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Conserved domains on  [gi|281399025|gb|ADA68358|]
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myocardium-enriched Zo-associated protein [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 ...
 122-423 1.47e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.54  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   122 YDEMRQKIRQLTQELSVSHAQQ-ENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASM 200
Cdd:TIGR02168  215 YKELKAELRELELALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   201 DKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREmtkklysqyEEKLQEEQRKHSAEKEALLEETNSFLKVIEEANK 280
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESK---------LDELAEELAELEEKLEELKEELESLEAELEELEA 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   281 KMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETemsgELTDSDKERYQQLEEASASLRERIRHLDDMVHCQ 360
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281399025   361 QKKVKQMVEEIESLKKKLQQKQLLILQLLEKIS----FLEGENNELQSRLDYLTETQAKTEVETREI 423
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEqaldAAERELAQLQARLDSLERLQENLEGFSEGV 508
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 122-423 1.47e-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: 63.54  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   122 YDEMRQKIRQLTQELSVSHAQQ-ENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASM 200
Cdd:TIGR02168  215 YKELKAELRELELALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   201 DKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREmtkklysqyEEKLQEEQRKHSAEKEALLEETNSFLKVIEEANK 280
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESK---------LDELAEELAELEEKLEELKEELESLEAELEELEA 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   281 KMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETemsgELTDSDKERYQQLEEASASLRERIRHLDDMVHCQ 360
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281399025   361 QKKVKQMVEEIESLKKKLQQKQLLILQLLEKIS----FLEGENNELQSRLDYLTETQAKTEVETREI 423
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEqaldAAERELAQLQARLDSLERLQENLEGFSEGV 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-423 4.58e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 4.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 177 DVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKklySQYEEKLQEEQRK 256
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR---LEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 257 HSAEKEALLEETnsflkvIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERY 336
Cdd:COG1196  313 ELEERLEELEEE------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 337 QQLEEASA--SLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQA 414
Cdd:COG1196  387 ELLEALRAaaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466


                 ....*....
gi 281399025 415 KTEVETREI 423
Cdd:COG1196  467 ELLEEAALL 475
PTZ00121 PTZ00121
MAEBL; Provisional
 186-372 2.79e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  186 KDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR-------EMTKKLYSQYEEKLQEEQRKHS 258
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeelkkaEEEKKKVEQLKKKEAEEKKKAE 1650

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  259 AEKEallEETNSFLKVIEEANK----KMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKE 334
Cdd:PTZ00121 1651 ELKK---AEEENKIKAAEEAKKaeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 281399025  335 RYQQLEEASASLRERIRHLDDMV--HCQQKKVKQMVEEIE 372
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKkdEEEKKKIAHLKKEEE 1767
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 96-373 3.35e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025    96 QLKEEMNYIKDVRATLEKVRKrMYGDYDEMRQKIRQLTQELSVSHAQQENHIQTQSSaldrfnaMNSALASDSIGLQKTL 175
Cdd:pfam15921  445 QMERQMAAIQGKNESLEKVSS-LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD-------LTASLQEKERAIEATN 516

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   176 VDVTLENSNIKDQIRNLQQtyeasmdkLREKQRQLEVAQVENQLLKMKVeSSQEANAEVMRemtkklysQYEEKLQEEQR 255
Cdd:pfam15921  517 AEITKLRSRVDLKLQELQH--------LKNEGDHLRNVQTECEALKLQM-AEKDKVIEILR--------QQIENMTQLVG 579

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   256 KHSAEKEALLEETNSFLKVIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERhqlqLQLLEHETEMSGELTDSDKER 335
Cdd:pfam15921  580 QHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEK----VKLVNAGSERLRAVKDIKQER 655

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 281399025   336 YQQLEEASASlRERIRHLDDMVHCQQKKVKQMVEEIES 373
Cdd:pfam15921  656 DQLLNEVKTS-RNELNSLSEDYEVLKRNFRNKSEEMET 692
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
 168-294 8.57e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 38.48  E-value: 8.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   168 SIGLQKTLVDVTLENSNIKDQI-----------------RNLQQTYEASMDKLREKQRQLEvaqveNQLLKMKVessqea 230
Cdd:smart00435 230 SITLQEQLKELTAKDGNVAEKIlaynranrevailcnhqRTVSKTHEKSMEKLQEKIKALK-----YQLKRLKK------ 298

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281399025   231 nAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFL---KVIEEANKKMQAAEISLEEKDQ 294
Cdd:smart00435 299 -MILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEkkkKQIERLEERIEKLEVQATDKEE 364
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 122-423 1.47e-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: 63.54  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   122 YDEMRQKIRQLTQELSVSHAQQ-ENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASM 200
Cdd:TIGR02168  215 YKELKAELRELELALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   201 DKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREmtkklysqyEEKLQEEQRKHSAEKEALLEETNSFLKVIEEANK 280
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESK---------LDELAEELAELEEKLEELKEELESLEAELEELEA 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   281 KMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETemsgELTDSDKERYQQLEEASASLRERIRHLDDMVHCQ 360
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281399025   361 QKKVKQMVEEIESLKKKLQQKQLLILQLLEKIS----FLEGENNELQSRLDYLTETQAKTEVETREI 423
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEqaldAAERELAQLQARLDSLERLQENLEGFSEGV 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-423 4.58e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 4.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 177 DVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKklySQYEEKLQEEQRK 256
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR---LEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 257 HSAEKEALLEETnsflkvIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERY 336
Cdd:COG1196  313 ELEERLEELEEE------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 337 QQLEEASA--SLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQA 414
Cdd:COG1196  387 ELLEALRAaaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466


                 ....*....
gi 281399025 415 KTEVETREI 423
Cdd:COG1196  467 ELLEEAALL 475
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 96-356 1.24e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  96 QLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQENHIQtqssALDRFNAMNSALASDSIGLQKTL 175
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA----ELARLEQDIARLEERRRELEERL 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 176 VDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREmTKKLYSQYEEKLQEEQR 255
Cdd:COG1196  319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-LEELAEELLEALRAAAE 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 256 KHSAEKEALLEETNSFLKVIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKE-RHQLQLQLLEHETEMSGELTDSDKE 334
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEaELEEEEEALLELLAELLEEAALLEA 477

                        250       260
                 ....*....|....*....|..
gi 281399025 335 RYQQLEEASASLRERIRHLDDM 356
Cdd:COG1196  478 ALAELLEELAEAAARLLLLLEA 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 189-423 1.34e-07

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: 54.29  E-value: 1.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   189 IRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQyeEKLQEEQRKHSAEKEALLEET 268
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL--ARLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   269 NSFLKVIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLleheTEMSGELTDSdKERYQQLEEASASLRE 348
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLL-NEEAANLRERLESLER 831

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281399025   349 RIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQAKTEVETREI 423
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 96-423 5.29e-07

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: 52.38  E-value: 5.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025    96 QLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQENhIQTQSSALDRFNAMNSALASDSIGLQKTL 175
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE-IEKEIEQLEQEEEKLKERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   176 VDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLE-------VAQVENQLLKMKVESSQeaNAEVMREMTKKLYS-QYE 247
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshsrIPEIQAELSKLEEEVSR--IEARLREIEQKLNRlTLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   248 EKLQEEQRKHSAEKEALLEET-NSFLKVIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQL--LEHETEM 324
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLreLERKIEE 907

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   325 SGELTDSDKERYQQLEEASASLRERIRHLDDMvhcqqkkvKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENN---- 400
Cdd:TIGR02169  908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDP--------KGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMlaiq 979

                          330       340
                   ....*....|....*....|....*.
gi 281399025   401 ---ELQSRLDYLTETQAKTEVETREI 423
Cdd:TIGR02169  980 eyeEVLKRLDELKEKRAKLEEERKAI 1005
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 121-353 1.64e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 1.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   121 DYDEMRQKIRQLTQELSVSHAQQENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASM 200
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   201 DKLREKQRQLEVAQVENQLLKMKVESSQEAnaevMREMTKKLysqyeEKLQEEQRKHSAEKEALLEETNSFLKVIEEANK 280
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEEL----IEELESEL-----EALLNERASLEEALALLRSELEELSEELRELES 908

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281399025   281 KMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHEtEMSGELtdsDKERYQQLEEASASLRERIRHL 353
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY-SLTLEE---AEALENKIEDDEEEARRRLKRL 977
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 95-415 1.01e-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: 48.09  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   95 SQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQENHIQTQSSALDrFNAMNSALASDSIGLQKT 174
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE-LKKQNNQLKDNIEKKQQE 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  175 LVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVA-----QVENQLLKMKVESS---QEANAEVMREMTKKLYSQY 246
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNnkkikELEKQLNQLKSEISdlnNQKEQDWNKELKSELKNQE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  247 EE-------------------------------------KLQEEQRKHSAEKEALLEETNSFLKVIEEANKKMQAAEISL 289
Cdd:TIGR04523 321 KKleeiqnqisqnnkiisqlneqisqlkkeltnsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  290 EEKDQRIGELDRLIERMEKErhqlqLQLLEHETEMSGELTDSDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVE 369
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQE-----KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 281399025  370 EIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQAK 415
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 95-310 2.49e-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: 46.30  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  95 SQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSvshaQQENHIQTQSSALDRFNAMNSALASDSIGLQKT 174
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR----ALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 175 LvdvtlensniKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKmKVESSQEANAEVMREMTKKLYSQYEE------ 248
Cdd:COG4942  106 L----------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAEleaera 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281399025 249 KLQEEQRKHSAEKEALLEETNSFLKVIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKER 310
Cdd:COG4942  175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 95-356 8.25e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 8.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025    95 SQLKEEMNYIKDVRATLEKVRKRMYGDYDEM-RQKIRQLTQELSvshaQQENHIQTQSSALDRFNAMNSALASDSIGLQK 173
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELS----KLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   174 TLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLE-----VAQVENQLLKMKVESSQ-EANAEVMREMTKKLYSQYE 247
Cdd:TIGR02169  834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEeleaaLRDLESRLGDLKKERDElEAQLRELERKIEELEAQIE 913

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   248 EKlqeeqRKHSAEKEALLEETNSFLKVIEEANKKMQ---AAEISLEEKDQRIGELDRLIERMEkERHQLQLQLLEHETEM 324
Cdd:TIGR02169  914 KK-----RKRLSELKAKLEALEEELSEIEDPKGEDEeipEEELSLEDVQAELQRVEEEIRALE-PVNMLAIQEYEEVLKR 987

                          250       260       270
                   ....*....|....*....|....*....|..
gi 281399025   325 SGELtdsdKERYQQLEEASASLRERIRHLDDM 356
Cdd:TIGR02169  988 LDEL----KEKRAKLEEERKAILERIEEYEKK 1015
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 243-423 1.01e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 243 YSQYEEKLQE-EQRKHSAEKEALLEETNSFLKVIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHE 321
Cdd:COG1196  215 YRELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 322 TEMSGELTDSD--KERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGEN 399
Cdd:COG1196  295 AELARLEQDIArlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                        170       180
                 ....*....|....*....|....
gi 281399025 400 NELQSRLDYLTETQAKTEVETREI 423
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAAEL 398
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 202-423 1.26e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   202 KLREKQRQLEVAQVENQLLKMKVESSQeanAEVMREMTKKL--YSQYEekLQEEQRKHSAEKEALLEETNSFLKVIEEAN 279
Cdd:TIGR02169  183 EENIERLDLIIDEKRQQLERLRREREK---AERYQALLKEKreYEGYE--LLKEKEALERQKEAIERQLASLEEELEKLT 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   280 KKMQAAEISLEEKDQRIGELDRLIERM-EKERHQLQLQLLEHETEMSG----------ELTDSDKERyQQLEEASASLRE 348
Cdd:TIGR02169  258 EEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASlersiaekerELEDAEERL-AKLEAEIDKLLA 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   349 RIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLL--------------ILQLLEKISFLEGENNELQSRLDYLTETQA 414
Cdd:TIGR02169  337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkefaetrdeLKDYREKLEKLKREINELKRELDRLQEELQ 416


                   ....*....
gi 281399025   415 KTEVETREI 423
Cdd:TIGR02169  417 RLSEELADL 425
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 123-345 2.28e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 123 DEMRQKIRQLTQELSVSHAQQENHIQTQSSALDRFNAMNSALASdsigLQKTLVDVTLENSNIKDQIRNLQQTYEASMDK 202
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA----LARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 203 LREKQ----RQLEVAQVENQLLKMKV-ESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKVIEE 277
Cdd:COG4942   99 LEAQKeelaELLRALYRLGRQPPLALlLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281399025 278 ANKKMQAAEISLE-EKDQRIGELDRLIERMEKERHQLQlQLLEHETEMSGELTDSDKERYQQLEEASAS 345
Cdd:COG4942  179 LLAELEEERAALEaLKAERQKLLARLEKELAELAAELA-ELQQEAEELEALIARLEAEAAAAAERTPAA 246
PTZ00121 PTZ00121
MAEBL; Provisional
 186-372 2.79e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  186 KDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR-------EMTKKLYSQYEEKLQEEQRKHS 258
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeelkkaEEEKKKVEQLKKKEAEEKKKAE 1650

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  259 AEKEallEETNSFLKVIEEANK----KMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKE 334
Cdd:PTZ00121 1651 ELKK---AEEENKIKAAEEAKKaeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 281399025  335 RYQQLEEASASLRERIRHLDDMV--HCQQKKVKQMVEEIE 372
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKkdEEEKKKIAHLKKEEE 1767
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
183-405 2.90e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 183 SNIKDQIRNLQQTYEA---SMDKLREKQRQL--EVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQ--EEQR 255
Cdd:PRK03918 189 ENIEELIKEKEKELEEvlrEINEISSELPELreELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRelEERI 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 256 KHSAEKEALLEETNSFLKVIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQL--LEHETEMSGELTDSDK 333
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeLEEKEERLEELKKKLK 348

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281399025 334 ERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSR 405
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
184-373 3.13e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  184 NIKDQIRNLQQTYEAsMDKLREKQRQLEVAQVENQLLKMKVESSQEANAevMREMTKKLYSQYE-EKLQEEQRKHSAEKE 262
Cdd:COG4913   229 ALVEHFDDLERAHEA-LEDAREQIELLEPIRELAERYAAARERLAELEY--LRAALRLWFAQRRlELLEAELEELRAELA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  263 ALLEETNSFLKVIEEANKKMQAAEISLEEKD-QRIGELDRLIERMEKERHQLQLQLLEHET-----EMSGELTDSD---- 332
Cdd:COG4913   306 RLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAllaalGLPLPASAEEfaal 385

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 281399025  333 ----KERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIES 373
Cdd:COG4913   386 raeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 96-373 3.35e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025    96 QLKEEMNYIKDVRATLEKVRKrMYGDYDEMRQKIRQLTQELSVSHAQQENHIQTQSSaldrfnaMNSALASDSIGLQKTL 175
Cdd:pfam15921  445 QMERQMAAIQGKNESLEKVSS-LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD-------LTASLQEKERAIEATN 516

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   176 VDVTLENSNIKDQIRNLQQtyeasmdkLREKQRQLEVAQVENQLLKMKVeSSQEANAEVMRemtkklysQYEEKLQEEQR 255
Cdd:pfam15921  517 AEITKLRSRVDLKLQELQH--------LKNEGDHLRNVQTECEALKLQM-AEKDKVIEILR--------QQIENMTQLVG 579

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   256 KHSAEKEALLEETNSFLKVIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERhqlqLQLLEHETEMSGELTDSDKER 335
Cdd:pfam15921  580 QHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEK----VKLVNAGSERLRAVKDIKQER 655

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 281399025   336 YQQLEEASASlRERIRHLDDMVHCQQKKVKQMVEEIES 373
Cdd:pfam15921  656 DQLLNEVKTS-RNELNSLSEDYEVLKRNFRNKSEEMET 692
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 203-357 4.58e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 203 LREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKVIEEANKKM 282
Cdd:COG1196  676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 283 QAAEISLEEKDQRIGELDRLIERME-------------KERHQlqlqllehetEMSGELTDsdkeryqqLEEASASLRER 349
Cdd:COG1196  756 LPEPPDLEELERELERLEREIEALGpvnllaieeyeelEERYD----------FLSEQRED--------LEEARETLEEA 817


                 ....*...
gi 281399025 350 IRHLDDMV 357
Cdd:COG1196  818 IEEIDRET 825
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 95-424 5.42e-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: 42.75  E-value: 5.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025    95 SQLKEEMNYIKDVRATLEKvrkrmygdYDEMRQKIRQLT--------QELSVSHAQQENHIQTQSSALDRFNAMNSALAS 166
Cdd:TIGR02169  194 DEKRQQLERLRREREKAER--------YQALLKEKREYEgyellkekEALERQKEAIERQLASLEEELEKLTEEISELEK 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   167 DSIGLQKTLVDVTLEnsnIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLlKMKVESSQEANAEVMREMTKKLYSQY 246
Cdd:TIGR02169  266 RLEEIEQLLEELNKK---IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER-ELEDAEERLAKLEAEIDKLLAEIEEL 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   247 EEKLQEEQRkhsaEKEALLEEtnsflkvIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMsg 326
Cdd:TIGR02169  342 EREIEEERK----RRDKLTEE-------YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL-- 408

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   327 eltDSDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRL 406
Cdd:TIGR02169  409 ---DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485

                          330
                   ....*....|....*...
gi 281399025   407 DYLTETQAKTEVETREIG 424
Cdd:TIGR02169  486 SKLQRELAEAEAQARASE 503
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 200-314 6.63e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 42.22  E-value: 6.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 200 MDKLREKQRQLEVAQVENqllkMKVESSQEANAEVMREMTK--------KLYSQYEEKLQEEQRKHSAEK-EALLEETNS 270
Cdd:PRK05771  18 KDEVLEALHELGVVHIED----LKEELSNERLRKLRSLLTKlsealdklRSYLPKLNPLREEKKKVSVKSlEELIKDVEE 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 281399025 271 FLKVIEEankkmqaaeiSLEEKDQRIGELDRLIERMEKERHQLQ 314
Cdd:PRK05771  94 ELEKIEK----------EIKELEEEISELENEIKELEQEIERLE 127
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 248-422 9.96e-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: 41.29  E-value: 9.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 248 EKLQEEQRKHSAEKEALLEETNSFLKVIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGE 327
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 328 LTDSDK-ERYQQL------EEASASLReRIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENN 400
Cdd:COG4942  110 LRALYRlGRQPPLalllspEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188

                        170       180
                 ....*....|....*....|..
gi 281399025 401 ELQSRLDYLTETQAKTEVETRE 422
Cdd:COG4942  189 ALEALKAERQKLLARLEKELAE 210
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 187-348 1.09e-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: 41.65  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  187 DQIRNLQQtyEASMDKLR----EKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKE 262
Cdd:pfam17380 423 EQIRAEQE--EARQREVRrleeERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKE 500

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  263 ------ALLEETNSfLKVIEEANKKMQAAeiSLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSG-ELTDSDKER 335
Cdd:pfam17380 501 leerkqAMIEEERK-RKLLEKEMEERQKA--IYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRlEAMEREREM 577

                         170
                  ....*....|...
gi 281399025  336 YQQLEEASASLRE 348
Cdd:pfam17380 578 MRQIVESEKARAE 590
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
183-372 1.47e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 183 SNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR-EMTKKLYSQYEEKLQEEQRkhsaEK 261
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELREIEK----RL 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 262 EALLEETNSFLKVIEEANKKmqaaEISLEEKDQRIGELDRLIERMEK------ERHQLQLQLLEHETEMSGELTDSDKER 335
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEErhelyeEAKAKKEELERLKKRLTGLTPEKLEKE 392

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 281399025 336 YQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIE 372
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 248-422 1.97e-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: 40.52  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 248 EKLQEEQRKHSAEKEALLEETNSFLKVIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQL---------- 317
Cdd:COG4942   37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrl 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 318 -----------------LEHETEMSGELTDSDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQ 380
Cdd:COG4942  117 grqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 281399025 381 KQLLILQLLEKISFLEGENNELQSRLDYLTETQAKTEVETRE 422
Cdd:COG4942  197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 107-321 2.16e-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: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  107 VRATLEKVRKRMYGDyDEMRQKIRQLTQELSVSHAQQENHIQTQSSALDRFNAmnsalasdsiglqKTLVDVTLENSNIK 186
Cdd:pfam17380 394 VRQELEAARKVKILE-EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA-------------REMERVRLEEQERQ 459

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  187 DQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVM------REMTKKLYSQYEEKLQEEQRKHSAE 260
Cdd:pfam17380 460 QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMieeerkRKLLEKEMEERQKAIYEEERRREAE 539

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281399025  261 KEALLEetnsflKVIEEANKKMQAAEISLEEKDQrigeldrlIERMEKERHQLQlQLLEHE 321
Cdd:pfam17380 540 EERRKQ------QEMEERRRIQEQMRKATEERSR--------LEAMEREREMMR-QIVESE 585
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 157-348 2.32e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 157 FNAMNSALASDSIG-LQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVM 235
Cdd:COG3883    6 LAAPTPAFADPQIQaKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 236 REMTKKLYSQYEEKLQeeqrkhSAEKEALLEETN--------SFLKVIEEANKKM----QAAEISLEEK----DQRIGEL 299
Cdd:COG3883   86 EELGERARALYRSGGS------VSYLDVLLGSESfsdfldrlSALSKIADADADLleelKADKAELEAKkaelEAKLAEL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 281399025 300 DRLIERMEKERHQLQLQLLEHETEMSgELTDSDKERYQQLEEASASLRE 348
Cdd:COG3883  160 EALKAELEAAKAELEAQQAEQEALLA-QLSAEEAAAEAQLAELEAELAA 207
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
201-341 3.50e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  201 DKLREKQRQL-----EVAQVENQLLKMKVEssQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKVI 275
Cdd:COG4913   610 AKLAALEAELaeleeELAEAEERLEALEAE--LDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281399025  276 EEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERYQQLEE 341
Cdd:COG4913   688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 96-441 5.15e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.32  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   96 QLKEEMNYIKDVRATLEKVRKRMygdyDEMRQKIRQLTQELSVSHAQQEN---HIQTQSSALDRFNAMNSALASDSIGLQ 172
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKA----NQLEEKTKLQDENLKELIEKKDHltkELEDIKMSLQRSMSTQKALEEDLQIAT 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  173 KTLVDVTLENSNIKDQIRNLQQTYEASMDK-----------LREKQRQLEVAQVENQLLKMKVESSQEAnaevMREMTKk 241
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEfeattcsleelLRTEQQRLEKNEDQLKIITMELQKKSSE----LEEMTK- 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  242 lYSQYEEKLQEEQRKHSAEKEALLEETNSFLKVIEEANKKMQaaeisleekdqrigELDRLIERMEKERHQLQLQL---- 317
Cdd:pfam05483 399 -FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQ--------------ELIFLLQAREKEIHDLEIQLtaik 463

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025  318 ----------------LEHETEMSGELT-DSDK---ERYQQLEEASASLRERIRHLDDMVHCqQKKVKQMVEEIESLKKK 377
Cdd:pfam05483 464 tseehylkevedlkteLEKEKLKNIELTaHCDKlllENKELTQEASDMTLELKKHQEDIINC-KKQEERMLKQIENLEEK 542

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281399025  378 LQQKQLLILQLLEKisfLEGENNELQSRLDYLTETQAKTEVETREIGVGCDLLPSQTGRTREIV 441
Cdd:pfam05483 543 EMNLRDELESVREE---FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
PRK12704 PRK12704
phosphodiesterase; Provisional
 215-372 5.86e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 5.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 215 VENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKVIEEANKKMQAAEISLEEKDQ 294
Cdd:PRK12704  24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025 295 RIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDK--ERYQQL--EEASASLRERIRhlDDMVHCQQKKVKQMVEE 370
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLtaEEAKEILLEKVE--EEARHEAAVLIKEIEEE 181


                 ..
gi 281399025 371 IE 372
Cdd:PRK12704 182 AK 183
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
 168-294 8.57e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 38.48  E-value: 8.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281399025   168 SIGLQKTLVDVTLENSNIKDQI-----------------RNLQQTYEASMDKLREKQRQLEvaqveNQLLKMKVessqea 230
Cdd:smart00435 230 SITLQEQLKELTAKDGNVAEKIlaynranrevailcnhqRTVSKTHEKSMEKLQEKIKALK-----YQLKRLKK------ 298

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281399025   231 nAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFL---KVIEEANKKMQAAEISLEEKDQ 294
Cdd:smart00435 299 -MILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEkkkKQIERLEERIEKLEVQATDKEE 364
 
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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