQDYLARVKQE-----------EQRYQALK--IHA-EEKL 314
Cdd:PRK04863   957 qaFALTEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRleqAEQERTRAREQlrqaqaqlaqyNQVLASLKssYDAkRQML 1036
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1209185276  315 DKANEEIAQ--VRTKAKAESAA------LHAGLRKEQMKVESLERALQQKNQEIEELTK 365
Cdd:PRK04863  1037 QELKQELQDlgVPADSGAEERArarrdeLHARLSANRSRRNQLEKQLTFCEAEMDNLTK 1095
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
193-370 6.30e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 193 EANEW-KKKYEETRQEVLEMRKIVAEYeKTIAQMIEDEQRTSMTSQKSfQQLTMEKEQALADLNSVERSLSDLFRRYENL 271
Cdd:COG3206   175 KALEFlEEQLPELRKELEEAEAALEEF-RQKNGLVDLSEEAKLLLQQL-SELESQLAEARAELAEAEARLAALRAQLGSG 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 272 KGVLEGFKKNEEAlkkcaQDYLARVKQEEQRYQALKIHAEEK---LDKANEEIAQVRTKAKAESAALHAGLRKE----QM 344
Cdd:COG3206   253 PDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAElealQA 327
                         170       180
                  ....*....|....*....|....*.
gi 1209185276 345 KVESLERALQQKNQEIEELTKICDEL 370
Cdd:COG3206   328 REASLQAQLAQLEARLAELPELEAEL 353
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
184-363 1.20e-03

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: 39.50  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 184 REEIITKEI-----EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTsQKSFQQLTMEKEQALADLNSVE 258
Cdd:pfam13851  41 KEERNEKLMseiqqENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVL-EKELKDLKWEHEVLEQRFEKVE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 259 RSLSDLFRRYEnlkgvlegfkkneealkKCAQDYLARVKQE----EQRYQALkihaEEKLDKANEEIAQVRTKAKAESAA 334
Cdd:pfam13851 120 RERDELYDKFE-----------------AAIQDVQQKTGLKnlllEKKLQAL----GETLEKKEAQLNEVLAAANLDPDA 178
                         170       180
                  ....*....|....*....|....*....
gi 1209185276 335 LhaglrkeQMKVESLERALQQKNQEIEEL 363
Cdd:pfam13851 179 L-------QAVTEKLEDVLESKNQLIKDL 200
PTZ00121 PTZ00121
MAEBL; Provisional
199-369 2.07e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  199 KKYEETRQEVLEMRKivAEYEKTIAQMIE-DEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEG 277
Cdd:PTZ00121  1230 KKAEEAKKDAEEAKK--AEEERNNEEIRKfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  278 FKKNEEALKkcAQDYLARVKQEEQRYQALKIHAEEKldKANEEIAQVRTKAKAESAalhaglRKEQMKVESLERALQQKN 357
Cdd:PTZ00121  1308 KKKAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEA--KKAAEAAKAEAEAAADEA------EAAEEKAEAAEKKKEEAK 1377
                          170
                   ....*....|..
gi 1209185276  358 QEIEELTKICDE 369
Cdd:PTZ00121  1378 KKADAAKKKAEE 1389
PTZ00121 PTZ00121
MAEBL; Provisional
173-362 4.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 4.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  173 ESDKTAVLTLIREEIITKEIEAnewkKKYEETRQEVLEMRKivaeyEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALA 252
Cdd:PTZ00121  1591 EARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKK-----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  253 DLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLA----RVKQEEQRYQALKIHAEEKLDKANEEIAQVRT-- 326
Cdd:PTZ00121  1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAee 1741
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1209185276  327 -KAKAESAALHAGlrkEQMKVESLERALQQKNQEIEE 362
Cdd:PTZ00121  1742 dKKKAEEAKKDEE---EKKKIAHLKKEEEKKAEEIRK 1775
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
180-370 4.98e-03

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: 39.18  E-value: 4.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  180 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQmiEDEQRTSMTSQKSFQQLTMEKEQALADLNSVER 259
Cdd:TIGR00618  692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA--REDALNQSLKELMHQARTVLKARTEAHFNNNEE 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276  260 SLSDLFR--RYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKaneEIAQVRTKAKAESAALHA 337
Cdd:TIGR00618  770 VTAALQTgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ---EEEQFLSRLEEKSATLGE 846
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1209185276  338 gLRKEQMKVESLERALQQKNQEIEELTKICDEL 370
Cdd:TIGR00618  847 -ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
183-341 7.71e-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: 37.60  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 183 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQR-----TSMTSQKSFQQLTMEKEQALADLNSV 257
Cdd:COG1579    29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlGNVRNNKEYEALQKEIESLKRRISDL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 258 ERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHA 337
Cdd:COG1579   109 EDEILELMERIEELEEELAELEAELAELE-------AELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYE 181

                  ....
gi 1209185276 338 GLRK 341
Cdd:COG1579   182 RIRK 185
PRK12704 PRK12704
phosphodiesterase; Provisional
269-373 8.61e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185276 269 ENLKGVLEGFKKNEEALKKcaqDYLARVKQEEQRyqaLKIHAEEKLDKANEEIAQVRTKAKAESAAL---HAGLRKEQMK 345
Cdd:PRK12704   38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEE 111
                          90       100
                  ....*....|....*....|....*...
gi 1209185276 346 VESLERALQQKNQEIEELTKICDELIAK 373
Cdd:PRK12704  112 LEKKEKELEQKQQELEKKEEELEELIEE 139
 
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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