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Conserved domains on  [gi|768025302|ref|XP_011528570|]
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coiled-coil domain-containing protein 157 isoform X8 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 276-501 1.06e-14

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.28  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLltetSDLKT 355
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEE 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 356 KMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEgagqqvcwASTELDKEKA 435
Cdd:COG1196  317 RLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--------AEEELEELAE 386

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768025302 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQ 501
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 276-501 1.06e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.28  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLltetSDLKT 355
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEE 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 356 KMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEgagqqvcwASTELDKEKA 435
Cdd:COG1196  317 RLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--------AEEELEELAE 386

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768025302 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQ 501
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 277-487 3.62e-13

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: 72.40  E-value: 3.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQalKQEQGARRR------------QAEEDEQCLSEWEHDKQ 344
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA--EVEQLEERIaqlskelteleaEIEELEERLEEAEEELA 778

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   345 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEG-----------ERRAAAERQVQQLEEQVQQLEAQVQLLV 413
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlrerlesleRRIAATERRLEDLEEQIEELSEDIESLA 858

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768025302   414 GRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQ 487
Cdd:TIGR02168  859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 291-484 3.92e-06

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 49.51  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  291 EALRAQLEEAegqkdglRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKqqlltetSDLKTKMATLERELKQQRES 370
Cdd:pfam07888  30 ELLQNRLEEC-------LQERAELLQAQEAANRQREKEKERYKRDREQWERQR-------RELESRVAELKEELRQSREK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  371 TQAVEAKAQQLQEEGERRAAAERqvqQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRH------- 443
Cdd:pfam07888  96 HEELEEKYKELSASSEELSEEKD---ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeeeae 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 768025302  444 QESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE 484
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQD 213
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
278-505 5.53e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 5.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 278 EQRKDLTRLSKHV---EALRAQLEEAEGQKDGLRKQAGKLEQALKQeqgaRRRQAEEDEQCLSEWEhDKQQLLTETSDLK 354
Cdd:PRK03918 218 ELREELEKLEKEVkelEELKEEIEELEKELESLEGSKRKLEEKIRE----LEERIEELKKEIEELE-EKVKELKELKEKA 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 355 TKMATLERELKQQRESTQAVE---AKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQqvcwastELD 431
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEkrlSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE-------LYE 365

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768025302 432 KEKARVDSMVRHQESLQAKQ-RALLKQLDSLDQEREELRGSLDEAEAQRARVeEQLQSEREQGQCQLRAQQGRCP 505
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGEL-KKEIKELKKAIEELKKAKGKCP 439
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 278-367 8.05e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 37.01  E-value: 8.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAgKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:smart01071  53 YELIMNDHLNKRIDKLLKGLREEELSPETPTYNE-MLAELQDQLKKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKL 131

                           90
                   ....*....|
gi 768025302   358 ATLERELKQQ 367
Cdd:smart01071 132 DELEKEEKKK 141
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 276-501 1.06e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.28  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLltetSDLKT 355
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEE 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 356 KMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEgagqqvcwASTELDKEKA 435
Cdd:COG1196  317 RLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--------AEEELEELAE 386

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768025302 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQ 501
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-501 4.64e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.97  E-value: 4.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDL 353
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 354 KTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwASTELDKE 433
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA---EEALLERL 416

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768025302 434 KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQ 501
Cdd:COG1196  417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 277-487 3.62e-13

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: 72.40  E-value: 3.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQalKQEQGARRR------------QAEEDEQCLSEWEHDKQ 344
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA--EVEQLEERIaqlskelteleaEIEELEERLEEAEEELA 778

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   345 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEG-----------ERRAAAERQVQQLEEQVQQLEAQVQLLV 413
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlrerlesleRRIAATERRLEDLEEQIEELSEDIESLA 858

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768025302   414 GRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQ 487
Cdd:TIGR02168  859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 276-509 1.69e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 1.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKT 355
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 356 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwasTELDKEKA 435
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL----EEAAEEEA 452

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768025302 436 RVDsmvRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQGRCPRALS 509
Cdd:COG1196  453 ELE---EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 276-492 8.56e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 8.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQQLLTETSDLKT 355
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----LEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 356 KMATLERELKQQRESTQAVEAKAQQLQEEgerRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKA 435
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768025302 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQ 492
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 280-492 4.76e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 4.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 280 RKDLTRlskhVEALRAQLEeaeGQKDGLRKQAGKLEQALKQEQGARRRQAE----EDEQCLSEWEHDKQQLL---TETSD 352
Cdd:COG1196  185 EENLER----LEDILGELE---RQLEPLERQAEKAERYRELKEELKELEAEllllKLRELEAELEELEAELEeleAELEE 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 353 LKTKMATLERELKQQRESTQAVEAKAQQLQEEgERRAAAErqvqqleeqVQQLEAQVQLLVGRLEGAGQqvcwastELDK 432
Cdd:COG1196  258 LEAELAELEAELEELRLELEELELELEEAQAE-EYELLAE---------LARLEQDIARLEERRRELEE-------RLEE 320

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 433 EKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQ 492
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 277-511 1.13e-10

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: 64.31  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQagklEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTK 356
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKE----LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   357 MATLERELKQQRESTQAVEAKAQQLQEE-----------GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCW 425
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQieqlkeelkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   426 ASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcQLRAQQGRCP 505
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS-ELRRELEELR 921


                   ....*.
gi 768025302   506 RALSTM 511
Cdd:TIGR02168  922 EKLAQL 927
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
276-508 2.41e-10

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 63.40  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  276 AAEQRKDLTRLSKHVEALRAQ---LEEAEGQKDGLRKQAGKLEQalkQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSD 352
Cdd:COG4913   230 LVEHFDDLERAHEALEDAREQielLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAELEELRAELAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  353 LKTKMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwasteldk 432
Cdd:COG4913   307 LEAELERLEARLDALRE--ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL--------- 375

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768025302  433 ekarvdsmVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQ---LQSEREqgqcQLRAQQGRCPRAL 508
Cdd:COG4913   376 --------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRElreLEAEIA----SLERRKSNIPARL 442
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 278-503 3.41e-10

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: 62.77  E-value: 3.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQeqgaRRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   358 ATLERELKqqrESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 437
Cdd:TIGR02168  750 AQLSKELT---ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768025302   438 DSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS---EREQGQCQLRAQQGR 503
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSE 895
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 277-504 5.93e-10

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: 62.00  E-value: 5.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAL--------------------KQEQGARRRQAEEDEQCL 336
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeelqkelyalaneisrleqqKQILRERLANLERQLEEL 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   337 SEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQA-VEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGR 415
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAeLEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   416 LEGAGQQVcwasTELDKEKARVDSMVR-HQESLQAKQRALLK-QLDSLDQEREELRGSLDEAEAQRARVEEQL---QSER 490
Cdd:TIGR02168  402 IERLEARL----ERLEDRRERLQQEIEeLLKKLEEAELKELQaELEELEEELEELQEELERLEEALEELREELeeaEQAL 477

                          250
                   ....*....|....
gi 768025302   491 EQGQCQLRAQQGRC 504
Cdd:TIGR02168  478 DAAERELAQLQARL 491
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 266-501 1.12e-08

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: 57.08  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 266 PLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgaRRRQAEEDEQclsewehdkQQ 345
Cdd:COG4942   12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA--RRIRALEQEL---------AA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 346 LLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEG--------ERRAAAERQVQQLEEQVQQLEAQVQLLVGRLE 417
Cdd:COG4942   81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 418 gagqqvcwastELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQL 497
Cdd:COG4942  161 -----------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229


                 ....
gi 768025302 498 RAQQ 501
Cdd:COG4942  230 ARLE 233
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 276-501 1.23e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   276 AAEQRKDLTRLSKHVE------ALRAQLEEAEGQKDGLRKQA--GKLEQALKQEQGARRRQAEEDEQcLSEWEHDKQQLL 347
Cdd:TIGR02168  195 LNELERQLKSLERQAEkaerykELKAELRELELALLVLRLEElrEELEELQEELKEAEEELEELTAE-LQELEEKLEELR 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   348 TETSDLKTKMATLERELKqqrESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAS 427
Cdd:TIGR02168  274 LEVSELEEEIEELQKELY---ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768025302   428 TELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE---EQLQSEREQGQCQLRAQQ 501
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarlERLEDRRERLQQEIEELL 427
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 285-484 1.77e-08

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: 57.39  E-value: 1.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   285 RLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQC---LSEWEHDKQQLLTETSDLKTKMATLE 361
Cdd:TIGR02169  291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELereIEEERKRRDKLTEEYAELKEELEDLR 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   362 RELKQQRESTQAVEAKAQQLQEE----GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwasTELDKEKARV 437
Cdd:TIGR02169  371 AELEEVDKEFAETRDELKDYREKleklKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI----NELEEEKEDK 446

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 768025302   438 DSMVRHQE-----------SLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE 484
Cdd:TIGR02169  447 ALEIKKQEwkleqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 280-507 5.37e-08

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: 55.84  E-value: 5.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   280 RKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLE--QALKQEQGARRrqaeedeqcLSEWEHDKQQLLTETSDLKTKM 357
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYE---------GYELLKEKEALERQKEAIERQL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   358 ATLERELKQQRESTQA----VEAKAQQLQEEGER-RAAAERQVQQLEEQVQQLEAQVQLLVG-------RLEGAGQQVCW 425
Cdd:TIGR02169  247 ASLEEELEKLTEEISElekrLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERsiaekerELEDAEERLAK 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   426 ASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDE--AEAQRARVE--------EQLQSEREQGQC 495
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdKEFAETRDElkdyreklEKLKREINELKR 406

                          250
                   ....*....|..
gi 768025302   496 QLRAQQGRCPRA 507
Cdd:TIGR02169  407 ELDRLQEELQRL 418
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
276-475 1.40e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  276 AAEQRKDLTRLSKHVE---ALRAQLEEAEGQKDGLRKQAGKLEQAL-KQEQGARRRQAEEDEQCLSEWEHDKQQLLTETS 351
Cdd:COG4913   247 AREQIELLEPIRELAEryaAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELD 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  352 DLKTKMAT--------LERELKQQRESTQAVEAKAQQLQEegerraAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQV 423
Cdd:COG4913   327 ELEAQIRGnggdrleqLEREIERLERELEERERRRARLEA------LLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768025302  424 CWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEA 475
Cdd:COG4913   401 EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
277-492 1.46e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAlkQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLktk 356
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASSDDL--- 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  357 mATLERELKQQRESTQAVEAKAQQLQEEgERRAAAERQvqqleeqvqQLEAQVQLLVGRLEGAGQQVC-WASTELDKEKA 435
Cdd:COG4913   688 -AALEEQLEELEAELEELEEELDELKGE-IGRLEKELE---------QAEEELDELQDRLEAAEDLARlELRALLEERFA 756

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768025302  436 rvdsmvrhqeslQAKQRALLKQLdsldqeREELRGSLDEAEAQRARVEEQLQSEREQ 492
Cdd:COG4913   757 ------------AALGDAVEREL------RENLEERIDALRARLNRAEEELERAMRA 795
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
291-494 1.07e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 291 EALRAQLEEA-EGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWehdkQQLLTETSDLKTKMATLERELKQQRE 369
Cdd:COG4717   41 AFIRAMLLERlEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELRE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 370 STQAVEaKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVG---RLEGAGQQVCWASTELDKEKARVDSMVRHQ-E 445
Cdd:COG4717  117 ELEKLE-KLLQLLPLYQELEALEAELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEEElQ 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 768025302 446 SLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQ 494
Cdd:COG4717  196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
253-393 2.42e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  253 QFQQLVQDSMGLRPLpAATVGRWAAEQRKDL-----TRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRR 327
Cdd:COG4913   263 RYAAARERLAELEYL-RAALRLWFAQRRLELleaelEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE 341

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768025302  328 QAEED----EQCLSEWEHDKQQLLTETSDLKTKMATLERELK-QQRESTQAVEAKAQQLQEEGERRAAAER 393
Cdd:COG4913   342 QLEREierlERELEERERRRARLEALLAALGLPLPASAEEFAaLRAEAAALLEALEEELEALEEALAEAEA 412
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 291-484 3.92e-06

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 49.51  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  291 EALRAQLEEAegqkdglRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKqqlltetSDLKTKMATLERELKQQRES 370
Cdd:pfam07888  30 ELLQNRLEEC-------LQERAELLQAQEAANRQREKEKERYKRDREQWERQR-------RELESRVAELKEELRQSREK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  371 TQAVEAKAQQLQEEGERRAAAERqvqQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRH------- 443
Cdd:pfam07888  96 HEELEEKYKELSASSEELSEEKD---ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeeeae 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 768025302  444 QESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE 484
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQD 213
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
339-500 4.49e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 4.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  339 WEHDKQQLLTET----SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEgERRAAAERQVQQLEEQVQQLEAQVQLLVG 414
Cdd:COG4913   590 HEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAE-LDALQERREALQRLAEYSWDEIDVASAER 668

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  415 RLEGAGQQVcwasTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQ 494
Cdd:COG4913   669 EIAELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744


                  ....*.
gi 768025302  495 CQLRAQ 500
Cdd:COG4913   745 LELRAL 750
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
278-505 5.53e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 5.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 278 EQRKDLTRLSKHV---EALRAQLEEAEGQKDGLRKQAGKLEQALKQeqgaRRRQAEEDEQCLSEWEhDKQQLLTETSDLK 354
Cdd:PRK03918 218 ELREELEKLEKEVkelEELKEEIEELEKELESLEGSKRKLEEKIRE----LEERIEELKKEIEELE-EKVKELKELKEKA 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 355 TKMATLERELKQQRESTQAVE---AKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQqvcwastELD 431
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEkrlSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE-------LYE 365

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768025302 432 KEKARVDSMVRHQESLQAKQ-RALLKQLDSLDQEREELRGSLDEAEAQRARVeEQLQSEREQGQCQLRAQQGRCP 505
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGEL-KKEIKELKKAIEELKKAKGKCP 439
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 360-494 9.37e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 9.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 360 LERELKQQRES--TQAVEA-KAQQLQEEGERRAAAERQVQ--QLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEK 434
Cdd:COG1196  194 ILGELERQLEPleRQAEKAeRYRELKEELKELEAELLLLKlrELEAELEELEAELEELEAELEELEAELAELEAELEELR 273

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 435 ARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQ 494
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
278-501 1.70e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQC-------LSEWEHDKQQLLTET 350
Cdd:COG4717  122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELeelleqlSLATEEELQDLAEEL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 351 SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAER-------------------QVQQLEEQVQQLEAQVQL 411
Cdd:COG4717  202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallgLGGSLLSLILTIAGVLFL 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 412 LVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLD-SLDQEREELRGSLDEAEA--QRARVEEQLQS 488
Cdd:COG4717  282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEElqELLREAEELEE 361

                        250
                 ....*....|...
gi 768025302 489 EREQGQCQLRAQQ 501
Cdd:COG4717  362 ELQLEELEQEIAA 374
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 275-386 2.65e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  275 WAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ---EQGARRRQAEEDEQCLSEWEHDKQQLLTETS 351
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsesENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 768025302  352 DLKTKMATLERELKQQRESTQAVEAKAQQLQEEGE 386
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
277-500 2.81e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 277 AEQRKDLTRLskhVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSewehdkqqlltETSDLKTK 356
Cdd:PRK02224 515 EERREDLEEL---IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE-----------EVAELNSK 580

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 357 MATLERE---LKQQRESTQAVEAKAQQLQEEGERRAA-----AERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAST 428
Cdd:PRK02224 581 LAELKERiesLERIRTLLAAIADAEDEIERLREKREAlaelnDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEE 660

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768025302 429 ELDKEKARVDSMVRHQESLQAKQRAL---LKQLDSLDQEREELRGSLDEAEAQRARVEEqLQSEREQGQCQLRAQ 500
Cdd:PRK02224 661 YLEQVEEKLDELREERDDLQAEIGAVeneLEELEELRERREALENRVEALEALYDEAEE-LESMYGDLRAELRQR 734
PTZ00121 PTZ00121
MAEBL; Provisional
 274-392 3.25e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRK-----QAGKLEQALKQEQGARR----RQAEEDEQCLSEWEHDKQ 344
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKaeeenKIKAAEEAKKAEEDKKKaeeaKKAEEDEKKAAEALKKEA 1698

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 768025302  345 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQ--EEGERRAAAE 392
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKkeAEEDKKKAEE 1748
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 276-503 3.28e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.87  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALK-------QEQGARRRQAEEDEQC---------LSEW 339
Cdd:COG3096   363 LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiQYQQAVQALEKARALCglpdltpenAEDY 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  340 EH---DKQQLLTETS-DLKTKMATLERELKQQRESTQAVEAKAqqlqEEGERRAAAERqvqqlEEQVQQLEAQVQLLVGR 415
Cdd:COG3096   443 LAafrAKEQQATEEVlELEQKLSVADAARRQFEKAYELVCKIA----GEVERSQAWQT-----ARELLRRYRSQQALAQR 513

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  416 LEGAGQQVcwasTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQlQSEREQGQC 495
Cdd:COG3096   514 LQQLRAQL----AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ-RSELRQQLE 588


                  ....*...
gi 768025302  496 QLRAQQGR 503
Cdd:COG3096   589 QLRARIKE 596
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
371-501 5.51e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  371 TQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTEldKEKARVDSMVRHQESLQAK 450
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE--REIAELEAELERLDASSDD 686

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768025302  451 QRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQL-QSEREQGQCQLRAQQ 501
Cdd:COG4913   687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELeQAEEELDELQDRLEA 738
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 276-456 7.64e-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: 45.43  E-value: 7.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALkQEQGARRRQAEEDEQCLSEwehDKQQLLTETSDLKT 355
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-ETLRSKVAQLELQIASLNN---EIERLEARLERLED 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   356 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAErqvqqleeqvqqLEAQVQLLVGRLEGAGQQVCWASTELDKEKA 435
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEE------------LQEELERLEEALEELREELEEAEQALDAAER 482

                          170       180
                   ....*....|....*....|.
gi 768025302   436 RVDSMVRHQESLQAKQRALLK 456
Cdd:TIGR02168  483 ELAQLQARLDSLERLQENLEG 503
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 276-492 1.32e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.78  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   276 AAEQRKDLtrlSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSE----------------- 338
Cdd:pfam01576  290 AEKQRRDL---GEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEmrqkhtqaleelteqle 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   339 --------WEHDKQQLLTETSDLKTKMATLErelKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQ 410
Cdd:pfam01576  367 qakrnkanLEKAKQALESENAELQAELRTLQ---QAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELE 443

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   411 LLVGRLEGAGQQvcwaSTELDKEKARVDSMVRH-QESLQAKQRALLK---QLDSLDQEREELRGSLDEAEAQRARVEEQL 486
Cdd:pfam01576  444 SVSSLLNEAEGK----NIKLSKDVSSLESQLQDtQELLQEETRQKLNlstRLRQLEDERNSLQEQLEEEEEAKRNVERQL 519


                   ....*.
gi 768025302   487 QSEREQ 492
Cdd:pfam01576  520 STLQAQ 525
PTZ00121 PTZ00121
MAEBL; Provisional
 274-494 1.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  274 RWAAEQRKDLTRLSKHVEALRAQlEEAEGQKDGLRK--QAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETS 351
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKA-AEAKKKADEAKKaeEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  352 DL-KTKMATLERE-----LKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQllvgRLEGAGQQVCW 425
Cdd:PTZ00121 1562 EKkKAEEAKKAEEdknmaLRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK----KAEEEKKKVEQ 1637

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768025302  426 ASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRgsldEAEAQRARVEEQLQSEREQGQ 494
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK----KAEEDEKKAAEALKKEAEEAK 1702
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 282-387 1.46e-04

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 44.67  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  282 DLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAlkqeqgarRRQAEEDEQCLSE----WEHDKQQLLTETSDLKTKM 357
Cdd:pfam05911 703 ELASCTENLESTKSQLQESEQLIAELRSELASLKES--------NSLAETQLKCMAEsyedLETRLTELEAELNELRQKF 774

                          90       100       110
                  ....*....|....*....|....*....|
gi 768025302  358 ATLERELKQQRESTQAVEAKAQQLQEEGER 387
Cdd:pfam05911 775 EALEVELEEEKNCHEELEAKCLELQEQLER 804
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-468 1.71e-04

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: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDL 353
Cdd:COG1196  627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 354 KTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwAS------ 427
Cdd:COG1196  707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI--EAlgpvnl 784

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 768025302 428 ---TELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREEL 468
Cdd:COG1196  785 laiEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
277-383 1.78e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEqclsewehdkqqlltETSDLKTK 356
Cdd:COG2433  409 TEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR---------------EISRLDRE 473

                         90       100
                 ....*....|....*....|....*..
gi 768025302 357 MATLERELKQQRESTQAVEAKAQQLQE 383
Cdd:COG2433  474 IERLERELEEERERIEELKRKLERLKE 500
PTZ00121 PTZ00121
MAEBL; Provisional
 269-498 2.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  269 AATVGRWAAEQRKD-LTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLL 347
Cdd:PTZ00121 1344 AAEAAKAEAEAAADeAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  348 TETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwaS 427
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK----A 1499

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  428 TELDK---EKARVDSMVRHQESLQAKQRALLKQLDSLDQER--------EELRGSLDEAEAQRARVEEQLQSEREQGQCQ 496
Cdd:PTZ00121 1500 DEAKKaaeAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaeekkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579


                  ..
gi 768025302  497 LR 498
Cdd:PTZ00121 1580 LR 1581
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
276-452 2.91e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQA--EEDEQCLSEWEHDKQQLltetsdl 353
Cdd:COG4717   83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleAELAELPERLEELEERL------- 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 354 ktkmatleRELKQQRESTQAVEAKAQQLQEegERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKE 433
Cdd:COG4717  156 --------EELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225

                        170
                 ....*....|....*....
gi 768025302 434 KARVDSMVRHQESLQAKQR 452
Cdd:COG4717  226 EEELEQLENELEAAALEER 244
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 267-492 3.00e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.67  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   267 LPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR--RQAEEDeqcLSEWEHDKQ 344
Cdd:pfam12128  587 LKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTalKNARLD---LRRLFDEKQ 663

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   345 QLltetSDLKTKmaTLERELKQQRESTQAVEAKAQQLqeEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVc 424
Cdd:pfam12128  664 SE----KDKKNK--ALAERKDSANERLNSLEAQLKQL--DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL- 734

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768025302   425 waSTELDKEKARVDsmvRHQESLQAKQRALLKQLD-------SLDQEREELRGSLDEAEAQRARVEEQLQSEREQ 492
Cdd:pfam12128  735 --KAAIAARRSGAK---AELKALETWYKRDLASLGvdpdviaKLKREIRTLERKIERIAVRRQEVLRYFDWYQET 804
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 278-392 3.06e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 3.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKqeqgARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:TIGR02169  403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE----DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 768025302   358 ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAE 392
Cdd:TIGR02169  479 DRVEKELSKLQRELAEAEAQARASEERVRGGRAVE 513
PTZ00121 PTZ00121
MAEBL; Provisional
 277-492 3.53e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  277 AEQRKDLTRLSKHVEALRA-QLEEAEGQK--DGLRK--------QAGKLEQALKQEQ--GARRRQAEEDEQCLSEWEHDK 343
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKAdEAKKAEEKKkaDELKKaeelkkaeEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEV 1597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  344 QQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQV 423
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768025302  424 CWASTELDKEKARVDSMVRHQESlQAKQRALLKQLDSLDQEREELRgsldEAEAQRARVEEQLQSEREQ 492
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKKKAEELK----KAEEENKIKAEEAKKEAEE 1741
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 281-474 4.26e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 4.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 281 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEqgarRRQAEEDEQCLSEWEHDK--QQLLTETSDLKTKMA 358
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQLGNVRNNKeyEALQKEIESLKRRIS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 359 TLERELKQQREstqAVEAKAQQLQEEGERRAAAErqvqqleeqvqqleaqvqllvgrlegagqqvcwasTELDKEKARVD 438
Cdd:COG1579  107 DLEDEILELME---RIEELEEELAELEAELAELE-----------------------------------AELEEKKAELD 148

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 768025302 439 smvrhqeslqAKQRALLKQLDSLDQEREELRGSLDE 474
Cdd:COG1579  149 ----------EELAELEAELEELEAEREELAAKIPP 174
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 310-492 5.67e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 5.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 310 QAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE-GERR 388
Cdd:COG3883   13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 389 AAAERQVQQLEEQVQQLEAQ-VQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREE 467
Cdd:COG3883   93 RALYRSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172

                        170       180
                 ....*....|....*....|....*
gi 768025302 468 LRGSLDEAEAQRARVEEQLQSEREQ 492
Cdd:COG3883  173 LEAQQAEQEALLAQLSAEEAAAEAQ 197
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 290-492 6.29e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.63  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  290 VEALRAQLEEAEGQKDGLR---KQAGKLE--------------------QALKQEQGARRRQAEEDEQCLSEWEH----D 342
Cdd:COG3096   895 LEELREELDAAQEAQAFIQqhgKALAQLEplvavlqsdpeqfeqlqadyLQAKEQQRRLKQQIFALSEVVQRRPHfsyeD 974

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  343 KQQLLTETSDLKTKM-ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAErqvqqleEQVQQLEAQVQLLVGRLEGAGQ 421
Cdd:COG3096   975 AVGLLGENSDLNEKLrARLEQAEEARREAREQLRQAQAQYSQYNQVLASLK-------SSRDAKQQTLQELEQELEELGV 1047

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768025302  422 QVCwASTEldkEKARVDSMVRHQESLQAKQR--ALLKQLDSLDQEREELRGSLDEAeaqrarvEEQLQSEREQ 492
Cdd:COG3096  1048 QAD-AEAE---ERARIRRDELHEELSQNRSRrsQLEKQLTRCEAEMDSLQKRLRKA-------ERDYKQEREQ 1109
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 272-373 7.40e-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: 42.06  E-value: 7.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 272 VGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETS 351
Cdd:COG4942  144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223

                         90       100
                 ....*....|....*....|..
gi 768025302 352 DLKTKMATLERELKQQRESTQA 373
Cdd:COG4942  224 ELEALIARLEAEAAAAAERTPA 245
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
355-503 8.41e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 8.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 355 TKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQL--LVGRLEGAGQQVCWASTELDK 432
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEE 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768025302 433 EKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQGR 503
Cdd:COG4717  151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 269-499 1.02e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.65  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEgqkDGLRKQAgKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT 348
Cdd:pfam05557  36 ASALKRQLDRESDRNQELQKRIRLLEKREAEAE---EALREQA-ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  349 ETSDLKTKMATLERELKQQRESTQAVEakaQQLQEEGERRAAAERQVQQLEEQVQQLEA---QVQLLVGRLEgagQQVCW 425
Cdd:pfam05557 112 ELSELRRQIQRAELELQSTNSELEELQ---ERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQ---SQEQD 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  426 aSTELDKEKARVDSMVRhQESLQAKQRALLKQLDS-------LDQEREELRGSLDEAEAQRARVEEqLQSEREQGQCQLR 498
Cdd:pfam05557 186 -SEIVKNSKSELARIPE-LEKELERLREHNKHLNEnienkllLKEEVEDLKRKLEREEKYREEAAT-LELEKEKLEQELQ 262


                  .
gi 768025302  499 A 499
Cdd:pfam05557 263 S 263
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
344-492 1.02e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 344 QQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERraaaerqvqqleeqvqqLEAQVQLLVGRLEGAGQQV 423
Cdd:COG4372   34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-----------------LEEELEELNEQLQAAQAEL 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768025302 424 CWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQ 492
Cdd:COG4372   97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 269-384 1.15e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.86  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEgQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT 348
Cdd:COG3096   493 AWQTARELLRRYRSQQALAQRLQQLRAQLAELE-QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE 571

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 768025302  349 ETSDLKTKMATLERELKQQRESTQAVEAKA----------QQLQEE 384
Cdd:COG3096   572 QAAEAVEQRSELRQQLEQLRARIKELAARApawlaaqdalERLREQ 617
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
277-505 1.43e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALkqEQGARRRQAEEDEQCLSEweHDKQQLLTETSDLKTK 356
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERL--EELEEERDDLLAEAGLDD--ADAEAVEARREELEDR 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 357 MATLERELKQQRESTQAVEAKAQQLQEEG-----------ERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCW 425
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDAddleeraeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 426 ASTELDKEKARvdsmvrhqeslqakqrallkqLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREqgqcqLRAqQGRCP 505
Cdd:PRK02224 403 APVDLGNAEDF---------------------LEELREERDELREREAELEATLRTARERVEEAEA-----LLE-AGKCP 455
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 294-388 1.47e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.48  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  294 RAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEED---EQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRES 370
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELvalEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220

                          90
                  ....*....|....*...
gi 768025302  371 TQAVEAKAQQLQEEGERR 388
Cdd:PRK11448  221 ITDQAAKRLELSEEETRI 238
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 252-503 1.47e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.48  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  252 GQFQQLVQ------DSMGLRPLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAegqkDGLRKQAGKLEQALKQEQGAR 325
Cdd:COG3096   413 IQYQQAVQalekarALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVA----DAARRQFEKAYELVCKIAGEV 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  326 RRQA--EEDEQCLSEWEhDKQQLLTETSDLKTKMATLERELKQQREstqaveakAQQLQEEGERRAAAERqvqqleeqvq 403
Cdd:COG3096   489 ERSQawQTARELLRRYR-SQQALAQRLQQLRAQLAELEQRLRQQQN--------AERLLEEFCQRIGQQL---------- 549

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  404 QLEAQVQLLVGRLEgagQQVCWASTELDKEKARVDSMVRHQESLQAKQRAL-------LKQLDSLDQEREELRGSLDEAE 476
Cdd:COG3096   550 DAAEELEELLAELE---AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawLAAQDALERLREQSGEALADSQ 626

                         250       260
                  ....*....|....*....|....*....
gi 768025302  477 AQRARVEEQLQSERE--QGQCQLRAQQGR 503
Cdd:COG3096   627 EVTAAMQQLLEREREatVERDELAARKQA 655
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
277-466 1.53e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 277 AEQRKDLTRLSKHVEALRAQLEEAE----------------GQKDGLRKQAGKLEQALKQEQgARRRQAEEDEQCLSEWE 340
Cdd:COG3206  171 EEARKALEFLEEQLPELRKELEEAEaaleefrqknglvdlsEEAKLLLQQLSELESQLAEAR-AELAEAEARLAALRAQL 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 341 HDKQQLLTETS------DLKTKMATLERELKQQR-----ESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQV 409
Cdd:COG3206  250 GSGPDALPELLqspviqQLRAQLAELEAELAELSarytpNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768025302 410 QLLVGRLEGAGQQVcwasTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQERE 466
Cdd:COG3206  330 ASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
277-484 1.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 277 AEQRKDL-TRLSKH-VEALRAQLEEAEGQK---DGLRKQAGKLEQALKQEQGARRRQAEEDEQcLSEWEHDKQQLLTETS 351
Cdd:PRK03918 502 AEQLKELeEKLKKYnLEELEKKAEEYEKLKeklIKLKGEIKSLKKELEKLEELKKKLAELEKK-LDELEEELAELLKELE 580

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 352 DLKTK-MATLERELKQ----QRESTQAVEAKaQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQ----- 421
Cdd:PRK03918 581 ELGFEsVEELEERLKElepfYNEYLELKDAE-KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkysee 659

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768025302 422 ---QVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE 484
Cdd:PRK03918 660 eyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 283-486 2.06e-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: 39.91  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 283 LTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT-----ETSDLKTKM 357
Cdd:COG1579   19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkEYEALQKEI 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 358 ATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleeqvqqleaqvqllvgrlegagqqvcwasteLDKEKARV 437
Cdd:COG1579   99 ESLKRRISDLEDEILELMERIEELEEE---------------------------------------------LAELEAEL 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 768025302 438 DSMvrhQESLQAKQRALLKQLDSLDQEREELRgslDEAEAQRARVEEQL 486
Cdd:COG1579  134 AEL---EAELEEKKAELDEELAELEAELEELE---AEREELAAKIPPEL 176
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 290-492 2.10e-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: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   290 VEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGAR---RRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQ 366
Cdd:TIGR02169  793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKeylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   367 QRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQ-- 444
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEls 952

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 768025302   445 -ESLQAKQRALLKQLDSLD-------QEREELRGSLDEAEAQRARVEEqlqsEREQ 492
Cdd:TIGR02169  953 lEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEE----ERKA 1004
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 299-492 2.43e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.49  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  299 EAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEA-- 376
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEIsr 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  377 --KAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTE--------LDKEKARVDSMVRHQES 446
Cdd:pfam17380 377 mrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEarqrevrrLEEERAREMERVRLEEQ 456

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 768025302  447 LQAKQRALLKQldsLDQEREELRGSLDEAEAQRARVEEQLQSEREQ 492
Cdd:pfam17380 457 ERQQQVERLRQ---QEEERKRKKLELEKEKRDRKRAEEQRRKILEK 499
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 278-507 2.76e-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: 40.34  E-value: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   278 EQRKDLTRLSKHVEALRAQLEEAEGQkdgLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQlltETSDLKTKM 357
Cdd:TIGR00618  219 ERKQVLEKELKHLREALQQTQQSHAY---LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ---ERINRARKA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   358 ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVG------RLEGAGQQVCWASTELD 431
Cdd:TIGR00618  293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsqeiHIRDAHEVATSIREISC 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   432 KEKARVDSMVRHQESLQA-------------KQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLR 498
Cdd:TIGR00618  373 QQHTLTQHIHTLQQQKTTltqklqslckeldILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ 452


                   ....*....
gi 768025302   499 AQQGRCPRA 507
Cdd:TIGR00618  453 CEKLEKIHL 461
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
269-491 3.73e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALkqeqgarrrqaeedeqclsewehdkQQLLT 348
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-------------------------EELRE 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 349 ETSDLKTKMATLERELKQQRESTqaveAKAQQLQEEG-------------------ERRAAAErQVQQLEEQVQQLEAQV 409
Cdd:PRK02224 420 ERDELREREAELEATLRTARERV----EEAEALLEAGkcpecgqpvegsphvetieEDRERVE-ELEAELEDLEEEVEEV 494

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 410 QLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQrallKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSE 489
Cdd:PRK02224 495 EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKR----ERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570


                 ..
gi 768025302 490 RE 491
Cdd:PRK02224 571 RE 572
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 274-486 4.10e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 4.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALkqeqgarrrqaeedeqclseweHDKQQLLTETSDL 353
Cdd:pfam01576  426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL----------------------QDTQELLQEETRQ 483

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   354 KTKMATLERELKQQRESTQaveakaQQLQEEGERRAAAERqvqqleeqvqqleaqvqllvgrlegagqQVCWASTELDKE 433
Cdd:pfam01576  484 KLNLSTRLRQLEDERNSLQ------EQLEEEEEAKRNVER----------------------------QLSTLQAQLSDM 529

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 768025302   434 KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQL 486
Cdd:pfam01576  530 KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQEL 582
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
278-491 4.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQA--------------EEDEQCLSEWEHDK 343
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEelerlkkrltgltpEKLEKELEELEKAK 400

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 344 QQLLTETSDLKTKMATLERELKQQRESTQAVE-AKA------QQLQEEGERRAAAErqvqqleeqvqqLEAQVQLLVGRL 416
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKkAKGkcpvcgRELTEEHRKELLEE------------YTAELKRIEKEL 468

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 417 EGAGQQVcwasTELDKEKARVDsMVRHQESLQAKQRALLKQLDSLD---------------QEREELRGSLDEAEAQRAR 481
Cdd:PRK03918 469 KEIEEKE----RKLRKELRELE-KVLKKESELIKLKELAEQLKELEeklkkynleelekkaEEYEKLKEKLIKLKGEIKS 543

                        250
                 ....*....|
gi 768025302 482 VEEQLQSERE 491
Cdd:PRK03918 544 LKKELEKLEE 553
mukB PRK04863
chromosome partition protein MukB;
286-492 4.89e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  286 LSKHVEALRAQLEEAEGQKDGLRKQAGKLEQ----------------ALKQE-QGARRRQAEEDEQC--LSE-------- 338
Cdd:PRK04863  892 LADRVEEIREQLDEAEEAKRFVQQHGNALAQlepivsvlqsdpeqfeQLKQDyQQAQQTQRDAKQQAfaLTEvvqrrahf 971

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  339 -WEhDKQQLLTETSDLKTKM-ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEqvqqleaQVQLLVGRL 416
Cdd:PRK04863  972 sYE-DAAEMLAKNSDLNEKLrQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQ-------MLQELKQEL 1043

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768025302  417 EGAGQQVCwASTEldkEKARVDSMVRHQESLQAKQR--ALLKQLDSLDQEREELRGSLDEAEaqrarveEQLQSEREQ 492
Cdd:PRK04863 1044 QDLGVPAD-SGAE---ERARARRDELHARLSANRSRrnQLEKQLTFCEAEMDNLTKKLRKLE-------RDYHEMREQ 1110
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 426-503 5.24e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 5.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 426 ASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQ---LQSEREQGQCQLRAQQG 502
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAELRAELEAQKE 104


                 .
gi 768025302 503 R 503
Cdd:COG4942  105 E 105
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 326-494 5.44e-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: 38.49  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  326 RRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMAtlERELKQQRESTQAVEAKAQQLQEegERRAAAERqvqqleeqvQQL 405
Cdd:pfam15665  52 KRRIQTLEESLEQHERMKRQALTEFEQYKRRVE--ERELKAEAEHRQRVVELSREVEE--AKRAFEEK---------LES 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  406 EAQVQllvgrlegagqqvcwASTELDKEKARVDSMVRHQ---ESLQAKQRAL--------LKQLDSLDQEREELRGSLDE 474
Cdd:pfam15665 119 FEQLQ---------------AQFEQEKRKALEELRAKHRqeiQELLTTQRAQsasslaeqEKLEELHKAELESLRKEVED 183

                         170       180
                  ....*....|....*....|
gi 768025302  475 AEAQRARVEEQLQSEREQGQ 494
Cdd:pfam15665 184 LRKEKKKLAEEYEQKLSKAQ 203
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 286-384 6.04e-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: 37.96  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302  286 LSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgarrRQAEEDEQCLSEWEHDKQQLLTetsdLKTKMATLERELK 365
Cdd:pfam13851  31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQ----EEVEELRKQLENYEKDKQSLKN----LKARLKVLEKELK 102

                          90
                  ....*....|....*....
gi 768025302  366 QQRESTQAVEAKAQQLQEE 384
Cdd:pfam13851 103 DLKWEHEVLEQRFEKVERE 121
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 343-479 6.45e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 37.63  E-value: 6.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 343 KQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERqvqqleeqvQQLEAQVQLLVGRLEGAgqq 422
Cdd:PRK07352  52 REAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIR---------AEIEKQAIEDMARLKQT--- 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768025302 423 vcwASTELDKEKARVDSMVRHQESLQAKQRALlkqldsldqerEELRGSLDEAEAQR 479
Cdd:PRK07352 120 ---AAADLSAEQERVIAQLRREAAELAIAKAE-----------SQLPGRLDEDAQQR 162
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 278-367 8.05e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 37.01  E-value: 8.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302   278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAgKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:smart01071  53 YELIMNDHLNKRIDKLLKGLREEELSPETPTYNE-MLAELQDQLKKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKL 131

                           90
                   ....*....|
gi 768025302   358 ATLERELKQQ 367
Cdd:smart01071 132 DELEKEEKKK 141
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
269-492 9.23e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 9.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT 348
Cdd:COG4717  286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025302 349 EtsDLKTKMATLERELKQqrESTQAVEAKAQQLQEEGERRaaaerqvqqleeqvqqleAQVQLLVGRLEGAGQQVCWAST 428
Cdd:COG4717  366 E--ELEQEIAALLAEAGV--EDEEELRAALEQAEEYQELK------------------EELEELEEQLEELLGELEELLE 423

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768025302 429 ELDKE--KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELR--GSLDEAEAQRARVEEQLQSEREQ 492
Cdd:COG4717  424 ALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEE 491
 
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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