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Conserved domains on  [gi|530383679|ref|XP_005267028|]
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centrosomal protein of 85 kDa-like isoform X4 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

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_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 341-588 6.89e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 6.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   341 EFEQKLASTEKEVLQLNEflkQRLSLFSEEKKKLEEKLKTRDRyISSLKKKCQKESEQNKEKQRRIETLEKYL----ADL 416
Cdd:TIGR02168  236 ELREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKqilrERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   417 PTLDDVQSQ-SLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRL 495
Cdd:TIGR02168  312 ANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-LRSKVAQ 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   496 PMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMM-----EELEKKERNVQRLTKAL 570
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqEELERLEEALEELREEL 470

                          250
                   ....*....|....*...
gi 530383679   571 LENQRQTDETCSLLDQGQ 588
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQ 488
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 341-588 6.89e-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: 56.22  E-value: 6.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   341 EFEQKLASTEKEVLQLNEflkQRLSLFSEEKKKLEEKLKTRDRyISSLKKKCQKESEQNKEKQRRIETLEKYL----ADL 416
Cdd:TIGR02168  236 ELREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKqilrERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   417 PTLDDVQSQ-SLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRL 495
Cdd:TIGR02168  312 ANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-LRSKVAQ 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   496 PMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMM-----EELEKKERNVQRLTKAL 570
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqEELERLEEALEELREEL 470

                          250
                   ....*....|....*...
gi 530383679   571 LENQRQTDETCSLLDQGQ 588
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQ 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-596 8.58e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 8.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 398 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTT 477
Cdd:COG1196  219 KEELKELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 478 VQSLQQKVERCLEDGIRLPmLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELE 557
Cdd:COG1196  297 LARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 530383679 558 KKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSRQQ 596
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
341-561 8.54e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 8.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 341 EFEQKLASTEKEVLQLNEfLKQRLSlfseekkKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLD 420
Cdd:PRK03918 218 ELREELEKLEKEVKELEE-LKEEIE-------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 421 DVQSQSLQL-----QILEEKNkNLQEALIDTEKKLEEIKKQCQDKETqlicQKKKEKELVTTVQSLQQKVERcLEDGIRL 495
Cdd:PRK03918 290 EKAEEYIKLsefyeEYLDELR-EIEKRLSRLEEEINGIEERIKELEE----KEERLEELKKKLKELEKRLEE-LEERHEL 363

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530383679 496 pMLDAKQLQNENDNLRQQ--NETASKI------IDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKER 561
Cdd:PRK03918 364 -YEEAKAKKEELERLKKRltGLTPEKLekeleeLEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 337-699 1.04e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.65  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   337 SQQGEFEQKLASTEKEVLQLNEFLKqRLSLFSEEKKKLEEKLKTRDRYIS------SLKKKCQKESEQNKEKQR---RIE 407
Cdd:pfam02463  139 VQGGKIEIIAMMKPERRLEIEEEAA-GSRLKRKKKEALKKLIEETENLAEliidleELKLQELKLKEQAKKALEyyqLKE 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   408 TLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEaLIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVER 487
Cdd:pfam02463  218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE-EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   488 CLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLT 567
Cdd:pfam02463  297 ELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   568 KALLENQRQTDETCSLLDQGQEPDQSRQQTVLSKRPLFDLTVIDQLFKEMSCCLFDLKALCSILNQRAQGKE--PNLSLL 645
Cdd:pfam02463  377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEekEELEKQ 456

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530383679   646 LGIRSMNCSAEETENDHSTETLTKKLSDVCQLRRDIDELRT-TISDRYAQDMGDN 699
Cdd:pfam02463  457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEErSQKESKARSGLKV 511
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 341-588 6.89e-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: 56.22  E-value: 6.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   341 EFEQKLASTEKEVLQLNEflkQRLSLFSEEKKKLEEKLKTRDRyISSLKKKCQKESEQNKEKQRRIETLEKYL----ADL 416
Cdd:TIGR02168  236 ELREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKqilrERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   417 PTLDDVQSQ-SLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRL 495
Cdd:TIGR02168  312 ANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-LRSKVAQ 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   496 PMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMM-----EELEKKERNVQRLTKAL 570
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqEELERLEEALEELREEL 470

                          250
                   ....*....|....*...
gi 530383679   571 LENQRQTDETCSLLDQGQ 588
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQ 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-596 8.58e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 8.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 398 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTT 477
Cdd:COG1196  219 KEELKELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 478 VQSLQQKVERCLEDGIRLPmLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELE 557
Cdd:COG1196  297 LARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 530383679 558 KKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSRQQ 596
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
341-561 8.54e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 8.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 341 EFEQKLASTEKEVLQLNEfLKQRLSlfseekkKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLD 420
Cdd:PRK03918 218 ELREELEKLEKEVKELEE-LKEEIE-------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 421 DVQSQSLQL-----QILEEKNkNLQEALIDTEKKLEEIKKQCQDKETqlicQKKKEKELVTTVQSLQQKVERcLEDGIRL 495
Cdd:PRK03918 290 EKAEEYIKLsefyeEYLDELR-EIEKRLSRLEEEINGIEERIKELEE----KEERLEELKKKLKELEKRLEE-LEERHEL 363

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530383679 496 pMLDAKQLQNENDNLRQQ--NETASKI------IDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKER 561
Cdd:PRK03918 364 -YEEAKAKKEELERLKKRltGLTPEKLekeleeLEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 338-604 9.28e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 9.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 338 QQGEFEQKLASTEKEVLQLN---EFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLA 414
Cdd:COG1196  247 ELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 415 DLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEikkqcqdketqlicQKKKEKELVTTVQSLQQKVERCLEDGIR 494
Cdd:COG1196  327 EL--EEELEELEEELEELEEELEEAEEELEEAEAELAE--------------AEEALLEAEAELAEAEEELEELAEELLE 390

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 495 LpMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQ 574
Cdd:COG1196  391 A-LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                        250       260       270
                 ....*....|....*....|....*....|
gi 530383679 575 RQTDETCSLLDQGQEPDQSRQQTVLSKRPL 604
Cdd:COG1196  470 EEAALLEAALAELLEELAEAAARLLLLLEA 499
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 398-596 1.09e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 398 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqKKKEKELVTT 477
Cdd:COG3883   17 QIQAKQKELSELQAELEAA--QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGER 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 478 VQSLQQkvercleDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDrmilEIQSMQGKLSKEKLTTQKMMEELE 557
Cdd:COG3883   92 ARALYR-------SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELE 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 530383679 558 KKERNVQRLTKALlenQRQTDETCSLLDQGQEPDQSRQQ 596
Cdd:COG3883  161 ALKAELEAAKAEL---EAQQAEQEALLAQLSAEEAAAEA 196
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 341-579 1.62e-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: 48.51  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   341 EFEQKLASTEKEV---LQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLp 417
Cdd:TIGR02168  688 ELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL- 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   418 tLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEdgirlpm 497
Cdd:TIGR02168  767 -EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER------- 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   498 lDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQT 577
Cdd:TIGR02168  839 -RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917


                   ..
gi 530383679   578 DE 579
Cdd:TIGR02168  918 EE 919
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 440-602 1.80e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 440 QEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRLPMLDAKQLQNENDNLRQQNETASK 519
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 520 IIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKA---LLENQRQTDETCSLLDQGQEPDQSRQQ 596
Cdd:COG4942   98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELE 177


                 ....*.
gi 530383679 597 TVLSKR 602
Cdd:COG4942  178 ALLAEL 183
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 253-563 2.79e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   253 QDFSKWESMLKIKEGLLRQKEIVIDRQKQQITHLHERIRDNELRAqHAMLGHYVNCEDSYVASLQPQYENtslQTPFSEE 332
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL-HKLEEALNDLEARLSHSRIPEIQA---ELSKLEE 805

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   333 SVShsqqgEFEQKLASTEKE---VLQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETL 409
Cdd:TIGR02169  806 EVS-----RIEARLREIEQKlnrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   410 EKYLADlptlddvqsqslqlqiLEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCL 489
Cdd:TIGR02169  881 ESRLGD----------------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530383679   490 EDGIRLPMLD--AKQLQNENDNLRQQNETASKIIDSQQDEIDRMiLEIQSMQGKLSKEKLTTQKMMEELEKKERNV 563
Cdd:TIGR02169  945 EIPEEELSLEdvQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILERIEEYEKKKREV 1019
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 385-579 3.04e-04

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: 44.24  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679  385 ISSLKKKCQKESEQNKEKQRRIETLEKYLADLptldDVQSQSLQLQILEEKN--KNLQEALIDTEKKLEEIKKQCQDKET 462
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELL----EKEIERLKETIIKNNSeiKDLTNQDSVKELIIKNLDNTRESLET 468

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679  463 QLicqKKKEKELVTTVQSLQQKVERCLEDGIRLPMLDA--KQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQG 540
Cdd:TIGR04523 469 QL---KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEekKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 530383679  541 KLSKEK--LTTQKMMEELEKKERNVQRL---TKALLENQRQTDE 579
Cdd:TIGR04523 546 ELNKDDfeLKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQE 589
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 414-602 7.90e-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: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 414 ADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcledgi 493
Cdd:COG1579    4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK------ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 494 rlpmldakqlqnenDNLRQQNETASKIIDSQQDEIDRMILEIQsmqgKLSKEKLttqKMMEELEKKERNVQRLTKALLEN 573
Cdd:COG1579   78 --------------YEEQLGNVRNNKEYEALQKEIESLKRRIS----DLEDEIL---ELMERIEELEEELAELEAELAEL 136

                        170       180
                 ....*....|....*....|....*....
gi 530383679 574 QRQTDETCSLLDQGQEPDQSRQQTVLSKR 602
Cdd:COG1579  137 EAELEEKKAELDEELAELEAELEELEAER 165
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 337-699 1.04e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.65  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   337 SQQGEFEQKLASTEKEVLQLNEFLKqRLSLFSEEKKKLEEKLKTRDRYIS------SLKKKCQKESEQNKEKQR---RIE 407
Cdd:pfam02463  139 VQGGKIEIIAMMKPERRLEIEEEAA-GSRLKRKKKEALKKLIEETENLAEliidleELKLQELKLKEQAKKALEyyqLKE 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   408 TLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEaLIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVER 487
Cdd:pfam02463  218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE-EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   488 CLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLT 567
Cdd:pfam02463  297 ELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   568 KALLENQRQTDETCSLLDQGQEPDQSRQQTVLSKRPLFDLTVIDQLFKEMSCCLFDLKALCSILNQRAQGKE--PNLSLL 645
Cdd:pfam02463  377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEekEELEKQ 456

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530383679   646 LGIRSMNCSAEETENDHSTETLTKKLSDVCQLRRDIDELRT-TISDRYAQDMGDN 699
Cdd:pfam02463  457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEErSQKESKARSGLKV 511
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 385-580 1.10e-03

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: 42.31  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679  385 ISSLKKKCQKESEQNKEKQRRIETLEKYLADlptlddvqsqslqlqiLEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 464
Cdd:TIGR04523 126 LNKLEKQKKENKKNIDKFLTEIKKKEKELEK----------------LNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679  465 ICQKKKEKELVTTVQSLQQKVERcledgirlpmldAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSK 544
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQK------------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 530383679  545 EKLTTQKMMEELEKKERNVQRLTKAL--LENQRQTDET 580
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIkeLEKQLNQLKS 295
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 262-570 1.19e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   262 LKIKEGLLRQKEIVIDRQKQQITHLHERIRD-----NELRAQHAMLGHYVNCEDSYVASLQPQYENTS--LQTPFSEESV 334
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQlrkelEELSRQISALRKDLARLEAEVEQLEERIAQLSkeLTELEAEIEE 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   335 SHSQQGEFEQKLASTEKEVLQLNEFLKQ---RLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEK 411
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   412 YLADLptlddvqsqSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVercled 491
Cdd:TIGR02168  846 QIEEL---------SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR------ 910

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679   492 girlpmldaKQLQNENDNLRQQNETAskiidsqQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKK--------ERNV 563
Cdd:TIGR02168  911 ---------SELRRELEELREKLAQL-------ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKieddeeeaRRRL 974


                   ....*..
gi 530383679   564 QRLTKAL 570
Cdd:TIGR02168  975 KRLENKI 981
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 368-594 1.41e-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: 41.67  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 368 SEEKKKLeeklktrdryisslKKKCQKESEQNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTE 447
Cdd:COG4942   19 ADAAAEA--------------EAELEQLQQEIAELEKELAALKKEEKAL--LKQLAALERRIAALARRIRALEQELAALE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 448 KKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQ--------KVERCLEDGIRLPMLDA--KQLQNENDNLRQQNETA 517
Cdd:COG4942   83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAEL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 518 SKI---IDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSR 594
Cdd:COG4942  163 AALraeLEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
382-548 1.62e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 382 DRYISSLKKKCQKESEQnKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKE 461
Cdd:COG4717   88 EEYAELQEELEELEEEL-EELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 462 TQLICQKKKEKELVTTVQSLQQKVERCLEDGIRlpmlDAKQLQNENDNLRQQNETASKIIDSQQDEIDRM--ILEIQSMQ 539
Cdd:COG4717  167 ELEAELAELQEELEELLEQLSLATEEELQDLAE----ELEELQQRLAELEEELEEAQEELEELEEELEQLenELEAAALE 242


                 ....*....
gi 530383679 540 GKLSKEKLT 548
Cdd:COG4717  243 ERLKEARLL 251
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 262-578 1.65e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 262 LKIKEGLLRQKEIviDRQKQQITHLHERIRDNELRAQHAMLGhyvncedsyVASLQPQYENTSLQtpFSEESVSHSQQGE 341
Cdd:COG1196  222 LKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAE---------LAELEAELEELRLE--LEELELELEEAQA 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 342 FEQKLASTEKEVLQLNEFLKQRLSLFSEEKKKLEEKlktrdryISSLKKKCQKESEQNKEKQRRIETLEKYLADLptldd 421
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEA----- 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 422 vqsqSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEDGIRLpmldAK 501
Cdd:COG1196  357 ----EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL----EE 428

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530383679 502 QLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLtKALLENQRQTD 578
Cdd:COG1196  429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYE 504
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
341-572 2.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 341 EFEQKLASTEKEVLQLNEFLKqRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKES-EQNKEKQRRIETLEKYLADLPTL 419
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLEL 607

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 420 DDVQSqslQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqkkKEKELVTTVQSLQQKVERCLEDGIRLPMLD 499
Cdd:PRK03918 608 KDAEK---ELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL-----EELEKKYSEEEYEELREEYLELSRELAGLR 679

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383679 500 AKQLQNEndNLRQQNETASKIIDSQQDEIDRMILEIQSMqgklskeklttQKMMEELEKKERNVQRLtKALLE 572
Cdd:PRK03918 680 AELEELE--KRREEIKKTLEKLKEELEEREKAKKELEKL-----------EKALERVEELREKVKKY-KALLK 738
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 385-596 2.98e-03

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: 40.77  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679  385 ISSLKKKCQKeseqNKEKQRRIETLEKYLADLPtlDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 464
Cdd:TIGR04523 203 LSNLKKKIQK----NKSLESQISELKKQNNQLK--DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679  465 ICQKKKEKELVTTVQSLQQKVERC---LEDGIrlpmldAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGK 541
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLnnqKEQDW------NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530383679  542 LSKEKLTTQKMMEELEKKERNVQRLTKallENQRQTDETCSLLDQGQEPDQSRQQ 596
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKK---ENQSYKQEIKNLESQINDLESKIQN 402
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
383-576 3.82e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 383 RYISSLKKKCQKESEQNKEKQRRIETLEKyladlpTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKEt 462
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE- 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 463 qlicqkKKEKELvttvQSLQQKVERCLEDGirlpmldaKQLQNENDNLRQQNETASKIiDSQQDEIDRMILEIQSMQ--- 539
Cdd:PRK03918 280 ------EKVKEL----KELKEKAEEYIKLS--------EFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEerl 340

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530383679 540 GKLSKEKLTTQKMMEELEKKERNVQRLtKALLENQRQ 576
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEA-KAKKEELER 376
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 385-487 4.56e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 385 ISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 464
Cdd:COG1579   54 LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL 133

                         90       100
                 ....*....|....*....|...
gi 530383679 465 icqKKKEKELVTTVQSLQQKVER 487
Cdd:COG1579  134 ---AELEAELEEKKAELDEELAE 153
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 427-579 6.72e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.81  E-value: 6.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679 427 LQLQILEEKNKNLQEaliDTEKkLEEIKKQCQDKETQlicQKKKEKELvttvQSLQQKVERCLEDGIRLpmldAKQLQNE 506
Cdd:PRK00409 499 LPENIIEEAKKLIGE---DKEK-LNELIASLEELERE---LEQKAEEA----EALLKEAEKLKEELEEK----KEKLQEE 563

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530383679 507 NDNLRQ-QNETASKIIDSQQDEIDRMILEIQSMQgKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDE 579
Cdd:PRK00409 564 EDKLLEeAEKEAQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
PRK11281 PRK11281
mechanosensitive channel MscK;
414-602 6.83e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.89  E-value: 6.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679  414 ADLPTLDDVQSQSLQLQ---ILEEKNKNLQEALIDT----------EKKLEEIKKQCQDKETQLicqKKKEKELVTTVQS 480
Cdd:PRK11281   33 GDLPTEADVQAQLDALNkqkLLEAEDKLVQQDLEQTlalldkidrqKEETEQLKQQLAQAPAKL---RQAQAELEALKDD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679  481 LQQKVERCLEDgIRLPMLDAK------QLQNENDNLrqqNETASKIIDSQ------QDEIDRMILEIQSMQ-----GKLS 543
Cdd:PRK11281  110 NDEETRETLST-LSLRQLESRlaqtldQLQNAQNDL---AEYNSQLVSLQtqperaQAALYANSQRLQQIRnllkgGKVG 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383679  544 KEKLT-TQKMMEELEKKERNVQ-RLTKALLEN--------QRQTDETCSLLDQGQEPDQSRQQTVLSKR 602
Cdd:PRK11281  186 GKALRpSQRVLLQAEQALLNAQnDLQRKSLEGntqlqdllQKQRDYLTARIQRLEHQLQLLQEAINSKR 254
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 386-594 9.13e-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: 39.34  E-value: 9.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679  386 SSLKKKCQKESEQNKEKQRRIETLEKYLADlptlddvQSQSLQLQIleEKNKNLQEALIDTEKKLEEIKKQCQDKETQLI 465
Cdd:pfam05557  37 SALKRQLDRESDRNQELQKRIRLLEKREAE-------AEEALREQA--ELNRLKKKYLEALNKKLNEKESQLADAREVIS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679  466 CQKKKEKELVT-------TVQSLQQKVERCLEdgiRLPMLDAKQLQNEndNLRQQNETASKIIDSQQDEIDRMILEIQSM 538
Cdd:pfam05557 108 CLKNELSELRRqiqraelELQSTNSELEELQE---RLDLLKAKASEAE--QLRQNLEKQQSSLAEAEQRIKELEFEIQSQ 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530383679  539 qgklSKEKLTTQKMMEELE---KKERNVQRLtKALLENQRQTDETCSLLDQGQEPDQSR 594
Cdd:pfam05557 183 ----EQDSEIVKNSKSELAripELEKELERL-REHNKHLNENIENKLLLKEEVEDLKRK 236
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 381-539 9.34e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 39.24  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679  381 RDRYISSLKK---KCQKESEQNKEKQRRIETLEKYLADLPTLD--------DVQSQSLQLQILEEKNKNLQEALIdteKK 449
Cdd:pfam05667 358 IKKLESSIKQveeELEELKEQNEELEKQYKVKKKTLDLLPDAEeniaklqaLVDASAQRLVELAGQWEKHRVPLI---EE 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383679  450 LEEIKKQCQDKETQliCQKKKEKelvttVQSLQQKVERCLEDgIRLPMLDAKQLQNENDNLRQQ---NETASKI------ 520
Cdd:pfam05667 435 YRALKEAKSNKEDE--SQRKLEE-----IKELREKIKEVAEE-AKQKEELYKQLVAEYERLPKDvsrSAYTRRIleivkn 506

                         170
                  ....*....|....*....
gi 530383679  521 IDSQQDEIDRMILEIQSMQ 539
Cdd:pfam05667 507 IKKQKEEITKILSDTKSLQ 525
 
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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