NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039779461|ref|XP_017177903|]
View 

transforming acidic coiled-coil-containing protein 2 isoform X41 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 366-566 2.17e-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: 2.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 366 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA 445
Cdd:pfam05010   1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 446 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 525
Cdd:pfam05010  81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039779461 526 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 566
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 366-566 2.17e-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: 2.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 366 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA 445
Cdd:pfam05010   1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 446 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 525
Cdd:pfam05010  81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039779461 526 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 566
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 370-568 6.89e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 6.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 370 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISH---QTVQQLVLEKEQAL 446
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 447 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 526
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039779461 527 QAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 568
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
364-560 5.99e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 5.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 364 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSI--SHQTVQQLVLE 441
Cdd:PRK03918  184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegSKRKLEEKIRE 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 442 KEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA------- 514
Cdd:PRK03918  264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerlee 342

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779461 515 ----------EIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTK 560
Cdd:PRK03918  343 lkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 370-568 6.71e-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: 6.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  370 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREksisHQTVQQLVLEKEQALADL 449
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL----SKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  450 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 529
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039779461  530 YQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 568
Cdd:TIGR02168  844 EE---QIEELSED-----IESLAAEIEELEELIEELESE 874
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 366-566 2.17e-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: 2.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 366 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA 445
Cdd:pfam05010   1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 446 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 525
Cdd:pfam05010  81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039779461 526 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 566
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 370-568 6.89e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 6.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 370 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISH---QTVQQLVLEKEQAL 446
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 447 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 526
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039779461 527 QAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 568
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
364-560 5.99e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 5.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 364 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSI--SHQTVQQLVLE 441
Cdd:PRK03918  184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegSKRKLEEKIRE 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 442 KEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA------- 514
Cdd:PRK03918  264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerlee 342

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779461 515 ----------EIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTK 560
Cdd:PRK03918  343 lkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 370-568 6.71e-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: 6.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  370 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREksisHQTVQQLVLEKEQALADL 449
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL----SKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  450 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 529
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039779461  530 YQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 568
Cdd:TIGR02168  844 EE---QIEELSED-----IESLAAEIEELEELIEELESE 874
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 370-568 1.00e-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: 47.84  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 370 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADL 449
Cdd:COG4942    31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEAQKEELAEL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 450 NSV---------------EKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRyqalkvhAEEKLDRANA 514
Cdd:COG4942   110 LRAlyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEA-------ERAELEALLA 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039779461 515 EIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 568
Cdd:COG4942   182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
394-569 1.39e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 394 DKYEESRREVVEMRKIVAEYEKtiaqmIEDEQREKSISHQTVQQLVLEKEQALADLnSVEKSLADLFRRYEKMKEVLEGF 473
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAEL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 474 RKNEEVLKKCAQEYLSRvkkeEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNK 553
Cdd:COG4717   145 PERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220

                         170
                  ....*....|....*.
gi 1039779461 554 EIEELTKICDELIAKM 569
Cdd:COG4717   221 ELEELEEELEQLENEL 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 385-558 2.68e-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: 47.36  E-value: 2.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  385 KEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYE 464
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  465 KMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaayqasLRKEQLRVDAL 544
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAELEEL 370

                          170
                   ....*....|....
gi 1039779461  545 ERTLEQKNKEIEEL 558
Cdd:TIGR02168  371 ESRLEELEEQLETL 384
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 364-557 7.87e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 7.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  364 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQRE--KSISHQTVQQLVLE 441
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkEKIGELEAEIASLE 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  442 KEQALADLN--SVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEE---KLDRANAEI 516
Cdd:TIGR02169  308 RSIAEKEREleDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETRDEL 387

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039779461  517 AQVRgKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEE 557
Cdd:TIGR02169  388 KDYR-EKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 367-551 1.05e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  367 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM--IEDEQREKSISHQT-VQQLVLEKE 443
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesRLEELEEQLETLRSkVAQLELQIA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  444 QALADLNSVEKSLADLFRRYEKMKEVLEGFRKN-EEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRgk 522
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE-- 474

                          170       180
                   ....*....|....*....|....*....
gi 1039779461  523 aqQEQAAYQASLRKEQLRVDALERTLEQK 551
Cdd:TIGR02168  475 --QALDAAERELAQLQARLDSLERLQENL 501
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 377-567 1.56e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  377 VARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIED-----EQREKSISHQTVQQ---------LVLEK 442
Cdd:TIGR02169  153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlrREREKAERYQALLKekreyegyeLLKEK 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  443 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVRG 521
Cdd:TIGR02169  233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLER 308

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1039779461  522 KAQQEQAAYQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 567
Cdd:TIGR02169  309 SIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 378-560 2.94e-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: 43.89  E-value: 2.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  378 ARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEK--- 454
Cdd:TIGR02168  668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQlee 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  455 SLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHA---EEKLDRANAEIAQVRGKAQQEQAAYQ 531
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEEAANLRERLE 827

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1039779461  532 ASLRK---EQLRVDALERTLEQKNKEIEELTK 560
Cdd:TIGR02168  828 SLERRiaaTERRLEDLEEQIEELSEDIESLAA 859
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
360-540 6.51e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 360 KPPGLLFQQPDLDSALQVARAEV---IAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIaQMIEDEQREKSISHQTVQ 436
Cdd:COG4717    65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAE 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 437 -QLVLEK-EQALADLNSVEKSLADLFRRYEKMKEVLEgfrkneEVLKKCAQEYLSRVKKEEQRYQAL---KVHAEEKLDR 511
Cdd:COG4717   144 lPERLEElEERLEELRELEEELEELEAELAELQEELE------ELLEQLSLATEEELQDLAEELEELqqrLAELEEELEE 217

                         170       180
                  ....*....|....*....|....*....
gi 1039779461 512 ANAEIAQVRGKAQQEQAAYQASLRKEQLR 540
Cdd:COG4717   218 AQEELEELEEELEQLENELEAAALEERLK 246
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
371-558 6.73e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 6.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  371 LDSALQVARAEVIAKEREVSEWRDKYEESRR--EVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALAD 448
Cdd:COG4913    622 LEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAE-LEAELERLDASSDDLAALEEQLEELEAE 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  449 LNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQvrgkaqqeqa 528
Cdd:COG4913    701 LEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLARLELRALLEERFAAALGDAVERELRE---------- 769

                          170       180       190
                   ....*....|....*....|....*....|
gi 1039779461  529 ayqaSLRKeqlRVDALERTLEQKNKEIEEL 558
Cdd:COG4913    770 ----NLEE---RIDALRARLNRAEEELERA 792
PTZ00121 PTZ00121
MAEBL; Provisional
 384-568 8.14e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 8.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  384 AKEREVSEWRDKYEESRREVVEMRKIVAEYEKTiaqmiEDEQREKSISHQTVQQLVLEKEQALAD--LNSVEKSLADLFR 461
Cdd:PTZ00121  1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK-----ADEAKKAAEAKKKADEAKKAEEAKKADeaKKAEEAKKADEAK 1540

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  462 RYEKMKEVLEgFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRK-EQLR 540
Cdd:PTZ00121  1541 KAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAK 1619

                          170       180
                   ....*....|....*....|....*....
gi 1039779461  541 VDALE-RTLEQKNKEIEELTKICDELIAK 568
Cdd:PTZ00121  1620 IKAEElKKAEEEKKKVEQLKKKEAEEKKK 1648
PTZ00121 PTZ00121
MAEBL; Provisional
 370-568 9.82e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 9.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  370 DLDSALQVARAEVIAKEREV--SEWRDKYEESRREvvEMRKIVAEYEKTIAQMIEdEQREKSISHQTVQQLVLEKEQAla 447
Cdd:PTZ00121  1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEA-- 1612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  448 dlnsveksladlfRRYEKMKEVLEGFRKNEEVLKKCAQeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQ 527
Cdd:PTZ00121  1613 -------------KKAEEAKIKAEELKKAEEEKKKVEQ---LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039779461  528 AAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 568
Cdd:PTZ00121  1677 AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
PTZ00121 PTZ00121
MAEBL; Provisional
 365-560 1.99e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  365 LFQQPDLDSALQVARAEviaKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQ 444
Cdd:PTZ00121  1600 LYEEEKKMKAEEAKKAE---EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  445 A--LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAEEKLDRANAEIAQV--- 519
Cdd:PTZ00121  1677 AeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKKEAEEDKKKAEEAKKdee 1754

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1039779461  520 ------RGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTK 560
Cdd:PTZ00121  1755 ekkkiaHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 370-520 2.68e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  370 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM---IEDEQREKSISHQTVQQLVLEKEQAL 446
Cdd:TIGR02169  340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYrekLEKLKREINELKRELDRLQEELQRLS 419

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779461  447 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKvhaeEKLDRANAEIAQVR 520
Cdd:TIGR02169  420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQ 489
PTZ00121 PTZ00121
MAEBL; Provisional
 372-560 3.80e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  372 DSALQVARAEVI--AKEREVSEWRDKYEESRREVVEMRKiVAEYEKTIAQMIEDEQREKsishQTVQQLVLEKEQaladl 449
Cdd:PTZ00121  1575 DKNMALRKAEEAkkAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEK----KKVEQLKKKEAE----- 1644

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  450 nsvEKSLADLFRRYEKMKEV-LEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKldranAEIAQVRgKAQQEQA 528
Cdd:PTZ00121  1645 ---EKKKAEELKKAEEENKIkAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELK-KKEAEEK 1715

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1039779461  529 AYQASLRKEQ----LRVDALERTLEQKNKEIEELTK 560
Cdd:PTZ00121  1716 KKAEELKKAEeenkIKAEEAKKEAEEDKKKAEEAKK 1751
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
387-560 4.79e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 387 REVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSIShqtvqqlvLEKEQALADLNSVEKSLADL---FRRY 463
Cdd:PRK03918  269 EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE--------KRLSRLEEEINGIEERIKELeekEERL 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 464 EKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAyqasLRKEQLRVDA 543
Cdd:PRK03918  341 EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE----ISKITARIGE 416

                         170
                  ....*....|....*..
gi 1039779461 544 LERTLEQKNKEIEELTK 560
Cdd:PRK03918  417 LKKEIKELKKAIEELKK 433
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
371-565 5.00e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 371 LDSALQVARAEViakeREVSEW-RDKYEESRREVVEMRKIVAEYEKtiAQMIEDEQREKSISHQTVQQLVLEKEQALADL 449
Cdd:COG3206   162 LEQNLELRREEA----RKALEFlEEQLPELRKELEEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 450 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVlkkcaQEYLSRVKKEEQRYQALKVHAEEK---LDRANAEIAQVRGKAQQE 526
Cdd:COG3206   236 AEAEARLAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQE 310

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1039779461 527 QAAYQASLRKE----QLRVDALERTLEQKNKEIEELTKICDEL 565
Cdd:COG3206   311 AQRILASLEAElealQAREASLQAQLAQLEARLAELPELEAEL 353
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
379-565 5.93e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 379 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAE------YEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSV 452
Cdd:PRK03918  458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKL 537

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 453 EKSLADLFRRYEKMKE-----------VLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEiaqvrg 521
Cdd:PRK03918  538 KGEIKSLKKELEKLEElkkklaelekkLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE------ 611

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039779461 522 kaqQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDEL 565
Cdd:PRK03918  612 ---KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
PRK12704 PRK12704
phosphodiesterase; Provisional
 464-568 6.54e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461 464 EKMKEVLEGFRKNEEVLKKcaqEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAA---YQASLRKEQLR 540
Cdd:PRK12704   38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENldrKLELLEKREEE 111

                          90       100
                  ....*....|....*....|....*...
gi 1039779461 541 VDALERTLEQKNKEIEELTKICDELIAK 568
Cdd:PRK12704  112 LEKKEKELEQKQQELEKKEEELEELIEE 139
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
435-559 9.84e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 9.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779461  435 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVL---KKCAQEYLS-RVKKEEQRYQALKVH---AEE 507
Cdd:COG4913    213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLepiRELAERYAAaRERLAELEYLRAALRlwfAQR 288

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039779461  508 KLDRANAEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEIEELT 559
Cdd:COG4913    289 RLELLEAELEELRAE-----------LARLEAELERLEARLDALREELDELE 329
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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